data_4Q06
# 
_entry.id   4Q06 
# 
_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   4Q06         pdb_00004q06 10.2210/pdb4q06/pdb 
RCSB  RCSB085438   ?            ?                   
WWPDB D_1000085438 ?            ?                   
# 
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 4Q07 . unspecified 
PDB 4Q08 . unspecified 
PDB 4Q09 . unspecified 
PDB 4Q0L . unspecified 
# 
_pdbx_database_status.entry_id                        4Q06 
_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           4Q06 
_cell.length_a           42.015 
_cell.length_b           41.343 
_cell.length_c           72.194 
_cell.angle_alpha        90.00 
_cell.angle_beta         104.14 
_cell.angle_gamma        90.00 
_cell.Z_PDB              2 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4Q06 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                               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 BICINE                                                                               163.172   1   ?       ? ? ? 
5 non-polymer syn '2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' 412.491   1   ?       ? ? ? 
6 water       nat water                                                                                18.015    292 ?       ? ? ? 
# 
_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              4Q06 
_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 4Q06 SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 4Q06 GLN A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 4Q06 LEU A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 4Q06 VAL A 130 ? UNP P00918 PHE 130 'engineered mutation' 130 4 
1 4Q06 LEU A 134 ? UNP P00918 VAL 134 'engineered mutation' 134 5 
1 4Q06 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 
V90 non-polymer         . '2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' ? 
'C16 H23 F3 N2 O3 S2' 412.491 
VAL 'L-peptide linking' y VALINE                                                                               ? 'C5 H11 N O2' 
117.146 
ZN  non-polymer         . 'ZINC ION'                                                                           ? 'Zn 2' 65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4Q06 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   38.9 
_exptl_crystal.density_Matthews      2.03 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate, VAPOR DIFFUSION, SITTING DROP, temperature 291K
;
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'PSI PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   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                     4Q06 
_reflns.d_resolution_high            1.149 
_reflns.d_resolution_low             70.006 
_reflns.number_all                   ? 
_reflns.number_obs                   77998 
_reflns.pdbx_netI_over_sigmaI        14.700 
_reflns.pdbx_Rsym_value              0.063 
_reflns.pdbx_redundancy              7.000 
_reflns.percent_possible_obs         91.400 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.B_iso_Wilson_estimate        10.186 
_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  ? 59789 ? 0.189 4.0  0.189 ? 6.70 ? 8923  72.00 1  1 
1.21 1.28  ? 75741 ? 0.151 4.9  0.151 ? 7.00 ? 10851 92.40 2  1 
1.28 1.37  ? 71392 ? 0.119 6.1  0.119 ? 7.00 ? 10198 92.50 3  1 
1.37 1.48  ? 68043 ? 0.094 7.6  0.094 ? 7.00 ? 9732  94.40 4  1 
1.48 1.63  ? 62109 ? 0.077 8.8  0.077 ? 7.00 ? 8899  94.10 5  1 
1.63 1.82  ? 58117 ? 0.067 10.1 0.067 ? 7.00 ? 8257  96.10 6  1 
1.82 2.10  ? 50959 ? 0.062 10.5 0.062 ? 7.00 ? 7255  95.80 7  1 
2.10 2.57  ? 44139 ? 0.058 11.7 0.058 ? 7.00 ? 6286  97.60 8  1 
2.57 3.63  ? 34072 ? 0.058 10.3 0.058 ? 7.00 ? 4851  97.10 9  1 
3.63 70.01 ? 18738 ? 0.061 9.2  0.061 ? 6.80 ? 2746  97.20 10 1 
# 
_refine.entry_id                                 4Q06 
_refine.ls_d_res_high                            1.150 
_refine.ls_d_res_low                             40.740 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    91.010 
_refine.ls_number_reflns_obs                     77978 
_refine.ls_number_reflns_all                     77978 
_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                          0.140 
_refine.ls_R_factor_obs                          0.140 
_refine.ls_R_factor_R_work                       0.137 
_refine.ls_wR_factor_R_work                      0.146 
_refine.ls_R_factor_R_free                       0.168 
_refine.ls_wR_factor_R_free                      0.186 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  7910 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.922 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.080 
_refine.aniso_B[2][2]                            -0.150 
_refine.aniso_B[3][3]                            0.010 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.120 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.978 
_refine.correlation_coeff_Fo_to_Fc_free          0.971 
_refine.overall_SU_R_Cruickshank_DPI             0.039 
_refine.overall_SU_R_free                        0.040 
_refine.pdbx_overall_ESU_R                       0.039 
_refine.pdbx_overall_ESU_R_Free                  0.040 
_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                   0.929 
_refine.B_iso_max                                114.93 
_refine.B_iso_min                                5.74 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.01 
_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        2055 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             292 
_refine_hist.number_atoms_total               2389 
_refine_hist.d_res_high                       1.150 
_refine_hist.d_res_low                        40.740 
# 
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       2358 0.024  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    3231 2.448  1.971  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 302  7.018  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 104  36.144 25.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 392  14.055 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 7    20.563 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         333  0.168  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   1858 0.014  0.021  ? ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr     2358 8.976  3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_free      293  22.712 5.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded    2275 14.336 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               56.650 
_refine_ls_shell.number_reflns_R_work             3207 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.162 
_refine_ls_shell.R_factor_R_free                  0.199 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             384 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                3591 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4Q06 
_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        4Q06 
_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   ? 
# 
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 ? GLU A 14 ? GLY A 12 GLU A 14 5 ? 3 
HELX_P HELX_P2 2 HIS A 15 ? PHE A 20 ? HIS A 15 PHE A 20 1 ? 6 
HELX_P HELX_P3 3 PRO A 21 ? GLY A 25 ? PRO A 21 GLY A 25 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.973 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E V90 . N11 ? ? A ZN  301 A V90 304 1_555 ? ? ? ? ? ? ? 1.895 ? ? 
# 
_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 -2.57 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 15.96 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2 ? 
B ? 5 ? 
C ? 4 ? 
# 
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 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
B 4 5 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-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 ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 3 TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 4 PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 5 SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
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 
# 
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 2 3 O VAL A 121 ? O VAL A 121 N LEU A 91  ? N LEU A 91  
B 3 4 O LEU A 91  ? O LEU A 91  N PHE A 70  ? N PHE A 70  
B 4 5 O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
C 1 2 N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
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 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A DMS 302 ? 4  'BINDING SITE FOR RESIDUE DMS A 302' 
AC3 Software A BCN 303 ? 7  'BINDING SITE FOR RESIDUE BCN A 303' 
AC4 Software A V90 304 ? 14 'BINDING SITE FOR RESIDUE V90 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  V90 E .   ? V90 A 304 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 242 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 244 . ? 1_555 ? 
8  AC2 4  HOH F .   ? HOH A 594 . ? 1_555 ? 
9  AC3 7  LYS A 148 ? LYS A 148 . ? 1_555 ? 
10 AC3 7  LYS A 212 ? LYS A 212 . ? 1_555 ? 
11 AC3 7  GLU A 213 ? GLU A 213 . ? 1_555 ? 
12 AC3 7  PRO A 214 ? PRO A 214 . ? 1_555 ? 
13 AC3 7  HOH F .   ? HOH A 472 . ? 1_555 ? 
14 AC3 7  HOH F .   ? HOH A 644 . ? 1_555 ? 
15 AC3 7  HOH F .   ? HOH A 688 . ? 1_555 ? 
16 AC4 14 TYR A 7   ? TYR A 7   . ? 1_555 ? 
17 AC4 14 ASN A 62  ? ASN A 62  . ? 1_555 ? 
18 AC4 14 HIS A 64  ? HIS A 64  . ? 1_555 ? 
19 AC4 14 SER A 65  ? SER A 65  . ? 1_555 ? 
20 AC4 14 GLN A 92  ? GLN A 92  . ? 1_555 ? 
21 AC4 14 HIS A 94  ? HIS A 94  . ? 1_555 ? 
22 AC4 14 HIS A 96  ? HIS A 96  . ? 1_555 ? 
23 AC4 14 HIS A 119 ? HIS A 119 . ? 1_555 ? 
24 AC4 14 VAL A 121 ? VAL A 121 . ? 1_555 ? 
25 AC4 14 LEU A 197 ? LEU A 197 . ? 1_555 ? 
26 AC4 14 THR A 198 ? THR A 198 . ? 1_555 ? 
27 AC4 14 THR A 199 ? THR A 199 . ? 1_555 ? 
28 AC4 14 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
29 AC4 14 HOH F .   ? HOH A 479 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4Q06 
_atom_sites.fract_transf_matrix[1][1]   0.023801 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005996 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024188 
_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]   0.014284 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 3   ? 7.242   2.765   8.670   1.00  34.17  ? 3   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 3   ? 8.553   2.661   8.056   1.00  37.00  ? 3   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 3   ? 8.793   1.317   7.587   1.00  38.95  ? 3   HIS A C   1 
ATOM   4    O  O   . HIS A 1 3   ? 8.361   0.807   6.530   1.00  69.92  ? 3   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 3   ? 9.637   3.067   9.049   1.00  22.50  ? 3   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 3   ? 9.122   3.877   10.214  1.00  59.57  ? 3   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 3   ? 8.426   5.017   10.051  1.00  77.38  ? 3   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 3   ? 9.225   3.673   11.589  1.00  88.12  ? 3   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 3   ? 8.100   5.519   11.257  1.00  114.93 ? 3   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 3   ? 8.589   4.695   12.197  1.00  106.67 ? 3   HIS A NE2 1 
ATOM   11   N  N   . HIS A 1 4   ? 9.549   0.748   8.482   1.00  51.49  ? 4   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 4   ? 10.001  -0.510  8.304   1.00  43.00  ? 4   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 4   ? 9.371   -1.308  9.386   1.00  22.55  ? 4   HIS A C   1 
ATOM   14   O  O   . HIS A 1 4   ? 9.700   -2.458  9.358   1.00  27.01  ? 4   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 4   ? 11.537  -0.501  8.366   1.00  41.49  ? 4   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 4   ? 12.055  -0.431  9.784   1.00  64.98  ? 4   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 4   ? 11.783  0.622   10.600  1.00  59.67  ? 4   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 4   ? 12.787  -1.346  10.548  1.00  90.41  ? 4   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 4   ? 12.318  0.395   11.814  1.00  48.32  ? 4   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 4   ? 12.929  -0.813  11.781  1.00  79.14  ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 8.489   -0.773  10.291  1.00  21.01  ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 7.826   -1.638  11.247  1.00  15.70  ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 6.819   -2.439  10.493  1.00  15.60  ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 6.281   -1.999  9.487   1.00  17.59  ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 7.252   -0.927  12.430  1.00  16.55  ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 6.011   -0.109  12.078  1.00  16.10  ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 6.023   1.257   11.810  1.00  20.47  ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 4.644   -0.549  12.039  1.00  15.72  ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 4.780   1.652   11.559  1.00  20.75  ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 3.888   0.644   11.726  1.00  16.68  ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 3.997   -1.742  12.300  1.00  13.80  ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 2.533   0.612   11.553  1.00  18.75  ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 2.587   -1.807  12.140  1.00  15.91  ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 1.871   -0.594  11.832  1.00  17.76  ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 6.529   -3.620  10.990  1.00  14.25  ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 5.470   -4.430  10.371  1.00  15.03  ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 5.200   -5.545  11.384  1.00  13.31  ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 5.221   -5.337  12.588  1.00  13.77  ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 7   ? 4.903   -6.687  10.807  1.00  14.51  ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 7   ? 4.511   -7.835  11.663  1.00  14.32  ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 7   ? 5.454   -9.061  11.603  1.00  19.50  ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 7   ? 5.170   -10.121 12.339  1.00  22.49  ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 7   ? 3.026   -8.165  11.377  1.00  14.78  ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 7   ? 2.101   -7.100  11.875  1.00  12.08  ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 7   ? 1.719   -7.087  13.223  1.00  11.29  ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 7   ? 1.640   -6.111  11.040  1.00  12.70  ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 7   ? 0.874   -6.083  13.701  1.00  10.36  ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 7   ? 0.826   -5.088  11.507  1.00  11.46  ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 7   ? 0.425   -5.140  12.845  1.00  11.16  ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 7   ? -0.425  -4.137  13.253  1.00  10.95  ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 8   ? 6.526   -8.936  10.820  1.00  20.72  ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 8   ? 7.455   -10.151 10.612  1.00  23.48  ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 8   ? 8.461   -10.326 11.718  1.00  21.53  ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 8   ? 8.564   -9.559  12.694  1.00  21.29  ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 9   ? 9.326   -11.303 11.529  1.00  22.84  ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 10.333  -11.645 12.559  1.00  25.26  ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 11.286  -10.497 12.798  1.00  19.88  ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 11.795  -10.401 13.954  1.00  23.74  ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 11.203  -12.808 12.128  1.00  23.62  ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 12.054  -13.481 13.214  1.00  33.66  ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 12.942  -14.551 12.595  0.010 21.93  ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 13.982  -15.064 13.579  0.010 19.42  ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 14.899  -16.056 12.948  0.010 21.54  ? 9   LYS A NZ  1 
ATOM   64   N  N   . HIS A 1 10  ? 11.653  -9.764  11.697  1.00  21.25  ? 10  HIS A N   1 
ATOM   65   C  CA  . HIS A 1 10  ? 12.683  -8.810  11.824  1.00  23.49  ? 10  HIS A CA  1 
ATOM   66   C  C   . HIS A 1 10  ? 12.122  -7.469  12.085  1.00  18.02  ? 10  HIS A C   1 
ATOM   67   O  O   . HIS A 1 10  ? 12.904  -6.605  12.463  1.00  22.77  ? 10  HIS A O   1 
ATOM   68   C  CB  . HIS A 1 10  ? 13.548  -8.869  10.565  1.00  26.13  ? 10  HIS A CB  1 
ATOM   69   C  CG  . HIS A 1 10  ? 14.147  -10.212 10.352  1.00  29.28  ? 10  HIS A CG  1 
ATOM   70   N  ND1 . HIS A 1 10  ? 15.155  -10.703 11.132  1.00  32.03  ? 10  HIS A ND1 1 
ATOM   71   C  CD2 . HIS A 1 10  ? 13.776  -11.194 9.492   1.00  32.08  ? 10  HIS A CD2 1 
ATOM   72   C  CE1 . HIS A 1 10  ? 15.448  -11.942 10.722  1.00  29.33  ? 10  HIS A CE1 1 
ATOM   73   N  NE2 . HIS A 1 10  ? 14.607  -12.245 9.693   1.00  32.02  ? 10  HIS A NE2 1 
ATOM   74   N  N   . ASN A 1 11  ? 10.749  -7.281  11.900  1.00  18.44  ? 11  ASN A N   1 
ATOM   75   C  CA  . ASN A 1 11  ? 10.190  -5.949  12.080  1.00  17.83  ? 11  ASN A CA  1 
ATOM   76   C  C   . ASN A 1 11  ? 8.889   -5.881  12.875  1.00  15.37  ? 11  ASN A C   1 
ATOM   77   O  O   . ASN A 1 11  ? 8.272   -4.820  12.961  1.00  14.97  ? 11  ASN A O   1 
ATOM   78   C  CB  . ASN A 1 11  ? 9.947   -5.214  10.748  1.00  17.88  ? 11  ASN A CB  1 
ATOM   79   C  CG  . ASN A 1 11  ? 8.900   -5.813  9.895   1.00  19.30  ? 11  ASN A CG  1 
ATOM   80   O  OD1 . ASN A 1 11  ? 8.337   -6.838  10.219  1.00  20.36  ? 11  ASN A OD1 1 
ATOM   81   N  ND2 . ASN A 1 11  ? 8.632   -5.166  8.726   1.00  21.15  ? 11  ASN A ND2 1 
ATOM   82   N  N   . GLY A 1 12  ? 8.575   -6.983  13.564  1.00  14.81  ? 12  GLY A N   1 
ATOM   83   C  CA  . GLY A 1 12  ? 7.337   -7.128  14.251  1.00  15.32  ? 12  GLY A CA  1 
ATOM   84   C  C   . GLY A 1 12  ? 7.338   -6.575  15.632  1.00  13.06  ? 12  GLY A C   1 
ATOM   85   O  O   . GLY A 1 12  ? 8.217   -5.861  16.071  1.00  13.41  ? 12  GLY A O   1 
ATOM   86   N  N   . PRO A 1 13  ? 6.209   -6.868  16.337  1.00  11.51  ? 13  PRO A N   1 
ATOM   87   C  CA  . PRO A 1 13  ? 5.951   -6.294  17.659  1.00  12.75  ? 13  PRO A CA  1 
ATOM   88   C  C   . PRO A 1 13  ? 7.087   -6.333  18.601  1.00  13.01  ? 13  PRO A C   1 
ATOM   89   O  O   . PRO A 1 13  ? 7.200   -5.363  19.388  1.00  13.38  ? 13  PRO A O   1 
ATOM   90   C  CB  . PRO A 1 13  ? 4.797   -7.130  18.175  1.00  12.17  ? 13  PRO A CB  1 
ATOM   91   C  CG  . PRO A 1 13  ? 3.956   -7.334  16.947  1.00  11.94  ? 13  PRO A CG  1 
ATOM   92   C  CD  . PRO A 1 13  ? 5.028   -7.661  15.871  1.00  12.88  ? 13  PRO A CD  1 
ATOM   93   N  N   . GLU A 1 14  ? 7.946   -7.360  18.608  1.00  13.49  ? 14  GLU A N   1 
ATOM   94   C  CA  . GLU A 1 14  ? 9.066   -7.378  19.548  1.00  15.86  ? 14  GLU A CA  1 
ATOM   95   C  C   . GLU A 1 14  ? 10.171  -6.406  19.228  1.00  14.75  ? 14  GLU A C   1 
ATOM   96   O  O   . GLU A 1 14  ? 11.034  -6.238  20.074  1.00  16.11  ? 14  GLU A O   1 
ATOM   97   C  CB  . GLU A 1 14  ? 9.632   -8.807  19.563  1.00  19.20  ? 14  GLU A CB  1 
ATOM   98   C  CG  . GLU A 1 14  ? 8.697   -9.896  20.053  1.00  25.92  ? 14  GLU A CG  1 
ATOM   99   C  CD  . GLU A 1 14  ? 7.855   -9.494  21.242  1.00  32.08  ? 14  GLU A CD  1 
ATOM   100  O  OE1 . GLU A 1 14  ? 6.619   -9.434  21.098  1.00  40.03  ? 14  GLU A OE1 1 
ATOM   101  O  OE2 . GLU A 1 14  ? 8.431   -9.272  22.327  1.00  48.66  ? 14  GLU A OE2 1 
ATOM   102  N  N   . HIS A 1 15  ? 10.132  -5.795  18.047  1.00  12.50  ? 15  HIS A N   1 
ATOM   103  C  CA  . HIS A 1 15  ? 11.106  -4.802  17.641  1.00  13.00  ? 15  HIS A CA  1 
ATOM   104  C  C   . HIS A 1 15  ? 10.638  -3.405  17.827  1.00  12.32  ? 15  HIS A C   1 
ATOM   105  O  O   . HIS A 1 15  ? 11.464  -2.472  17.772  1.00  13.44  ? 15  HIS A O   1 
ATOM   106  C  CB  . HIS A 1 15  ? 11.480  -5.000  16.176  1.00  14.24  ? 15  HIS A CB  1 
ATOM   107  C  CG  . HIS A 1 15  ? 12.221  -6.253  15.934  1.00  16.27  ? 15  HIS A CG  1 
ATOM   108  N  ND1 . HIS A 1 15  ? 13.586  -6.321  16.014  1.00  18.24  ? 15  HIS A ND1 1 
ATOM   109  C  CD2 . HIS A 1 15  ? 11.750  -7.491  15.586  1.00  18.42  ? 15  HIS A CD2 1 
ATOM   110  C  CE1 . HIS A 1 15  ? 13.948  -7.551  15.680  1.00  22.35  ? 15  HIS A CE1 1 
ATOM   111  N  NE2 . HIS A 1 15  ? 12.842  -8.284  15.438  1.00  19.51  ? 15  HIS A NE2 1 
ATOM   112  N  N   . TRP A 1 16  ? 9.310   -3.184  17.970  1.00  11.20  ? 16  TRP A N   1 
ATOM   113  C  CA  . TRP A 1 16  ? 8.794   -1.813  17.898  1.00  10.85  ? 16  TRP A CA  1 
ATOM   114  C  C   . TRP A 1 16  ? 9.357   -0.851  18.919  1.00  10.62  ? 16  TRP A C   1 
ATOM   115  O  O   . TRP A 1 16  ? 9.455   0.330   18.662  1.00  11.89  ? 16  TRP A O   1 
ATOM   116  C  CB  . TRP A 1 16  ? 7.272   -1.839  17.990  1.00  10.64  ? 16  TRP A CB  1 
ATOM   117  C  CG  . TRP A 1 16  ? 6.602   -2.547  16.854  1.00  10.41  ? 16  TRP A CG  1 
ATOM   118  C  CD1 . TRP A 1 16  ? 7.160   -3.046  15.674  1.00  10.59  ? 16  TRP A CD1 1 
ATOM   119  C  CD2 . TRP A 1 16  ? 5.193   -2.877  16.783  1.00  9.54   ? 16  TRP A CD2 1 
ATOM   120  N  NE1 . TRP A 1 16  ? 6.177   -3.605  14.891  1.00  11.29  ? 16  TRP A NE1 1 
ATOM   121  C  CE2 . TRP A 1 16  ? 4.972   -3.517  15.520  1.00  9.45   ? 16  TRP A CE2 1 
ATOM   122  C  CE3 . TRP A 1 16  ? 4.114   -2.703  17.668  1.00  9.64   ? 16  TRP A CE3 1 
ATOM   123  C  CZ2 . TRP A 1 16  ? 3.666   -3.962  15.135  1.00  9.78   ? 16  TRP A CZ2 1 
ATOM   124  C  CZ3 . TRP A 1 16  ? 2.846   -3.119  17.286  1.00  9.98   ? 16  TRP A CZ3 1 
ATOM   125  C  CH2 . TRP A 1 16  ? 2.635   -3.739  16.057  1.00  10.70  ? 16  TRP A CH2 1 
ATOM   126  N  N   . HIS A 1 17  ? 9.709   -1.387  20.078  1.00  11.49  ? 17  HIS A N   1 
ATOM   127  C  CA  . HIS A 1 17  ? 10.226  -0.533  21.147  1.00  11.83  ? 17  HIS A CA  1 
ATOM   128  C  C   . HIS A 1 17  ? 11.447  0.250   20.729  1.00  13.55  ? 17  HIS A C   1 
ATOM   129  O  O   . HIS A 1 17  ? 11.754  1.295   21.361  1.00  14.29  ? 17  HIS A O   1 
ATOM   130  C  CB  . HIS A 1 17  ? 10.483  -1.328  22.425  1.00  14.88  ? 17  HIS A CB  1 
ATOM   131  C  CG  . HIS A 1 17  ? 11.702  -2.161  22.322  1.00  14.76  ? 17  HIS A CG  1 
ATOM   132  N  ND1 . HIS A 1 17  ? 12.933  -1.778  22.844  1.00  17.17  ? 17  HIS A ND1 1 
ATOM   133  C  CD2 . HIS A 1 17  ? 11.859  -3.371  21.763  1.00  15.12  ? 17  HIS A CD2 1 
ATOM   134  C  CE1 . HIS A 1 17  ? 13.860  -2.709  22.557  1.00  19.33  ? 17  HIS A CE1 1 
ATOM   135  N  NE2 . HIS A 1 17  ? 13.247  -3.703  21.876  1.00  17.68  ? 17  HIS A NE2 1 
ATOM   136  N  N   . LYS A 1 18  ? 12.248  -0.268  19.786  1.00  13.76  ? 18  LYS A N   1 
ATOM   137  C  CA  . LYS A 1 18  ? 13.478  0.494   19.410  1.00  16.13  ? 18  LYS A CA  1 
ATOM   138  C  C   . LYS A 1 18  ? 13.138  1.834   18.775  1.00  17.39  ? 18  LYS A C   1 
ATOM   139  O  O   . LYS A 1 18  ? 13.807  2.835   19.042  1.00  21.64  ? 18  LYS A O   1 
ATOM   140  C  CB  . LYS A 1 18  ? 14.331  -0.339  18.498  1.00  15.06  ? 18  LYS A CB  1 
ATOM   141  C  CG  . LYS A 1 18  ? 14.899  -1.575  19.183  1.00  16.13  ? 18  LYS A CG  1 
ATOM   142  C  CD  . LYS A 1 18  ? 15.674  -2.459  18.237  1.00  16.06  ? 18  LYS A CD  1 
ATOM   143  C  CE  . LYS A 1 18  ? 14.737  -3.471  17.654  1.00  16.19  ? 18  LYS A CE  1 
ATOM   144  N  NZ  . LYS A 1 18  ? 15.416  -4.294  16.619  1.00  15.83  ? 18  LYS A NZ  1 
ATOM   145  N  N   A ASP A 1 19  ? 12.068  1.845   17.982  0.50  16.37  ? 19  ASP A N   1 
ATOM   146  N  N   B ASP A 1 19  ? 12.103  1.943   17.960  0.50  15.18  ? 19  ASP A N   1 
ATOM   147  C  CA  A ASP A 1 19  ? 11.647  3.065   17.320  0.50  17.02  ? 19  ASP A CA  1 
ATOM   148  C  CA  B ASP A 1 19  ? 11.759  3.264   17.440  0.50  16.87  ? 19  ASP A CA  1 
ATOM   149  C  C   A ASP A 1 19  ? 10.597  3.808   18.078  0.50  15.50  ? 19  ASP A C   1 
ATOM   150  C  C   B ASP A 1 19  ? 10.706  3.922   18.338  0.50  15.51  ? 19  ASP A C   1 
ATOM   151  O  O   A ASP A 1 19  ? 10.398  5.004   17.740  0.50  13.58  ? 19  ASP A O   1 
ATOM   152  O  O   B ASP A 1 19  ? 10.609  5.144   18.399  0.50  14.74  ? 19  ASP A O   1 
ATOM   153  C  CB  A ASP A 1 19  ? 11.091  2.832   15.927  0.50  18.51  ? 19  ASP A CB  1 
ATOM   154  C  CB  B ASP A 1 19  ? 11.273  3.192   15.986  0.50  17.04  ? 19  ASP A CB  1 
ATOM   155  C  CG  A ASP A 1 19  ? 12.130  3.120   14.854  0.50  18.60  ? 19  ASP A CG  1 
ATOM   156  C  CG  B ASP A 1 19  ? 12.313  2.539   15.030  0.50  23.48  ? 19  ASP A CG  1 
ATOM   157  O  OD1 A ASP A 1 19  ? 13.242  3.545   15.226  0.50  19.05  ? 19  ASP A OD1 1 
ATOM   158  O  OD1 B ASP A 1 19  ? 13.155  3.309   14.561  0.50  28.60  ? 19  ASP A OD1 1 
ATOM   159  O  OD2 A ASP A 1 19  ? 11.862  2.895   13.681  0.50  29.46  ? 19  ASP A OD2 1 
ATOM   160  O  OD2 B ASP A 1 19  ? 12.332  1.295   14.773  0.50  24.13  ? 19  ASP A OD2 1 
ATOM   161  N  N   . PHE A 1 20  ? 9.915   3.144   19.034  1.00  13.71  ? 20  PHE A N   1 
ATOM   162  C  CA  . PHE A 1 20  ? 8.772   3.678   19.752  1.00  13.29  ? 20  PHE A CA  1 
ATOM   163  C  C   . PHE A 1 20  ? 8.893   3.195   21.176  1.00  12.92  ? 20  PHE A C   1 
ATOM   164  O  O   . PHE A 1 20  ? 8.255   2.203   21.534  1.00  13.34  ? 20  PHE A O   1 
ATOM   165  C  CB  . PHE A 1 20  ? 7.446   3.238   19.113  1.00  14.07  ? 20  PHE A CB  1 
ATOM   166  C  CG  . PHE A 1 20  ? 7.346   3.680   17.701  1.00  16.33  ? 20  PHE A CG  1 
ATOM   167  C  CD1 . PHE A 1 20  ? 6.993   4.979   17.392  1.00  20.08  ? 20  PHE A CD1 1 
ATOM   168  C  CD2 . PHE A 1 20  ? 7.712   2.775   16.703  1.00  18.43  ? 20  PHE A CD2 1 
ATOM   169  C  CE1 . PHE A 1 20  ? 6.979   5.384   16.023  1.00  19.90  ? 20  PHE A CE1 1 
ATOM   170  C  CE2 . PHE A 1 20  ? 7.725   3.125   15.376  1.00  20.23  ? 20  PHE A CE2 1 
ATOM   171  C  CZ  . PHE A 1 20  ? 7.331   4.435   15.049  1.00  21.33  ? 20  PHE A CZ  1 
ATOM   172  N  N   . PRO A 1 21  ? 9.772   3.779   22.038  1.00  14.26  ? 21  PRO A N   1 
ATOM   173  C  CA  . PRO A 1 21  ? 10.001  3.278   23.375  1.00  14.57  ? 21  PRO A CA  1 
ATOM   174  C  C   . PRO A 1 21  ? 8.778   3.169   24.256  1.00  12.88  ? 21  PRO A C   1 
ATOM   175  O  O   . PRO A 1 21  ? 8.812   2.403   25.226  1.00  13.99  ? 21  PRO A O   1 
ATOM   176  C  CB  . PRO A 1 21  ? 11.015  4.281   24.018  1.00  17.95  ? 21  PRO A CB  1 
ATOM   177  C  CG  . PRO A 1 21  ? 11.113  5.339   23.042  1.00  23.36  ? 21  PRO A CG  1 
ATOM   178  C  CD  . PRO A 1 21  ? 10.668  4.924   21.728  1.00  16.18  ? 21  PRO A CD  1 
ATOM   179  N  N   A ILE A 1 22  ? 7.693   3.954   24.076  0.50  11.86  ? 22  ILE A N   1 
ATOM   180  N  N   B ILE A 1 22  ? 7.716   3.904   23.863  0.50  12.65  ? 22  ILE A N   1 
ATOM   181  C  CA  A ILE A 1 22  ? 6.487   3.752   24.883  0.50  12.57  ? 22  ILE A CA  1 
ATOM   182  C  CA  B ILE A 1 22  ? 6.473   3.854   24.559  0.50  11.19  ? 22  ILE A CA  1 
ATOM   183  C  C   A ILE A 1 22  ? 5.932   2.338   24.693  0.50  11.07  ? 22  ILE A C   1 
ATOM   184  C  C   B ILE A 1 22  ? 5.853   2.466   24.455  0.50  10.71  ? 22  ILE A C   1 
ATOM   185  O  O   A ILE A 1 22  ? 5.016   1.955   25.500  0.50  9.66   ? 22  ILE A O   1 
ATOM   186  O  O   B ILE A 1 22  ? 4.906   2.156   25.136  0.50  10.08  ? 22  ILE A O   1 
ATOM   187  C  CB  A ILE A 1 22  ? 5.399   4.750   24.434  0.50  10.62  ? 22  ILE A CB  1 
ATOM   188  C  CB  B ILE A 1 22  ? 5.489   4.958   24.100  0.50  11.02  ? 22  ILE A CB  1 
ATOM   189  C  CG1 A ILE A 1 22  ? 4.322   4.998   25.488  0.50  13.78  ? 22  ILE A CG1 1 
ATOM   190  C  CG1 B ILE A 1 22  ? 4.505   5.239   25.239  0.50  9.58   ? 22  ILE A CG1 1 
ATOM   191  C  CG2 A ILE A 1 22  ? 4.742   4.344   23.097  0.50  11.18  ? 22  ILE A CG2 1 
ATOM   192  C  CG2 B ILE A 1 22  ? 4.826   4.620   22.752  0.50  10.07  ? 22  ILE A CG2 1 
ATOM   193  C  CD1 A ILE A 1 22  ? 4.758   5.965   26.527  0.50  18.19  ? 22  ILE A CD1 1 
ATOM   194  C  CD1 B ILE A 1 22  ? 3.552   6.359   25.028  0.50  12.30  ? 22  ILE A CD1 1 
ATOM   195  N  N   . ALA A 1 23  ? 6.405   1.576   23.648  1.00  10.76  ? 23  ALA A N   1 
ATOM   196  C  CA  . ALA A 1 23  ? 5.947   0.193   23.540  1.00  11.15  ? 23  ALA A CA  1 
ATOM   197  C  C   . ALA A 1 23  ? 6.077   -0.572  24.842  1.00  10.99  ? 23  ALA A C   1 
ATOM   198  O  O   . ALA A 1 23  ? 5.369   -1.526  25.019  1.00  11.76  ? 23  ALA A O   1 
ATOM   199  C  CB  . ALA A 1 23  ? 6.797   -0.557  22.467  1.00  11.26  ? 23  ALA A CB  1 
ATOM   200  N  N   . LYS A 1 24  ? 6.969   -0.111  25.747  1.00  13.16  ? 24  LYS A N   1 
ATOM   201  C  CA  . LYS A 1 24  ? 7.161   -0.735  27.048  1.00  13.64  ? 24  LYS A CA  1 
ATOM   202  C  C   . LYS A 1 24  ? 6.560   0.164   28.122  1.00  13.68  ? 24  LYS A C   1 
ATOM   203  O  O   . LYS A 1 24  ? 6.942   0.051   29.302  1.00  16.27  ? 24  LYS A O   1 
ATOM   204  C  CB  . LYS A 1 24  ? 8.625   -1.023  27.381  1.00  14.98  ? 24  LYS A CB  1 
ATOM   205  C  CG  . LYS A 1 24  ? 9.283   -1.945  26.386  1.00  17.40  ? 24  LYS A CG  1 
ATOM   206  C  CD  . LYS A 1 24  ? 10.696  -2.199  26.855  1.00  21.35  ? 24  LYS A CD  1 
ATOM   207  C  CE  . LYS A 1 24  ? 11.497  -3.034  25.898  1.00  25.11  ? 24  LYS A CE  1 
ATOM   208  N  NZ  . LYS A 1 24  ? 10.967  -4.420  25.795  1.00  26.82  ? 24  LYS A NZ  1 
ATOM   209  N  N   . GLY A 1 25  ? 5.531   0.955   27.779  1.00  12.93  ? 25  GLY A N   1 
ATOM   210  C  CA  . GLY A 1 25  ? 4.972   1.935   28.711  1.00  13.92  ? 25  GLY A CA  1 
ATOM   211  C  C   . GLY A 1 25  ? 3.988   1.288   29.666  1.00  12.64  ? 25  GLY A C   1 
ATOM   212  O  O   . GLY A 1 25  ? 3.795   0.070   29.756  1.00  13.54  ? 25  GLY A O   1 
ATOM   213  N  N   . GLU A 1 26  ? 3.350   2.201   30.360  1.00  13.11  ? 26  GLU A N   1 
ATOM   214  C  CA  . GLU A 1 26  ? 2.446   1.831   31.472  1.00  13.60  ? 26  GLU A CA  1 
ATOM   215  C  C   . GLU A 1 26  ? 1.015   1.579   31.075  1.00  11.16  ? 26  GLU A C   1 
ATOM   216  O  O   . GLU A 1 26  ? 0.261   1.079   31.908  1.00  12.80  ? 26  GLU A O   1 
ATOM   217  C  CB  . GLU A 1 26  ? 2.494   2.992   32.502  1.00  15.92  ? 26  GLU A CB  1 
ATOM   218  C  CG  . GLU A 1 26  ? 3.870   3.200   33.124  1.00  17.32  ? 26  GLU A CG  1 
ATOM   219  C  CD  . GLU A 1 26  ? 4.470   1.899   33.736  1.00  25.11  ? 26  GLU A CD  1 
ATOM   220  O  OE1 . GLU A 1 26  ? 3.750   1.235   34.546  1.00  28.04  ? 26  GLU A OE1 1 
ATOM   221  O  OE2 . GLU A 1 26  ? 5.581   1.509   33.322  1.00  35.41  ? 26  GLU A OE2 1 
ATOM   222  N  N   . ARG A 1 27  ? 0.631   1.890   29.847  1.00  10.08  ? 27  ARG A N   1 
ATOM   223  C  CA  . ARG A 1 27  ? -0.765  1.685   29.480  1.00  9.75   ? 27  ARG A CA  1 
ATOM   224  C  C   . ARG A 1 27  ? -0.866  1.245   28.022  1.00  8.53   ? 27  ARG A C   1 
ATOM   225  O  O   . ARG A 1 27  ? -1.576  1.795   27.178  1.00  8.99   ? 27  ARG A O   1 
ATOM   226  C  CB  . ARG A 1 27  ? -1.714  2.887   29.778  1.00  11.15  ? 27  ARG A CB  1 
ATOM   227  C  CG  . ARG A 1 27  ? -1.227  4.188   29.212  1.00  13.10  ? 27  ARG A CG  1 
ATOM   228  C  CD  . ARG A 1 27  ? -2.246  5.345   29.383  1.00  13.68  ? 27  ARG A CD  1 
ATOM   229  N  NE  . ARG A 1 27  ? -3.419  5.258   28.484  1.00  11.29  ? 27  ARG A NE  1 
ATOM   230  C  CZ  . ARG A 1 27  ? -4.392  6.131   28.469  1.00  10.99  ? 27  ARG A CZ  1 
ATOM   231  N  NH1 . ARG A 1 27  ? -4.420  7.162   29.326  1.00  13.97  ? 27  ARG A NH1 1 
ATOM   232  N  NH2 . ARG A 1 27  ? -5.367  6.033   27.629  1.00  12.63  ? 27  ARG A NH2 1 
ATOM   233  N  N   . GLN A 1 28  ? -0.132  0.172   27.726  1.00  8.60   ? 28  GLN A N   1 
ATOM   234  C  CA  . GLN A 1 28  ? -0.083  -0.393  26.360  1.00  7.82   ? 28  GLN A CA  1 
ATOM   235  C  C   . GLN A 1 28  ? -1.253  -1.361  26.121  1.00  7.52   ? 28  GLN A C   1 
ATOM   236  O  O   . GLN A 1 28  ? -1.768  -2.045  27.020  1.00  8.62   ? 28  GLN A O   1 
ATOM   237  C  CB  . GLN A 1 28  ? 1.239   -1.054  26.125  1.00  8.96   ? 28  GLN A CB  1 
ATOM   238  C  CG  . GLN A 1 28  ? 2.349   -0.018  26.024  1.00  9.54   ? 28  GLN A CG  1 
ATOM   239  C  CD  . GLN A 1 28  ? 2.248   0.765   24.756  1.00  8.28   ? 28  GLN A CD  1 
ATOM   240  O  OE1 . GLN A 1 28  ? 2.444   0.204   23.673  1.00  9.18   ? 28  GLN A OE1 1 
ATOM   241  N  NE2 . GLN A 1 28  ? 1.900   2.059   24.846  1.00  8.76   ? 28  GLN A NE2 1 
ATOM   242  N  N   . SER A 1 29  ? -1.616  -1.443  24.848  1.00  7.44   ? 29  SER A N   1 
ATOM   243  C  CA  . SER A 1 29  ? -2.687  -2.310  24.370  1.00  6.99   ? 29  SER A CA  1 
ATOM   244  C  C   . SER A 1 29  ? -2.148  -3.209  23.260  1.00  6.75   ? 29  SER A C   1 
ATOM   245  O  O   . SER A 1 29  ? -1.169  -2.849  22.580  1.00  7.84   ? 29  SER A O   1 
ATOM   246  C  CB  . SER A 1 29  ? -3.813  -1.467  23.806  1.00  7.47   ? 29  SER A CB  1 
ATOM   247  O  OG  . SER A 1 29  ? -4.427  -0.715  24.866  1.00  7.42   ? 29  SER A OG  1 
ATOM   248  N  N   . PRO A 1 30  ? -2.801  -4.344  22.998  1.00  6.80   ? 30  PRO A N   1 
ATOM   249  C  CA  . PRO A 1 30  ? -3.987  -4.878  23.705  1.00  6.72   ? 30  PRO A CA  1 
ATOM   250  C  C   . PRO A 1 30  ? -3.586  -5.528  25.017  1.00  6.90   ? 30  PRO A C   1 
ATOM   251  O  O   . PRO A 1 30  ? -2.394  -5.563  25.368  1.00  7.61   ? 30  PRO A O   1 
ATOM   252  C  CB  . PRO A 1 30  ? -4.470  -5.910  22.701  1.00  7.28   ? 30  PRO A CB  1 
ATOM   253  C  CG  . PRO A 1 30  ? -3.184  -6.471  22.121  1.00  7.65   ? 30  PRO A CG  1 
ATOM   254  C  CD  . PRO A 1 30  ? -2.307  -5.265  21.970  1.00  7.32   ? 30  PRO A CD  1 
ATOM   255  N  N   . VAL A 1 31  ? -4.582  -6.068  25.705  1.00  7.72   ? 31  VAL A N   1 
ATOM   256  C  CA  . VAL A 1 31  ? -4.400  -6.835  26.945  1.00  7.91   ? 31  VAL A CA  1 
ATOM   257  C  C   . VAL A 1 31  ? -5.271  -8.060  26.884  1.00  7.81   ? 31  VAL A C   1 
ATOM   258  O  O   . VAL A 1 31  ? -6.248  -8.103  26.125  1.00  8.08   ? 31  VAL A O   1 
ATOM   259  C  CB  . VAL A 1 31  ? -4.723  -5.979  28.186  1.00  8.17   ? 31  VAL A CB  1 
ATOM   260  C  CG1 . VAL A 1 31  ? -3.790  -4.786  28.303  1.00  9.84   ? 31  VAL A CG1 1 
ATOM   261  C  CG2 . VAL A 1 31  ? -6.160  -5.545  28.201  1.00  9.17   ? 31  VAL A CG2 1 
ATOM   262  N  N   . ASP A 1 32  ? -4.933  -9.008  27.754  1.00  8.17   ? 32  ASP A N   1 
ATOM   263  C  CA  . ASP A 1 32  ? -5.868  -10.087 28.058  1.00  8.40   ? 32  ASP A CA  1 
ATOM   264  C  C   . ASP A 1 32  ? -6.916  -9.578  29.032  1.00  8.56   ? 32  ASP A C   1 
ATOM   265  O  O   . ASP A 1 32  ? -6.605  -8.884  30.032  1.00  10.45  ? 32  ASP A O   1 
ATOM   266  C  CB  . ASP A 1 32  ? -5.131  -11.258 28.686  1.00  9.66   ? 32  ASP A CB  1 
ATOM   267  C  CG  . ASP A 1 32  ? -6.072  -12.432 28.958  1.00  9.96   ? 32  ASP A CG  1 
ATOM   268  O  OD1 . ASP A 1 32  ? -6.734  -12.899 28.020  1.00  9.21   ? 32  ASP A OD1 1 
ATOM   269  O  OD2 . ASP A 1 32  ? -6.145  -12.868 30.158  1.00  11.68  ? 32  ASP A OD2 1 
ATOM   270  N  N   A ILE A 1 33  ? -8.175  -9.911  28.755  0.50  8.25   ? 33  ILE A N   1 
ATOM   271  N  N   B ILE A 1 33  ? -8.141  -9.864  28.788  0.50  8.30   ? 33  ILE A N   1 
ATOM   272  C  CA  A ILE A 1 33  ? -9.390  -9.595  29.566  0.50  6.85   ? 33  ILE A CA  1 
ATOM   273  C  CA  B ILE A 1 33  ? -9.162  -9.463  29.674  0.50  9.02   ? 33  ILE A CA  1 
ATOM   274  C  C   A ILE A 1 33  ? -9.680  -10.809 30.456  0.50  8.73   ? 33  ILE A C   1 
ATOM   275  C  C   B ILE A 1 33  ? -9.442  -10.760 30.448  0.50  9.12   ? 33  ILE A C   1 
ATOM   276  O  O   A ILE A 1 33  ? -10.311 -11.792 29.988  0.50  7.75   ? 33  ILE A O   1 
ATOM   277  O  O   B ILE A 1 33  ? -9.852  -11.758 29.946  0.50  8.38   ? 33  ILE A O   1 
ATOM   278  C  CB  A ILE A 1 33  ? -10.604 -9.198  28.754  0.50  7.16   ? 33  ILE A CB  1 
ATOM   279  C  CB  B ILE A 1 33  ? -10.328 -9.060  28.865  0.50  8.42   ? 33  ILE A CB  1 
ATOM   280  C  CG1 A ILE A 1 33  ? -10.295 -7.901  27.984  0.50  6.26   ? 33  ILE A CG1 1 
ATOM   281  C  CG1 B ILE A 1 33  ? -9.874  -7.947  27.927  0.50  10.65  ? 33  ILE A CG1 1 
ATOM   282  C  CG2 A ILE A 1 33  ? -11.841 -9.054  29.668  0.50  8.00   ? 33  ILE A CG2 1 
ATOM   283  C  CG2 B ILE A 1 33  ? -11.501 -8.686  29.804  0.50  9.72   ? 33  ILE A CG2 1 
ATOM   284  C  CD1 A ILE A 1 33  ? -11.182 -7.613  26.818  0.50  5.74   ? 33  ILE A CD1 1 
ATOM   285  C  CD1 B ILE A 1 33  ? -10.281 -6.666  28.513  0.50  20.37  ? 33  ILE A CD1 1 
ATOM   286  N  N   . ASP A 1 34  ? -9.223  -10.713 31.740  1.00  10.01  ? 34  ASP A N   1 
ATOM   287  C  CA  . ASP A 1 34  ? -9.500  -11.758 32.674  1.00  11.06  ? 34  ASP A CA  1 
ATOM   288  C  C   . ASP A 1 34  ? -10.922 -11.530 33.174  1.00  11.15  ? 34  ASP A C   1 
ATOM   289  O  O   . ASP A 1 34  ? -11.150 -10.574 33.973  1.00  13.76  ? 34  ASP A O   1 
ATOM   290  C  CB  . ASP A 1 34  ? -8.438  -11.802 33.758  1.00  13.10  ? 34  ASP A CB  1 
ATOM   291  C  CG  . ASP A 1 34  ? -8.618  -12.998 34.586  1.00  15.96  ? 34  ASP A CG  1 
ATOM   292  O  OD1 . ASP A 1 34  ? -9.225  -12.985 35.550  1.00  25.47  ? 34  ASP A OD1 1 
ATOM   293  O  OD2 . ASP A 1 34  ? -8.100  -14.094 34.126  1.00  22.05  ? 34  ASP A OD2 1 
ATOM   294  N  N   . THR A 1 35  ? -11.891 -12.328 32.752  1.00  12.29  ? 35  THR A N   1 
ATOM   295  C  CA  . THR A 1 35  ? -13.265 -12.051 33.000  1.00  14.49  ? 35  THR A CA  1 
ATOM   296  C  C   . THR A 1 35  ? -13.642 -12.209 34.401  1.00  14.37  ? 35  THR A C   1 
ATOM   297  O  O   . THR A 1 35  ? -14.550 -11.511 34.815  1.00  17.54  ? 35  THR A O   1 
ATOM   298  C  CB  . THR A 1 35  ? -14.156 -12.956 32.188  1.00  14.54  ? 35  THR A CB  1 
ATOM   299  O  OG1 . THR A 1 35  ? -14.003 -14.326 32.603  1.00  15.34  ? 35  THR A OG1 1 
ATOM   300  C  CG2 . THR A 1 35  ? -13.901 -12.806 30.719  1.00  16.26  ? 35  THR A CG2 1 
ATOM   301  N  N   . HIS A 1 36  ? -12.916 -13.028 35.177  1.00  14.93  ? 36  HIS A N   1 
ATOM   302  C  CA  . HIS A 1 36  ? -13.236 -13.159 36.568  1.00  17.41  ? 36  HIS A CA  1 
ATOM   303  C  C   . HIS A 1 36  ? -12.740 -12.051 37.383  1.00  22.14  ? 36  HIS A C   1 
ATOM   304  O  O   . HIS A 1 36  ? -13.393 -11.817 38.449  1.00  19.37  ? 36  HIS A O   1 
ATOM   305  C  CB  . HIS A 1 36  ? -12.745 -14.568 37.017  1.00  18.95  ? 36  HIS A CB  1 
ATOM   306  C  CG  . HIS A 1 36  ? -13.661 -15.675 36.495  1.00  19.73  ? 36  HIS A CG  1 
ATOM   307  N  ND1 . HIS A 1 36  ? -14.945 -15.768 36.885  1.00  25.22  ? 36  HIS A ND1 1 
ATOM   308  C  CD2 . HIS A 1 36  ? -13.468 -16.652 35.522  1.00  19.03  ? 36  HIS A CD2 1 
ATOM   309  C  CE1 . HIS A 1 36  ? -15.540 -16.793 36.233  1.00  28.82  ? 36  HIS A CE1 1 
ATOM   310  N  NE2 . HIS A 1 36  ? -14.637 -17.332 35.409  1.00  28.24  ? 36  HIS A NE2 1 
ATOM   311  N  N   . THR A 1 37  ? -11.693 -11.295 36.948  1.00  18.30  ? 37  THR A N   1 
ATOM   312  C  CA  . THR A 1 37  ? -11.159 -10.131 37.634  1.00  18.50  ? 37  THR A CA  1 
ATOM   313  C  C   . THR A 1 37  ? -11.721 -8.772  37.241  1.00  17.65  ? 37  THR A C   1 
ATOM   314  O  O   . THR A 1 37  ? -11.634 -7.815  38.018  1.00  22.71  ? 37  THR A O   1 
ATOM   315  C  CB  . THR A 1 37  ? -9.668  -10.062 37.635  1.00  23.64  ? 37  THR A CB  1 
ATOM   316  O  OG1 . THR A 1 37  ? -9.116  -9.719  36.377  1.00  51.02  ? 37  THR A OG1 1 
ATOM   317  C  CG2 . THR A 1 37  ? -9.214  -11.351 37.955  1.00  22.00  ? 37  THR A CG2 1 
ATOM   318  N  N   . ALA A 1 38  ? -12.316 -8.691  36.071  1.00  14.05  ? 38  ALA A N   1 
ATOM   319  C  CA  . ALA A 1 38  ? -12.933 -7.473  35.651  1.00  13.16  ? 38  ALA A CA  1 
ATOM   320  C  C   . ALA A 1 38  ? -14.153 -7.254  36.523  1.00  18.01  ? 38  ALA A C   1 
ATOM   321  O  O   . ALA A 1 38  ? -15.025 -8.107  36.615  1.00  24.47  ? 38  ALA A O   1 
ATOM   322  C  CB  . ALA A 1 38  ? -13.360 -7.623  34.203  1.00  13.86  ? 38  ALA A CB  1 
ATOM   323  N  N   . LYS A 1 39  ? -14.229 -6.105  37.183  1.00  18.40  ? 39  LYS A N   1 
ATOM   324  C  CA  . LYS A 1 39  ? -15.333 -5.856  38.109  1.00  22.48  ? 39  LYS A CA  1 
ATOM   325  C  C   . LYS A 1 39  ? -16.467 -5.034  37.497  1.00  16.13  ? 39  LYS A C   1 
ATOM   326  O  O   . LYS A 1 39  ? -16.237 -3.942  36.977  1.00  14.34  ? 39  LYS A O   1 
ATOM   327  C  CB  . LYS A 1 39  ? -14.819 -5.171  39.378  1.00  20.87  ? 39  LYS A CB  1 
ATOM   328  C  CG  . LYS A 1 39  ? -15.902 -4.859  40.397  1.00  37.52  ? 39  LYS A CG  1 
ATOM   329  C  CD  . LYS A 1 39  ? -15.346 -4.063  41.567  1.00  29.15  ? 39  LYS A CD  1 
ATOM   330  C  CE  . LYS A 1 39  ? -16.461 -3.548  42.463  1.00  29.50  ? 39  LYS A CE  1 
ATOM   331  N  NZ  . LYS A 1 39  ? -16.850 -4.549  43.495  1.00  29.07  ? 39  LYS A NZ  1 
ATOM   332  N  N   . TYR A 1 40  ? -17.691 -5.555  37.568  1.00  17.23  ? 40  TYR A N   1 
ATOM   333  C  CA  . TYR A 1 40  ? -18.807 -4.820  37.143  1.00  15.00  ? 40  TYR A CA  1 
ATOM   334  C  C   . TYR A 1 40  ? -18.804 -3.456  37.814  1.00  14.65  ? 40  TYR A C   1 
ATOM   335  O  O   . TYR A 1 40  ? -18.716 -3.339  39.069  1.00  16.04  ? 40  TYR A O   1 
ATOM   336  C  CB  . TYR A 1 40  ? -20.087 -5.584  37.597  1.00  17.88  ? 40  TYR A CB  1 
ATOM   337  C  CG  . TYR A 1 40  ? -21.288 -4.811  37.428  1.00  20.34  ? 40  TYR A CG  1 
ATOM   338  C  CD1 . TYR A 1 40  ? -21.618 -4.247  36.202  1.00  19.17  ? 40  TYR A CD1 1 
ATOM   339  C  CD2 . TYR A 1 40  ? -22.149 -4.642  38.503  1.00  25.22  ? 40  TYR A CD2 1 
ATOM   340  C  CE1 . TYR A 1 40  ? -22.761 -3.480  36.068  1.00  21.67  ? 40  TYR A CE1 1 
ATOM   341  C  CE2 . TYR A 1 40  ? -23.322 -3.917  38.354  1.00  28.34  ? 40  TYR A CE2 1 
ATOM   342  C  CZ  . TYR A 1 40  ? -23.643 -3.352  37.143  1.00  28.25  ? 40  TYR A CZ  1 
ATOM   343  O  OH  . TYR A 1 40  ? -24.803 -2.606  37.039  1.00  33.50  ? 40  TYR A OH  1 
ATOM   344  N  N   . ASP A 1 41  ? -19.018 -2.443  37.014  1.00  13.54  ? 41  ASP A N   1 
ATOM   345  C  CA  . ASP A 1 41  ? -19.057 -1.062  37.486  1.00  14.24  ? 41  ASP A CA  1 
ATOM   346  C  C   . ASP A 1 41  ? -20.438 -0.503  37.251  1.00  16.32  ? 41  ASP A C   1 
ATOM   347  O  O   . ASP A 1 41  ? -20.752 -0.087  36.088  1.00  17.44  ? 41  ASP A O   1 
ATOM   348  C  CB  . ASP A 1 41  ? -17.972 -0.206  36.800  1.00  16.79  ? 41  ASP A CB  1 
ATOM   349  C  CG  . ASP A 1 41  ? -17.896 1.159   37.344  1.00  18.16  ? 41  ASP A CG  1 
ATOM   350  O  OD1 . ASP A 1 41  ? -18.804 1.543   38.123  1.00  19.51  ? 41  ASP A OD1 1 
ATOM   351  O  OD2 . ASP A 1 41  ? -16.954 1.888   36.942  1.00  20.66  ? 41  ASP A OD2 1 
ATOM   352  N  N   A PRO A 1 42  ? -21.254 -0.386  38.314  0.50  16.75  ? 42  PRO A N   1 
ATOM   353  N  N   B PRO A 1 42  ? -21.315 -0.553  38.276  0.50  18.74  ? 42  PRO A N   1 
ATOM   354  C  CA  A PRO A 1 42  ? -22.630 0.003   38.072  0.50  20.37  ? 42  PRO A CA  1 
ATOM   355  C  CA  B PRO A 1 42  ? -22.656 0.028   38.172  0.50  22.68  ? 42  PRO A CA  1 
ATOM   356  C  C   A PRO A 1 42  ? -22.727 1.506   37.804  0.50  23.33  ? 42  PRO A C   1 
ATOM   357  C  C   B PRO A 1 42  ? -22.669 1.463   37.657  0.50  20.26  ? 42  PRO A C   1 
ATOM   358  O  O   A PRO A 1 42  ? -23.813 2.025   37.484  0.50  26.25  ? 42  PRO A O   1 
ATOM   359  O  O   B PRO A 1 42  ? -23.671 1.906   37.041  0.50  25.64  ? 42  PRO A O   1 
ATOM   360  C  CB  A PRO A 1 42  ? -23.322 -0.413  39.360  0.50  22.02  ? 42  PRO A CB  1 
ATOM   361  C  CB  B PRO A 1 42  ? -23.127 0.011   39.614  0.50  28.56  ? 42  PRO A CB  1 
ATOM   362  C  CG  A PRO A 1 42  ? -22.266 -0.170  40.428  0.50  18.95  ? 42  PRO A CG  1 
ATOM   363  C  CG  B PRO A 1 42  ? -22.549 -1.254  40.142  0.50  25.23  ? 42  PRO A CG  1 
ATOM   364  C  CD  A PRO A 1 42  ? -20.979 -0.605  39.761  0.50  16.50  ? 42  PRO A CD  1 
ATOM   365  C  CD  B PRO A 1 42  ? -21.160 -1.301  39.553  0.50  21.11  ? 42  PRO A CD  1 
ATOM   366  N  N   . SER A 1 43  ? -21.600 2.199   37.915  1.00  22.07  ? 43  SER A N   1 
ATOM   367  C  CA  . SER A 1 43  ? -21.518 3.631   37.474  1.00  24.51  ? 43  SER A CA  1 
ATOM   368  C  C   . SER A 1 43  ? -21.283 3.862   35.972  1.00  23.28  ? 43  SER A C   1 
ATOM   369  O  O   . SER A 1 43  ? -21.523 4.943   35.494  1.00  31.25  ? 43  SER A O   1 
ATOM   370  C  CB  . SER A 1 43  ? -20.505 4.416   38.255  1.00  26.84  ? 43  SER A CB  1 
ATOM   371  O  OG  . SER A 1 43  ? -19.209 4.141   37.803  1.00  26.94  ? 43  SER A OG  1 
ATOM   372  N  N   . LEU A 1 44  ? -20.900 2.871   35.211  1.00  21.92  ? 44  LEU A N   1 
ATOM   373  C  CA  . LEU A 1 44  ? -20.788 3.016   33.776  1.00  21.82  ? 44  LEU A CA  1 
ATOM   374  C  C   . LEU A 1 44  ? -22.168 3.189   33.146  1.00  27.96  ? 44  LEU A C   1 
ATOM   375  O  O   . LEU A 1 44  ? -23.135 2.741   33.660  1.00  34.83  ? 44  LEU A O   1 
ATOM   376  C  CB  . LEU A 1 44  ? -20.186 1.774   33.184  1.00  18.74  ? 44  LEU A CB  1 
ATOM   377  C  CG  . LEU A 1 44  ? -18.699 1.622   33.402  1.00  16.24  ? 44  LEU A CG  1 
ATOM   378  C  CD1 . LEU A 1 44  ? -18.248 0.224   33.021  1.00  17.43  ? 44  LEU A CD1 1 
ATOM   379  C  CD2 . LEU A 1 44  ? -17.828 2.640   32.667  1.00  16.28  ? 44  LEU A CD2 1 
ATOM   380  N  N   . LYS A 1 45  ? -22.205 3.813   32.001  1.00  23.56  ? 45  LYS A N   1 
ATOM   381  C  CA  . LYS A 1 45  ? -23.426 3.983   31.197  1.00  25.31  ? 45  LYS A CA  1 
ATOM   382  C  C   . LYS A 1 45  ? -23.459 3.155   29.979  1.00  25.29  ? 45  LYS A C   1 
ATOM   383  O  O   . LYS A 1 45  ? -22.445 2.586   29.545  1.00  22.50  ? 45  LYS A O   1 
ATOM   384  C  CB  . LYS A 1 45  ? -23.541 5.378   30.802  1.00  21.91  ? 45  LYS A CB  1 
ATOM   385  C  CG  . LYS A 1 45  ? -23.301 6.304   31.928  1.00  25.33  ? 45  LYS A CG  1 
ATOM   386  C  CD  . LYS A 1 45  ? -23.551 7.748   31.558  1.00  41.23  ? 45  LYS A CD  1 
ATOM   387  C  CE  . LYS A 1 45  ? -24.099 8.519   32.758  1.00  52.20  ? 45  LYS A CE  1 
ATOM   388  N  NZ  . LYS A 1 45  ? -23.305 8.259   33.985  1.00  49.54  ? 45  LYS A NZ  1 
ATOM   389  N  N   . PRO A 1 46  ? -24.735 2.960   29.461  1.00  23.42  ? 46  PRO A N   1 
ATOM   390  C  CA  . PRO A 1 46  ? -24.826 2.239   28.185  1.00  19.73  ? 46  PRO A CA  1 
ATOM   391  C  C   . PRO A 1 46  ? -24.006 2.962   27.157  1.00  15.28  ? 46  PRO A C   1 
ATOM   392  O  O   . PRO A 1 46  ? -23.981 4.129   27.236  1.00  20.57  ? 46  PRO A O   1 
ATOM   393  C  CB  . PRO A 1 46  ? -26.332 2.305   27.874  1.00  24.18  ? 46  PRO A CB  1 
ATOM   394  C  CG  . PRO A 1 46  ? -27.012 2.430   29.213  1.00  29.69  ? 46  PRO A CG  1 
ATOM   395  C  CD  . PRO A 1 46  ? -26.034 3.255   30.049  1.00  24.72  ? 46  PRO A CD  1 
ATOM   396  N  N   . LEU A 1 47  ? -23.385 2.260   26.207  1.00  20.53  ? 47  LEU A N   1 
ATOM   397  C  CA  . LEU A 1 47  ? -22.678 2.979   25.216  1.00  19.82  ? 47  LEU A CA  1 
ATOM   398  C  C   . LEU A 1 47  ? -23.834 3.654   24.378  1.00  20.57  ? 47  LEU A C   1 
ATOM   399  O  O   . LEU A 1 47  ? -24.896 3.106   24.270  1.00  25.06  ? 47  LEU A O   1 
ATOM   400  C  CB  . LEU A 1 47  ? -22.024 2.013   24.235  1.00  23.80  ? 47  LEU A CB  1 
ATOM   401  C  CG  . LEU A 1 47  ? -20.570 1.571   24.330  1.00  28.23  ? 47  LEU A CG  1 
ATOM   402  C  CD1 . LEU A 1 47  ? -20.164 0.910   23.018  1.00  26.30  ? 47  LEU A CD1 1 
ATOM   403  C  CD2 . LEU A 1 47  ? -19.699 2.782   24.600  1.00  30.23  ? 47  LEU A CD2 1 
ATOM   404  N  N   . SER A 1 48  ? -23.522 4.780   23.790  1.00  15.04  ? 48  SER A N   1 
ATOM   405  C  CA  . SER A 1 48  ? -24.286 5.363   22.751  1.00  14.94  ? 48  SER A CA  1 
ATOM   406  C  C   . SER A 1 48  ? -23.518 5.339   21.451  1.00  14.33  ? 48  SER A C   1 
ATOM   407  O  O   . SER A 1 48  ? -22.539 6.095   21.260  1.00  15.37  ? 48  SER A O   1 
ATOM   408  C  CB  . SER A 1 48  ? -24.679 6.781   23.117  1.00  16.49  ? 48  SER A CB  1 
ATOM   409  O  OG  . SER A 1 48  ? -25.306 7.469   22.083  1.00  19.82  ? 48  SER A OG  1 
ATOM   410  N  N   . VAL A 1 49  ? -23.939 4.523   20.527  1.00  15.90  ? 49  VAL A N   1 
ATOM   411  C  CA  . VAL A 1 49  ? -23.352 4.387   19.217  1.00  17.59  ? 49  VAL A CA  1 
ATOM   412  C  C   . VAL A 1 49  ? -24.314 5.003   18.209  1.00  20.21  ? 49  VAL A C   1 
ATOM   413  O  O   . VAL A 1 49  ? -25.392 4.499   17.990  1.00  23.22  ? 49  VAL A O   1 
ATOM   414  C  CB  . VAL A 1 49  ? -23.091 2.901   18.840  1.00  21.35  ? 49  VAL A CB  1 
ATOM   415  C  CG1 . VAL A 1 49  ? -22.417 2.853   17.486  1.00  25.59  ? 49  VAL A CG1 1 
ATOM   416  C  CG2 . VAL A 1 49  ? -22.256 2.227   19.928  1.00  21.73  ? 49  VAL A CG2 1 
ATOM   417  N  N   . SER A 1 50  ? -23.990 6.146   17.654  1.00  18.13  ? 50  SER A N   1 
ATOM   418  C  CA  . SER A 1 50  ? -24.882 6.876   16.736  1.00  22.04  ? 50  SER A CA  1 
ATOM   419  C  C   . SER A 1 50  ? -24.241 6.977   15.401  1.00  19.01  ? 50  SER A C   1 
ATOM   420  O  O   . SER A 1 50  ? -23.502 7.908   15.112  1.00  19.09  ? 50  SER A O   1 
ATOM   421  C  CB  . SER A 1 50  ? -25.284 8.286   17.225  1.00  29.10  ? 50  SER A CB  1 
ATOM   422  O  OG  . SER A 1 50  ? -25.923 8.246   18.475  1.00  32.79  ? 50  SER A OG  1 
ATOM   423  N  N   . TYR A 1 51  ? -24.566 5.983   14.573  1.00  18.68  ? 51  TYR A N   1 
ATOM   424  C  CA  . TYR A 1 51  ? -23.987 5.802   13.282  1.00  21.01  ? 51  TYR A CA  1 
ATOM   425  C  C   . TYR A 1 51  ? -24.970 6.069   12.144  1.00  23.47  ? 51  TYR A C   1 
ATOM   426  O  O   . TYR A 1 51  ? -24.577 5.907   10.978  1.00  22.45  ? 51  TYR A O   1 
ATOM   427  C  CB  . TYR A 1 51  ? -23.381 4.421   13.124  1.00  18.62  ? 51  TYR A CB  1 
ATOM   428  C  CG  . TYR A 1 51  ? -22.081 4.138   13.862  1.00  16.10  ? 51  TYR A CG  1 
ATOM   429  C  CD1 . TYR A 1 51  ? -21.356 5.140   14.526  1.00  16.23  ? 51  TYR A CD1 1 
ATOM   430  C  CD2 . TYR A 1 51  ? -21.594 2.808   13.972  1.00  16.13  ? 51  TYR A CD2 1 
ATOM   431  C  CE1 . TYR A 1 51  ? -20.190 4.837   15.223  1.00  14.37  ? 51  TYR A CE1 1 
ATOM   432  C  CE2 . TYR A 1 51  ? -20.399 2.512   14.636  1.00  15.17  ? 51  TYR A CE2 1 
ATOM   433  C  CZ  . TYR A 1 51  ? -19.701 3.548   15.247  1.00  13.67  ? 51  TYR A CZ  1 
ATOM   434  O  OH  . TYR A 1 51  ? -18.561 3.192   15.882  1.00  13.68  ? 51  TYR A OH  1 
ATOM   435  N  N   A ASP A 1 52  ? -26.204 6.493   12.461  0.50  25.01  ? 52  ASP A N   1 
ATOM   436  N  N   B ASP A 1 52  ? -26.222 6.442   12.429  0.50  24.74  ? 52  ASP A N   1 
ATOM   437  C  CA  A ASP A 1 52  ? -27.251 6.743   11.462  0.50  26.58  ? 52  ASP A CA  1 
ATOM   438  C  CA  B ASP A 1 52  ? -27.216 6.696   11.386  0.50  28.31  ? 52  ASP A CA  1 
ATOM   439  C  C   A ASP A 1 52  ? -26.856 7.688   10.316  0.50  24.38  ? 52  ASP A C   1 
ATOM   440  C  C   B ASP A 1 52  ? -26.676 7.575   10.248  0.50  29.50  ? 52  ASP A C   1 
ATOM   441  O  O   A ASP A 1 52  ? -27.291 7.459   9.175   0.50  29.18  ? 52  ASP A O   1 
ATOM   442  O  O   B ASP A 1 52  ? -26.872 7.236   9.056   0.50  34.35  ? 52  ASP A O   1 
ATOM   443  C  CB  A ASP A 1 52  ? -28.575 7.169   12.133  0.50  30.81  ? 52  ASP A CB  1 
ATOM   444  C  CB  B ASP A 1 52  ? -28.454 7.332   12.021  0.50  33.56  ? 52  ASP A CB  1 
ATOM   445  C  CG  A ASP A 1 52  ? -28.387 8.205   13.234  0.50  36.09  ? 52  ASP A CG  1 
ATOM   446  C  CG  B ASP A 1 52  ? -29.627 7.408   11.071  0.50  32.26  ? 52  ASP A CG  1 
ATOM   447  O  OD1 A ASP A 1 52  ? -27.710 7.911   14.255  0.50  40.64  ? 52  ASP A OD1 1 
ATOM   448  O  OD1 B ASP A 1 52  ? -29.983 8.561   10.729  0.50  32.90  ? 52  ASP A OD1 1 
ATOM   449  O  OD2 A ASP A 1 52  ? -28.984 9.302   13.102  0.50  41.53  ? 52  ASP A OD2 1 
ATOM   450  O  OD2 B ASP A 1 52  ? -30.175 6.328   10.692  0.50  33.00  ? 52  ASP A OD2 1 
ATOM   451  N  N   . GLN A 1 53  ? -25.996 8.674   10.593  1.00  27.97  ? 53  GLN A N   1 
ATOM   452  C  CA  . GLN A 1 53  ? -25.528 9.615   9.568   1.00  28.02  ? 53  GLN A CA  1 
ATOM   453  C  C   . GLN A 1 53  ? -24.112 9.401   9.034   1.00  22.88  ? 53  GLN A C   1 
ATOM   454  O  O   . GLN A 1 53  ? -23.550 10.295  8.475   1.00  23.18  ? 53  GLN A O   1 
ATOM   455  C  CB  . GLN A 1 53  ? -25.658 11.073  10.028  1.00  30.60  ? 53  GLN A CB  1 
ATOM   456  C  CG  . GLN A 1 53  ? -27.043 11.476  10.483  1.00  39.88  ? 53  GLN A CG  1 
ATOM   457  C  CD  . GLN A 1 53  ? -28.026 11.517  9.348   1.00  49.44  ? 53  GLN A CD  1 
ATOM   458  O  OE1 . GLN A 1 53  ? -27.641 11.631  8.179   1.00  50.71  ? 53  GLN A OE1 1 
ATOM   459  N  NE2 . GLN A 1 53  ? -29.305 11.434  9.676   1.00  58.63  ? 53  GLN A NE2 1 
ATOM   460  N  N   . ALA A 1 54  ? -23.504 8.247   9.280   1.00  21.61  ? 54  ALA A N   1 
ATOM   461  C  CA  . ALA A 1 54  ? -22.134 7.967   8.809   1.00  20.29  ? 54  ALA A CA  1 
ATOM   462  C  C   . ALA A 1 54  ? -21.934 8.153   7.306   1.00  24.12  ? 54  ALA A C   1 
ATOM   463  O  O   . ALA A 1 54  ? -22.810 7.784   6.515   1.00  29.68  ? 54  ALA A O   1 
ATOM   464  C  CB  . ALA A 1 54  ? -21.721 6.562   9.236   1.00  23.78  ? 54  ALA A CB  1 
ATOM   465  N  N   . THR A 1 55  ? -20.773 8.739   6.943   1.00  20.62  ? 55  THR A N   1 
ATOM   466  C  CA  . THR A 1 55  ? -20.485 8.961   5.533   1.00  21.19  ? 55  THR A CA  1 
ATOM   467  C  C   . THR A 1 55  ? -19.166 8.349   5.325   1.00  18.10  ? 55  THR A C   1 
ATOM   468  O  O   . THR A 1 55  ? -18.133 8.928   5.625   1.00  21.43  ? 55  THR A O   1 
ATOM   469  C  CB  . THR A 1 55  ? -20.302 10.450  5.144   1.00  26.10  ? 55  THR A CB  1 
ATOM   470  O  OG1 . THR A 1 55  ? -21.555 11.029  5.203   1.00  29.78  ? 55  THR A OG1 1 
ATOM   471  C  CG2 . THR A 1 55  ? -19.881 10.530  3.667   1.00  30.94  ? 55  THR A CG2 1 
ATOM   472  N  N   . SER A 1 56  ? -19.196 7.100   4.833   1.00  20.21  ? 56  SER A N   1 
ATOM   473  C  CA  . SER A 1 56  ? -17.965 6.456   4.461   1.00  20.17  ? 56  SER A CA  1 
ATOM   474  C  C   . SER A 1 56  ? -17.483 7.100   3.148   1.00  23.02  ? 56  SER A C   1 
ATOM   475  O  O   . SER A 1 56  ? -18.240 7.608   2.318   1.00  26.11  ? 56  SER A O   1 
ATOM   476  C  CB  . SER A 1 56  ? -18.115 4.947   4.309   1.00  19.64  ? 56  SER A CB  1 
ATOM   477  O  OG  . SER A 1 56  ? -18.991 4.653   3.189   1.00  22.79  ? 56  SER A OG  1 
ATOM   478  N  N   . LEU A 1 57  ? -16.202 7.150   2.992   1.00  18.84  ? 57  LEU A N   1 
ATOM   479  C  CA  . LEU A 1 57  ? -15.646 7.760   1.821   1.00  24.76  ? 57  LEU A CA  1 
ATOM   480  C  C   . LEU A 1 57  ? -14.823 6.796   0.978   1.00  20.16  ? 57  LEU A C   1 
ATOM   481  O  O   . LEU A 1 57  ? -14.905 6.831   -0.243  1.00  21.92  ? 57  LEU A O   1 
ATOM   482  C  CB  . LEU A 1 57  ? -14.809 8.935   2.247   1.00  30.94  ? 57  LEU A CB  1 
ATOM   483  C  CG  . LEU A 1 57  ? -15.815 10.034  2.738   1.00  29.19  ? 57  LEU A CG  1 
ATOM   484  C  CD1 . LEU A 1 57  ? -14.902 11.134  3.234   1.00  29.40  ? 57  LEU A CD1 1 
ATOM   485  C  CD2 . LEU A 1 57  ? -16.926 10.508  1.763   1.00  29.51  ? 57  LEU A CD2 1 
ATOM   486  N  N   . ARG A 1 58  ? -13.939 6.043   1.620   1.00  23.27  ? 58  ARG A N   1 
ATOM   487  C  CA  . ARG A 1 58  ? -12.929 5.335   0.840   1.00  19.61  ? 58  ARG A CA  1 
ATOM   488  C  C   . ARG A 1 58  ? -12.441 4.141   1.677   1.00  18.01  ? 58  ARG A C   1 
ATOM   489  O  O   . ARG A 1 58  ? -12.546 4.118   2.912   1.00  19.01  ? 58  ARG A O   1 
ATOM   490  C  CB  . ARG A 1 58  ? -11.706 6.292   0.801   1.00  24.17  ? 58  ARG A CB  1 
ATOM   491  C  CG  . ARG A 1 58  ? -11.287 6.956   -0.497  1.00  36.75  ? 58  ARG A CG  1 
ATOM   492  C  CD  . ARG A 1 58  ? -9.766  7.008   -0.587  1.00  26.12  ? 58  ARG A CD  1 
ATOM   493  N  NE  . ARG A 1 58  ? -9.046  7.014   0.686   1.00  21.89  ? 58  ARG A NE  1 
ATOM   494  C  CZ  . ARG A 1 58  ? -7.751  7.283   0.767   1.00  24.72  ? 58  ARG A CZ  1 
ATOM   495  N  NH1 . ARG A 1 58  ? -7.098  7.537   -0.359  1.00  23.17  ? 58  ARG A NH1 1 
ATOM   496  N  NH2 . ARG A 1 58  ? -7.090  7.289   1.921   1.00  21.47  ? 58  ARG A NH2 1 
ATOM   497  N  N   . ILE A 1 59  ? -11.888 3.147   0.974   1.00  17.59  ? 59  ILE A N   1 
ATOM   498  C  CA  . ILE A 1 59  ? -11.250 2.059   1.632   1.00  17.54  ? 59  ILE A CA  1 
ATOM   499  C  C   . ILE A 1 59  ? -9.834  2.027   1.120   1.00  15.31  ? 59  ILE A C   1 
ATOM   500  O  O   . ILE A 1 59  ? -9.542  2.270   -0.101  1.00  18.14  ? 59  ILE A O   1 
ATOM   501  C  CB  . ILE A 1 59  ? -12.001 0.754   1.354   1.00  16.39  ? 59  ILE A CB  1 
ATOM   502  C  CG1 . ILE A 1 59  ? -11.453 -0.446  2.208   1.00  16.07  ? 59  ILE A CG1 1 
ATOM   503  C  CG2 . ILE A 1 59  ? -11.954 0.351   -0.154  1.00  16.80  ? 59  ILE A CG2 1 
ATOM   504  C  CD1 . ILE A 1 59  ? -12.350 -1.674  2.150   1.00  16.23  ? 59  ILE A CD1 1 
ATOM   505  N  N   . LEU A 1 60  ? -8.872  1.695   1.976   1.00  17.13  ? 60  LEU A N   1 
ATOM   506  C  CA  . LEU A 1 60  ? -7.495  1.841   1.720   1.00  15.58  ? 60  LEU A CA  1 
ATOM   507  C  C   . LEU A 1 60  ? -6.612  0.665   2.243   1.00  14.75  ? 60  LEU A C   1 
ATOM   508  O  O   . LEU A 1 60  ? -6.849  0.258   3.389   1.00  14.98  ? 60  LEU A O   1 
ATOM   509  C  CB  . LEU A 1 60  ? -7.043  3.174   2.420   1.00  16.78  ? 60  LEU A CB  1 
ATOM   510  C  CG  . LEU A 1 60  ? -5.561  3.307   2.353   1.00  15.37  ? 60  LEU A CG  1 
ATOM   511  C  CD1 . LEU A 1 60  ? -5.009  3.657   0.962   1.00  19.42  ? 60  LEU A CD1 1 
ATOM   512  C  CD2 . LEU A 1 60  ? -5.158  4.399   3.343   1.00  19.25  ? 60  LEU A CD2 1 
ATOM   513  N  N   . ASN A 1 61  ? -5.775  0.011   1.440   1.00  13.77  ? 61  ASN A N   1 
ATOM   514  C  CA  . ASN A 1 61  ? -4.688  -0.923  1.910   1.00  14.25  ? 61  ASN A CA  1 
ATOM   515  C  C   . ASN A 1 61  ? -3.435  -0.166  2.328   1.00  15.46  ? 61  ASN A C   1 
ATOM   516  O  O   . ASN A 1 61  ? -2.843  0.426   1.474   1.00  18.10  ? 61  ASN A O   1 
ATOM   517  C  CB  . ASN A 1 61  ? -4.399  -2.007  0.869   1.00  14.92  ? 61  ASN A CB  1 
ATOM   518  C  CG  . ASN A 1 61  ? -3.341  -2.989  1.297   1.00  12.99  ? 61  ASN A CG  1 
ATOM   519  O  OD1 . ASN A 1 61  ? -2.480  -2.708  2.194   1.00  15.34  ? 61  ASN A OD1 1 
ATOM   520  N  ND2 . ASN A 1 61  ? -3.380  -4.161  0.721   1.00  14.18  ? 61  ASN A ND2 1 
ATOM   521  N  N   . ASN A 1 62  ? -3.239  -0.042  3.644   1.00  15.76  ? 62  ASN A N   1 
ATOM   522  C  CA  . ASN A 1 62  ? -2.102  0.760   4.082   1.00  19.35  ? 62  ASN A CA  1 
ATOM   523  C  C   . ASN A 1 62  ? -0.853  -0.026  4.351   1.00  15.47  ? 62  ASN A C   1 
ATOM   524  O  O   . ASN A 1 62  ? 0.166   0.515   4.896   1.00  24.09  ? 62  ASN A O   1 
ATOM   525  C  CB  . ASN A 1 62  ? -2.499  1.535   5.349   1.00  23.48  ? 62  ASN A CB  1 
ATOM   526  C  CG  . ASN A 1 62  ? -2.925  0.578   6.480   1.00  19.92  ? 62  ASN A CG  1 
ATOM   527  O  OD1 . ASN A 1 62  ? -2.383  -0.468  6.654   1.00  15.19  ? 62  ASN A OD1 1 
ATOM   528  N  ND2 . ASN A 1 62  ? -4.040  0.937   7.177   1.00  25.29  ? 62  ASN A ND2 1 
ATOM   529  N  N   . GLY A 1 63  ? -0.790  -1.266  3.948   1.00  16.39  ? 63  GLY A N   1 
ATOM   530  C  CA  . GLY A 1 63  ? 0.321   -2.107  4.119   1.00  17.84  ? 63  GLY A CA  1 
ATOM   531  C  C   . GLY A 1 63  ? 0.379   -2.819  5.452   1.00  14.09  ? 63  GLY A C   1 
ATOM   532  O  O   . GLY A 1 63  ? 1.212   -3.696  5.631   1.00  18.29  ? 63  GLY A O   1 
ATOM   533  N  N   . HIS A 1 64  ? -0.534  -2.516  6.358   1.00  13.41  ? 64  HIS A N   1 
ATOM   534  C  CA  . HIS A 1 64  ? -0.632  -3.172  7.678   1.00  12.45  ? 64  HIS A CA  1 
ATOM   535  C  C   . HIS A 1 64  ? -1.995  -3.794  7.880   1.00  12.67  ? 64  HIS A C   1 
ATOM   536  O  O   . HIS A 1 64  ? -2.098  -4.786  8.657   1.00  19.07  ? 64  HIS A O   1 
ATOM   537  C  CB  . HIS A 1 64  ? -0.374  -2.131  8.753   1.00  14.41  ? 64  HIS A CB  1 
ATOM   538  C  CG  . HIS A 1 64  ? 0.953   -1.457  8.596   1.00  15.28  ? 64  HIS A CG  1 
ATOM   539  N  ND1 . HIS A 1 64  ? 2.154   -2.120  8.785   1.00  18.03  ? 64  HIS A ND1 1 
ATOM   540  C  CD2 . HIS A 1 64  ? 1.263   -0.186  8.303   1.00  18.83  ? 64  HIS A CD2 1 
ATOM   541  C  CE1 . HIS A 1 64  ? 3.195   -1.278  8.577   1.00  19.92  ? 64  HIS A CE1 1 
ATOM   542  N  NE2 . HIS A 1 64  ? 2.666   -0.068  8.303   1.00  21.69  ? 64  HIS A NE2 1 
ATOM   543  N  N   A SER A 1 65  ? -3.006  -3.138  7.339   0.50  11.70  ? 65  SER A N   1 
ATOM   544  N  N   B SER A 1 65  ? -3.049  -3.234  7.338   0.50  11.80  ? 65  SER A N   1 
ATOM   545  C  CA  A SER A 1 65  ? -4.388  -3.512  7.392   0.50  9.80   ? 65  SER A CA  1 
ATOM   546  C  CA  B SER A 1 65  ? -4.362  -3.825  7.321   0.50  11.62  ? 65  SER A CA  1 
ATOM   547  C  C   A SER A 1 65  ? -5.136  -2.824  6.222   0.50  10.77  ? 65  SER A C   1 
ATOM   548  C  C   B SER A 1 65  ? -5.043  -3.088  6.157   0.50  10.01  ? 65  SER A C   1 
ATOM   549  O  O   A SER A 1 65  ? -4.600  -2.089  5.403   0.50  10.41  ? 65  SER A O   1 
ATOM   550  O  O   B SER A 1 65  ? -4.293  -2.528  5.320   0.50  10.20  ? 65  SER A O   1 
ATOM   551  C  CB  A SER A 1 65  ? -5.031  -3.135  8.716   0.50  9.54   ? 65  SER A CB  1 
ATOM   552  C  CB  B SER A 1 65  ? -5.052  -3.612  8.639   0.50  12.86  ? 65  SER A CB  1 
ATOM   553  O  OG  A SER A 1 65  ? -6.327  -3.729  8.833   0.50  10.42  ? 65  SER A OG  1 
ATOM   554  O  OG  B SER A 1 65  ? -5.208  -2.265  8.879   0.50  14.04  ? 65  SER A OG  1 
ATOM   555  N  N   . PHE A 1 66  ? -6.394  -3.095  6.150   1.00  11.18  ? 66  PHE A N   1 
ATOM   556  C  CA  . PHE A 1 66  ? -7.211  -2.191  5.306   1.00  12.19  ? 66  PHE A CA  1 
ATOM   557  C  C   . PHE A 1 66  ? -8.111  -1.370  6.211   1.00  11.73  ? 66  PHE A C   1 
ATOM   558  O  O   . PHE A 1 66  ? -8.504  -1.813  7.297   1.00  11.94  ? 66  PHE A O   1 
ATOM   559  C  CB  . PHE A 1 66  ? -8.008  -2.929  4.266   1.00  12.74  ? 66  PHE A CB  1 
ATOM   560  C  CG  . PHE A 1 66  ? -9.090  -3.768  4.811   1.00  13.06  ? 66  PHE A CG  1 
ATOM   561  C  CD1 . PHE A 1 66  ? -10.331 -3.216  5.005   1.00  12.90  ? 66  PHE A CD1 1 
ATOM   562  C  CD2 . PHE A 1 66  ? -8.922  -5.122  5.130   1.00  12.45  ? 66  PHE A CD2 1 
ATOM   563  C  CE1 . PHE A 1 66  ? -11.370 -3.939  5.507   1.00  14.41  ? 66  PHE A CE1 1 
ATOM   564  C  CE2 . PHE A 1 66  ? -9.963  -5.874  5.641   1.00  13.11  ? 66  PHE A CE2 1 
ATOM   565  C  CZ  . PHE A 1 66  ? -11.199 -5.324  5.801   1.00  12.00  ? 66  PHE A CZ  1 
ATOM   566  N  N   . GLN A 1 67  ? -8.402  -0.166  5.778   1.00  13.64  ? 67  GLN A N   1 
ATOM   567  C  CA  . GLN A 1 67  ? -9.164  0.756   6.584   1.00  13.78  ? 67  GLN A CA  1 
ATOM   568  C  C   . GLN A 1 67  ? -10.304 1.429   5.795   1.00  14.31  ? 67  GLN A C   1 
ATOM   569  O  O   . GLN A 1 67  ? -10.064 1.851   4.619   1.00  18.15  ? 67  GLN A O   1 
ATOM   570  C  CB  . GLN A 1 67  ? -8.274  1.746   7.233   1.00  20.61  ? 67  GLN A CB  1 
ATOM   571  C  CG  . GLN A 1 67  ? -7.901  2.802   6.363   1.00  18.74  ? 67  GLN A CG  1 
ATOM   572  C  CD  . GLN A 1 67  ? -6.918  3.657   7.029   1.00  22.39  ? 67  GLN A CD  1 
ATOM   573  O  OE1 . GLN A 1 67  ? -6.114  3.147   7.809   1.00  26.07  ? 67  GLN A OE1 1 
ATOM   574  N  NE2 . GLN A 1 67  ? -6.949  4.987   6.702   1.00  28.94  ? 67  GLN A NE2 1 
ATOM   575  N  N   . VAL A 1 68  ? -11.499 1.462   6.312   1.00  14.92  ? 68  VAL A N   1 
ATOM   576  C  CA  . VAL A 1 68  ? -12.648 2.193   5.776   1.00  14.53  ? 68  VAL A CA  1 
ATOM   577  C  C   . VAL A 1 68  ? -12.707 3.565   6.448   1.00  16.00  ? 68  VAL A C   1 
ATOM   578  O  O   . VAL A 1 68  ? -12.791 3.615   7.704   1.00  15.21  ? 68  VAL A O   1 
ATOM   579  C  CB  . VAL A 1 68  ? -13.993 1.449   5.890   1.00  16.77  ? 68  VAL A CB  1 
ATOM   580  C  CG1 . VAL A 1 68  ? -15.167 2.352   5.479   1.00  18.88  ? 68  VAL A CG1 1 
ATOM   581  C  CG2 . VAL A 1 68  ? -13.951 0.156   5.093   1.00  15.53  ? 68  VAL A CG2 1 
ATOM   582  N  N   . GLU A 1 69  ? -12.570 4.654   5.692   1.00  17.98  ? 69  GLU A N   1 
ATOM   583  C  CA  . GLU A 1 69  ? -12.582 5.982   6.225   1.00  17.26  ? 69  GLU A CA  1 
ATOM   584  C  C   . GLU A 1 69  ? -13.847 6.709   6.122   1.00  18.40  ? 69  GLU A C   1 
ATOM   585  O  O   . GLU A 1 69  ? -14.692 6.465   5.182   1.00  18.36  ? 69  GLU A O   1 
ATOM   586  C  CB  . GLU A 1 69  ? -11.687 6.745   5.413   1.00  19.40  ? 69  GLU A CB  1 
ATOM   587  C  CG  . GLU A 1 69  ? -10.356 6.190   5.528   1.00  18.07  ? 69  GLU A CG  1 
ATOM   588  C  CD  . GLU A 1 69  ? -9.427  6.694   4.482   1.00  17.48  ? 69  GLU A CD  1 
ATOM   589  O  OE1 . GLU A 1 69  ? -9.900  7.439   3.526   1.00  22.97  ? 69  GLU A OE1 1 
ATOM   590  O  OE2 . GLU A 1 69  ? -8.246  6.301   4.491   1.00  23.97  ? 69  GLU A OE2 1 
ATOM   591  N  N   . PHE A 1 70  ? -13.992 7.590   7.079   1.00  17.08  ? 70  PHE A N   1 
ATOM   592  C  CA  . PHE A 1 70  ? -15.222 8.392   7.119   1.00  15.89  ? 70  PHE A CA  1 
ATOM   593  C  C   . PHE A 1 70  ? -15.024 9.884   7.110   1.00  16.44  ? 70  PHE A C   1 
ATOM   594  O  O   . PHE A 1 70  ? -13.985 10.314  7.490   1.00  18.12  ? 70  PHE A O   1 
ATOM   595  C  CB  . PHE A 1 70  ? -16.035 8.006   8.356   1.00  15.17  ? 70  PHE A CB  1 
ATOM   596  C  CG  . PHE A 1 70  ? -16.541 6.596   8.324   1.00  14.91  ? 70  PHE A CG  1 
ATOM   597  C  CD1 . PHE A 1 70  ? -15.699 5.537   8.616   1.00  14.69  ? 70  PHE A CD1 1 
ATOM   598  C  CD2 . PHE A 1 70  ? -17.856 6.329   7.989   1.00  14.01  ? 70  PHE A CD2 1 
ATOM   599  C  CE1 . PHE A 1 70  ? -16.162 4.236   8.580   1.00  15.06  ? 70  PHE A CE1 1 
ATOM   600  C  CE2 . PHE A 1 70  ? -18.326 5.032   7.950   1.00  16.55  ? 70  PHE A CE2 1 
ATOM   601  C  CZ  . PHE A 1 70  ? -17.478 3.983   8.246   1.00  15.13  ? 70  PHE A CZ  1 
ATOM   602  N  N   . ASP A 1 71  ? -16.060 10.593  6.684   1.00  21.77  ? 71  ASP A N   1 
ATOM   603  C  CA  . ASP A 1 71  ? -16.001 12.049  6.846   1.00  19.51  ? 71  ASP A CA  1 
ATOM   604  C  C   . ASP A 1 71  ? -16.256 12.403  8.317   1.00  21.35  ? 71  ASP A C   1 
ATOM   605  O  O   . ASP A 1 71  ? -17.404 12.255  8.827   1.00  28.71  ? 71  ASP A O   1 
ATOM   606  C  CB  . ASP A 1 71  ? -17.075 12.648  5.964   1.00  23.35  ? 71  ASP A CB  1 
ATOM   607  C  CG  . ASP A 1 71  ? -17.250 14.173  6.180   1.00  26.30  ? 71  ASP A CG  1 
ATOM   608  O  OD1 . ASP A 1 71  ? -16.400 14.792  6.812   1.00  27.92  ? 71  ASP A OD1 1 
ATOM   609  O  OD2 . ASP A 1 71  ? -18.304 14.719  5.838   1.00  28.17  ? 71  ASP A OD2 1 
ATOM   610  N  N   . ASP A 1 72  ? -15.199 12.889  8.980   1.00  20.67  ? 72  ASP A N   1 
ATOM   611  C  CA  . ASP A 1 72  ? -15.281 13.284  10.392  1.00  20.21  ? 72  ASP A CA  1 
ATOM   612  C  C   . ASP A 1 72  ? -15.173 14.830  10.491  1.00  22.74  ? 72  ASP A C   1 
ATOM   613  O  O   . ASP A 1 72  ? -14.691 15.283  11.544  1.00  29.12  ? 72  ASP A O   1 
ATOM   614  C  CB  . ASP A 1 72  ? -14.118 12.636  11.171  1.00  24.09  ? 72  ASP A CB  1 
ATOM   615  C  CG  . ASP A 1 72  ? -12.725 13.107  10.709  1.00  24.81  ? 72  ASP A CG  1 
ATOM   616  O  OD1 . ASP A 1 72  ? -12.603 13.648  9.563   1.00  33.86  ? 72  ASP A OD1 1 
ATOM   617  O  OD2 . ASP A 1 72  ? -11.726 12.972  11.440  1.00  26.86  ? 72  ASP A OD2 1 
ATOM   618  N  N   . SER A 1 73  ? -15.588 15.556  9.458   1.00  24.83  ? 73  SER A N   1 
ATOM   619  C  CA  . SER A 1 73  ? -15.434 17.027  9.418   1.00  28.57  ? 73  SER A CA  1 
ATOM   620  C  C   . SER A 1 73  ? -16.725 17.615  10.023  1.00  26.51  ? 73  SER A C   1 
ATOM   621  O  O   . SER A 1 73  ? -16.836 18.829  10.077  1.00  27.07  ? 73  SER A O   1 
ATOM   622  C  CB  . SER A 1 73  ? -15.196 17.537  8.014   1.00  29.67  ? 73  SER A CB  1 
ATOM   623  O  OG  . SER A 1 73  ? -16.407 17.428  7.277   1.00  25.36  ? 73  SER A OG  1 
ATOM   624  N  N   . GLN A 1 74  ? -17.691 16.775  10.429  1.00  30.79  ? 74  GLN A N   1 
ATOM   625  C  CA  . GLN A 1 74  ? -18.746 17.202  11.406  1.00  30.47  ? 74  GLN A CA  1 
ATOM   626  C  C   . GLN A 1 74  ? -19.245 15.999  12.187  1.00  27.54  ? 74  GLN A C   1 
ATOM   627  O  O   . GLN A 1 74  ? -18.758 14.906  11.906  1.00  25.18  ? 74  GLN A O   1 
ATOM   628  C  CB  . GLN A 1 74  ? -19.866 17.953  10.728  1.00  39.71  ? 74  GLN A CB  1 
ATOM   629  C  CG  . GLN A 1 74  ? -20.281 17.368  9.412   1.00  46.21  ? 74  GLN A CG  1 
ATOM   630  C  CD  . GLN A 1 74  ? -21.303 18.267  8.741   1.00  44.42  ? 74  GLN A CD  1 
ATOM   631  O  OE1 . GLN A 1 74  ? -21.944 19.127  9.399   1.00  41.52  ? 74  GLN A OE1 1 
ATOM   632  N  NE2 . GLN A 1 74  ? -21.451 18.105  7.433   1.00  40.36  ? 74  GLN A NE2 1 
ATOM   633  N  N   . ASP A 1 75  ? -20.193 16.214  13.140  1.00  27.37  ? 75  ASP A N   1 
ATOM   634  C  CA  . ASP A 1 75  ? -20.768 15.201  14.088  1.00  31.64  ? 75  ASP A CA  1 
ATOM   635  C  C   . ASP A 1 75  ? -21.758 14.171  13.484  1.00  26.60  ? 75  ASP A C   1 
ATOM   636  O  O   . ASP A 1 75  ? -22.892 14.008  13.965  1.00  42.51  ? 75  ASP A O   1 
ATOM   637  C  CB  . ASP A 1 75  ? -21.396 15.863  15.349  1.00  34.66  ? 75  ASP A CB  1 
ATOM   638  C  CG  . ASP A 1 75  ? -20.346 16.300  16.406  1.00  38.28  ? 75  ASP A CG  1 
ATOM   639  O  OD1 . ASP A 1 75  ? -19.142 16.031  16.178  1.00  41.31  ? 75  ASP A OD1 1 
ATOM   640  O  OD2 . ASP A 1 75  ? -20.714 16.927  17.449  1.00  48.81  ? 75  ASP A OD2 1 
ATOM   641  N  N   A LYS A 1 76  ? -21.337 13.444  12.460  0.50  26.42  ? 76  LYS A N   1 
ATOM   642  N  N   B LYS A 1 76  ? -21.260 13.476  12.458  0.50  22.22  ? 76  LYS A N   1 
ATOM   643  C  CA  A LYS A 1 76  ? -22.227 12.428  11.910  0.50  25.96  ? 76  LYS A CA  1 
ATOM   644  C  CA  B LYS A 1 76  ? -22.000 12.508  11.645  0.50  21.68  ? 76  LYS A CA  1 
ATOM   645  C  C   A LYS A 1 76  ? -22.186 11.142  12.734  0.50  25.66  ? 76  LYS A C   1 
ATOM   646  C  C   B LYS A 1 76  ? -22.227 11.164  12.316  0.50  19.19  ? 76  LYS A C   1 
ATOM   647  O  O   A LYS A 1 76  ? -22.962 10.995  13.678  0.50  25.11  ? 76  LYS A O   1 
ATOM   648  O  O   B LYS A 1 76  ? -23.312 10.589  12.232  0.50  23.39  ? 76  LYS A O   1 
ATOM   649  C  CB  A LYS A 1 76  ? -21.937 12.188  10.438  0.50  27.73  ? 76  LYS A CB  1 
ATOM   650  C  CB  B LYS A 1 76  ? -21.249 12.266  10.318  0.50  18.79  ? 76  LYS A CB  1 
ATOM   651  C  CG  A LYS A 1 76  ? -22.307 13.391  9.572   0.50  32.73  ? 76  LYS A CG  1 
ATOM   652  C  CG  B LYS A 1 76  ? -21.328 13.461  9.406   0.50  24.69  ? 76  LYS A CG  1 
ATOM   653  C  CD  A LYS A 1 76  ? -21.712 13.271  8.176   0.50  32.86  ? 76  LYS A CD  1 
ATOM   654  C  CD  B LYS A 1 76  ? -20.793 13.149  8.022   0.50  24.40  ? 76  LYS A CD  1 
ATOM   655  C  CE  A LYS A 1 76  ? -22.057 14.475  7.314   0.50  29.91  ? 76  LYS A CE  1 
ATOM   656  C  CE  B LYS A 1 76  ? -21.411 14.144  7.053   0.50  21.09  ? 76  LYS A CE  1 
ATOM   657  N  NZ  A LYS A 1 76  ? -21.813 14.117  5.895   0.50  31.79  ? 76  LYS A NZ  1 
ATOM   658  N  NZ  B LYS A 1 76  ? -21.082 13.874  5.647   0.50  23.57  ? 76  LYS A NZ  1 
ATOM   659  N  N   A ALA A 1 77  ? -21.289 10.216  12.405  0.50  19.25  ? 77  ALA A N   1 
ATOM   660  N  N   B ALA A 1 77  ? -21.187 10.660  12.965  0.50  19.91  ? 77  ALA A N   1 
ATOM   661  C  CA  A ALA A 1 77  ? -21.140 9.036   13.265  0.50  19.04  ? 77  ALA A CA  1 
ATOM   662  C  CA  B ALA A 1 77  ? -21.124 9.306   13.333  0.50  17.87  ? 77  ALA A CA  1 
ATOM   663  C  C   A ALA A 1 77  ? -20.344 9.350   14.574  0.50  17.25  ? 77  ALA A C   1 
ATOM   664  C  C   B ALA A 1 77  ? -20.334 9.438   14.605  0.50  15.37  ? 77  ALA A C   1 
ATOM   665  O  O   A ALA A 1 77  ? -19.150 9.677   14.514  0.50  19.80  ? 77  ALA A O   1 
ATOM   666  O  O   B ALA A 1 77  ? -19.145 9.751   14.563  0.50  18.01  ? 77  ALA A O   1 
ATOM   667  C  CB  A ALA A 1 77  ? -20.523 7.893   12.474  0.50  22.88  ? 77  ALA A CB  1 
ATOM   668  C  CB  B ALA A 1 77  ? -20.356 8.595   12.240  0.50  15.03  ? 77  ALA A CB  1 
ATOM   669  N  N   . VAL A 1 78  ? -20.997 9.218   15.743  1.00  15.40  ? 78  VAL A N   1 
ATOM   670  C  CA  . VAL A 1 78  ? -20.362 9.522   17.018  1.00  16.08  ? 78  VAL A CA  1 
ATOM   671  C  C   . VAL A 1 78  ? -20.595 8.459   18.059  1.00  14.44  ? 78  VAL A C   1 
ATOM   672  O  O   . VAL A 1 78  ? -21.591 7.721   18.077  1.00  16.17  ? 78  VAL A O   1 
ATOM   673  C  CB  . VAL A 1 78  ? -20.775 10.859  17.594  1.00  19.38  ? 78  VAL A CB  1 
ATOM   674  C  CG1 . VAL A 1 78  ? -20.413 12.048  16.725  1.00  21.21  ? 78  VAL A CG1 1 
ATOM   675  C  CG2 . VAL A 1 78  ? -22.178 10.816  18.021  1.00  22.21  ? 78  VAL A CG2 1 
ATOM   676  N  N   . LEU A 1 79  ? -19.610 8.296   18.954  1.00  12.86  ? 79  LEU A N   1 
ATOM   677  C  CA  . LEU A 1 79  ? -19.680 7.437   20.103  1.00  11.85  ? 79  LEU A CA  1 
ATOM   678  C  C   . LEU A 1 79  ? -19.672 8.304   21.321  1.00  12.34  ? 79  LEU A C   1 
ATOM   679  O  O   . LEU A 1 79  ? -18.849 9.268   21.430  1.00  13.73  ? 79  LEU A O   1 
ATOM   680  C  CB  . LEU A 1 79  ? -18.462 6.521   20.084  1.00  13.43  ? 79  LEU A CB  1 
ATOM   681  C  CG  . LEU A 1 79  ? -18.332 5.488   21.127  1.00  13.71  ? 79  LEU A CG  1 
ATOM   682  C  CD1 . LEU A 1 79  ? -19.407 4.437   20.995  1.00  17.36  ? 79  LEU A CD1 1 
ATOM   683  C  CD2 . LEU A 1 79  ? -16.931 4.859   21.024  1.00  14.76  ? 79  LEU A CD2 1 
ATOM   684  N  N   A LYS A 1 80  ? -20.520 7.989   22.292  0.50  13.85  ? 80  LYS A N   1 
ATOM   685  N  N   B LYS A 1 80  ? -20.595 7.990   22.230  0.50  13.06  ? 80  LYS A N   1 
ATOM   686  C  CA  A LYS A 1 80  ? -20.454 8.707   23.584  0.50  15.31  ? 80  LYS A CA  1 
ATOM   687  C  CA  B LYS A 1 80  ? -20.775 8.757   23.478  0.50  12.52  ? 80  LYS A CA  1 
ATOM   688  C  C   A LYS A 1 80  ? -21.078 7.786   24.619  0.50  15.08  ? 80  LYS A C   1 
ATOM   689  C  C   B LYS A 1 80  ? -21.153 7.784   24.615  0.50  13.17  ? 80  LYS A C   1 
ATOM   690  O  O   A LYS A 1 80  ? -21.441 6.642   24.279  0.50  15.28  ? 80  LYS A O   1 
ATOM   691  O  O   B LYS A 1 80  ? -21.373 6.582   24.347  0.50  13.40  ? 80  LYS A O   1 
ATOM   692  C  CB  A LYS A 1 80  ? -21.200 10.048  23.547  0.50  15.90  ? 80  LYS A CB  1 
ATOM   693  C  CB  B LYS A 1 80  ? -21.851 9.876   23.323  0.50  14.96  ? 80  LYS A CB  1 
ATOM   694  C  CG  A LYS A 1 80  ? -22.707 9.850   23.288  0.50  18.74  ? 80  LYS A CG  1 
ATOM   695  C  CG  B LYS A 1 80  ? -21.649 10.947  22.266  0.50  16.62  ? 80  LYS A CG  1 
ATOM   696  C  CD  A LYS A 1 80  ? -23.440 11.180  23.184  0.50  20.76  ? 80  LYS A CD  1 
ATOM   697  C  CD  B LYS A 1 80  ? -22.980 11.660  22.021  0.50  22.29  ? 80  LYS A CD  1 
ATOM   698  C  CE  A LYS A 1 80  ? -22.480 12.322  22.966  0.50  29.10  ? 80  LYS A CE  1 
ATOM   699  C  CE  B LYS A 1 80  ? -22.855 12.960  21.189  0.50  23.55  ? 80  LYS A CE  1 
ATOM   700  N  NZ  A LYS A 1 80  ? -22.733 13.370  23.988  0.50  34.42  ? 80  LYS A NZ  1 
ATOM   701  N  NZ  B LYS A 1 80  ? -24.176 13.675  20.956  0.50  29.77  ? 80  LYS A NZ  1 
ATOM   702  N  N   . GLY A 1 81  ? -21.149 8.243   25.862  1.00  15.18  ? 81  GLY A N   1 
ATOM   703  C  CA  . GLY A 1 81  ? -21.632 7.431   26.948  1.00  15.55  ? 81  GLY A CA  1 
ATOM   704  C  C   . GLY A 1 81  ? -20.628 6.346   27.324  1.00  15.87  ? 81  GLY A C   1 
ATOM   705  O  O   . GLY A 1 81  ? -19.446 6.503   27.080  1.00  14.33  ? 81  GLY A O   1 
ATOM   706  N  N   . GLY A 1 82  ? -21.121 5.268   27.918  1.00  20.13  ? 82  GLY A N   1 
ATOM   707  C  CA  . GLY A 1 82  ? -20.170 4.269   28.447  1.00  21.15  ? 82  GLY A CA  1 
ATOM   708  C  C   . GLY A 1 82  ? -19.253 4.929   29.454  1.00  19.74  ? 82  GLY A C   1 
ATOM   709  O  O   . GLY A 1 82  ? -19.699 5.678   30.350  1.00  26.40  ? 82  GLY A O   1 
ATOM   710  N  N   . PRO A 1 83  ? -17.941 4.691   29.286  1.00  15.28  ? 83  PRO A N   1 
ATOM   711  C  CA  . PRO A 1 83  ? -16.989 5.331   30.131  1.00  16.23  ? 83  PRO A CA  1 
ATOM   712  C  C   . PRO A 1 83  ? -16.614 6.732   29.704  1.00  15.54  ? 83  PRO A C   1 
ATOM   713  O  O   . PRO A 1 83  ? -15.826 7.363   30.385  1.00  18.60  ? 83  PRO A O   1 
ATOM   714  C  CB  . PRO A 1 83  ? -15.755 4.362   30.020  1.00  15.01  ? 83  PRO A CB  1 
ATOM   715  C  CG  . PRO A 1 83  ? -15.809 3.997   28.544  1.00  12.30  ? 83  PRO A CG  1 
ATOM   716  C  CD  . PRO A 1 83  ? -17.327 3.862   28.263  1.00  13.85  ? 83  PRO A CD  1 
ATOM   717  N  N   . LEU A 1 84  ? -17.156 7.224   28.587  1.00  13.77  ? 84  LEU A N   1 
ATOM   718  C  CA  . LEU A 1 84  ? -16.614 8.408   27.949  1.00  13.20  ? 84  LEU A CA  1 
ATOM   719  C  C   . LEU A 1 84  ? -17.278 9.682   28.497  1.00  13.93  ? 84  LEU A C   1 
ATOM   720  O  O   . LEU A 1 84  ? -18.445 9.684   28.854  1.00  15.99  ? 84  LEU A O   1 
ATOM   721  C  CB  . LEU A 1 84  ? -16.919 8.351   26.455  1.00  13.02  ? 84  LEU A CB  1 
ATOM   722  C  CG  . LEU A 1 84  ? -16.321 7.096   25.791  1.00  10.89  ? 84  LEU A CG  1 
ATOM   723  C  CD1 . LEU A 1 84  ? -16.795 7.070   24.363  1.00  13.60  ? 84  LEU A CD1 1 
ATOM   724  C  CD2 . LEU A 1 84  ? -14.788 7.089   25.844  1.00  11.54  ? 84  LEU A CD2 1 
ATOM   725  N  N   A ASP A 1 85  ? -16.497 10.750  28.524  0.50  16.84  ? 85  ASP A N   1 
ATOM   726  N  N   B ASP A 1 85  ? -16.463 10.728  28.551  0.50  16.32  ? 85  ASP A N   1 
ATOM   727  C  CA  A ASP A 1 85  ? -17.101 12.078  28.674  0.50  18.66  ? 85  ASP A CA  1 
ATOM   728  C  CA  B ASP A 1 85  ? -16.937 12.031  29.047  0.50  17.20  ? 85  ASP A CA  1 
ATOM   729  C  C   A ASP A 1 85  ? -16.907 12.778  27.367  0.50  15.44  ? 85  ASP A C   1 
ATOM   730  C  C   B ASP A 1 85  ? -17.259 13.025  27.949  0.50  23.85  ? 85  ASP A C   1 
ATOM   731  O  O   A ASP A 1 85  ? -15.865 12.691  26.755  0.50  17.67  ? 85  ASP A O   1 
ATOM   732  O  O   B ASP A 1 85  ? -17.603 14.147  28.267  0.50  25.85  ? 85  ASP A O   1 
ATOM   733  C  CB  A ASP A 1 85  ? -16.430 12.857  29.754  0.50  22.81  ? 85  ASP A CB  1 
ATOM   734  C  CB  B ASP A 1 85  ? -15.904 12.671  29.987  0.50  19.92  ? 85  ASP A CB  1 
ATOM   735  C  CG  A ASP A 1 85  ? -16.292 12.048  31.016  0.50  34.39  ? 85  ASP A CG  1 
ATOM   736  C  CG  B ASP A 1 85  ? -16.251 12.462  31.458  0.50  23.95  ? 85  ASP A CG  1 
ATOM   737  O  OD1 A ASP A 1 85  ? -17.345 11.603  31.542  0.50  37.58  ? 85  ASP A OD1 1 
ATOM   738  O  OD1 B ASP A 1 85  ? -17.453 12.230  31.768  0.50  33.97  ? 85  ASP A OD1 1 
ATOM   739  O  OD2 A ASP A 1 85  ? -15.132 11.841  31.456  0.50  37.08  ? 85  ASP A OD2 1 
ATOM   740  O  OD2 B ASP A 1 85  ? -15.313 12.560  32.288  0.50  26.37  ? 85  ASP A OD2 1 
ATOM   741  N  N   A GLY A 1 86  ? -17.956 13.480  26.949  0.50  14.67  ? 86  GLY A N   1 
ATOM   742  N  N   B GLY A 1 86  ? -17.136 12.687  26.665  0.50  26.71  ? 86  GLY A N   1 
ATOM   743  C  CA  A GLY A 1 86  ? -18.040 14.118  25.665  0.50  18.18  ? 86  GLY A CA  1 
ATOM   744  C  CA  B GLY A 1 86  ? -17.439 13.695  25.649  0.50  25.20  ? 86  GLY A CA  1 
ATOM   745  C  C   A GLY A 1 86  ? -18.106 13.146  24.448  0.50  19.90  ? 86  GLY A C   1 
ATOM   746  C  C   B GLY A 1 86  ? -18.236 13.201  24.440  0.50  16.76  ? 86  GLY A C   1 
ATOM   747  O  O   A GLY A 1 86  ? -18.281 11.888  24.565  0.50  19.58  ? 86  GLY A O   1 
ATOM   748  O  O   B GLY A 1 86  ? -19.096 12.305  24.552  0.50  18.38  ? 86  GLY A O   1 
ATOM   749  N  N   . THR A 1 87  ? -17.881 13.720  23.286  1.00  15.48  ? 87  THR A N   1 
ATOM   750  C  CA  . THR A 1 87  ? -18.298 13.149  22.044  1.00  15.78  ? 87  THR A CA  1 
ATOM   751  C  C   . THR A 1 87  ? -17.087 12.770  21.235  1.00  13.53  ? 87  THR A C   1 
ATOM   752  O  O   . THR A 1 87  ? -16.179 13.534  21.108  1.00  13.53  ? 87  THR A O   1 
ATOM   753  C  CB  . THR A 1 87  ? -19.079 14.251  21.259  1.00  21.09  ? 87  THR A CB  1 
ATOM   754  O  OG1 . THR A 1 87  ? -20.228 14.665  22.070  1.00  29.11  ? 87  THR A OG1 1 
ATOM   755  C  CG2 . THR A 1 87  ? -19.545 13.725  19.910  1.00  21.85  ? 87  THR A CG2 1 
ATOM   756  N  N   . TYR A 1 88  ? -17.143 11.574  20.662  1.00  11.54  ? 88  TYR A N   1 
ATOM   757  C  CA  . TYR A 1 88  ? -16.050 11.066  19.855  1.00  10.79  ? 88  TYR A CA  1 
ATOM   758  C  C   . TYR A 1 88  ? -16.497 10.759  18.465  1.00  12.13  ? 88  TYR A C   1 
ATOM   759  O  O   . TYR A 1 88  ? -17.466 9.992   18.256  1.00  13.80  ? 88  TYR A O   1 
ATOM   760  C  CB  . TYR A 1 88  ? -15.460 9.815   20.496  1.00  10.94  ? 88  TYR A CB  1 
ATOM   761  C  CG  . TYR A 1 88  ? -14.711 10.021  21.810  1.00  10.60  ? 88  TYR A CG  1 
ATOM   762  C  CD1 . TYR A 1 88  ? -15.363 10.429  22.984  1.00  11.38  ? 88  TYR A CD1 1 
ATOM   763  C  CD2 . TYR A 1 88  ? -13.324 9.853   21.860  1.00  9.60   ? 88  TYR A CD2 1 
ATOM   764  C  CE1 . TYR A 1 88  ? -14.677 10.594  24.151  1.00  10.24  ? 88  TYR A CE1 1 
ATOM   765  C  CE2 . TYR A 1 88  ? -12.622 9.978   23.045  1.00  9.58   ? 88  TYR A CE2 1 
ATOM   766  C  CZ  . TYR A 1 88  ? -13.299 10.320  24.170  1.00  9.83   ? 88  TYR A CZ  1 
ATOM   767  O  OH  . TYR A 1 88  ? -12.609 10.434  25.346  1.00  10.58  ? 88  TYR A OH  1 
ATOM   768  N  N   . ARG A 1 89  ? -15.880 11.333  17.455  1.00  11.52  ? 89  ARG A N   1 
ATOM   769  C  CA  . ARG A 1 89  ? -16.261 11.093  16.089  1.00  12.07  ? 89  ARG A CA  1 
ATOM   770  C  C   . ARG A 1 89  ? -15.569 9.962   15.437  1.00  9.84   ? 89  ARG A C   1 
ATOM   771  O  O   . ARG A 1 89  ? -14.380 9.750   15.600  1.00  10.38  ? 89  ARG A O   1 
ATOM   772  C  CB  . ARG A 1 89  ? -15.827 12.372  15.307  1.00  14.18  ? 89  ARG A CB  1 
ATOM   773  C  CG  . ARG A 1 89  ? -16.712 13.566  15.555  1.00  20.31  ? 89  ARG A CG  1 
ATOM   774  C  CD  . ARG A 1 89  ? -16.521 14.568  14.444  1.00  24.91  ? 89  ARG A CD  1 
ATOM   775  N  NE  . ARG A 1 89  ? -17.113 15.824  14.829  1.00  29.36  ? 89  ARG A NE  1 
ATOM   776  C  CZ  . ARG A 1 89  ? -16.740 17.019  14.413  1.00  28.17  ? 89  ARG A CZ  1 
ATOM   777  N  NH1 . ARG A 1 89  ? -15.732 17.182  13.560  1.00  27.42  ? 89  ARG A NH1 1 
ATOM   778  N  NH2 . ARG A 1 89  ? -17.380 18.087  14.890  1.00  37.36  ? 89  ARG A NH2 1 
ATOM   779  N  N   . LEU A 1 90  ? -16.352 9.179   14.658  1.00  10.88  ? 90  LEU A N   1 
ATOM   780  C  CA  . LEU A 1 90  ? -15.780 8.044   13.942  1.00  11.34  ? 90  LEU A CA  1 
ATOM   781  C  C   . LEU A 1 90  ? -14.888 8.507   12.808  1.00  10.92  ? 90  LEU A C   1 
ATOM   782  O  O   . LEU A 1 90  ? -15.330 9.293   11.937  1.00  13.06  ? 90  LEU A O   1 
ATOM   783  C  CB  . LEU A 1 90  ? -16.891 7.184   13.385  1.00  11.97  ? 90  LEU A CB  1 
ATOM   784  C  CG  . LEU A 1 90  ? -16.488 5.995   12.507  1.00  13.00  ? 90  LEU A CG  1 
ATOM   785  C  CD1 . LEU A 1 90  ? -15.695 4.962   13.325  1.00  13.10  ? 90  LEU A CD1 1 
ATOM   786  C  CD2 . LEU A 1 90  ? -17.684 5.311   11.905  1.00  16.35  ? 90  LEU A CD2 1 
ATOM   787  N  N   . LEU A 1 91  ? -13.649 8.034   12.802  1.00  10.91  ? 91  LEU A N   1 
ATOM   788  C  CA  . LEU A 1 91  ? -12.684 8.346   11.801  1.00  10.82  ? 91  LEU A CA  1 
ATOM   789  C  C   . LEU A 1 91  ? -12.515 7.267   10.771  1.00  9.74   ? 91  LEU A C   1 
ATOM   790  O  O   . LEU A 1 91  ? -12.502 7.476   9.563   1.00  12.05  ? 91  LEU A O   1 
ATOM   791  C  CB  . LEU A 1 91  ? -11.356 8.593   12.479  1.00  14.56  ? 91  LEU A CB  1 
ATOM   792  C  CG  . LEU A 1 91  ? -10.176 8.796   11.579  1.00  13.40  ? 91  LEU A CG  1 
ATOM   793  C  CD1 . LEU A 1 91  ? -10.362 10.050  10.805  1.00  17.50  ? 91  LEU A CD1 1 
ATOM   794  C  CD2 . LEU A 1 91  ? -8.892  8.751   12.427  1.00  20.55  ? 91  LEU A CD2 1 
ATOM   795  N  N   . GLN A 1 92  ? -12.392 6.012   11.256  1.00  10.56  ? 92  GLN A N   1 
ATOM   796  C  CA  . GLN A 1 92  ? -12.059 4.893   10.360  1.00  10.50  ? 92  GLN A CA  1 
ATOM   797  C  C   . GLN A 1 92  ? -12.292 3.605   11.144  1.00  9.61   ? 92  GLN A C   1 
ATOM   798  O  O   . GLN A 1 92  ? -12.357 3.612   12.376  1.00  9.75   ? 92  GLN A O   1 
ATOM   799  C  CB  . GLN A 1 92  ? -10.587 4.912   9.846   1.00  12.90  ? 92  GLN A CB  1 
ATOM   800  C  CG  . GLN A 1 92  ? -9.605  5.067   10.967  1.00  13.93  ? 92  GLN A CG  1 
ATOM   801  C  CD  . GLN A 1 92  ? -8.842  3.800   11.314  1.00  14.32  ? 92  GLN A CD  1 
ATOM   802  O  OE1 . GLN A 1 92  ? -9.371  2.691   11.301  1.00  12.93  ? 92  GLN A OE1 1 
ATOM   803  N  NE2 . GLN A 1 92  ? -7.640  4.001   11.779  1.00  19.95  ? 92  GLN A NE2 1 
ATOM   804  N  N   . PHE A 1 93  ? -12.461 2.510   10.396  1.00  10.27  ? 93  PHE A N   1 
ATOM   805  C  CA  . PHE A 1 93  ? -12.356 1.201   11.008  1.00  9.66   ? 93  PHE A CA  1 
ATOM   806  C  C   . PHE A 1 93  ? -11.398 0.351   10.231  1.00  9.75   ? 93  PHE A C   1 
ATOM   807  O  O   . PHE A 1 93  ? -11.144 0.598   9.019   1.00  10.54  ? 93  PHE A O   1 
ATOM   808  C  CB  . PHE A 1 93  ? -13.732 0.515   11.203  1.00  10.50  ? 93  PHE A CB  1 
ATOM   809  C  CG  . PHE A 1 93  ? -14.444 0.069   9.956   1.00  10.80  ? 93  PHE A CG  1 
ATOM   810  C  CD1 . PHE A 1 93  ? -14.068 -1.060  9.247   1.00  11.46  ? 93  PHE A CD1 1 
ATOM   811  C  CD2 . PHE A 1 93  ? -15.613 0.766   9.559   1.00  12.61  ? 93  PHE A CD2 1 
ATOM   812  C  CE1 . PHE A 1 93  ? -14.802 -1.460  8.139   1.00  13.04  ? 93  PHE A CE1 1 
ATOM   813  C  CE2 . PHE A 1 93  ? -16.328 0.337   8.435   1.00  14.14  ? 93  PHE A CE2 1 
ATOM   814  C  CZ  . PHE A 1 93  ? -15.922 -0.723  7.715   1.00  14.59  ? 93  PHE A CZ  1 
ATOM   815  N  N   . HIS A 1 94  ? -10.836 -0.627  10.888  1.00  9.34   ? 94  HIS A N   1 
ATOM   816  C  CA  . HIS A 1 94  ? -9.898  -1.560  10.312  1.00  8.61   ? 94  HIS A CA  1 
ATOM   817  C  C   . HIS A 1 94  ? -9.979  -2.861  11.104  1.00  8.38   ? 94  HIS A C   1 
ATOM   818  O  O   . HIS A 1 94  ? -10.651 -2.931  12.113  1.00  8.49   ? 94  HIS A O   1 
ATOM   819  C  CB  . HIS A 1 94  ? -8.468  -1.013  10.257  1.00  9.92   ? 94  HIS A CB  1 
ATOM   820  C  CG  . HIS A 1 94  ? -7.933  -0.739  11.647  1.00  8.85   ? 94  HIS A CG  1 
ATOM   821  N  ND1 . HIS A 1 94  ? -8.135  0.427   12.320  1.00  9.49   ? 94  HIS A ND1 1 
ATOM   822  C  CD2 . HIS A 1 94  ? -7.348  -1.598  12.536  1.00  8.41   ? 94  HIS A CD2 1 
ATOM   823  C  CE1 . HIS A 1 94  ? -7.613  0.303   13.566  1.00  8.75   ? 94  HIS A CE1 1 
ATOM   824  N  NE2 . HIS A 1 94  ? -7.149  -0.956  13.729  1.00  8.49   ? 94  HIS A NE2 1 
ATOM   825  N  N   . PHE A 1 95  ? -9.257  -3.872  10.630  1.00  8.19   ? 95  PHE A N   1 
ATOM   826  C  CA  . PHE A 1 95  ? -9.268  -5.190  11.260  1.00  8.15   ? 95  PHE A CA  1 
ATOM   827  C  C   . PHE A 1 95  ? -7.866  -5.669  11.500  1.00  7.62   ? 95  PHE A C   1 
ATOM   828  O  O   . PHE A 1 95  ? -6.909  -5.256  10.862  1.00  8.98   ? 95  PHE A O   1 
ATOM   829  C  CB  . PHE A 1 95  ? -9.989  -6.232  10.365  1.00  9.13   ? 95  PHE A CB  1 
ATOM   830  C  CG  . PHE A 1 95  ? -11.462 -5.937  10.097  1.00  8.93   ? 95  PHE A CG  1 
ATOM   831  C  CD1 . PHE A 1 95  ? -11.839 -5.047  9.115   1.00  10.56  ? 95  PHE A CD1 1 
ATOM   832  C  CD2 . PHE A 1 95  ? -12.480 -6.611  10.773  1.00  9.25   ? 95  PHE A CD2 1 
ATOM   833  C  CE1 . PHE A 1 95  ? -13.155 -4.844  8.791   1.00  11.45  ? 95  PHE A CE1 1 
ATOM   834  C  CE2 . PHE A 1 95  ? -13.787 -6.417  10.485  1.00  10.05  ? 95  PHE A CE2 1 
ATOM   835  C  CZ  . PHE A 1 95  ? -14.150 -5.488  9.489   1.00  10.92  ? 95  PHE A CZ  1 
ATOM   836  N  N   . HIS A 1 96  ? -7.771  -6.669  12.407  1.00  7.50   ? 96  HIS A N   1 
ATOM   837  C  CA  . HIS A 1 96  ? -6.611  -7.473  12.622  1.00  7.56   ? 96  HIS A CA  1 
ATOM   838  C  C   . HIS A 1 96  ? -7.060  -8.928  12.489  1.00  7.34   ? 96  HIS A C   1 
ATOM   839  O  O   . HIS A 1 96  ? -8.158  -9.242  12.971  1.00  7.57   ? 96  HIS A O   1 
ATOM   840  C  CB  . HIS A 1 96  ? -6.005  -7.228  14.031  1.00  8.32   ? 96  HIS A CB  1 
ATOM   841  C  CG  . HIS A 1 96  ? -5.708  -5.765  14.267  1.00  7.62   ? 96  HIS A CG  1 
ATOM   842  N  ND1 . HIS A 1 96  ? -4.488  -5.228  14.045  1.00  8.04   ? 96  HIS A ND1 1 
ATOM   843  C  CD2 . HIS A 1 96  ? -6.530  -4.763  14.701  1.00  7.69   ? 96  HIS A CD2 1 
ATOM   844  C  CE1 . HIS A 1 96  ? -4.501  -3.948  14.330  1.00  8.16   ? 96  HIS A CE1 1 
ATOM   845  N  NE2 . HIS A 1 96  ? -5.710  -3.611  14.721  1.00  7.51   ? 96  HIS A NE2 1 
ATOM   846  N  N   . TRP A 1 97  ? -6.257  -9.762  11.853  1.00  7.21   ? 97  TRP A N   1 
ATOM   847  C  CA  . TRP A 1 97  ? -6.675  -11.162 11.666  1.00  7.81   ? 97  TRP A CA  1 
ATOM   848  C  C   . TRP A 1 97  ? -5.514  -12.040 11.555  1.00  7.62   ? 97  TRP A C   1 
ATOM   849  O  O   . TRP A 1 97  ? -4.332  -11.624 11.457  1.00  8.82   ? 97  TRP A O   1 
ATOM   850  C  CB  . TRP A 1 97  ? -7.569  -11.298 10.446  1.00  8.52   ? 97  TRP A CB  1 
ATOM   851  C  CG  . TRP A 1 97  ? -6.906  -10.922 9.157   1.00  8.71   ? 97  TRP A CG  1 
ATOM   852  C  CD1 . TRP A 1 97  ? -6.238  -11.749 8.306   1.00  9.22   ? 97  TRP A CD1 1 
ATOM   853  C  CD2 . TRP A 1 97  ? -6.872  -9.610  8.562   1.00  8.47   ? 97  TRP A CD2 1 
ATOM   854  N  NE1 . TRP A 1 97  ? -5.808  -11.041 7.222   1.00  9.56   ? 97  TRP A NE1 1 
ATOM   855  C  CE2 . TRP A 1 97  ? -6.119  -9.726  7.351   1.00  8.87   ? 97  TRP A CE2 1 
ATOM   856  C  CE3 . TRP A 1 97  ? -7.379  -8.341  8.909   1.00  8.09   ? 97  TRP A CE3 1 
ATOM   857  C  CZ2 . TRP A 1 97  ? -5.925  -8.674  6.487   1.00  10.05  ? 97  TRP A CZ2 1 
ATOM   858  C  CZ3 . TRP A 1 97  ? -7.135  -7.237  8.050   1.00  9.99   ? 97  TRP A CZ3 1 
ATOM   859  C  CH2 . TRP A 1 97  ? -6.416  -7.409  6.862   1.00  10.64  ? 97  TRP A CH2 1 
ATOM   860  N  N   . GLY A 1 98  ? -5.791  -13.354 11.564  1.00  8.69   ? 98  GLY A N   1 
ATOM   861  C  CA  . GLY A 1 98  ? -4.751  -14.360 11.629  1.00  8.67   ? 98  GLY A CA  1 
ATOM   862  C  C   . GLY A 1 98  ? -4.575  -15.112 10.348  1.00  9.39   ? 98  GLY A C   1 
ATOM   863  O  O   . GLY A 1 98  ? -5.321  -14.976 9.375   1.00  9.59   ? 98  GLY A O   1 
ATOM   864  N  N   . SER A 1 99  ? -3.553  -15.974 10.318  1.00  10.01  ? 99  SER A N   1 
ATOM   865  C  CA  . SER A 1 99  ? -3.372  -16.943 9.241   1.00  11.43  ? 99  SER A CA  1 
ATOM   866  C  C   . SER A 1 99  ? -4.295  -18.166 9.392   1.00  11.49  ? 99  SER A C   1 
ATOM   867  O  O   . SER A 1 99  ? -4.542  -18.840 8.392   1.00  13.50  ? 99  SER A O   1 
ATOM   868  C  CB  . SER A 1 99  ? -1.899  -17.316 9.234   1.00  13.21  ? 99  SER A CB  1 
ATOM   869  O  OG  . SER A 1 99  ? -1.461  -17.760 10.509  1.00  13.23  ? 99  SER A OG  1 
ATOM   870  N  N   A LEU A 1 100 ? -4.654  -18.460 10.631  0.50  11.78  ? 100 LEU A N   1 
ATOM   871  N  N   B LEU A 1 100 ? -4.856  -18.410 10.548  0.50  10.53  ? 100 LEU A N   1 
ATOM   872  C  CA  A LEU A 1 100 ? -5.470  -19.615 11.054  0.50  11.35  ? 100 LEU A CA  1 
ATOM   873  C  CA  B LEU A 1 100 ? -5.820  -19.493 10.776  0.50  11.24  ? 100 LEU A CA  1 
ATOM   874  C  C   A LEU A 1 100 ? -6.583  -19.097 11.952  0.50  9.65   ? 100 LEU A C   1 
ATOM   875  C  C   B LEU A 1 100 ? -6.796  -18.982 11.788  0.50  11.55  ? 100 LEU A C   1 
ATOM   876  O  O   A LEU A 1 100 ? -6.306  -18.042 12.608  0.50  9.33   ? 100 LEU A O   1 
ATOM   877  O  O   B LEU A 1 100 ? -6.706  -17.891 12.373  0.50  10.17  ? 100 LEU A O   1 
ATOM   878  C  CB  A LEU A 1 100 ? -4.615  -20.532 11.884  0.50  14.32  ? 100 LEU A CB  1 
ATOM   879  C  CB  B LEU A 1 100 ? -5.170  -20.791 11.257  0.50  11.22  ? 100 LEU A CB  1 
ATOM   880  C  CG  A LEU A 1 100 ? -3.319  -20.969 11.243  0.50  17.59  ? 100 LEU A CG  1 
ATOM   881  C  CG  B LEU A 1 100 ? -4.306  -21.561 10.268  0.50  13.17  ? 100 LEU A CG  1 
ATOM   882  C  CD1 A LEU A 1 100 ? -2.491  -21.687 12.289  0.50  21.98  ? 100 LEU A CD1 1 
ATOM   883  C  CD1 B LEU A 1 100 ? -3.603  -22.739 10.907  0.50  16.02  ? 100 LEU A CD1 1 
ATOM   884  C  CD2 A LEU A 1 100 ? -3.738  -21.926 10.155  0.50  17.20  ? 100 LEU A CD2 1 
ATOM   885  C  CD2 B LEU A 1 100 ? -5.159  -22.067 9.110   0.50  14.13  ? 100 LEU A CD2 1 
ATOM   886  N  N   . ASP A 1 101 ? -7.809  -19.742 12.022  1.00  11.18  ? 101 ASP A N   1 
ATOM   887  C  CA  . ASP A 1 101 ? -8.916  -19.189 12.791  1.00  11.35  ? 101 ASP A CA  1 
ATOM   888  C  C   . ASP A 1 101 ? -8.651  -19.062 14.254  1.00  10.51  ? 101 ASP A C   1 
ATOM   889  O  O   . ASP A 1 101 ? -9.364  -18.349 14.910  1.00  12.62  ? 101 ASP A O   1 
ATOM   890  C  CB  . ASP A 1 101 ? -10.200 -20.019 12.555  1.00  14.07  ? 101 ASP A CB  1 
ATOM   891  C  CG  . ASP A 1 101 ? -10.696 -20.057 11.126  1.00  14.86  ? 101 ASP A CG  1 
ATOM   892  O  OD1 . ASP A 1 101 ? -10.261 -19.286 10.272  1.00  15.09  ? 101 ASP A OD1 1 
ATOM   893  O  OD2 . ASP A 1 101 ? -11.576 -20.957 10.912  1.00  21.16  ? 101 ASP A OD2 1 
ATOM   894  N  N   . GLY A 1 102 ? -7.647  -19.818 14.800  1.00  10.86  ? 102 GLY A N   1 
ATOM   895  C  CA  . GLY A 1 102 ? -7.308  -19.771 16.208  1.00  12.12  ? 102 GLY A CA  1 
ATOM   896  C  C   . GLY A 1 102 ? -6.476  -18.606 16.646  1.00  9.95   ? 102 GLY A C   1 
ATOM   897  O  O   . GLY A 1 102 ? -6.075  -18.617 17.826  1.00  11.55  ? 102 GLY A O   1 
ATOM   898  N  N   A GLN A 1 103 ? -6.409  -17.603 15.769  0.50  10.17  ? 103 GLN A N   1 
ATOM   899  N  N   B GLN A 1 103 ? -6.013  -17.695 15.786  0.50  8.51   ? 103 GLN A N   1 
ATOM   900  C  CA  A GLN A 1 103 ? -5.631  -16.451 16.094  0.50  9.43   ? 103 GLN A CA  1 
ATOM   901  C  CA  B GLN A 1 103 ? -5.333  -16.468 16.262  0.50  7.80   ? 103 GLN A CA  1 
ATOM   902  C  C   A GLN A 1 103 ? -6.037  -15.315 15.236  0.50  8.18   ? 103 GLN A C   1 
ATOM   903  C  C   B GLN A 1 103 ? -5.759  -15.370 15.294  0.50  7.58   ? 103 GLN A C   1 
ATOM   904  O  O   A GLN A 1 103 ? -6.642  -15.515 14.146  0.50  7.89   ? 103 GLN A O   1 
ATOM   905  O  O   B GLN A 1 103 ? -6.206  -15.625 14.197  0.50  7.44   ? 103 GLN A O   1 
ATOM   906  C  CB  A GLN A 1 103 ? -4.134  -16.693 16.011  0.50  8.87   ? 103 GLN A CB  1 
ATOM   907  C  CB  B GLN A 1 103 ? -3.834  -16.590 16.366  0.50  9.25   ? 103 GLN A CB  1 
ATOM   908  C  CG  A GLN A 1 103 ? -3.543  -16.950 14.589  0.50  12.27  ? 103 GLN A CG  1 
ATOM   909  C  CG  B GLN A 1 103 ? -3.274  -16.960 15.020  0.50  10.60  ? 103 GLN A CG  1 
ATOM   910  C  CD  A GLN A 1 103 ? -2.179  -17.657 14.630  0.50  13.85  ? 103 GLN A CD  1 
ATOM   911  C  CD  B GLN A 1 103 ? -1.830  -17.347 15.067  0.50  12.10  ? 103 GLN A CD  1 
ATOM   912  O  OE1 A GLN A 1 103 ? -2.095  -18.800 15.076  0.50  15.97  ? 103 GLN A OE1 1 
ATOM   913  O  OE1 B GLN A 1 103 ? -1.341  -17.871 16.084  0.50  12.90  ? 103 GLN A OE1 1 
ATOM   914  N  NE2 A GLN A 1 103 ? -1.088  -16.953 14.217  0.50  15.31  ? 103 GLN A NE2 1 
ATOM   915  N  NE2 B GLN A 1 103 ? -1.159  -17.201 13.888  0.50  12.79  ? 103 GLN A NE2 1 
ATOM   916  N  N   . GLY A 1 104 ? -5.601  -14.125 15.701  1.00  8.01   ? 104 GLY A N   1 
ATOM   917  C  CA  . GLY A 1 104 ? -5.914  -12.965 14.891  1.00  7.87   ? 104 GLY A CA  1 
ATOM   918  C  C   . GLY A 1 104 ? -6.372  -11.771 15.712  1.00  7.23   ? 104 GLY A C   1 
ATOM   919  O  O   . GLY A 1 104 ? -6.094  -10.635 15.340  1.00  8.05   ? 104 GLY A O   1 
ATOM   920  N  N   . SER A 1 105 ? -7.072  -12.013 16.849  1.00  7.27   ? 105 SER A N   1 
ATOM   921  C  CA  . SER A 1 105 ? -7.445  -10.926 17.698  1.00  6.78   ? 105 SER A CA  1 
ATOM   922  C  C   . SER A 1 105 ? -6.295  -10.353 18.429  1.00  7.17   ? 105 SER A C   1 
ATOM   923  O  O   . SER A 1 105 ? -5.231  -11.024 18.651  1.00  8.47   ? 105 SER A O   1 
ATOM   924  C  CB  . SER A 1 105 ? -8.601  -11.247 18.624  1.00  7.50   ? 105 SER A CB  1 
ATOM   925  O  OG  . SER A 1 105 ? -8.226  -12.207 19.604  1.00  7.99   ? 105 SER A OG  1 
ATOM   926  N  N   . GLU A 1 106 ? -6.424  -9.096  18.827  1.00  6.87   ? 106 GLU A N   1 
ATOM   927  C  CA  . GLU A 1 106 ? -5.396  -8.400  19.651  1.00  7.00   ? 106 GLU A CA  1 
ATOM   928  C  C   . GLU A 1 106 ? -5.750  -8.575  21.110  1.00  6.72   ? 106 GLU A C   1 
ATOM   929  O  O   . GLU A 1 106 ? -4.977  -9.137  21.899  1.00  7.59   ? 106 GLU A O   1 
ATOM   930  C  CB  . GLU A 1 106 ? -5.318  -6.951  19.200  1.00  6.93   ? 106 GLU A CB  1 
ATOM   931  C  CG  . GLU A 1 106 ? -4.780  -6.860  17.779  1.00  8.80   ? 106 GLU A CG  1 
ATOM   932  C  CD  . GLU A 1 106 ? -4.178  -5.548  17.459  1.00  7.14   ? 106 GLU A CD  1 
ATOM   933  O  OE1 . GLU A 1 106 ? -4.804  -4.500  17.750  1.00  8.00   ? 106 GLU A OE1 1 
ATOM   934  O  OE2 . GLU A 1 106 ? -3.044  -5.550  16.916  1.00  8.50   ? 106 GLU A OE2 1 
ATOM   935  N  N   . HIS A 1 107 ? -6.923  -8.097  21.544  1.00  6.66   ? 107 HIS A N   1 
ATOM   936  C  CA  . HIS A 1 107 ? -7.395  -8.487  22.861  1.00  6.67   ? 107 HIS A CA  1 
ATOM   937  C  C   . HIS A 1 107 ? -7.679  -9.985  22.895  1.00  6.85   ? 107 HIS A C   1 
ATOM   938  O  O   . HIS A 1 107 ? -8.033  -10.597 21.865  1.00  7.29   ? 107 HIS A O   1 
ATOM   939  C  CB  . HIS A 1 107 ? -8.659  -7.700  23.202  1.00  7.12   ? 107 HIS A CB  1 
ATOM   940  C  CG  . HIS A 1 107 ? -8.319  -6.233  23.365  1.00  6.35   ? 107 HIS A CG  1 
ATOM   941  N  ND1 . HIS A 1 107 ? -8.358  -5.351  22.297  1.00  6.98   ? 107 HIS A ND1 1 
ATOM   942  C  CD2 . HIS A 1 107 ? -7.860  -5.522  24.421  1.00  6.95   ? 107 HIS A CD2 1 
ATOM   943  C  CE1 . HIS A 1 107 ? -7.903  -4.147  22.741  1.00  7.39   ? 107 HIS A CE1 1 
ATOM   944  N  NE2 . HIS A 1 107 ? -7.616  -4.226  24.017  1.00  7.27   ? 107 HIS A NE2 1 
ATOM   945  N  N   . THR A 1 108 ? -7.591  -10.539 24.086  1.00  7.27   ? 108 THR A N   1 
ATOM   946  C  CA  . THR A 1 108 ? -7.940  -11.914 24.347  1.00  7.66   ? 108 THR A CA  1 
ATOM   947  C  C   . THR A 1 108 ? -8.897  -11.927 25.530  1.00  7.54   ? 108 THR A C   1 
ATOM   948  O  O   . THR A 1 108 ? -8.922  -10.959 26.306  1.00  8.17   ? 108 THR A O   1 
ATOM   949  C  CB  . THR A 1 108 ? -6.690  -12.815 24.543  1.00  8.55   ? 108 THR A CB  1 
ATOM   950  O  OG1 . THR A 1 108 ? -5.874  -12.324 25.587  1.00  8.80   ? 108 THR A OG1 1 
ATOM   951  C  CG2 . THR A 1 108 ? -5.879  -12.858 23.265  1.00  8.66   ? 108 THR A CG2 1 
ATOM   952  N  N   . VAL A 1 109 ? -9.652  -13.007 25.666  1.00  8.07   ? 109 VAL A N   1 
ATOM   953  C  CA  . VAL A 1 109 ? -10.634 -13.096 26.749  1.00  9.01   ? 109 VAL A CA  1 
ATOM   954  C  C   . VAL A 1 109 ? -10.337 -14.379 27.497  1.00  8.56   ? 109 VAL A C   1 
ATOM   955  O  O   . VAL A 1 109 ? -10.476 -15.496 26.937  1.00  9.41   ? 109 VAL A O   1 
ATOM   956  C  CB  . VAL A 1 109 ? -12.052 -13.089 26.222  1.00  9.85   ? 109 VAL A CB  1 
ATOM   957  C  CG1 . VAL A 1 109 ? -13.098 -13.245 27.355  1.00  10.65  ? 109 VAL A CG1 1 
ATOM   958  C  CG2 . VAL A 1 109 ? -12.355 -11.798 25.457  1.00  10.80  ? 109 VAL A CG2 1 
ATOM   959  N  N   . ASP A 1 110 ? -9.820  -14.298 28.702  1.00  9.12   ? 110 ASP A N   1 
ATOM   960  C  CA  . ASP A 1 110 ? -9.356  -15.483 29.419  1.00  10.35  ? 110 ASP A CA  1 
ATOM   961  C  C   . ASP A 1 110 ? -8.407  -16.269 28.538  1.00  10.65  ? 110 ASP A C   1 
ATOM   962  O  O   . ASP A 1 110 ? -8.431  -17.525 28.503  1.00  11.34  ? 110 ASP A O   1 
ATOM   963  C  CB  . ASP A 1 110 ? -10.491 -16.338 29.909  1.00  11.45  ? 110 ASP A CB  1 
ATOM   964  C  CG  . ASP A 1 110 ? -11.316 -15.580 30.949  1.00  11.35  ? 110 ASP A CG  1 
ATOM   965  O  OD1 . ASP A 1 110 ? -10.827 -14.684 31.613  1.00  12.78  ? 110 ASP A OD1 1 
ATOM   966  O  OD2 . ASP A 1 110 ? -12.506 -15.941 31.076  1.00  14.44  ? 110 ASP A OD2 1 
ATOM   967  N  N   . LYS A 1 111 ? -7.507  -15.552 27.867  1.00  10.02  ? 111 LYS A N   1 
ATOM   968  C  CA  . LYS A 1 111 ? -6.507  -16.113 26.989  1.00  10.30  ? 111 LYS A CA  1 
ATOM   969  C  C   . LYS A 1 111 ? -7.041  -16.626 25.661  1.00  9.85   ? 111 LYS A C   1 
ATOM   970  O  O   . LYS A 1 111 ? -6.207  -16.974 24.785  1.00  11.53  ? 111 LYS A O   1 
ATOM   971  C  CB  . LYS A 1 111 ? -5.526  -17.096 27.649  1.00  12.60  ? 111 LYS A CB  1 
ATOM   972  C  CG  . LYS A 1 111 ? -4.797  -16.461 28.915  1.00  15.31  ? 111 LYS A CG  1 
ATOM   973  C  CD  . LYS A 1 111 ? -3.875  -15.301 28.559  1.00  17.31  ? 111 LYS A CD  1 
ATOM   974  C  CE  . LYS A 1 111 ? -3.184  -14.709 29.806  1.00  21.14  ? 111 LYS A CE  1 
ATOM   975  N  NZ  . LYS A 1 111 ? -1.973  -15.475 30.161  1.00  21.76  ? 111 LYS A NZ  1 
ATOM   976  N  N   . LYS A 1 112 ? -8.335  -16.609 25.448  1.00  9.24   ? 112 LYS A N   1 
ATOM   977  C  CA  . LYS A 1 112 ? -8.882  -17.019 24.139  1.00  10.30  ? 112 LYS A CA  1 
ATOM   978  C  C   . LYS A 1 112 ? -8.585  -15.961 23.093  1.00  9.10   ? 112 LYS A C   1 
ATOM   979  O  O   . LYS A 1 112 ? -8.879  -14.764 23.303  1.00  8.62   ? 112 LYS A O   1 
ATOM   980  C  CB  . LYS A 1 112 ? -10.415 -17.147 24.241  1.00  11.40  ? 112 LYS A CB  1 
ATOM   981  C  CG  . LYS A 1 112 ? -11.116 -17.497 22.900  1.00  12.26  ? 112 LYS A CG  1 
ATOM   982  C  CD  . LYS A 1 112 ? -12.627 -17.511 22.987  1.00  14.83  ? 112 LYS A CD  1 
ATOM   983  C  CE  . LYS A 1 112 ? -13.176 -17.715 21.605  1.00  15.42  ? 112 LYS A CE  1 
ATOM   984  N  NZ  . LYS A 1 112 ? -13.029 -19.085 21.159  1.00  18.10  ? 112 LYS A NZ  1 
ATOM   985  N  N   A LYS A 1 113 ? -8.218  -16.494 21.941  0.50  8.07   ? 113 LYS A N   1 
ATOM   986  N  N   B LYS A 1 113 ? -7.861  -16.335 22.018  0.50  7.98   ? 113 LYS A N   1 
ATOM   987  C  CA  A LYS A 1 113 ? -7.986  -15.668 20.815  0.50  8.14   ? 113 LYS A CA  1 
ATOM   988  C  CA  B LYS A 1 113 ? -7.724  -15.506 20.774  0.50  8.68   ? 113 LYS A CA  1 
ATOM   989  C  C   A LYS A 1 113 ? -9.140  -15.873 19.871  0.50  8.06   ? 113 LYS A C   1 
ATOM   990  C  C   B LYS A 1 113 ? -8.838  -15.809 19.774  0.50  9.11   ? 113 LYS A C   1 
ATOM   991  O  O   A LYS A 1 113 ? -9.650  -16.990 19.659  0.50  8.53   ? 113 LYS A O   1 
ATOM   992  O  O   B LYS A 1 113 ? -9.062  -16.980 19.471  0.50  8.98   ? 113 LYS A O   1 
ATOM   993  C  CB  A LYS A 1 113 ? -6.677  -16.137 20.158  0.50  8.15   ? 113 LYS A CB  1 
ATOM   994  C  CB  B LYS A 1 113 ? -6.383  -15.840 20.075  0.50  9.52   ? 113 LYS A CB  1 
ATOM   995  C  CG  A LYS A 1 113 ? -5.363  -15.791 20.859  0.50  8.86   ? 113 LYS A CG  1 
ATOM   996  C  CG  B LYS A 1 113 ? -5.170  -15.468 20.878  0.50  10.51  ? 113 LYS A CG  1 
ATOM   997  C  CD  A LYS A 1 113 ? -4.182  -16.397 20.132  0.50  10.40  ? 113 LYS A CD  1 
ATOM   998  C  CD  B LYS A 1 113 ? -3.922  -16.103 20.379  0.50  11.45  ? 113 LYS A CD  1 
ATOM   999  C  CE  A LYS A 1 113 ? -2.800  -15.914 20.645  0.50  11.92  ? 113 LYS A CE  1 
ATOM   1000 C  CE  B LYS A 1 113 ? -2.722  -15.520 21.129  0.50  13.08  ? 113 LYS A CE  1 
ATOM   1001 N  NZ  A LYS A 1 113 ? -2.372  -16.444 21.962  0.50  12.01  ? 113 LYS A NZ  1 
ATOM   1002 N  NZ  B LYS A 1 113 ? -1.570  -16.434 20.932  0.50  16.39  ? 113 LYS A NZ  1 
ATOM   1003 N  N   . TYR A 1 114 ? -9.549  -14.764 19.295  1.00  8.43   ? 114 TYR A N   1 
ATOM   1004 C  CA  . TYR A 1 114 ? -10.527 -14.824 18.252  1.00  8.77   ? 114 TYR A CA  1 
ATOM   1005 C  C   . TYR A 1 114 ? -9.863  -14.803 16.895  1.00  7.55   ? 114 TYR A C   1 
ATOM   1006 O  O   . TYR A 1 114 ? -8.701  -14.504 16.765  1.00  8.11   ? 114 TYR A O   1 
ATOM   1007 C  CB  . TYR A 1 114 ? -11.596 -13.738 18.392  1.00  8.64   ? 114 TYR A CB  1 
ATOM   1008 C  CG  . TYR A 1 114 ? -12.516 -13.936 19.534  1.00  8.56   ? 114 TYR A CG  1 
ATOM   1009 C  CD1 . TYR A 1 114 ? -12.228 -13.507 20.834  1.00  9.60   ? 114 TYR A CD1 1 
ATOM   1010 C  CD2 . TYR A 1 114 ? -13.734 -14.611 19.304  1.00  9.64   ? 114 TYR A CD2 1 
ATOM   1011 C  CE1 . TYR A 1 114 ? -13.139 -13.744 21.868  1.00  11.81  ? 114 TYR A CE1 1 
ATOM   1012 C  CE2 . TYR A 1 114 ? -14.694 -14.802 20.329  1.00  12.70  ? 114 TYR A CE2 1 
ATOM   1013 C  CZ  . TYR A 1 114 ? -14.379 -14.333 21.590  1.00  12.66  ? 114 TYR A CZ  1 
ATOM   1014 O  OH  . TYR A 1 114 ? -15.226 -14.476 22.671  1.00  18.02  ? 114 TYR A OH  1 
ATOM   1015 N  N   . ALA A 1 115 ? -10.634 -15.146 15.856  1.00  8.66   ? 115 ALA A N   1 
ATOM   1016 C  CA  . ALA A 1 115 ? -10.114 -15.158 14.487  1.00  8.21   ? 115 ALA A CA  1 
ATOM   1017 C  C   . ALA A 1 115 ? -9.719  -13.795 14.001  1.00  7.90   ? 115 ALA A C   1 
ATOM   1018 O  O   . ALA A 1 115 ? -8.856  -13.658 13.109  1.00  8.41   ? 115 ALA A O   1 
ATOM   1019 C  CB  . ALA A 1 115 ? -11.090 -15.816 13.557  1.00  9.41   ? 115 ALA A CB  1 
ATOM   1020 N  N   . ALA A 1 116 ? -10.382 -12.737 14.499  1.00  7.99   ? 116 ALA A N   1 
ATOM   1021 C  CA  . ALA A 1 116 ? -10.075 -11.395 14.029  1.00  7.57   ? 116 ALA A CA  1 
ATOM   1022 C  C   . ALA A 1 116 ? -10.639 -10.439 15.033  1.00  7.03   ? 116 ALA A C   1 
ATOM   1023 O  O   . ALA A 1 116 ? -11.404 -10.823 15.945  1.00  7.60   ? 116 ALA A O   1 
ATOM   1024 C  CB  . ALA A 1 116 ? -10.636 -11.146 12.573  1.00  8.40   ? 116 ALA A CB  1 
ATOM   1025 N  N   . GLU A 1 117 ? -10.316 -9.170  14.836  1.00  6.97   ? 117 GLU A N   1 
ATOM   1026 C  CA  . GLU A 1 117 ? -10.828 -8.094  15.706  1.00  6.95   ? 117 GLU A CA  1 
ATOM   1027 C  C   . GLU A 1 117 ? -11.004 -6.848  14.834  1.00  7.17   ? 117 GLU A C   1 
ATOM   1028 O  O   . GLU A 1 117 ? -10.104 -6.478  14.069  1.00  8.09   ? 117 GLU A O   1 
ATOM   1029 C  CB  . GLU A 1 117 ? -9.888  -7.861  16.888  1.00  7.10   ? 117 GLU A CB  1 
ATOM   1030 C  CG  . GLU A 1 117 ? -10.377 -6.890  17.932  1.00  8.17   ? 117 GLU A CG  1 
ATOM   1031 C  CD  . GLU A 1 117 ? -9.482  -6.835  19.151  1.00  6.94   ? 117 GLU A CD  1 
ATOM   1032 O  OE1 . GLU A 1 117 ? -8.844  -7.850  19.466  1.00  7.64   ? 117 GLU A OE1 1 
ATOM   1033 O  OE2 . GLU A 1 117 ? -9.425  -5.767  19.783  1.00  8.23   ? 117 GLU A OE2 1 
ATOM   1034 N  N   . LEU A 1 118 ? -12.168 -6.251  14.983  1.00  7.27   ? 118 LEU A N   1 
ATOM   1035 C  CA  . LEU A 1 118 ? -12.523 -5.007  14.292  1.00  7.41   ? 118 LEU A CA  1 
ATOM   1036 C  C   . LEU A 1 118 ? -12.298 -3.854  15.273  1.00  7.35   ? 118 LEU A C   1 
ATOM   1037 O  O   . LEU A 1 118 ? -12.757 -3.933  16.439  1.00  7.45   ? 118 LEU A O   1 
ATOM   1038 C  CB  . LEU A 1 118 ? -13.991 -5.135  13.966  1.00  8.65   ? 118 LEU A CB  1 
ATOM   1039 C  CG  . LEU A 1 118 ? -14.778 -3.853  13.583  1.00  9.50   ? 118 LEU A CG  1 
ATOM   1040 C  CD1 . LEU A 1 118 ? -14.187 -3.149  12.362  1.00  10.12  ? 118 LEU A CD1 1 
ATOM   1041 C  CD2 . LEU A 1 118 ? -16.268 -4.213  13.331  1.00  10.61  ? 118 LEU A CD2 1 
ATOM   1042 N  N   . HIS A 1 119 ? -11.676 -2.795  14.786  1.00  7.23   ? 119 HIS A N   1 
ATOM   1043 C  CA  . HIS A 1 119 ? -11.429 -1.567  15.581  1.00  7.31   ? 119 HIS A CA  1 
ATOM   1044 C  C   . HIS A 1 119 ? -12.144 -0.432  14.887  1.00  7.34   ? 119 HIS A C   1 
ATOM   1045 O  O   . HIS A 1 119 ? -11.776 -0.095  13.752  1.00  8.19   ? 119 HIS A O   1 
ATOM   1046 C  CB  . HIS A 1 119 ? -9.961  -1.282  15.707  1.00  7.47   ? 119 HIS A CB  1 
ATOM   1047 C  CG  . HIS A 1 119 ? -9.270  -2.275  16.593  1.00  7.16   ? 119 HIS A CG  1 
ATOM   1048 N  ND1 . HIS A 1 119 ? -7.946  -2.520  16.607  1.00  7.89   ? 119 HIS A ND1 1 
ATOM   1049 C  CD2 . HIS A 1 119 ? -9.802  -3.082  17.536  1.00  8.47   ? 119 HIS A CD2 1 
ATOM   1050 C  CE1 . HIS A 1 119 ? -7.647  -3.417  17.512  1.00  7.52   ? 119 HIS A CE1 1 
ATOM   1051 N  NE2 . HIS A 1 119 ? -8.765  -3.776  18.075  1.00  7.66   ? 119 HIS A NE2 1 
ATOM   1052 N  N   . LEU A 1 120 ? -13.098 0.189   15.547  1.00  7.40   ? 120 LEU A N   1 
ATOM   1053 C  CA  . LEU A 1 120 ? -13.732 1.448   15.084  1.00  8.66   ? 120 LEU A CA  1 
ATOM   1054 C  C   . LEU A 1 120 ? -13.102 2.558   15.902  1.00  7.69   ? 120 LEU A C   1 
ATOM   1055 O  O   . LEU A 1 120 ? -13.250 2.616   17.129  1.00  7.69   ? 120 LEU A O   1 
ATOM   1056 C  CB  . LEU A 1 120 ? -15.244 1.363   15.290  1.00  8.69   ? 120 LEU A CB  1 
ATOM   1057 C  CG  . LEU A 1 120 ? -15.906 0.292   14.392  1.00  9.80   ? 120 LEU A CG  1 
ATOM   1058 C  CD1 . LEU A 1 120 ? -16.709 -0.679  15.283  1.00  13.24  ? 120 LEU A CD1 1 
ATOM   1059 C  CD2 . LEU A 1 120 ? -16.832 0.955   13.371  1.00  12.98  ? 120 LEU A CD2 1 
ATOM   1060 N  N   . VAL A 1 121 ? -12.364 3.429   15.202  1.00  8.37   ? 121 VAL A N   1 
ATOM   1061 C  CA  . VAL A 1 121 ? -11.523 4.434   15.809  1.00  8.57   ? 121 VAL A CA  1 
ATOM   1062 C  C   . VAL A 1 121 ? -12.210 5.788   15.834  1.00  8.84   ? 121 VAL A C   1 
ATOM   1063 O  O   . VAL A 1 121 ? -12.656 6.255   14.757  1.00  10.39  ? 121 VAL A O   1 
ATOM   1064 C  CB  . VAL A 1 121 ? -10.175 4.547   15.078  1.00  9.74   ? 121 VAL A CB  1 
ATOM   1065 C  CG1 . VAL A 1 121 ? -9.297  5.609   15.721  1.00  10.78  ? 121 VAL A CG1 1 
ATOM   1066 C  CG2 . VAL A 1 121 ? -9.454  3.180   15.062  1.00  10.18  ? 121 VAL A CG2 1 
ATOM   1067 N  N   . HIS A 1 122 ? -12.342 6.386   17.001  1.00  8.73   ? 122 HIS A N   1 
ATOM   1068 C  CA  . HIS A 1 122 ? -13.024 7.667   17.168  1.00  8.92   ? 122 HIS A CA  1 
ATOM   1069 C  C   . HIS A 1 122 ? -12.157 8.625   17.891  1.00  9.60   ? 122 HIS A C   1 
ATOM   1070 O  O   . HIS A 1 122 ? -11.393 8.226   18.765  1.00  9.65   ? 122 HIS A O   1 
ATOM   1071 C  CB  . HIS A 1 122 ? -14.279 7.484   17.991  1.00  9.95   ? 122 HIS A CB  1 
ATOM   1072 C  CG  . HIS A 1 122 ? -15.187 6.343   17.612  1.00  9.10   ? 122 HIS A CG  1 
ATOM   1073 N  ND1 . HIS A 1 122 ? -14.871 5.072   17.875  1.00  9.22   ? 122 HIS A ND1 1 
ATOM   1074 C  CD2 . HIS A 1 122 ? -16.439 6.306   17.008  1.00  10.29  ? 122 HIS A CD2 1 
ATOM   1075 C  CE1 . HIS A 1 122 ? -15.860 4.295   17.418  1.00  10.21  ? 122 HIS A CE1 1 
ATOM   1076 N  NE2 . HIS A 1 122 ? -16.844 5.028   16.915  1.00  10.41  ? 122 HIS A NE2 1 
ATOM   1077 N  N   . TRP A 1 123 ? -12.316 9.943   17.620  1.00  9.52   ? 123 TRP A N   1 
ATOM   1078 C  CA  . TRP A 1 123 ? -11.454 10.946  18.335  1.00  9.42   ? 123 TRP A CA  1 
ATOM   1079 C  C   . TRP A 1 123 ? -12.353 11.951  19.037  1.00  9.17   ? 123 TRP A C   1 
ATOM   1080 O  O   . TRP A 1 123 ? -13.460 12.305  18.609  1.00  9.86   ? 123 TRP A O   1 
ATOM   1081 C  CB  . TRP A 1 123 ? -10.493 11.632  17.406  1.00  11.89  ? 123 TRP A CB  1 
ATOM   1082 C  CG  . TRP A 1 123 ? -11.040 12.304  16.207  1.00  13.68  ? 123 TRP A CG  1 
ATOM   1083 C  CD1 . TRP A 1 123 ? -11.320 11.723  15.019  1.00  15.21  ? 123 TRP A CD1 1 
ATOM   1084 C  CD2 . TRP A 1 123 ? -11.465 13.685  16.110  1.00  12.44  ? 123 TRP A CD2 1 
ATOM   1085 N  NE1 . TRP A 1 123 ? -11.863 12.626  14.155  1.00  15.75  ? 123 TRP A NE1 1 
ATOM   1086 C  CE2 . TRP A 1 123 ? -11.990 13.844  14.791  1.00  15.86  ? 123 TRP A CE2 1 
ATOM   1087 C  CE3 . TRP A 1 123 ? -11.392 14.772  16.957  1.00  14.90  ? 123 TRP A CE3 1 
ATOM   1088 C  CZ2 . TRP A 1 123 ? -12.432 15.065  14.318  1.00  15.13  ? 123 TRP A CZ2 1 
ATOM   1089 C  CZ3 . TRP A 1 123 ? -11.854 15.979  16.460  1.00  15.59  ? 123 TRP A CZ3 1 
ATOM   1090 C  CH2 . TRP A 1 123 ? -12.403 16.119  15.187  1.00  15.95  ? 123 TRP A CH2 1 
ATOM   1091 N  N   . ASN A 1 124 ? -11.836 12.452  20.154  1.00  9.68   ? 124 ASN A N   1 
ATOM   1092 C  CA  . ASN A 1 124 ? -12.592 13.360  21.032  1.00  9.98   ? 124 ASN A CA  1 
ATOM   1093 C  C   . ASN A 1 124 ? -12.662 14.743  20.417  1.00  10.11  ? 124 ASN A C   1 
ATOM   1094 O  O   . ASN A 1 124 ? -11.595 15.399  20.244  1.00  10.23  ? 124 ASN A O   1 
ATOM   1095 C  CB  . ASN A 1 124 ? -11.781 13.355  22.339  1.00  10.33  ? 124 ASN A CB  1 
ATOM   1096 C  CG  . ASN A 1 124 ? -12.540 13.998  23.466  1.00  11.40  ? 124 ASN A CG  1 
ATOM   1097 O  OD1 . ASN A 1 124 ? -13.381 14.910  23.253  1.00  12.35  ? 124 ASN A OD1 1 
ATOM   1098 N  ND2 . ASN A 1 124 ? -12.279 13.566  24.674  1.00  11.62  ? 124 ASN A ND2 1 
ATOM   1099 N  N   . THR A 1 125 ? -13.890 15.210  20.177  1.00  11.87  ? 125 THR A N   1 
ATOM   1100 C  CA  . THR A 1 125 ? -14.051 16.470  19.480  1.00  13.14  ? 125 THR A CA  1 
ATOM   1101 C  C   . THR A 1 125 ? -13.539 17.627  20.305  1.00  13.34  ? 125 THR A C   1 
ATOM   1102 O  O   . THR A 1 125 ? -13.362 18.704  19.709  1.00  14.67  ? 125 THR A O   1 
ATOM   1103 C  CB  . THR A 1 125 ? -15.482 16.656  19.096  1.00  17.00  ? 125 THR A CB  1 
ATOM   1104 O  OG1 . THR A 1 125 ? -16.279 16.741  20.308  1.00  20.92  ? 125 THR A OG1 1 
ATOM   1105 C  CG2 . THR A 1 125 ? -15.822 15.587  18.014  1.00  20.01  ? 125 THR A CG2 1 
ATOM   1106 N  N   . LYS A 1 126 ? -13.277 17.487  21.657  1.00  12.61  ? 126 LYS A N   1 
ATOM   1107 C  CA  . LYS A 1 126 ? -12.769 18.618  22.375  1.00  13.20  ? 126 LYS A CA  1 
ATOM   1108 C  C   . LYS A 1 126 ? -11.340 18.962  21.943  1.00  13.24  ? 126 LYS A C   1 
ATOM   1109 O  O   . LYS A 1 126 ? -10.926 20.058  22.318  1.00  15.78  ? 126 LYS A O   1 
ATOM   1110 C  CB  . LYS A 1 126 ? -12.898 18.373  23.852  1.00  16.58  ? 126 LYS A CB  1 
ATOM   1111 C  CG  . LYS A 1 126 ? -11.807 17.529  24.478  1.00  15.38  ? 126 LYS A CG  1 
ATOM   1112 C  CD  . LYS A 1 126 ? -12.346 17.102  25.812  1.00  24.78  ? 126 LYS A CD  1 
ATOM   1113 C  CE  . LYS A 1 126 ? -11.321 16.731  26.820  1.00  31.29  ? 126 LYS A CE  1 
ATOM   1114 N  NZ  . LYS A 1 126 ? -10.988 17.832  27.734  1.00  50.97  ? 126 LYS A NZ  1 
ATOM   1115 N  N   . TYR A 1 127 ? -10.655 18.105  21.200  1.00  10.85  ? 127 TYR A N   1 
ATOM   1116 C  CA  . TYR A 1 127 ? -9.323  18.396  20.726  1.00  11.28  ? 127 TYR A CA  1 
ATOM   1117 C  C   . TYR A 1 127 ? -9.247  18.847  19.304  1.00  11.05  ? 127 TYR A C   1 
ATOM   1118 O  O   . TYR A 1 127 ? -8.145  19.108  18.819  1.00  11.75  ? 127 TYR A O   1 
ATOM   1119 C  CB  . TYR A 1 127 ? -8.337  17.238  21.031  1.00  11.89  ? 127 TYR A CB  1 
ATOM   1120 C  CG  . TYR A 1 127 ? -8.302  16.889  22.510  1.00  11.66  ? 127 TYR A CG  1 
ATOM   1121 C  CD1 . TYR A 1 127 ? -7.931  17.852  23.483  1.00  12.52  ? 127 TYR A CD1 1 
ATOM   1122 C  CD2 . TYR A 1 127 ? -8.657  15.619  22.969  1.00  11.06  ? 127 TYR A CD2 1 
ATOM   1123 C  CE1 . TYR A 1 127 ? -7.960  17.541  24.817  1.00  13.61  ? 127 TYR A CE1 1 
ATOM   1124 C  CE2 . TYR A 1 127 ? -8.696  15.297  24.286  1.00  11.26  ? 127 TYR A CE2 1 
ATOM   1125 C  CZ  . TYR A 1 127 ? -8.303  16.245  25.247  1.00  12.18  ? 127 TYR A CZ  1 
ATOM   1126 O  OH  . TYR A 1 127 ? -8.281  16.042  26.548  1.00  14.26  ? 127 TYR A OH  1 
ATOM   1127 N  N   . GLY A 1 128 ? -10.403 18.904  18.644  1.00  11.48  ? 128 GLY A N   1 
ATOM   1128 C  CA  . GLY A 1 128 ? -10.488 19.595  17.347  1.00  12.47  ? 128 GLY A CA  1 
ATOM   1129 C  C   . GLY A 1 128 ? -10.015 18.790  16.145  1.00  11.39  ? 128 GLY A C   1 
ATOM   1130 O  O   . GLY A 1 128 ? -10.607 18.895  15.065  1.00  12.72  ? 128 GLY A O   1 
ATOM   1131 N  N   . ASP A 1 129 ? -8.952  17.967  16.272  1.00  12.14  ? 129 ASP A N   1 
ATOM   1132 C  CA  . ASP A 1 129 ? -8.495  17.156  15.127  1.00  12.18  ? 129 ASP A CA  1 
ATOM   1133 C  C   . ASP A 1 129 ? -7.788  15.906  15.708  1.00  11.72  ? 129 ASP A C   1 
ATOM   1134 O  O   . ASP A 1 129 ? -7.254  15.936  16.830  1.00  11.76  ? 129 ASP A O   1 
ATOM   1135 C  CB  . ASP A 1 129 ? -7.663  17.911  14.074  1.00  12.67  ? 129 ASP A CB  1 
ATOM   1136 C  CG  . ASP A 1 129 ? -6.273  18.286  14.552  1.00  12.23  ? 129 ASP A CG  1 
ATOM   1137 O  OD1 . ASP A 1 129 ? -5.477  17.392  14.915  1.00  15.36  ? 129 ASP A OD1 1 
ATOM   1138 O  OD2 . ASP A 1 129 ? -5.967  19.495  14.528  1.00  16.63  ? 129 ASP A OD2 1 
ATOM   1139 N  N   A VAL A 1 130 ? -7.856  14.844  14.934  0.50  11.14  ? 130 VAL A N   1 
ATOM   1140 N  N   B VAL A 1 130 ? -7.463  14.913  14.854  0.50  12.14  ? 130 VAL A N   1 
ATOM   1141 C  CA  A VAL A 1 130 ? -7.244  13.634  15.393  0.50  12.02  ? 130 VAL A CA  1 
ATOM   1142 C  CA  B VAL A 1 130 ? -6.940  13.576  15.318  0.50  11.96  ? 130 VAL A CA  1 
ATOM   1143 C  C   A VAL A 1 130 ? -5.774  13.766  15.789  0.50  10.46  ? 130 VAL A C   1 
ATOM   1144 C  C   B VAL A 1 130 ? -5.564  13.698  15.806  0.50  12.24  ? 130 VAL A C   1 
ATOM   1145 O  O   A VAL A 1 130 ? -5.439  13.140  16.744  0.50  9.41   ? 130 VAL A O   1 
ATOM   1146 O  O   B VAL A 1 130 ? -5.068  13.056  16.733  0.50  11.14  ? 130 VAL A O   1 
ATOM   1147 C  CB  A VAL A 1 130 ? -7.495  12.477  14.445  0.50  9.15   ? 130 VAL A CB  1 
ATOM   1148 C  CB  B VAL A 1 130 ? -6.951  12.565  14.171  0.50  14.25  ? 130 VAL A CB  1 
ATOM   1149 C  CG1 A VAL A 1 130 ? -6.681  12.690  13.186  0.50  10.50  ? 130 VAL A CG1 1 
ATOM   1150 C  CG1 B VAL A 1 130 ? -6.246  11.252  14.569  0.50  16.21  ? 130 VAL A CG1 1 
ATOM   1151 C  CG2 A VAL A 1 130 ? -7.104  11.152  15.071  0.50  9.96   ? 130 VAL A CG2 1 
ATOM   1152 C  CG2 B VAL A 1 130 ? -8.411  12.288  13.782  0.50  16.45  ? 130 VAL A CG2 1 
ATOM   1153 N  N   . GLY A 1 131 ? -4.881  14.523  15.081  1.00  11.91  ? 131 GLY A N   1 
ATOM   1154 C  CA  . GLY A 1 131 ? -3.541  14.663  15.402  1.00  12.61  ? 131 GLY A CA  1 
ATOM   1155 C  C   . GLY A 1 131 ? -3.305  15.266  16.831  1.00  11.28  ? 131 GLY A C   1 
ATOM   1156 O  O   . GLY A 1 131 ? -2.431  14.836  17.587  1.00  12.93  ? 131 GLY A O   1 
ATOM   1157 N  N   A LYS A 1 132 ? -4.164  16.232  17.206  0.50  10.91  ? 132 LYS A N   1 
ATOM   1158 N  N   B LYS A 1 132 ? -4.174  16.200  17.215  0.50  10.87  ? 132 LYS A N   1 
ATOM   1159 C  CA  A LYS A 1 132 ? -4.119  16.778  18.560  0.50  10.72  ? 132 LYS A CA  1 
ATOM   1160 C  CA  B LYS A 1 132 ? -4.113  16.762  18.546  0.50  11.26  ? 132 LYS A CA  1 
ATOM   1161 C  C   A LYS A 1 132 ? -4.550  15.691  19.517  0.50  9.69   ? 132 LYS A C   1 
ATOM   1162 C  C   B LYS A 1 132 ? -4.693  15.793  19.568  0.50  11.25  ? 132 LYS A C   1 
ATOM   1163 O  O   A LYS A 1 132 ? -3.906  15.507  20.577  0.50  8.88   ? 132 LYS A O   1 
ATOM   1164 O  O   B LYS A 1 132 ? -4.290  15.758  20.708  0.50  10.33  ? 132 LYS A O   1 
ATOM   1165 C  CB  A LYS A 1 132 ? -5.014  18.054  18.716  0.50  11.79  ? 132 LYS A CB  1 
ATOM   1166 C  CB  B LYS A 1 132 ? -4.871  18.101  18.533  0.50  11.03  ? 132 LYS A CB  1 
ATOM   1167 C  CG  A LYS A 1 132 ? -4.496  19.335  18.005  0.50  15.23  ? 132 LYS A CG  1 
ATOM   1168 C  CG  B LYS A 1 132 ? -4.109  19.245  17.841  0.50  12.50  ? 132 LYS A CG  1 
ATOM   1169 C  CD  A LYS A 1 132 ? -3.021  19.606  18.380  0.50  16.57  ? 132 LYS A CD  1 
ATOM   1170 C  CD  B LYS A 1 132 ? -3.132  19.842  18.875  0.50  14.26  ? 132 LYS A CD  1 
ATOM   1171 C  CE  A LYS A 1 132 ? -2.519  20.943  17.844  0.50  18.58  ? 132 LYS A CE  1 
ATOM   1172 C  CE  B LYS A 1 132 ? -2.516  21.127  18.328  0.50  16.82  ? 132 LYS A CE  1 
ATOM   1173 N  NZ  A LYS A 1 132 ? -1.653  21.574  18.874  0.50  25.81  ? 132 LYS A NZ  1 
ATOM   1174 N  NZ  B LYS A 1 132 ? -1.880  20.871  16.989  0.50  17.02  ? 132 LYS A NZ  1 
ATOM   1175 N  N   . ALA A 1 133 ? -5.676  14.985  19.173  1.00  9.96   ? 133 ALA A N   1 
ATOM   1176 C  CA  . ALA A 1 133 ? -6.241  13.984  20.058  1.00  10.34  ? 133 ALA A CA  1 
ATOM   1177 C  C   . ALA A 1 133 ? -5.214  12.905  20.380  1.00  10.26  ? 133 ALA A C   1 
ATOM   1178 O  O   . ALA A 1 133 ? -5.214  12.370  21.506  1.00  10.06  ? 133 ALA A O   1 
ATOM   1179 C  CB  . ALA A 1 133 ? -7.489  13.392  19.427  1.00  10.33  ? 133 ALA A CB  1 
ATOM   1180 N  N   . LEU A 1 134 ? -4.326  12.573  19.440  1.00  10.12  ? 134 LEU A N   1 
ATOM   1181 C  CA  . LEU A 1 134 ? -3.301  11.528  19.697  1.00  10.81  ? 134 LEU A CA  1 
ATOM   1182 C  C   . LEU A 1 134 ? -2.373  11.908  20.777  1.00  9.85   ? 134 LEU A C   1 
ATOM   1183 O  O   . LEU A 1 134 ? -1.647  11.042  21.296  1.00  12.62  ? 134 LEU A O   1 
ATOM   1184 C  CB  . LEU A 1 134 ? -2.524  11.272  18.393  1.00  12.06  ? 134 LEU A CB  1 
ATOM   1185 C  CG  . LEU A 1 134 ? -3.274  10.525  17.275  1.00  14.81  ? 134 LEU A CG  1 
ATOM   1186 C  CD1 . LEU A 1 134 ? -2.554  10.586  15.946  1.00  21.53  ? 134 LEU A CD1 1 
ATOM   1187 C  CD2 . LEU A 1 134 ? -3.600  9.110   17.637  1.00  16.79  ? 134 LEU A CD2 1 
ATOM   1188 N  N   . GLN A 1 135 ? -2.312  13.186  21.143  1.00  10.96  ? 135 GLN A N   1 
ATOM   1189 C  CA  . GLN A 1 135 ? -1.417  13.686  22.161  1.00  12.13  ? 135 GLN A CA  1 
ATOM   1190 C  C   . GLN A 1 135 ? -2.053  13.771  23.536  1.00  11.31  ? 135 GLN A C   1 
ATOM   1191 O  O   . GLN A 1 135 ? -1.459  14.312  24.451  1.00  13.51  ? 135 GLN A O   1 
ATOM   1192 C  CB  . GLN A 1 135 ? -0.844  15.069  21.729  1.00  13.36  ? 135 GLN A CB  1 
ATOM   1193 C  CG  . GLN A 1 135 ? -0.201  14.978  20.386  1.00  16.54  ? 135 GLN A CG  1 
ATOM   1194 C  CD  . GLN A 1 135 ? 0.327   16.318  19.953  1.00  17.88  ? 135 GLN A CD  1 
ATOM   1195 O  OE1 . GLN A 1 135 ? 1.132   16.886  20.635  1.00  28.35  ? 135 GLN A OE1 1 
ATOM   1196 N  NE2 . GLN A 1 135 ? -0.172  16.827  18.850  1.00  23.16  ? 135 GLN A NE2 1 
ATOM   1197 N  N   . GLN A 1 136 ? -3.269  13.233  23.709  1.00  10.07  ? 136 GLN A N   1 
ATOM   1198 C  CA  . GLN A 1 136 ? -4.009  13.387  24.942  1.00  10.46  ? 136 GLN A CA  1 
ATOM   1199 C  C   . GLN A 1 136 ? -4.416  12.034  25.496  1.00  9.44   ? 136 GLN A C   1 
ATOM   1200 O  O   . GLN A 1 136 ? -4.754  11.125  24.732  1.00  9.87   ? 136 GLN A O   1 
ATOM   1201 C  CB  . GLN A 1 136 ? -5.300  14.169  24.675  1.00  11.20  ? 136 GLN A CB  1 
ATOM   1202 C  CG  . GLN A 1 136 ? -4.985  15.595  24.059  1.00  13.85  ? 136 GLN A CG  1 
ATOM   1203 C  CD  . GLN A 1 136 ? -4.215  16.510  25.120  1.00  16.70  ? 136 GLN A CD  1 
ATOM   1204 O  OE1 . GLN A 1 136 ? -4.341  16.260  26.289  1.00  25.00  ? 136 GLN A OE1 1 
ATOM   1205 N  NE2 . GLN A 1 136 ? -3.582  17.529  24.696  1.00  25.17  ? 136 GLN A NE2 1 
ATOM   1206 N  N   . PRO A 1 137 ? -4.410  11.886  26.835  1.00  9.91   ? 137 PRO A N   1 
ATOM   1207 C  CA  . PRO A 1 137 ? -4.754  10.560  27.438  1.00  9.91   ? 137 PRO A CA  1 
ATOM   1208 C  C   . PRO A 1 137 ? -6.169  10.133  27.146  1.00  10.13  ? 137 PRO A C   1 
ATOM   1209 O  O   . PRO A 1 137 ? -6.431  8.931   27.178  1.00  12.84  ? 137 PRO A O   1 
ATOM   1210 C  CB  . PRO A 1 137 ? -4.477  10.753  28.937  1.00  12.88  ? 137 PRO A CB  1 
ATOM   1211 C  CG  . PRO A 1 137 ? -4.480  12.207  29.090  1.00  18.64  ? 137 PRO A CG  1 
ATOM   1212 C  CD  . PRO A 1 137 ? -3.946  12.820  27.855  1.00  12.15  ? 137 PRO A CD  1 
ATOM   1213 N  N   . ASP A 1 138 ? -7.051  11.066  26.856  1.00  9.99   ? 138 ASP A N   1 
ATOM   1214 C  CA  . ASP A 1 138 ? -8.435  10.800  26.551  1.00  10.18  ? 138 ASP A CA  1 
ATOM   1215 C  C   . ASP A 1 138 ? -8.764  11.244  25.099  1.00  9.79   ? 138 ASP A C   1 
ATOM   1216 O  O   . ASP A 1 138 ? -9.886  11.669  24.816  1.00  10.80  ? 138 ASP A O   1 
ATOM   1217 C  CB  . ASP A 1 138 ? -9.424  11.375  27.520  1.00  12.61  ? 138 ASP A CB  1 
ATOM   1218 C  CG  . ASP A 1 138 ? -9.339  12.881  27.617  1.00  13.59  ? 138 ASP A CG  1 
ATOM   1219 O  OD1 . ASP A 1 138 ? -8.361  13.462  27.081  1.00  13.16  ? 138 ASP A OD1 1 
ATOM   1220 O  OD2 . ASP A 1 138 ? -10.132 13.481  28.356  1.00  15.89  ? 138 ASP A OD2 1 
ATOM   1221 N  N   . GLY A 1 139 ? -7.794  11.142  24.201  1.00  8.87   ? 139 GLY A N   1 
ATOM   1222 C  CA  . GLY A 1 139 ? -8.001  11.624  22.890  1.00  9.27   ? 139 GLY A CA  1 
ATOM   1223 C  C   . GLY A 1 139 ? -8.816  10.742  21.990  1.00  7.61   ? 139 GLY A C   1 
ATOM   1224 O  O   . GLY A 1 139 ? -9.499  11.243  21.089  1.00  9.37   ? 139 GLY A O   1 
ATOM   1225 N  N   A LEU A 1 140 ? -8.697  9.413   22.091  0.50  8.32   ? 140 LEU A N   1 
ATOM   1226 N  N   B LEU A 1 140 ? -8.688  9.420   22.180  0.50  8.32   ? 140 LEU A N   1 
ATOM   1227 C  CA  A LEU A 1 140 ? -9.384  8.488   21.168  0.50  8.12   ? 140 LEU A CA  1 
ATOM   1228 C  CA  B LEU A 1 140 ? -9.326  8.439   21.287  0.50  8.10   ? 140 LEU A CA  1 
ATOM   1229 C  C   A LEU A 1 140 ? -10.195 7.548   21.984  0.50  7.18   ? 140 LEU A C   1 
ATOM   1230 C  C   B LEU A 1 140 ? -10.187 7.508   22.052  0.50  7.50   ? 140 LEU A C   1 
ATOM   1231 O  O   A LEU A 1 140 ? -9.922  7.268   23.142  0.50  8.20   ? 140 LEU A O   1 
ATOM   1232 O  O   B LEU A 1 140 ? -9.920  7.181   23.238  0.50  8.09   ? 140 LEU A O   1 
ATOM   1233 C  CB  A LEU A 1 140 ? -8.359  7.678   20.365  0.50  9.41   ? 140 LEU A CB  1 
ATOM   1234 C  CB  B LEU A 1 140 ? -8.264  7.634   20.512  0.50  8.68   ? 140 LEU A CB  1 
ATOM   1235 C  CG  A LEU A 1 140 ? -7.416  8.373   19.387  0.50  9.57   ? 140 LEU A CG  1 
ATOM   1236 C  CG  B LEU A 1 140 ? -7.883  8.250   19.150  0.50  9.04   ? 140 LEU A CG  1 
ATOM   1237 C  CD1 A LEU A 1 140 ? -6.584  7.274   18.710  0.50  10.92  ? 140 LEU A CD1 1 
ATOM   1238 C  CD1 B LEU A 1 140 ? -7.128  9.554   19.365  0.50  10.95  ? 140 LEU A CD1 1 
ATOM   1239 C  CD2 A LEU A 1 140 ? -8.161  9.209   18.366  0.50  10.23  ? 140 LEU A CD2 1 
ATOM   1240 C  CD2 B LEU A 1 140 ? -7.029  7.275   18.357  0.50  10.58  ? 140 LEU A CD2 1 
ATOM   1241 N  N   . ALA A 1 141 ? -11.206 6.996   21.367  1.00  8.04   ? 141 ALA A N   1 
ATOM   1242 C  CA  . ALA A 1 141 ? -12.012 5.861   21.914  1.00  8.68   ? 141 ALA A CA  1 
ATOM   1243 C  C   . ALA A 1 141 ? -12.064 4.871   20.782  1.00  7.46   ? 141 ALA A C   1 
ATOM   1244 O  O   . ALA A 1 141 ? -12.498 5.207   19.657  1.00  9.18   ? 141 ALA A O   1 
ATOM   1245 C  CB  . ALA A 1 141 ? -13.403 6.329   22.281  1.00  9.96   ? 141 ALA A CB  1 
ATOM   1246 N  N   . VAL A 1 142 ? -11.670 3.625   21.081  1.00  7.90   ? 142 VAL A N   1 
ATOM   1247 C  CA  . VAL A 1 142 ? -11.684 2.569   20.066  1.00  7.93   ? 142 VAL A CA  1 
ATOM   1248 C  C   . VAL A 1 142 ? -12.663 1.520   20.561  1.00  7.11   ? 142 VAL A C   1 
ATOM   1249 O  O   . VAL A 1 142 ? -12.560 1.016   21.683  1.00  7.60   ? 142 VAL A O   1 
ATOM   1250 C  CB  . VAL A 1 142 ? -10.310 1.977   19.758  1.00  8.41   ? 142 VAL A CB  1 
ATOM   1251 C  CG1 . VAL A 1 142 ? -10.426 0.967   18.638  1.00  8.78   ? 142 VAL A CG1 1 
ATOM   1252 C  CG2 . VAL A 1 142 ? -9.335  3.092   19.319  1.00  10.17  ? 142 VAL A CG2 1 
ATOM   1253 N  N   . LEU A 1 143 ? -13.640 1.252   19.709  1.00  7.22   ? 143 LEU A N   1 
ATOM   1254 C  CA  . LEU A 1 143 ? -14.608 0.189   19.927  1.00  7.71   ? 143 LEU A CA  1 
ATOM   1255 C  C   . LEU A 1 143 ? -14.046 -1.055  19.288  1.00  7.48   ? 143 LEU A C   1 
ATOM   1256 O  O   . LEU A 1 143 ? -13.849 -1.089  18.047  1.00  8.92   ? 143 LEU A O   1 
ATOM   1257 C  CB  . LEU A 1 143 ? -15.961 0.663   19.349  1.00  9.97   ? 143 LEU A CB  1 
ATOM   1258 C  CG  . LEU A 1 143 ? -17.136 -0.261  19.507  1.00  11.27  ? 143 LEU A CG  1 
ATOM   1259 C  CD1 . LEU A 1 143 ? -17.384 -0.626  20.962  1.00  13.34  ? 143 LEU A CD1 1 
ATOM   1260 C  CD2 . LEU A 1 143 ? -18.415 0.332   18.868  1.00  12.60  ? 143 LEU A CD2 1 
ATOM   1261 N  N   . GLY A 1 144 ? -13.813 -2.083  20.068  1.00  7.76   ? 144 GLY A N   1 
ATOM   1262 C  CA  . GLY A 1 144 ? -13.230 -3.340  19.599  1.00  7.47   ? 144 GLY A CA  1 
ATOM   1263 C  C   . GLY A 1 144 ? -14.307 -4.413  19.592  1.00  6.87   ? 144 GLY A C   1 
ATOM   1264 O  O   . GLY A 1 144 ? -15.046 -4.561  20.559  1.00  8.10   ? 144 GLY A O   1 
ATOM   1265 N  N   . ILE A 1 145 ? -14.365 -5.179  18.496  1.00  6.69   ? 145 ILE A N   1 
ATOM   1266 C  CA  . ILE A 1 145 ? -15.376 -6.192  18.298  1.00  7.61   ? 145 ILE A CA  1 
ATOM   1267 C  C   . ILE A 1 145 ? -14.676 -7.454  17.811  1.00  7.14   ? 145 ILE A C   1 
ATOM   1268 O  O   . ILE A 1 145 ? -13.935 -7.406  16.816  1.00  8.18   ? 145 ILE A O   1 
ATOM   1269 C  CB  . ILE A 1 145 ? -16.461 -5.723  17.316  1.00  8.42   ? 145 ILE A CB  1 
ATOM   1270 C  CG1 . ILE A 1 145 ? -17.113 -4.444  17.812  1.00  10.94  ? 145 ILE A CG1 1 
ATOM   1271 C  CG2 . ILE A 1 145 ? -17.464 -6.849  17.075  1.00  10.60  ? 145 ILE A CG2 1 
ATOM   1272 C  CD1 . ILE A 1 145 ? -18.129 -3.827  16.896  1.00  10.98  ? 145 ILE A CD1 1 
ATOM   1273 N  N   . PHE A 1 146 ? -14.870 -8.543  18.509  1.00  6.97   ? 146 PHE A N   1 
ATOM   1274 C  CA  . PHE A 1 146 ? -14.287 -9.821  18.107  1.00  7.16   ? 146 PHE A CA  1 
ATOM   1275 C  C   . PHE A 1 146 ? -15.028 -10.435 16.933  1.00  7.58   ? 146 PHE A C   1 
ATOM   1276 O  O   . PHE A 1 146 ? -16.249 -10.309 16.892  1.00  8.69   ? 146 PHE A O   1 
ATOM   1277 C  CB  . PHE A 1 146 ? -14.293 -10.779 19.286  1.00  7.28   ? 146 PHE A CB  1 
ATOM   1278 C  CG  . PHE A 1 146 ? -13.434 -10.330 20.465  1.00  7.17   ? 146 PHE A CG  1 
ATOM   1279 C  CD1 . PHE A 1 146 ? -12.075 -10.127 20.292  1.00  7.28   ? 146 PHE A CD1 1 
ATOM   1280 C  CD2 . PHE A 1 146 ? -14.011 -10.068 21.715  1.00  8.09   ? 146 PHE A CD2 1 
ATOM   1281 C  CE1 . PHE A 1 146 ? -11.268 -9.746  21.354  1.00  7.34   ? 146 PHE A CE1 1 
ATOM   1282 C  CE2 . PHE A 1 146 ? -13.219 -9.673  22.763  1.00  7.79   ? 146 PHE A CE2 1 
ATOM   1283 C  CZ  . PHE A 1 146 ? -11.839 -9.570  22.583  1.00  7.87   ? 146 PHE A CZ  1 
ATOM   1284 N  N   . LEU A 1 147 ? -14.322 -11.155 16.135  1.00  7.66   ? 147 LEU A N   1 
ATOM   1285 C  CA  . LEU A 1 147 ? -14.898 -11.940 15.027  1.00  8.00   ? 147 LEU A CA  1 
ATOM   1286 C  C   . LEU A 1 147 ? -14.562 -13.417 15.287  1.00  8.13   ? 147 LEU A C   1 
ATOM   1287 O  O   . LEU A 1 147 ? -13.383 -13.773 15.500  1.00  8.61   ? 147 LEU A O   1 
ATOM   1288 C  CB  . LEU A 1 147 ? -14.248 -11.564 13.680  1.00  8.40   ? 147 LEU A CB  1 
ATOM   1289 C  CG  . LEU A 1 147 ? -14.853 -10.320 12.993  1.00  9.26   ? 147 LEU A CG  1 
ATOM   1290 C  CD1 . LEU A 1 147 ? -14.666 -9.043  13.840  1.00  10.25  ? 147 LEU A CD1 1 
ATOM   1291 C  CD2 . LEU A 1 147 ? -14.205 -10.116 11.646  1.00  10.68  ? 147 LEU A CD2 1 
ATOM   1292 N  N   . LYS A 1 148 ? -15.593 -14.237 15.178  1.00  8.84   ? 148 LYS A N   1 
ATOM   1293 C  CA  . LYS A 1 148 ? -15.415 -15.687 15.159  1.00  9.66   ? 148 LYS A CA  1 
ATOM   1294 C  C   . LYS A 1 148 ? -15.925 -16.177 13.819  1.00  10.18  ? 148 LYS A C   1 
ATOM   1295 O  O   . LYS A 1 148 ? -16.713 -15.533 13.145  1.00  10.92  ? 148 LYS A O   1 
ATOM   1296 C  CB  . LYS A 1 148 ? -16.152 -16.371 16.307  1.00  10.36  ? 148 LYS A CB  1 
ATOM   1297 C  CG  . LYS A 1 148 ? -17.671 -16.232 16.256  1.00  12.69  ? 148 LYS A CG  1 
ATOM   1298 C  CD  . LYS A 1 148 ? -18.263 -16.936 17.493  1.00  18.00  ? 148 LYS A CD  1 
ATOM   1299 C  CE  . LYS A 1 148 ? -19.701 -17.119 17.282  1.00  25.83  ? 148 LYS A CE  1 
ATOM   1300 N  NZ  . LYS A 1 148 ? -20.287 -17.844 18.439  1.00  36.76  ? 148 LYS A NZ  1 
ATOM   1301 N  N   . VAL A 1 149 ? -15.472 -17.368 13.405  1.00  10.80  ? 149 VAL A N   1 
ATOM   1302 C  CA  . VAL A 1 149 ? -15.807 -17.925 12.129  1.00  11.17  ? 149 VAL A CA  1 
ATOM   1303 C  C   . VAL A 1 149 ? -16.995 -18.857 12.269  1.00  12.89  ? 149 VAL A C   1 
ATOM   1304 O  O   . VAL A 1 149 ? -16.941 -19.821 13.050  1.00  15.54  ? 149 VAL A O   1 
ATOM   1305 C  CB  . VAL A 1 149 ? -14.614 -18.657 11.511  1.00  13.04  ? 149 VAL A CB  1 
ATOM   1306 C  CG1 . VAL A 1 149 ? -15.057 -19.360 10.212  1.00  15.78  ? 149 VAL A CG1 1 
ATOM   1307 C  CG2 . VAL A 1 149 ? -13.503 -17.689 11.259  1.00  15.64  ? 149 VAL A CG2 1 
ATOM   1308 N  N   . GLY A 1 150 ? -18.039 -18.573 11.540  1.00  13.30  ? 150 GLY A N   1 
ATOM   1309 C  CA  . GLY A 1 150 ? -19.259 -19.439 11.621  1.00  17.22  ? 150 GLY A CA  1 
ATOM   1310 C  C   . GLY A 1 150 ? -20.116 -18.947 10.473  1.00  15.67  ? 150 GLY A C   1 
ATOM   1311 O  O   . GLY A 1 150 ? -19.699 -19.051 9.275   1.00  15.60  ? 150 GLY A O   1 
ATOM   1312 N  N   A SER A 1 151 ? -21.316 -18.414 10.757  0.50  16.16  ? 151 SER A N   1 
ATOM   1313 N  N   B SER A 1 151 ? -21.308 -18.432 10.773  0.50  16.59  ? 151 SER A N   1 
ATOM   1314 C  CA  A SER A 1 151 ? -22.217 -17.865 9.733   0.50  17.06  ? 151 SER A CA  1 
ATOM   1315 C  CA  B SER A 1 151 ? -22.178 -17.821 9.789   0.50  16.28  ? 151 SER A CA  1 
ATOM   1316 C  C   A SER A 1 151 ? -21.718 -16.521 9.215   0.50  14.68  ? 151 SER A C   1 
ATOM   1317 C  C   B SER A 1 151 ? -21.484 -16.607 9.150   0.50  13.88  ? 151 SER A C   1 
ATOM   1318 O  O   A SER A 1 151 ? -21.145 -15.739 9.974   0.50  11.56  ? 151 SER A O   1 
ATOM   1319 O  O   B SER A 1 151 ? -20.560 -16.014 9.791   0.50  13.24  ? 151 SER A O   1 
ATOM   1320 C  CB  A SER A 1 151 ? -23.631 -17.709 10.267  0.50  19.05  ? 151 SER A CB  1 
ATOM   1321 C  CB  B SER A 1 151 ? -23.482 -17.423 10.466  0.50  19.36  ? 151 SER A CB  1 
ATOM   1322 O  OG  A SER A 1 151 ? -23.709 -16.714 11.257  0.50  21.55  ? 151 SER A OG  1 
ATOM   1323 O  OG  B SER A 1 151 ? -24.057 -18.588 11.045  0.50  22.38  ? 151 SER A OG  1 
ATOM   1324 N  N   . ALA A 1 152 ? -21.958 -16.229 7.946   1.00  14.08  ? 152 ALA A N   1 
ATOM   1325 C  CA  . ALA A 1 152 ? -21.567 -14.941 7.326   1.00  14.27  ? 152 ALA A CA  1 
ATOM   1326 C  C   . ALA A 1 152 ? -22.190 -13.762 8.038   1.00  14.17  ? 152 ALA A C   1 
ATOM   1327 O  O   . ALA A 1 152 ? -23.339 -13.843 8.477   1.00  16.17  ? 152 ALA A O   1 
ATOM   1328 C  CB  . ALA A 1 152 ? -21.929 -14.947 5.842   1.00  17.68  ? 152 ALA A CB  1 
ATOM   1329 N  N   . LYS A 1 153 ? -21.448 -12.656 8.053   1.00  14.37  ? 153 LYS A N   1 
ATOM   1330 C  CA  . LYS A 1 153 ? -22.023 -11.351 8.503   1.00  14.70  ? 153 LYS A CA  1 
ATOM   1331 C  C   . LYS A 1 153 ? -22.472 -10.623 7.252   1.00  14.95  ? 153 LYS A C   1 
ATOM   1332 O  O   . LYS A 1 153 ? -21.636 -10.159 6.460   1.00  14.67  ? 153 LYS A O   1 
ATOM   1333 C  CB  . LYS A 1 153 ? -20.939 -10.541 9.245   1.00  14.45  ? 153 LYS A CB  1 
ATOM   1334 C  CG  . LYS A 1 153 ? -21.442 -9.358  9.969   1.00  15.81  ? 153 LYS A CG  1 
ATOM   1335 C  CD  . LYS A 1 153 ? -22.362 -9.716  11.111  1.00  18.69  ? 153 LYS A CD  1 
ATOM   1336 C  CE  . LYS A 1 153 ? -22.336 -8.568  12.064  1.00  21.58  ? 153 LYS A CE  1 
ATOM   1337 N  NZ  . LYS A 1 153 ? -23.342 -8.861  13.096  1.00  24.10  ? 153 LYS A NZ  1 
ATOM   1338 N  N   . PRO A 1 154 ? -23.773 -10.496 7.003   1.00  17.02  ? 154 PRO A N   1 
ATOM   1339 C  CA  . PRO A 1 154 ? -24.165 -9.876  5.694   1.00  18.59  ? 154 PRO A CA  1 
ATOM   1340 C  C   . PRO A 1 154 ? -23.659 -8.416  5.540   1.00  17.31  ? 154 PRO A C   1 
ATOM   1341 O  O   . PRO A 1 154 ? -23.231 -8.012  4.489   1.00  19.80  ? 154 PRO A O   1 
ATOM   1342 C  CB  . PRO A 1 154 ? -25.707 -9.944  5.745   1.00  18.97  ? 154 PRO A CB  1 
ATOM   1343 C  CG  . PRO A 1 154 ? -26.011 -10.990 6.768   1.00  25.38  ? 154 PRO A CG  1 
ATOM   1344 C  CD  . PRO A 1 154 ? -24.927 -11.004 7.774   1.00  19.12  ? 154 PRO A CD  1 
ATOM   1345 N  N   . GLY A 1 155 ? -23.557 -7.718  6.675   1.00  18.54  ? 155 GLY A N   1 
ATOM   1346 C  CA  . GLY A 1 155 ? -23.061 -6.320  6.662   1.00  20.30  ? 155 GLY A CA  1 
ATOM   1347 C  C   . GLY A 1 155 ? -21.586 -6.145  6.387   1.00  17.14  ? 155 GLY A C   1 
ATOM   1348 O  O   . GLY A 1 155 ? -21.178 -5.030  6.165   1.00  20.63  ? 155 GLY A O   1 
ATOM   1349 N  N   . LEU A 1 156 ? -20.837 -7.236  6.439   1.00  16.29  ? 156 LEU A N   1 
ATOM   1350 C  CA  . LEU A 1 156 ? -19.451 -7.245  6.018   1.00  15.86  ? 156 LEU A CA  1 
ATOM   1351 C  C   . LEU A 1 156 ? -19.233 -7.497  4.522   1.00  13.54  ? 156 LEU A C   1 
ATOM   1352 O  O   . LEU A 1 156 ? -18.108 -7.239  4.001   1.00  14.22  ? 156 LEU A O   1 
ATOM   1353 C  CB  . LEU A 1 156 ? -18.731 -8.289  6.892   1.00  14.12  ? 156 LEU A CB  1 
ATOM   1354 C  CG  . LEU A 1 156 ? -17.205 -8.368  6.709   1.00  14.24  ? 156 LEU A CG  1 
ATOM   1355 C  CD1 . LEU A 1 156 ? -16.464 -7.061  7.042   1.00  15.11  ? 156 LEU A CD1 1 
ATOM   1356 C  CD2 . LEU A 1 156 ? -16.659 -9.556  7.543   1.00  15.07  ? 156 LEU A CD2 1 
ATOM   1357 N  N   . GLN A 1 157 ? -20.235 -8.067  3.808   1.00  15.06  ? 157 GLN A N   1 
ATOM   1358 C  CA  . GLN A 1 157 ? -19.962 -8.532  2.435   1.00  16.92  ? 157 GLN A CA  1 
ATOM   1359 C  C   . GLN A 1 157 ? -19.521 -7.398  1.558   1.00  14.76  ? 157 GLN A C   1 
ATOM   1360 O  O   . GLN A 1 157 ? -18.642 -7.653  0.723   1.00  15.61  ? 157 GLN A O   1 
ATOM   1361 C  CB  . GLN A 1 157 ? -21.168 -9.320  1.878   1.00  19.44  ? 157 GLN A CB  1 
ATOM   1362 C  CG  . GLN A 1 157 ? -20.746 -10.062 0.598   1.00  21.35  ? 157 GLN A CG  1 
ATOM   1363 C  CD  . GLN A 1 157 ? -19.661 -11.135 0.856   1.00  19.97  ? 157 GLN A CD  1 
ATOM   1364 O  OE1 . GLN A 1 157 ? -19.586 -11.678 1.976   1.00  17.76  ? 157 GLN A OE1 1 
ATOM   1365 N  NE2 . GLN A 1 157 ? -18.826 -11.472 -0.175  1.00  21.95  ? 157 GLN A NE2 1 
ATOM   1366 N  N   . LYS A 1 158 ? -20.088 -6.193  1.686   1.00  16.55  ? 158 LYS A N   1 
ATOM   1367 C  CA  . LYS A 1 158 ? -19.642 -5.139  0.807   1.00  16.20  ? 158 LYS A CA  1 
ATOM   1368 C  C   . LYS A 1 158 ? -18.147 -4.836  0.953   1.00  15.86  ? 158 LYS A C   1 
ATOM   1369 O  O   . LYS A 1 158 ? -17.537 -4.415  -0.021  1.00  16.09  ? 158 LYS A O   1 
ATOM   1370 C  CB  . LYS A 1 158 ? -20.488 -3.871  0.965   1.00  19.52  ? 158 LYS A CB  1 
ATOM   1371 C  CG  . LYS A 1 158 ? -21.814 -4.130  0.259   1.00  28.69  ? 158 LYS A CG  1 
ATOM   1372 C  CD  . LYS A 1 158 ? -22.904 -3.072  0.473   1.00  39.57  ? 158 LYS A CD  1 
ATOM   1373 C  CE  . LYS A 1 158 ? -24.218 -3.528  -0.164  1.00  43.07  ? 158 LYS A CE  1 
ATOM   1374 N  NZ  . LYS A 1 158 ? -24.006 -4.128  -1.521  1.00  53.03  ? 158 LYS A NZ  1 
ATOM   1375 N  N   . VAL A 1 159 ? -17.612 -4.944  2.179   1.00  14.11  ? 159 VAL A N   1 
ATOM   1376 C  CA  . VAL A 1 159 ? -16.161 -4.712  2.415   1.00  13.51  ? 159 VAL A CA  1 
ATOM   1377 C  C   . VAL A 1 159 ? -15.423 -5.841  1.725   1.00  13.52  ? 159 VAL A C   1 
ATOM   1378 O  O   . VAL A 1 159 ? -14.510 -5.592  0.955   1.00  14.77  ? 159 VAL A O   1 
ATOM   1379 C  CB  . VAL A 1 159 ? -15.900 -4.728  3.931   1.00  14.31  ? 159 VAL A CB  1 
ATOM   1380 C  CG1 . VAL A 1 159 ? -14.381 -4.785  4.158   1.00  15.89  ? 159 VAL A CG1 1 
ATOM   1381 C  CG2 . VAL A 1 159 ? -16.597 -3.518  4.545   1.00  16.12  ? 159 VAL A CG2 1 
ATOM   1382 N  N   . VAL A 1 160 ? -15.767 -7.090  2.007   1.00  12.81  ? 160 VAL A N   1 
ATOM   1383 C  CA  . VAL A 1 160 ? -15.025 -8.214  1.462   1.00  14.19  ? 160 VAL A CA  1 
ATOM   1384 C  C   . VAL A 1 160 ? -15.000 -8.160  -0.081  1.00  14.88  ? 160 VAL A C   1 
ATOM   1385 O  O   . VAL A 1 160 ? -14.004 -8.442  -0.679  1.00  14.86  ? 160 VAL A O   1 
ATOM   1386 C  CB  . VAL A 1 160 ? -15.660 -9.585  1.973   1.00  22.34  ? 160 VAL A CB  1 
ATOM   1387 C  CG1 . VAL A 1 160 ? -15.388 -10.785 1.082   1.00  22.06  ? 160 VAL A CG1 1 
ATOM   1388 C  CG2 . VAL A 1 160 ? -15.275 -9.735  3.449   1.00  25.38  ? 160 VAL A CG2 1 
ATOM   1389 N  N   . ASP A 1 161 ? -16.088 -7.700  -0.695  1.00  15.51  ? 161 ASP A N   1 
ATOM   1390 C  CA  . ASP A 1 161 ? -16.159 -7.732  -2.163  1.00  16.73  ? 161 ASP A CA  1 
ATOM   1391 C  C   . ASP A 1 161 ? -15.309 -6.709  -2.855  1.00  17.60  ? 161 ASP A C   1 
ATOM   1392 O  O   . ASP A 1 161 ? -15.005 -6.885  -4.008  1.00  23.46  ? 161 ASP A O   1 
ATOM   1393 C  CB  . ASP A 1 161 ? -17.571 -7.684  -2.538  1.00  20.09  ? 161 ASP A CB  1 
ATOM   1394 C  CG  . ASP A 1 161 ? -18.193 -9.114  -2.551  1.00  21.96  ? 161 ASP A CG  1 
ATOM   1395 O  OD1 . ASP A 1 161 ? -17.443 -10.166 -2.679  1.00  22.33  ? 161 ASP A OD1 1 
ATOM   1396 O  OD2 . ASP A 1 161 ? -19.386 -9.187  -2.370  1.00  29.34  ? 161 ASP A OD2 1 
ATOM   1397 N  N   . VAL A 1 162 ? -14.812 -5.693  -2.144  1.00  16.24  ? 162 VAL A N   1 
ATOM   1398 C  CA  . VAL A 1 162 ? -13.931 -4.687  -2.733  1.00  16.90  ? 162 VAL A CA  1 
ATOM   1399 C  C   . VAL A 1 162 ? -12.405 -4.986  -2.520  1.00  15.23  ? 162 VAL A C   1 
ATOM   1400 O  O   . VAL A 1 162 ? -11.603 -4.283  -3.027  1.00  16.67  ? 162 VAL A O   1 
ATOM   1401 C  CB  . VAL A 1 162 ? -14.370 -3.270  -2.255  1.00  24.64  ? 162 VAL A CB  1 
ATOM   1402 C  CG1 . VAL A 1 162 ? -13.965 -2.936  -0.824  1.00  20.86  ? 162 VAL A CG1 1 
ATOM   1403 C  CG2 . VAL A 1 162 ? -13.898 -2.131  -3.153  1.00  32.49  ? 162 VAL A CG2 1 
ATOM   1404 N  N   . LEU A 1 163 ? -12.067 -6.011  -1.675  1.00  15.70  ? 163 LEU A N   1 
ATOM   1405 C  CA  . LEU A 1 163 ? -10.712 -6.212  -1.291  1.00  14.02  ? 163 LEU A CA  1 
ATOM   1406 C  C   . LEU A 1 163 ? -9.848  -6.581  -2.482  1.00  13.59  ? 163 LEU A C   1 
ATOM   1407 O  O   . LEU A 1 163 ? -8.655  -6.252  -2.491  1.00  16.17  ? 163 LEU A O   1 
ATOM   1408 C  CB  . LEU A 1 163 ? -10.604 -7.238  -0.219  1.00  13.57  ? 163 LEU A CB  1 
ATOM   1409 C  CG  . LEU A 1 163 ? -11.284 -6.861  1.120   1.00  13.84  ? 163 LEU A CG  1 
ATOM   1410 C  CD1 . LEU A 1 163 ? -11.022 -7.948  2.144   1.00  15.33  ? 163 LEU A CD1 1 
ATOM   1411 C  CD2 . LEU A 1 163 ? -10.709 -5.552  1.682   1.00  15.26  ? 163 LEU A CD2 1 
ATOM   1412 N  N   . ASP A 1 164 ? -10.413 -7.247  -3.481  1.00  16.52  ? 164 ASP A N   1 
ATOM   1413 C  CA  . ASP A 1 164 ? -9.526  -7.567  -4.606  1.00  18.99  ? 164 ASP A CA  1 
ATOM   1414 C  C   . ASP A 1 164 ? -9.112  -6.322  -5.373  1.00  19.22  ? 164 ASP A C   1 
ATOM   1415 O  O   . ASP A 1 164 ? -8.165  -6.409  -6.148  1.00  24.47  ? 164 ASP A O   1 
ATOM   1416 C  CB  . ASP A 1 164 ? -10.194 -8.565  -5.554  1.00  25.23  ? 164 ASP A CB  1 
ATOM   1417 C  CG  . ASP A 1 164 ? -11.392 -7.976  -6.268  1.00  29.16  ? 164 ASP A CG  1 
ATOM   1418 O  OD1 . ASP A 1 164 ? -12.142 -7.206  -5.632  1.00  33.17  ? 164 ASP A OD1 1 
ATOM   1419 O  OD2 . ASP A 1 164 ? -11.587 -8.282  -7.463  1.00  72.69  ? 164 ASP A OD2 1 
ATOM   1420 N  N   . SER A 1 165 ? -9.773  -5.175  -5.182  1.00  16.97  ? 165 SER A N   1 
ATOM   1421 C  CA  . SER A 1 165 ? -9.350  -3.914  -5.835  1.00  17.12  ? 165 SER A CA  1 
ATOM   1422 C  C   . SER A 1 165 ? -8.359  -3.165  -5.028  1.00  17.77  ? 165 SER A C   1 
ATOM   1423 O  O   . SER A 1 165 ? -7.828  -2.144  -5.546  1.00  20.82  ? 165 SER A O   1 
ATOM   1424 C  CB  . SER A 1 165 ? -10.546 -3.017  -6.081  1.00  18.89  ? 165 SER A CB  1 
ATOM   1425 O  OG  . SER A 1 165 ? -11.096 -2.384  -4.913  1.00  21.92  ? 165 SER A OG  1 
ATOM   1426 N  N   . ILE A 1 166 ? -8.036  -3.635  -3.824  1.00  16.83  ? 166 ILE A N   1 
ATOM   1427 C  CA  . ILE A 1 166 ? -7.006  -3.007  -3.003  1.00  17.14  ? 166 ILE A CA  1 
ATOM   1428 C  C   . ILE A 1 166 ? -5.965  -4.017  -2.485  1.00  15.64  ? 166 ILE A C   1 
ATOM   1429 O  O   . ILE A 1 166 ? -5.599  -4.019  -1.308  1.00  15.91  ? 166 ILE A O   1 
ATOM   1430 C  CB  . ILE A 1 166 ? -7.561  -2.112  -1.848  1.00  17.22  ? 166 ILE A CB  1 
ATOM   1431 C  CG1 . ILE A 1 166 ? -8.499  -2.962  -0.961  1.00  16.20  ? 166 ILE A CG1 1 
ATOM   1432 C  CG2 . ILE A 1 166 ? -8.289  -0.905  -2.462  1.00  17.07  ? 166 ILE A CG2 1 
ATOM   1433 C  CD1 . ILE A 1 166 ? -8.650  -2.327  0.434   1.00  16.00  ? 166 ILE A CD1 1 
ATOM   1434 N  N   . LYS A 1 167 ? -5.553  -4.945  -3.360  1.00  16.02  ? 167 LYS A N   1 
ATOM   1435 C  CA  . LYS A 1 167 ? -4.800  -6.154  -2.892  1.00  15.96  ? 167 LYS A CA  1 
ATOM   1436 C  C   . LYS A 1 167 ? -3.488  -5.733  -2.241  1.00  15.14  ? 167 LYS A C   1 
ATOM   1437 O  O   . LYS A 1 167 ? -3.049  -6.399  -1.286  1.00  15.16  ? 167 LYS A O   1 
ATOM   1438 C  CB  . LYS A 1 167 ? -4.511  -7.046  -4.102  1.00  16.13  ? 167 LYS A CB  1 
ATOM   1439 C  CG  . LYS A 1 167 ? -3.822  -8.310  -3.676  1.00  20.45  ? 167 LYS A CG  1 
ATOM   1440 C  CD  . LYS A 1 167 ? -3.710  -9.231  -4.873  1.00  24.71  ? 167 LYS A CD  1 
ATOM   1441 C  CE  . LYS A 1 167 ? -2.684  -10.320 -4.683  1.00  35.63  ? 167 LYS A CE  1 
ATOM   1442 N  NZ  . LYS A 1 167 ? -2.722  -11.212 -5.910  1.00  45.56  ? 167 LYS A NZ  1 
ATOM   1443 N  N   . THR A 1 168 ? -2.886  -4.664  -2.764  1.00  16.33  ? 168 THR A N   1 
ATOM   1444 C  CA  . THR A 1 168 ? -1.531  -4.300  -2.378  1.00  17.41  ? 168 THR A CA  1 
ATOM   1445 C  C   . THR A 1 168 ? -1.508  -2.868  -1.712  1.00  13.54  ? 168 THR A C   1 
ATOM   1446 O  O   . THR A 1 168 ? -2.395  -2.054  -1.860  1.00  19.07  ? 168 THR A O   1 
ATOM   1447 C  CB  . THR A 1 168 ? -0.524  -4.394  -3.607  1.00  19.64  ? 168 THR A CB  1 
ATOM   1448 O  OG1 . THR A 1 168 ? -1.107  -3.675  -4.672  1.00  22.89  ? 168 THR A OG1 1 
ATOM   1449 C  CG2 . THR A 1 168 ? -0.310  -5.850  -4.009  1.00  20.94  ? 168 THR A CG2 1 
ATOM   1450 N  N   . LYS A 1 169 ? -0.417  -2.813  -0.965  1.00  16.88  ? 169 LYS A N   1 
ATOM   1451 C  CA  . LYS A 1 169 ? -0.139  -1.617  -0.201  1.00  17.42  ? 169 LYS A CA  1 
ATOM   1452 C  C   . LYS A 1 169 ? -0.178  -0.359  -1.059  1.00  18.34  ? 169 LYS A C   1 
ATOM   1453 O  O   . LYS A 1 169 ? 0.403   -0.337  -2.146  1.00  22.67  ? 169 LYS A O   1 
ATOM   1454 C  CB  . LYS A 1 169 ? 1.263   -1.737  0.370   1.00  18.52  ? 169 LYS A CB  1 
ATOM   1455 C  CG  . LYS A 1 169 ? 1.724   -0.539  1.195   1.00  20.15  ? 169 LYS A CG  1 
ATOM   1456 C  CD  . LYS A 1 169 ? 3.105   -0.663  1.880   1.00  25.91  ? 169 LYS A CD  1 
ATOM   1457 C  CE  . LYS A 1 169 ? 3.653   0.653   2.461   1.00  37.57  ? 169 LYS A CE  1 
ATOM   1458 N  NZ  . LYS A 1 169 ? 5.131   0.589   2.691   1.00  42.50  ? 169 LYS A NZ  1 
ATOM   1459 N  N   . GLY A 1 170 ? -0.976  0.610   -0.611  1.00  20.47  ? 170 GLY A N   1 
ATOM   1460 C  CA  . GLY A 1 170 ? -1.071  1.914   -1.254  1.00  23.55  ? 170 GLY A CA  1 
ATOM   1461 C  C   . GLY A 1 170 ? -2.275  1.964   -2.158  1.00  23.53  ? 170 GLY A C   1 
ATOM   1462 O  O   . GLY A 1 170 ? -2.468  3.001   -2.767  1.00  27.32  ? 170 GLY A O   1 
ATOM   1463 N  N   . LYS A 1 171 ? -2.920  0.886   -2.469  1.00  20.94  ? 171 LYS A N   1 
ATOM   1464 C  CA  . LYS A 1 171 ? -4.143  0.926   -3.215  1.00  19.35  ? 171 LYS A CA  1 
ATOM   1465 C  C   . LYS A 1 171 ? -5.375  1.431   -2.426  1.00  17.54  ? 171 LYS A C   1 
ATOM   1466 O  O   . LYS A 1 171 ? -5.592  1.000   -1.301  1.00  18.77  ? 171 LYS A O   1 
ATOM   1467 C  CB  . LYS A 1 171 ? -4.459  -0.419  -3.913  1.00  19.87  ? 171 LYS A CB  1 
ATOM   1468 C  CG  . LYS A 1 171 ? -3.365  -0.864  -4.925  1.00  22.18  ? 171 LYS A CG  1 
ATOM   1469 C  CD  . LYS A 1 171 ? -3.751  -2.008  -5.904  1.00  29.93  ? 171 LYS A CD  1 
ATOM   1470 C  CE  . LYS A 1 171 ? -4.438  -1.530  -7.193  1.00  58.66  ? 171 LYS A CE  1 
ATOM   1471 N  NZ  . LYS A 1 171 ? -5.415  -2.512  -7.809  1.00  49.48  ? 171 LYS A NZ  1 
ATOM   1472 N  N   . SER A 1 172 ? -6.193  2.270   -2.986  1.00  20.45  ? 172 SER A N   1 
ATOM   1473 C  CA  . SER A 1 172 ? -7.479  2.655   -2.384  1.00  21.70  ? 172 SER A CA  1 
ATOM   1474 C  C   . SER A 1 172 ? -8.693  2.615   -3.345  1.00  18.12  ? 172 SER A C   1 
ATOM   1475 O  O   . SER A 1 172 ? -8.447  2.569   -4.641  1.00  21.98  ? 172 SER A O   1 
ATOM   1476 C  CB  . SER A 1 172 ? -7.348  4.083   -1.831  1.00  21.01  ? 172 SER A CB  1 
ATOM   1477 O  OG  . SER A 1 172 ? -7.119  4.997   -2.868  1.00  30.50  ? 172 SER A OG  1 
ATOM   1478 N  N   . ALA A 1 173 ? -9.965  2.713   -2.911  1.00  18.91  ? 173 ALA A N   1 
ATOM   1479 C  CA  . ALA A 1 173 ? -11.188 2.704   -3.773  1.00  21.43  ? 173 ALA A CA  1 
ATOM   1480 C  C   . ALA A 1 173 ? -12.279 3.499   -3.074  1.00  19.13  ? 173 ALA A C   1 
ATOM   1481 O  O   . ALA A 1 173 ? -12.353 3.535   -1.883  1.00  17.95  ? 173 ALA A O   1 
ATOM   1482 C  CB  . ALA A 1 173 ? -11.618 1.283   -4.046  1.00  23.71  ? 173 ALA A CB  1 
ATOM   1483 N  N   A ASP A 1 174 ? -12.895 4.418   -3.806  0.50  23.13  ? 174 ASP A N   1 
ATOM   1484 N  N   B ASP A 1 174 ? -13.240 3.975   -3.910  0.50  14.49  ? 174 ASP A N   1 
ATOM   1485 C  CA  A ASP A 1 174 ? -14.112 4.973   -3.203  0.50  23.18  ? 174 ASP A CA  1 
ATOM   1486 C  CA  B ASP A 1 174 ? -14.565 4.509   -3.469  0.50  16.56  ? 174 ASP A CA  1 
ATOM   1487 C  C   A ASP A 1 174 ? -14.884 3.825   -2.560  0.50  26.26  ? 174 ASP A C   1 
ATOM   1488 C  C   B ASP A 1 174 ? -15.323 3.582   -2.590  0.50  16.70  ? 174 ASP A C   1 
ATOM   1489 O  O   A ASP A 1 174 ? -14.750 2.701   -3.080  0.50  22.17  ? 174 ASP A O   1 
ATOM   1490 O  O   B ASP A 1 174 ? -15.543 2.412   -2.883  0.50  21.26  ? 174 ASP A O   1 
ATOM   1491 C  CB  A ASP A 1 174 ? -14.943 5.603   -4.296  0.50  29.47  ? 174 ASP A CB  1 
ATOM   1492 C  CB  B ASP A 1 174 ? -15.537 4.769   -4.624  0.50  22.27  ? 174 ASP A CB  1 
ATOM   1493 C  CG  A ASP A 1 174 ? -14.120 6.461   -5.225  0.50  31.40  ? 174 ASP A CG  1 
ATOM   1494 C  CG  B ASP A 1 174 ? -17.033 4.600   -4.163  0.50  23.84  ? 174 ASP A CG  1 
ATOM   1495 O  OD1 A ASP A 1 174 ? -13.374 7.362   -4.759  0.50  31.92  ? 174 ASP A OD1 1 
ATOM   1496 O  OD1 B ASP A 1 174 ? -17.508 5.428   -3.409  0.50  22.54  ? 174 ASP A OD1 1 
ATOM   1497 O  OD2 A ASP A 1 174 ? -14.218 6.241   -6.453  0.50  38.52  ? 174 ASP A OD2 1 
ATOM   1498 O  OD2 B ASP A 1 174 ? -17.664 3.566   -4.435  0.50  58.15  ? 174 ASP A OD2 1 
ATOM   1499 N  N   . PHE A 1 175 ? -15.644 4.114   -1.463  1.00  23.48  ? 175 PHE A N   1 
ATOM   1500 C  CA  . PHE A 1 175 ? -16.357 3.190   -0.657  1.00  22.76  ? 175 PHE A CA  1 
ATOM   1501 C  C   . PHE A 1 175 ? -17.351 4.029   0.064   1.00  20.94  ? 175 PHE A C   1 
ATOM   1502 O  O   . PHE A 1 175 ? -17.275 4.262   1.214   1.00  24.36  ? 175 PHE A O   1 
ATOM   1503 C  CB  . PHE A 1 175 ? -15.404 2.469   0.304   1.00  23.83  ? 175 PHE A CB  1 
ATOM   1504 C  CG  . PHE A 1 175 ? -15.954 1.193   0.773   1.00  22.67  ? 175 PHE A CG  1 
ATOM   1505 C  CD1 . PHE A 1 175 ? -16.164 0.153   -0.083  1.00  23.39  ? 175 PHE A CD1 1 
ATOM   1506 C  CD2 . PHE A 1 175 ? -16.330 1.035   2.067   1.00  19.20  ? 175 PHE A CD2 1 
ATOM   1507 C  CE1 . PHE A 1 175 ? -16.727 -1.060  0.344   1.00  23.06  ? 175 PHE A CE1 1 
ATOM   1508 C  CE2 . PHE A 1 175 ? -16.908 -0.137  2.531   1.00  21.94  ? 175 PHE A CE2 1 
ATOM   1509 C  CZ  . PHE A 1 175 ? -17.121 -1.169  1.660   1.00  20.44  ? 175 PHE A CZ  1 
ATOM   1510 N  N   . THR A 1 176 ? -18.280 4.508   -0.721  1.00  20.68  ? 176 THR A N   1 
ATOM   1511 C  CA  . THR A 1 176 ? -19.253 5.386   -0.180  1.00  19.37  ? 176 THR A CA  1 
ATOM   1512 C  C   . THR A 1 176 ? -20.437 4.586   0.204   1.00  18.54  ? 176 THR A C   1 
ATOM   1513 O  O   . THR A 1 176 ? -20.664 3.413   -0.227  1.00  19.22  ? 176 THR A O   1 
ATOM   1514 C  CB  . THR A 1 176 ? -19.706 6.436   -1.289  1.00  22.03  ? 176 THR A CB  1 
ATOM   1515 O  OG1 . THR A 1 176 ? -20.023 5.760   -2.506  1.00  25.29  ? 176 THR A OG1 1 
ATOM   1516 C  CG2 . THR A 1 176 ? -18.606 7.378   -1.482  1.00  30.20  ? 176 THR A CG2 1 
ATOM   1517 N  N   . ASN A 1 177 ? -21.211 5.186   1.059   1.00  18.66  ? 177 ASN A N   1 
ATOM   1518 C  CA  . ASN A 1 177 ? -22.493 4.633   1.440   1.00  17.52  ? 177 ASN A CA  1 
ATOM   1519 C  C   . ASN A 1 177 ? -22.359 3.350   2.251   1.00  20.17  ? 177 ASN A C   1 
ATOM   1520 O  O   . ASN A 1 177 ? -23.334 2.577   2.223   1.00  23.30  ? 177 ASN A O   1 
ATOM   1521 C  CB  . ASN A 1 177 ? -23.503 4.538   0.278   1.00  18.25  ? 177 ASN A CB  1 
ATOM   1522 C  CG  . ASN A 1 177 ? -23.752 5.915   -0.275  1.00  19.94  ? 177 ASN A CG  1 
ATOM   1523 O  OD1 . ASN A 1 177 ? -24.380 6.769   0.333   1.00  22.85  ? 177 ASN A OD1 1 
ATOM   1524 N  ND2 . ASN A 1 177 ? -23.189 6.123   -1.467  1.00  18.54  ? 177 ASN A ND2 1 
ATOM   1525 N  N   . PHE A 1 178 ? -21.220 3.110   2.921   1.00  17.28  ? 178 PHE A N   1 
ATOM   1526 C  CA  . PHE A 1 178 ? -21.146 1.889   3.736   1.00  18.19  ? 178 PHE A CA  1 
ATOM   1527 C  C   . PHE A 1 178 ? -21.717 2.221   5.136   1.00  18.06  ? 178 PHE A C   1 
ATOM   1528 O  O   . PHE A 1 178 ? -21.329 3.182   5.778   1.00  18.29  ? 178 PHE A O   1 
ATOM   1529 C  CB  . PHE A 1 178 ? -19.746 1.372   3.821   1.00  18.94  ? 178 PHE A CB  1 
ATOM   1530 C  CG  . PHE A 1 178 ? -19.679 0.152   4.671   1.00  17.44  ? 178 PHE A CG  1 
ATOM   1531 C  CD1 . PHE A 1 178 ? -20.020 -1.135  4.178   1.00  19.67  ? 178 PHE A CD1 1 
ATOM   1532 C  CD2 . PHE A 1 178 ? -19.344 0.253   6.062   1.00  15.55  ? 178 PHE A CD2 1 
ATOM   1533 C  CE1 . PHE A 1 178 ? -20.011 -2.215  4.948   1.00  16.98  ? 178 PHE A CE1 1 
ATOM   1534 C  CE2 . PHE A 1 178 ? -19.315 -0.904  6.842   1.00  16.58  ? 178 PHE A CE2 1 
ATOM   1535 C  CZ  . PHE A 1 178 ? -19.656 -2.093  6.301   1.00  16.49  ? 178 PHE A CZ  1 
ATOM   1536 N  N   . ASP A 1 179 ? -22.571 1.348   5.647   1.00  15.21  ? 179 ASP A N   1 
ATOM   1537 C  CA  . ASP A 1 179 ? -23.188 1.565   6.990   1.00  16.38  ? 179 ASP A CA  1 
ATOM   1538 C  C   . ASP A 1 179 ? -22.560 0.684   8.055   1.00  15.54  ? 179 ASP A C   1 
ATOM   1539 O  O   . ASP A 1 179 ? -22.736 -0.557  8.071   1.00  14.64  ? 179 ASP A O   1 
ATOM   1540 C  CB  . ASP A 1 179 ? -24.649 1.188   6.874   1.00  18.78  ? 179 ASP A CB  1 
ATOM   1541 C  CG  . ASP A 1 179 ? -25.436 1.494   8.146   1.00  21.56  ? 179 ASP A CG  1 
ATOM   1542 O  OD1 . ASP A 1 179 ? -24.861 1.812   9.190   1.00  17.63  ? 179 ASP A OD1 1 
ATOM   1543 O  OD2 . ASP A 1 179 ? -26.659 1.375   8.150   1.00  29.93  ? 179 ASP A OD2 1 
ATOM   1544 N  N   . PRO A 1 180 ? -21.747 1.268   8.928   1.00  13.93  ? 180 PRO A N   1 
ATOM   1545 C  CA  . PRO A 1 180 ? -21.023 0.437   9.914   1.00  14.32  ? 180 PRO A CA  1 
ATOM   1546 C  C   . PRO A 1 180 ? -21.912 -0.213  10.956  1.00  13.54  ? 180 PRO A C   1 
ATOM   1547 O  O   . PRO A 1 180 ? -21.492 -1.089  11.708  1.00  13.15  ? 180 PRO A O   1 
ATOM   1548 C  CB  . PRO A 1 180 ? -20.034 1.425   10.487  1.00  15.01  ? 180 PRO A CB  1 
ATOM   1549 C  CG  . PRO A 1 180 ? -20.692 2.767   10.392  1.00  15.24  ? 180 PRO A CG  1 
ATOM   1550 C  CD  . PRO A 1 180 ? -21.373 2.689   9.014   1.00  15.22  ? 180 PRO A CD  1 
ATOM   1551 N  N   . ARG A 1 181 ? -23.190 0.224   11.025  1.00  13.62  ? 181 ARG A N   1 
ATOM   1552 C  CA  . ARG A 1 181 ? -24.143 -0.416  11.933  1.00  14.68  ? 181 ARG A CA  1 
ATOM   1553 C  C   . ARG A 1 181 ? -24.239 -1.883  11.628  1.00  14.02  ? 181 ARG A C   1 
ATOM   1554 O  O   . ARG A 1 181 ? -24.537 -2.692  12.551  1.00  16.78  ? 181 ARG A O   1 
ATOM   1555 C  CB  . ARG A 1 181 ? -25.516 0.226   11.902  1.00  16.34  ? 181 ARG A CB  1 
ATOM   1556 C  CG  . ARG A 1 181 ? -25.524 1.624   12.506  1.00  17.28  ? 181 ARG A CG  1 
ATOM   1557 C  CD  . ARG A 1 181 ? -26.884 2.240   12.438  1.00  19.50  ? 181 ARG A CD  1 
ATOM   1558 N  NE  . ARG A 1 181 ? -27.242 2.456   11.046  1.00  19.29  ? 181 ARG A NE  1 
ATOM   1559 C  CZ  . ARG A 1 181 ? -28.282 3.195   10.742  1.00  25.49  ? 181 ARG A CZ  1 
ATOM   1560 N  NH1 . ARG A 1 181 ? -29.036 3.751   11.720  1.00  29.48  ? 181 ARG A NH1 1 
ATOM   1561 N  NH2 . ARG A 1 181 ? -28.539 3.385   9.483   1.00  24.71  ? 181 ARG A NH2 1 
ATOM   1562 N  N   . GLY A 1 182 ? -24.016 -2.317  10.391  1.00  14.42  ? 182 GLY A N   1 
ATOM   1563 C  CA  . GLY A 1 182 ? -24.173 -3.717  10.081  1.00  15.87  ? 182 GLY A CA  1 
ATOM   1564 C  C   . GLY A 1 182 ? -22.985 -4.566  10.543  1.00  15.39  ? 182 GLY A C   1 
ATOM   1565 O  O   . GLY A 1 182 ? -23.007 -5.752  10.285  1.00  18.10  ? 182 GLY A O   1 
ATOM   1566 N  N   . LEU A 1 183 ? -21.985 -3.980  11.220  1.00  14.09  ? 183 LEU A N   1 
ATOM   1567 C  CA  . LEU A 1 183 ? -20.842 -4.742  11.779  1.00  13.31  ? 183 LEU A CA  1 
ATOM   1568 C  C   . LEU A 1 183 ? -20.997 -4.994  13.270  1.00  13.26  ? 183 LEU A C   1 
ATOM   1569 O  O   . LEU A 1 183 ? -20.130 -5.599  13.893  1.00  14.09  ? 183 LEU A O   1 
ATOM   1570 C  CB  . LEU A 1 183 ? -19.580 -3.970  11.517  1.00  13.60  ? 183 LEU A CB  1 
ATOM   1571 C  CG  . LEU A 1 183 ? -19.301 -3.906  10.011  1.00  15.20  ? 183 LEU A CG  1 
ATOM   1572 C  CD1 . LEU A 1 183 ? -18.044 -3.033  9.871   1.00  19.36  ? 183 LEU A CD1 1 
ATOM   1573 C  CD2 . LEU A 1 183 ? -19.157 -5.204  9.273   1.00  17.99  ? 183 LEU A CD2 1 
ATOM   1574 N  N   . LEU A 1 184 ? -22.062 -4.481  13.909  1.00  13.01  ? 184 LEU A N   1 
ATOM   1575 C  CA  . LEU A 1 184 ? -22.224 -4.548  15.350  1.00  13.28  ? 184 LEU A CA  1 
ATOM   1576 C  C   . LEU A 1 184 ? -22.898 -5.845  15.741  1.00  14.80  ? 184 LEU A C   1 
ATOM   1577 O  O   . LEU A 1 184 ? -23.686 -6.381  15.005  1.00  21.32  ? 184 LEU A O   1 
ATOM   1578 C  CB  . LEU A 1 184 ? -23.030 -3.285  15.873  1.00  13.27  ? 184 LEU A CB  1 
ATOM   1579 C  CG  . LEU A 1 184 ? -22.429 -1.922  15.455  1.00  13.15  ? 184 LEU A CG  1 
ATOM   1580 C  CD1 . LEU A 1 184 ? -23.398 -0.819  15.949  1.00  14.56  ? 184 LEU A CD1 1 
ATOM   1581 C  CD2 . LEU A 1 184 ? -21.034 -1.825  16.004  1.00  15.58  ? 184 LEU A CD2 1 
ATOM   1582 N  N   . PRO A 1 185 ? -22.633 -6.360  16.917  1.00  13.06  ? 185 PRO A N   1 
ATOM   1583 C  CA  . PRO A 1 185 ? -23.396 -7.490  17.473  1.00  13.33  ? 185 PRO A CA  1 
ATOM   1584 C  C   . PRO A 1 185 ? -24.648 -6.922  18.125  1.00  13.16  ? 185 PRO A C   1 
ATOM   1585 O  O   . PRO A 1 185 ? -24.899 -5.731  18.197  1.00  15.45  ? 185 PRO A O   1 
ATOM   1586 C  CB  . PRO A 1 185 ? -22.447 -8.071  18.539  1.00  12.26  ? 185 PRO A CB  1 
ATOM   1587 C  CG  . PRO A 1 185 ? -21.705 -6.824  19.043  1.00  11.29  ? 185 PRO A CG  1 
ATOM   1588 C  CD  . PRO A 1 185 ? -21.488 -5.969  17.749  1.00  10.85  ? 185 PRO A CD  1 
ATOM   1589 N  N   A GLU A 1 186 ? -25.534 -7.792  18.675  0.50  12.46  ? 186 GLU A N   1 
ATOM   1590 N  N   B GLU A 1 186 ? -25.439 -7.921  18.503  0.50  14.69  ? 186 GLU A N   1 
ATOM   1591 C  CA  A GLU A 1 186 ? -26.815 -7.299  19.306  0.50  12.78  ? 186 GLU A CA  1 
ATOM   1592 C  CA  B GLU A 1 186 ? -26.667 -7.608  19.116  0.50  14.63  ? 186 GLU A CA  1 
ATOM   1593 C  C   A GLU A 1 186 ? -26.554 -6.576  20.593  0.50  12.39  ? 186 GLU A C   1 
ATOM   1594 C  C   B GLU A 1 186 ? -26.515 -6.738  20.384  0.50  13.64  ? 186 GLU A C   1 
ATOM   1595 O  O   A GLU A 1 186 ? -27.185 -5.570  20.980  0.50  13.51  ? 186 GLU A O   1 
ATOM   1596 O  O   B GLU A 1 186 ? -27.114 -5.648  20.420  0.50  15.83  ? 186 GLU A O   1 
ATOM   1597 C  CB  A GLU A 1 186 ? -27.664 -8.479  19.713  0.50  14.24  ? 186 GLU A CB  1 
ATOM   1598 C  CB  B GLU A 1 186 ? -27.416 -8.893  19.319  0.50  14.59  ? 186 GLU A CB  1 
ATOM   1599 C  CG  A GLU A 1 186 ? -28.400 -9.206  18.620  0.50  16.20  ? 186 GLU A CG  1 
ATOM   1600 C  CG  B GLU A 1 186 ? -28.659 -8.683  20.136  0.50  20.24  ? 186 GLU A CG  1 
ATOM   1601 C  CD  A GLU A 1 186 ? -29.139 -10.478 19.113  0.50  15.23  ? 186 GLU A CD  1 
ATOM   1602 C  CD  B GLU A 1 186 ? -29.310 -9.979  20.516  0.50  20.48  ? 186 GLU A CD  1 
ATOM   1603 O  OE1 A GLU A 1 186 ? -29.677 -11.240 18.279  0.50  18.02  ? 186 GLU A OE1 1 
ATOM   1604 O  OE1 B GLU A 1 186 ? -29.215 -10.967 19.703  0.50  22.02  ? 186 GLU A OE1 1 
ATOM   1605 O  OE2 A GLU A 1 186 ? -29.170 -10.756 20.372  0.50  17.05  ? 186 GLU A OE2 1 
ATOM   1606 O  OE2 B GLU A 1 186 ? -29.951 -9.975  21.586  0.50  25.47  ? 186 GLU A OE2 1 
ATOM   1607 N  N   . SER A 1 187 ? -25.705 -7.198  21.362  1.00  12.91  ? 187 SER A N   1 
ATOM   1608 C  CA  . SER A 1 187 ? -25.474 -6.589  22.647  1.00  12.75  ? 187 SER A CA  1 
ATOM   1609 C  C   . SER A 1 187 ? -24.315 -5.599  22.636  1.00  12.17  ? 187 SER A C   1 
ATOM   1610 O  O   . SER A 1 187 ? -23.294 -5.868  22.022  1.00  13.42  ? 187 SER A O   1 
ATOM   1611 C  CB  . SER A 1 187 ? -25.101 -7.661  23.662  1.00  13.95  ? 187 SER A CB  1 
ATOM   1612 O  OG  . SER A 1 187 ? -24.830 -7.096  24.922  1.00  14.76  ? 187 SER A OG  1 
ATOM   1613 N  N   . LEU A 1 188 ? -24.495 -4.508  23.360  1.00  12.30  ? 188 LEU A N   1 
ATOM   1614 C  CA  . LEU A 1 188 ? -23.400 -3.526  23.615  1.00  13.24  ? 188 LEU A CA  1 
ATOM   1615 C  C   . LEU A 1 188 ? -22.791 -3.729  24.988  1.00  12.00  ? 188 LEU A C   1 
ATOM   1616 O  O   . LEU A 1 188 ? -22.090 -2.786  25.440  1.00  14.87  ? 188 LEU A O   1 
ATOM   1617 C  CB  . LEU A 1 188 ? -23.890 -2.101  23.416  1.00  16.28  ? 188 LEU A CB  1 
ATOM   1618 C  CG  . LEU A 1 188 ? -24.333 -1.701  22.010  1.00  17.73  ? 188 LEU A CG  1 
ATOM   1619 C  CD1 . LEU A 1 188 ? -24.902 -0.271  21.965  1.00  21.28  ? 188 LEU A CD1 1 
ATOM   1620 C  CD2 . LEU A 1 188 ? -23.241 -1.983  20.990  1.00  17.77  ? 188 LEU A CD2 1 
ATOM   1621 N  N   . ASP A 1 189 ? -22.917 -4.876  25.647  1.00  11.63  ? 189 ASP A N   1 
ATOM   1622 C  CA  . ASP A 1 189 ? -22.162 -5.118  26.877  1.00  12.80  ? 189 ASP A CA  1 
ATOM   1623 C  C   . ASP A 1 189 ? -20.652 -5.080  26.547  1.00  10.12  ? 189 ASP A C   1 
ATOM   1624 O  O   . ASP A 1 189 ? -20.247 -5.559  25.484  1.00  10.03  ? 189 ASP A O   1 
ATOM   1625 C  CB  . ASP A 1 189 ? -22.434 -6.486  27.444  1.00  16.25  ? 189 ASP A CB  1 
ATOM   1626 C  CG  . ASP A 1 189 ? -23.864 -6.666  28.102  1.00  18.39  ? 189 ASP A CG  1 
ATOM   1627 O  OD1 . ASP A 1 189 ? -24.472 -5.642  28.271  1.00  23.88  ? 189 ASP A OD1 1 
ATOM   1628 O  OD2 . ASP A 1 189 ? -24.250 -7.815  28.315  1.00  28.04  ? 189 ASP A OD2 1 
ATOM   1629 N  N   . TYR A 1 190 ? -19.892 -4.452  27.420  1.00  10.03  ? 190 TYR A N   1 
ATOM   1630 C  CA  . TYR A 1 190 ? -18.450 -4.215  27.111  1.00  9.56   ? 190 TYR A CA  1 
ATOM   1631 C  C   . TYR A 1 190 ? -17.595 -4.287  28.345  1.00  8.60   ? 190 TYR A C   1 
ATOM   1632 O  O   . TYR A 1 190 ? -18.050 -4.144  29.483  1.00  9.69   ? 190 TYR A O   1 
ATOM   1633 C  CB  . TYR A 1 190 ? -18.327 -2.823  26.423  1.00  10.03  ? 190 TYR A CB  1 
ATOM   1634 C  CG  . TYR A 1 190 ? -18.710 -1.646  27.276  1.00  9.82   ? 190 TYR A CG  1 
ATOM   1635 C  CD1 . TYR A 1 190 ? -17.751 -1.040  28.139  1.00  10.55  ? 190 TYR A CD1 1 
ATOM   1636 C  CD2 . TYR A 1 190 ? -19.994 -1.116  27.215  1.00  10.05  ? 190 TYR A CD2 1 
ATOM   1637 C  CE1 . TYR A 1 190 ? -18.147 0.032   28.948  1.00  10.61  ? 190 TYR A CE1 1 
ATOM   1638 C  CE2 . TYR A 1 190 ? -20.367 -0.032  28.036  1.00  11.15  ? 190 TYR A CE2 1 
ATOM   1639 C  CZ  . TYR A 1 190 ? -19.442 0.514   28.886  1.00  10.48  ? 190 TYR A CZ  1 
ATOM   1640 O  OH  . TYR A 1 190 ? -19.765 1.552   29.719  1.00  12.76  ? 190 TYR A OH  1 
ATOM   1641 N  N   . TRP A 1 191 ? -16.311 -4.373  28.043  1.00  7.75   ? 191 TRP A N   1 
ATOM   1642 C  CA  . TRP A 1 191 ? -15.235 -4.097  29.015  1.00  8.30   ? 191 TRP A CA  1 
ATOM   1643 C  C   . TRP A 1 191 ? -14.553 -2.843  28.606  1.00  7.66   ? 191 TRP A C   1 
ATOM   1644 O  O   . TRP A 1 191 ? -14.439 -2.523  27.399  1.00  8.73   ? 191 TRP A O   1 
ATOM   1645 C  CB  . TRP A 1 191 ? -14.211 -5.251  29.028  1.00  9.90   ? 191 TRP A CB  1 
ATOM   1646 C  CG  . TRP A 1 191 ? -14.764 -6.575  29.455  1.00  8.51   ? 191 TRP A CG  1 
ATOM   1647 C  CD1 . TRP A 1 191 ? -14.990 -6.987  30.731  1.00  10.17  ? 191 TRP A CD1 1 
ATOM   1648 C  CD2 . TRP A 1 191 ? -15.014 -7.697  28.625  1.00  8.85   ? 191 TRP A CD2 1 
ATOM   1649 N  NE1 . TRP A 1 191 ? -15.417 -8.298  30.713  1.00  10.81  ? 191 TRP A NE1 1 
ATOM   1650 C  CE2 . TRP A 1 191 ? -15.412 -8.779  29.465  1.00  10.04  ? 191 TRP A CE2 1 
ATOM   1651 C  CE3 . TRP A 1 191 ? -14.939 -7.920  27.221  1.00  10.00  ? 191 TRP A CE3 1 
ATOM   1652 C  CZ2 . TRP A 1 191 ? -15.749 -10.037 28.931  1.00  11.87  ? 191 TRP A CZ2 1 
ATOM   1653 C  CZ3 . TRP A 1 191 ? -15.204 -9.212  26.743  1.00  11.33  ? 191 TRP A CZ3 1 
ATOM   1654 C  CH2 . TRP A 1 191 ? -15.596 -10.191 27.575  1.00  11.33  ? 191 TRP A CH2 1 
ATOM   1655 N  N   . THR A 1 192 ? -13.999 -2.111  29.558  1.00  7.82   ? 192 THR A N   1 
ATOM   1656 C  CA  . THR A 1 192 ? -13.260 -0.934  29.235  1.00  7.68   ? 192 THR A CA  1 
ATOM   1657 C  C   . THR A 1 192 ? -12.059 -0.747  30.100  1.00  7.55   ? 192 THR A C   1 
ATOM   1658 O  O   . THR A 1 192 ? -12.024 -1.126  31.286  1.00  8.72   ? 192 THR A O   1 
ATOM   1659 C  CB  . THR A 1 192 ? -14.192 0.318   29.340  1.00  8.48   ? 192 THR A CB  1 
ATOM   1660 O  OG1 . THR A 1 192 ? -13.508 1.511   28.972  1.00  8.52   ? 192 THR A OG1 1 
ATOM   1661 C  CG2 . THR A 1 192 ? -14.730 0.520   30.754  1.00  9.37   ? 192 THR A CG2 1 
ATOM   1662 N  N   . TYR A 1 193 ? -10.987 -0.156  29.535  1.00  7.64   ? 193 TYR A N   1 
ATOM   1663 C  CA  . TYR A 1 193 ? -9.783  0.125   30.258  1.00  7.84   ? 193 TYR A CA  1 
ATOM   1664 C  C   . TYR A 1 193 ? -9.002  1.190   29.483  1.00  7.31   ? 193 TYR A C   1 
ATOM   1665 O  O   . TYR A 1 193 ? -9.225  1.375   28.275  1.00  7.57   ? 193 TYR A O   1 
ATOM   1666 C  CB  . TYR A 1 193 ? -8.940  -1.189  30.446  1.00  8.21   ? 193 TYR A CB  1 
ATOM   1667 C  CG  . TYR A 1 193 ? -8.249  -1.627  29.191  1.00  7.51   ? 193 TYR A CG  1 
ATOM   1668 C  CD1 . TYR A 1 193 ? -8.929  -2.355  28.192  1.00  7.55   ? 193 TYR A CD1 1 
ATOM   1669 C  CD2 . TYR A 1 193 ? -6.931  -1.278  28.950  1.00  7.74   ? 193 TYR A CD2 1 
ATOM   1670 C  CE1 . TYR A 1 193 ? -8.274  -2.685  26.991  1.00  7.18   ? 193 TYR A CE1 1 
ATOM   1671 C  CE2 . TYR A 1 193 ? -6.257  -1.629  27.757  1.00  8.11   ? 193 TYR A CE2 1 
ATOM   1672 C  CZ  . TYR A 1 193 ? -6.981  -2.306  26.759  1.00  7.34   ? 193 TYR A CZ  1 
ATOM   1673 O  OH  . TYR A 1 193 ? -6.308  -2.609  25.630  1.00  7.15   ? 193 TYR A OH  1 
ATOM   1674 N  N   . PRO A 1 194 ? -8.063  1.875   30.136  1.00  7.83   ? 194 PRO A N   1 
ATOM   1675 C  CA  . PRO A 1 194 ? -7.231  2.888   29.483  1.00  7.83   ? 194 PRO A CA  1 
ATOM   1676 C  C   . PRO A 1 194 ? -6.045  2.226   28.799  1.00  7.18   ? 194 PRO A C   1 
ATOM   1677 O  O   . PRO A 1 194 ? -5.315  1.456   29.436  1.00  8.27   ? 194 PRO A O   1 
ATOM   1678 C  CB  . PRO A 1 194 ? -6.756  3.794   30.615  1.00  9.38   ? 194 PRO A CB  1 
ATOM   1679 C  CG  . PRO A 1 194 ? -6.718  2.860   31.831  1.00  10.35  ? 194 PRO A CG  1 
ATOM   1680 C  CD  . PRO A 1 194 ? -7.892  1.919   31.620  1.00  9.36   ? 194 PRO A CD  1 
ATOM   1681 N  N   . GLY A 1 195 ? -5.805  2.530   27.534  1.00  7.19   ? 195 GLY A N   1 
ATOM   1682 C  CA  . GLY A 1 195 ? -4.665  1.918   26.821  1.00  7.53   ? 195 GLY A CA  1 
ATOM   1683 C  C   . GLY A 1 195 ? -4.143  2.779   25.720  1.00  7.23   ? 195 GLY A C   1 
ATOM   1684 O  O   . GLY A 1 195 ? -4.013  4.015   25.875  1.00  7.95   ? 195 GLY A O   1 
ATOM   1685 N  N   . SER A 1 196 ? -3.758  2.102   24.654  1.00  6.95   ? 196 SER A N   1 
ATOM   1686 C  CA  . SER A 1 196 ? -2.924  2.711   23.621  1.00  7.11   ? 196 SER A CA  1 
ATOM   1687 C  C   . SER A 1 196 ? -3.404  2.316   22.259  1.00  6.59   ? 196 SER A C   1 
ATOM   1688 O  O   . SER A 1 196 ? -4.157  1.365   22.079  1.00  7.48   ? 196 SER A O   1 
ATOM   1689 C  CB  . SER A 1 196 ? -1.441  2.351   23.809  1.00  7.93   ? 196 SER A CB  1 
ATOM   1690 O  OG  . SER A 1 196 ? -1.220  1.006   23.400  1.00  7.66   ? 196 SER A OG  1 
ATOM   1691 N  N   . LEU A 1 197 ? -2.856  2.974   21.225  1.00  7.47   ? 197 LEU A N   1 
ATOM   1692 C  CA  . LEU A 1 197 ? -2.870  2.396   19.899  1.00  7.94   ? 197 LEU A CA  1 
ATOM   1693 C  C   . LEU A 1 197 ? -2.128  1.083   19.918  1.00  7.84   ? 197 LEU A C   1 
ATOM   1694 O  O   . LEU A 1 197 ? -1.127  0.932   20.677  1.00  8.06   ? 197 LEU A O   1 
ATOM   1695 C  CB  . LEU A 1 197 ? -2.151  3.307   18.938  1.00  9.75   ? 197 LEU A CB  1 
ATOM   1696 C  CG  . LEU A 1 197 ? -2.637  4.757   18.777  1.00  11.91  ? 197 LEU A CG  1 
ATOM   1697 C  CD1 . LEU A 1 197 ? -1.733  5.503   17.807  1.00  13.67  ? 197 LEU A CD1 1 
ATOM   1698 C  CD2 . LEU A 1 197 ? -4.078  4.757   18.409  1.00  15.72  ? 197 LEU A CD2 1 
ATOM   1699 N  N   . THR A 1 198 ? -2.547  0.156   19.050  1.00  7.80   ? 198 THR A N   1 
ATOM   1700 C  CA  . THR A 1 198 ? -1.831  -1.136  18.984  1.00  8.47   ? 198 THR A CA  1 
ATOM   1701 C  C   . THR A 1 198 ? -0.870  -1.200  17.857  1.00  7.86   ? 198 THR A C   1 
ATOM   1702 O  O   . THR A 1 198 ? -0.263  -2.251  17.623  1.00  9.11   ? 198 THR A O   1 
ATOM   1703 C  CB  . THR A 1 198 ? -2.807  -2.289  18.937  1.00  7.70   ? 198 THR A CB  1 
ATOM   1704 O  OG1 . THR A 1 198 ? -3.454  -2.253  17.685  1.00  7.60   ? 198 THR A OG1 1 
ATOM   1705 C  CG2 . THR A 1 198 ? -3.788  -2.325  20.109  1.00  8.18   ? 198 THR A CG2 1 
ATOM   1706 N  N   . THR A 1 199 ? -0.708  -0.131  17.104  1.00  9.42   ? 199 THR A N   1 
ATOM   1707 C  CA  . THR A 1 199 ? 0.320   -0.001  16.100  1.00  10.42  ? 199 THR A CA  1 
ATOM   1708 C  C   . THR A 1 199 ? 1.126   1.254   16.410  1.00  9.80   ? 199 THR A C   1 
ATOM   1709 O  O   . THR A 1 199 ? 0.647   2.181   17.037  1.00  9.90   ? 199 THR A O   1 
ATOM   1710 C  CB  . THR A 1 199 ? -0.291  0.172   14.716  1.00  11.87  ? 199 THR A CB  1 
ATOM   1711 O  OG1 . THR A 1 199 ? -1.238  1.269   14.681  1.00  14.37  ? 199 THR A OG1 1 
ATOM   1712 C  CG2 . THR A 1 199 ? -0.917  -1.122  14.218  1.00  15.06  ? 199 THR A CG2 1 
ATOM   1713 N  N   . PRO A 1 200 ? 2.399   1.298   15.961  1.00  10.85  ? 200 PRO A N   1 
ATOM   1714 C  CA  . PRO A 1 200 ? 3.200   2.564   16.063  1.00  11.65  ? 200 PRO A CA  1 
ATOM   1715 C  C   . PRO A 1 200 ? 2.365   3.732   15.562  1.00  11.61  ? 200 PRO A C   1 
ATOM   1716 O  O   . PRO A 1 200 ? 1.668   3.619   14.532  1.00  13.90  ? 200 PRO A O   1 
ATOM   1717 C  CB  . PRO A 1 200 ? 4.373   2.257   15.103  1.00  13.85  ? 200 PRO A CB  1 
ATOM   1718 C  CG  . PRO A 1 200 ? 4.593   0.766   15.321  1.00  13.55  ? 200 PRO A CG  1 
ATOM   1719 C  CD  . PRO A 1 200 ? 3.162   0.218   15.309  1.00  12.43  ? 200 PRO A CD  1 
ATOM   1720 N  N   . PRO A 1 201 ? 2.357   4.849   16.282  1.00  11.73  ? 201 PRO A N   1 
ATOM   1721 C  CA  . PRO A 1 201 ? 3.318   5.215   17.347  1.00  11.75  ? 201 PRO A CA  1 
ATOM   1722 C  C   . PRO A 1 201 ? 2.956   4.676   18.734  1.00  10.25  ? 201 PRO A C   1 
ATOM   1723 O  O   . PRO A 1 201 ? 3.635   5.045   19.713  1.00  11.45  ? 201 PRO A O   1 
ATOM   1724 C  CB  . PRO A 1 201 ? 3.316   6.743   17.350  1.00  14.89  ? 201 PRO A CB  1 
ATOM   1725 C  CG  . PRO A 1 201 ? 1.895   7.052   16.967  1.00  14.56  ? 201 PRO A CG  1 
ATOM   1726 C  CD  . PRO A 1 201 ? 1.550   6.021   15.880  1.00  14.15  ? 201 PRO A CD  1 
ATOM   1727 N  N   . LEU A 1 202 ? 1.920   3.841   18.897  1.00  9.41   ? 202 LEU A N   1 
ATOM   1728 C  CA  . LEU A 1 202 ? 1.612   3.204   20.157  1.00  8.60   ? 202 LEU A CA  1 
ATOM   1729 C  C   . LEU A 1 202 ? 1.233   4.239   21.249  1.00  8.61   ? 202 LEU A C   1 
ATOM   1730 O  O   . LEU A 1 202 ? 1.414   4.000   22.425  1.00  9.03   ? 202 LEU A O   1 
ATOM   1731 C  CB  . LEU A 1 202 ? 2.767   2.314   20.696  1.00  9.22   ? 202 LEU A CB  1 
ATOM   1732 C  CG  . LEU A 1 202 ? 3.153   1.187   19.666  1.00  9.51   ? 202 LEU A CG  1 
ATOM   1733 C  CD1 . LEU A 1 202 ? 4.473   0.527   20.150  1.00  11.44  ? 202 LEU A CD1 1 
ATOM   1734 C  CD2 . LEU A 1 202 ? 2.062   0.170   19.520  1.00  10.30  ? 202 LEU A CD2 1 
ATOM   1735 N  N   . ALA A 1 203 ? 0.695   5.355   20.790  1.00  9.13   ? 203 ALA A N   1 
ATOM   1736 C  CA  . ALA A 1 203 ? 0.384   6.449   21.685  1.00  9.50   ? 203 ALA A CA  1 
ATOM   1737 C  C   . ALA A 1 203 ? -0.614  6.044   22.728  1.00  9.22   ? 203 ALA A C   1 
ATOM   1738 O  O   . ALA A 1 203 ? -1.577  5.309   22.456  1.00  8.59   ? 203 ALA A O   1 
ATOM   1739 C  CB  . ALA A 1 203 ? -0.160  7.613   20.819  1.00  11.13  ? 203 ALA A CB  1 
ATOM   1740 N  N   . GLU A 1 204 ? -0.401  6.525   23.929  1.00  8.67   ? 204 GLU A N   1 
ATOM   1741 C  CA  . GLU A 1 204 ? -1.191  6.182   25.074  1.00  8.97   ? 204 GLU A CA  1 
ATOM   1742 C  C   . GLU A 1 204 ? -2.393  7.114   25.242  1.00  8.63   ? 204 GLU A C   1 
ATOM   1743 O  O   . GLU A 1 204 ? -2.482  7.845   26.224  1.00  10.86  ? 204 GLU A O   1 
ATOM   1744 C  CB  . GLU A 1 204 ? -0.315  6.052   26.343  1.00  9.90   ? 204 GLU A CB  1 
ATOM   1745 C  CG  . GLU A 1 204 ? 0.555   4.771   26.215  1.00  11.19  ? 204 GLU A CG  1 
ATOM   1746 C  CD  . GLU A 1 204 ? 1.480   4.498   27.410  1.00  10.41  ? 204 GLU A CD  1 
ATOM   1747 O  OE1 . GLU A 1 204 ? 1.816   5.434   28.130  1.00  12.52  ? 204 GLU A OE1 1 
ATOM   1748 O  OE2 . GLU A 1 204 ? 1.856   3.334   27.549  1.00  10.77  ? 204 GLU A OE2 1 
ATOM   1749 N  N   . CYS A 1 205 ? -3.288  7.033   24.284  1.00  8.41   ? 205 CYS A N   1 
ATOM   1750 C  CA  . CYS A 1 205 ? -4.325  8.060   24.091  1.00  8.34   ? 205 CYS A CA  1 
ATOM   1751 C  C   . CYS A 1 205 ? -5.717  7.434   23.963  1.00  8.02   ? 205 CYS A C   1 
ATOM   1752 O  O   . CYS A 1 205 ? -6.640  8.150   23.586  1.00  9.93   ? 205 CYS A O   1 
ATOM   1753 C  CB  . CYS A 1 205 ? -4.016  8.917   22.891  1.00  8.83   ? 205 CYS A CB  1 
ATOM   1754 S  SG  . CYS A 1 205 ? -3.989  7.962   21.333  1.00  10.33  ? 205 CYS A SG  1 
ATOM   1755 N  N   . VAL A 1 206 ? -5.847  6.145   24.253  1.00  7.55   ? 206 VAL A N   1 
ATOM   1756 C  CA  . VAL A 1 206 ? -7.079  5.438   23.905  1.00  7.60   ? 206 VAL A CA  1 
ATOM   1757 C  C   . VAL A 1 206 ? -7.858  4.984   25.114  1.00  7.44   ? 206 VAL A C   1 
ATOM   1758 O  O   . VAL A 1 206 ? -7.314  4.330   26.015  1.00  8.70   ? 206 VAL A O   1 
ATOM   1759 C  CB  . VAL A 1 206 ? -6.786  4.172   23.035  1.00  8.11   ? 206 VAL A CB  1 
ATOM   1760 C  CG1 . VAL A 1 206 ? -8.090  3.460   22.702  1.00  8.21   ? 206 VAL A CG1 1 
ATOM   1761 C  CG2 . VAL A 1 206 ? -6.029  4.592   21.767  1.00  8.67   ? 206 VAL A CG2 1 
ATOM   1762 N  N   . THR A 1 207 ? -9.147  5.279   25.149  1.00  6.88   ? 207 THR A N   1 
ATOM   1763 C  CA  . THR A 1 207 ? -10.080 4.554   25.989  1.00  7.91   ? 207 THR A CA  1 
ATOM   1764 C  C   . THR A 1 207 ? -10.625 3.374   25.204  1.00  7.01   ? 207 THR A C   1 
ATOM   1765 O  O   . THR A 1 207 ? -11.264 3.586   24.145  1.00  7.86   ? 207 THR A O   1 
ATOM   1766 C  CB  . THR A 1 207 ? -11.256 5.426   26.440  1.00  8.52   ? 207 THR A CB  1 
ATOM   1767 O  OG1 . THR A 1 207 ? -10.776 6.553   27.176  1.00  8.77   ? 207 THR A OG1 1 
ATOM   1768 C  CG2 . THR A 1 207 ? -12.161 4.590   27.373  1.00  9.47   ? 207 THR A CG2 1 
ATOM   1769 N  N   . TRP A 1 208 ? -10.301 2.158   25.626  1.00  7.12   ? 208 TRP A N   1 
ATOM   1770 C  CA  . TRP A 1 208 ? -10.766 0.960   24.924  1.00  6.71   ? 208 TRP A CA  1 
ATOM   1771 C  C   . TRP A 1 208 ? -12.123 0.574   25.436  1.00  6.54   ? 208 TRP A C   1 
ATOM   1772 O  O   . TRP A 1 208 ? -12.354 0.542   26.638  1.00  7.27   ? 208 TRP A O   1 
ATOM   1773 C  CB  . TRP A 1 208 ? -9.783  -0.201  25.153  1.00  7.35   ? 208 TRP A CB  1 
ATOM   1774 C  CG  . TRP A 1 208 ? -8.662  -0.096  24.175  1.00  6.86   ? 208 TRP A CG  1 
ATOM   1775 C  CD1 . TRP A 1 208 ? -7.406  0.467   24.369  1.00  7.69   ? 208 TRP A CD1 1 
ATOM   1776 C  CD2 . TRP A 1 208 ? -8.691  -0.526  22.831  1.00  6.92   ? 208 TRP A CD2 1 
ATOM   1777 N  NE1 . TRP A 1 208 ? -6.691  0.440   23.211  1.00  7.61   ? 208 TRP A NE1 1 
ATOM   1778 C  CE2 . TRP A 1 208 ? -7.436  -0.164  22.244  1.00  7.15   ? 208 TRP A CE2 1 
ATOM   1779 C  CE3 . TRP A 1 208 ? -9.655  -1.157  22.038  1.00  7.33   ? 208 TRP A CE3 1 
ATOM   1780 C  CZ2 . TRP A 1 208 ? -7.138  -0.440  20.911  1.00  7.95   ? 208 TRP A CZ2 1 
ATOM   1781 C  CZ3 . TRP A 1 208 ? -9.338  -1.446  20.724  1.00  7.59   ? 208 TRP A CZ3 1 
ATOM   1782 C  CH2 . TRP A 1 208 ? -8.095  -1.088  20.187  1.00  8.32   ? 208 TRP A CH2 1 
ATOM   1783 N  N   . ILE A 1 209 ? -13.000 0.194   24.496  1.00  7.02   ? 209 ILE A N   1 
ATOM   1784 C  CA  . ILE A 1 209 ? -14.299 -0.316  24.749  1.00  7.06   ? 209 ILE A CA  1 
ATOM   1785 C  C   . ILE A 1 209 ? -14.400 -1.567  23.950  1.00  6.55   ? 209 ILE A C   1 
ATOM   1786 O  O   . ILE A 1 209 ? -14.495 -1.494  22.720  1.00  8.24   ? 209 ILE A O   1 
ATOM   1787 C  CB  . ILE A 1 209 ? -15.391 0.694   24.409  1.00  8.62   ? 209 ILE A CB  1 
ATOM   1788 C  CG1 . ILE A 1 209 ? -15.197 1.951   25.237  1.00  9.51   ? 209 ILE A CG1 1 
ATOM   1789 C  CG2 . ILE A 1 209 ? -16.787 0.071   24.619  1.00  9.13   ? 209 ILE A CG2 1 
ATOM   1790 C  CD1 . ILE A 1 209 ? -16.004 3.185   24.789  1.00  12.85  ? 209 ILE A CD1 1 
ATOM   1791 N  N   . VAL A 1 210 ? -14.324 -2.753  24.593  1.00  6.79   ? 210 VAL A N   1 
ATOM   1792 C  CA  . VAL A 1 210 ? -14.299 -4.033  23.903  1.00  7.07   ? 210 VAL A CA  1 
ATOM   1793 C  C   . VAL A 1 210 ? -15.613 -4.729  24.140  1.00  7.07   ? 210 VAL A C   1 
ATOM   1794 O  O   . VAL A 1 210 ? -15.949 -5.017  25.286  1.00  8.06   ? 210 VAL A O   1 
ATOM   1795 C  CB  . VAL A 1 210 ? -13.088 -4.875  24.362  1.00  7.62   ? 210 VAL A CB  1 
ATOM   1796 C  CG1 . VAL A 1 210 ? -13.091 -6.230  23.705  1.00  7.95   ? 210 VAL A CG1 1 
ATOM   1797 C  CG2 . VAL A 1 210 ? -11.803 -4.125  24.108  1.00  8.97   ? 210 VAL A CG2 1 
ATOM   1798 N  N   . LEU A 1 211 ? -16.344 -5.007  23.076  1.00  8.20   ? 211 LEU A N   1 
ATOM   1799 C  CA  . LEU A 1 211 ? -17.626 -5.643  23.250  1.00  8.64   ? 211 LEU A CA  1 
ATOM   1800 C  C   . LEU A 1 211 ? -17.468 -7.120  23.629  1.00  8.26   ? 211 LEU A C   1 
ATOM   1801 O  O   . LEU A 1 211 ? -16.609 -7.811  23.071  1.00  8.98   ? 211 LEU A O   1 
ATOM   1802 C  CB  . LEU A 1 211 ? -18.446 -5.516  21.982  1.00  9.62   ? 211 LEU A CB  1 
ATOM   1803 C  CG  . LEU A 1 211 ? -18.804 -4.106  21.553  1.00  9.49   ? 211 LEU A CG  1 
ATOM   1804 C  CD1 . LEU A 1 211 ? -19.837 -4.171  20.398  1.00  12.09  ? 211 LEU A CD1 1 
ATOM   1805 C  CD2 . LEU A 1 211 ? -19.369 -3.235  22.696  1.00  11.08  ? 211 LEU A CD2 1 
ATOM   1806 N  N   . LYS A 1 212 ? -18.322 -7.567  24.527  1.00  9.02   ? 212 LYS A N   1 
ATOM   1807 C  CA  . LYS A 1 212 ? -18.281 -8.981  24.946  1.00  9.47   ? 212 LYS A CA  1 
ATOM   1808 C  C   . LYS A 1 212 ? -18.776 -9.902  23.860  1.00  9.57   ? 212 LYS A C   1 
ATOM   1809 O  O   . LYS A 1 212 ? -18.274 -11.004 23.737  1.00  11.55  ? 212 LYS A O   1 
ATOM   1810 C  CB  . LYS A 1 212 ? -19.027 -9.191  26.197  1.00  11.43  ? 212 LYS A CB  1 
ATOM   1811 C  CG  . LYS A 1 212 ? -19.141 -10.672 26.646  1.00  14.76  ? 212 LYS A CG  1 
ATOM   1812 C  CD  . LYS A 1 212 ? -19.719 -10.869 28.013  1.00  20.25  ? 212 LYS A CD  1 
ATOM   1813 C  CE  . LYS A 1 212 ? -19.854 -12.322 28.393  1.00  23.78  ? 212 LYS A CE  1 
ATOM   1814 N  NZ  . LYS A 1 212 ? -20.741 -12.422 29.585  1.00  33.94  ? 212 LYS A NZ  1 
ATOM   1815 N  N   . GLU A 1 213 ? -19.806 -9.531  23.085  1.00  9.31   ? 213 GLU A N   1 
ATOM   1816 C  CA  . GLU A 1 213 ? -20.407 -10.432 22.121  1.00  9.70   ? 213 GLU A CA  1 
ATOM   1817 C  C   . GLU A 1 213 ? -19.618 -10.333 20.830  1.00  9.41   ? 213 GLU A C   1 
ATOM   1818 O  O   . GLU A 1 213 ? -19.568 -9.267  20.216  1.00  9.52   ? 213 GLU A O   1 
ATOM   1819 C  CB  . GLU A 1 213 ? -21.850 -10.058 21.856  1.00  10.61  ? 213 GLU A CB  1 
ATOM   1820 C  CG  . GLU A 1 213 ? -22.549 -11.037 20.946  1.00  13.48  ? 213 GLU A CG  1 
ATOM   1821 C  CD  . GLU A 1 213 ? -24.035 -10.719 20.724  1.00  17.50  ? 213 GLU A CD  1 
ATOM   1822 O  OE1 . GLU A 1 213 ? -24.604 -9.860  21.349  1.00  15.48  ? 213 GLU A OE1 1 
ATOM   1823 O  OE2 . GLU A 1 213 ? -24.562 -11.428 19.864  1.00  34.08  ? 213 GLU A OE2 1 
ATOM   1824 N  N   . PRO A 1 214 ? -19.054 -11.459 20.351  1.00  9.69   ? 214 PRO A N   1 
ATOM   1825 C  CA  . PRO A 1 214 ? -18.389 -11.415 19.016  1.00  9.83   ? 214 PRO A CA  1 
ATOM   1826 C  C   . PRO A 1 214 ? -19.388 -11.376 17.903  1.00  10.16  ? 214 PRO A C   1 
ATOM   1827 O  O   . PRO A 1 214 ? -20.578 -11.742 18.105  1.00  12.19  ? 214 PRO A O   1 
ATOM   1828 C  CB  . PRO A 1 214 ? -17.662 -12.756 18.928  1.00  10.02  ? 214 PRO A CB  1 
ATOM   1829 C  CG  . PRO A 1 214 ? -18.440 -13.628 19.796  1.00  17.35  ? 214 PRO A CG  1 
ATOM   1830 C  CD  . PRO A 1 214 ? -19.000 -12.799 20.969  1.00  11.31  ? 214 PRO A CD  1 
ATOM   1831 N  N   . ILE A 1 215 ? -18.997 -10.959 16.725  1.00  9.80   ? 215 ILE A N   1 
ATOM   1832 C  CA  . ILE A 1 215 ? -19.771 -11.166 15.522  1.00  9.96   ? 215 ILE A CA  1 
ATOM   1833 C  C   . ILE A 1 215 ? -19.268 -12.417 14.850  1.00  10.27  ? 215 ILE A C   1 
ATOM   1834 O  O   . ILE A 1 215 ? -18.103 -12.786 14.992  1.00  10.70  ? 215 ILE A O   1 
ATOM   1835 C  CB  . ILE A 1 215 ? -19.770 -9.936  14.562  1.00  10.72  ? 215 ILE A CB  1 
ATOM   1836 C  CG1 . ILE A 1 215 ? -18.379 -9.620  14.071  1.00  10.68  ? 215 ILE A CG1 1 
ATOM   1837 C  CG2 . ILE A 1 215 ? -20.507 -8.743  15.250  1.00  11.71  ? 215 ILE A CG2 1 
ATOM   1838 C  CD1 . ILE A 1 215 ? -18.413 -8.602  12.904  1.00  13.26  ? 215 ILE A CD1 1 
ATOM   1839 N  N   A SER A 1 216 ? -20.151 -13.175 14.180  0.50  10.46  ? 216 SER A N   1 
ATOM   1840 N  N   B SER A 1 216 ? -20.126 -12.978 13.990  0.50  10.78  ? 216 SER A N   1 
ATOM   1841 C  CA  A SER A 1 216 ? -19.680 -14.260 13.289  0.50  11.64  ? 216 SER A CA  1 
ATOM   1842 C  CA  B SER A 1 216 ? -19.843 -14.178 13.248  0.50  11.37  ? 216 SER A CA  1 
ATOM   1843 C  C   A SER A 1 216 ? -19.545 -13.791 11.906  0.50  9.95   ? 216 SER A C   1 
ATOM   1844 C  C   B SER A 1 216 ? -19.571 -13.765 11.844  0.50  11.19  ? 216 SER A C   1 
ATOM   1845 O  O   A SER A 1 216 ? -20.412 -13.098 11.397  0.50  11.86  ? 216 SER A O   1 
ATOM   1846 O  O   B SER A 1 216 ? -20.336 -13.000 11.274  0.50  11.74  ? 216 SER A O   1 
ATOM   1847 C  CB  A SER A 1 216 ? -20.665 -15.419 13.254  0.50  12.33  ? 216 SER A CB  1 
ATOM   1848 C  CB  B SER A 1 216 ? -21.017 -15.177 13.346  0.50  14.93  ? 216 SER A CB  1 
ATOM   1849 O  OG  A SER A 1 216 ? -20.889 -15.981 14.496  0.50  15.08  ? 216 SER A OG  1 
ATOM   1850 O  OG  B SER A 1 216 ? -20.618 -16.328 12.651  0.50  17.23  ? 216 SER A OG  1 
ATOM   1851 N  N   . VAL A 1 217 ? -18.468 -14.241 11.271  1.00  10.66  ? 217 VAL A N   1 
ATOM   1852 C  CA  . VAL A 1 217 ? -18.190 -14.033 9.848   1.00  11.53  ? 217 VAL A CA  1 
ATOM   1853 C  C   . VAL A 1 217 ? -17.950 -15.403 9.228   1.00  11.16  ? 217 VAL A C   1 
ATOM   1854 O  O   . VAL A 1 217 ? -17.602 -16.383 9.958   1.00  11.53  ? 217 VAL A O   1 
ATOM   1855 C  CB  . VAL A 1 217 ? -16.971 -13.126 9.634   1.00  11.21  ? 217 VAL A CB  1 
ATOM   1856 C  CG1 . VAL A 1 217 ? -17.242 -11.783 10.280  1.00  11.82  ? 217 VAL A CG1 1 
ATOM   1857 C  CG2 . VAL A 1 217 ? -15.706 -13.759 10.132  1.00  13.19  ? 217 VAL A CG2 1 
ATOM   1858 N  N   . SER A 1 218 ? -18.109 -15.574 7.944   1.00  11.14  ? 218 SER A N   1 
ATOM   1859 C  CA  . SER A 1 218 ? -17.923 -16.923 7.362   1.00  12.22  ? 218 SER A CA  1 
ATOM   1860 C  C   . SER A 1 218 ? -16.462 -17.174 7.023   1.00  11.24  ? 218 SER A C   1 
ATOM   1861 O  O   . SER A 1 218 ? -15.649 -16.261 6.889   1.00  11.63  ? 218 SER A O   1 
ATOM   1862 C  CB  . SER A 1 218 ? -18.766 -17.056 6.120   1.00  12.94  ? 218 SER A CB  1 
ATOM   1863 O  OG  . SER A 1 218 ? -18.320 -16.182 5.140   1.00  13.33  ? 218 SER A OG  1 
ATOM   1864 N  N   A SER A 1 219 ? -16.206 -18.447 6.870   0.50  12.88  ? 219 SER A N   1 
ATOM   1865 N  N   B SER A 1 219 ? -16.101 -18.443 6.866   0.50  12.72  ? 219 SER A N   1 
ATOM   1866 C  CA  A SER A 1 219 ? -14.904 -18.831 6.458   0.50  13.85  ? 219 SER A CA  1 
ATOM   1867 C  CA  B SER A 1 219 ? -14.753 -18.768 6.395   0.50  14.14  ? 219 SER A CA  1 
ATOM   1868 C  C   A SER A 1 219 ? -14.524 -18.133 5.119   0.50  13.87  ? 219 SER A C   1 
ATOM   1869 C  C   B SER A 1 219 ? -14.458 -18.113 5.027   0.50  13.11  ? 219 SER A C   1 
ATOM   1870 O  O   A SER A 1 219 ? -13.390 -17.683 4.996   0.50  14.64  ? 219 SER A O   1 
ATOM   1871 O  O   B SER A 1 219 ? -13.341 -17.686 4.773   0.50  14.69  ? 219 SER A O   1 
ATOM   1872 C  CB  A SER A 1 219 ? -14.780 -20.359 6.450   0.50  15.35  ? 219 SER A CB  1 
ATOM   1873 C  CB  B SER A 1 219 ? -14.533 -20.291 6.356   0.50  16.34  ? 219 SER A CB  1 
ATOM   1874 O  OG  A SER A 1 219 ? -15.670 -20.889 5.506   0.50  14.70  ? 219 SER A OG  1 
ATOM   1875 O  OG  B SER A 1 219 ? -13.155 -20.660 6.377   0.50  22.14  ? 219 SER A OG  1 
ATOM   1876 N  N   . GLU A 1 220 ? -15.467 -17.995 4.165   1.00  13.28  ? 220 GLU A N   1 
ATOM   1877 C  CA  . GLU A 1 220 ? -15.236 -17.347 2.910   1.00  14.03  ? 220 GLU A CA  1 
ATOM   1878 C  C   . GLU A 1 220 ? -14.881 -15.885 3.105   1.00  12.99  ? 220 GLU A C   1 
ATOM   1879 O  O   . GLU A 1 220 ? -14.053 -15.303 2.373   1.00  14.22  ? 220 GLU A O   1 
ATOM   1880 C  CB  . GLU A 1 220 ? -16.386 -17.440 1.974   1.00  16.33  ? 220 GLU A CB  1 
ATOM   1881 C  CG  . GLU A 1 220 ? -16.624 -18.876 1.504   1.00  21.58  ? 220 GLU A CG  1 
ATOM   1882 C  CD  . GLU A 1 220 ? -17.475 -19.715 2.479   1.00  20.40  ? 220 GLU A CD  1 
ATOM   1883 O  OE1 . GLU A 1 220 ? -17.940 -19.250 3.515   1.00  19.03  ? 220 GLU A OE1 1 
ATOM   1884 O  OE2 . GLU A 1 220 ? -17.728 -20.882 2.157   1.00  35.04  ? 220 GLU A OE2 1 
ATOM   1885 N  N   . GLN A 1 221 ? -15.529 -15.216 4.054   1.00  11.98  ? 221 GLN A N   1 
ATOM   1886 C  CA  . GLN A 1 221 ? -15.237 -13.809 4.309   1.00  11.83  ? 221 GLN A CA  1 
ATOM   1887 C  C   . GLN A 1 221 ? -13.790 -13.631 4.823   1.00  10.82  ? 221 GLN A C   1 
ATOM   1888 O  O   . GLN A 1 221 ? -13.045 -12.761 4.333   1.00  12.05  ? 221 GLN A O   1 
ATOM   1889 C  CB  . GLN A 1 221 ? -16.277 -13.209 5.232   1.00  11.74  ? 221 GLN A CB  1 
ATOM   1890 C  CG  . GLN A 1 221 ? -17.671 -13.101 4.581   1.00  12.67  ? 221 GLN A CG  1 
ATOM   1891 C  CD  . GLN A 1 221 ? -18.734 -12.536 5.490   1.00  12.87  ? 221 GLN A CD  1 
ATOM   1892 O  OE1 . GLN A 1 221 ? -18.848 -12.914 6.676   1.00  12.63  ? 221 GLN A OE1 1 
ATOM   1893 N  NE2 . GLN A 1 221 ? -19.541 -11.646 4.923   1.00  13.79  ? 221 GLN A NE2 1 
ATOM   1894 N  N   A VAL A 1 222 ? -13.493 -14.363 5.891   0.50  11.49  ? 222 VAL A N   1 
ATOM   1895 N  N   B VAL A 1 222 ? -13.337 -14.528 5.688   0.50  11.56  ? 222 VAL A N   1 
ATOM   1896 C  CA  A VAL A 1 222 ? -12.155 -14.238 6.417   0.50  11.94  ? 222 VAL A CA  1 
ATOM   1897 C  CA  B VAL A 1 222 ? -12.026 -14.362 6.313   0.50  13.69  ? 222 VAL A CA  1 
ATOM   1898 C  C   A VAL A 1 222 ? -11.083 -14.698 5.379   0.50  12.86  ? 222 VAL A C   1 
ATOM   1899 C  C   B VAL A 1 222 ? -10.961 -14.763 5.336   0.50  14.70  ? 222 VAL A C   1 
ATOM   1900 O  O   A VAL A 1 222 ? -10.017 -14.072 5.352   0.50  12.99  ? 222 VAL A O   1 
ATOM   1901 O  O   B VAL A 1 222 ? -9.820  -14.245 5.306   0.50  14.98  ? 222 VAL A O   1 
ATOM   1902 C  CB  A VAL A 1 222 ? -11.963 -14.825 7.828   0.50  12.26  ? 222 VAL A CB  1 
ATOM   1903 C  CB  B VAL A 1 222 ? -11.914 -15.282 7.481   0.50  15.20  ? 222 VAL A CB  1 
ATOM   1904 C  CG1 A VAL A 1 222 ? -11.877 -16.373 7.763   0.50  12.73  ? 222 VAL A CG1 1 
ATOM   1905 C  CG1 B VAL A 1 222 ? -10.495 -15.374 7.969   0.50  18.43  ? 222 VAL A CG1 1 
ATOM   1906 C  CG2 A VAL A 1 222 ? -10.722 -14.254 8.510   0.50  13.10  ? 222 VAL A CG2 1 
ATOM   1907 C  CG2 B VAL A 1 222 ? -12.742 -14.688 8.572   0.50  15.27  ? 222 VAL A CG2 1 
ATOM   1908 N  N   . LEU A 1 223 ? -11.344 -15.695 4.479   1.00  13.98  ? 223 LEU A N   1 
ATOM   1909 C  CA  . LEU A 1 223 ? -10.449 -16.056 3.436   1.00  16.64  ? 223 LEU A CA  1 
ATOM   1910 C  C   . LEU A 1 223 ? -10.076 -14.881 2.552   1.00  13.81  ? 223 LEU A C   1 
ATOM   1911 O  O   . LEU A 1 223 ? -8.897  -14.731 2.118   1.00  15.73  ? 223 LEU A O   1 
ATOM   1912 C  CB  . LEU A 1 223 ? -11.007 -17.214 2.653   1.00  20.12  ? 223 LEU A CB  1 
ATOM   1913 C  CG  . LEU A 1 223 ? -10.826 -18.558 3.366   1.00  32.89  ? 223 LEU A CG  1 
ATOM   1914 C  CD1 . LEU A 1 223 ? -11.653 -19.694 2.738   1.00  40.66  ? 223 LEU A CD1 1 
ATOM   1915 C  CD2 . LEU A 1 223 ? -9.397  -19.013 3.446   1.00  31.45  ? 223 LEU A CD2 1 
ATOM   1916 N  N   . LYS A 1 224 ? -11.058 -14.026 2.308   1.00  14.68  ? 224 LYS A N   1 
ATOM   1917 C  CA  . LYS A 1 224 ? -10.815 -12.856 1.458   1.00  14.06  ? 224 LYS A CA  1 
ATOM   1918 C  C   . LYS A 1 224 ? -9.861  -11.889 2.193   1.00  12.80  ? 224 LYS A C   1 
ATOM   1919 O  O   . LYS A 1 224 ? -9.017  -11.272 1.554   1.00  13.26  ? 224 LYS A O   1 
ATOM   1920 C  CB  . LYS A 1 224 ? -12.100 -12.197 1.041   1.00  20.46  ? 224 LYS A CB  1 
ATOM   1921 C  CG  . LYS A 1 224 ? -12.807 -13.058 -0.037  1.00  20.32  ? 224 LYS A CG  1 
ATOM   1922 C  CD  . LYS A 1 224 ? -14.104 -12.471 -0.581  1.00  32.79  ? 224 LYS A CD  1 
ATOM   1923 C  CE  . LYS A 1 224 ? -14.450 -12.867 -2.024  1.00  41.43  ? 224 LYS A CE  1 
ATOM   1924 N  NZ  . LYS A 1 224 ? -15.521 -13.925 -2.114  1.00  39.65  ? 224 LYS A NZ  1 
ATOM   1925 N  N   . PHE A 1 225 ? -9.936  -11.751 3.519   1.00  11.22  ? 225 PHE A N   1 
ATOM   1926 C  CA  . PHE A 1 225 ? -8.957  -10.910 4.241   1.00  11.14  ? 225 PHE A CA  1 
ATOM   1927 C  C   . PHE A 1 225 ? -7.560  -11.438 4.010   1.00  10.64  ? 225 PHE A C   1 
ATOM   1928 O  O   . PHE A 1 225 ? -6.623  -10.678 3.797   1.00  11.46  ? 225 PHE A O   1 
ATOM   1929 C  CB  . PHE A 1 225 ? -9.186  -10.948 5.770   1.00  11.64  ? 225 PHE A CB  1 
ATOM   1930 C  CG  . PHE A 1 225 ? -10.402 -10.190 6.313   1.00  11.40  ? 225 PHE A CG  1 
ATOM   1931 C  CD1 . PHE A 1 225 ? -11.399 -9.687  5.556   1.00  14.22  ? 225 PHE A CD1 1 
ATOM   1932 C  CD2 . PHE A 1 225 ? -10.510 -10.022 7.712   1.00  13.54  ? 225 PHE A CD2 1 
ATOM   1933 C  CE1 . PHE A 1 225 ? -12.501 -8.946  6.110   1.00  14.22  ? 225 PHE A CE1 1 
ATOM   1934 C  CE2 . PHE A 1 225 ? -11.558 -9.310  8.279   1.00  16.65  ? 225 PHE A CE2 1 
ATOM   1935 C  CZ  . PHE A 1 225 ? -12.532 -8.751  7.436   1.00  15.06  ? 225 PHE A CZ  1 
ATOM   1936 N  N   . ARG A 1 226 ? -7.469  -12.768 4.040   1.00  10.39  ? 226 ARG A N   1 
ATOM   1937 C  CA  . ARG A 1 226 ? -6.149  -13.391 4.001   1.00  11.42  ? 226 ARG A CA  1 
ATOM   1938 C  C   . ARG A 1 226 ? -5.523  -13.418 2.600   1.00  12.84  ? 226 ARG A C   1 
ATOM   1939 O  O   . ARG A 1 226 ? -4.399  -13.822 2.464   1.00  13.44  ? 226 ARG A O   1 
ATOM   1940 C  CB  . ARG A 1 226 ? -6.258  -14.815 4.495   1.00  11.73  ? 226 ARG A CB  1 
ATOM   1941 C  CG  . ARG A 1 226 ? -6.633  -14.929 5.981   1.00  11.73  ? 226 ARG A CG  1 
ATOM   1942 C  CD  . ARG A 1 226 ? -6.663  -16.404 6.413   1.00  13.96  ? 226 ARG A CD  1 
ATOM   1943 N  NE  . ARG A 1 226 ? -7.125  -16.517 7.783   1.00  11.81  ? 226 ARG A NE  1 
ATOM   1944 C  CZ  . ARG A 1 226 ? -7.955  -17.419 8.241   1.00  13.21  ? 226 ARG A CZ  1 
ATOM   1945 N  NH1 . ARG A 1 226 ? -8.393  -18.410 7.457   1.00  17.54  ? 226 ARG A NH1 1 
ATOM   1946 N  NH2 . ARG A 1 226 ? -8.329  -17.404 9.492   1.00  15.07  ? 226 ARG A NH2 1 
ATOM   1947 N  N   . LYS A 1 227 ? -6.257  -12.948 1.582   1.00  11.68  ? 227 LYS A N   1 
ATOM   1948 C  CA  . LYS A 1 227 ? -5.705  -12.788 0.247   1.00  13.34  ? 227 LYS A CA  1 
ATOM   1949 C  C   . LYS A 1 227 ? -5.109  -11.449 -0.001  1.00  11.70  ? 227 LYS A C   1 
ATOM   1950 O  O   . LYS A 1 227 ? -4.443  -11.221 -1.034  1.00  15.35  ? 227 LYS A O   1 
ATOM   1951 C  CB  . LYS A 1 227 ? -6.801  -13.040 -0.790  1.00  15.64  ? 227 LYS A CB  1 
ATOM   1952 C  CG  . LYS A 1 227 ? -7.219  -14.510 -0.850  1.00  19.30  ? 227 LYS A CG  1 
ATOM   1953 C  CD  . LYS A 1 227 ? -8.280  -14.700 -1.978  1.00  26.50  ? 227 LYS A CD  1 
ATOM   1954 C  CE  . LYS A 1 227 ? -7.730  -14.728 -3.428  1.00  37.93  ? 227 LYS A CE  1 
ATOM   1955 N  NZ  . LYS A 1 227 ? -8.675  -14.708 -4.605  1.00  55.70  ? 227 LYS A NZ  1 
ATOM   1956 N  N   . LEU A 1 228 ? -5.288  -10.499 0.914   1.00  11.88  ? 228 LEU A N   1 
ATOM   1957 C  CA  . LEU A 1 228 ? -4.576  -9.243  0.848   1.00  12.09  ? 228 LEU A CA  1 
ATOM   1958 C  C   . LEU A 1 228 ? -3.079  -9.425  0.947   1.00  13.72  ? 228 LEU A C   1 
ATOM   1959 O  O   . LEU A 1 228 ? -2.635  -10.453 1.383   1.00  13.20  ? 228 LEU A O   1 
ATOM   1960 C  CB  . LEU A 1 228 ? -5.072  -8.288  1.947   1.00  12.40  ? 228 LEU A CB  1 
ATOM   1961 C  CG  . LEU A 1 228 ? -6.517  -7.812  1.721   1.00  12.23  ? 228 LEU A CG  1 
ATOM   1962 C  CD1 . LEU A 1 228 ? -7.063  -7.177  2.999   1.00  12.86  ? 228 LEU A CD1 1 
ATOM   1963 C  CD2 . LEU A 1 228 ? -6.600  -6.746  0.558   1.00  16.43  ? 228 LEU A CD2 1 
ATOM   1964 N  N   . ASN A 1 229 ? -2.348  -8.390  0.510   1.00  14.26  ? 229 ASN A N   1 
ATOM   1965 C  CA  . ASN A 1 229 ? -0.868  -8.409  0.566   1.00  15.18  ? 229 ASN A CA  1 
ATOM   1966 C  C   . ASN A 1 229 ? -0.402  -7.246  1.393   1.00  16.15  ? 229 ASN A C   1 
ATOM   1967 O  O   . ASN A 1 229 ? -0.870  -6.143  1.317   1.00  16.13  ? 229 ASN A O   1 
ATOM   1968 C  CB  . ASN A 1 229 ? -0.270  -8.252  -0.818  1.00  16.66  ? 229 ASN A CB  1 
ATOM   1969 C  CG  . ASN A 1 229 ? -0.433  -9.436  -1.775  1.00  17.62  ? 229 ASN A CG  1 
ATOM   1970 O  OD1 . ASN A 1 229 ? 0.063   -9.322  -2.887  1.00  24.10  ? 229 ASN A OD1 1 
ATOM   1971 N  ND2 . ASN A 1 229 ? -1.029  -10.532 -1.406  1.00  17.53  ? 229 ASN A ND2 1 
ATOM   1972 N  N   . PHE A 1 230 ? 0.616   -7.582  2.156   1.00  16.53  ? 230 PHE A N   1 
ATOM   1973 C  CA  . PHE A 1 230 ? 1.368   -6.507  2.823   1.00  18.47  ? 230 PHE A CA  1 
ATOM   1974 C  C   . PHE A 1 230 ? 2.213   -5.680  1.849   1.00  17.38  ? 230 PHE A C   1 
ATOM   1975 O  O   . PHE A 1 230 ? 2.483   -4.490  2.095   1.00  17.65  ? 230 PHE A O   1 
ATOM   1976 C  CB  . PHE A 1 230 ? 2.375   -7.052  3.819   1.00  19.24  ? 230 PHE A CB  1 
ATOM   1977 C  CG  . PHE A 1 230 ? 1.775   -7.608  5.068   1.00  16.60  ? 230 PHE A CG  1 
ATOM   1978 C  CD1 . PHE A 1 230 ? 1.058   -6.807  5.970   1.00  15.15  ? 230 PHE A CD1 1 
ATOM   1979 C  CD2 . PHE A 1 230 ? 2.117   -8.848  5.463   1.00  14.85  ? 230 PHE A CD2 1 
ATOM   1980 C  CE1 . PHE A 1 230 ? 0.611   -7.284  7.200   1.00  15.40  ? 230 PHE A CE1 1 
ATOM   1981 C  CE2 . PHE A 1 230 ? 1.674   -9.393  6.707   1.00  16.75  ? 230 PHE A CE2 1 
ATOM   1982 C  CZ  . PHE A 1 230 ? 0.923   -8.600  7.578   1.00  14.85  ? 230 PHE A CZ  1 
ATOM   1983 N  N   . ASN A 1 231 ? 2.733   -6.321  0.808   1.00  18.39  ? 231 ASN A N   1 
ATOM   1984 C  CA  . ASN A 1 231 ? 3.603   -5.664  -0.194  1.00  19.29  ? 231 ASN A CA  1 
ATOM   1985 C  C   . ASN A 1 231 ? 2.851   -4.735  -1.140  1.00  21.17  ? 231 ASN A C   1 
ATOM   1986 O  O   . ASN A 1 231 ? 1.697   -4.879  -1.274  1.00  20.13  ? 231 ASN A O   1 
ATOM   1987 C  CB  . ASN A 1 231 ? 4.311   -6.790  -0.938  1.00  24.16  ? 231 ASN A CB  1 
ATOM   1988 C  CG  . ASN A 1 231 ? 3.367   -7.776  -1.531  1.00  24.45  ? 231 ASN A CG  1 
ATOM   1989 O  OD1 . ASN A 1 231 ? 2.886   -8.690  -0.816  1.00  21.16  ? 231 ASN A OD1 1 
ATOM   1990 N  ND2 . ASN A 1 231 ? 3.045   -7.605  -2.819  1.00  25.29  ? 231 ASN A ND2 1 
ATOM   1991 N  N   . GLY A 1 232 ? 3.502   -3.825  -1.866  1.00  22.75  ? 232 GLY A N   1 
ATOM   1992 C  CA  . GLY A 1 232 ? 2.778   -3.020  -2.861  1.00  24.50  ? 232 GLY A CA  1 
ATOM   1993 C  C   . GLY A 1 232 ? 2.879   -3.638  -4.253  1.00  23.94  ? 232 GLY A C   1 
ATOM   1994 O  O   . GLY A 1 232 ? 3.707   -4.511  -4.355  1.00  23.83  ? 232 GLY A O   1 
ATOM   1995 N  N   . GLU A 1 233 ? 2.052   -3.178  -5.230  1.00  19.65  ? 233 GLU A N   1 
ATOM   1996 C  CA  . GLU A 1 233 ? 1.985   -3.736  -6.651  1.00  19.14  ? 233 GLU A CA  1 
ATOM   1997 C  C   . GLU A 1 233 ? 3.428   -3.953  -7.111  1.00  26.61  ? 233 GLU A C   1 
ATOM   1998 O  O   . GLU A 1 233 ? 4.266   -3.095  -6.994  1.00  31.56  ? 233 GLU A O   1 
ATOM   1999 C  CB  . GLU A 1 233 ? 1.111   -2.861  -7.540  1.00  22.60  ? 233 GLU A CB  1 
ATOM   2000 C  CG  . GLU A 1 233 ? 0.717   -3.478  -8.916  1.00  23.50  ? 233 GLU A CG  1 
ATOM   2001 C  CD  . GLU A 1 233 ? -0.072  -2.510  -9.724  1.00  39.00  ? 233 GLU A CD  1 
ATOM   2002 O  OE1 . GLU A 1 233 ? -0.289  -1.316  -9.274  1.00  34.05  ? 233 GLU A OE1 1 
ATOM   2003 O  OE2 . GLU A 1 233 ? -0.412  -2.955  -10.851 1.00  40.29  ? 233 GLU A OE2 1 
ATOM   2004 N  N   . GLY A 1 234 ? 3.821   -5.182  -7.432  1.00  44.64  ? 234 GLY A N   1 
ATOM   2005 C  CA  . GLY A 1 234 ? 5.232   -5.443  -7.754  1.00  38.10  ? 234 GLY A CA  1 
ATOM   2006 C  C   . GLY A 1 234 ? 6.374   -5.391  -6.711  1.00  60.96  ? 234 GLY A C   1 
ATOM   2007 O  O   . GLY A 1 234 ? 7.269   -4.550  -6.791  1.00  100.47 ? 234 GLY A O   1 
ATOM   2008 N  N   . GLU A 1 235 ? 6.323   -6.310  -5.746  1.00  30.56  ? 235 GLU A N   1 
ATOM   2009 C  CA  . GLU A 1 235 ? 7.402   -6.755  -4.761  1.00  29.94  ? 235 GLU A CA  1 
ATOM   2010 C  C   . GLU A 1 235 ? 7.115   -8.283  -4.430  1.00  18.79  ? 235 GLU A C   1 
ATOM   2011 O  O   . GLU A 1 235 ? 5.979   -8.638  -4.767  1.00  29.30  ? 235 GLU A O   1 
ATOM   2012 C  CB  . GLU A 1 235 ? 7.210   -5.852  -3.529  1.00  37.38  ? 235 GLU A CB  1 
ATOM   2013 C  CG  . GLU A 1 235 ? 7.413   -4.360  -3.823  1.00  35.80  ? 235 GLU A CG  1 
ATOM   2014 C  CD  . GLU A 1 235 ? 7.097   -3.508  -2.580  1.00  47.67  ? 235 GLU A CD  1 
ATOM   2015 O  OE1 . GLU A 1 235 ? 6.545   -4.015  -1.560  1.00  61.65  ? 235 GLU A OE1 1 
ATOM   2016 O  OE2 . GLU A 1 235 ? 7.403   -2.293  -2.604  1.00  52.41  ? 235 GLU A OE2 1 
ATOM   2017 N  N   . PRO A 1 236 ? 8.047   -9.109  -3.853  1.00  26.32  ? 236 PRO A N   1 
ATOM   2018 C  CA  . PRO A 1 236 ? 7.552   -10.451 -3.620  1.00  25.56  ? 236 PRO A CA  1 
ATOM   2019 C  C   . PRO A 1 236 ? 6.205   -10.444 -2.781  1.00  27.59  ? 236 PRO A C   1 
ATOM   2020 O  O   . PRO A 1 236 ? 6.012   -9.613  -1.830  1.00  28.72  ? 236 PRO A O   1 
ATOM   2021 C  CB  . PRO A 1 236 ? 8.730   -11.092 -2.865  1.00  32.98  ? 236 PRO A CB  1 
ATOM   2022 C  CG  . PRO A 1 236 ? 9.884   -10.496 -3.520  1.00  27.82  ? 236 PRO A CG  1 
ATOM   2023 C  CD  . PRO A 1 236 ? 9.493   -9.060  -3.566  1.00  23.12  ? 236 PRO A CD  1 
ATOM   2024 N  N   . GLU A 1 237 ? 5.300   -11.354 -3.162  1.00  25.23  ? 237 GLU A N   1 
ATOM   2025 C  CA  . GLU A 1 237 ? 4.026   -11.478 -2.488  1.00  21.26  ? 237 GLU A CA  1 
ATOM   2026 C  C   . GLU A 1 237 ? 4.166   -12.000 -1.085  1.00  19.44  ? 237 GLU A C   1 
ATOM   2027 O  O   . GLU A 1 237 ? 4.640   -13.116 -0.898  1.00  23.14  ? 237 GLU A O   1 
ATOM   2028 C  CB  . GLU A 1 237 ? 3.057   -12.498 -3.175  1.00  19.68  ? 237 GLU A CB  1 
ATOM   2029 C  CG  . GLU A 1 237 ? 1.601   -12.290 -2.683  1.00  26.59  ? 237 GLU A CG  1 
ATOM   2030 C  CD  . GLU A 1 237 ? 0.475   -13.145 -3.288  1.00  23.39  ? 237 GLU A CD  1 
ATOM   2031 O  OE1 . GLU A 1 237 ? 0.793   -14.182 -3.909  1.00  40.35  ? 237 GLU A OE1 1 
ATOM   2032 O  OE2 . GLU A 1 237 ? -0.732  -12.753 -3.171  1.00  24.91  ? 237 GLU A OE2 1 
ATOM   2033 N  N   . GLU A 1 238 ? 3.645   -11.179 -0.133  1.00  19.02  ? 238 GLU A N   1 
ATOM   2034 C  CA  . GLU A 1 238 ? 3.584   -11.543 1.274   1.00  20.47  ? 238 GLU A CA  1 
ATOM   2035 C  C   . GLU A 1 238 ? 2.143   -11.363 1.721   1.00  15.89  ? 238 GLU A C   1 
ATOM   2036 O  O   . GLU A 1 238 ? 1.610   -10.258 1.751   1.00  19.08  ? 238 GLU A O   1 
ATOM   2037 C  CB  . GLU A 1 238 ? 4.574   -10.695 2.099   1.00  24.94  ? 238 GLU A CB  1 
ATOM   2038 C  CG  . GLU A 1 238 ? 6.091   -10.944 1.952   1.00  33.71  ? 238 GLU A CG  1 
ATOM   2039 C  CD  . GLU A 1 238 ? 6.954   -9.970  2.732   0.010 29.24  ? 238 GLU A CD  1 
ATOM   2040 O  OE1 . GLU A 1 238 ? 6.411   -9.146  3.502   0.010 25.65  ? 238 GLU A OE1 1 
ATOM   2041 O  OE2 . GLU A 1 238 ? 8.191   -10.038 2.569   0.010 17.09  ? 238 GLU A OE2 1 
ATOM   2042 N  N   . LEU A 1 239 ? 1.474   -12.500 1.989   1.00  14.86  ? 239 LEU A N   1 
ATOM   2043 C  CA  . LEU A 1 239 ? 0.090   -12.390 2.368   1.00  12.56  ? 239 LEU A CA  1 
ATOM   2044 C  C   . LEU A 1 239 ? -0.110  -11.565 3.636   1.00  11.97  ? 239 LEU A C   1 
ATOM   2045 O  O   . LEU A 1 239 ? 0.665   -11.754 4.629   1.00  14.30  ? 239 LEU A O   1 
ATOM   2046 C  CB  . LEU A 1 239 ? -0.533  -13.772 2.592   1.00  15.62  ? 239 LEU A CB  1 
ATOM   2047 C  CG  . LEU A 1 239 ? -0.637  -14.678 1.346   1.00  16.09  ? 239 LEU A CG  1 
ATOM   2048 C  CD1 . LEU A 1 239 ? -1.278  -15.983 1.798   1.00  22.82  ? 239 LEU A CD1 1 
ATOM   2049 C  CD2 . LEU A 1 239 ? -1.419  -13.957 0.277   1.00  17.72  ? 239 LEU A CD2 1 
ATOM   2050 N  N   . MET A 1 240 ? -1.131  -10.718 3.687   1.00  12.63  ? 240 MET A N   1 
ATOM   2051 C  CA  . MET A 1 240 ? -1.447  -9.901  4.879   1.00  11.78  ? 240 MET A CA  1 
ATOM   2052 C  C   . MET A 1 240 ? -2.244  -10.837 5.805   1.00  10.76  ? 240 MET A C   1 
ATOM   2053 O  O   . MET A 1 240 ? -3.458  -10.968 5.684   1.00  11.10  ? 240 MET A O   1 
ATOM   2054 C  CB  . MET A 1 240 ? -2.274  -8.707  4.432   1.00  13.56  ? 240 MET A CB  1 
ATOM   2055 C  CG  . MET A 1 240 ? -2.573  -7.733  5.632   1.00  13.44  ? 240 MET A CG  1 
ATOM   2056 S  SD  . MET A 1 240 ? -3.555  -6.317  5.101   1.00  14.12  ? 240 MET A SD  1 
ATOM   2057 C  CE  . MET A 1 240 ? -2.201  -5.277  4.488   1.00  14.91  ? 240 MET A CE  1 
ATOM   2058 N  N   . VAL A 1 241 ? -1.485  -11.430 6.726   1.00  10.73  ? 241 VAL A N   1 
ATOM   2059 C  CA  . VAL A 1 241 ? -2.057  -12.278 7.790   1.00  10.22  ? 241 VAL A CA  1 
ATOM   2060 C  C   . VAL A 1 241 ? -1.273  -12.056 9.052   1.00  9.76   ? 241 VAL A C   1 
ATOM   2061 O  O   . VAL A 1 241 ? -0.091  -11.647 8.961   1.00  11.05  ? 241 VAL A O   1 
ATOM   2062 C  CB  . VAL A 1 241 ? -2.037  -13.797 7.408   1.00  10.95  ? 241 VAL A CB  1 
ATOM   2063 C  CG1 . VAL A 1 241 ? -2.947  -14.102 6.232   1.00  12.65  ? 241 VAL A CG1 1 
ATOM   2064 C  CG2 . VAL A 1 241 ? -0.593  -14.249 7.147   1.00  13.16  ? 241 VAL A CG2 1 
ATOM   2065 N  N   . ASP A 1 242 ? -1.843  -12.341 10.213  1.00  8.99   ? 242 ASP A N   1 
ATOM   2066 C  CA  . ASP A 1 242 ? -1.141  -12.180 11.482  1.00  9.21   ? 242 ASP A CA  1 
ATOM   2067 C  C   . ASP A 1 242 ? -0.675  -10.754 11.669  1.00  9.05   ? 242 ASP A C   1 
ATOM   2068 O  O   . ASP A 1 242 ? 0.424   -10.515 12.173  1.00  11.16  ? 242 ASP A O   1 
ATOM   2069 C  CB  . ASP A 1 242 ? -0.054  -13.242 11.648  1.00  10.39  ? 242 ASP A CB  1 
ATOM   2070 C  CG  . ASP A 1 242 ? -0.669  -14.619 11.781  1.00  10.21  ? 242 ASP A CG  1 
ATOM   2071 O  OD1 . ASP A 1 242 ? -1.736  -14.765 12.456  1.00  10.35  ? 242 ASP A OD1 1 
ATOM   2072 O  OD2 . ASP A 1 242 ? -0.118  -15.554 11.152  1.00  12.02  ? 242 ASP A OD2 1 
ATOM   2073 N  N   . ASN A 1 243 ? -1.565  -9.816  11.415  1.00  8.72   ? 243 ASN A N   1 
ATOM   2074 C  CA  . ASN A 1 243 ? -1.272  -8.385  11.591  1.00  9.13   ? 243 ASN A CA  1 
ATOM   2075 C  C   . ASN A 1 243 ? -1.881  -7.927  12.952  1.00  8.27   ? 243 ASN A C   1 
ATOM   2076 O  O   . ASN A 1 243 ? -2.541  -6.897  13.055  1.00  9.75   ? 243 ASN A O   1 
ATOM   2077 C  CB  . ASN A 1 243 ? -1.853  -7.543  10.447  1.00  9.16   ? 243 ASN A CB  1 
ATOM   2078 C  CG  . ASN A 1 243 ? -3.287  -7.766  10.246  1.00  8.40   ? 243 ASN A CG  1 
ATOM   2079 O  OD1 . ASN A 1 243 ? -3.922  -8.610  10.806  1.00  10.46  ? 243 ASN A OD1 1 
ATOM   2080 N  ND2 . ASN A 1 243 ? -3.875  -6.943  9.361   1.00  11.42  ? 243 ASN A ND2 1 
ATOM   2081 N  N   . TRP A 1 244 ? -1.548  -8.674  13.997  1.00  8.32   ? 244 TRP A N   1 
ATOM   2082 C  CA  . TRP A 1 244 ? -2.015  -8.403  15.373  1.00  7.73   ? 244 TRP A CA  1 
ATOM   2083 C  C   . TRP A 1 244 ? -0.793  -8.270  16.282  1.00  7.72   ? 244 TRP A C   1 
ATOM   2084 O  O   . TRP A 1 244 ? 0.183   -9.008  16.182  1.00  9.60   ? 244 TRP A O   1 
ATOM   2085 C  CB  . TRP A 1 244 ? -2.952  -9.493  15.867  1.00  8.36   ? 244 TRP A CB  1 
ATOM   2086 C  CG  . TRP A 1 244 ? -2.463  -10.901 15.730  1.00  7.85   ? 244 TRP A CG  1 
ATOM   2087 C  CD1 . TRP A 1 244 ? -2.565  -11.648 14.602  1.00  8.44   ? 244 TRP A CD1 1 
ATOM   2088 C  CD2 . TRP A 1 244 ? -1.895  -11.744 16.714  1.00  8.11   ? 244 TRP A CD2 1 
ATOM   2089 N  NE1 . TRP A 1 244 ? -2.054  -12.933 14.798  1.00  8.90   ? 244 TRP A NE1 1 
ATOM   2090 C  CE2 . TRP A 1 244 ? -1.635  -12.988 16.109  1.00  8.52   ? 244 TRP A CE2 1 
ATOM   2091 C  CE3 . TRP A 1 244 ? -1.576  -11.563 18.083  1.00  9.49   ? 244 TRP A CE3 1 
ATOM   2092 C  CZ2 . TRP A 1 244 ? -1.078  -14.039 16.809  1.00  10.08  ? 244 TRP A CZ2 1 
ATOM   2093 C  CZ3 . TRP A 1 244 ? -1.058  -12.621 18.762  1.00  10.01  ? 244 TRP A CZ3 1 
ATOM   2094 C  CH2 . TRP A 1 244 ? -0.834  -13.861 18.123  1.00  10.52  ? 244 TRP A CH2 1 
ATOM   2095 N  N   . ARG A 1 245 ? -0.950  -7.373  17.235  1.00  8.24   ? 245 ARG A N   1 
ATOM   2096 C  CA  . ARG A 1 245 ? 0.003   -7.230  18.359  1.00  7.99   ? 245 ARG A CA  1 
ATOM   2097 C  C   . ARG A 1 245 ? -0.479  -8.124  19.493  1.00  7.63   ? 245 ARG A C   1 
ATOM   2098 O  O   . ARG A 1 245 ? -1.652  -8.122  19.807  1.00  8.54   ? 245 ARG A O   1 
ATOM   2099 C  CB  . ARG A 1 245 ? 0.041   -5.812  18.832  1.00  8.86   ? 245 ARG A CB  1 
ATOM   2100 C  CG  . ARG A 1 245 ? 1.134   -5.521  19.847  1.00  8.37   ? 245 ARG A CG  1 
ATOM   2101 C  CD  . ARG A 1 245 ? 1.065   -4.143  20.454  1.00  8.99   ? 245 ARG A CD  1 
ATOM   2102 N  NE  . ARG A 1 245 ? 2.311   -3.856  21.159  1.00  9.19   ? 245 ARG A NE  1 
ATOM   2103 C  CZ  . ARG A 1 245 ? 2.508   -2.850  22.011  1.00  8.63   ? 245 ARG A CZ  1 
ATOM   2104 N  NH1 . ARG A 1 245 ? 1.513   -2.086  22.371  1.00  9.89   ? 245 ARG A NH1 1 
ATOM   2105 N  NH2 . ARG A 1 245 ? 3.750   -2.594  22.436  1.00  10.35  ? 245 ARG A NH2 1 
ATOM   2106 N  N   A PRO A 1 246 ? 0.383   -8.929  20.108  0.50  7.88   ? 246 PRO A N   1 
ATOM   2107 N  N   B PRO A 1 246 ? 0.441   -8.881  20.130  0.50  8.54   ? 246 PRO A N   1 
ATOM   2108 C  CA  A PRO A 1 246 ? -0.150  -9.738  21.200  0.50  8.69   ? 246 PRO A CA  1 
ATOM   2109 C  CA  B PRO A 1 246 ? 0.087   -9.728  21.268  0.50  8.87   ? 246 PRO A CA  1 
ATOM   2110 C  C   A PRO A 1 246 ? -0.422  -8.904  22.472  0.50  8.39   ? 246 PRO A C   1 
ATOM   2111 C  C   B PRO A 1 246 ? -0.303  -8.909  22.499  0.50  8.68   ? 246 PRO A C   1 
ATOM   2112 O  O   A PRO A 1 246 ? -0.115  -7.716  22.601  0.50  8.57   ? 246 PRO A O   1 
ATOM   2113 O  O   B PRO A 1 246 ? 0.079   -7.723  22.620  0.50  8.90   ? 246 PRO A O   1 
ATOM   2114 C  CB  A PRO A 1 246 ? 0.986   -10.771 21.448  0.50  10.07  ? 246 PRO A CB  1 
ATOM   2115 C  CB  B PRO A 1 246 ? 1.405   -10.471 21.569  0.50  8.62   ? 246 PRO A CB  1 
ATOM   2116 C  CG  A PRO A 1 246 ? 1.957   -10.593 20.324  0.50  10.14  ? 246 PRO A CG  1 
ATOM   2117 C  CG  B PRO A 1 246 ? 2.442   -9.718  21.020  0.50  12.74  ? 246 PRO A CG  1 
ATOM   2118 C  CD  A PRO A 1 246 ? 1.792   -9.240  19.785  0.50  9.24   ? 246 PRO A CD  1 
ATOM   2119 C  CD  B PRO A 1 246 ? 1.905   -8.915  19.865  0.50  10.01  ? 246 PRO A CD  1 
ATOM   2120 N  N   . ALA A 1 247 ? -1.005  -9.567  23.443  1.00  9.20   ? 247 ALA A N   1 
ATOM   2121 C  CA  . ALA A 1 247 ? -1.343  -8.938  24.718  1.00  9.10   ? 247 ALA A CA  1 
ATOM   2122 C  C   . ALA A 1 247 ? -0.135  -8.421  25.452  1.00  9.43   ? 247 ALA A C   1 
ATOM   2123 O  O   . ALA A 1 247 ? 0.919   -9.081  25.491  1.00  10.37  ? 247 ALA A O   1 
ATOM   2124 C  CB  . ALA A 1 247 ? -2.151  -9.932  25.562  1.00  11.93  ? 247 ALA A CB  1 
ATOM   2125 N  N   . GLN A 1 248 ? -0.293  -7.237  26.021  1.00  9.07   ? 248 GLN A N   1 
ATOM   2126 C  CA  . GLN A 1 248 ? 0.763   -6.523  26.754  1.00  9.22   ? 248 GLN A CA  1 
ATOM   2127 C  C   . GLN A 1 248 ? 0.471   -6.544  28.231  1.00  9.58   ? 248 GLN A C   1 
ATOM   2128 O  O   . GLN A 1 248 ? -0.650  -6.738  28.664  1.00  9.96   ? 248 GLN A O   1 
ATOM   2129 C  CB  . GLN A 1 248 ? 0.816   -5.100  26.223  1.00  10.28  ? 248 GLN A CB  1 
ATOM   2130 C  CG  . GLN A 1 248 ? 1.135   -5.015  24.735  1.00  10.14  ? 248 GLN A CG  1 
ATOM   2131 C  CD  . GLN A 1 248 ? 2.440   -5.659  24.411  1.00  11.01  ? 248 GLN A CD  1 
ATOM   2132 O  OE1 . GLN A 1 248 ? 3.475   -5.312  24.969  1.00  13.37  ? 248 GLN A OE1 1 
ATOM   2133 N  NE2 . GLN A 1 248 ? 2.444   -6.591  23.460  1.00  11.68  ? 248 GLN A NE2 1 
ATOM   2134 N  N   . PRO A 1 249 ? 1.481   -6.192  29.085  1.00  11.41  ? 249 PRO A N   1 
ATOM   2135 C  CA  . PRO A 1 249 ? 1.270   -6.266  30.518  1.00  11.88  ? 249 PRO A CA  1 
ATOM   2136 C  C   . PRO A 1 249 ? 0.173   -5.272  30.965  1.00  10.71  ? 249 PRO A C   1 
ATOM   2137 O  O   . PRO A 1 249 ? 0.210   -4.077  30.608  1.00  11.31  ? 249 PRO A O   1 
ATOM   2138 C  CB  . PRO A 1 249 ? 2.637   -5.866  31.093  1.00  15.24  ? 249 PRO A CB  1 
ATOM   2139 C  CG  . PRO A 1 249 ? 3.588   -6.305  30.026  1.00  15.83  ? 249 PRO A CG  1 
ATOM   2140 C  CD  . PRO A 1 249 ? 2.895   -5.929  28.772  1.00  12.60  ? 249 PRO A CD  1 
ATOM   2141 N  N   . LEU A 1 250 ? -0.690  -5.746  31.838  1.00  11.69  ? 250 LEU A N   1 
ATOM   2142 C  CA  . LEU A 1 250 ? -1.775  -4.895  32.349  1.00  11.74  ? 250 LEU A CA  1 
ATOM   2143 C  C   . LEU A 1 250 ? -1.262  -3.802  33.280  1.00  10.99  ? 250 LEU A C   1 
ATOM   2144 O  O   . LEU A 1 250 ? -1.831  -2.709  33.345  1.00  11.63  ? 250 LEU A O   1 
ATOM   2145 C  CB  . LEU A 1 250 ? -2.775  -5.745  33.049  1.00  12.53  ? 250 LEU A CB  1 
ATOM   2146 C  CG  . LEU A 1 250 ? -4.112  -5.038  33.425  1.00  13.46  ? 250 LEU A CG  1 
ATOM   2147 C  CD1 . LEU A 1 250 ? -4.840  -4.424  32.228  1.00  13.39  ? 250 LEU A CD1 1 
ATOM   2148 C  CD2 . LEU A 1 250 ? -5.026  -5.996  34.221  1.00  18.74  ? 250 LEU A CD2 1 
ATOM   2149 N  N   . LYS A 1 251 ? -0.193  -4.080  34.024  1.00  11.75  ? 251 LYS A N   1 
ATOM   2150 C  CA  . LYS A 1 251 ? 0.388   -3.095  34.916  1.00  12.67  ? 251 LYS A CA  1 
ATOM   2151 C  C   . LYS A 1 251 ? -0.657  -2.550  35.875  1.00  15.99  ? 251 LYS A C   1 
ATOM   2152 O  O   . LYS A 1 251 ? -1.501  -3.322  36.353  1.00  17.97  ? 251 LYS A O   1 
ATOM   2153 C  CB  . LYS A 1 251 ? 1.162   -2.009  34.151  1.00  15.39  ? 251 LYS A CB  1 
ATOM   2154 C  CG  . LYS A 1 251 ? 2.375   -2.670  33.465  1.00  21.55  ? 251 LYS A CG  1 
ATOM   2155 C  CD  . LYS A 1 251 ? 3.267   -1.728  32.713  1.00  21.47  ? 251 LYS A CD  1 
ATOM   2156 C  CE  . LYS A 1 251 ? 4.526   -2.455  32.341  1.00  24.96  ? 251 LYS A CE  1 
ATOM   2157 N  NZ  . LYS A 1 251 ? 5.361   -1.659  31.371  1.00  28.13  ? 251 LYS A NZ  1 
ATOM   2158 N  N   . ASN A 1 252 ? -0.635  -1.250  36.118  1.00  15.03  ? 252 ASN A N   1 
ATOM   2159 C  CA  . ASN A 1 252 ? -1.502  -0.731  37.165  1.00  18.32  ? 252 ASN A CA  1 
ATOM   2160 C  C   . ASN A 1 252 ? -2.814  -0.321  36.563  1.00  19.35  ? 252 ASN A C   1 
ATOM   2161 O  O   . ASN A 1 252 ? -2.995  0.993   36.497  1.00  22.30  ? 252 ASN A O   1 
ATOM   2162 C  CB  . ASN A 1 252 ? -0.827  0.455   37.873  1.00  26.29  ? 252 ASN A CB  1 
ATOM   2163 C  CG  . ASN A 1 252 ? -1.577  0.875   39.140  1.00  31.77  ? 252 ASN A CG  1 
ATOM   2164 O  OD1 . ASN A 1 252 ? -2.055  0.008   39.913  1.00  34.60  ? 252 ASN A OD1 1 
ATOM   2165 N  ND2 . ASN A 1 252 ? -1.764  2.194   39.335  1.00  36.24  ? 252 ASN A ND2 1 
ATOM   2166 N  N   . ARG A 1 253 ? -3.613  -1.313  35.955  1.00  15.64  ? 253 ARG A N   1 
ATOM   2167 C  CA  . ARG A 1 253 ? -4.864  -0.973  35.371  1.00  11.62  ? 253 ARG A CA  1 
ATOM   2168 C  C   . ARG A 1 253 ? -5.927  -1.881  35.802  1.00  11.51  ? 253 ARG A C   1 
ATOM   2169 O  O   . ARG A 1 253 ? -5.725  -3.018  36.129  1.00  17.55  ? 253 ARG A O   1 
ATOM   2170 C  CB  . ARG A 1 253 ? -4.789  -0.964  33.845  1.00  11.33  ? 253 ARG A CB  1 
ATOM   2171 C  CG  . ARG A 1 253 ? -3.828  0.173   33.355  1.00  11.07  ? 253 ARG A CG  1 
ATOM   2172 C  CD  . ARG A 1 253 ? -3.719  0.187   31.862  1.00  10.44  ? 253 ARG A CD  1 
ATOM   2173 N  NE  . ARG A 1 253 ? -2.878  -0.954  31.399  1.00  9.45   ? 253 ARG A NE  1 
ATOM   2174 C  CZ  . ARG A 1 253 ? -2.658  -1.256  30.125  1.00  8.34   ? 253 ARG A CZ  1 
ATOM   2175 N  NH1 . ARG A 1 253 ? -3.262  -0.549  29.154  1.00  8.98   ? 253 ARG A NH1 1 
ATOM   2176 N  NH2 . ARG A 1 253 ? -1.825  -2.222  29.809  1.00  8.70   ? 253 ARG A NH2 1 
ATOM   2177 N  N   . GLN A 1 254 ? -7.151  -1.341  35.797  1.00  12.80  ? 254 GLN A N   1 
ATOM   2178 C  CA  . GLN A 1 254 ? -8.340  -2.122  36.067  1.00  13.56  ? 254 GLN A CA  1 
ATOM   2179 C  C   . GLN A 1 254 ? -9.178  -2.163  34.809  1.00  12.64  ? 254 GLN A C   1 
ATOM   2180 O  O   . GLN A 1 254 ? -9.380  -1.147  34.110  1.00  14.91  ? 254 GLN A O   1 
ATOM   2181 C  CB  . GLN A 1 254 ? -9.105  -1.435  37.170  1.00  20.36  ? 254 GLN A CB  1 
ATOM   2182 C  CG  . GLN A 1 254 ? -8.423  -1.634  38.538  1.00  29.15  ? 254 GLN A CG  1 
ATOM   2183 C  CD  . GLN A 1 254 ? -9.278  -2.507  39.397  1.00  54.40  ? 254 GLN A CD  1 
ATOM   2184 O  OE1 . GLN A 1 254 ? -10.084 -3.301  38.885  1.00  77.09  ? 254 GLN A OE1 1 
ATOM   2185 N  NE2 . GLN A 1 254 ? -9.119  -2.389  40.711  1.00  57.33  ? 254 GLN A NE2 1 
ATOM   2186 N  N   . ILE A 1 255 ? -9.658  -3.337  34.499  1.00  10.30  ? 255 ILE A N   1 
ATOM   2187 C  CA  . ILE A 1 255 ? -10.633 -3.533  33.430  1.00  9.64   ? 255 ILE A CA  1 
ATOM   2188 C  C   . ILE A 1 255 ? -12.018 -3.574  34.057  1.00  9.95   ? 255 ILE A C   1 
ATOM   2189 O  O   . ILE A 1 255 ? -12.201 -4.328  35.042  1.00  12.32  ? 255 ILE A O   1 
ATOM   2190 C  CB  . ILE A 1 255 ? -10.367 -4.749  32.616  1.00  10.20  ? 255 ILE A CB  1 
ATOM   2191 C  CG1 . ILE A 1 255 ? -8.912  -4.779  32.128  1.00  10.66  ? 255 ILE A CG1 1 
ATOM   2192 C  CG2 . ILE A 1 255 ? -11.377 -4.885  31.507  1.00  12.08  ? 255 ILE A CG2 1 
ATOM   2193 C  CD1 . ILE A 1 255 ? -8.536  -5.966  31.311  1.00  12.40  ? 255 ILE A CD1 1 
ATOM   2194 N  N   . LYS A 1 256 ? -12.916 -2.712  33.627  1.00  9.23   ? 256 LYS A N   1 
ATOM   2195 C  CA  . LYS A 1 256 ? -14.263 -2.624  34.178  1.00  9.94   ? 256 LYS A CA  1 
ATOM   2196 C  C   . LYS A 1 256 ? -15.257 -3.246  33.214  1.00  9.97   ? 256 LYS A C   1 
ATOM   2197 O  O   . LYS A 1 256 ? -15.082 -3.108  32.000  1.00  11.68  ? 256 LYS A O   1 
ATOM   2198 C  CB  . LYS A 1 256 ? -14.617 -1.137  34.385  1.00  12.17  ? 256 LYS A CB  1 
ATOM   2199 C  CG  . LYS A 1 256 ? -13.685 -0.521  35.415  1.00  15.17  ? 256 LYS A CG  1 
ATOM   2200 C  CD  . LYS A 1 256 ? -13.874 0.893   35.704  1.00  23.61  ? 256 LYS A CD  1 
ATOM   2201 C  CE  . LYS A 1 256 ? -12.748 1.382   36.611  1.00  37.42  ? 256 LYS A CE  1 
ATOM   2202 N  NZ  . LYS A 1 256 ? -12.871 2.860   36.698  1.00  43.90  ? 256 LYS A NZ  1 
ATOM   2203 N  N   . ALA A 1 257 ? -16.252 -3.907  33.748  1.00  10.77  ? 257 ALA A N   1 
ATOM   2204 C  CA  . ALA A 1 257 ? -17.328 -4.483  32.984  1.00  11.68  ? 257 ALA A CA  1 
ATOM   2205 C  C   . ALA A 1 257 ? -18.573 -3.647  33.084  1.00  10.98  ? 257 ALA A C   1 
ATOM   2206 O  O   . ALA A 1 257 ? -18.963 -3.205  34.192  1.00  12.70  ? 257 ALA A O   1 
ATOM   2207 C  CB  . ALA A 1 257 ? -17.582 -5.902  33.427  1.00  12.76  ? 257 ALA A CB  1 
ATOM   2208 N  N   . SER A 1 258 ? -19.295 -3.480  31.990  1.00  10.61  ? 258 SER A N   1 
ATOM   2209 C  CA  . SER A 1 258 ? -20.576 -2.736  31.994  1.00  12.08  ? 258 SER A CA  1 
ATOM   2210 C  C   . SER A 1 258 ? -21.730 -3.609  32.413  1.00  12.82  ? 258 SER A C   1 
ATOM   2211 O  O   . SER A 1 258 ? -22.848 -3.084  32.510  1.00  16.42  ? 258 SER A O   1 
ATOM   2212 C  CB  . SER A 1 258 ? -20.856 -2.183  30.598  1.00  12.30  ? 258 SER A CB  1 
ATOM   2213 O  OG  . SER A 1 258 ? -21.278 -3.251  29.711  1.00  11.45  ? 258 SER A OG  1 
ATOM   2214 N  N   . PHE A 1 259 ? -21.485 -4.883  32.657  1.00  13.01  ? 259 PHE A N   1 
ATOM   2215 C  CA  . PHE A 1 259 ? -22.617 -5.848  32.792  1.00  15.23  ? 259 PHE A CA  1 
ATOM   2216 C  C   . PHE A 1 259 ? -22.265 -6.751  33.936  1.00  20.16  ? 259 PHE A C   1 
ATOM   2217 O  O   . PHE A 1 259 ? -21.084 -6.904  34.331  1.00  20.82  ? 259 PHE A O   1 
ATOM   2218 C  CB  . PHE A 1 259 ? -22.718 -6.697  31.514  1.00  16.59  ? 259 PHE A CB  1 
ATOM   2219 C  CG  . PHE A 1 259 ? -21.431 -7.412  31.174  1.00  13.31  ? 259 PHE A CG  1 
ATOM   2220 C  CD1 . PHE A 1 259 ? -20.412 -6.762  30.431  1.00  13.67  ? 259 PHE A CD1 1 
ATOM   2221 C  CD2 . PHE A 1 259 ? -21.187 -8.679  31.700  1.00  18.77  ? 259 PHE A CD2 1 
ATOM   2222 C  CE1 . PHE A 1 259 ? -19.200 -7.437  30.189  1.00  16.12  ? 259 PHE A CE1 1 
ATOM   2223 C  CE2 . PHE A 1 259 ? -19.996 -9.309  31.494  1.00  21.81  ? 259 PHE A CE2 1 
ATOM   2224 C  CZ  . PHE A 1 259 ? -19.018 -8.715  30.687  1.00  19.64  ? 259 PHE A CZ  1 
ATOM   2225 N  N   . LYS A 1 260 ? -23.363 -7.284  34.494  1.00  25.17  ? 260 LYS A N   1 
ATOM   2226 C  CA  . LYS A 1 260 ? -23.548 -8.401  35.416  1.00  33.29  ? 260 LYS A CA  1 
ATOM   2227 C  C   . LYS A 1 260 ? -23.653 -8.191  36.915  1.00  41.36  ? 260 LYS A C   1 
ATOM   2228 O  O   . LYS A 1 260 ? -22.704 -8.458  37.663  1.00  68.20  ? 260 LYS A O   1 
ATOM   2229 C  CB  . LYS A 1 260 ? -22.744 -9.629  35.039  1.00  37.38  ? 260 LYS A CB  1 
ATOM   2230 C  CG  . LYS A 1 260 ? -23.375 -10.406 33.873  1.00  44.75  ? 260 LYS A CG  1 
ATOM   2231 C  CD  . LYS A 1 260 ? -22.361 -11.381 33.245  1.00  47.76  ? 260 LYS A CD  1 
ATOM   2232 C  CE  . LYS A 1 260 ? -21.576 -12.125 34.349  1.00  85.34  ? 260 LYS A CE  1 
ATOM   2233 N  NZ  . LYS A 1 260 ? -20.069 -12.047 34.275  1.00  85.43  ? 260 LYS A NZ  1 
ATOM   2234 O  OXT . LYS A 1 260 ? -24.685 -7.745  37.429  1.00  55.52  ? 260 LYS A OXT 1 
HETATM 2235 ZN ZN  . ZN  B 2 .   ? -6.445  -1.816  15.359  1.00  7.70   ? 301 ZN  A ZN  1 
HETATM 2236 S  S   . DMS C 3 .   ? 1.484   -11.737 15.099  1.00  19.57  ? 302 DMS A S   1 
HETATM 2237 O  O   . DMS C 3 .   ? 2.056   -13.067 14.660  1.00  27.69  ? 302 DMS A O   1 
HETATM 2238 C  C1  . DMS C 3 .   ? 1.851   -11.542 16.710  1.00  17.02  ? 302 DMS A C1  1 
HETATM 2239 C  C2  . DMS C 3 .   ? 2.642   -10.537 14.751  1.00  21.07  ? 302 DMS A C2  1 
HETATM 2240 N  N1  . BCN D 4 .   ? -20.562 -14.778 23.537  1.00  38.41  ? 303 BCN A N1  1 
HETATM 2241 C  C1  . BCN D 4 .   ? -19.829 -15.593 22.473  1.00  22.21  ? 303 BCN A C1  1 
HETATM 2242 C  C2  . BCN D 4 .   ? -20.587 -16.408 21.489  1.00  52.70  ? 303 BCN A C2  1 
HETATM 2243 O  O21 . BCN D 4 .   ? -21.734 -16.900 21.722  1.00  95.96  ? 303 BCN A O21 1 
HETATM 2244 O  O22 . BCN D 4 .   ? -19.921 -16.551 20.452  1.00  51.06  ? 303 BCN A O22 1 
HETATM 2245 C  C3  . BCN D 4 .   ? -19.609 -14.076 24.453  1.00  29.25  ? 303 BCN A C3  1 
HETATM 2246 C  C4  . BCN D 4 .   ? -20.053 -14.749 25.745  1.00  37.29  ? 303 BCN A C4  1 
HETATM 2247 O  O4  . BCN D 4 .   ? -18.936 -15.220 26.438  1.00  49.34  ? 303 BCN A O4  1 
HETATM 2248 C  C5  . BCN D 4 .   ? -21.575 -13.812 23.092  1.00  27.63  ? 303 BCN A C5  1 
HETATM 2249 C  C6  . BCN D 4 .   ? -22.701 -13.374 24.062  1.00  43.92  ? 303 BCN A C6  1 
HETATM 2250 O  O6  . BCN D 4 .   ? -22.281 -12.425 25.078  1.00  32.51  ? 303 BCN A O6  1 
HETATM 2251 F  F18 . V90 E 5 .   ? -4.764  2.641   11.368  1.00  27.60  ? 304 V90 A F18 1 
HETATM 2252 C  C5  . V90 E 5 .   ? -4.527  1.717   12.300  1.00  22.25  ? 304 V90 A C5  1 
HETATM 2253 C  C6  . V90 E 5 .   ? -3.758  0.594   11.822  1.00  24.94  ? 304 V90 A C6  1 
HETATM 2254 S  S12 . V90 E 5 .   ? -3.140  0.341   10.189  1.00  27.30  ? 304 V90 A S12 1 
HETATM 2255 C  C13 . V90 E 5 .   ? -1.529  1.131   10.131  1.00  26.84  ? 304 V90 A C13 1 
HETATM 2256 C  C14 . V90 E 5 .   ? -1.293  2.152   11.188  1.00  32.40  ? 304 V90 A C14 1 
HETATM 2257 O  O15 . V90 E 5 .   ? -1.020  3.323   10.508  1.00  57.06  ? 304 V90 A O15 1 
HETATM 2258 C  C1  . V90 E 5 .   ? -3.423  -0.352  12.754  1.00  26.10  ? 304 V90 A C1  1 
HETATM 2259 F  F17 . V90 E 5 .   ? -2.665  -1.431  12.434  1.00  26.01  ? 304 V90 A F17 1 
HETATM 2260 C  C4  . V90 E 5 .   ? -4.934  1.925   13.537  1.00  19.16  ? 304 V90 A C4  1 
HETATM 2261 C  C3  . V90 E 5 .   ? -4.561  0.927   14.445  1.00  21.37  ? 304 V90 A C3  1 
HETATM 2262 S  S8  . V90 E 5 .   ? -5.159  0.873   16.175  1.00  19.55  ? 304 V90 A S8  1 
HETATM 2263 O  O10 . V90 E 5 .   ? -6.385  1.725   16.242  1.00  22.42  ? 304 V90 A O10 1 
HETATM 2264 N  N11 . V90 E 5 .   ? -5.275  -0.685  16.330  1.00  16.54  ? 304 V90 A N11 1 
HETATM 2265 O  O9  . V90 E 5 .   ? -4.183  1.378   17.097  1.00  16.54  ? 304 V90 A O9  1 
HETATM 2266 C  C2  . V90 E 5 .   ? -3.758  -0.113  13.984  1.00  18.16  ? 304 V90 A C2  1 
HETATM 2267 F  F16 . V90 E 5 .   ? -3.522  -1.137  15.023  1.00  25.29  ? 304 V90 A F16 1 
HETATM 2268 N  N7  . V90 E 5 .   ? -5.630  3.042   13.901  1.00  21.54  ? 304 V90 A N7  1 
HETATM 2269 C  C19 . V90 E 5 .   ? -4.996  4.308   14.449  1.00  33.05  ? 304 V90 A C19 1 
HETATM 2270 C  C26 . V90 E 5 .   ? -3.443  4.368   14.561  1.00  27.79  ? 304 V90 A C26 1 
HETATM 2271 C  C25 . V90 E 5 .   ? -2.565  5.166   13.636  1.00  32.66  ? 304 V90 A C25 1 
HETATM 2272 C  C24 . V90 E 5 .   ? -2.497  6.678   13.886  1.00  32.13  ? 304 V90 A C24 1 
HETATM 2273 C  C23 . V90 E 5 .   ? -3.440  7.474   12.980  1.00  37.97  ? 304 V90 A C23 1 
HETATM 2274 C  C22 . V90 E 5 .   ? -4.841  7.748   13.558  1.00  31.02  ? 304 V90 A C22 1 
HETATM 2275 C  C21 . V90 E 5 .   ? -5.375  6.911   14.718  1.00  29.40  ? 304 V90 A C21 1 
HETATM 2276 C  C20 . V90 E 5 .   ? -5.793  5.559   14.208  1.00  25.07  ? 304 V90 A C20 1 
HETATM 2277 O  O   . HOH F 6 .   ? -16.884 -8.435  20.429  1.00  9.16   ? 401 HOH A O   1 
HETATM 2278 O  O   . HOH F 6 .   ? 3.668   4.979   29.986  1.00  17.10  ? 402 HOH A O   1 
HETATM 2279 O  O   . HOH F 6 .   ? -1.177  -4.113  15.728  1.00  9.85   ? 403 HOH A O   1 
HETATM 2280 O  O   . HOH F 6 .   ? 4.993   -4.908  21.077  1.00  13.16  ? 404 HOH A O   1 
HETATM 2281 O  O   . HOH F 6 .   ? -1.969  -12.334 22.992  1.00  9.88   ? 405 HOH A O   1 
HETATM 2282 O  O   . HOH F 6 .   ? -4.371  -13.585 18.203  1.00  9.42   ? 406 HOH A O   1 
HETATM 2283 O  O   . HOH F 6 .   ? -3.371  -11.172 21.016  1.00  9.74   ? 407 HOH A O   1 
HETATM 2284 O  O   . HOH F 6 .   ? -6.496  -20.295 19.819  1.00  12.58  ? 408 HOH A O   1 
HETATM 2285 O  O   . HOH F 6 .   ? -2.444  -8.745  29.215  1.00  10.80  ? 409 HOH A O   1 
HETATM 2286 O  O   . HOH F 6 .   ? -7.816  -15.631 11.611  1.00  10.44  ? 410 HOH A O   1 
HETATM 2287 O  O   . HOH F 6 .   ? -3.288  -13.251 25.310  1.00  11.25  ? 411 HOH A O   1 
HETATM 2288 O  O   . HOH F 6 .   ? -10.515 8.649   25.529  1.00  10.49  ? 412 HOH A O   1 
HETATM 2289 O  O   . HOH F 6 .   ? -3.641  -15.902 24.575  1.00  13.08  ? 413 HOH A O   1 
HETATM 2290 O  O   . HOH F 6 .   ? -8.069  -19.369 21.854  1.00  15.38  ? 414 HOH A O   1 
HETATM 2291 O  O   . HOH F 6 .   ? 7.596   6.065   21.875  1.00  16.20  ? 415 HOH A O   1 
HETATM 2292 O  O   . HOH F 6 .   ? -15.950 -12.332 24.507  1.00  13.94  ? 416 HOH A O   1 
HETATM 2293 O  O   . HOH F 6 .   ? -21.442 -7.214  23.643  1.00  12.65  ? 417 HOH A O   1 
HETATM 2294 O  O   . HOH F 6 .   ? -17.725 10.315  11.251  1.00  23.29  ? 418 HOH A O   1 
HETATM 2295 O  O   . HOH F 6 .   ? -9.488  -8.029  34.197  1.00  20.72  ? 419 HOH A O   1 
HETATM 2296 O  O   . HOH F 6 .   ? -22.702 -11.627 14.062  1.00  20.99  ? 420 HOH A O   1 
HETATM 2297 O  O   . HOH F 6 .   ? 8.653   -3.800  21.177  1.00  14.40  ? 421 HOH A O   1 
HETATM 2298 O  O   . HOH F 6 .   ? -4.942  15.737  12.336  1.00  25.97  ? 422 HOH A O   1 
HETATM 2299 O  O   . HOH F 6 .   ? -12.939 -16.900 26.770  1.00  12.98  ? 423 HOH A O   1 
HETATM 2300 O  O   . HOH F 6 .   ? -21.719 5.757   4.799   1.00  24.08  ? 424 HOH A O   1 
HETATM 2301 O  O   . HOH F 6 .   ? -12.772 -17.265 17.054  1.00  12.76  ? 425 HOH A O   1 
HETATM 2302 O  O   . HOH F 6 .   ? -11.950 2.633   31.135  1.00  14.36  ? 426 HOH A O   1 
HETATM 2303 O  O   . HOH F 6 .   ? 1.315   -1.576  29.543  1.00  13.92  ? 427 HOH A O   1 
HETATM 2304 O  O   . HOH F 6 .   ? -10.350 -18.350 17.437  1.00  13.18  ? 428 HOH A O   1 
HETATM 2305 O  O   . HOH F 6 .   ? -13.629 10.349  27.934  1.00  15.88  ? 429 HOH A O   1 
HETATM 2306 O  O   . HOH F 6 .   ? -0.458  10.599  23.708  1.00  20.97  ? 430 HOH A O   1 
HETATM 2307 O  O   . HOH F 6 .   ? -19.083 10.018  8.906   1.00  18.60  ? 431 HOH A O   1 
HETATM 2308 O  O   . HOH F 6 .   ? -12.724 -19.585 26.336  1.00  19.60  ? 432 HOH A O   1 
HETATM 2309 O  O   . HOH F 6 .   ? -23.680 -0.789  3.993   1.00  25.41  ? 433 HOH A O   1 
HETATM 2310 O  O   . HOH F 6 .   ? -1.006  9.164   28.079  1.00  18.23  ? 434 HOH A O   1 
HETATM 2311 O  O   . HOH F 6 .   ? -6.940  16.610  10.786  1.00  21.31  ? 435 HOH A O   1 
HETATM 2312 O  O   . HOH F 6 .   ? -13.126 20.062  15.138  1.00  15.94  ? 436 HOH A O   1 
HETATM 2313 O  O   . HOH F 6 .   ? -0.150  -14.330 22.355  1.00  18.69  ? 437 HOH A O   1 
HETATM 2314 O  O   . HOH F 6 .   ? -6.066  -4.843  -6.308  1.00  25.95  ? 438 HOH A O   1 
HETATM 2315 O  O   . HOH F 6 .   ? -25.465 9.592   13.441  1.00  32.71  ? 439 HOH A O   1 
HETATM 2316 O  O   . HOH F 6 .   ? 2.111   -14.046 20.603  1.00  27.11  ? 440 HOH A O   1 
HETATM 2317 O  O   . HOH F 6 .   ? -26.060 2.795   20.963  1.00  20.78  ? 441 HOH A O   1 
HETATM 2318 O  O   . HOH F 6 .   ? 1.922   -15.825 9.349   1.00  20.54  ? 442 HOH A O   1 
HETATM 2319 O  O   . HOH F 6 .   ? -1.151  -11.123 29.152  1.00  17.04  ? 443 HOH A O   1 
HETATM 2320 O  O   . HOH F 6 .   ? -17.732 -20.577 8.111   1.00  18.85  ? 444 HOH A O   1 
HETATM 2321 O  O   . HOH F 6 .   ? 4.289   -3.419  26.664  1.00  18.72  ? 445 HOH A O   1 
HETATM 2322 O  O   . HOH F 6 .   ? 1.314   -11.774 25.244  1.00  22.46  ? 446 HOH A O   1 
HETATM 2323 O  O   . HOH F 6 .   ? -9.074  -5.729  36.049  1.00  17.43  ? 447 HOH A O   1 
HETATM 2324 O  O   . HOH F 6 .   ? -9.036  5.858   29.002  1.00  16.23  ? 448 HOH A O   1 
HETATM 2325 O  O   . HOH F 6 .   ? -27.886 5.674   19.429  1.00  31.05  ? 449 HOH A O   1 
HETATM 2326 O  O   . HOH F 6 .   ? -1.199  -12.984 27.114  1.00  21.08  ? 450 HOH A O   1 
HETATM 2327 O  O   . HOH F 6 .   ? 13.477  0.266   24.574  1.00  22.09  ? 451 HOH A O   1 
HETATM 2328 O  O   . HOH F 6 .   ? -16.198 -9.991  33.028  1.00  18.95  ? 452 HOH A O   1 
HETATM 2329 O  O   . HOH F 6 .   ? 5.197   7.065   20.616  1.00  16.44  ? 453 HOH A O   1 
HETATM 2330 O  O   . HOH F 6 .   ? 3.672   8.739   22.291  1.00  22.42  ? 454 HOH A O   1 
HETATM 2331 O  O   . HOH F 6 .   ? 1.516   8.651   24.080  1.00  13.61  ? 455 HOH A O   1 
HETATM 2332 O  O   . HOH F 6 .   ? -9.094  -10.215 -1.085  1.00  20.28  ? 456 HOH A O   1 
HETATM 2333 O  O   . HOH F 6 .   ? -1.286  11.388  26.217  1.00  25.27  ? 457 HOH A O   1 
HETATM 2334 O  O   . HOH F 6 .   ? -20.834 7.761   1.851   1.00  21.91  ? 458 HOH A O   1 
HETATM 2335 O  O   . HOH F 6 .   ? -17.418 19.868  17.499  1.00  26.51  ? 459 HOH A O   1 
HETATM 2336 O  O   . HOH F 6 .   ? -9.106  15.292  12.296  1.00  22.47  ? 460 HOH A O   1 
HETATM 2337 O  O   . HOH F 6 .   ? -19.871 -4.365  41.319  1.00  28.73  ? 461 HOH A O   1 
HETATM 2338 O  O   . HOH F 6 .   ? -4.182  -8.473  31.289  1.00  17.40  ? 462 HOH A O   1 
HETATM 2339 O  O   . HOH F 6 .   ? -14.963 2.627   38.651  1.00  21.86  ? 463 HOH A O   1 
HETATM 2340 O  O   . HOH F 6 .   ? -6.911  -14.835 31.735  1.00  20.19  ? 464 HOH A O   1 
HETATM 2341 O  O   . HOH F 6 .   ? -24.706 -7.681  9.221   1.00  21.38  ? 465 HOH A O   1 
HETATM 2342 O  O   . HOH F 6 .   ? 1.610   -6.254  34.550  1.00  21.53  ? 466 HOH A O   1 
HETATM 2343 O  O   . HOH F 6 .   ? 4.530   -2.600  29.193  1.00  22.90  ? 467 HOH A O   1 
HETATM 2344 O  O   . HOH F 6 .   ? -14.528 -18.661 18.800  1.00  14.84  ? 468 HOH A O   1 
HETATM 2345 O  O   . HOH F 6 .   ? -7.332  -8.662  32.716  1.00  15.67  ? 469 HOH A O   1 
HETATM 2346 O  O   . HOH F 6 .   ? -10.666 17.645  12.420  1.00  19.34  ? 470 HOH A O   1 
HETATM 2347 O  O   . HOH F 6 .   ? -23.073 -3.022  6.860   1.00  25.80  ? 471 HOH A O   1 
HETATM 2348 O  O   . HOH F 6 .   ? -16.725 -14.002 26.436  1.00  19.01  ? 472 HOH A O   1 
HETATM 2349 O  O   . HOH F 6 .   ? -7.965  -19.236 30.832  1.00  27.84  ? 473 HOH A O   1 
HETATM 2350 O  O   . HOH F 6 .   ? -22.087 3.917   -3.108  1.00  21.16  ? 474 HOH A O   1 
HETATM 2351 O  O   . HOH F 6 .   ? -11.098 -19.693 7.774   1.00  31.29  ? 475 HOH A O   1 
HETATM 2352 O  O   . HOH F 6 .   ? -12.694 13.205  32.029  1.00  28.01  ? 476 HOH A O   1 
HETATM 2353 O  O   . HOH F 6 .   ? -9.894  15.696  29.789  1.00  28.61  ? 477 HOH A O   1 
HETATM 2354 O  O   . HOH F 6 .   ? -15.864 15.875  23.696  1.00  17.60  ? 478 HOH A O   1 
HETATM 2355 O  O   . HOH F 6 .   ? -2.496  -3.782  11.572  1.00  17.97  ? 479 HOH A O   1 
HETATM 2356 O  O   . HOH F 6 .   ? -13.266 -18.597 14.752  1.00  16.04  ? 480 HOH A O   1 
HETATM 2357 O  O   . HOH F 6 .   ? -22.749 -5.850  2.970   1.00  26.94  ? 481 HOH A O   1 
HETATM 2358 O  O   . HOH F 6 .   ? -11.020 1.187   33.542  1.00  16.95  ? 482 HOH A O   1 
HETATM 2359 O  O   . HOH F 6 .   ? -20.022 10.803  26.664  1.00  19.64  ? 483 HOH A O   1 
HETATM 2360 O  O   . HOH F 6 .   ? -1.543  -5.263  -6.926  1.00  32.53  ? 484 HOH A O   1 
HETATM 2361 O  O   . HOH F 6 .   ? 0.933   11.057  20.075  1.00  28.13  ? 485 HOH A O   1 
HETATM 2362 O  O   . HOH F 6 .   ? -6.982  1.543   35.261  1.00  18.45  ? 486 HOH A O   1 
HETATM 2363 O  O   . HOH F 6 .   ? -12.759 7.822   28.706  1.00  22.26  ? 487 HOH A O   1 
HETATM 2364 O  O   . HOH F 6 .   ? -4.574  -16.099 0.722   1.00  26.00  ? 488 HOH A O   1 
HETATM 2365 O  O   . HOH F 6 .   ? -8.679  -15.523 36.864  1.00  17.52  ? 489 HOH A O   1 
HETATM 2366 O  O   . HOH F 6 .   ? -13.653 14.203  27.299  1.00  24.24  ? 490 HOH A O   1 
HETATM 2367 O  O   . HOH F 6 .   ? -4.741  20.462  21.853  1.00  19.27  ? 491 HOH A O   1 
HETATM 2368 O  O   . HOH F 6 .   ? -1.796  -17.424 25.822  1.00  24.45  ? 492 HOH A O   1 
HETATM 2369 O  O   . HOH F 6 .   ? 4.421   -6.896  8.036   1.00  24.18  ? 493 HOH A O   1 
HETATM 2370 O  O   . HOH F 6 .   ? -20.252 13.896  28.742  1.00  41.39  ? 494 HOH A O   1 
HETATM 2371 O  O   . HOH F 6 .   ? -0.085  1.080   34.611  1.00  23.05  ? 495 HOH A O   1 
HETATM 2372 O  O   . HOH F 6 .   ? -10.443 -19.608 20.187  1.00  17.10  ? 496 HOH A O   1 
HETATM 2373 O  O   . HOH F 6 .   ? 5.139   -7.352  22.406  1.00  23.90  ? 497 HOH A O   1 
HETATM 2374 O  O   . HOH F 6 .   ? -26.601 -3.903  25.190  1.00  20.65  ? 498 HOH A O   1 
HETATM 2375 O  O   . HOH F 6 .   ? -3.617  -13.144 -2.762  1.00  22.38  ? 499 HOH A O   1 
HETATM 2376 O  O   . HOH F 6 .   ? 10.469  -9.193  8.813   1.00  36.25  ? 500 HOH A O   1 
HETATM 2377 O  O   . HOH F 6 .   ? -22.010 -18.511 13.628  1.00  24.27  ? 501 HOH A O   1 
HETATM 2378 O  O   . HOH F 6 .   ? -7.182  -8.863  -2.254  1.00  23.65  ? 502 HOH A O   1 
HETATM 2379 O  O   . HOH F 6 .   ? -4.952  3.282   -5.611  1.00  29.87  ? 503 HOH A O   1 
HETATM 2380 O  O   . HOH F 6 .   ? 2.803   0.990   -2.163  1.00  41.35  ? 504 HOH A O   1 
HETATM 2381 O  O   . HOH F 6 .   ? -3.326  18.029  21.891  1.00  17.81  ? 505 HOH A O   1 
HETATM 2382 O  O   . HOH F 6 .   ? -2.617  17.809  14.421  1.00  22.94  ? 506 HOH A O   1 
HETATM 2383 O  O   . HOH F 6 .   ? -7.195  -16.936 1.488   1.00  20.84  ? 507 HOH A O   1 
HETATM 2384 O  O   . HOH F 6 .   ? 5.228   -10.972 19.178  1.00  37.91  ? 508 HOH A O   1 
HETATM 2385 O  O   . HOH F 6 .   ? -5.195  2.214   37.550  1.00  23.81  ? 509 HOH A O   1 
HETATM 2386 O  O   . HOH F 6 .   ? -23.429 -0.184  32.010  1.00  27.73  ? 510 HOH A O   1 
HETATM 2387 O  O   . HOH F 6 .   ? -0.656  -8.576  32.683  1.00  22.58  ? 511 HOH A O   1 
HETATM 2388 O  O   . HOH F 6 .   ? 11.545  -7.279  22.444  1.00  28.30  ? 512 HOH A O   1 
HETATM 2389 O  O   . HOH F 6 .   ? 2.612   -13.442 5.240   1.00  25.41  ? 513 HOH A O   1 
HETATM 2390 O  O   . HOH F 6 .   ? -20.746 -7.232  -1.898  1.00  36.00  ? 514 HOH A O   1 
HETATM 2391 O  O   . HOH F 6 .   ? 2.561   9.537   26.481  1.00  27.96  ? 515 HOH A O   1 
HETATM 2392 O  O   . HOH F 6 .   ? -14.983 -21.866 13.112  1.00  21.91  ? 516 HOH A O   1 
HETATM 2393 O  O   . HOH F 6 .   ? -7.205  -17.366 32.552  1.00  32.75  ? 517 HOH A O   1 
HETATM 2394 O  O   . HOH F 6 .   ? -10.508 4.951   31.044  1.00  18.02  ? 518 HOH A O   1 
HETATM 2395 O  O   . HOH F 6 .   ? -16.227 -15.679 32.967  1.00  30.11  ? 519 HOH A O   1 
HETATM 2396 O  O   . HOH F 6 .   ? -13.746 3.717   33.240  1.00  22.74  ? 520 HOH A O   1 
HETATM 2397 O  O   . HOH F 6 .   ? -0.108  13.661  16.664  1.00  25.74  ? 521 HOH A O   1 
HETATM 2398 O  O   . HOH F 6 .   ? -12.789 -8.985  -3.193  1.00  25.43  ? 522 HOH A O   1 
HETATM 2399 O  O   . HOH F 6 .   ? -23.159 -13.338 11.348  1.00  19.76  ? 523 HOH A O   1 
HETATM 2400 O  O   . HOH F 6 .   ? 13.914  2.118   22.840  1.00  23.55  ? 524 HOH A O   1 
HETATM 2401 O  O   . HOH F 6 .   ? -11.114 -11.287 -2.697  1.00  29.73  ? 525 HOH A O   1 
HETATM 2402 O  O   . HOH F 6 .   ? -8.258  0.404   -6.401  1.00  30.98  ? 526 HOH A O   1 
HETATM 2403 O  O   . HOH F 6 .   ? 2.612   -11.573 9.510   1.00  22.70  ? 527 HOH A O   1 
HETATM 2404 O  O   . HOH F 6 .   ? 2.846   -4.583  7.752   1.00  22.07  ? 528 HOH A O   1 
HETATM 2405 O  O   . HOH F 6 .   ? 11.252  1.297   25.991  1.00  24.82  ? 529 HOH A O   1 
HETATM 2406 O  O   . HOH F 6 .   ? -23.902 8.695   20.251  1.00  23.35  ? 530 HOH A O   1 
HETATM 2407 O  O   . HOH F 6 .   ? 5.929   -12.899 -5.396  1.00  28.48  ? 531 HOH A O   1 
HETATM 2408 O  O   . HOH F 6 .   ? -25.362 -9.045  11.244  1.00  30.90  ? 532 HOH A O   1 
HETATM 2409 O  O   . HOH F 6 .   ? -21.078 -19.715 6.760   1.00  28.25  ? 533 HOH A O   1 
HETATM 2410 O  O   . HOH F 6 .   ? -0.837  18.589  22.855  1.00  43.80  ? 534 HOH A O   1 
HETATM 2411 O  O   . HOH F 6 .   ? -3.220  -19.769 6.348   1.00  31.45  ? 535 HOH A O   1 
HETATM 2412 O  O   . HOH F 6 .   ? -27.922 11.577  5.203   1.00  32.16  ? 536 HOH A O   1 
HETATM 2413 O  O   . HOH F 6 .   ? -10.974 -15.181 34.281  1.00  23.71  ? 537 HOH A O   1 
HETATM 2414 O  O   . HOH F 6 .   ? -11.074 -19.181 5.603   1.00  26.17  ? 538 HOH A O   1 
HETATM 2415 O  O   . HOH F 6 .   ? 0.501   0.204   -6.804  1.00  57.94  ? 539 HOH A O   1 
HETATM 2416 O  O   . HOH F 6 .   ? -15.412 0.620   -4.677  1.00  30.77  ? 540 HOH A O   1 
HETATM 2417 O  O   . HOH F 6 .   ? -4.821  -9.688  33.620  1.00  23.37  ? 541 HOH A O   1 
HETATM 2418 O  O   . HOH F 6 .   ? -18.861 -19.843 19.616  1.00  49.04  ? 542 HOH A O   1 
HETATM 2419 O  O   . HOH F 6 .   ? -11.131 12.039  7.322   1.00  28.60  ? 543 HOH A O   1 
HETATM 2420 O  O   . HOH F 6 .   ? -26.169 -7.535  30.352  1.00  37.29  ? 544 HOH A O   1 
HETATM 2421 O  O   . HOH F 6 .   ? 1.799   -9.818  31.744  1.00  36.96  ? 545 HOH A O   1 
HETATM 2422 O  O   . HOH F 6 .   ? -23.142 -11.242 17.212  1.00  26.03  ? 546 HOH A O   1 
HETATM 2423 O  O   . HOH F 6 .   ? 13.101  -5.880  24.514  1.00  24.12  ? 547 HOH A O   1 
HETATM 2424 O  O   . HOH F 6 .   ? -12.337 12.564  29.181  1.00  24.98  ? 548 HOH A O   1 
HETATM 2425 O  O   . HOH F 6 .   ? -14.102 -20.992 2.977   1.00  30.34  ? 549 HOH A O   1 
HETATM 2426 O  O   . HOH F 6 .   ? 1.711   -17.739 13.874  1.00  39.94  ? 550 HOH A O   1 
HETATM 2427 O  O   . HOH F 6 .   ? -3.145  -18.128 0.148   1.00  31.66  ? 551 HOH A O   1 
HETATM 2428 O  O   . HOH F 6 .   ? -23.770 -0.697  26.508  1.00  22.48  ? 552 HOH A O   1 
HETATM 2429 O  O   . HOH F 6 .   ? 1.492   8.147   28.388  1.00  22.30  ? 553 HOH A O   1 
HETATM 2430 O  O   . HOH F 6 .   ? 2.923   -13.692 8.148   1.00  30.03  ? 554 HOH A O   1 
HETATM 2431 O  O   . HOH F 6 .   ? -1.884  8.313   30.759  1.00  24.27  ? 555 HOH A O   1 
HETATM 2432 O  O   . HOH F 6 .   ? -5.219  -13.579 34.475  1.00  39.57  ? 556 HOH A O   1 
HETATM 2433 O  O   . HOH F 6 .   ? -17.600 6.292   38.507  1.00  29.88  ? 557 HOH A O   1 
HETATM 2434 O  O   . HOH F 6 .   ? -18.077 -9.018  34.824  1.00  41.94  ? 558 HOH A O   1 
HETATM 2435 O  O   . HOH F 6 .   ? 8.602   -4.612  23.788  1.00  22.50  ? 559 HOH A O   1 
HETATM 2436 O  O   . HOH F 6 .   ? -25.949 3.369   15.545  1.00  29.13  ? 560 HOH A O   1 
HETATM 2437 O  O   . HOH F 6 .   ? -0.756  -17.476 18.427  1.00  29.13  ? 561 HOH A O   1 
HETATM 2438 O  O   . HOH F 6 .   ? -11.946 9.250   3.292   1.00  22.59  ? 562 HOH A O   1 
HETATM 2439 O  O   . HOH F 6 .   ? -3.733  -15.764 -2.193  1.00  32.16  ? 563 HOH A O   1 
HETATM 2440 O  O   . HOH F 6 .   ? -12.800 -22.220 9.001   1.00  33.93  ? 564 HOH A O   1 
HETATM 2441 O  O   . HOH F 6 .   ? -17.794 -12.040 31.582  1.00  31.23  ? 565 HOH A O   1 
HETATM 2442 O  O   . HOH F 6 .   ? 15.475  -1.271  26.082  1.00  26.45  ? 566 HOH A O   1 
HETATM 2443 O  O   . HOH F 6 .   ? 9.299   7.484   18.547  1.00  36.99  ? 567 HOH A O   1 
HETATM 2444 O  O   . HOH F 6 .   ? -1.899  -17.612 5.028   1.00  39.39  ? 568 HOH A O   1 
HETATM 2445 O  O   . HOH F 6 .   ? 1.813   12.676  22.874  1.00  36.76  ? 569 HOH A O   1 
HETATM 2446 O  O   . HOH F 6 .   ? -6.690  -5.334  37.531  1.00  20.24  ? 570 HOH A O   1 
HETATM 2447 O  O   . HOH F 6 .   ? 3.672   -14.270 -6.381  1.00  35.72  ? 571 HOH A O   1 
HETATM 2448 O  O   . HOH F 6 .   ? -17.661 19.105  6.220   1.00  18.30  ? 572 HOH A O   1 
HETATM 2449 O  O   . HOH F 6 .   ? -18.538 -3.959  -2.528  1.00  29.92  ? 573 HOH A O   1 
HETATM 2450 O  O   . HOH F 6 .   ? -15.215 -16.250 25.505  1.00  31.77  ? 574 HOH A O   1 
HETATM 2451 O  O   . HOH F 6 .   ? 15.454  -2.390  14.578  1.00  21.59  ? 575 HOH A O   1 
HETATM 2452 O  O   . HOH F 6 .   ? 4.666   -1.107  -5.275  1.00  25.53  ? 576 HOH A O   1 
HETATM 2453 O  O   . HOH F 6 .   ? 9.007   -10.744 -6.755  1.00  36.76  ? 577 HOH A O   1 
HETATM 2454 O  O   . HOH F 6 .   ? 7.654   -7.994  -0.283  1.00  32.48  ? 578 HOH A O   1 
HETATM 2455 O  O   . HOH F 6 .   ? -18.683 1.860   41.005  1.00  33.64  ? 579 HOH A O   1 
HETATM 2456 O  O   . HOH F 6 .   ? 11.852  -6.806  7.742   1.00  40.08  ? 580 HOH A O   1 
HETATM 2457 O  O   . HOH F 6 .   ? -1.757  4.312   -4.940  1.00  50.86  ? 581 HOH A O   1 
HETATM 2458 O  O   . HOH F 6 .   ? -27.528 4.433   24.024  1.00  30.10  ? 582 HOH A O   1 
HETATM 2459 O  O   . HOH F 6 .   ? -24.483 -20.345 8.379   1.00  57.02  ? 583 HOH A O   1 
HETATM 2460 O  O   . HOH F 6 .   ? 1.977   -4.542  -12.408 1.00  33.35  ? 584 HOH A O   1 
HETATM 2461 O  O   . HOH F 6 .   ? -6.801  -8.749  -6.932  1.00  31.62  ? 585 HOH A O   1 
HETATM 2462 O  O   . HOH F 6 .   ? -9.263  3.075   34.897  1.00  18.01  ? 586 HOH A O   1 
HETATM 2463 O  O   . HOH F 6 .   ? -14.494 -21.177 17.628  1.00  18.32  ? 587 HOH A O   1 
HETATM 2464 O  O   . HOH F 6 .   ? -0.239  12.908  13.916  1.00  41.92  ? 588 HOH A O   1 
HETATM 2465 O  O   . HOH F 6 .   ? 14.975  -6.613  8.014   1.00  38.52  ? 589 HOH A O   1 
HETATM 2466 O  O   . HOH F 6 .   ? 11.341  -3.964  7.488   1.00  40.14  ? 590 HOH A O   1 
HETATM 2467 O  O   . HOH F 6 .   ? 10.196  -2.594  13.705  1.00  27.83  ? 591 HOH A O   1 
HETATM 2468 O  O   . HOH F 6 .   ? 11.711  -0.364  16.188  1.00  23.84  ? 592 HOH A O   1 
HETATM 2469 O  O   . HOH F 6 .   ? 14.996  -10.279 14.689  1.00  29.24  ? 593 HOH A O   1 
HETATM 2470 O  O   . HOH F 6 .   ? 3.502   -13.976 12.701  1.00  39.28  ? 594 HOH A O   1 
HETATM 2471 O  O   . HOH F 6 .   ? 6.210   -11.140 15.512  1.00  35.75  ? 595 HOH A O   1 
HETATM 2472 O  O   . HOH F 6 .   ? 8.357   3.244   27.914  1.00  35.81  ? 596 HOH A O   1 
HETATM 2473 O  O   . HOH F 6 .   ? 6.202   5.575   29.431  1.00  33.68  ? 597 HOH A O   1 
HETATM 2474 O  O   . HOH F 6 .   ? 2.912   6.464   32.245  1.00  30.37  ? 598 HOH A O   1 
HETATM 2475 O  O   . HOH F 6 .   ? 6.813   -5.217  27.538  1.00  36.34  ? 599 HOH A O   1 
HETATM 2476 O  O   . HOH F 6 .   ? 6.869   -3.700  30.291  1.00  31.88  ? 600 HOH A O   1 
HETATM 2477 O  O   . HOH F 6 .   ? 1.914   1.971   36.052  1.00  46.96  ? 601 HOH A O   1 
HETATM 2478 O  O   . HOH F 6 .   ? -2.092  -11.718 31.739  1.00  27.97  ? 602 HOH A O   1 
HETATM 2479 O  O   . HOH F 6 .   ? -4.702  -12.000 32.261  1.00  19.07  ? 603 HOH A O   1 
HETATM 2480 O  O   . HOH F 6 .   ? -5.999  -11.551 36.652  1.00  33.67  ? 604 HOH A O   1 
HETATM 2481 O  O   . HOH F 6 .   ? -10.259 -12.664 40.302  1.00  24.92  ? 605 HOH A O   1 
HETATM 2482 O  O   . HOH F 6 .   ? -14.192 -16.722 29.131  1.00  18.91  ? 606 HOH A O   1 
HETATM 2483 O  O   . HOH F 6 .   ? -15.618 -10.061 38.257  1.00  45.11  ? 607 HOH A O   1 
HETATM 2484 O  O   . HOH F 6 .   ? -17.020 -14.019 37.776  1.00  28.70  ? 608 HOH A O   1 
HETATM 2485 O  O   . HOH F 6 .   ? -16.850 -1.025  40.127  1.00  30.82  ? 609 HOH A O   1 
HETATM 2486 O  O   . HOH F 6 .   ? -23.077 0.454   34.693  1.00  32.49  ? 610 HOH A O   1 
HETATM 2487 O  O   . HOH F 6 .   ? -20.391 8.350   30.064  1.00  28.82  ? 611 HOH A O   1 
HETATM 2488 O  O   . HOH F 6 .   ? -25.724 6.295   27.077  1.00  26.50  ? 612 HOH A O   1 
HETATM 2489 O  O   . HOH F 6 .   ? -27.610 6.304   21.740  1.00  29.71  ? 613 HOH A O   1 
HETATM 2490 O  O   . HOH F 6 .   ? -24.993 11.179  19.799  1.00  31.07  ? 614 HOH A O   1 
HETATM 2491 O  O   . HOH F 6 .   ? -15.535 3.664   35.330  1.00  32.79  ? 615 HOH A O   1 
HETATM 2492 O  O   . HOH F 6 .   ? -14.666 6.190   32.623  1.00  29.17  ? 616 HOH A O   1 
HETATM 2493 O  O   . HOH F 6 .   ? -12.505 6.926   31.234  1.00  24.61  ? 617 HOH A O   1 
HETATM 2494 O  O   . HOH F 6 .   ? -18.549 12.144  13.073  1.00  24.51  ? 618 HOH A O   1 
HETATM 2495 O  O   . HOH F 6 .   ? -20.472 18.909  13.720  1.00  36.59  ? 619 HOH A O   1 
HETATM 2496 O  O   . HOH F 6 .   ? -18.588 17.623  18.649  1.00  26.63  ? 620 HOH A O   1 
HETATM 2497 O  O   . HOH F 6 .   ? -22.291 19.696  12.067  1.00  42.64  ? 621 HOH A O   1 
HETATM 2498 O  O   . HOH F 6 .   ? -24.733 4.560   8.492   1.00  32.87  ? 622 HOH A O   1 
HETATM 2499 O  O   . HOH F 6 .   ? -23.389 8.042   3.457   1.00  37.18  ? 623 HOH A O   1 
HETATM 2500 O  O   . HOH F 6 .   ? -25.702 8.037   6.332   1.00  39.79  ? 624 HOH A O   1 
HETATM 2501 O  O   . HOH F 6 .   ? -15.548 8.664   -2.266  1.00  66.72  ? 625 HOH A O   1 
HETATM 2502 O  O   . HOH F 6 .   ? -12.176 10.647  5.765   1.00  31.50  ? 626 HOH A O   1 
HETATM 2503 O  O   . HOH F 6 .   ? -11.691 10.628  0.828   1.00  31.07  ? 627 HOH A O   1 
HETATM 2504 O  O   . HOH F 6 .   ? -12.423 13.579  5.147   1.00  38.20  ? 628 HOH A O   1 
HETATM 2505 O  O   . HOH F 6 .   ? -14.647 9.472   31.519  1.00  42.74  ? 629 HOH A O   1 
HETATM 2506 O  O   . HOH F 6 .   ? 1.538   -17.779 7.273   1.00  35.18  ? 630 HOH A O   1 
HETATM 2507 O  O   . HOH F 6 .   ? 0.211   -20.517 15.129  1.00  39.57  ? 631 HOH A O   1 
HETATM 2508 O  O   . HOH F 6 .   ? -2.402  -19.231 21.738  1.00  25.11  ? 632 HOH A O   1 
HETATM 2509 O  O   . HOH F 6 .   ? -6.168  -19.905 24.157  1.00  22.09  ? 633 HOH A O   1 
HETATM 2510 O  O   . HOH F 6 .   ? -8.562  -19.870 26.934  1.00  27.02  ? 634 HOH A O   1 
HETATM 2511 O  O   . HOH F 6 .   ? -10.348 -20.542 25.116  1.00  23.84  ? 635 HOH A O   1 
HETATM 2512 O  O   . HOH F 6 .   ? -3.730  -20.424 14.850  1.00  26.00  ? 636 HOH A O   1 
HETATM 2513 O  O   . HOH F 6 .   ? 0.337   -21.720 18.180  1.00  39.20  ? 637 HOH A O   1 
HETATM 2514 O  O   . HOH F 6 .   ? -15.075 -20.313 22.835  1.00  29.84  ? 638 HOH A O   1 
HETATM 2515 O  O   . HOH F 6 .   ? -16.591 -17.842 24.183  1.00  29.22  ? 639 HOH A O   1 
HETATM 2516 O  O   . HOH F 6 .   ? -1.120  17.998  16.401  1.00  34.95  ? 640 HOH A O   1 
HETATM 2517 O  O   . HOH F 6 .   ? -22.831 -14.754 16.114  1.00  35.43  ? 641 HOH A O   1 
HETATM 2518 O  O   . HOH F 6 .   ? -21.915 -14.111 18.756  1.00  32.49  ? 642 HOH A O   1 
HETATM 2519 O  O   . HOH F 6 .   ? -25.309 -10.667 17.766  1.00  26.52  ? 643 HOH A O   1 
HETATM 2520 O  O   . HOH F 6 .   ? -22.555 -9.681  25.378  1.00  20.62  ? 644 HOH A O   1 
HETATM 2521 O  O   . HOH F 6 .   ? -23.337 -10.417 29.320  1.00  46.50  ? 645 HOH A O   1 
HETATM 2522 O  O   . HOH F 6 .   ? -23.400 -18.078 6.318   1.00  34.75  ? 646 HOH A O   1 
HETATM 2523 O  O   . HOH F 6 .   ? -19.158 -20.932 5.228   1.00  26.00  ? 647 HOH A O   1 
HETATM 2524 O  O   . HOH F 6 .   ? -16.762 -22.091 0.002   1.00  33.14  ? 648 HOH A O   1 
HETATM 2525 O  O   . HOH F 6 .   ? -13.667 -16.071 -0.356  1.00  34.92  ? 649 HOH A O   1 
HETATM 2526 O  O   . HOH F 6 .   ? -26.221 -6.311  5.006   1.00  38.75  ? 650 HOH A O   1 
HETATM 2527 O  O   . HOH F 6 .   ? -24.568 -9.816  1.973   1.00  27.81  ? 651 HOH A O   1 
HETATM 2528 O  O   . HOH F 6 .   ? -23.615 -7.665  -0.075  1.00  42.25  ? 652 HOH A O   1 
HETATM 2529 O  O   . HOH F 6 .   ? -13.964 -5.119  -6.293  1.00  44.31  ? 653 HOH A O   1 
HETATM 2530 O  O   . HOH F 6 .   ? -13.302 -1.010  -5.863  1.00  30.26  ? 654 HOH A O   1 
HETATM 2531 O  O   . HOH F 6 .   ? -7.314  -10.431 -4.406  1.00  35.59  ? 655 HOH A O   1 
HETATM 2532 O  O   . HOH F 6 .   ? -5.359  -12.690 -5.104  1.00  40.53  ? 656 HOH A O   1 
HETATM 2533 O  O   . HOH F 6 .   ? -5.469  -17.057 -3.724  1.00  40.05  ? 657 HOH A O   1 
HETATM 2534 O  O   . HOH F 6 .   ? 1.884   -15.740 -5.231  1.00  46.95  ? 658 HOH A O   1 
HETATM 2535 O  O   . HOH F 6 .   ? -1.248  -17.617 -1.875  1.00  37.73  ? 659 HOH A O   1 
HETATM 2536 O  O   . HOH F 6 .   ? 0.330   -1.410  -4.618  1.00  25.85  ? 660 HOH A O   1 
HETATM 2537 O  O   . HOH F 6 .   ? -2.779  5.911   -0.786  1.00  38.43  ? 661 HOH A O   1 
HETATM 2538 O  O   . HOH F 6 .   ? -9.869  6.479   -4.065  1.00  101.93 ? 662 HOH A O   1 
HETATM 2539 O  O   . HOH F 6 .   ? -25.351 4.138   4.091   1.00  36.33  ? 663 HOH A O   1 
HETATM 2540 O  O   . HOH F 6 .   ? -23.983 -0.071  1.324   1.00  31.36  ? 664 HOH A O   1 
HETATM 2541 O  O   . HOH F 6 .   ? -24.870 -9.802  15.215  1.00  38.74  ? 665 HOH A O   1 
HETATM 2542 O  O   . HOH F 6 .   ? -27.196 -7.350  26.124  1.00  37.74  ? 666 HOH A O   1 
HETATM 2543 O  O   . HOH F 6 .   ? -23.868 -2.976  29.147  1.00  31.56  ? 667 HOH A O   1 
HETATM 2544 O  O   . HOH F 6 .   ? -1.109  -6.116  36.663  1.00  34.40  ? 668 HOH A O   1 
HETATM 2545 O  O   . HOH F 6 .   ? -0.015  -2.264  39.505  1.00  41.60  ? 669 HOH A O   1 
HETATM 2546 O  O   . HOH F 6 .   ? -6.263  6.402   10.372  1.00  32.82  ? 670 HOH A O   1 
HETATM 2547 O  O   . HOH F 6 .   ? 3.837   -0.608  5.543   1.00  41.80  ? 671 HOH A O   1 
HETATM 2548 O  O   . HOH F 6 .   ? 8.068   -9.418  16.715  1.00  22.00  ? 672 HOH A O   1 
HETATM 2549 O  O   . HOH F 6 .   ? 10.468  -10.836 16.308  1.00  21.67  ? 673 HOH A O   1 
HETATM 2550 O  O   . HOH F 6 .   ? -2.920  -14.866 33.063  1.00  30.96  ? 674 HOH A O   1 
HETATM 2551 O  O   . HOH F 6 .   ? -1.368  -13.196 33.437  1.00  26.68  ? 675 HOH A O   1 
HETATM 2552 O  O   . HOH F 6 .   ? -25.452 -0.987  35.138  1.00  32.98  ? 676 HOH A O   1 
HETATM 2553 O  O   . HOH F 6 .   ? -28.088 5.460   26.110  1.00  38.20  ? 677 HOH A O   1 
HETATM 2554 O  O   . HOH F 6 .   ? -31.457 5.768   13.248  1.00  41.63  ? 678 HOH A O   1 
HETATM 2555 O  O   . HOH F 6 .   ? -9.278  13.444  10.302  1.00  42.60  ? 679 HOH A O   1 
HETATM 2556 O  O   . HOH F 6 .   ? -25.816 11.885  17.221  1.00  34.75  ? 680 HOH A O   1 
HETATM 2557 O  O   . HOH F 6 .   ? -10.692 8.574   7.985   1.00  30.00  ? 681 HOH A O   1 
HETATM 2558 O  O   . HOH F 6 .   ? -7.873  -19.259 5.063   1.00  32.34  ? 682 HOH A O   1 
HETATM 2559 O  O   . HOH F 6 .   ? -8.283  -22.240 10.696  1.00  20.86  ? 683 HOH A O   1 
HETATM 2560 O  O   . HOH F 6 .   ? -5.855  20.468  26.490  1.00  28.82  ? 684 HOH A O   1 
HETATM 2561 O  O   . HOH F 6 .   ? -25.415 -15.319 7.586   1.00  32.27  ? 685 HOH A O   1 
HETATM 2562 O  O   . HOH F 6 .   ? -3.374  5.182   -2.926  1.00  25.42  ? 686 HOH A O   1 
HETATM 2563 O  O   . HOH F 6 .   ? -11.881 -4.270  37.621  1.00  38.04  ? 687 HOH A O   1 
HETATM 2564 O  O   . HOH F 6 .   ? -17.247 -16.380 22.173  1.00  23.13  ? 688 HOH A O   1 
HETATM 2565 O  O   . HOH F 6 .   ? -16.729 -18.166 20.294  1.00  27.06  ? 689 HOH A O   1 
HETATM 2566 O  O   . HOH F 6 .   ? 5.825   0.723   8.434   1.00  30.18  ? 690 HOH A O   1 
HETATM 2567 O  O   . HOH F 6 .   ? 6.558   8.498   18.578  1.00  34.76  ? 691 HOH A O   1 
HETATM 2568 O  O   . HOH F 6 .   ? 1.249   -10.060 29.124  1.00  44.59  ? 692 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS A 3   ? 0.5857 0.4234 0.2890 -0.0696 0.0421  0.0132  3   HIS A N   
2    C  CA  . HIS A 3   ? 0.5432 0.5328 0.3296 -0.0524 -0.0504 -0.1317 3   HIS A CA  
3    C  C   . HIS A 3   ? 0.3474 0.4415 0.6909 0.0975  0.1583  0.2056  3   HIS A C   
4    O  O   . HIS A 3   ? 0.8963 1.0735 0.6866 -0.2472 0.1149  0.1298  3   HIS A O   
5    C  CB  . HIS A 3   ? 0.1371 0.2840 0.4336 0.0241  0.0130  0.0716  3   HIS A CB  
6    C  CG  . HIS A 3   ? 0.7742 0.6934 0.7954 0.1084  0.1750  -0.2786 3   HIS A CG  
7    N  ND1 . HIS A 3   ? 1.1647 0.7968 0.9786 -0.0394 -0.0329 0.1288  3   HIS A ND1 
8    C  CD2 . HIS A 3   ? 0.8526 1.6575 0.8381 -0.1624 0.0077  -0.3445 3   HIS A CD2 
9    C  CE1 . HIS A 3   ? 2.0014 1.2948 1.0706 -0.0573 -0.0540 -0.0627 3   HIS A CE1 
10   N  NE2 . HIS A 3   ? 1.6963 1.8522 0.5042 -0.0432 -0.1076 -0.3260 3   HIS A NE2 
11   N  N   . HIS A 4   ? 0.3883 0.6736 0.8942 0.0832  0.0894  0.3091  4   HIS A N   
12   C  CA  . HIS A 4   ? 0.4269 0.6082 0.5985 -0.0894 0.1620  0.3416  4   HIS A CA  
13   C  C   . HIS A 4   ? 0.2150 0.3679 0.2737 -0.0982 0.0929  0.0680  4   HIS A C   
14   O  O   . HIS A 4   ? 0.3251 0.3118 0.3892 -0.0317 0.0820  0.0297  4   HIS A O   
15   C  CB  . HIS A 4   ? 0.4282 0.7088 0.4393 -0.1120 0.2210  0.0689  4   HIS A CB  
16   C  CG  . HIS A 4   ? 1.0700 0.7502 0.6488 -0.4311 -0.2226 -0.0076 4   HIS A CG  
17   N  ND1 . HIS A 4   ? 0.9139 0.6234 0.7294 -0.5766 -0.2274 0.1081  4   HIS A ND1 
18   C  CD2 . HIS A 4   ? 1.0305 1.1102 1.2942 -0.1597 -0.3984 0.1213  4   HIS A CD2 
19   C  CE1 . HIS A 4   ? 0.6664 0.5867 0.5828 -0.4582 -0.1216 0.0992  4   HIS A CE1 
20   N  NE2 . HIS A 4   ? 0.8342 0.9628 1.2098 -0.2624 -0.4050 0.0166  4   HIS A NE2 
21   N  N   . TRP A 5   ? 0.1878 0.3034 0.3072 -0.0311 0.0754  0.0615  5   TRP A N   
22   C  CA  . TRP A 5   ? 0.1410 0.2104 0.2451 -0.0232 0.0265  0.0328  5   TRP A CA  
23   C  C   . TRP A 5   ? 0.1489 0.2081 0.2355 -0.0099 0.0306  0.0142  5   TRP A C   
24   O  O   . TRP A 5   ? 0.2023 0.2328 0.2332 -0.0162 0.0693  0.0381  5   TRP A O   
25   C  CB  . TRP A 5   ? 0.1991 0.2025 0.2271 -0.0197 0.0159  -0.0060 5   TRP A CB  
26   C  CG  . TRP A 5   ? 0.1897 0.2266 0.1951 -0.0553 0.0719  0.0175  5   TRP A CG  
27   C  CD1 . TRP A 5   ? 0.2651 0.2535 0.2590 -0.0082 0.0612  0.0131  5   TRP A CD1 
28   C  CD2 . TRP A 5   ? 0.1630 0.2202 0.2141 -0.0103 0.0441  -0.0187 5   TRP A CD2 
29   N  NE1 . TRP A 5   ? 0.2775 0.2569 0.2538 0.0250  0.0917  0.0524  5   TRP A NE1 
30   C  CE2 . TRP A 5   ? 0.2204 0.2354 0.1781 0.0082  0.0465  0.0198  5   TRP A CE2 
31   C  CE3 . TRP A 5   ? 0.1701 0.1815 0.1727 -0.0372 0.0471  -0.0231 5   TRP A CE3 
32   C  CZ2 . TRP A 5   ? 0.2416 0.3352 0.1357 0.0155  -0.0008 0.0103  5   TRP A CZ2 
33   C  CZ3 . TRP A 5   ? 0.2145 0.2269 0.1630 0.0063  0.0160  -0.0401 5   TRP A CZ3 
34   C  CH2 . TRP A 5   ? 0.2005 0.2825 0.1917 0.0414  0.0181  -0.0610 5   TRP A CH2 
35   N  N   . GLY A 6   ? 0.1511 0.1710 0.2192 0.0110  0.0597  -0.0059 6   GLY A N   
36   C  CA  . GLY A 6   ? 0.1994 0.1926 0.1791 -0.0272 0.0384  -0.0324 6   GLY A CA  
37   C  C   . GLY A 6   ? 0.1613 0.1671 0.1773 0.0073  0.0582  -0.0190 6   GLY A C   
38   O  O   . GLY A 6   ? 0.1362 0.1885 0.1985 0.0119  0.0471  -0.0115 6   GLY A O   
39   N  N   . TYR A 7   ? 0.1407 0.1935 0.2172 -0.0049 0.0637  -0.0242 7   TYR A N   
40   C  CA  . TYR A 7   ? 0.1243 0.1689 0.2506 -0.0049 0.0751  -0.0346 7   TYR A CA  
41   C  C   . TYR A 7   ? 0.1297 0.2294 0.3817 0.0024  0.0549  -0.0324 7   TYR A C   
42   O  O   . TYR A 7   ? 0.1847 0.2384 0.4311 -0.0252 0.0841  -0.0449 7   TYR A O   
43   C  CB  . TYR A 7   ? 0.1262 0.2025 0.2330 0.0010  0.0741  -0.0406 7   TYR A CB  
44   C  CG  . TYR A 7   ? 0.1206 0.1567 0.1816 -0.0286 0.0430  -0.0359 7   TYR A CG  
45   C  CD1 . TYR A 7   ? 0.1037 0.1441 0.1809 -0.0222 0.0286  -0.0142 7   TYR A CD1 
46   C  CD2 . TYR A 7   ? 0.1350 0.1737 0.1737 -0.0251 0.0560  -0.0244 7   TYR A CD2 
47   C  CE1 . TYR A 7   ? 0.1154 0.1341 0.1441 -0.0188 0.0305  -0.0177 7   TYR A CE1 
48   C  CE2 . TYR A 7   ? 0.1188 0.1764 0.1403 -0.0166 0.0185  -0.0182 7   TYR A CE2 
49   C  CZ  . TYR A 7   ? 0.1387 0.1527 0.1326 0.0027  0.0366  -0.0274 7   TYR A CZ  
50   O  OH  . TYR A 7   ? 0.1262 0.1620 0.1279 0.0027  0.0171  -0.0030 7   TYR A OH  
51   N  N   . GLY A 8   ? 0.1773 0.2303 0.3792 0.0099  0.1001  -0.0577 8   GLY A N   
52   C  CA  . GLY A 8   ? 0.1457 0.2730 0.4733 0.0048  0.0975  -0.1090 8   GLY A CA  
53   C  C   . GLY A 8   ? 0.2766 0.2097 0.3316 0.0469  0.0938  -0.0666 8   GLY A C   
54   O  O   . GLY A 8   ? 0.2003 0.2635 0.3449 0.0093  0.1059  -0.0617 8   GLY A O   
55   N  N   . LYS A 9   ? 0.2615 0.2113 0.3948 0.0328  0.0516  -0.0621 9   LYS A N   
56   C  CA  . LYS A 9   ? 0.3490 0.1932 0.4176 0.0115  -0.0719 -0.0520 9   LYS A CA  
57   C  C   . LYS A 9   ? 0.2712 0.1804 0.3037 0.0520  0.0421  -0.0197 9   LYS A C   
58   O  O   . LYS A 9   ? 0.1940 0.3258 0.3820 0.0017  0.0533  -0.0513 9   LYS A O   
59   C  CB  . LYS A 9   ? 0.2240 0.2933 0.3799 0.0208  -0.0540 -0.0217 9   LYS A CB  
60   C  CG  . LYS A 9   ? 0.4099 0.4077 0.4612 0.1440  -0.1168 -0.0627 9   LYS A CG  
61   C  CD  . LYS A 9   ? 0.1869 0.4715 0.1747 0.0980  -0.1533 -0.0542 9   LYS A CD  
62   C  CE  . LYS A 9   ? 0.2558 0.2470 0.2350 0.2048  -0.1738 -0.1339 9   LYS A CE  
63   N  NZ  . LYS A 9   ? 0.2092 0.3492 0.2598 0.1649  -0.1837 -0.2593 9   LYS A NZ  
64   N  N   . HIS A 10  ? 0.2023 0.2145 0.3905 0.0725  0.1272  0.0071  10  HIS A N   
65   C  CA  . HIS A 10  ? 0.2111 0.2639 0.4176 0.0436  0.1542  0.0324  10  HIS A CA  
66   C  C   . HIS A 10  ? 0.1717 0.2190 0.2937 0.0384  0.0758  0.0054  10  HIS A C   
67   O  O   . HIS A 10  ? 0.1912 0.3179 0.3560 0.0680  0.0856  0.0388  10  HIS A O   
68   C  CB  . HIS A 10  ? 0.2524 0.2949 0.4454 0.1120  0.2021  0.0951  10  HIS A CB  
69   C  CG  . HIS A 10  ? 0.3005 0.3151 0.4970 0.0934  0.2397  0.0890  10  HIS A CG  
70   N  ND1 . HIS A 10  ? 0.3388 0.3571 0.5210 0.0575  0.2354  -0.0177 10  HIS A ND1 
71   C  CD2 . HIS A 10  ? 0.3804 0.2885 0.5498 0.0900  0.2345  0.0306  10  HIS A CD2 
72   C  CE1 . HIS A 10  ? 0.2949 0.2975 0.5217 0.1088  0.2404  0.0467  10  HIS A CE1 
73   N  NE2 . HIS A 10  ? 0.2926 0.3643 0.5598 0.0935  0.2344  0.0529  10  HIS A NE2 
74   N  N   . ASN A 11  ? 0.1619 0.2488 0.2899 0.0533  0.1093  0.0214  11  ASN A N   
75   C  CA  . ASN A 11  ? 0.1447 0.2504 0.2822 0.0658  0.0892  0.0051  11  ASN A CA  
76   C  C   . ASN A 11  ? 0.1498 0.2055 0.2285 0.0408  0.0866  0.0142  11  ASN A C   
77   O  O   . ASN A 11  ? 0.1421 0.2009 0.2258 0.0361  0.0807  0.0046  11  ASN A O   
78   C  CB  . ASN A 11  ? 0.1486 0.2624 0.2684 0.0146  0.1211  0.0295  11  ASN A CB  
79   C  CG  . ASN A 11  ? 0.2500 0.1994 0.2838 0.0188  0.1190  -0.0260 11  ASN A CG  
80   O  OD1 . ASN A 11  ? 0.2362 0.2407 0.2967 0.0208  0.0890  0.0205  11  ASN A OD1 
81   N  ND2 . ASN A 11  ? 0.2416 0.2881 0.2737 -0.0052 0.1049  0.0003  11  ASN A ND2 
82   N  N   . GLY A 12  ? 0.1006 0.2060 0.2561 0.0206  0.0586  0.0049  12  GLY A N   
83   C  CA  . GLY A 12  ? 0.1500 0.2468 0.1852 0.0335  0.0729  0.0023  12  GLY A CA  
84   C  C   . GLY A 12  ? 0.1471 0.1611 0.1879 0.0131  0.0540  0.0122  12  GLY A C   
85   O  O   . GLY A 12  ? 0.1304 0.1649 0.2143 0.0104  0.0342  0.0040  12  GLY A O   
86   N  N   . PRO A 13  ? 0.1177 0.1333 0.1863 0.0037  0.0511  0.0017  13  PRO A N   
87   C  CA  . PRO A 13  ? 0.1307 0.1464 0.2072 0.0133  0.0491  -0.0071 13  PRO A CA  
88   C  C   . PRO A 13  ? 0.1475 0.1599 0.1870 0.0126  0.0628  0.0020  13  PRO A C   
89   O  O   . PRO A 13  ? 0.1303 0.1832 0.1948 -0.0119 0.0346  -0.0096 13  PRO A O   
90   C  CB  . PRO A 13  ? 0.1610 0.1283 0.1730 -0.0265 0.0562  -0.0320 13  PRO A CB  
91   C  CG  . PRO A 13  ? 0.1333 0.1441 0.1764 -0.0096 0.0505  -0.0156 13  PRO A CG  
92   C  CD  . PRO A 13  ? 0.1216 0.1890 0.1784 0.0125  0.0471  -0.0086 13  PRO A CD  
93   N  N   . GLU A 14  ? 0.1454 0.1524 0.2148 0.0126  0.0505  0.0110  14  GLU A N   
94   C  CA  . GLU A 14  ? 0.2362 0.1507 0.2158 0.0289  0.0083  0.0233  14  GLU A CA  
95   C  C   . GLU A 14  ? 0.1511 0.1729 0.2364 0.0702  0.0021  -0.0051 14  GLU A C   
96   O  O   . GLU A 14  ? 0.1836 0.1948 0.2337 0.0570  -0.0031 0.0306  14  GLU A O   
97   C  CB  . GLU A 14  ? 0.3145 0.1653 0.2495 0.0379  -0.0153 0.0185  14  GLU A CB  
98   C  CG  . GLU A 14  ? 0.2709 0.2381 0.4758 -0.0007 0.0755  -0.0167 14  GLU A CG  
99   C  CD  . GLU A 14  ? 0.4537 0.4038 0.3612 -0.0313 0.0555  0.0621  14  GLU A CD  
100  O  OE1 . GLU A 14  ? 0.5568 0.4280 0.5361 0.0522  0.1083  -0.1638 14  GLU A OE1 
101  O  OE2 . GLU A 14  ? 0.6168 0.8048 0.4269 0.0878  -0.1228 0.0366  14  GLU A OE2 
102  N  N   . HIS A 15  ? 0.1188 0.1450 0.2108 0.0305  0.0307  -0.0082 15  HIS A N   
103  C  CA  . HIS A 15  ? 0.1044 0.1525 0.2369 0.0181  0.0310  -0.0035 15  HIS A CA  
104  C  C   . HIS A 15  ? 0.0940 0.1565 0.2175 0.0119  0.0135  -0.0151 15  HIS A C   
105  O  O   . HIS A 15  ? 0.0777 0.1823 0.2506 0.0219  0.0212  0.0146  15  HIS A O   
106  C  CB  . HIS A 15  ? 0.1191 0.1838 0.2380 0.0461  0.0232  -0.0062 15  HIS A CB  
107  C  CG  . HIS A 15  ? 0.1396 0.2157 0.2626 0.0676  0.0271  0.0120  15  HIS A CG  
108  N  ND1 . HIS A 15  ? 0.1520 0.2664 0.2743 0.1001  0.0068  -0.0408 15  HIS A ND1 
109  C  CD2 . HIS A 15  ? 0.2323 0.2091 0.2581 0.0898  0.0700  0.0120  15  HIS A CD2 
110  C  CE1 . HIS A 15  ? 0.2219 0.2953 0.3318 0.1324  0.0132  -0.0489 15  HIS A CE1 
111  N  NE2 . HIS A 15  ? 0.2181 0.2666 0.2565 0.1067  0.0410  -0.0244 15  HIS A NE2 
112  N  N   . TRP A 16  ? 0.0817 0.1497 0.1941 0.0200  0.0214  0.0006  16  TRP A N   
113  C  CA  . TRP A 16  ? 0.0698 0.1283 0.2141 0.0055  0.0142  -0.0165 16  TRP A CA  
114  C  C   . TRP A 16  ? 0.0793 0.1447 0.1795 0.0063  0.0135  -0.0073 16  TRP A C   
115  O  O   . TRP A 16  ? 0.0991 0.1471 0.2055 -0.0017 -0.0062 -0.0003 16  TRP A O   
116  C  CB  . TRP A 16  ? 0.0737 0.1495 0.1809 -0.0098 0.0105  -0.0154 16  TRP A CB  
117  C  CG  . TRP A 16  ? 0.0924 0.1448 0.1581 0.0093  0.0021  0.0043  16  TRP A CG  
118  C  CD1 . TRP A 16  ? 0.0964 0.1443 0.1615 0.0088  0.0059  -0.0140 16  TRP A CD1 
119  C  CD2 . TRP A 16  ? 0.0781 0.1161 0.1682 0.0098  0.0195  -0.0006 16  TRP A CD2 
120  N  NE1 . TRP A 16  ? 0.0856 0.1705 0.1725 0.0133  0.0274  -0.0125 16  TRP A NE1 
121  C  CE2 . TRP A 16  ? 0.0899 0.1133 0.1556 0.0125  0.0296  0.0001  16  TRP A CE2 
122  C  CE3 . TRP A 16  ? 0.0860 0.1125 0.1678 0.0148  0.0241  -0.0035 16  TRP A CE3 
123  C  CZ2 . TRP A 16  ? 0.0985 0.1319 0.1412 -0.0007 0.0278  -0.0091 16  TRP A CZ2 
124  C  CZ3 . TRP A 16  ? 0.0930 0.1368 0.1493 -0.0015 0.0183  -0.0086 16  TRP A CZ3 
125  C  CH2 . TRP A 16  ? 0.0958 0.1439 0.1668 -0.0048 0.0276  -0.0120 16  TRP A CH2 
126  N  N   . HIS A 17  ? 0.0760 0.1603 0.2003 0.0060  0.0027  -0.0010 17  HIS A N   
127  C  CA  . HIS A 17  ? 0.0690 0.1802 0.2003 0.0055  0.0098  -0.0087 17  HIS A CA  
128  C  C   . HIS A 17  ? 0.0824 0.2048 0.2275 -0.0256 0.0055  -0.0149 17  HIS A C   
129  O  O   . HIS A 17  ? 0.0851 0.2118 0.2460 -0.0038 -0.0166 -0.0046 17  HIS A O   
130  C  CB  . HIS A 17  ? 0.1369 0.1991 0.2294 0.0438  0.0178  -0.0003 17  HIS A CB  
131  C  CG  . HIS A 17  ? 0.1133 0.2170 0.2303 0.0335  -0.0209 0.0165  17  HIS A CG  
132  N  ND1 . HIS A 17  ? 0.1486 0.2569 0.2467 0.0264  -0.0209 0.0184  17  HIS A ND1 
133  C  CD2 . HIS A 17  ? 0.1115 0.2504 0.2125 0.0568  0.0177  0.0432  17  HIS A CD2 
134  C  CE1 . HIS A 17  ? 0.2271 0.2465 0.2610 0.0654  0.0285  0.0443  17  HIS A CE1 
135  N  NE2 . HIS A 17  ? 0.1249 0.2533 0.2935 0.0690  -0.0142 0.0478  17  HIS A NE2 
136  N  N   . LYS A 18  ? 0.0843 0.1987 0.2398 0.0087  0.0148  0.0085  18  LYS A N   
137  C  CA  . LYS A 18  ? 0.0593 0.2497 0.3034 0.0010  0.0110  0.0204  18  LYS A CA  
138  C  C   . LYS A 18  ? 0.1036 0.2177 0.3393 -0.0146 -0.0091 0.0244  18  LYS A C   
139  O  O   . LYS A 18  ? 0.1599 0.2116 0.4505 -0.0379 -0.0311 0.0513  18  LYS A O   
140  C  CB  . LYS A 18  ? 0.0947 0.2398 0.2377 0.0120  -0.0092 0.0454  18  LYS A CB  
141  C  CG  . LYS A 18  ? 0.0949 0.2210 0.2969 0.0355  0.0324  0.0265  18  LYS A CG  
142  C  CD  . LYS A 18  ? 0.0873 0.2545 0.2682 0.0410  -0.0100 0.0125  18  LYS A CD  
143  C  CE  . LYS A 18  ? 0.1486 0.1872 0.2793 0.0326  0.0051  0.0315  18  LYS A CE  
144  N  NZ  . LYS A 18  ? 0.1145 0.2486 0.2382 0.0557  0.0274  0.0344  18  LYS A NZ  
145  N  N   A ASP A 19  ? 0.1017 0.2389 0.2813 0.0640  0.0041  -0.0019 19  ASP A N   
146  N  N   B ASP A 19  ? 0.1173 0.2078 0.2517 0.0043  0.0103  0.0197  19  ASP A N   
147  C  CA  A ASP A 19  ? 0.1028 0.2529 0.2908 0.0071  0.0082  0.0285  19  ASP A CA  
148  C  CA  B ASP A 19  ? 0.1254 0.2152 0.3000 0.0057  0.0078  0.0136  19  ASP A CA  
149  C  C   A ASP A 19  ? 0.1268 0.1842 0.2779 -0.0082 0.0000  0.0322  19  ASP A C   
150  C  C   B ASP A 19  ? 0.1129 0.1721 0.3041 -0.0636 0.0080  -0.0038 19  ASP A C   
151  O  O   A ASP A 19  ? 0.1382 0.1684 0.2095 -0.0434 0.0216  0.0278  19  ASP A O   
152  O  O   B ASP A 19  ? 0.1712 0.1577 0.2312 -0.0493 -0.0254 -0.0076 19  ASP A O   
153  C  CB  A ASP A 19  ? 0.1991 0.2818 0.2224 0.0881  0.0194  0.0375  19  ASP A CB  
154  C  CB  B ASP A 19  ? 0.0834 0.3093 0.2547 -0.0262 0.0452  0.0001  19  ASP A CB  
155  C  CG  A ASP A 19  ? 0.1438 0.2554 0.3077 0.0357  0.0432  0.0111  19  ASP A CG  
156  C  CG  B ASP A 19  ? 0.3025 0.2998 0.2897 0.0218  0.0516  -0.1168 19  ASP A CG  
157  O  OD1 A ASP A 19  ? 0.1741 0.3046 0.2449 -0.0216 0.0593  -0.0192 19  ASP A OD1 
158  O  OD1 B ASP A 19  ? 0.2536 0.5522 0.2809 0.0697  0.1344  -0.0533 19  ASP A OD1 
159  O  OD2 A ASP A 19  ? 0.3195 0.4656 0.3339 -0.0942 0.0353  0.0469  19  ASP A OD2 
160  O  OD2 B ASP A 19  ? 0.3330 0.2894 0.2942 0.0049  0.0842  -0.0819 19  ASP A OD2 
161  N  N   . PHE A 20  ? 0.0939 0.1705 0.2565 -0.0160 0.0234  0.0060  20  PHE A N   
162  C  CA  . PHE A 20  ? 0.0994 0.1662 0.2391 -0.0028 0.0054  0.0164  20  PHE A CA  
163  C  C   . PHE A 20  ? 0.1102 0.1590 0.2215 -0.0006 -0.0010 -0.0183 20  PHE A C   
164  O  O   . PHE A 20  ? 0.1057 0.1574 0.2434 -0.0104 0.0059  -0.0109 20  PHE A O   
165  C  CB  . PHE A 20  ? 0.0944 0.1978 0.2421 -0.0143 0.0049  0.0172  20  PHE A CB  
166  C  CG  . PHE A 20  ? 0.0938 0.2416 0.2847 -0.0403 0.0049  0.0526  20  PHE A CG  
167  C  CD1 . PHE A 20  ? 0.1475 0.2716 0.3438 -0.0416 0.0292  0.1040  20  PHE A CD1 
168  C  CD2 . PHE A 20  ? 0.1527 0.3025 0.2450 -0.0551 0.0044  0.0471  20  PHE A CD2 
169  C  CE1 . PHE A 20  ? 0.1382 0.2795 0.3384 -0.0242 0.0024  0.1014  20  PHE A CE1 
170  C  CE2 . PHE A 20  ? 0.1869 0.3197 0.2619 -0.0118 0.0184  0.0357  20  PHE A CE2 
171  C  CZ  . PHE A 20  ? 0.1507 0.3404 0.3192 -0.0392 0.0024  0.0983  20  PHE A CZ  
172  N  N   . PRO A 21  ? 0.1181 0.1870 0.2364 -0.0242 0.0120  -0.0098 21  PRO A N   
173  C  CA  . PRO A 21  ? 0.0897 0.2226 0.2412 -0.0500 0.0099  -0.0121 21  PRO A CA  
174  C  C   . PRO A 21  ? 0.0994 0.1711 0.2188 -0.0142 -0.0052 -0.0276 21  PRO A C   
175  O  O   . PRO A 21  ? 0.0931 0.1996 0.2387 -0.0118 -0.0372 -0.0054 21  PRO A O   
176  C  CB  . PRO A 21  ? 0.1138 0.2574 0.3107 -0.0610 -0.0282 -0.0132 21  PRO A CB  
177  C  CG  . PRO A 21  ? 0.2951 0.2386 0.3538 -0.1557 -0.0815 0.0226  21  PRO A CG  
178  C  CD  . PRO A 21  ? 0.1534 0.1764 0.2847 -0.0533 -0.0098 0.0035  21  PRO A CD  
179  N  N   A ILE A 22  ? 0.0816 0.1447 0.2244 -0.0105 -0.0108 -0.0531 22  ILE A N   
180  N  N   B ILE A 22  ? 0.0795 0.1736 0.2276 -0.0092 -0.0152 -0.0240 22  ILE A N   
181  C  CA  A ILE A 22  ? 0.0974 0.1447 0.2355 0.0057  -0.0008 0.0093  22  ILE A CA  
182  C  CA  B ILE A 22  ? 0.1082 0.1489 0.1678 -0.0080 -0.0291 -0.0467 22  ILE A CA  
183  C  C   A ILE A 22  ? 0.0846 0.1601 0.1757 -0.0148 -0.0197 -0.0102 22  ILE A C   
184  C  C   B ILE A 22  ? 0.0869 0.1292 0.1906 0.0148  -0.0144 -0.0073 22  ILE A C   
185  O  O   A ILE A 22  ? 0.0777 0.1252 0.1640 0.0037  -0.0142 -0.0148 22  ILE A O   
186  O  O   B ILE A 22  ? 0.0856 0.1430 0.1543 0.0190  -0.0131 0.0126  22  ILE A O   
187  C  CB  A ILE A 22  ? 0.1240 0.1240 0.1554 -0.0020 -0.0142 -0.0259 22  ILE A CB  
188  C  CB  B ILE A 22  ? 0.1251 0.1240 0.1696 -0.0274 0.0103  -0.0063 22  ILE A CB  
189  C  CG1 A ILE A 22  ? 0.1542 0.1683 0.2011 0.0208  0.0201  -0.0181 22  ILE A CG1 
190  C  CG1 B ILE A 22  ? 0.0998 0.1137 0.1504 -0.0125 -0.0127 -0.0104 22  ILE A CG1 
191  C  CG2 A ILE A 22  ? 0.1292 0.1477 0.1479 0.0060  -0.0153 -0.0092 22  ILE A CG2 
192  C  CG2 B ILE A 22  ? 0.1032 0.1216 0.1576 -0.0296 -0.0086 0.0231  22  ILE A CG2 
193  C  CD1 A ILE A 22  ? 0.2506 0.2495 0.1911 -0.0819 -0.0199 0.0143  22  ILE A CD1 
194  C  CD1 B ILE A 22  ? 0.1116 0.1319 0.2237 0.0138  -0.0080 -0.0262 22  ILE A CD1 
195  N  N   . ALA A 23  ? 0.1027 0.1272 0.1787 -0.0103 -0.0197 -0.0143 23  ALA A N   
196  C  CA  . ALA A 23  ? 0.1033 0.1373 0.1831 -0.0017 0.0082  -0.0044 23  ALA A CA  
197  C  C   . ALA A 23  ? 0.1030 0.1335 0.1809 -0.0118 0.0052  -0.0227 23  ALA A C   
198  O  O   . ALA A 23  ? 0.1179 0.1541 0.1748 -0.0094 -0.0046 -0.0054 23  ALA A O   
199  C  CB  . ALA A 23  ? 0.0961 0.1326 0.1991 -0.0017 -0.0041 -0.0136 23  ALA A CB  
200  N  N   . LYS A 24  ? 0.1445 0.1836 0.1721 0.0001  -0.0324 0.0008  24  LYS A N   
201  C  CA  . LYS A 24  ? 0.1186 0.2025 0.1969 0.0006  -0.0173 -0.0197 24  LYS A CA  
202  C  C   . LYS A 24  ? 0.1308 0.2123 0.1766 -0.0040 -0.0241 -0.0256 24  LYS A C   
203  O  O   . LYS A 24  ? 0.1741 0.2460 0.1981 -0.0017 -0.0392 -0.0003 24  LYS A O   
204  C  CB  . LYS A 24  ? 0.1068 0.2343 0.2278 0.0059  -0.0193 0.0026  24  LYS A CB  
205  C  CG  . LYS A 24  ? 0.1536 0.2676 0.2396 0.0351  -0.0015 -0.0149 24  LYS A CG  
206  C  CD  . LYS A 24  ? 0.1583 0.3037 0.3490 0.0649  0.0019  0.0498  24  LYS A CD  
207  C  CE  . LYS A 24  ? 0.2326 0.3014 0.4199 0.0934  -0.0096 0.0241  24  LYS A CE  
208  N  NZ  . LYS A 24  ? 0.2337 0.3273 0.4577 0.0175  0.1081  -0.0425 24  LYS A NZ  
209  N  N   . GLY A 25  ? 0.0978 0.1912 0.2021 0.0043  -0.0137 -0.0370 25  GLY A N   
210  C  CA  . GLY A 25  ? 0.1407 0.2003 0.1876 -0.0131 -0.0020 -0.0445 25  GLY A CA  
211  C  C   . GLY A 25  ? 0.1425 0.1743 0.1633 0.0083  -0.0465 -0.0432 25  GLY A C   
212  O  O   . GLY A 25  ? 0.1265 0.2113 0.1764 0.0000  -0.0244 -0.0249 25  GLY A O   
213  N  N   . GLU A 26  ? 0.1199 0.2240 0.1543 -0.0176 -0.0296 -0.0472 26  GLU A N   
214  C  CA  . GLU A 26  ? 0.1500 0.2332 0.1337 -0.0304 -0.0359 -0.0296 26  GLU A CA  
215  C  C   . GLU A 26  ? 0.1215 0.1640 0.1384 0.0034  -0.0218 -0.0023 26  GLU A C   
216  O  O   . GLU A 26  ? 0.1685 0.2034 0.1145 -0.0253 -0.0419 -0.0183 26  GLU A O   
217  C  CB  . GLU A 26  ? 0.1937 0.2603 0.1509 -0.0253 -0.0645 -0.0701 26  GLU A CB  
218  C  CG  . GLU A 26  ? 0.1703 0.2831 0.2045 -0.0223 -0.0480 -0.0524 26  GLU A CG  
219  C  CD  . GLU A 26  ? 0.3009 0.3838 0.2691 -0.0559 -0.1244 -0.0252 26  GLU A CD  
220  O  OE1 . GLU A 26  ? 0.3725 0.3822 0.3106 -0.0825 -0.1340 0.0217  26  GLU A OE1 
221  O  OE2 . GLU A 26  ? 0.3677 0.4993 0.4783 0.1092  -0.1717 -0.0653 26  GLU A OE2 
222  N  N   . ARG A 27  ? 0.1303 0.1283 0.1244 -0.0048 -0.0320 -0.0329 27  ARG A N   
223  C  CA  . ARG A 27  ? 0.1161 0.1230 0.1314 -0.0024 -0.0109 -0.0192 27  ARG A CA  
224  C  C   . ARG A 27  ? 0.1143 0.1021 0.1077 -0.0071 -0.0098 -0.0221 27  ARG A C   
225  O  O   . ARG A 27  ? 0.1111 0.1161 0.1145 0.0015  -0.0129 -0.0162 27  ARG A O   
226  C  CB  . ARG A 27  ? 0.1691 0.1365 0.1179 -0.0032 -0.0153 -0.0285 27  ARG A CB  
227  C  CG  . ARG A 27  ? 0.1556 0.1739 0.1680 -0.0240 -0.0093 -0.0166 27  ARG A CG  
228  C  CD  . ARG A 27  ? 0.1854 0.1928 0.1416 -0.0026 -0.0288 -0.0241 27  ARG A CD  
229  N  NE  . ARG A 27  ? 0.1872 0.1246 0.1170 -0.0068 0.0085  -0.0296 27  ARG A NE  
230  C  CZ  . ARG A 27  ? 0.1488 0.1563 0.1124 0.0020  0.0143  -0.0124 27  ARG A CZ  
231  N  NH1 . ARG A 27  ? 0.2231 0.1597 0.1480 0.0113  0.0300  -0.0476 27  ARG A NH1 
232  N  NH2 . ARG A 27  ? 0.1380 0.1738 0.1682 0.0038  -0.0003 -0.0193 27  ARG A NH2 
233  N  N   . GLN A 28  ? 0.1044 0.1115 0.1107 -0.0028 -0.0174 -0.0230 28  GLN A N   
234  C  CA  . GLN A 28  ? 0.0940 0.1059 0.0973 -0.0068 0.0010  -0.0120 28  GLN A CA  
235  C  C   . GLN A 28  ? 0.0873 0.0940 0.1042 0.0103  -0.0121 -0.0066 28  GLN A C   
236  O  O   . GLN A 28  ? 0.1064 0.1295 0.0917 -0.0021 -0.0115 -0.0070 28  GLN A O   
237  C  CB  . GLN A 28  ? 0.0780 0.1288 0.1335 0.0031  -0.0105 -0.0194 28  GLN A CB  
238  C  CG  . GLN A 28  ? 0.1010 0.1303 0.1312 0.0003  -0.0107 -0.0223 28  GLN A CG  
239  C  CD  . GLN A 28  ? 0.0740 0.1173 0.1231 -0.0037 -0.0111 -0.0218 28  GLN A CD  
240  O  OE1 . GLN A 28  ? 0.0971 0.1154 0.1360 -0.0076 -0.0030 -0.0179 28  GLN A OE1 
241  N  NE2 . GLN A 28  ? 0.0926 0.1085 0.1317 -0.0071 -0.0038 -0.0208 28  GLN A NE2 
242  N  N   . SER A 29  ? 0.0847 0.0960 0.1018 0.0102  -0.0104 -0.0177 29  SER A N   
243  C  CA  . SER A 29  ? 0.0951 0.0775 0.0929 0.0043  -0.0024 -0.0190 29  SER A CA  
244  C  C   . SER A 29  ? 0.0764 0.0983 0.0816 0.0000  -0.0162 0.0000  29  SER A C   
245  O  O   . SER A 29  ? 0.0879 0.1066 0.1032 -0.0068 0.0082  -0.0109 29  SER A O   
246  C  CB  . SER A 29  ? 0.0994 0.0825 0.1019 0.0164  -0.0006 -0.0214 29  SER A CB  
247  O  OG  . SER A 29  ? 0.0886 0.0913 0.1019 0.0024  0.0021  -0.0216 29  SER A OG  
248  N  N   . PRO A 30  ? 0.0838 0.0872 0.0872 0.0065  -0.0092 -0.0071 30  PRO A N   
249  C  CA  . PRO A 30  ? 0.0882 0.0861 0.0807 -0.0085 0.0035  -0.0032 30  PRO A CA  
250  C  C   . PRO A 30  ? 0.0815 0.0874 0.0933 0.0071  -0.0030 -0.0044 30  PRO A C   
251  O  O   . PRO A 30  ? 0.0944 0.0962 0.0983 0.0119  -0.0068 -0.0035 30  PRO A O   
252  C  CB  . PRO A 30  ? 0.0945 0.0957 0.0861 0.0078  -0.0078 -0.0098 30  PRO A CB  
253  C  CG  . PRO A 30  ? 0.0906 0.1014 0.0987 0.0086  0.0057  -0.0105 30  PRO A CG  
254  C  CD  . PRO A 30  ? 0.1130 0.0727 0.0924 -0.0034 0.0179  -0.0173 30  PRO A CD  
255  N  N   . VAL A 31  ? 0.1019 0.0962 0.0951 0.0062  0.0027  -0.0041 31  VAL A N   
256  C  CA  . VAL A 31  ? 0.1177 0.1033 0.0791 0.0037  -0.0057 0.0057  31  VAL A CA  
257  C  C   . VAL A 31  ? 0.1041 0.1082 0.0843 0.0073  0.0020  -0.0024 31  VAL A C   
258  O  O   . VAL A 31  ? 0.1058 0.1042 0.0967 0.0019  -0.0076 0.0081  31  VAL A O   
259  C  CB  . VAL A 31  ? 0.0969 0.1294 0.0842 0.0051  0.0032  -0.0171 31  VAL A CB  
260  C  CG1 . VAL A 31  ? 0.1376 0.1208 0.1154 -0.0060 0.0000  -0.0151 31  VAL A CG1 
261  C  CG2 . VAL A 31  ? 0.1298 0.1199 0.0985 0.0211  0.0093  -0.0148 31  VAL A CG2 
262  N  N   . ASP A 32  ? 0.1182 0.1030 0.0891 0.0083  -0.0015 0.0114  32  ASP A N   
263  C  CA  . ASP A 32  ? 0.1179 0.1009 0.1003 0.0131  -0.0010 0.0080  32  ASP A CA  
264  C  C   . ASP A 32  ? 0.1341 0.1014 0.0899 0.0175  -0.0037 0.0038  32  ASP A C   
265  O  O   . ASP A 32  ? 0.1419 0.1439 0.1112 0.0013  -0.0132 -0.0107 32  ASP A O   
266  C  CB  . ASP A 32  ? 0.1459 0.1071 0.1136 0.0146  -0.0146 0.0078  32  ASP A CB  
267  C  CG  . ASP A 32  ? 0.1507 0.1124 0.1152 0.0296  -0.0035 0.0138  32  ASP A CG  
268  O  OD1 . ASP A 32  ? 0.1391 0.1055 0.1053 0.0161  -0.0040 0.0078  32  ASP A OD1 
269  O  OD2 . ASP A 32  ? 0.1870 0.1412 0.1152 0.0100  -0.0105 0.0333  32  ASP A OD2 
270  N  N   A ILE A 33  ? 0.1172 0.1055 0.0908 0.0251  0.0017  0.0199  33  ILE A N   
271  N  N   B ILE A 33  ? 0.1190 0.1105 0.0856 0.0208  0.0007  0.0081  33  ILE A N   
272  C  CA  A ILE A 33  ? 0.1176 0.0782 0.0643 0.0254  -0.0104 -0.0013 33  ILE A CA  
273  C  CA  B ILE A 33  ? 0.0960 0.1351 0.1116 0.0070  0.0168  0.0307  33  ILE A CA  
274  C  C   A ILE A 33  ? 0.1197 0.1146 0.0971 0.0102  0.0102  0.0168  33  ILE A C   
275  C  C   B ILE A 33  ? 0.1382 0.1053 0.1030 0.0308  -0.0026 0.0031  33  ILE A C   
276  O  O   A ILE A 33  ? 0.0913 0.1085 0.0945 0.0172  0.0278  0.0236  33  ILE A O   
277  O  O   B ILE A 33  ? 0.0956 0.1224 0.1003 -0.0027 0.0149  0.0141  33  ILE A O   
278  C  CB  A ILE A 33  ? 0.0926 0.0942 0.0851 0.0035  0.0006  0.0220  33  ILE A CB  
279  C  CB  B ILE A 33  ? 0.1086 0.1010 0.1102 -0.0114 -0.0152 -0.0181 33  ILE A CB  
280  C  CG1 A ILE A 33  ? 0.0810 0.0705 0.0863 0.0266  0.0126  0.0116  33  ILE A CG1 
281  C  CG1 B ILE A 33  ? 0.1158 0.1337 0.1552 0.0037  -0.0390 0.0582  33  ILE A CG1 
282  C  CG2 A ILE A 33  ? 0.0734 0.1097 0.1208 -0.0104 0.0082  -0.0311 33  ILE A CG2 
283  C  CG2 B ILE A 33  ? 0.1258 0.1206 0.1228 -0.0230 0.0193  0.0214  33  ILE A CG2 
284  C  CD1 A ILE A 33  ? 0.0747 0.0688 0.0745 0.0124  0.0052  0.0148  33  ILE A CD1 
285  C  CD1 B ILE A 33  ? 0.2745 0.2405 0.2587 -0.0109 -0.0020 -0.0715 33  ILE A CD1 
286  N  N   . ASP A 34  ? 0.1639 0.1254 0.0909 0.0241  0.0000  0.0273  34  ASP A N   
287  C  CA  . ASP A 34  ? 0.1782 0.1330 0.1091 0.0179  0.0038  0.0222  34  ASP A CA  
288  C  C   . ASP A 34  ? 0.1890 0.1411 0.0933 0.0242  0.0113  0.0357  34  ASP A C   
289  O  O   . ASP A 34  ? 0.2633 0.1662 0.0931 0.0384  0.0368  0.0282  34  ASP A O   
290  C  CB  . ASP A 34  ? 0.2384 0.1662 0.0930 0.0229  -0.0199 0.0282  34  ASP A CB  
291  C  CG  . ASP A 34  ? 0.2447 0.2114 0.1502 0.0340  -0.0148 0.0274  34  ASP A CG  
292  O  OD1 . ASP A 34  ? 0.5365 0.1892 0.2421 0.0498  0.1412  0.0403  34  ASP A OD1 
293  O  OD2 . ASP A 34  ? 0.3668 0.2579 0.2129 0.1102  0.0028  0.0297  34  ASP A OD2 
294  N  N   . THR A 35  ? 0.1861 0.1787 0.1019 0.0243  0.0392  0.0491  35  THR A N   
295  C  CA  . THR A 35  ? 0.2129 0.1870 0.1504 0.0491  0.0725  0.0406  35  THR A CA  
296  C  C   . THR A 35  ? 0.2515 0.1507 0.1437 0.0483  0.0811  0.0297  35  THR A C   
297  O  O   . THR A 35  ? 0.2784 0.2202 0.1676 0.0812  0.0662  0.0392  35  THR A O   
298  C  CB  . THR A 35  ? 0.1874 0.1887 0.1764 0.0375  0.0302  0.0631  35  THR A CB  
299  O  OG1 . THR A 35  ? 0.2384 0.1720 0.1723 0.0214  0.0535  0.0368  35  THR A OG1 
300  C  CG2 . THR A 35  ? 0.2556 0.1993 0.1630 0.0196  0.0383  0.0662  35  THR A CG2 
301  N  N   . HIS A 36  ? 0.2852 0.1535 0.1283 0.0320  0.0685  0.0538  36  HIS A N   
302  C  CA  . HIS A 36  ? 0.3427 0.1796 0.1391 0.0436  0.0692  0.0860  36  HIS A CA  
303  C  C   . HIS A 36  ? 0.4352 0.2854 0.1206 0.0317  0.0410  -0.0088 36  HIS A C   
304  O  O   . HIS A 36  ? 0.2685 0.2786 0.1888 0.0689  0.0068  -0.0120 36  HIS A O   
305  C  CB  . HIS A 36  ? 0.3668 0.2361 0.1172 0.0428  0.0239  0.0820  36  HIS A CB  
306  C  CG  . HIS A 36  ? 0.3978 0.1452 0.2064 0.0412  0.0582  0.0342  36  HIS A CG  
307  N  ND1 . HIS A 36  ? 0.4296 0.2953 0.2333 -0.0832 -0.0362 0.0947  36  HIS A ND1 
308  C  CD2 . HIS A 36  ? 0.3371 0.2213 0.1644 0.1024  -0.0489 0.0296  36  HIS A CD2 
309  C  CE1 . HIS A 36  ? 0.5343 0.2355 0.3249 -0.0122 -0.0348 0.0320  36  HIS A CE1 
310  N  NE2 . HIS A 36  ? 0.4526 0.3203 0.2998 0.0846  -0.0711 0.0930  36  HIS A NE2 
311  N  N   . THR A 37  ? 0.3215 0.1933 0.1805 0.0829  0.0640  -0.0173 37  THR A N   
312  C  CA  . THR A 37  ? 0.3228 0.2082 0.1718 0.0939  0.0157  0.0768  37  THR A CA  
313  C  C   . THR A 37  ? 0.2937 0.2204 0.1563 0.1171  0.0118  0.0026  37  THR A C   
314  O  O   . THR A 37  ? 0.4573 0.2260 0.1793 0.1169  -0.0538 -0.0172 37  THR A O   
315  C  CB  . THR A 37  ? 0.3436 0.2424 0.3122 0.1331  -0.0441 0.0623  37  THR A CB  
316  O  OG1 . THR A 37  ? 0.6693 0.7412 0.5278 -0.1568 0.0934  -0.0322 37  THR A OG1 
317  C  CG2 . THR A 37  ? 0.3474 0.2165 0.2718 0.0850  -0.0471 0.0542  37  THR A CG2 
318  N  N   . ALA A 38  ? 0.2256 0.1799 0.1283 0.0671  0.0308  0.0324  38  ALA A N   
319  C  CA  . ALA A 38  ? 0.2359 0.1525 0.1116 0.0465  0.0335  0.0259  38  ALA A CA  
320  C  C   . ALA A 38  ? 0.2477 0.1914 0.2450 0.0529  0.0507  -0.0366 38  ALA A C   
321  O  O   . ALA A 38  ? 0.2960 0.2791 0.3544 0.0210  0.0847  -0.0335 38  ALA A O   
322  C  CB  . ALA A 38  ? 0.2104 0.1739 0.1421 0.0291  -0.0127 0.0348  38  ALA A CB  
323  N  N   . LYS A 39  ? 0.3093 0.2224 0.1673 0.1189  0.0074  -0.0240 39  LYS A N   
324  C  CA  . LYS A 39  ? 0.3808 0.3386 0.1347 0.1711  0.0469  -0.0372 39  LYS A CA  
325  C  C   . LYS A 39  ? 0.2254 0.2682 0.1190 0.0456  -0.0023 -0.0253 39  LYS A C   
326  O  O   . LYS A 39  ? 0.1583 0.2520 0.1342 0.0109  0.0116  -0.0381 39  LYS A O   
327  C  CB  . LYS A 39  ? 0.2755 0.3082 0.2089 0.0540  0.0285  0.0142  39  LYS A CB  
328  C  CG  . LYS A 39  ? 0.4792 0.4992 0.4469 0.2002  -0.2459 -0.0489 39  LYS A CG  
329  C  CD  . LYS A 39  ? 0.4158 0.3278 0.3639 0.1641  -0.1614 -0.0285 39  LYS A CD  
330  C  CE  . LYS A 39  ? 0.5081 0.2869 0.3257 0.0824  -0.0384 0.0291  39  LYS A CE  
331  N  NZ  . LYS A 39  ? 0.2802 0.4260 0.3980 0.1002  0.0000  0.1591  39  LYS A NZ  
332  N  N   . TYR A 40  ? 0.2660 0.2387 0.1499 0.0322  0.0388  -0.0020 40  TYR A N   
333  C  CA  . TYR A 40  ? 0.1869 0.2177 0.1651 0.0021  0.0498  -0.0010 40  TYR A CA  
334  C  C   . TYR A 40  ? 0.1897 0.2344 0.1324 0.0147  0.0183  -0.0078 40  TYR A C   
335  O  O   . TYR A 40  ? 0.2238 0.2549 0.1308 0.0296  0.0223  -0.0225 40  TYR A O   
336  C  CB  . TYR A 40  ? 0.2623 0.2605 0.1567 -0.0912 0.0337  0.0140  40  TYR A CB  
337  C  CG  . TYR A 40  ? 0.2278 0.3512 0.1939 -0.0898 0.0520  0.0001  40  TYR A CG  
338  C  CD1 . TYR A 40  ? 0.2675 0.2635 0.1973 -0.0790 0.0300  -0.0021 40  TYR A CD1 
339  C  CD2 . TYR A 40  ? 0.3445 0.4187 0.1947 -0.0194 0.0887  -0.0351 40  TYR A CD2 
340  C  CE1 . TYR A 40  ? 0.2327 0.4257 0.1649 -0.0357 0.0233  0.0234  40  TYR A CE1 
341  C  CE2 . TYR A 40  ? 0.3524 0.5465 0.1779 0.0005  0.1014  -0.0309 40  TYR A CE2 
342  C  CZ  . TYR A 40  ? 0.3014 0.5519 0.2199 0.0168  0.0754  -0.0283 40  TYR A CZ  
343  O  OH  . TYR A 40  ? 0.3425 0.6276 0.3027 0.0593  0.0548  -0.0954 40  TYR A OH  
344  N  N   . ASP A 41  ? 0.1682 0.1955 0.1508 0.0322  0.0384  -0.0118 41  ASP A N   
345  C  CA  . ASP A 41  ? 0.1475 0.2170 0.1764 0.0233  0.0229  -0.0020 41  ASP A CA  
346  C  C   . ASP A 41  ? 0.1520 0.2878 0.1800 0.0253  0.0344  -0.0295 41  ASP A C   
347  O  O   . ASP A 41  ? 0.1791 0.2939 0.1896 0.0307  0.0027  0.0000  41  ASP A O   
348  C  CB  . ASP A 41  ? 0.2287 0.2169 0.1923 -0.0195 -0.0209 -0.0243 41  ASP A CB  
349  C  CG  . ASP A 41  ? 0.2158 0.2470 0.2272 0.0068  -0.0408 -0.0074 41  ASP A CG  
350  O  OD1 . ASP A 41  ? 0.2739 0.2569 0.2102 0.0384  -0.0193 -0.0450 41  ASP A OD1 
351  O  OD2 . ASP A 41  ? 0.2763 0.2732 0.2354 -0.0260 -0.0331 -0.0485 41  ASP A OD2 
352  N  N   A PRO A 42  ? 0.1659 0.2976 0.1727 0.0432  0.0315  -0.0388 42  PRO A N   
353  N  N   B PRO A 42  ? 0.1809 0.3325 0.1987 0.0135  0.0573  0.0076  42  PRO A N   
354  C  CA  A PRO A 42  ? 0.1712 0.3652 0.2375 0.0698  0.0286  0.0157  42  PRO A CA  
355  C  CA  B PRO A 42  ? 0.1789 0.4074 0.2752 0.0597  0.0781  0.0131  42  PRO A CA  
356  C  C   A PRO A 42  ? 0.2646 0.3395 0.2822 0.0820  0.0044  0.0419  42  PRO A C   
357  C  C   B PRO A 42  ? 0.2026 0.3707 0.1962 0.1092  0.1084  -0.0019 42  PRO A C   
358  O  O   A PRO A 42  ? 0.2425 0.4368 0.3181 0.1360  0.0564  -0.0328 42  PRO A O   
359  O  O   B PRO A 42  ? 0.2678 0.3549 0.3512 0.1182  0.0379  0.0320  42  PRO A O   
360  C  CB  A PRO A 42  ? 0.2587 0.3592 0.2188 0.0747  0.0666  -0.0259 42  PRO A CB  
361  C  CB  B PRO A 42  ? 0.3479 0.4262 0.3109 0.1288  0.1677  0.0143  42  PRO A CB  
362  C  CG  A PRO A 42  ? 0.2685 0.3075 0.1439 0.0769  0.0772  -0.0342 42  PRO A CG  
363  C  CG  B PRO A 42  ? 0.2460 0.4244 0.2881 0.0940  0.1062  0.0511  42  PRO A CG  
364  C  CD  A PRO A 42  ? 0.2565 0.2285 0.1418 0.0261  0.0500  -0.0803 42  PRO A CD  
365  C  CD  B PRO A 42  ? 0.2930 0.3433 0.1655 0.0417  0.1256  0.0031  42  PRO A CD  
366  N  N   . SER A 43  ? 0.2526 0.3156 0.2705 0.1036  0.0044  -0.0359 43  SER A N   
367  C  CA  . SER A 43  ? 0.3370 0.2904 0.3036 0.0830  0.0211  -0.0355 43  SER A CA  
368  C  C   . SER A 43  ? 0.2626 0.3244 0.2976 0.1456  0.0179  -0.0010 43  SER A C   
369  O  O   . SER A 43  ? 0.4950 0.3012 0.3908 0.1701  0.0403  0.0013  43  SER A O   
370  C  CB  . SER A 43  ? 0.3118 0.3095 0.3982 0.0445  0.0275  -0.0610 43  SER A CB  
371  O  OG  . SER A 43  ? 0.3887 0.3276 0.3070 0.0102  -0.0194 -0.1130 43  SER A OG  
372  N  N   . LEU A 44  ? 0.2702 0.3316 0.2310 0.0834  0.0320  -0.0129 44  LEU A N   
373  C  CA  . LEU A 44  ? 0.1985 0.4079 0.2224 0.0282  -0.0524 -0.0020 44  LEU A CA  
374  C  C   . LEU A 44  ? 0.1960 0.6055 0.2606 -0.0456 -0.0461 0.1203  44  LEU A C   
375  O  O   . LEU A 44  ? 0.2032 0.7405 0.3792 -0.0750 0.0918  0.0060  44  LEU A O   
376  C  CB  . LEU A 44  ? 0.1606 0.3711 0.1804 -0.0461 0.0469  0.0234  44  LEU A CB  
377  C  CG  . LEU A 44  ? 0.1385 0.2734 0.2050 -0.0454 0.0438  -0.0163 44  LEU A CG  
378  C  CD1 . LEU A 44  ? 0.2597 0.2529 0.1495 -0.0627 0.0377  -0.0320 44  LEU A CD1 
379  C  CD2 . LEU A 44  ? 0.2073 0.2400 0.1711 -0.0214 0.0100  -0.0019 44  LEU A CD2 
380  N  N   . LYS A 45  ? 0.2326 0.4025 0.2601 0.0412  -0.0138 0.0610  45  LYS A N   
381  C  CA  . LYS A 45  ? 0.2612 0.3212 0.3790 0.0353  -0.1292 -0.1221 45  LYS A CA  
382  C  C   . LYS A 45  ? 0.2813 0.4463 0.2333 0.1031  0.0707  -0.0740 45  LYS A C   
383  O  O   . LYS A 45  ? 0.2463 0.3328 0.2755 -0.0003 0.0626  -0.0886 45  LYS A O   
384  C  CB  . LYS A 45  ? 0.2802 0.3036 0.2484 0.0700  0.0590  -0.0463 45  LYS A CB  
385  C  CG  . LYS A 45  ? 0.2522 0.4828 0.2272 0.1310  0.0088  -0.0693 45  LYS A CG  
386  C  CD  . LYS A 45  ? 0.6485 0.5006 0.4174 0.0296  -0.0028 -0.0052 45  LYS A CD  
387  C  CE  . LYS A 45  ? 0.8026 0.6733 0.5074 0.0991  -0.1023 -0.1521 45  LYS A CE  
388  N  NZ  . LYS A 45  ? 0.7360 0.4893 0.6568 0.2419  -0.1075 -0.0114 45  LYS A NZ  
389  N  N   . PRO A 46  ? 0.2192 0.3883 0.2824 -0.0837 0.0760  -0.0401 46  PRO A N   
390  C  CA  . PRO A 46  ? 0.1838 0.3330 0.2326 0.0057  -0.0125 -0.0010 46  PRO A CA  
391  C  C   . PRO A 46  ? 0.1541 0.2483 0.1780 0.0021  0.0271  0.0001  46  PRO A C   
392  O  O   . PRO A 46  ? 0.1281 0.3314 0.3217 -0.0384 -0.0120 0.0249  46  PRO A O   
393  C  CB  . PRO A 46  ? 0.1526 0.4300 0.3361 -0.0549 0.0377  0.0305  46  PRO A CB  
394  C  CG  . PRO A 46  ? 0.1834 0.5626 0.3819 0.0220  0.0542  -0.1217 46  PRO A CG  
395  C  CD  . PRO A 46  ? 0.2105 0.3865 0.3422 0.0724  0.0366  -0.0318 46  PRO A CD  
396  N  N   . LEU A 47  ? 0.2499 0.3136 0.2165 0.0200  -0.0317 -0.0043 47  LEU A N   
397  C  CA  . LEU A 47  ? 0.1450 0.3420 0.2658 -0.0740 0.0223  0.0141  47  LEU A CA  
398  C  C   . LEU A 47  ? 0.1457 0.2183 0.4174 -0.0625 -0.0074 0.0813  47  LEU A C   
399  O  O   . LEU A 47  ? 0.1696 0.3181 0.4641 -0.1158 -0.0584 0.1551  47  LEU A O   
400  C  CB  . LEU A 47  ? 0.2921 0.3431 0.2691 0.0970  0.1250  0.0185  47  LEU A CB  
401  C  CG  . LEU A 47  ? 0.1565 0.4729 0.4431 -0.0527 0.0432  -0.0838 47  LEU A CG  
402  C  CD1 . LEU A 47  ? 0.1513 0.3490 0.4986 0.0672  0.0297  -0.1375 47  LEU A CD1 
403  C  CD2 . LEU A 47  ? 0.1723 0.4946 0.4816 -0.1177 -0.0925 -0.0637 47  LEU A CD2 
404  N  N   . SER A 48  ? 0.1340 0.2087 0.2289 -0.0189 0.0005  0.0307  48  SER A N   
405  C  CA  . SER A 48  ? 0.1380 0.2172 0.2124 -0.0083 0.0049  0.0192  48  SER A CA  
406  C  C   . SER A 48  ? 0.1163 0.2282 0.1999 -0.0088 0.0098  -0.0120 48  SER A C   
407  O  O   . SER A 48  ? 0.1696 0.1946 0.2196 -0.0348 0.0217  -0.0153 48  SER A O   
408  C  CB  . SER A 48  ? 0.1610 0.2341 0.2312 -0.0120 0.0032  0.0245  48  SER A CB  
409  O  OG  . SER A 48  ? 0.1929 0.2630 0.2969 0.0320  -0.0096 0.0482  48  SER A OG  
410  N  N   . VAL A 49  ? 0.1768 0.2134 0.2136 -0.0456 -0.0073 -0.0071 49  VAL A N   
411  C  CA  . VAL A 49  ? 0.1958 0.2299 0.2427 -0.0537 0.0048  -0.0456 49  VAL A CA  
412  C  C   . VAL A 49  ? 0.2208 0.2931 0.2538 -0.0712 -0.0082 -0.0498 49  VAL A C   
413  O  O   . VAL A 49  ? 0.2120 0.4199 0.2502 -0.1592 -0.0271 -0.0003 49  VAL A O   
414  C  CB  . VAL A 49  ? 0.2145 0.3000 0.2964 -0.0680 0.0542  -0.0799 49  VAL A CB  
415  C  CG1 . VAL A 49  ? 0.3388 0.2727 0.3605 -0.0995 0.1386  -0.0710 49  VAL A CG1 
416  C  CG2 . VAL A 49  ? 0.1845 0.2678 0.3732 -0.0573 0.0812  -0.0643 49  VAL A CG2 
417  N  N   . SER A 50  ? 0.1912 0.2436 0.2542 -0.0478 0.0068  -0.0291 50  SER A N   
418  C  CA  . SER A 50  ? 0.1472 0.3409 0.3492 -0.0154 0.0020  -0.0430 50  SER A CA  
419  C  C   . SER A 50  ? 0.1305 0.3190 0.2727 -0.0282 -0.0837 -0.0143 50  SER A C   
420  O  O   . SER A 50  ? 0.1887 0.2377 0.2987 -0.0082 -0.0489 0.0175  50  SER A O   
421  C  CB  . SER A 50  ? 0.3544 0.3303 0.4210 0.0275  0.0405  -0.0566 50  SER A CB  
422  O  OG  . SER A 50  ? 0.3612 0.4384 0.4460 0.0203  -0.0164 -0.0540 50  SER A OG  
423  N  N   . TYR A 51  ? 0.1689 0.2554 0.2854 -0.0217 -0.0684 -0.0176 51  TYR A N   
424  C  CA  . TYR A 51  ? 0.2384 0.3075 0.2524 -0.0010 -0.0767 -0.0211 51  TYR A CA  
425  C  C   . TYR A 51  ? 0.2745 0.2928 0.3244 0.0175  -0.0675 0.0278  51  TYR A C   
426  O  O   . TYR A 51  ? 0.2694 0.3323 0.2513 0.0103  -0.1054 0.0068  51  TYR A O   
427  C  CB  . TYR A 51  ? 0.1746 0.3194 0.2134 -0.0051 -0.0427 -0.0307 51  TYR A CB  
428  C  CG  . TYR A 51  ? 0.1831 0.2450 0.1836 -0.0430 -0.0340 0.0093  51  TYR A CG  
429  C  CD1 . TYR A 51  ? 0.1737 0.2197 0.2231 0.0057  -0.0401 -0.0055 51  TYR A CD1 
430  C  CD2 . TYR A 51  ? 0.2107 0.2334 0.1689 -0.0074 -0.0226 0.0043  51  TYR A CD2 
431  C  CE1 . TYR A 51  ? 0.1588 0.2219 0.1651 -0.0126 -0.0082 0.0131  51  TYR A CE1 
432  C  CE2 . TYR A 51  ? 0.2037 0.1949 0.1775 -0.0395 -0.0200 0.0087  51  TYR A CE2 
433  C  CZ  . TYR A 51  ? 0.1335 0.2028 0.1831 -0.0137 -0.0091 0.0019  51  TYR A CZ  
434  O  OH  . TYR A 51  ? 0.1500 0.1825 0.1872 -0.0234 -0.0164 -0.0098 51  TYR A OH  
435  N  N   A ASP A 52  ? 0.2485 0.3179 0.3837 -0.0170 -0.0456 -0.0006 52  ASP A N   
436  N  N   B ASP A 52  ? 0.2472 0.3368 0.3558 -0.0088 -0.0599 0.0066  52  ASP A N   
437  C  CA  A ASP A 52  ? 0.2960 0.3815 0.3323 0.0608  -0.0038 0.0859  52  ASP A CA  
438  C  CA  B ASP A 52  ? 0.3018 0.4228 0.3510 0.0546  -0.0458 0.0895  52  ASP A CA  
439  C  C   A ASP A 52  ? 0.3190 0.2556 0.3517 0.0417  -0.0720 0.0544  52  ASP A C   
440  C  C   B ASP A 52  ? 0.3014 0.4234 0.3959 -0.0507 -0.1500 0.0934  52  ASP A C   
441  O  O   A ASP A 52  ? 0.2488 0.4041 0.4557 0.0498  -0.2093 0.0671  52  ASP A O   
442  O  O   B ASP A 52  ? 0.3747 0.5447 0.3858 -0.0454 -0.0993 0.1556  52  ASP A O   
443  C  CB  A ASP A 52  ? 0.2427 0.4729 0.4548 0.1999  -0.1031 -0.0217 52  ASP A CB  
444  C  CB  B ASP A 52  ? 0.3339 0.4332 0.5081 0.0555  0.0310  0.0161  52  ASP A CB  
445  C  CG  A ASP A 52  ? 0.3416 0.5029 0.5267 0.1076  -0.0153 -0.0471 52  ASP A CG  
446  C  CG  B ASP A 52  ? 0.3705 0.4113 0.4438 0.0505  0.1017  0.2272  52  ASP A CG  
447  O  OD1 A ASP A 52  ? 0.3411 0.6761 0.5267 0.0410  -0.0035 -0.0233 52  ASP A OD1 
448  O  OD1 B ASP A 52  ? 0.2768 0.4607 0.5127 0.1815  0.1482  0.1498  52  ASP A OD1 
449  O  OD2 A ASP A 52  ? 0.6992 0.3826 0.4959 0.0509  0.1107  0.1366  52  ASP A OD2 
450  O  OD2 B ASP A 52  ? 0.2673 0.4277 0.5586 0.2164  0.0028  0.1802  52  ASP A OD2 
451  N  N   . GLN A 53  ? 0.2469 0.3406 0.4751 0.0441  -0.0522 0.0662  53  GLN A N   
452  C  CA  . GLN A 53  ? 0.2492 0.3045 0.5108 -0.0184 -0.0570 0.0549  53  GLN A CA  
453  C  C   . GLN A 53  ? 0.3018 0.2355 0.3319 0.0428  -0.0891 -0.0032 53  GLN A C   
454  O  O   . GLN A 53  ? 0.3001 0.2518 0.3287 0.0412  -0.0509 -0.0168 53  GLN A O   
455  C  CB  . GLN A 53  ? 0.2612 0.4102 0.4911 0.0716  -0.0970 -0.0899 53  GLN A CB  
456  C  CG  . GLN A 53  ? 0.2696 0.5552 0.6901 0.0021  0.0218  0.0935  53  GLN A CG  
457  C  CD  . GLN A 53  ? 0.5202 0.6929 0.6654 -0.0738 -0.0357 0.2268  53  GLN A CD  
458  O  OE1 . GLN A 53  ? 0.3998 0.7247 0.8019 0.2295  -0.1180 0.1050  53  GLN A OE1 
459  N  NE2 . GLN A 53  ? 0.4952 0.7411 0.9912 -0.1028 -0.0834 0.2084  53  GLN A NE2 
460  N  N   . ALA A 54  ? 0.3330 0.2324 0.2554 0.0557  -0.0575 -0.0104 54  ALA A N   
461  C  CA  . ALA A 54  ? 0.2951 0.2127 0.2630 0.0465  -0.0970 -0.0593 54  ALA A CA  
462  C  C   . ALA A 54  ? 0.2928 0.4027 0.2208 0.0595  -0.0970 -0.0658 54  ALA A C   
463  O  O   . ALA A 54  ? 0.4178 0.4068 0.3030 -0.0571 -0.1120 -0.1096 54  ALA A O   
464  C  CB  . ALA A 54  ? 0.3745 0.2166 0.3124 0.0513  0.0195  -0.0065 54  ALA A CB  
465  N  N   . THR A 55  ? 0.2797 0.2644 0.2389 0.0917  -0.0835 0.0074  55  THR A N   
466  C  CA  . THR A 55  ? 0.2910 0.2409 0.2732 0.0751  -0.0723 0.0816  55  THR A CA  
467  C  C   . THR A 55  ? 0.2910 0.2061 0.1905 0.0500  -0.0491 0.0842  55  THR A C   
468  O  O   . THR A 55  ? 0.3921 0.2001 0.2219 0.0724  -0.0423 0.0856  55  THR A O   
469  C  CB  . THR A 55  ? 0.4007 0.2254 0.3653 0.0807  -0.0903 0.1319  55  THR A CB  
470  O  OG1 . THR A 55  ? 0.5052 0.2395 0.3867 0.1018  -0.1468 0.0304  55  THR A OG1 
471  C  CG2 . THR A 55  ? 0.5649 0.2845 0.3260 0.1677  -0.0698 0.1102  55  THR A CG2 
472  N  N   . SER A 56  ? 0.3855 0.2008 0.1814 0.0390  -0.1040 0.0740  56  SER A N   
473  C  CA  . SER A 56  ? 0.4077 0.1899 0.1687 0.0253  -0.0793 0.0375  56  SER A CA  
474  C  C   . SER A 56  ? 0.4377 0.2732 0.1639 0.0874  -0.0568 0.0623  56  SER A C   
475  O  O   . SER A 56  ? 0.5533 0.2439 0.1947 0.1150  -0.1292 0.0671  56  SER A O   
476  C  CB  . SER A 56  ? 0.4122 0.1948 0.1391 0.0245  -0.0922 0.0144  56  SER A CB  
477  O  OG  . SER A 56  ? 0.4327 0.2594 0.1736 0.0293  -0.1358 0.0526  56  SER A OG  
478  N  N   . LEU A 57  ? 0.4088 0.1517 0.1554 0.0644  -0.0377 0.0359  57  LEU A N   
479  C  CA  . LEU A 57  ? 0.4972 0.1969 0.2467 0.1076  0.0271  0.1083  57  LEU A CA  
480  C  C   . LEU A 57  ? 0.4368 0.1756 0.1536 0.0582  0.0159  0.0715  57  LEU A C   
481  O  O   . LEU A 57  ? 0.4824 0.2084 0.1419 0.0454  -0.0177 0.0883  57  LEU A O   
482  C  CB  . LEU A 57  ? 0.5963 0.3014 0.2777 0.0249  0.0496  0.1288  57  LEU A CB  
483  C  CG  . LEU A 57  ? 0.5231 0.2601 0.3255 0.0190  -0.0496 0.0666  57  LEU A CG  
484  C  CD1 . LEU A 57  ? 0.4539 0.3862 0.2768 -0.1191 0.0731  0.0359  57  LEU A CD1 
485  C  CD2 . LEU A 57  ? 0.6355 0.2545 0.2310 0.0901  -0.0775 0.0601  57  LEU A CD2 
486  N  N   . ARG A 58  ? 0.5105 0.2089 0.1648 0.0696  -0.0566 0.0615  58  ARG A N   
487  C  CA  . ARG A 58  ? 0.4174 0.1632 0.1646 0.0357  -0.0315 0.0557  58  ARG A CA  
488  C  C   . ARG A 58  ? 0.3603 0.2095 0.1143 0.0236  -0.0171 0.0526  58  ARG A C   
489  O  O   . ARG A 58  ? 0.4101 0.1930 0.1193 0.0663  -0.0275 0.0449  58  ARG A O   
490  C  CB  . ARG A 58  ? 0.5002 0.1649 0.2531 -0.0175 -0.1369 0.0671  58  ARG A CB  
491  C  CG  . ARG A 58  ? 0.2655 0.7491 0.3815 -0.1819 0.1435  -0.1190 58  ARG A CG  
492  C  CD  . ARG A 58  ? 0.3887 0.3984 0.2055 -0.1212 0.0245  0.1071  58  ARG A CD  
493  N  NE  . ARG A 58  ? 0.2597 0.2664 0.3057 -0.0267 0.0204  0.0824  58  ARG A NE  
494  C  CZ  . ARG A 58  ? 0.2671 0.4203 0.2520 -0.1301 -0.0362 0.1788  58  ARG A CZ  
495  N  NH1 . ARG A 58  ? 0.3366 0.2490 0.2946 -0.0505 0.0702  0.0780  58  ARG A NH1 
496  N  NH2 . ARG A 58  ? 0.2757 0.2768 0.2630 -0.0304 -0.0170 0.0627  58  ARG A NH2 
497  N  N   . ILE A 59  ? 0.3776 0.1836 0.1071 0.0223  -0.0087 0.0439  59  ILE A N   
498  C  CA  . ILE A 59  ? 0.3750 0.1703 0.1212 -0.0052 -0.0232 0.0549  59  ILE A CA  
499  C  C   . ILE A 59  ? 0.3027 0.1592 0.1195 -0.0215 -0.0575 0.0357  59  ILE A C   
500  O  O   . ILE A 59  ? 0.3607 0.2310 0.0974 -0.0046 -0.0342 0.0520  59  ILE A O   
501  C  CB  . ILE A 59  ? 0.3531 0.1565 0.1129 0.0086  -0.0306 0.0286  59  ILE A CB  
502  C  CG1 . ILE A 59  ? 0.3165 0.1823 0.1116 0.0059  -0.0333 0.0441  59  ILE A CG1 
503  C  CG2 . ILE A 59  ? 0.3504 0.1811 0.1067 0.0070  -0.0584 0.0315  59  ILE A CG2 
504  C  CD1 . ILE A 59  ? 0.3111 0.1712 0.1342 0.0251  -0.0212 0.0132  59  ILE A CD1 
505  N  N   . LEU A 60  ? 0.3422 0.1680 0.1404 -0.0073 -0.0692 0.0219  60  LEU A N   
506  C  CA  . LEU A 60  ? 0.3194 0.1534 0.1190 -0.0322 -0.0764 0.0447  60  LEU A CA  
507  C  C   . LEU A 60  ? 0.2858 0.1577 0.1170 -0.0560 -0.0294 0.0283  60  LEU A C   
508  O  O   . LEU A 60  ? 0.2845 0.1854 0.0989 -0.0551 -0.0274 0.0359  60  LEU A O   
509  C  CB  . LEU A 60  ? 0.2642 0.1572 0.2160 -0.0357 -0.0315 0.0193  60  LEU A CB  
510  C  CG  . LEU A 60  ? 0.2497 0.1484 0.1858 0.0184  -0.0217 0.0175  60  LEU A CG  
511  C  CD1 . LEU A 60  ? 0.3152 0.2353 0.1870 -0.0855 -0.0138 0.0701  60  LEU A CD1 
512  C  CD2 . LEU A 60  ? 0.3206 0.1678 0.2429 -0.0489 -0.0542 -0.0020 60  LEU A CD2 
513  N  N   . ASN A 61  ? 0.2484 0.1446 0.1301 -0.0562 -0.0421 0.0460  61  ASN A N   
514  C  CA  . ASN A 61  ? 0.2454 0.1847 0.1111 -0.0822 -0.0062 0.0038  61  ASN A CA  
515  C  C   . ASN A 61  ? 0.2685 0.1957 0.1231 -0.1145 -0.0031 -0.0038 61  ASN A C   
516  O  O   . ASN A 61  ? 0.3476 0.1859 0.1544 -0.1271 -0.0260 0.0538  61  ASN A O   
517  C  CB  . ASN A 61  ? 0.2746 0.1953 0.0967 -0.0696 0.0178  0.0010  61  ASN A CB  
518  C  CG  . ASN A 61  ? 0.2016 0.1933 0.0987 -0.0948 0.0187  0.0027  61  ASN A CG  
519  O  OD1 . ASN A 61  ? 0.2422 0.2220 0.1186 -0.1072 0.0208  -0.0038 61  ASN A OD1 
520  N  ND2 . ASN A 61  ? 0.2109 0.1861 0.1418 -0.1010 0.0283  -0.0120 61  ASN A ND2 
521  N  N   . ASN A 62  ? 0.3226 0.1502 0.1256 -0.0822 -0.0428 0.0017  62  ASN A N   
522  C  CA  . ASN A 62  ? 0.3384 0.1689 0.2278 -0.0945 -0.0763 0.0010  62  ASN A CA  
523  C  C   . ASN A 62  ? 0.2416 0.2109 0.1350 -0.1053 -0.0048 0.0125  62  ASN A C   
524  O  O   . ASN A 62  ? 0.4255 0.3055 0.1843 -0.2273 -0.0617 0.0483  62  ASN A O   
525  C  CB  . ASN A 62  ? 0.4941 0.1741 0.2240 -0.0741 -0.1224 -0.0021 62  ASN A CB  
526  C  CG  . ASN A 62  ? 0.3438 0.2301 0.1827 0.0054  -0.0768 -0.0494 62  ASN A CG  
527  O  OD1 . ASN A 62  ? 0.2391 0.1493 0.1888 -0.0322 -0.0244 0.0046  62  ASN A OD1 
528  N  ND2 . ASN A 62  ? 0.4674 0.3289 0.1644 0.1479  -0.0627 -0.0104 62  ASN A ND2 
529  N  N   . GLY A 63  ? 0.2833 0.2066 0.1326 -0.1027 0.0527  -0.0028 63  GLY A N   
530  C  CA  . GLY A 63  ? 0.2517 0.2502 0.1759 -0.1336 0.0361  0.0160  63  GLY A CA  
531  C  C   . GLY A 63  ? 0.1942 0.1773 0.1638 -0.0834 0.0296  -0.0195 63  GLY A C   
532  O  O   . GLY A 63  ? 0.2120 0.2635 0.2192 -0.0711 0.0445  -0.0568 63  GLY A O   
533  N  N   . HIS A 64  ? 0.1883 0.1747 0.1465 -0.0566 0.0205  0.0013  64  HIS A N   
534  C  CA  . HIS A 64  ? 0.1644 0.1755 0.1328 -0.0412 0.0156  0.0331  64  HIS A CA  
535  C  C   . HIS A 64  ? 0.1687 0.1531 0.1595 -0.0326 0.0177  0.0234  64  HIS A C   
536  O  O   . HIS A 64  ? 0.1847 0.1951 0.3449 -0.0478 -0.0207 0.1237  64  HIS A O   
537  C  CB  . HIS A 64  ? 0.1914 0.2175 0.1385 -0.0610 0.0034  0.0197  64  HIS A CB  
538  C  CG  . HIS A 64  ? 0.1886 0.2152 0.1764 -0.0298 0.0097  -0.0143 64  HIS A CG  
539  N  ND1 . HIS A 64  ? 0.1901 0.2843 0.2106 -0.0298 0.0340  -0.0454 64  HIS A ND1 
540  C  CD2 . HIS A 64  ? 0.2755 0.2515 0.1884 -0.0929 -0.0048 0.0041  64  HIS A CD2 
541  C  CE1 . HIS A 64  ? 0.1920 0.3314 0.2335 -0.0571 0.0644  -0.0342 64  HIS A CE1 
542  N  NE2 . HIS A 64  ? 0.2059 0.3445 0.2736 -0.0590 0.0160  -0.0377 64  HIS A NE2 
543  N  N   A SER A 65  ? 0.1486 0.1556 0.1401 -0.0520 0.0196  -0.0035 65  SER A N   
544  N  N   B SER A 65  ? 0.1683 0.1621 0.1181 -0.0430 0.0291  0.0239  65  SER A N   
545  C  CA  A SER A 65  ? 0.1445 0.1112 0.1165 -0.0109 0.0081  -0.0120 65  SER A CA  
546  C  CA  B SER A 65  ? 0.1811 0.1313 0.1290 -0.0209 0.0110  0.0344  65  SER A CA  
547  C  C   A SER A 65  ? 0.1797 0.1288 0.1008 -0.0221 0.0088  0.0093  65  SER A C   
548  C  C   B SER A 65  ? 0.1903 0.1254 0.0644 -0.0362 0.0166  0.0006  65  SER A C   
549  O  O   A SER A 65  ? 0.1523 0.1237 0.1197 0.0006  0.0160  0.0108  65  SER A O   
550  O  O   B SER A 65  ? 0.1644 0.1057 0.1172 0.0226  0.0355  0.0403  65  SER A O   
551  C  CB  A SER A 65  ? 0.1398 0.1233 0.0992 -0.0167 0.0088  -0.0046 65  SER A CB  
552  C  CB  B SER A 65  ? 0.1981 0.1583 0.1321 -0.0162 0.0192  0.0274  65  SER A CB  
553  O  OG  A SER A 65  ? 0.1498 0.1493 0.0969 -0.0311 -0.0020 0.0498  65  SER A OG  
554  O  OG  B SER A 65  ? 0.2260 0.1984 0.1091 -0.0044 -0.0153 0.0310  65  SER A OG  
555  N  N   . PHE A 66  ? 0.1764 0.1387 0.1097 -0.0306 0.0005  0.0147  66  PHE A N   
556  C  CA  . PHE A 66  ? 0.2046 0.1594 0.0991 -0.0068 -0.0227 0.0092  66  PHE A CA  
557  C  C   . PHE A 66  ? 0.2206 0.1312 0.0939 -0.0154 -0.0247 0.0154  66  PHE A C   
558  O  O   . PHE A 66  ? 0.1976 0.1572 0.0985 -0.0193 -0.0107 0.0030  66  PHE A O   
559  C  CB  . PHE A 66  ? 0.2169 0.1674 0.0996 -0.0102 -0.0186 -0.0001 66  PHE A CB  
560  C  CG  . PHE A 66  ? 0.2149 0.1614 0.1199 -0.0333 -0.0116 -0.0254 66  PHE A CG  
561  C  CD1 . PHE A 66  ? 0.1999 0.1888 0.1012 -0.0285 -0.0288 0.0031  66  PHE A CD1 
562  C  CD2 . PHE A 66  ? 0.1680 0.1687 0.1360 -0.0154 -0.0019 -0.0461 66  PHE A CD2 
563  C  CE1 . PHE A 66  ? 0.2314 0.1615 0.1545 -0.0261 -0.0189 -0.0203 66  PHE A CE1 
564  C  CE2 . PHE A 66  ? 0.1845 0.1777 0.1357 -0.0366 -0.0261 -0.0373 66  PHE A CE2 
565  C  CZ  . PHE A 66  ? 0.1714 0.1807 0.1036 -0.0342 -0.0296 -0.0187 66  PHE A CZ  
566  N  N   . GLN A 67  ? 0.2509 0.1473 0.1199 -0.0093 -0.0272 0.0236  67  GLN A N   
567  C  CA  . GLN A 67  ? 0.2757 0.1256 0.1222 -0.0031 -0.0357 0.0092  67  GLN A CA  
568  C  C   . GLN A 67  ? 0.2777 0.1534 0.1125 -0.0141 -0.0551 0.0537  67  GLN A C   
569  O  O   . GLN A 67  ? 0.3517 0.2477 0.0900 0.0291  -0.0162 0.0529  67  GLN A O   
570  C  CB  . GLN A 67  ? 0.4264 0.2138 0.1427 -0.0741 -0.0768 0.0474  67  GLN A CB  
571  C  CG  . GLN A 67  ? 0.3104 0.2393 0.1623 -0.0964 -0.0189 0.0142  67  GLN A CG  
572  C  CD  . GLN A 67  ? 0.2736 0.2888 0.2883 -0.0918 -0.0929 0.0458  67  GLN A CD  
573  O  OE1 . GLN A 67  ? 0.2937 0.3768 0.3199 -0.0430 -0.1301 0.0032  67  GLN A OE1 
574  N  NE2 . GLN A 67  ? 0.4772 0.2642 0.3578 0.0019  -0.1221 -0.0582 67  GLN A NE2 
575  N  N   . VAL A 68  ? 0.2924 0.1484 0.1260 0.0153  -0.0394 0.0372  68  VAL A N   
576  C  CA  . VAL A 68  ? 0.2967 0.1696 0.0857 0.0874  -0.0370 0.0060  68  VAL A CA  
577  C  C   . VAL A 68  ? 0.3497 0.1543 0.1040 0.0471  -0.0137 0.0242  68  VAL A C   
578  O  O   . VAL A 68  ? 0.3341 0.1374 0.1064 0.0441  -0.0109 0.0280  68  VAL A O   
579  C  CB  . VAL A 68  ? 0.3064 0.1942 0.1362 0.0681  -0.0672 -0.0074 68  VAL A CB  
580  C  CG1 . VAL A 68  ? 0.3418 0.2275 0.1477 0.1054  -0.0813 0.0019  68  VAL A CG1 
581  C  CG2 . VAL A 68  ? 0.2820 0.1854 0.1224 0.0258  -0.0186 0.0131  68  VAL A CG2 
582  N  N   . GLU A 69  ? 0.4257 0.1561 0.1014 0.0942  -0.0227 0.0346  69  GLU A N   
583  C  CA  . GLU A 69  ? 0.3592 0.1656 0.1310 0.0487  0.0307  0.0366  69  GLU A CA  
584  C  C   . GLU A 69  ? 0.3794 0.1315 0.1883 0.0614  -0.0604 0.0430  69  GLU A C   
585  O  O   . GLU A 69  ? 0.3413 0.1784 0.1779 0.0496  -0.0357 0.0586  69  GLU A O   
586  C  CB  . GLU A 69  ? 0.2569 0.2964 0.1836 0.0263  0.0141  0.0040  69  GLU A CB  
587  C  CG  . GLU A 69  ? 0.2332 0.2522 0.2012 -0.0326 0.0364  0.0540  69  GLU A CG  
588  C  CD  . GLU A 69  ? 0.2159 0.2224 0.2258 -0.0071 0.0240  0.0218  69  GLU A CD  
589  O  OE1 . GLU A 69  ? 0.3529 0.2759 0.2439 -0.0105 0.0487  0.0975  69  GLU A OE1 
590  O  OE2 . GLU A 69  ? 0.2361 0.2822 0.3925 0.0127  0.0533  0.0507  69  GLU A OE2 
591  N  N   . PHE A 70  ? 0.3504 0.1455 0.1527 0.0436  0.0043  0.0491  70  PHE A N   
592  C  CA  . PHE A 70  ? 0.2849 0.1506 0.1684 0.0073  -0.0318 0.0533  70  PHE A CA  
593  C  C   . PHE A 70  ? 0.2827 0.1632 0.1787 0.0328  -0.0008 0.0710  70  PHE A C   
594  O  O   . PHE A 70  ? 0.3030 0.1486 0.2366 0.0339  0.0109  0.0837  70  PHE A O   
595  C  CB  . PHE A 70  ? 0.2822 0.1349 0.1592 0.0242  -0.0414 0.0318  70  PHE A CB  
596  C  CG  . PHE A 70  ? 0.2624 0.1562 0.1481 0.0381  -0.0710 0.0362  70  PHE A CG  
597  C  CD1 . PHE A 70  ? 0.2632 0.1402 0.1547 0.0443  -0.0432 0.0544  70  PHE A CD1 
598  C  CD2 . PHE A 70  ? 0.2420 0.1407 0.1495 0.0359  -0.0546 0.0318  70  PHE A CD2 
599  C  CE1 . PHE A 70  ? 0.2592 0.1674 0.1457 0.0450  -0.0256 0.0333  70  PHE A CE1 
600  C  CE2 . PHE A 70  ? 0.3109 0.1538 0.1642 0.0421  -0.0715 0.0251  70  PHE A CE2 
601  C  CZ  . PHE A 70  ? 0.2470 0.1545 0.1732 0.0320  0.0007  0.0262  70  PHE A CZ  
602  N  N   . ASP A 71  ? 0.4074 0.1606 0.2590 0.0678  -0.0399 0.1102  71  ASP A N   
603  C  CA  . ASP A 71  ? 0.3474 0.1483 0.2456 0.0564  -0.0140 0.0829  71  ASP A CA  
604  C  C   . ASP A 71  ? 0.3614 0.1238 0.3258 0.0744  -0.0562 0.0154  71  ASP A C   
605  O  O   . ASP A 71  ? 0.4185 0.1978 0.4745 0.0125  0.0410  0.0790  71  ASP A O   
606  C  CB  . ASP A 71  ? 0.3865 0.2079 0.2928 0.1049  -0.0238 0.0947  71  ASP A CB  
607  C  CG  . ASP A 71  ? 0.3948 0.1832 0.4212 0.0815  -0.1228 0.0441  71  ASP A CG  
608  O  OD1 . ASP A 71  ? 0.4101 0.1969 0.4537 0.0553  -0.0531 0.1456  71  ASP A OD1 
609  O  OD2 . ASP A 71  ? 0.4056 0.2752 0.3894 0.0524  -0.1293 0.0017  71  ASP A OD2 
610  N  N   . ASP A 72  ? 0.3170 0.1488 0.3195 0.0452  0.0105  0.0856  72  ASP A N   
611  C  CA  . ASP A 72  ? 0.2969 0.1784 0.2922 -0.0017 0.0531  0.0368  72  ASP A CA  
612  C  C   . ASP A 72  ? 0.3574 0.1576 0.3490 0.0162  0.0241  0.0678  72  ASP A C   
613  O  O   . ASP A 72  ? 0.4892 0.1621 0.4550 0.0480  -0.0998 0.0665  72  ASP A O   
614  C  CB  . ASP A 72  ? 0.4232 0.1709 0.3210 0.0652  0.0478  0.0944  72  ASP A CB  
615  C  CG  . ASP A 72  ? 0.4018 0.2272 0.3134 0.0646  -0.0286 0.1212  72  ASP A CG  
616  O  OD1 . ASP A 72  ? 0.4763 0.4435 0.3668 0.0612  0.0114  0.2581  72  ASP A OD1 
617  O  OD2 . ASP A 72  ? 0.3619 0.3068 0.3519 0.0458  -0.0010 0.1310  72  ASP A OD2 
618  N  N   . SER A 73  ? 0.3544 0.1533 0.4359 0.0311  0.0161  0.0948  73  SER A N   
619  C  CA  . SER A 73  ? 0.4183 0.1949 0.4722 -0.0795 -0.0137 0.0848  73  SER A CA  
620  C  C   . SER A 73  ? 0.4620 0.1682 0.3770 -0.0546 -0.0041 -0.0051 73  SER A C   
621  O  O   . SER A 73  ? 0.4485 0.1507 0.4291 0.0048  -0.0828 0.0164  73  SER A O   
622  C  CB  . SER A 73  ? 0.5052 0.1693 0.4526 -0.0275 -0.0925 0.1072  73  SER A CB  
623  O  OG  . SER A 73  ? 0.3731 0.1932 0.3971 0.0262  -0.0252 0.0476  73  SER A OG  
624  N  N   . GLN A 74  ? 0.4637 0.2053 0.5009 -0.0274 0.0749  0.0658  74  GLN A N   
625  C  CA  . GLN A 74  ? 0.4675 0.3537 0.3362 0.0516  -0.0263 0.1044  74  GLN A CA  
626  C  C   . GLN A 74  ? 0.4336 0.2278 0.3849 0.0099  -0.0469 -0.0151 74  GLN A C   
627  O  O   . GLN A 74  ? 0.2606 0.2178 0.4783 0.0143  -0.0560 -0.0386 74  GLN A O   
628  C  CB  . GLN A 74  ? 0.4104 0.4936 0.6044 0.0908  -0.1509 -0.0522 74  GLN A CB  
629  C  CG  . GLN A 74  ? 0.5293 0.6722 0.5539 0.0381  -0.2415 0.0092  74  GLN A CG  
630  C  CD  . GLN A 74  ? 0.6701 0.5892 0.4282 0.1365  -0.0606 0.0820  74  GLN A CD  
631  O  OE1 . GLN A 74  ? 0.5318 0.3677 0.6779 0.0518  0.1323  0.1307  74  GLN A OE1 
632  N  NE2 . GLN A 74  ? 0.8496 0.2621 0.4217 0.0910  0.0076  0.0760  74  GLN A NE2 
633  N  N   . ASP A 75  ? 0.4498 0.2592 0.3310 0.0449  -0.1023 -0.0873 75  ASP A N   
634  C  CA  . ASP A 75  ? 0.3731 0.2985 0.5303 0.0322  -0.0804 0.0241  75  ASP A CA  
635  C  C   . ASP A 75  ? 0.3404 0.2642 0.4059 0.1802  -0.0921 -0.0339 75  ASP A C   
636  O  O   . ASP A 75  ? 0.3219 0.6827 0.6104 0.1277  -0.1541 -0.0640 75  ASP A O   
637  C  CB  . ASP A 75  ? 0.4985 0.2908 0.5274 0.0062  -0.1398 -0.0542 75  ASP A CB  
638  C  CG  . ASP A 75  ? 0.5435 0.4988 0.4120 -0.0200 -0.0223 -0.1204 75  ASP A CG  
639  O  OD1 . ASP A 75  ? 0.5565 0.6140 0.3989 0.0592  -0.1968 -0.1705 75  ASP A OD1 
640  O  OD2 . ASP A 75  ? 0.7637 0.5521 0.5386 -0.0346 0.1027  -0.2108 75  ASP A OD2 
641  N  N   A LYS A 76  ? 0.4404 0.1913 0.3722 0.0599  0.0093  0.0148  76  LYS A N   
642  N  N   B LYS A 76  ? 0.3334 0.1872 0.3235 0.0625  -0.0621 0.0066  76  LYS A N   
643  C  CA  A LYS A 76  ? 0.4101 0.2059 0.3704 0.0031  0.0149  0.0778  76  LYS A CA  
644  C  CA  B LYS A 76  ? 0.2942 0.1427 0.3869 0.0230  -0.0346 -0.0052 76  LYS A CA  
645  C  C   A LYS A 76  ? 0.3817 0.2612 0.3319 0.0952  -0.1169 0.1017  76  LYS A C   
646  C  C   B LYS A 76  ? 0.2495 0.2271 0.2522 -0.0274 -0.0756 0.0472  76  LYS A C   
647  O  O   A LYS A 76  ? 0.2955 0.3014 0.3569 0.0636  -0.1112 0.0976  76  LYS A O   
648  O  O   B LYS A 76  ? 0.2777 0.3253 0.2854 -0.0886 -0.0688 -0.0038 76  LYS A O   
649  C  CB  A LYS A 76  ? 0.3643 0.3231 0.3659 -0.1378 0.0637  0.0781  76  LYS A CB  
650  C  CB  B LYS A 76  ? 0.1143 0.2373 0.3621 -0.0082 -0.0663 0.0898  76  LYS A CB  
651  C  CG  A LYS A 76  ? 0.5113 0.3102 0.4219 -0.0540 0.0786  0.0750  76  LYS A CG  
652  C  CG  B LYS A 76  ? 0.3777 0.2045 0.3558 -0.0465 -0.0851 0.0800  76  LYS A CG  
653  C  CD  A LYS A 76  ? 0.3093 0.5074 0.4318 -0.1206 0.0168  0.0617  76  LYS A CD  
654  C  CD  B LYS A 76  ? 0.3156 0.2711 0.3402 0.0071  -0.0847 0.0544  76  LYS A CD  
655  C  CE  A LYS A 76  ? 0.2402 0.3767 0.5194 -0.0324 0.0571  -0.0098 76  LYS A CE  
656  C  CE  B LYS A 76  ? 0.2445 0.2921 0.2644 0.0507  -0.0729 -0.0010 76  LYS A CE  
657  N  NZ  A LYS A 76  ? 0.1398 0.5235 0.5442 0.1046  -0.0640 -0.1254 76  LYS A NZ  
658  N  NZ  B LYS A 76  ? 0.3246 0.2621 0.3084 0.0078  0.0496  0.0452  76  LYS A NZ  
659  N  N   A ALA A 77  ? 0.2820 0.2263 0.2233 0.0000  -0.1156 0.0687  77  ALA A N   
660  N  N   B ALA A 77  ? 0.2642 0.2583 0.2339 0.0329  -0.0617 0.0000  77  ALA A N   
661  C  CA  A ALA A 77  ? 0.2770 0.2084 0.2381 0.0196  -0.0869 0.0579  77  ALA A CA  
662  C  CA  B ALA A 77  ? 0.2671 0.2398 0.1718 -0.0190 -0.0549 -0.0174 77  ALA A CA  
663  C  C   A ALA A 77  ? 0.1854 0.2188 0.2513 -0.0035 -0.0577 0.0307  77  ALA A C   
664  C  C   B ALA A 77  ? 0.1748 0.1890 0.2202 -0.0028 -0.0681 0.0348  77  ALA A C   
665  O  O   A ALA A 77  ? 0.2023 0.2759 0.2739 -0.0277 -0.0397 -0.0024 77  ALA A O   
666  O  O   B ALA A 77  ? 0.1976 0.2500 0.2364 -0.0337 -0.0375 0.0421  77  ALA A O   
667  C  CB  A ALA A 77  ? 0.4144 0.2061 0.2488 0.0417  -0.0653 0.0657  77  ALA A CB  
668  C  CB  B ALA A 77  ? 0.2111 0.2346 0.1249 0.0035  -0.0373 0.0679  77  ALA A CB  
669  N  N   . VAL A 78  ? 0.1544 0.1974 0.2332 -0.0038 -0.0586 0.0059  78  VAL A N   
670  C  CA  . VAL A 78  ? 0.2301 0.1592 0.2215 0.0298  -0.0756 0.0397  78  VAL A CA  
671  C  C   . VAL A 78  ? 0.1683 0.1637 0.2167 -0.0049 -0.0405 0.0013  78  VAL A C   
672  O  O   . VAL A 78  ? 0.1633 0.1750 0.2759 -0.0219 -0.0463 0.0229  78  VAL A O   
673  C  CB  . VAL A 78  ? 0.1999 0.2339 0.3023 0.0049  -0.0859 -0.0275 78  VAL A CB  
674  C  CG1 . VAL A 78  ? 0.2926 0.1576 0.3553 0.0430  -0.1058 0.0020  78  VAL A CG1 
675  C  CG2 . VAL A 78  ? 0.2336 0.2560 0.3544 -0.0238 0.0020  -0.0118 78  VAL A CG2 
676  N  N   . LEU A 79  ? 0.1375 0.1648 0.1861 0.0057  -0.0220 0.0044  79  LEU A N   
677  C  CA  . LEU A 79  ? 0.1304 0.1405 0.1793 0.0035  0.0005  -0.0063 79  LEU A CA  
678  C  C   . LEU A 79  ? 0.1493 0.1386 0.1809 -0.0230 -0.0107 -0.0028 79  LEU A C   
679  O  O   . LEU A 79  ? 0.1513 0.1554 0.2149 -0.0274 -0.0010 -0.0115 79  LEU A O   
680  C  CB  . LEU A 79  ? 0.1392 0.1479 0.2230 0.0017  -0.0164 0.0082  79  LEU A CB  
681  C  CG  . LEU A 79  ? 0.1471 0.1795 0.1944 0.0098  0.0055  0.0179  79  LEU A CG  
682  C  CD1 . LEU A 79  ? 0.1479 0.2023 0.3093 0.0060  0.0035  0.0731  79  LEU A CD1 
683  C  CD2 . LEU A 79  ? 0.1726 0.1883 0.2001 0.0428  -0.0027 -0.0082 79  LEU A CD2 
684  N  N   A LYS A 80  ? 0.1509 0.1791 0.1960 -0.0049 0.0190  -0.0159 80  LYS A N   
685  N  N   B LYS A 80  ? 0.1360 0.1764 0.1836 -0.0114 0.0076  -0.0199 80  LYS A N   
686  C  CA  A LYS A 80  ? 0.1824 0.1703 0.2289 0.0065  0.0078  -0.0278 80  LYS A CA  
687  C  CA  B LYS A 80  ? 0.1437 0.1283 0.2036 -0.0379 0.0306  0.0031  80  LYS A CA  
688  C  C   A LYS A 80  ? 0.1644 0.1691 0.2396 0.0379  0.0178  -0.0161 80  LYS A C   
689  C  C   B LYS A 80  ? 0.1445 0.1377 0.2183 0.0074  0.0242  0.0179  80  LYS A C   
690  O  O   A LYS A 80  ? 0.1371 0.1860 0.2572 -0.0001 0.0187  0.0049  80  LYS A O   
691  O  O   B LYS A 80  ? 0.1221 0.1486 0.2386 -0.0049 0.0241  0.0144  80  LYS A O   
692  C  CB  A LYS A 80  ? 0.1996 0.1477 0.2567 -0.0231 0.0608  -0.0168 80  LYS A CB  
693  C  CB  B LYS A 80  ? 0.1653 0.1669 0.2362 -0.0099 -0.0138 -0.0147 80  LYS A CB  
694  C  CG  A LYS A 80  ? 0.1842 0.2248 0.3032 0.0076  0.0230  0.0138  80  LYS A CG  
695  C  CG  B LYS A 80  ? 0.2044 0.1732 0.2536 0.0071  0.0272  0.0092  80  LYS A CG  
696  C  CD  A LYS A 80  ? 0.1707 0.2718 0.3459 0.0200  0.0168  0.0494  80  LYS A CD  
697  C  CD  B LYS A 80  ? 0.3054 0.2869 0.2547 0.0768  -0.1683 -0.0309 80  LYS A CD  
698  C  CE  A LYS A 80  ? 0.3366 0.3508 0.4180 -0.0595 -0.1375 0.1281  80  LYS A CE  
699  C  CE  B LYS A 80  ? 0.2842 0.3079 0.3025 0.0375  -0.0197 -0.0381 80  LYS A CE  
700  N  NZ  A LYS A 80  ? 0.3587 0.5511 0.3977 0.0907  -0.0943 0.1042  80  LYS A NZ  
701  N  NZ  B LYS A 80  ? 0.3231 0.4165 0.3914 0.1263  0.0474  0.0644  80  LYS A NZ  
702  N  N   . GLY A 81  ? 0.1906 0.1770 0.2091 0.0071  0.0487  0.0068  81  GLY A N   
703  C  CA  . GLY A 81  ? 0.1743 0.1743 0.2424 0.0203  0.0467  0.0283  81  GLY A CA  
704  C  C   . GLY A 81  ? 0.1310 0.1775 0.2944 0.0329  0.0573  0.0109  81  GLY A C   
705  O  O   . GLY A 81  ? 0.1420 0.1872 0.2151 -0.0054 0.0505  -0.0071 81  GLY A O   
706  N  N   . GLY A 82  ? 0.1323 0.2181 0.4144 0.0010  0.0381  0.0874  82  GLY A N   
707  C  CA  . GLY A 82  ? 0.1465 0.2156 0.4415 0.0243  0.0549  0.0702  82  GLY A CA  
708  C  C   . GLY A 82  ? 0.1735 0.2481 0.3285 0.0428  0.0927  0.0509  82  GLY A C   
709  O  O   . GLY A 82  ? 0.2531 0.4320 0.3179 0.1615  0.1536  0.0760  82  GLY A O   
710  N  N   . PRO A 83  ? 0.1562 0.1944 0.2299 0.0172  0.0751  0.0308  83  PRO A N   
711  C  CA  . PRO A 83  ? 0.1893 0.2088 0.2187 0.0599  0.0434  0.0206  83  PRO A CA  
712  C  C   . PRO A 83  ? 0.1599 0.2136 0.2168 0.0395  0.0251  -0.0460 83  PRO A C   
713  O  O   . PRO A 83  ? 0.2235 0.2330 0.2500 0.0306  -0.0046 -0.0340 83  PRO A O   
714  C  CB  . PRO A 83  ? 0.1775 0.1929 0.1998 0.0461  -0.0019 0.0034  83  PRO A CB  
715  C  CG  . PRO A 83  ? 0.1290 0.1590 0.1793 0.0283  0.0303  -0.0073 83  PRO A CG  
716  C  CD  . PRO A 83  ? 0.1094 0.1644 0.2524 0.0177  0.0285  -0.0135 83  PRO A CD  
717  N  N   . LEU A 84  ? 0.1843 0.1571 0.1818 0.0447  0.0390  -0.0184 84  LEU A N   
718  C  CA  . LEU A 84  ? 0.1729 0.1457 0.1829 0.0386  0.0239  -0.0259 84  LEU A CA  
719  C  C   . LEU A 84  ? 0.1347 0.1583 0.2361 0.0478  -0.0043 -0.0443 84  LEU A C   
720  O  O   . LEU A 84  ? 0.1635 0.1814 0.2626 0.0305  0.0335  -0.0627 84  LEU A O   
721  C  CB  . LEU A 84  ? 0.1789 0.1344 0.1811 0.0364  0.0403  -0.0280 84  LEU A CB  
722  C  CG  . LEU A 84  ? 0.1331 0.1247 0.1560 0.0120  0.0326  -0.0228 84  LEU A CG  
723  C  CD1 . LEU A 84  ? 0.1660 0.1648 0.1860 0.0375  0.0052  -0.0417 84  LEU A CD1 
724  C  CD2 . LEU A 84  ? 0.1156 0.1419 0.1809 0.0137  0.0388  -0.0236 84  LEU A CD2 
725  N  N   A ASP A 85  ? 0.2159 0.1547 0.2691 0.0120  0.0500  -0.0599 85  ASP A N   
726  N  N   B ASP A 85  ? 0.2099 0.1358 0.2745 0.0241  0.0472  -0.0562 85  ASP A N   
727  C  CA  A ASP A 85  ? 0.2615 0.1653 0.2822 0.0333  0.0071  -0.0625 85  ASP A CA  
728  C  CA  B ASP A 85  ? 0.2120 0.1364 0.3048 0.0328  -0.0239 -0.0865 85  ASP A CA  
729  C  C   A ASP A 85  ? 0.2003 0.1386 0.2475 0.0241  0.0196  -0.0821 85  ASP A C   
730  C  C   B ASP A 85  ? 0.3723 0.2188 0.3149 -0.0445 -0.0425 -0.0612 85  ASP A C   
731  O  O   A ASP A 85  ? 0.2260 0.1775 0.2676 0.0329  0.0758  -0.0496 85  ASP A O   
732  O  O   B ASP A 85  ? 0.4392 0.2707 0.2723 0.0804  -0.0379 -0.0129 85  ASP A O   
733  C  CB  A ASP A 85  ? 0.2818 0.2143 0.3702 0.0412  0.0226  -0.1331 85  ASP A CB  
734  C  CB  B ASP A 85  ? 0.3635 0.1541 0.2393 -0.0013 -0.0531 -0.0707 85  ASP A CB  
735  C  CG  A ASP A 85  ? 0.4672 0.4210 0.4183 0.0074  -0.0298 -0.0533 85  ASP A CG  
736  C  CG  B ASP A 85  ? 0.3253 0.3109 0.2737 0.0908  0.0421  -0.0458 85  ASP A CG  
737  O  OD1 A ASP A 85  ? 0.5268 0.3797 0.5210 -0.0948 -0.0599 -0.1695 85  ASP A OD1 
738  O  OD1 B ASP A 85  ? 0.4449 0.5206 0.3251 -0.0219 0.1871  -0.1147 85  ASP A OD1 
739  O  OD2 A ASP A 85  ? 0.4009 0.5098 0.4982 0.0782  0.0359  -0.0388 85  ASP A OD2 
740  O  OD2 B ASP A 85  ? 0.2782 0.3698 0.3538 -0.0375 0.0130  -0.0822 85  ASP A OD2 
741  N  N   A GLY A 86  ? 0.1586 0.1763 0.2224 0.0126  0.0230  -0.0417 86  GLY A N   
742  N  N   B GLY A 86  ? 0.4541 0.2581 0.3025 -0.0463 -0.1314 -0.0859 86  GLY A N   
743  C  CA  A GLY A 86  ? 0.2023 0.2278 0.2603 0.0842  0.0080  -0.0137 86  GLY A CA  
744  C  CA  B GLY A 86  ? 0.4658 0.2764 0.2151 -0.1172 -0.0131 -0.0527 86  GLY A CA  
745  C  C   A GLY A 86  ? 0.2421 0.2328 0.2813 -0.0205 -0.0113 -0.0155 86  GLY A C   
746  C  C   B GLY A 86  ? 0.2434 0.1368 0.2563 -0.0048 0.0197  -0.0631 86  GLY A C   
747  O  O   A GLY A 86  ? 0.2266 0.2278 0.2896 -0.0083 0.0059  -0.0498 86  GLY A O   
748  O  O   B GLY A 86  ? 0.1946 0.1685 0.3352 0.0121  0.0254  0.0395  86  GLY A O   
749  N  N   . THR A 87  ? 0.1668 0.1748 0.2463 0.0228  0.0258  -0.0351 87  THR A N   
750  C  CA  . THR A 87  ? 0.1583 0.1869 0.2542 0.0320  0.0205  -0.0469 87  THR A CA  
751  C  C   . THR A 87  ? 0.1317 0.1423 0.2397 0.0157  -0.0008 -0.0564 87  THR A C   
752  O  O   . THR A 87  ? 0.1653 0.1137 0.2348 0.0115  0.0250  -0.0218 87  THR A O   
753  C  CB  . THR A 87  ? 0.1820 0.3625 0.2569 0.1493  -0.0181 -0.0577 87  THR A CB  
754  O  OG1 . THR A 87  ? 0.2366 0.4287 0.4406 0.1630  0.0160  -0.1181 87  THR A OG1 
755  C  CG2 . THR A 87  ? 0.2300 0.3055 0.2946 0.1013  -0.0300 -0.0211 87  THR A CG2 
756  N  N   . TYR A 88  ? 0.1288 0.1252 0.1843 0.0130  0.0027  -0.0244 88  TYR A N   
757  C  CA  . TYR A 88  ? 0.1351 0.1195 0.1552 0.0015  0.0093  -0.0147 88  TYR A CA  
758  C  C   . TYR A 88  ? 0.1260 0.1360 0.1987 0.0237  -0.0086 -0.0219 88  TYR A C   
759  O  O   . TYR A 88  ? 0.1562 0.1580 0.2100 -0.0266 -0.0211 0.0122  88  TYR A O   
760  C  CB  . TYR A 88  ? 0.1328 0.1308 0.1518 0.0147  -0.0108 -0.0098 88  TYR A CB  
761  C  CG  . TYR A 88  ? 0.1378 0.1023 0.1626 0.0103  0.0109  -0.0131 88  TYR A CG  
762  C  CD1 . TYR A 88  ? 0.1341 0.1317 0.1662 0.0051  -0.0071 -0.0126 88  TYR A CD1 
763  C  CD2 . TYR A 88  ? 0.1240 0.0866 0.1538 0.0160  -0.0020 0.0021  88  TYR A CD2 
764  C  CE1 . TYR A 88  ? 0.1118 0.1279 0.1493 0.0098  0.0234  -0.0089 88  TYR A CE1 
765  C  CE2 . TYR A 88  ? 0.1268 0.0996 0.1375 0.0024  0.0162  0.0000  88  TYR A CE2 
766  C  CZ  . TYR A 88  ? 0.1158 0.1000 0.1578 -0.0098 0.0073  -0.0219 88  TYR A CZ  
767  O  OH  . TYR A 88  ? 0.1342 0.1182 0.1493 0.0052  0.0109  -0.0199 88  TYR A OH  
768  N  N   . ARG A 89  ? 0.1326 0.1218 0.1831 0.0215  -0.0093 -0.0127 89  ARG A N   
769  C  CA  . ARG A 89  ? 0.1816 0.1036 0.1734 0.0318  -0.0368 0.0102  89  ARG A CA  
770  C  C   . ARG A 89  ? 0.1319 0.1021 0.1398 -0.0038 -0.0082 0.0137  89  ARG A C   
771  O  O   . ARG A 89  ? 0.1407 0.0964 0.1572 0.0080  -0.0131 0.0120  89  ARG A O   
772  C  CB  . ARG A 89  ? 0.1894 0.1195 0.2298 0.0251  -0.0425 0.0062  89  ARG A CB  
773  C  CG  . ARG A 89  ? 0.2504 0.1775 0.3436 0.0825  -0.0364 -0.0176 89  ARG A CG  
774  C  CD  . ARG A 89  ? 0.3244 0.1583 0.4637 0.0285  -0.0346 0.1464  89  ARG A CD  
775  N  NE  . ARG A 89  ? 0.3483 0.2723 0.4949 0.1199  -0.0535 0.0964  89  ARG A NE  
776  C  CZ  . ARG A 89  ? 0.5105 0.2737 0.2860 0.0825  -0.1085 0.1111  89  ARG A CZ  
777  N  NH1 . ARG A 89  ? 0.4687 0.2702 0.3028 0.0970  -0.0772 0.0617  89  ARG A NH1 
778  N  NH2 . ARG A 89  ? 0.4900 0.3585 0.5709 0.1328  -0.1124 -0.0408 89  ARG A NH2 
779  N  N   . LEU A 90  ? 0.1495 0.1125 0.1511 0.0086  -0.0317 0.0049  90  LEU A N   
780  C  CA  . LEU A 90  ? 0.1692 0.1071 0.1544 -0.0031 -0.0225 -0.0030 90  LEU A CA  
781  C  C   . LEU A 90  ? 0.1603 0.1316 0.1229 -0.0140 -0.0351 0.0092  90  LEU A C   
782  O  O   . LEU A 90  ? 0.2068 0.1430 0.1463 0.0221  -0.0226 0.0445  90  LEU A O   
783  C  CB  . LEU A 90  ? 0.1795 0.1374 0.1380 -0.0115 -0.0211 0.0077  90  LEU A CB  
784  C  CG  . LEU A 90  ? 0.2192 0.1416 0.1332 -0.0214 -0.0395 -0.0076 90  LEU A CG  
785  C  CD1 . LEU A 90  ? 0.2442 0.1066 0.1466 0.0037  0.0038  0.0256  90  LEU A CD1 
786  C  CD2 . LEU A 90  ? 0.2097 0.2194 0.1921 -0.0203 -0.0416 -0.0071 90  LEU A CD2 
787  N  N   . LEU A 91  ? 0.1617 0.1070 0.1459 0.0109  -0.0240 0.0071  91  LEU A N   
788  C  CA  . LEU A 91  ? 0.1559 0.1024 0.1527 0.0068  -0.0113 0.0049  91  LEU A CA  
789  C  C   . LEU A 91  ? 0.1507 0.0974 0.1218 -0.0024 -0.0132 0.0263  91  LEU A C   
790  O  O   . LEU A 91  ? 0.2287 0.1071 0.1222 0.0010  -0.0157 0.0249  91  LEU A O   
791  C  CB  . LEU A 91  ? 0.2036 0.1687 0.1807 0.0159  -0.0438 -0.0232 91  LEU A CB  
792  C  CG  . LEU A 91  ? 0.1805 0.1272 0.2014 -0.0171 -0.0194 -0.0151 91  LEU A CG  
793  C  CD1 . LEU A 91  ? 0.2132 0.1475 0.3043 -0.0460 -0.0161 0.0265  91  LEU A CD1 
794  C  CD2 . LEU A 91  ? 0.2066 0.2745 0.2994 0.0026  -0.0489 -0.0071 91  LEU A CD2 
795  N  N   . GLN A 92  ? 0.1826 0.0837 0.1351 0.0013  -0.0119 0.0208  92  GLN A N   
796  C  CA  . GLN A 92  ? 0.2046 0.0842 0.1102 0.0160  -0.0074 0.0266  92  GLN A CA  
797  C  C   . GLN A 92  ? 0.1791 0.1001 0.0859 -0.0060 -0.0097 0.0200  92  GLN A C   
798  O  O   . GLN A 92  ? 0.1838 0.0847 0.1019 -0.0034 -0.0038 0.0080  92  GLN A O   
799  C  CB  . GLN A 92  ? 0.2184 0.1324 0.1393 0.0253  0.0280  0.0295  92  GLN A CB  
800  C  CG  . GLN A 92  ? 0.2183 0.1181 0.1928 0.0130  0.0054  0.0571  92  GLN A CG  
801  C  CD  . GLN A 92  ? 0.2215 0.1225 0.1999 0.0163  0.0502  0.0458  92  GLN A CD  
802  O  OE1 . GLN A 92  ? 0.2363 0.1138 0.1411 0.0043  -0.0164 0.0395  92  GLN A OE1 
803  N  NE2 . GLN A 92  ? 0.1947 0.1770 0.3862 -0.0118 0.0304  0.0793  92  GLN A NE2 
804  N  N   . PHE A 93  ? 0.2124 0.0970 0.0808 0.0049  -0.0196 0.0152  93  PHE A N   
805  C  CA  . PHE A 93  ? 0.1684 0.0904 0.1084 0.0102  -0.0232 0.0362  93  PHE A CA  
806  C  C   . PHE A 93  ? 0.2025 0.0906 0.0773 0.0104  -0.0245 0.0074  93  PHE A C   
807  O  O   . PHE A 93  ? 0.2075 0.1028 0.0899 0.0071  -0.0167 0.0155  93  PHE A O   
808  C  CB  . PHE A 93  ? 0.1917 0.1140 0.0931 0.0054  -0.0397 0.0236  93  PHE A CB  
809  C  CG  . PHE A 93  ? 0.1994 0.1046 0.1064 -0.0046 -0.0364 0.0192  93  PHE A CG  
810  C  CD1 . PHE A 93  ? 0.2080 0.1233 0.1042 0.0192  -0.0362 0.0081  93  PHE A CD1 
811  C  CD2 . PHE A 93  ? 0.2289 0.1429 0.1073 0.0225  -0.0573 0.0303  93  PHE A CD2 
812  C  CE1 . PHE A 93  ? 0.2495 0.1297 0.1163 0.0278  -0.0588 0.0065  93  PHE A CE1 
813  C  CE2 . PHE A 93  ? 0.2276 0.1782 0.1314 0.0408  -0.0733 -0.0040 93  PHE A CE2 
814  C  CZ  . PHE A 93  ? 0.2874 0.1471 0.1195 0.0346  -0.0526 0.0120  93  PHE A CZ  
815  N  N   . HIS A 94  ? 0.1759 0.0933 0.0856 -0.0006 -0.0256 0.0185  94  HIS A N   
816  C  CA  . HIS A 94  ? 0.1662 0.0913 0.0696 0.0000  -0.0111 0.0136  94  HIS A CA  
817  C  C   . HIS A 94  ? 0.1385 0.1050 0.0746 -0.0155 -0.0141 0.0082  94  HIS A C   
818  O  O   . HIS A 94  ? 0.1462 0.0897 0.0866 -0.0006 0.0015  0.0108  94  HIS A O   
819  C  CB  . HIS A 94  ? 0.1816 0.0883 0.1071 -0.0201 -0.0195 0.0078  94  HIS A CB  
820  C  CG  . HIS A 94  ? 0.1538 0.0936 0.0886 -0.0217 -0.0102 0.0080  94  HIS A CG  
821  N  ND1 . HIS A 94  ? 0.1653 0.0917 0.1033 -0.0063 -0.0233 0.0048  94  HIS A ND1 
822  C  CD2 . HIS A 94  ? 0.1377 0.1057 0.0762 -0.0164 -0.0037 0.0078  94  HIS A CD2 
823  C  CE1 . HIS A 94  ? 0.1382 0.0945 0.0997 -0.0127 -0.0144 0.0186  94  HIS A CE1 
824  N  NE2 . HIS A 94  ? 0.1350 0.0876 0.1001 -0.0162 -0.0165 0.0076  94  HIS A NE2 
825  N  N   . PHE A 95  ? 0.1387 0.0841 0.0881 -0.0063 -0.0149 0.0052  95  PHE A N   
826  C  CA  . PHE A 95  ? 0.1283 0.0821 0.0989 -0.0131 -0.0148 0.0118  95  PHE A CA  
827  C  C   . PHE A 95  ? 0.1154 0.0888 0.0851 -0.0193 0.0073  -0.0093 95  PHE A C   
828  O  O   . PHE A 95  ? 0.1333 0.1077 0.1001 -0.0240 0.0013  0.0153  95  PHE A O   
829  C  CB  . PHE A 95  ? 0.1601 0.0895 0.0971 -0.0082 -0.0201 -0.0082 95  PHE A CB  
830  C  CG  . PHE A 95  ? 0.1547 0.0895 0.0949 -0.0199 -0.0147 -0.0038 95  PHE A CG  
831  C  CD1 . PHE A 95  ? 0.1702 0.1215 0.1097 -0.0031 -0.0302 -0.0041 95  PHE A CD1 
832  C  CD2 . PHE A 95  ? 0.1290 0.1115 0.1109 -0.0219 -0.0103 -0.0263 95  PHE A CD2 
833  C  CE1 . PHE A 95  ? 0.1818 0.1484 0.1046 -0.0065 -0.0296 -0.0034 95  PHE A CE1 
834  C  CE2 . PHE A 95  ? 0.1416 0.1310 0.1091 -0.0114 -0.0217 -0.0102 95  PHE A CE2 
835  C  CZ  . PHE A 95  ? 0.1556 0.1326 0.1265 -0.0122 -0.0263 -0.0388 95  PHE A CZ  
836  N  N   . HIS A 96  ? 0.1234 0.0873 0.0741 -0.0137 -0.0065 -0.0013 96  HIS A N   
837  C  CA  . HIS A 96  ? 0.1145 0.0874 0.0851 -0.0074 -0.0010 -0.0005 96  HIS A CA  
838  C  C   . HIS A 96  ? 0.0985 0.0939 0.0863 -0.0054 0.0071  -0.0102 96  HIS A C   
839  O  O   . HIS A 96  ? 0.1076 0.0908 0.0890 -0.0108 0.0091  -0.0031 96  HIS A O   
840  C  CB  . HIS A 96  ? 0.1307 0.0956 0.0899 -0.0137 -0.0083 -0.0105 96  HIS A CB  
841  C  CG  . HIS A 96  ? 0.1118 0.1064 0.0715 0.0010  0.0048  0.0065  96  HIS A CG  
842  N  ND1 . HIS A 96  ? 0.1143 0.0870 0.1039 -0.0040 0.0010  -0.0038 96  HIS A ND1 
843  C  CD2 . HIS A 96  ? 0.1179 0.0860 0.0882 -0.0007 -0.0021 0.0035  96  HIS A CD2 
844  C  CE1 . HIS A 96  ? 0.1093 0.0957 0.1050 0.0100  0.0063  -0.0001 96  HIS A CE1 
845  N  NE2 . HIS A 96  ? 0.1158 0.0874 0.0820 -0.0006 0.0041  -0.0024 96  HIS A NE2 
846  N  N   . TRP A 97  ? 0.1100 0.0870 0.0771 -0.0085 0.0111  0.0006  97  TRP A N   
847  C  CA  . TRP A 97  ? 0.1111 0.0834 0.1021 -0.0021 0.0049  -0.0115 97  TRP A CA  
848  C  C   . TRP A 97  ? 0.1052 0.1042 0.0798 0.0000  0.0166  -0.0063 97  TRP A C   
849  O  O   . TRP A 97  ? 0.1288 0.1075 0.0987 -0.0026 0.0208  -0.0206 97  TRP A O   
850  C  CB  . TRP A 97  ? 0.1305 0.1071 0.0861 -0.0167 0.0107  -0.0119 97  TRP A CB  
851  C  CG  . TRP A 97  ? 0.1416 0.1005 0.0888 -0.0118 -0.0135 -0.0076 97  TRP A CG  
852  C  CD1 . TRP A 97  ? 0.1483 0.1222 0.0797 -0.0177 0.0091  -0.0173 97  TRP A CD1 
853  C  CD2 . TRP A 97  ? 0.1353 0.1075 0.0790 -0.0220 0.0017  -0.0073 97  TRP A CD2 
854  N  NE1 . TRP A 97  ? 0.1574 0.1102 0.0958 -0.0116 0.0167  -0.0021 97  TRP A NE1 
855  C  CE2 . TRP A 97  ? 0.1351 0.1240 0.0776 -0.0305 0.0051  -0.0066 97  TRP A CE2 
856  C  CE3 . TRP A 97  ? 0.1149 0.0933 0.0988 -0.0238 -0.0015 -0.0165 97  TRP A CE3 
857  C  CZ2 . TRP A 97  ? 0.1603 0.1215 0.0997 -0.0164 0.0021  0.0015  97  TRP A CZ2 
858  C  CZ3 . TRP A 97  ? 0.1574 0.1359 0.0860 -0.0245 -0.0052 0.0074  97  TRP A CZ3 
859  C  CH2 . TRP A 97  ? 0.1689 0.1298 0.1054 -0.0285 0.0094  -0.0030 97  TRP A CH2 
860  N  N   . GLY A 98  ? 0.1456 0.0927 0.0915 -0.0041 0.0181  -0.0136 98  GLY A N   
861  C  CA  . GLY A 98  ? 0.1265 0.1093 0.0933 0.0001  0.0212  -0.0161 98  GLY A CA  
862  C  C   . GLY A 98  ? 0.1506 0.1134 0.0926 -0.0096 0.0031  -0.0171 98  GLY A C   
863  O  O   . GLY A 98  ? 0.1359 0.1100 0.1181 0.0035  0.0046  -0.0237 98  GLY A O   
864  N  N   . SER A 99  ? 0.1590 0.1134 0.1075 0.0094  0.0245  -0.0187 99  SER A N   
865  C  CA  . SER A 99  ? 0.1615 0.1347 0.1380 0.0034  0.0183  -0.0535 99  SER A CA  
866  C  C   . SER A 99  ? 0.1987 0.1041 0.1335 0.0114  0.0263  -0.0491 99  SER A C   
867  O  O   . SER A 99  ? 0.2154 0.1472 0.1502 -0.0085 0.0276  -0.0584 99  SER A O   
868  C  CB  . SER A 99  ? 0.1780 0.1685 0.1552 -0.0076 0.0390  -0.0756 99  SER A CB  
869  O  OG  . SER A 99  ? 0.1741 0.1392 0.1893 0.0362  0.0237  -0.0328 99  SER A OG  
870  N  N   A LEU A 100 ? 0.1583 0.1341 0.1551 0.0110  0.0155  -0.0043 100 LEU A N   
871  N  N   B LEU A 100 ? 0.1502 0.1225 0.1272 -0.0109 0.0170  -0.0351 100 LEU A N   
872  C  CA  A LEU A 100 ? 0.1771 0.0973 0.1567 0.0340  0.0259  -0.0204 100 LEU A CA  
873  C  CA  B LEU A 100 ? 0.1741 0.1028 0.1500 0.0043  0.0232  0.0100  100 LEU A CA  
874  C  C   A LEU A 100 ? 0.1278 0.0992 0.1396 0.0308  -0.0043 -0.0219 100 LEU A C   
875  C  C   B LEU A 100 ? 0.1699 0.1150 0.1540 -0.0035 0.0193  -0.0161 100 LEU A C   
876  O  O   A LEU A 100 ? 0.1362 0.0834 0.1349 0.0181  -0.0212 -0.0088 100 LEU A O   
877  O  O   B LEU A 100 ? 0.1489 0.1067 0.1308 0.0196  0.0097  -0.0266 100 LEU A O   
878  C  CB  A LEU A 100 ? 0.1780 0.1815 0.1845 0.0355  -0.0078 0.0015  100 LEU A CB  
879  C  CB  B LEU A 100 ? 0.1671 0.1279 0.1313 0.0188  0.0109  -0.0060 100 LEU A CB  
880  C  CG  A LEU A 100 ? 0.2284 0.1658 0.2741 0.0671  0.0197  -0.0568 100 LEU A CG  
881  C  CG  B LEU A 100 ? 0.1972 0.1283 0.1748 0.0124  0.0469  -0.0121 100 LEU A CG  
882  C  CD1 A LEU A 100 ? 0.2851 0.2258 0.3242 0.1387  0.0535  0.0214  100 LEU A CD1 
883  C  CD1 B LEU A 100 ? 0.2590 0.1444 0.2050 0.0518  0.0381  -0.0553 100 LEU A CD1 
884  C  CD2 A LEU A 100 ? 0.1872 0.2610 0.2050 0.0579  0.0375  -0.0683 100 LEU A CD2 
885  C  CD2 B LEU A 100 ? 0.2053 0.1545 0.1768 0.0533  0.0410  -0.0447 100 LEU A CD2 
886  N  N   . ASP A 101 ? 0.1518 0.1053 0.1674 0.0012  0.0054  -0.0184 101 ASP A N   
887  C  CA  . ASP A 101 ? 0.1693 0.1118 0.1502 0.0046  0.0096  -0.0005 101 ASP A CA  
888  C  C   . ASP A 101 ? 0.1535 0.1036 0.1423 0.0019  0.0359  0.0071  101 ASP A C   
889  O  O   . ASP A 101 ? 0.1941 0.1159 0.1696 0.0242  0.0287  0.0068  101 ASP A O   
890  C  CB  . ASP A 101 ? 0.1940 0.1337 0.2069 -0.0274 -0.0001 0.0399  101 ASP A CB  
891  C  CG  . ASP A 101 ? 0.1865 0.1484 0.2296 -0.0020 -0.0175 0.0346  101 ASP A CG  
892  O  OD1 . ASP A 101 ? 0.2260 0.1511 0.1962 -0.0237 -0.0125 0.0326  101 ASP A OD1 
893  O  OD2 . ASP A 101 ? 0.3005 0.2335 0.2698 -0.0975 -0.0671 0.0662  101 ASP A OD2 
894  N  N   . GLY A 102 ? 0.1527 0.0952 0.1646 -0.0057 -0.0126 -0.0116 102 GLY A N   
895  C  CA  . GLY A 102 ? 0.2007 0.1084 0.1513 -0.0364 0.0010  -0.0012 102 GLY A CA  
896  C  C   . GLY A 102 ? 0.1371 0.0985 0.1423 -0.0241 0.0023  0.0003  102 GLY A C   
897  O  O   . GLY A 102 ? 0.1912 0.1033 0.1443 -0.0003 0.0142  0.0081  102 GLY A O   
898  N  N   A GLN A 103 ? 0.1312 0.1181 0.1371 -0.0118 0.0339  0.0049  103 GLN A N   
899  N  N   B GLN A 103 ? 0.1146 0.0933 0.1154 0.0076  0.0146  -0.0221 103 GLN A N   
900  C  CA  A GLN A 103 ? 0.1360 0.1079 0.1145 0.0118  0.0044  -0.0243 103 GLN A CA  
901  C  CA  B GLN A 103 ? 0.1102 0.0825 0.1037 0.0062  0.0126  0.0065  103 GLN A CA  
902  C  C   A GLN A 103 ? 0.1163 0.0961 0.0982 -0.0031 0.0283  -0.0236 103 GLN A C   
903  C  C   B GLN A 103 ? 0.1068 0.0890 0.0920 0.0052  0.0020  -0.0131 103 GLN A C   
904  O  O   A GLN A 103 ? 0.0940 0.0888 0.1170 0.0131  0.0233  -0.0189 103 GLN A O   
905  O  O   B GLN A 103 ? 0.1021 0.0815 0.0989 -0.0041 -0.0070 -0.0055 103 GLN A O   
906  C  CB  A GLN A 103 ? 0.1446 0.0870 0.1054 0.0051  0.0110  0.0080  103 GLN A CB  
907  C  CB  B GLN A 103 ? 0.1159 0.1328 0.1028 0.0032  -0.0170 0.0068  103 GLN A CB  
908  C  CG  A GLN A 103 ? 0.1509 0.1764 0.1389 0.0707  0.0482  -0.0227 103 GLN A CG  
909  C  CG  B GLN A 103 ? 0.1254 0.1215 0.1559 0.0251  0.0399  0.0034  103 GLN A CG  
910  C  CD  A GLN A 103 ? 0.1646 0.1680 0.1933 0.0606  0.0604  0.0496  103 GLN A CD  
911  C  CD  B GLN A 103 ? 0.1353 0.1701 0.1545 0.0151  0.0093  -0.0010 103 GLN A CD  
912  O  OE1 A GLN A 103 ? 0.2196 0.1396 0.2472 0.0751  0.0251  0.0100  103 GLN A OE1 
913  O  OE1 B GLN A 103 ? 0.1604 0.1569 0.1728 0.0313  0.0186  -0.0038 103 GLN A OE1 
914  N  NE2 A GLN A 103 ? 0.1448 0.2266 0.2102 0.0474  0.0666  -0.0586 103 GLN A NE2 
915  N  NE2 B GLN A 103 ? 0.1507 0.1594 0.1759 0.0337  0.0467  -0.0031 103 GLN A NE2 
916  N  N   . GLY A 104 ? 0.1190 0.0824 0.1030 0.0035  0.0148  -0.0054 104 GLY A N   
917  C  CA  . GLY A 104 ? 0.1177 0.0881 0.0931 0.0104  0.0089  0.0019  104 GLY A CA  
918  C  C   . GLY A 104 ? 0.1010 0.0816 0.0920 -0.0088 -0.0017 0.0007  104 GLY A C   
919  O  O   . GLY A 104 ? 0.1129 0.0924 0.1003 -0.0077 0.0107  -0.0024 104 GLY A O   
920  N  N   . SER A 105 ? 0.1045 0.0922 0.0793 -0.0093 -0.0010 -0.0059 105 SER A N   
921  C  CA  . SER A 105 ? 0.0926 0.0856 0.0793 0.0015  0.0005  -0.0071 105 SER A CA  
922  C  C   . SER A 105 ? 0.0945 0.0886 0.0892 0.0020  0.0089  -0.0083 105 SER A C   
923  O  O   . SER A 105 ? 0.1152 0.0988 0.1076 0.0035  -0.0017 -0.0190 105 SER A O   
924  C  CB  . SER A 105 ? 0.1105 0.0869 0.0876 -0.0121 0.0100  0.0114  105 SER A CB  
925  O  OG  . SER A 105 ? 0.1261 0.0825 0.0948 -0.0008 0.0087  0.0027  105 SER A OG  
926  N  N   . GLU A 106 ? 0.0922 0.0838 0.0848 -0.0027 0.0054  -0.0052 106 GLU A N   
927  C  CA  . GLU A 106 ? 0.0965 0.0852 0.0839 -0.0043 -0.0015 -0.0006 106 GLU A CA  
928  C  C   . GLU A 106 ? 0.0965 0.0755 0.0834 0.0027  -0.0043 0.0013  106 GLU A C   
929  O  O   . GLU A 106 ? 0.1023 0.0913 0.0948 0.0015  -0.0073 -0.0013 106 GLU A O   
930  C  CB  . GLU A 106 ? 0.0987 0.0870 0.0776 -0.0035 0.0049  0.0082  106 GLU A CB  
931  C  CG  . GLU A 106 ? 0.1331 0.1005 0.1005 -0.0148 0.0218  0.0028  106 GLU A CG  
932  C  CD  . GLU A 106 ? 0.1026 0.0947 0.0741 0.0024  0.0115  0.0006  106 GLU A CD  
933  O  OE1 . GLU A 106 ? 0.0922 0.1059 0.1058 -0.0032 0.0062  -0.0030 106 GLU A OE1 
934  O  OE2 . GLU A 106 ? 0.1026 0.1152 0.1050 -0.0049 0.0147  -0.0031 106 GLU A OE2 
935  N  N   . HIS A 107 ? 0.0985 0.0728 0.0816 0.0051  0.0156  0.0062  107 HIS A N   
936  C  CA  . HIS A 107 ? 0.1010 0.0729 0.0795 0.0060  0.0151  0.0041  107 HIS A CA  
937  C  C   . HIS A 107 ? 0.1037 0.0812 0.0754 0.0148  0.0013  -0.0010 107 HIS A C   
938  O  O   . HIS A 107 ? 0.1062 0.0865 0.0838 0.0021  -0.0074 0.0059  107 HIS A O   
939  C  CB  . HIS A 107 ? 0.0979 0.0861 0.0863 0.0012  0.0055  -0.0017 107 HIS A CB  
940  C  CG  . HIS A 107 ? 0.0788 0.0856 0.0767 0.0092  0.0110  -0.0049 107 HIS A CG  
941  N  ND1 . HIS A 107 ? 0.0935 0.0817 0.0897 0.0086  0.0041  0.0013  107 HIS A ND1 
942  C  CD2 . HIS A 107 ? 0.0759 0.0851 0.1030 0.0183  0.0030  -0.0177 107 HIS A CD2 
943  C  CE1 . HIS A 107 ? 0.0960 0.0897 0.0949 0.0097  -0.0003 -0.0116 107 HIS A CE1 
944  N  NE2 . HIS A 107 ? 0.0926 0.0904 0.0931 0.0007  -0.0012 -0.0104 107 HIS A NE2 
945  N  N   . THR A 108 ? 0.1068 0.0870 0.0821 0.0152  0.0010  0.0076  108 THR A N   
946  C  CA  . THR A 108 ? 0.1142 0.0883 0.0883 0.0052  0.0035  0.0063  108 THR A CA  
947  C  C   . THR A 108 ? 0.1217 0.0890 0.0756 -0.0046 -0.0003 0.0073  108 THR A C   
948  O  O   . THR A 108 ? 0.1299 0.0910 0.0894 0.0041  0.0032  0.0006  108 THR A O   
949  C  CB  . THR A 108 ? 0.1120 0.1080 0.1046 0.0177  -0.0082 -0.0074 108 THR A CB  
950  O  OG1 . THR A 108 ? 0.1246 0.1026 0.1070 0.0185  -0.0120 0.0057  108 THR A OG1 
951  C  CG2 . THR A 108 ? 0.1190 0.1173 0.0926 0.0186  0.0080  0.0035  108 THR A CG2 
952  N  N   . VAL A 109 ? 0.1167 0.0878 0.1019 0.0024  0.0100  0.0120  109 VAL A N   
953  C  CA  . VAL A 109 ? 0.1168 0.1100 0.1154 0.0044  0.0098  0.0293  109 VAL A CA  
954  C  C   . VAL A 109 ? 0.1254 0.0890 0.1107 -0.0023 0.0149  0.0078  109 VAL A C   
955  O  O   . VAL A 109 ? 0.1475 0.0978 0.1120 0.0054  0.0080  0.0177  109 VAL A O   
956  C  CB  . VAL A 109 ? 0.1499 0.1222 0.1021 0.0007  0.0040  0.0244  109 VAL A CB  
957  C  CG1 . VAL A 109 ? 0.1448 0.1359 0.1238 -0.0048 0.0266  0.0359  109 VAL A CG1 
958  C  CG2 . VAL A 109 ? 0.1493 0.1263 0.1347 0.0005  -0.0043 0.0403  109 VAL A CG2 
959  N  N   . ASP A 110 ? 0.1419 0.1044 0.1001 -0.0013 -0.0013 0.0285  110 ASP A N   
960  C  CA  . ASP A 110 ? 0.1808 0.1132 0.0992 0.0187  0.0109  0.0329  110 ASP A CA  
961  C  C   . ASP A 110 ? 0.1842 0.1098 0.1107 0.0195  0.0062  0.0089  110 ASP A C   
962  O  O   . ASP A 110 ? 0.2028 0.1106 0.1172 0.0256  0.0000  0.0227  110 ASP A O   
963  C  CB  . ASP A 110 ? 0.1905 0.1324 0.1120 0.0037  0.0186  0.0372  110 ASP A CB  
964  C  CG  . ASP A 110 ? 0.1787 0.1434 0.1089 -0.0088 0.0105  0.0388  110 ASP A CG  
965  O  OD1 . ASP A 110 ? 0.2203 0.1430 0.1222 0.0017  0.0348  0.0177  110 ASP A OD1 
966  O  OD2 . ASP A 110 ? 0.2059 0.1852 0.1574 0.0044  0.0292  0.0254  110 ASP A OD2 
967  N  N   . LYS A 111 ? 0.1499 0.1199 0.1107 0.0204  0.0010  0.0241  111 LYS A N   
968  C  CA  . LYS A 111 ? 0.1465 0.1142 0.1305 0.0192  -0.0109 0.0249  111 LYS A CA  
969  C  C   . LYS A 111 ? 0.1629 0.1048 0.1062 0.0219  0.0057  0.0087  111 LYS A C   
970  O  O   . LYS A 111 ? 0.1529 0.1292 0.1560 0.0329  0.0071  0.0121  111 LYS A O   
971  C  CB  . LYS A 111 ? 0.1833 0.1333 0.1623 0.0434  -0.0126 0.0267  111 LYS A CB  
972  C  CG  . LYS A 111 ? 0.2354 0.2238 0.1225 0.0741  -0.0313 0.0522  111 LYS A CG  
973  C  CD  . LYS A 111 ? 0.2912 0.1905 0.1761 0.0750  -0.0038 0.0192  111 LYS A CD  
974  C  CE  . LYS A 111 ? 0.2734 0.2955 0.2342 0.0414  -0.0747 0.0535  111 LYS A CE  
975  N  NZ  . LYS A 111 ? 0.2217 0.2863 0.3183 0.0280  -0.0068 0.0636  111 LYS A NZ  
976  N  N   . LYS A 112 ? 0.1615 0.0851 0.1042 0.0170  0.0048  0.0130  112 LYS A N   
977  C  CA  . LYS A 112 ? 0.1675 0.1206 0.1033 -0.0136 0.0013  0.0074  112 LYS A CA  
978  C  C   . LYS A 112 ? 0.1385 0.0998 0.1073 -0.0013 -0.0043 0.0010  112 LYS A C   
979  O  O   . LYS A 112 ? 0.1249 0.0952 0.1071 0.0068  -0.0046 -0.0010 112 LYS A O   
980  C  CB  . LYS A 112 ? 0.1851 0.1274 0.1204 -0.0309 -0.0020 0.0074  112 LYS A CB  
981  C  CG  . LYS A 112 ? 0.1773 0.1585 0.1299 -0.0307 0.0043  -0.0230 112 LYS A CG  
982  C  CD  . LYS A 112 ? 0.1637 0.2233 0.1764 -0.0082 -0.0034 -0.0017 112 LYS A CD  
983  C  CE  . LYS A 112 ? 0.1985 0.2014 0.1858 0.0208  -0.0098 -0.0410 112 LYS A CE  
984  N  NZ  . LYS A 112 ? 0.2860 0.1788 0.2229 -0.0318 -0.0129 0.0068  112 LYS A NZ  
985  N  N   A LYS A 113 ? 0.1068 0.0966 0.1030 -0.0006 0.0070  -0.0087 113 LYS A N   
986  N  N   B LYS A 113 ? 0.0974 0.1017 0.1039 0.0222  -0.0031 0.0156  113 LYS A N   
987  C  CA  A LYS A 113 ? 0.1301 0.0688 0.1102 -0.0082 0.0017  -0.0086 113 LYS A CA  
988  C  CA  B LYS A 113 ? 0.1244 0.1073 0.0979 -0.0078 0.0068  0.0111  113 LYS A CA  
989  C  C   A LYS A 113 ? 0.1170 0.0895 0.0994 -0.0225 0.0173  0.0098  113 LYS A C   
990  C  C   B LYS A 113 ? 0.1262 0.1046 0.1150 0.0245  0.0049  -0.0185 113 LYS A C   
991  O  O   A LYS A 113 ? 0.1194 0.0706 0.1341 -0.0063 0.0037  0.0172  113 LYS A O   
992  O  O   B LYS A 113 ? 0.1109 0.1093 0.1208 0.0060  0.0068  -0.0137 113 LYS A O   
993  C  CB  A LYS A 113 ? 0.1307 0.0826 0.0964 -0.0168 -0.0040 0.0021  113 LYS A CB  
994  C  CB  B LYS A 113 ? 0.1057 0.1369 0.1193 -0.0024 -0.0006 0.0076  113 LYS A CB  
995  C  CG  A LYS A 113 ? 0.1064 0.0982 0.1319 0.0013  0.0034  -0.0092 113 LYS A CG  
996  C  CG  B LYS A 113 ? 0.1369 0.1468 0.1154 0.0026  -0.0124 -0.0274 113 LYS A CG  
997  C  CD  A LYS A 113 ? 0.1247 0.1418 0.1288 -0.0142 0.0287  -0.0221 113 LYS A CD  
998  C  CD  B LYS A 113 ? 0.1249 0.1547 0.1554 0.0015  0.0020  -0.0038 113 LYS A CD  
999  C  CE  A LYS A 113 ? 0.1617 0.1298 0.1614 -0.0098 -0.0143 -0.0094 113 LYS A CE  
1000 C  CE  B LYS A 113 ? 0.1416 0.2284 0.1269 0.0127  -0.0225 -0.0329 113 LYS A CE  
1001 N  NZ  A LYS A 113 ? 0.1623 0.1270 0.1671 -0.0010 -0.0353 0.0115  113 LYS A NZ  
1002 N  NZ  B LYS A 113 ? 0.1729 0.1888 0.2608 0.0076  0.0417  0.0049  113 LYS A NZ  
1003 N  N   . TYR A 114 ? 0.1208 0.1005 0.0987 -0.0043 0.0041  0.0129  114 TYR A N   
1004 C  CA  . TYR A 114 ? 0.1191 0.1141 0.0998 0.0031  0.0116  -0.0007 114 TYR A CA  
1005 C  C   . TYR A 114 ? 0.1071 0.0701 0.1094 -0.0156 0.0082  0.0031  114 TYR A C   
1006 O  O   . TYR A 114 ? 0.1121 0.0895 0.1062 -0.0059 0.0093  -0.0024 114 TYR A O   
1007 C  CB  . TYR A 114 ? 0.1003 0.1018 0.1262 -0.0013 0.0209  -0.0038 114 TYR A CB  
1008 C  CG  . TYR A 114 ? 0.1138 0.0954 0.1159 0.0102  0.0046  -0.0001 114 TYR A CG  
1009 C  CD1 . TYR A 114 ? 0.1556 0.1037 0.1055 0.0218  -0.0027 0.0019  114 TYR A CD1 
1010 C  CD2 . TYR A 114 ? 0.1224 0.0954 0.1484 -0.0049 0.0148  0.0141  114 TYR A CD2 
1011 C  CE1 . TYR A 114 ? 0.1840 0.1393 0.1254 0.0179  0.0155  0.0208  114 TYR A CE1 
1012 C  CE2 . TYR A 114 ? 0.1633 0.1337 0.1854 -0.0076 0.0524  0.0026  114 TYR A CE2 
1013 C  CZ  . TYR A 114 ? 0.1754 0.1527 0.1529 0.0149  0.0496  0.0159  114 TYR A CZ  
1014 O  OH  . TYR A 114 ? 0.2664 0.2354 0.1827 0.0021  0.1093  0.0351  114 TYR A OH  
1015 N  N   . ALA A 115 ? 0.1423 0.0865 0.1001 -0.0138 -0.0020 0.0076  115 ALA A N   
1016 C  CA  . ALA A 115 ? 0.1265 0.0772 0.1082 -0.0107 0.0006  -0.0060 115 ALA A CA  
1017 C  C   . ALA A 115 ? 0.1177 0.0909 0.0913 0.0068  0.0038  0.0017  115 ALA A C   
1018 O  O   . ALA A 115 ? 0.1298 0.0828 0.1071 0.0000  0.0089  -0.0087 115 ALA A O   
1019 C  CB  . ALA A 115 ? 0.1416 0.1107 0.1053 -0.0083 -0.0093 -0.0041 115 ALA A CB  
1020 N  N   . ALA A 116 ? 0.1289 0.0693 0.1054 -0.0032 -0.0020 -0.0080 116 ALA A N   
1021 C  CA  . ALA A 116 ? 0.1177 0.0854 0.0843 -0.0167 0.0005  -0.0031 116 ALA A CA  
1022 C  C   . ALA A 116 ? 0.0951 0.0771 0.0949 -0.0012 -0.0040 -0.0017 116 ALA A C   
1023 O  O   . ALA A 116 ? 0.1096 0.0848 0.0942 -0.0065 0.0063  -0.0027 116 ALA A O   
1024 C  CB  . ALA A 116 ? 0.1267 0.0948 0.0976 -0.0104 -0.0010 -0.0020 116 ALA A CB  
1025 N  N   . GLU A 117 ? 0.1091 0.0724 0.0834 0.0010  -0.0059 0.0020  117 GLU A N   
1026 C  CA  . GLU A 117 ? 0.1161 0.0701 0.0776 -0.0052 0.0017  -0.0055 117 GLU A CA  
1027 C  C   . GLU A 117 ? 0.1136 0.0904 0.0684 -0.0065 0.0003  -0.0027 117 GLU A C   
1028 O  O   . GLU A 117 ? 0.1154 0.0922 0.0996 -0.0024 0.0110  0.0199  117 GLU A O   
1029 C  CB  . GLU A 117 ? 0.1073 0.0960 0.0662 -0.0028 0.0001  0.0010  117 GLU A CB  
1030 C  CG  . GLU A 117 ? 0.1195 0.1059 0.0850 0.0074  -0.0104 -0.0041 117 GLU A CG  
1031 C  CD  . GLU A 117 ? 0.1062 0.0771 0.0800 0.0085  0.0020  -0.0020 117 GLU A CD  
1032 O  OE1 . GLU A 117 ? 0.1024 0.1037 0.0842 0.0073  -0.0065 0.0076  117 GLU A OE1 
1033 O  OE2 . GLU A 117 ? 0.1430 0.0851 0.0844 0.0007  -0.0118 0.0003  117 GLU A OE2 
1034 N  N   . LEU A 118 ? 0.1070 0.0825 0.0866 0.0020  -0.0130 -0.0015 118 LEU A N   
1035 C  CA  . LEU A 118 ? 0.1159 0.0816 0.0838 -0.0023 -0.0146 0.0074  118 LEU A CA  
1036 C  C   . LEU A 118 ? 0.1120 0.0903 0.0768 -0.0006 -0.0020 0.0071  118 LEU A C   
1037 O  O   . LEU A 118 ? 0.1177 0.0747 0.0904 -0.0006 -0.0020 0.0057  118 LEU A O   
1038 C  CB  . LEU A 118 ? 0.1432 0.0872 0.0979 0.0010  -0.0147 0.0138  118 LEU A CB  
1039 C  CG  . LEU A 118 ? 0.1425 0.1181 0.1001 0.0066  -0.0313 0.0199  118 LEU A CG  
1040 C  CD1 . LEU A 118 ? 0.1702 0.1032 0.1111 0.0066  -0.0302 0.0189  118 LEU A CD1 
1041 C  CD2 . LEU A 118 ? 0.1350 0.1398 0.1281 0.0142  -0.0228 0.0077  118 LEU A CD2 
1042 N  N   . HIS A 119 ? 0.1271 0.0676 0.0798 0.0013  -0.0083 0.0086  119 HIS A N   
1043 C  CA  . HIS A 119 ? 0.1244 0.0731 0.0799 0.0010  -0.0030 0.0176  119 HIS A CA  
1044 C  C   . HIS A 119 ? 0.1235 0.0826 0.0724 -0.0142 -0.0060 0.0124  119 HIS A C   
1045 O  O   . HIS A 119 ? 0.1410 0.0811 0.0888 0.0001  -0.0057 0.0119  119 HIS A O   
1046 C  CB  . HIS A 119 ? 0.1093 0.0969 0.0776 0.0102  -0.0063 0.0083  119 HIS A CB  
1047 C  CG  . HIS A 119 ? 0.1270 0.0816 0.0634 0.0052  -0.0120 -0.0040 119 HIS A CG  
1048 N  ND1 . HIS A 119 ? 0.1384 0.0852 0.0762 0.0037  -0.0024 -0.0089 119 HIS A ND1 
1049 C  CD2 . HIS A 119 ? 0.1425 0.0927 0.0864 0.0131  -0.0115 0.0032  119 HIS A CD2 
1050 C  CE1 . HIS A 119 ? 0.1213 0.0938 0.0706 0.0048  0.0015  -0.0012 119 HIS A CE1 
1051 N  NE2 . HIS A 119 ? 0.1128 0.0930 0.0851 0.0188  -0.0104 -0.0026 119 HIS A NE2 
1052 N  N   . LEU A 120 ? 0.1150 0.0825 0.0834 0.0020  -0.0111 0.0026  120 LEU A N   
1053 C  CA  . LEU A 120 ? 0.1324 0.0864 0.1102 0.0082  -0.0159 0.0110  120 LEU A CA  
1054 C  C   . LEU A 120 ? 0.1109 0.0874 0.0935 0.0142  -0.0080 0.0028  120 LEU A C   
1055 O  O   . LEU A 120 ? 0.1161 0.0808 0.0951 -0.0010 -0.0060 -0.0020 120 LEU A O   
1056 C  CB  . LEU A 120 ? 0.1270 0.0906 0.1124 0.0105  -0.0278 -0.0046 120 LEU A CB  
1057 C  CG  . LEU A 120 ? 0.1394 0.1127 0.1203 -0.0041 -0.0329 0.0074  120 LEU A CG  
1058 C  CD1 . LEU A 120 ? 0.2115 0.1565 0.1349 -0.0732 -0.0026 -0.0164 120 LEU A CD1 
1059 C  CD2 . LEU A 120 ? 0.1921 0.1527 0.1482 0.0225  -0.0604 0.0094  120 LEU A CD2 
1060 N  N   . VAL A 121 ? 0.1184 0.0948 0.1049 -0.0012 -0.0015 0.0120  121 VAL A N   
1061 C  CA  . VAL A 121 ? 0.1242 0.0834 0.1177 0.0017  -0.0104 0.0024  121 VAL A CA  
1062 C  C   . VAL A 121 ? 0.1367 0.0882 0.1109 0.0165  -0.0015 0.0130  121 VAL A C   
1063 O  O   . VAL A 121 ? 0.1844 0.0915 0.1188 0.0187  -0.0144 0.0220  121 VAL A O   
1064 C  CB  . VAL A 121 ? 0.1416 0.1014 0.1268 0.0003  -0.0003 -0.0030 121 VAL A CB  
1065 C  CG1 . VAL A 121 ? 0.1596 0.0994 0.1506 -0.0178 0.0203  0.0038  121 VAL A CG1 
1066 C  CG2 . VAL A 121 ? 0.1581 0.0980 0.1307 0.0102  0.0089  0.0098  121 VAL A CG2 
1067 N  N   . HIS A 122 ? 0.1411 0.0799 0.1105 -0.0024 0.0055  0.0068  122 HIS A N   
1068 C  CA  . HIS A 122 ? 0.1387 0.0866 0.1134 0.0046  -0.0024 -0.0015 122 HIS A CA  
1069 C  C   . HIS A 122 ? 0.1457 0.0850 0.1342 0.0120  -0.0120 0.0109  122 HIS A C   
1070 O  O   . HIS A 122 ? 0.1466 0.0929 0.1272 -0.0038 -0.0142 0.0108  122 HIS A O   
1071 C  CB  . HIS A 122 ? 0.1441 0.0741 0.1596 0.0198  -0.0074 -0.0017 122 HIS A CB  
1072 C  CG  . HIS A 122 ? 0.1225 0.0938 0.1292 0.0035  0.0003  0.0156  122 HIS A CG  
1073 N  ND1 . HIS A 122 ? 0.1295 0.0816 0.1394 0.0028  -0.0017 -0.0026 122 HIS A ND1 
1074 C  CD2 . HIS A 122 ? 0.1310 0.1112 0.1486 0.0057  0.0003  -0.0041 122 HIS A CD2 
1075 C  CE1 . HIS A 122 ? 0.1158 0.1310 0.1409 -0.0087 -0.0013 0.0021  122 HIS A CE1 
1076 N  NE2 . HIS A 122 ? 0.1277 0.1240 0.1439 -0.0060 -0.0120 -0.0147 122 HIS A NE2 
1077 N  N   . TRP A 123 ? 0.1423 0.0791 0.1401 0.0049  0.0114  0.0114  123 TRP A N   
1078 C  CA  . TRP A 123 ? 0.1128 0.0927 0.1523 -0.0026 0.0196  -0.0097 123 TRP A CA  
1079 C  C   . TRP A 123 ? 0.1177 0.0846 0.1462 -0.0070 0.0019  0.0120  123 TRP A C   
1080 O  O   . TRP A 123 ? 0.1317 0.0942 0.1489 0.0032  -0.0074 -0.0092 123 TRP A O   
1081 C  CB  . TRP A 123 ? 0.1571 0.1134 0.1813 -0.0046 0.0277  0.0137  123 TRP A CB  
1082 C  CG  . TRP A 123 ? 0.2053 0.1237 0.1908 -0.0245 0.0220  0.0104  123 TRP A CG  
1083 C  CD1 . TRP A 123 ? 0.3131 0.0951 0.1696 -0.0283 0.0348  0.0049  123 TRP A CD1 
1084 C  CD2 . TRP A 123 ? 0.1798 0.1075 0.1854 -0.0264 0.0251  0.0083  123 TRP A CD2 
1085 N  NE1 . TRP A 123 ? 0.3001 0.1080 0.1901 -0.0159 0.0153  -0.0057 123 TRP A NE1 
1086 C  CE2 . TRP A 123 ? 0.2885 0.1008 0.2132 -0.0601 0.0153  0.0068  123 TRP A CE2 
1087 C  CE3 . TRP A 123 ? 0.2293 0.1077 0.2290 -0.0670 -0.0028 -0.0060 123 TRP A CE3 
1088 C  CZ2 . TRP A 123 ? 0.2150 0.1188 0.2411 -0.0285 0.0006  -0.0037 123 TRP A CZ2 
1089 C  CZ3 . TRP A 123 ? 0.2576 0.0860 0.2486 -0.0516 -0.0129 0.0044  123 TRP A CZ3 
1090 C  CH2 . TRP A 123 ? 0.2732 0.1134 0.2195 -0.0203 0.0088  0.0097  123 TRP A CH2 
1091 N  N   . ASN A 124 ? 0.1259 0.0886 0.1532 0.0049  -0.0017 0.0035  124 ASN A N   
1092 C  CA  . ASN A 124 ? 0.1384 0.0859 0.1550 0.0214  -0.0035 -0.0174 124 ASN A CA  
1093 C  C   . ASN A 124 ? 0.1231 0.0982 0.1626 0.0076  0.0020  -0.0225 124 ASN A C   
1094 O  O   . ASN A 124 ? 0.1268 0.0949 0.1669 0.0012  -0.0052 -0.0034 124 ASN A O   
1095 C  CB  . ASN A 124 ? 0.1243 0.1064 0.1615 0.0063  0.0229  -0.0089 124 ASN A CB  
1096 C  CG  . ASN A 124 ? 0.1568 0.1042 0.1719 0.0104  0.0153  -0.0044 124 ASN A CG  
1097 O  OD1 . ASN A 124 ? 0.1644 0.1076 0.1969 0.0153  0.0070  -0.0143 124 ASN A OD1 
1098 N  ND2 . ASN A 124 ? 0.1572 0.1199 0.1642 0.0120  0.0119  -0.0218 124 ASN A ND2 
1099 N  N   . THR A 125 ? 0.1577 0.0870 0.2061 0.0250  -0.0060 -0.0035 125 THR A N   
1100 C  CA  . THR A 125 ? 0.1606 0.1149 0.2237 0.0230  -0.0326 0.0163  125 THR A CA  
1101 C  C   . THR A 125 ? 0.1849 0.0821 0.2398 0.0228  0.0283  0.0017  125 THR A C   
1102 O  O   . THR A 125 ? 0.1939 0.1150 0.2485 0.0189  -0.0094 0.0251  125 THR A O   
1103 C  CB  . THR A 125 ? 0.1831 0.1520 0.3106 0.0171  -0.0794 0.0261  125 THR A CB  
1104 O  OG1 . THR A 125 ? 0.2084 0.1475 0.4386 0.0557  0.0082  0.0377  125 THR A OG1 
1105 C  CG2 . THR A 125 ? 0.2344 0.1748 0.3510 -0.0085 -0.1351 0.0366  125 THR A CG2 
1106 N  N   . LYS A 126 ? 0.1326 0.1120 0.2342 0.0111  0.0313  -0.0331 126 LYS A N   
1107 C  CA  . LYS A 126 ? 0.1752 0.1097 0.2165 0.0071  0.0223  -0.0315 126 LYS A CA  
1108 C  C   . LYS A 126 ? 0.2026 0.0821 0.2181 -0.0113 0.0300  -0.0233 126 LYS A C   
1109 O  O   . LYS A 126 ? 0.2396 0.1055 0.2545 -0.0135 0.0190  -0.0487 126 LYS A O   
1110 C  CB  . LYS A 126 ? 0.2436 0.1551 0.2312 -0.0137 -0.0305 -0.0513 126 LYS A CB  
1111 C  CG  . LYS A 126 ? 0.2152 0.1574 0.2117 -0.0136 0.0093  -0.0131 126 LYS A CG  
1112 C  CD  . LYS A 126 ? 0.4961 0.2737 0.1717 -0.0487 0.0582  -0.0746 126 LYS A CD  
1113 C  CE  . LYS A 126 ? 0.3583 0.3043 0.5261 0.1018  0.0015  -0.1370 126 LYS A CE  
1114 N  NZ  . LYS A 126 ? 0.8858 0.2635 0.7872 -0.0648 0.0403  -0.1939 126 LYS A NZ  
1115 N  N   . TYR A 127 ? 0.1504 0.0886 0.1730 0.0046  -0.0017 -0.0099 127 TYR A N   
1116 C  CA  . TYR A 127 ? 0.1597 0.1046 0.1639 -0.0052 -0.0122 -0.0162 127 TYR A CA  
1117 C  C   . TYR A 127 ? 0.1495 0.0888 0.1815 -0.0052 0.0030  -0.0307 127 TYR A C   
1118 O  O   . TYR A 127 ? 0.1628 0.1055 0.1781 -0.0233 0.0115  -0.0228 127 TYR A O   
1119 C  CB  . TYR A 127 ? 0.1644 0.1054 0.1818 -0.0005 0.0149  -0.0046 127 TYR A CB  
1120 C  CG  . TYR A 127 ? 0.1495 0.1159 0.1777 -0.0086 0.0000  -0.0098 127 TYR A CG  
1121 C  CD1 . TYR A 127 ? 0.1879 0.1071 0.1805 -0.0141 -0.0154 -0.0152 127 TYR A CD1 
1122 C  CD2 . TYR A 127 ? 0.1678 0.1021 0.1500 0.0006  0.0116  -0.0110 127 TYR A CD2 
1123 C  CE1 . TYR A 127 ? 0.2195 0.1454 0.1524 -0.0010 -0.0129 -0.0031 127 TYR A CE1 
1124 C  CE2 . TYR A 127 ? 0.1631 0.1222 0.1425 0.0164  -0.0034 -0.0226 127 TYR A CE2 
1125 C  CZ  . TYR A 127 ? 0.1590 0.1443 0.1592 0.0015  0.0249  -0.0170 127 TYR A CZ  
1126 O  OH  . TYR A 127 ? 0.2245 0.1583 0.1588 0.0162  0.0031  -0.0266 127 TYR A OH  
1127 N  N   . GLY A 128 ? 0.1752 0.0807 0.1800 -0.0086 -0.0140 -0.0010 128 GLY A N   
1128 C  CA  . GLY A 128 ? 0.1935 0.1077 0.1723 -0.0274 -0.0088 -0.0038 128 GLY A CA  
1129 C  C   . GLY A 128 ? 0.1651 0.1288 0.1386 -0.0255 -0.0137 0.0185  128 GLY A C   
1130 O  O   . GLY A 128 ? 0.2178 0.1055 0.1601 -0.0102 -0.0258 0.0155  128 GLY A O   
1131 N  N   . ASP A 129 ? 0.1739 0.1167 0.1703 -0.0010 -0.0126 -0.0048 129 ASP A N   
1132 C  CA  . ASP A 129 ? 0.1958 0.1089 0.1580 -0.0035 -0.0212 -0.0006 129 ASP A CA  
1133 C  C   . ASP A 129 ? 0.1710 0.1242 0.1500 -0.0253 -0.0192 -0.0006 129 ASP A C   
1134 O  O   . ASP A 129 ? 0.1856 0.1172 0.1439 0.0027  -0.0267 -0.0080 129 ASP A O   
1135 C  CB  . ASP A 129 ? 0.1829 0.1490 0.1493 0.0034  -0.0151 -0.0080 129 ASP A CB  
1136 C  CG  . ASP A 129 ? 0.1768 0.1036 0.1843 0.0114  0.0094  -0.0183 129 ASP A CG  
1137 O  OD1 . ASP A 129 ? 0.2122 0.1594 0.2120 -0.0065 -0.0355 0.0087  129 ASP A OD1 
1138 O  OD2 . ASP A 129 ? 0.1890 0.1784 0.2642 0.0103  0.0212  0.0181  129 ASP A OD2 
1139 N  N   A VAL A 130 ? 0.1495 0.1134 0.1604 -0.0362 -0.0008 -0.0176 130 VAL A N   
1140 N  N   B VAL A 130 ? 0.1976 0.0960 0.1675 0.0005  -0.0275 -0.0006 130 VAL A N   
1141 C  CA  A VAL A 130 ? 0.1899 0.1037 0.1628 -0.0241 -0.0006 -0.0405 130 VAL A CA  
1142 C  CA  B VAL A 130 ? 0.1795 0.1200 0.1547 0.0335  -0.0208 -0.0035 130 VAL A CA  
1143 C  C   A VAL A 130 ? 0.1655 0.0969 0.1351 0.0107  0.0220  -0.0261 130 VAL A C   
1144 C  C   B VAL A 130 ? 0.1991 0.1127 0.1533 -0.0093 -0.0126 -0.0164 130 VAL A C   
1145 O  O   A VAL A 130 ? 0.1170 0.1184 0.1222 -0.0093 0.0265  -0.0032 130 VAL A O   
1146 O  O   B VAL A 130 ? 0.1587 0.1146 0.1499 0.0054  -0.0195 -0.0147 130 VAL A O   
1147 C  CB  A VAL A 130 ? 0.1052 0.0790 0.1635 -0.0074 0.0031  -0.0346 130 VAL A CB  
1148 C  CB  B VAL A 130 ? 0.2384 0.1342 0.1685 -0.0156 0.0120  -0.0331 130 VAL A CB  
1149 C  CG1 A VAL A 130 ? 0.1630 0.1084 0.1276 -0.0344 0.0063  -0.0265 130 VAL A CG1 
1150 C  CG1 B VAL A 130 ? 0.2590 0.1152 0.2415 -0.0041 0.0184  -0.0710 130 VAL A CG1 
1151 C  CG2 A VAL A 130 ? 0.1287 0.0930 0.1567 0.0201  -0.0142 -0.0537 130 VAL A CG2 
1152 C  CG2 B VAL A 130 ? 0.2321 0.1608 0.2321 -0.0478 0.0509  -0.0258 130 VAL A CG2 
1153 N  N   . GLY A 131 ? 0.1692 0.1396 0.1437 -0.0147 0.0052  -0.0088 131 GLY A N   
1154 C  CA  . GLY A 131 ? 0.1660 0.1407 0.1723 -0.0126 0.0241  -0.0110 131 GLY A CA  
1155 C  C   . GLY A 131 ? 0.1468 0.1238 0.1578 -0.0217 0.0080  0.0092  131 GLY A C   
1156 O  O   . GLY A 131 ? 0.1835 0.1506 0.1570 -0.0052 0.0197  -0.0065 131 GLY A O   
1157 N  N   A LYS A 132 ? 0.1712 0.1120 0.1310 -0.0270 0.0057  -0.0041 132 LYS A N   
1158 N  N   B LYS A 132 ? 0.1676 0.1143 0.1310 -0.0308 0.0073  -0.0032 132 LYS A N   
1159 C  CA  A LYS A 132 ? 0.1529 0.1107 0.1438 -0.0214 -0.0013 0.0089  132 LYS A CA  
1160 C  CA  B LYS A 132 ? 0.1622 0.1200 0.1457 -0.0262 -0.0078 0.0038  132 LYS A CA  
1161 C  C   A LYS A 132 ? 0.1319 0.1137 0.1224 -0.0199 0.0114  -0.0031 132 LYS A C   
1162 C  C   B LYS A 132 ? 0.1721 0.1140 0.1411 -0.0329 -0.0031 -0.0098 132 LYS A C   
1163 O  O   A LYS A 132 ? 0.1220 0.0935 0.1217 -0.0227 0.0046  -0.0302 132 LYS A O   
1164 O  O   B LYS A 132 ? 0.1313 0.1181 0.1430 0.0006  0.0086  0.0000  132 LYS A O   
1165 C  CB  A LYS A 132 ? 0.1477 0.1107 0.1895 0.0024  0.0062  0.0372  132 LYS A CB  
1166 C  CB  B LYS A 132 ? 0.1299 0.1254 0.1637 -0.0207 -0.0335 0.0078  132 LYS A CB  
1167 C  CG  A LYS A 132 ? 0.1764 0.1586 0.2434 -0.0408 0.0758  0.0333  132 LYS A CG  
1168 C  CG  B LYS A 132 ? 0.2075 0.0769 0.1904 -0.0177 -0.0588 0.0307  132 LYS A CG  
1169 C  CD  A LYS A 132 ? 0.2215 0.1297 0.2784 -0.0417 0.0372  0.0395  132 LYS A CD  
1170 C  CD  B LYS A 132 ? 0.2364 0.1186 0.1869 -0.0307 -0.0430 -0.0230 132 LYS A CD  
1171 C  CE  A LYS A 132 ? 0.2640 0.1545 0.2874 -0.0573 0.0797  0.0478  132 LYS A CE  
1172 C  CE  B LYS A 132 ? 0.2694 0.1985 0.1709 -0.0758 -0.0520 0.0141  132 LYS A CE  
1173 N  NZ  A LYS A 132 ? 0.2861 0.2840 0.4102 -0.1054 0.0395  -0.0258 132 LYS A NZ  
1174 N  NZ  B LYS A 132 ? 0.2649 0.1628 0.2187 -0.0427 0.0077  0.0425  132 LYS A NZ  
1175 N  N   . ALA A 133 ? 0.1364 0.0997 0.1423 -0.0241 -0.0013 -0.0024 133 ALA A N   
1176 C  CA  . ALA A 133 ? 0.1492 0.1102 0.1335 -0.0210 -0.0074 0.0057  133 ALA A CA  
1177 C  C   . ALA A 133 ? 0.1551 0.1070 0.1279 -0.0082 -0.0013 0.0008  133 ALA A C   
1178 O  O   . ALA A 133 ? 0.1351 0.1186 0.1283 -0.0037 0.0008  -0.0080 133 ALA A O   
1179 C  CB  . ALA A 133 ? 0.1461 0.1134 0.1330 -0.0144 -0.0077 0.0066  133 ALA A CB  
1180 N  N   . LEU A 134 ? 0.1554 0.0926 0.1362 -0.0066 -0.0052 -0.0005 134 LEU A N   
1181 C  CA  . LEU A 134 ? 0.1456 0.1351 0.1301 0.0133  0.0082  0.0161  134 LEU A CA  
1182 C  C   . LEU A 134 ? 0.1268 0.1170 0.1304 -0.0057 0.0157  0.0175  134 LEU A C   
1183 O  O   . LEU A 134 ? 0.1629 0.1374 0.1791 0.0099  -0.0017 0.0147  134 LEU A O   
1184 C  CB  . LEU A 134 ? 0.1793 0.1204 0.1581 -0.0168 0.0324  -0.0068 134 LEU A CB  
1185 C  CG  . LEU A 134 ? 0.2531 0.1624 0.1472 0.0189  0.0211  -0.0195 134 LEU A CG  
1186 C  CD1 . LEU A 134 ? 0.4151 0.2017 0.2010 -0.0627 0.1138  -0.0443 134 LEU A CD1 
1187 C  CD2 . LEU A 134 ? 0.3034 0.1509 0.1835 -0.0465 0.0189  -0.0351 134 LEU A CD2 
1188 N  N   . GLN A 135 ? 0.1475 0.1172 0.1518 -0.0277 0.0114  0.0068  135 GLN A N   
1189 C  CA  . GLN A 135 ? 0.1703 0.1378 0.1524 -0.0465 0.0114  -0.0035 135 GLN A CA  
1190 C  C   . GLN A 135 ? 0.1506 0.1313 0.1479 -0.0148 -0.0160 -0.0085 135 GLN A C   
1191 O  O   . GLN A 135 ? 0.1741 0.1798 0.1595 -0.0472 0.0013  -0.0337 135 GLN A O   
1192 C  CB  . GLN A 135 ? 0.1703 0.1545 0.1825 -0.0612 0.0140  0.0006  135 GLN A CB  
1193 C  CG  . GLN A 135 ? 0.2064 0.2242 0.1978 -0.0729 0.0322  0.0205  135 GLN A CG  
1194 C  CD  . GLN A 135 ? 0.1949 0.2576 0.2269 -0.0636 0.0166  0.0271  135 GLN A CD  
1195 O  OE1 . GLN A 135 ? 0.3361 0.3725 0.3686 -0.1655 -0.0300 0.0430  135 GLN A OE1 
1196 N  NE2 . GLN A 135 ? 0.3075 0.2962 0.2761 -0.0861 0.0097  0.0595  135 GLN A NE2 
1197 N  N   . GLN A 136 ? 0.1281 0.1094 0.1448 -0.0049 0.0143  -0.0008 136 GLN A N   
1198 C  CA  . GLN A 136 ? 0.1511 0.1071 0.1392 -0.0092 0.0032  -0.0078 136 GLN A CA  
1199 C  C   . GLN A 136 ? 0.1326 0.1084 0.1174 0.0000  0.0109  -0.0109 136 GLN A C   
1200 O  O   . GLN A 136 ? 0.1353 0.1091 0.1305 -0.0040 0.0015  -0.0162 136 GLN A O   
1201 C  CB  . GLN A 136 ? 0.1714 0.1138 0.1401 0.0010  -0.0151 -0.0040 136 GLN A CB  
1202 C  CG  . GLN A 136 ? 0.2239 0.1479 0.1543 0.0383  0.0001  0.0237  136 GLN A CG  
1203 C  CD  . GLN A 136 ? 0.2662 0.0962 0.2718 -0.0104 0.0013  0.0198  136 GLN A CD  
1204 O  OE1 . GLN A 136 ? 0.4268 0.1662 0.3567 0.0201  -0.1033 -0.0762 136 GLN A OE1 
1205 N  NE2 . GLN A 136 ? 0.4652 0.1773 0.3138 -0.0861 -0.1050 -0.0531 136 GLN A NE2 
1206 N  N   . PRO A 137 ? 0.1333 0.1085 0.1344 -0.0040 0.0024  -0.0163 137 PRO A N   
1207 C  CA  . PRO A 137 ? 0.1283 0.1195 0.1286 -0.0028 0.0015  -0.0057 137 PRO A CA  
1208 C  C   . PRO A 137 ? 0.1340 0.1215 0.1295 0.0003  0.0071  -0.0057 137 PRO A C   
1209 O  O   . PRO A 137 ? 0.1574 0.1279 0.2025 0.0003  0.0068  0.0046  137 PRO A O   
1210 C  CB  . PRO A 137 ? 0.2081 0.1576 0.1237 -0.0085 0.0043  -0.0138 137 PRO A CB  
1211 C  CG  . PRO A 137 ? 0.3393 0.1989 0.1702 -0.0162 -0.0052 -0.0074 137 PRO A CG  
1212 C  CD  . PRO A 137 ? 0.1804 0.1371 0.1439 -0.0265 -0.0190 -0.0239 137 PRO A CD  
1213 N  N   . ASP A 138 ? 0.1136 0.1231 0.1425 -0.0113 -0.0026 0.0082  138 ASP A N   
1214 C  CA  . ASP A 138 ? 0.1230 0.1326 0.1312 -0.0209 0.0137  -0.0046 138 ASP A CA  
1215 C  C   . ASP A 138 ? 0.1080 0.1215 0.1421 -0.0153 0.0057  -0.0051 138 ASP A C   
1216 O  O   . ASP A 138 ? 0.1261 0.1307 0.1536 0.0006  0.0098  0.0005  138 ASP A O   
1217 C  CB  . ASP A 138 ? 0.1590 0.1716 0.1486 0.0272  0.0295  -0.0035 138 ASP A CB  
1218 C  CG  . ASP A 138 ? 0.1297 0.1969 0.1897 0.0214  0.0272  -0.0265 138 ASP A CG  
1219 O  OD1 . ASP A 138 ? 0.1999 0.1276 0.1726 0.0119  0.0154  -0.0190 138 ASP A OD1 
1220 O  OD2 . ASP A 138 ? 0.1976 0.2111 0.1947 0.0509  0.0167  -0.0520 138 ASP A OD2 
1221 N  N   . GLY A 139 ? 0.1253 0.0992 0.1125 -0.0035 0.0041  -0.0104 139 GLY A N   
1222 C  CA  . GLY A 139 ? 0.1333 0.1082 0.1105 -0.0125 0.0007  -0.0046 139 GLY A CA  
1223 C  C   . GLY A 139 ? 0.0829 0.0918 0.1141 -0.0024 0.0082  0.0085  139 GLY A C   
1224 O  O   . GLY A 139 ? 0.1154 0.0954 0.1450 0.0086  -0.0041 0.0034  139 GLY A O   
1225 N  N   A LEU A 140 ? 0.0983 0.0838 0.1337 0.0019  0.0030  -0.0041 140 LEU A N   
1226 N  N   B LEU A 140 ? 0.0933 0.0804 0.1425 -0.0044 0.0237  -0.0049 140 LEU A N   
1227 C  CA  A LEU A 140 ? 0.1167 0.0755 0.1163 -0.0040 0.0060  -0.0048 140 LEU A CA  
1228 C  CA  B LEU A 140 ? 0.1052 0.0771 0.1253 0.0063  0.0135  0.0003  140 LEU A CA  
1229 C  C   A LEU A 140 ? 0.1019 0.0640 0.1068 0.0074  0.0035  -0.0066 140 LEU A C   
1230 C  C   B LEU A 140 ? 0.1048 0.0667 0.1130 0.0027  0.0088  -0.0099 140 LEU A C   
1231 O  O   A LEU A 140 ? 0.1014 0.0958 0.1143 -0.0040 -0.0046 -0.0055 140 LEU A O   
1232 O  O   B LEU A 140 ? 0.0974 0.0897 0.1202 0.0102  0.0065  -0.0059 140 LEU A O   
1233 C  CB  A LEU A 140 ? 0.1261 0.1102 0.1213 0.0121  0.0055  0.0073  140 LEU A CB  
1234 C  CB  B LEU A 140 ? 0.1165 0.0978 0.1152 0.0141  0.0020  -0.0085 140 LEU A CB  
1235 C  CG  A LEU A 140 ? 0.1154 0.0987 0.1495 -0.0060 0.0038  0.0023  140 LEU A CG  
1236 C  CG  B LEU A 140 ? 0.0847 0.1279 0.1306 0.0177  0.0222  -0.0006 140 LEU A CG  
1237 C  CD1 A LEU A 140 ? 0.1170 0.1395 0.1581 -0.0131 -0.0085 -0.0293 140 LEU A CD1 
1238 C  CD1 B LEU A 140 ? 0.1377 0.1138 0.1644 0.0080  0.0392  -0.0086 140 LEU A CD1 
1239 C  CD2 A LEU A 140 ? 0.1928 0.0874 0.1084 0.0240  0.0210  0.0031  140 LEU A CD2 
1240 C  CD2 B LEU A 140 ? 0.1116 0.1921 0.0983 0.0197  0.0176  -0.0320 140 LEU A CD2 
1241 N  N   . ALA A 141 ? 0.1067 0.0833 0.1154 -0.0054 0.0052  -0.0021 141 ALA A N   
1242 C  CA  . ALA A 141 ? 0.1208 0.0803 0.1286 -0.0085 0.0088  -0.0081 141 ALA A CA  
1243 C  C   . ALA A 141 ? 0.0948 0.0846 0.1040 -0.0143 -0.0006 0.0071  141 ALA A C   
1244 O  O   . ALA A 141 ? 0.1556 0.0857 0.1071 0.0000  -0.0070 0.0073  141 ALA A O   
1245 C  CB  . ALA A 141 ? 0.1247 0.1019 0.1518 -0.0211 0.0138  0.0093  141 ALA A CB  
1246 N  N   . VAL A 142 ? 0.1143 0.0860 0.0996 0.0030  0.0020  -0.0024 142 VAL A N   
1247 C  CA  . VAL A 142 ? 0.1146 0.0951 0.0915 -0.0122 0.0003  -0.0026 142 VAL A CA  
1248 C  C   . VAL A 142 ? 0.0915 0.0835 0.0951 0.0007  -0.0019 0.0043  142 VAL A C   
1249 O  O   . VAL A 142 ? 0.1118 0.0868 0.0900 -0.0024 -0.0082 0.0041  142 VAL A O   
1250 C  CB  . VAL A 142 ? 0.1010 0.1195 0.0987 0.0015  0.0037  -0.0032 142 VAL A CB  
1251 C  CG1 . VAL A 142 ? 0.1161 0.1233 0.0940 0.0104  -0.0007 -0.0073 142 VAL A CG1 
1252 C  CG2 . VAL A 142 ? 0.1274 0.1337 0.1251 -0.0071 0.0109  -0.0010 142 VAL A CG2 
1253 N  N   . LEU A 143 ? 0.0994 0.0771 0.0978 -0.0031 -0.0086 -0.0049 143 LEU A N   
1254 C  CA  . LEU A 143 ? 0.0948 0.0895 0.1086 -0.0055 -0.0126 -0.0065 143 LEU A CA  
1255 C  C   . LEU A 143 ? 0.1046 0.0952 0.0843 -0.0228 -0.0059 -0.0003 143 LEU A C   
1256 O  O   . LEU A 143 ? 0.1502 0.0933 0.0954 -0.0071 0.0031  -0.0024 143 LEU A O   
1257 C  CB  . LEU A 143 ? 0.1328 0.1313 0.1145 -0.0041 -0.0140 0.0161  143 LEU A CB  
1258 C  CG  . LEU A 143 ? 0.1459 0.1317 0.1504 -0.0110 -0.0131 0.0010  143 LEU A CG  
1259 C  CD1 . LEU A 143 ? 0.1563 0.1926 0.1577 -0.0231 0.0118  0.0313  143 LEU A CD1 
1260 C  CD2 . LEU A 143 ? 0.1215 0.2050 0.1520 0.0081  -0.0240 0.0329  143 LEU A CD2 
1261 N  N   . GLY A 144 ? 0.1195 0.0802 0.0949 -0.0026 -0.0049 -0.0013 144 GLY A N   
1262 C  CA  . GLY A 144 ? 0.1080 0.0785 0.0974 -0.0074 0.0133  -0.0094 144 GLY A CA  
1263 C  C   . GLY A 144 ? 0.0929 0.0857 0.0822 0.0082  -0.0021 0.0044  144 GLY A C   
1264 O  O   . GLY A 144 ? 0.1155 0.0988 0.0933 -0.0109 0.0104  -0.0041 144 GLY A O   
1265 N  N   . ILE A 145 ? 0.0933 0.0800 0.0807 -0.0003 -0.0076 0.0000  145 ILE A N   
1266 C  CA  . ILE A 145 ? 0.1093 0.0918 0.0877 0.0068  -0.0082 -0.0023 145 ILE A CA  
1267 C  C   . ILE A 145 ? 0.0891 0.0917 0.0903 0.0028  0.0031  0.0013  145 ILE A C   
1268 O  O   . ILE A 145 ? 0.1127 0.0927 0.1054 0.0046  0.0027  0.0007  145 ILE A O   
1269 C  CB  . ILE A 145 ? 0.1203 0.1024 0.0973 0.0000  -0.0142 0.0076  145 ILE A CB  
1270 C  CG1 . ILE A 145 ? 0.1499 0.1188 0.1468 0.0297  -0.0175 -0.0013 145 ILE A CG1 
1271 C  CG2 . ILE A 145 ? 0.1289 0.1299 0.1439 -0.0038 -0.0260 0.0065  145 ILE A CG2 
1272 C  CD1 . ILE A 145 ? 0.1333 0.1414 0.1425 0.0266  -0.0252 0.0115  145 ILE A CD1 
1273 N  N   . PHE A 146 ? 0.0982 0.0825 0.0842 -0.0037 -0.0098 -0.0026 146 PHE A N   
1274 C  CA  . PHE A 146 ? 0.1048 0.0817 0.0851 -0.0024 -0.0049 0.0020  146 PHE A CA  
1275 C  C   . PHE A 146 ? 0.1058 0.0920 0.0901 -0.0037 0.0082  -0.0010 146 PHE A C   
1276 O  O   . PHE A 146 ? 0.1098 0.1091 0.1112 -0.0006 -0.0076 -0.0099 146 PHE A O   
1277 C  CB  . PHE A 146 ? 0.1140 0.0791 0.0834 -0.0044 -0.0017 0.0071  146 PHE A CB  
1278 C  CG  . PHE A 146 ? 0.1030 0.0851 0.0842 0.0006  -0.0034 0.0137  146 PHE A CG  
1279 C  CD1 . PHE A 146 ? 0.0978 0.0885 0.0900 0.0087  0.0013  0.0091  146 PHE A CD1 
1280 C  CD2 . PHE A 146 ? 0.1353 0.0837 0.0885 -0.0055 0.0031  0.0179  146 PHE A CD2 
1281 C  CE1 . PHE A 146 ? 0.1026 0.0816 0.0944 -0.0013 -0.0152 0.0076  146 PHE A CE1 
1282 C  CE2 . PHE A 146 ? 0.1137 0.0856 0.0966 0.0031  -0.0027 0.0204  146 PHE A CE2 
1283 C  CZ  . PHE A 146 ? 0.1068 0.0939 0.0980 -0.0017 -0.0122 0.0200  146 PHE A CZ  
1284 N  N   . LEU A 147 ? 0.1134 0.0933 0.0842 -0.0071 0.0105  0.0010  147 LEU A N   
1285 C  CA  . LEU A 147 ? 0.1393 0.0830 0.0813 -0.0104 -0.0008 -0.0125 147 LEU A CA  
1286 C  C   . LEU A 147 ? 0.1076 0.1008 0.1003 -0.0089 0.0012  -0.0041 147 LEU A C   
1287 O  O   . LEU A 147 ? 0.1188 0.0838 0.1242 -0.0115 -0.0015 -0.0010 147 LEU A O   
1288 C  CB  . LEU A 147 ? 0.1405 0.0942 0.0842 -0.0126 -0.0104 0.0020  147 LEU A CB  
1289 C  CG  . LEU A 147 ? 0.1712 0.0846 0.0958 -0.0252 -0.0152 -0.0015 147 LEU A CG  
1290 C  CD1 . LEU A 147 ? 0.1840 0.1057 0.0996 -0.0094 -0.0375 0.0041  147 LEU A CD1 
1291 C  CD2 . LEU A 147 ? 0.1664 0.1387 0.1006 -0.0031 -0.0116 0.0091  147 LEU A CD2 
1292 N  N   . LYS A 148 ? 0.1335 0.0863 0.1158 -0.0217 -0.0015 -0.0159 148 LYS A N   
1293 C  CA  . LYS A 148 ? 0.1592 0.0933 0.1145 -0.0115 -0.0048 0.0017  148 LYS A CA  
1294 C  C   . LYS A 148 ? 0.1242 0.1137 0.1486 -0.0065 -0.0111 -0.0166 148 LYS A C   
1295 O  O   . LYS A 148 ? 0.1565 0.1349 0.1237 -0.0013 -0.0285 -0.0092 148 LYS A O   
1296 C  CB  . LYS A 148 ? 0.1434 0.1075 0.1428 -0.0208 0.0015  0.0021  148 LYS A CB  
1297 C  CG  . LYS A 148 ? 0.1723 0.1463 0.1635 -0.0229 0.0263  0.0120  148 LYS A CG  
1298 C  CD  . LYS A 148 ? 0.1944 0.2370 0.2526 -0.0182 0.0315  0.0701  148 LYS A CD  
1299 C  CE  . LYS A 148 ? 0.2285 0.4444 0.3084 -0.1274 0.0631  0.0566  148 LYS A CE  
1300 N  NZ  . LYS A 148 ? 0.4273 0.5044 0.4650 -0.1457 0.1088  0.1527  148 LYS A NZ  
1301 N  N   . VAL A 149 ? 0.1595 0.1057 0.1452 -0.0153 -0.0199 -0.0251 149 VAL A N   
1302 C  CA  . VAL A 149 ? 0.1789 0.1141 0.1315 -0.0186 -0.0159 -0.0292 149 VAL A CA  
1303 C  C   . VAL A 149 ? 0.1965 0.1258 0.1673 -0.0205 -0.0307 -0.0054 149 VAL A C   
1304 O  O   . VAL A 149 ? 0.2370 0.1470 0.2066 -0.0452 -0.0401 0.0073  149 VAL A O   
1305 C  CB  . VAL A 149 ? 0.2059 0.1558 0.1339 0.0148  -0.0161 -0.0251 149 VAL A CB  
1306 C  CG1 . VAL A 149 ? 0.2050 0.2456 0.1491 -0.0099 -0.0109 -0.0601 149 VAL A CG1 
1307 C  CG2 . VAL A 149 ? 0.2028 0.2066 0.1847 0.0085  -0.0247 -0.0111 149 VAL A CG2 
1308 N  N   . GLY A 150 ? 0.1761 0.1533 0.1757 -0.0410 -0.0326 -0.0003 150 GLY A N   
1309 C  CA  . GLY A 150 ? 0.2278 0.2237 0.2025 -0.0847 -0.0263 0.0073  150 GLY A CA  
1310 C  C   . GLY A 150 ? 0.2016 0.2028 0.1910 -0.0817 -0.0241 0.0015  150 GLY A C   
1311 O  O   . GLY A 150 ? 0.2071 0.1924 0.1930 -0.0890 -0.0144 -0.0217 150 GLY A O   
1312 N  N   A SER A 151 ? 0.2424 0.2089 0.1626 -0.0900 -0.0137 -0.0309 151 SER A N   
1313 N  N   B SER A 151 ? 0.2443 0.2150 0.1710 -0.0886 -0.0107 -0.0335 151 SER A N   
1314 C  CA  A SER A 151 ? 0.2202 0.2267 0.2012 -0.0860 -0.0096 -0.0386 151 SER A CA  
1315 C  CA  B SER A 151 ? 0.2029 0.2052 0.2106 -0.0892 0.0126  -0.0340 151 SER A CA  
1316 C  C   A SER A 151 ? 0.2136 0.1831 0.1608 -0.0467 -0.0154 -0.0715 151 SER A C   
1317 C  C   B SER A 151 ? 0.1764 0.1878 0.1631 -0.0668 0.0043  -0.0368 151 SER A C   
1318 O  O   A SER A 151 ? 0.1277 0.1720 0.1394 -0.0133 -0.0162 -0.0555 151 SER A O   
1319 O  O   B SER A 151 ? 0.1858 0.1757 0.1414 -0.0208 -0.0140 -0.0405 151 SER A O   
1320 C  CB  A SER A 151 ? 0.1926 0.2127 0.3185 -0.1500 -0.0220 -0.0388 151 SER A CB  
1321 C  CB  B SER A 151 ? 0.2535 0.1597 0.3222 -0.0643 0.0566  -0.0891 151 SER A CB  
1322 O  OG  A SER A 151 ? 0.2278 0.3298 0.2612 -0.0710 0.0208  -0.0397 151 SER A OG  
1323 O  OG  B SER A 151 ? 0.1897 0.3348 0.3255 -0.0939 0.0108  0.0566  151 SER A OG  
1324 N  N   . ALA A 152 ? 0.1721 0.1906 0.1721 -0.0548 -0.0153 -0.0208 152 ALA A N   
1325 C  CA  . ALA A 152 ? 0.1967 0.1841 0.1612 -0.0085 -0.0152 -0.0286 152 ALA A CA  
1326 C  C   . ALA A 152 ? 0.1804 0.2125 0.1454 -0.0026 -0.0260 -0.0276 152 ALA A C   
1327 O  O   . ALA A 152 ? 0.1888 0.2148 0.2106 -0.0483 0.0057  -0.0324 152 ALA A O   
1328 C  CB  . ALA A 152 ? 0.2639 0.2551 0.1525 -0.0597 -0.0368 -0.0197 152 ALA A CB  
1329 N  N   . LYS A 153 ? 0.2017 0.1653 0.1788 -0.0263 -0.0315 -0.0089 153 LYS A N   
1330 C  CA  . LYS A 153 ? 0.1835 0.1747 0.2005 0.0048  -0.0255 -0.0032 153 LYS A CA  
1331 C  C   . LYS A 153 ? 0.1628 0.1981 0.2072 0.0001  -0.0430 -0.0001 153 LYS A C   
1332 O  O   . LYS A 153 ? 0.1642 0.2291 0.1642 -0.0015 -0.0372 0.0032  153 LYS A O   
1333 C  CB  . LYS A 153 ? 0.1522 0.1881 0.2084 0.0193  -0.0408 -0.0193 153 LYS A CB  
1334 C  CG  . LYS A 153 ? 0.2702 0.1536 0.1770 0.0118  -0.0480 -0.0203 153 LYS A CG  
1335 C  CD  . LYS A 153 ? 0.3389 0.1924 0.1787 -0.0305 -0.0288 -0.0399 153 LYS A CD  
1336 C  CE  . LYS A 153 ? 0.4007 0.2201 0.1993 0.0172  -0.0007 -0.0228 153 LYS A CE  
1337 N  NZ  . LYS A 153 ? 0.3697 0.3504 0.1955 0.0584  -0.0065 0.0000  153 LYS A NZ  
1338 N  N   . PRO A 154 ? 0.1700 0.2651 0.2113 0.0115  -0.0645 0.0019  154 PRO A N   
1339 C  CA  . PRO A 154 ? 0.1752 0.2958 0.2354 0.0126  -0.0148 0.0372  154 PRO A CA  
1340 C  C   . PRO A 154 ? 0.1763 0.2903 0.1910 0.0284  -0.0630 0.0350  154 PRO A C   
1341 O  O   . PRO A 154 ? 0.2068 0.3131 0.2325 -0.0288 -0.0680 0.0776  154 PRO A O   
1342 C  CB  . PRO A 154 ? 0.1554 0.2980 0.2673 -0.0091 0.0031  0.0086  154 PRO A CB  
1343 C  CG  . PRO A 154 ? 0.2800 0.4291 0.2552 0.0164  -0.0313 0.0702  154 PRO A CG  
1344 C  CD  . PRO A 154 ? 0.2081 0.2876 0.2307 -0.0292 0.0060  -0.0003 154 PRO A CD  
1345 N  N   . GLY A 155 ? 0.1915 0.2536 0.2592 0.0636  -0.0542 0.0201  155 GLY A N   
1346 C  CA  . GLY A 155 ? 0.2405 0.2515 0.2791 0.0394  -0.0465 0.0683  155 GLY A CA  
1347 C  C   . GLY A 155 ? 0.2344 0.2073 0.2093 0.0476  -0.0573 0.0395  155 GLY A C   
1348 O  O   . GLY A 155 ? 0.2721 0.2184 0.2933 0.0646  -0.0355 0.0634  155 GLY A O   
1349 N  N   . LEU A 156 ? 0.2284 0.1817 0.2087 0.0238  -0.0317 0.0153  156 LEU A N   
1350 C  CA  . LEU A 156 ? 0.2211 0.2014 0.1799 0.0210  -0.0386 0.0003  156 LEU A CA  
1351 C  C   . LEU A 156 ? 0.2186 0.1394 0.1563 0.0060  -0.0458 -0.0055 156 LEU A C   
1352 O  O   . LEU A 156 ? 0.2039 0.1815 0.1549 -0.0226 -0.0535 -0.0152 156 LEU A O   
1353 C  CB  . LEU A 156 ? 0.2100 0.1651 0.1613 -0.0293 -0.0627 0.0078  156 LEU A CB  
1354 C  CG  . LEU A 156 ? 0.2020 0.1788 0.1601 -0.0137 -0.0537 -0.0041 156 LEU A CG  
1355 C  CD1 . LEU A 156 ? 0.2260 0.1929 0.1554 -0.0439 -0.0445 -0.0199 156 LEU A CD1 
1356 C  CD2 . LEU A 156 ? 0.1658 0.2183 0.1886 0.0043  -0.0504 0.0177  156 LEU A CD2 
1357 N  N   . GLN A 157 ? 0.1894 0.2120 0.1710 -0.0221 -0.0553 0.0329  157 GLN A N   
1358 C  CA  . GLN A 157 ? 0.2411 0.2721 0.1295 -0.0584 -0.0544 -0.0051 157 GLN A CA  
1359 C  C   . GLN A 157 ? 0.2012 0.2096 0.1499 0.0074  -0.0575 -0.0083 157 GLN A C   
1360 O  O   . GLN A 157 ? 0.2151 0.2193 0.1588 0.0126  -0.0562 -0.0129 157 GLN A O   
1361 C  CB  . GLN A 157 ? 0.2339 0.2951 0.2098 -0.0575 -0.0736 -0.0003 157 GLN A CB  
1362 C  CG  . GLN A 157 ? 0.3183 0.3088 0.1840 -0.0401 -0.1185 -0.0430 157 GLN A CG  
1363 C  CD  . GLN A 157 ? 0.3018 0.2682 0.1886 -0.0339 -0.0908 0.0126  157 GLN A CD  
1364 O  OE1 . GLN A 157 ? 0.3167 0.1935 0.1644 -0.0559 -0.0465 -0.0094 157 GLN A OE1 
1365 N  NE2 . GLN A 157 ? 0.3851 0.2267 0.2221 -0.0670 -0.0912 -0.0179 157 GLN A NE2 
1366 N  N   . LYS A 158 ? 0.2290 0.2353 0.1646 -0.0038 -0.0684 0.0262  158 LYS A N   
1367 C  CA  . LYS A 158 ? 0.2050 0.2429 0.1675 0.0140  -0.0531 0.0359  158 LYS A CA  
1368 C  C   . LYS A 158 ? 0.2165 0.2339 0.1522 0.0195  -0.0434 0.0274  158 LYS A C   
1369 O  O   . LYS A 158 ? 0.2648 0.1999 0.1466 -0.0074 -0.0432 0.0126  158 LYS A O   
1370 C  CB  . LYS A 158 ? 0.2703 0.2460 0.2254 0.0031  -0.0581 0.0608  158 LYS A CB  
1371 C  CG  . LYS A 158 ? 0.2847 0.4759 0.3294 0.0923  -0.0948 0.0143  158 LYS A CG  
1372 C  CD  . LYS A 158 ? 0.3546 0.5860 0.5627 0.0690  -0.1787 -0.0979 158 LYS A CD  
1373 C  CE  . LYS A 158 ? 0.5582 0.4408 0.6373 -0.0449 -0.3438 -0.0560 158 LYS A CE  
1374 N  NZ  . LYS A 158 ? 1.0307 0.3763 0.6076 0.1929  -0.3616 0.0447  158 LYS A NZ  
1375 N  N   . VAL A 159 ? 0.2348 0.1701 0.1310 0.0206  -0.0326 -0.0140 159 VAL A N   
1376 C  CA  . VAL A 159 ? 0.2102 0.1583 0.1448 -0.0148 -0.0485 0.0059  159 VAL A CA  
1377 C  C   . VAL A 159 ? 0.2070 0.1536 0.1531 -0.0070 -0.0436 0.0107  159 VAL A C   
1378 O  O   . VAL A 159 ? 0.2274 0.1743 0.1596 -0.0137 -0.0469 0.0034  159 VAL A O   
1379 C  CB  . VAL A 159 ? 0.2520 0.1612 0.1307 -0.0093 -0.0474 -0.0130 159 VAL A CB  
1380 C  CG1 . VAL A 159 ? 0.2210 0.2192 0.1635 -0.0370 -0.0736 0.0137  159 VAL A CG1 
1381 C  CG2 . VAL A 159 ? 0.2676 0.1712 0.1736 0.0307  -0.0659 -0.0306 159 VAL A CG2 
1382 N  N   . VAL A 160 ? 0.2107 0.1439 0.1321 0.0102  -0.0296 -0.0019 160 VAL A N   
1383 C  CA  . VAL A 160 ? 0.2312 0.1588 0.1490 0.0350  -0.0313 0.0044  160 VAL A CA  
1384 C  C   . VAL A 160 ? 0.2046 0.1875 0.1732 -0.0520 0.0000  0.0006  160 VAL A C   
1385 O  O   . VAL A 160 ? 0.2400 0.1646 0.1599 -0.0256 0.0041  -0.0013 160 VAL A O   
1386 C  CB  . VAL A 160 ? 0.5217 0.1628 0.1642 0.0562  0.0306  0.0189  160 VAL A CB  
1387 C  CG1 . VAL A 160 ? 0.3224 0.1994 0.3161 -0.0614 -0.0167 -0.0111 160 VAL A CG1 
1388 C  CG2 . VAL A 160 ? 0.5422 0.2685 0.1533 0.0619  0.0637  0.0263  160 VAL A CG2 
1389 N  N   . ASP A 161 ? 0.2527 0.1928 0.1438 -0.0390 -0.0423 -0.0147 161 ASP A N   
1390 C  CA  . ASP A 161 ? 0.2538 0.2533 0.1283 -0.0287 -0.0430 -0.0049 161 ASP A CA  
1391 C  C   . ASP A 161 ? 0.3235 0.2151 0.1299 -0.0274 -0.0461 0.0129  161 ASP A C   
1392 O  O   . ASP A 161 ? 0.3968 0.3553 0.1392 -0.1121 -0.0057 0.0020  161 ASP A O   
1393 C  CB  . ASP A 161 ? 0.2928 0.3188 0.1518 -0.0401 -0.0688 -0.0129 161 ASP A CB  
1394 C  CG  . ASP A 161 ? 0.3305 0.2712 0.2326 -0.0234 -0.0346 -0.0816 161 ASP A CG  
1395 O  OD1 . ASP A 161 ? 0.3052 0.2899 0.2533 -0.0502 -0.0467 0.0000  161 ASP A OD1 
1396 O  OD2 . ASP A 161 ? 0.3691 0.4875 0.2581 -0.0187 -0.0769 -0.0417 161 ASP A OD2 
1397 N  N   . VAL A 162 ? 0.2800 0.1947 0.1421 -0.0423 -0.0555 0.0048  162 VAL A N   
1398 C  CA  . VAL A 162 ? 0.2971 0.2014 0.1435 -0.0357 -0.0331 0.0273  162 VAL A CA  
1399 C  C   . VAL A 162 ? 0.2617 0.1729 0.1439 -0.0662 -0.0540 0.0307  162 VAL A C   
1400 O  O   . VAL A 162 ? 0.2944 0.1956 0.1432 -0.0555 -0.0203 0.0126  162 VAL A O   
1401 C  CB  . VAL A 162 ? 0.4490 0.1815 0.3057 0.0051  -0.0416 0.0441  162 VAL A CB  
1402 C  CG1 . VAL A 162 ? 0.3824 0.1441 0.2657 -0.0148 -0.0248 0.0474  162 VAL A CG1 
1403 C  CG2 . VAL A 162 ? 0.4931 0.3524 0.3887 -0.0935 0.0065  0.0939  162 VAL A CG2 
1404 N  N   . LEU A 163 ? 0.2651 0.1835 0.1477 -0.0285 -0.0337 0.0000  163 LEU A N   
1405 C  CA  . LEU A 163 ? 0.2396 0.1787 0.1143 -0.0162 -0.0021 0.0115  163 LEU A CA  
1406 C  C   . LEU A 163 ? 0.2301 0.1771 0.1091 -0.0126 -0.0063 -0.0054 163 LEU A C   
1407 O  O   . LEU A 163 ? 0.2698 0.2120 0.1326 -0.0412 -0.0063 0.0111  163 LEU A O   
1408 C  CB  . LEU A 163 ? 0.2321 0.1547 0.1288 -0.0233 -0.0081 0.0003  163 LEU A CB  
1409 C  CG  . LEU A 163 ? 0.2488 0.1698 0.1071 -0.0361 0.0041  0.0218  163 LEU A CG  
1410 C  CD1 . LEU A 163 ? 0.2942 0.1369 0.1511 0.0046  -0.0359 0.0331  163 LEU A CD1 
1411 C  CD2 . LEU A 163 ? 0.2431 0.1998 0.1369 -0.0269 -0.0406 -0.0088 163 LEU A CD2 
1412 N  N   . ASP A 164 ? 0.3111 0.1888 0.1276 -0.0210 -0.0149 -0.0229 164 ASP A N   
1413 C  CA  . ASP A 164 ? 0.3222 0.2316 0.1676 0.0089  -0.0057 -0.0340 164 ASP A CA  
1414 C  C   . ASP A 164 ? 0.3287 0.2709 0.1304 -0.0142 0.0159  -0.0076 164 ASP A C   
1415 O  O   . ASP A 164 ? 0.4363 0.3255 0.1680 0.0408  0.0649  0.0099  164 ASP A O   
1416 C  CB  . ASP A 164 ? 0.4004 0.3125 0.2458 -0.0410 0.0177  -0.1111 164 ASP A CB  
1417 C  CG  . ASP A 164 ? 0.3736 0.5029 0.2314 -0.1330 -0.0320 -0.1544 164 ASP A CG  
1418 O  OD1 . ASP A 164 ? 0.4657 0.4487 0.3459 -0.1093 -0.0438 -0.0450 164 ASP A OD1 
1419 O  OD2 . ASP A 164 ? 1.0745 1.3079 0.3794 0.0931  -0.0740 -0.5552 164 ASP A OD2 
1420 N  N   . SER A 165 ? 0.2854 0.2434 0.1158 -0.0480 -0.0253 0.0133  165 SER A N   
1421 C  CA  . SER A 165 ? 0.2917 0.2371 0.1216 -0.0428 -0.0054 0.0256  165 SER A CA  
1422 C  C   . SER A 165 ? 0.3280 0.2567 0.0904 -0.0579 0.0019  0.0078  165 SER A C   
1423 O  O   . SER A 165 ? 0.4555 0.2220 0.1134 -0.0758 -0.0126 0.0346  165 SER A O   
1424 C  CB  . SER A 165 ? 0.2768 0.2881 0.1529 -0.0333 -0.0232 -0.0098 165 SER A CB  
1425 O  OG  . SER A 165 ? 0.4399 0.2314 0.1615 -0.0399 -0.0414 0.0193  165 SER A OG  
1426 N  N   . ILE A 166 ? 0.3598 0.1956 0.0842 -0.0615 -0.0066 0.0206  166 ILE A N   
1427 C  CA  . ILE A 166 ? 0.3181 0.2314 0.1014 -0.0718 0.0186  -0.0023 166 ILE A CA  
1428 C  C   . ILE A 166 ? 0.2809 0.1928 0.1204 -0.0750 -0.0104 -0.0104 166 ILE A C   
1429 O  O   . ILE A 166 ? 0.3100 0.1958 0.0985 -0.0659 0.0065  0.0088  166 ILE A O   
1430 C  CB  . ILE A 166 ? 0.3495 0.1869 0.1176 -0.0812 0.0138  0.0122  166 ILE A CB  
1431 C  CG1 . ILE A 166 ? 0.3055 0.2100 0.0998 -0.0949 -0.0010 -0.0060 166 ILE A CG1 
1432 C  CG2 . ILE A 166 ? 0.3377 0.1827 0.1280 -0.0714 -0.0272 0.0129  166 ILE A CG2 
1433 C  CD1 . ILE A 166 ? 0.2380 0.2366 0.1332 -0.0320 -0.0124 -0.0138 166 ILE A CD1 
1434 N  N   . LYS A 167 ? 0.2644 0.2168 0.1274 -0.0601 0.0092  -0.0135 167 LYS A N   
1435 C  CA  . LYS A 167 ? 0.2454 0.2443 0.1165 -0.0644 0.0303  0.0032  167 LYS A CA  
1436 C  C   . LYS A 167 ? 0.2547 0.2206 0.0998 -0.0982 0.0428  -0.0083 167 LYS A C   
1437 O  O   . LYS A 167 ? 0.2678 0.1858 0.1222 -0.0648 0.0483  -0.0160 167 LYS A O   
1438 C  CB  . LYS A 167 ? 0.2791 0.2289 0.1049 -0.0762 0.0225  -0.0357 167 LYS A CB  
1439 C  CG  . LYS A 167 ? 0.3447 0.2497 0.1825 -0.0742 0.0295  -0.0586 167 LYS A CG  
1440 C  CD  . LYS A 167 ? 0.3785 0.3296 0.2305 -0.0239 -0.0146 -0.1053 167 LYS A CD  
1441 C  CE  . LYS A 167 ? 0.4988 0.5059 0.3488 0.1325  -0.0263 -0.1905 167 LYS A CE  
1442 N  NZ  . LYS A 167 ? 0.6103 0.6977 0.4232 -0.0007 -0.1186 -0.2910 167 LYS A NZ  
1443 N  N   . THR A 168 ? 0.2957 0.1994 0.1253 -0.0942 0.0465  0.0003  168 THR A N   
1444 C  CA  . THR A 168 ? 0.2926 0.2172 0.1517 -0.1160 0.0320  0.0008  168 THR A CA  
1445 C  C   . THR A 168 ? 0.1788 0.2188 0.1168 -0.0958 0.0297  0.0357  168 THR A C   
1446 O  O   . THR A 168 ? 0.3359 0.2664 0.1222 -0.0802 0.0403  0.0373  168 THR A O   
1447 C  CB  . THR A 168 ? 0.3395 0.2723 0.1342 -0.1378 0.0465  -0.0132 168 THR A CB  
1448 O  OG1 . THR A 168 ? 0.4072 0.3449 0.1174 -0.1418 0.0675  0.0043  168 THR A OG1 
1449 C  CG2 . THR A 168 ? 0.3316 0.2698 0.1941 -0.1391 0.0948  -0.0436 168 THR A CG2 
1450 N  N   . LYS A 169 ? 0.2424 0.2515 0.1475 -0.1019 0.0408  0.0054  169 LYS A N   
1451 C  CA  . LYS A 169 ? 0.3348 0.1879 0.1389 -0.1127 0.0516  0.0017  169 LYS A CA  
1452 C  C   . LYS A 169 ? 0.2969 0.2623 0.1376 -0.1380 0.0285  0.0617  169 LYS A C   
1453 O  O   . LYS A 169 ? 0.4172 0.3156 0.1281 -0.1949 0.0436  0.0217  169 LYS A O   
1454 C  CB  . LYS A 169 ? 0.3228 0.2115 0.1693 -0.0474 0.1128  -0.0223 169 LYS A CB  
1455 C  CG  . LYS A 169 ? 0.3704 0.2102 0.1847 -0.0931 0.1014  -0.0137 169 LYS A CG  
1456 C  CD  . LYS A 169 ? 0.3957 0.3269 0.2619 -0.1477 0.0564  0.0247  169 LYS A CD  
1457 C  CE  . LYS A 169 ? 0.5350 0.4720 0.4205 -0.2070 -0.2080 0.0032  169 LYS A CE  
1458 N  NZ  . LYS A 169 ? 0.5250 0.4666 0.6230 0.1132  -0.1207 -0.1360 169 LYS A NZ  
1459 N  N   . GLY A 170 ? 0.3797 0.2054 0.1926 -0.1248 0.0063  0.0333  170 GLY A N   
1460 C  CA  . GLY A 170 ? 0.4553 0.2221 0.2174 -0.1335 -0.0269 0.0913  170 GLY A CA  
1461 C  C   . GLY A 170 ? 0.4948 0.1962 0.2028 -0.1392 0.0219  0.0724  170 GLY A C   
1462 O  O   . GLY A 170 ? 0.5810 0.2272 0.2299 -0.2046 -0.0177 0.0657  170 GLY A O   
1463 N  N   . LYS A 171 ? 0.4110 0.2255 0.1590 -0.1353 -0.0120 0.0676  171 LYS A N   
1464 C  CA  . LYS A 171 ? 0.3653 0.1861 0.1836 -0.0816 -0.0055 0.0581  171 LYS A CA  
1465 C  C   . LYS A 171 ? 0.3248 0.2157 0.1258 -0.0763 -0.0263 0.0564  171 LYS A C   
1466 O  O   . LYS A 171 ? 0.3556 0.2431 0.1143 -0.1027 0.0130  0.0540  171 LYS A O   
1467 C  CB  . LYS A 171 ? 0.3770 0.2436 0.1344 -0.1111 -0.0164 0.0326  171 LYS A CB  
1468 C  CG  . LYS A 171 ? 0.3987 0.2167 0.2274 -0.0443 0.0019  0.0175  171 LYS A CG  
1469 C  CD  . LYS A 171 ? 0.5278 0.3445 0.2648 -0.1497 0.1120  -0.0732 171 LYS A CD  
1470 C  CE  . LYS A 171 ? 0.9017 0.7753 0.5515 -0.1098 -0.2131 -0.0886 171 LYS A CE  
1471 N  NZ  . LYS A 171 ? 1.1289 0.4070 0.3438 -0.3567 0.2687  -0.0296 171 LYS A NZ  
1472 N  N   . SER A 172 ? 0.4298 0.1876 0.1597 -0.0822 -0.0579 0.0676  172 SER A N   
1473 C  CA  . SER A 172 ? 0.3373 0.2773 0.2098 -0.0133 -0.0482 0.0040  172 SER A CA  
1474 C  C   . SER A 172 ? 0.3113 0.2210 0.1560 -0.0111 -0.0265 0.0769  172 SER A C   
1475 O  O   . SER A 172 ? 0.4688 0.2538 0.1123 -0.0263 -0.0377 0.0542  172 SER A O   
1476 C  CB  . SER A 172 ? 0.4063 0.2465 0.1453 -0.0551 0.0461  0.0520  172 SER A CB  
1477 O  OG  . SER A 172 ? 0.6764 0.2734 0.2089 -0.0441 0.0401  0.0996  172 SER A OG  
1478 N  N   . ALA A 173 ? 0.3291 0.2246 0.1648 0.0478  -0.0548 0.0160  173 ALA A N   
1479 C  CA  . ALA A 173 ? 0.3095 0.3592 0.1454 0.0273  -0.0186 0.0944  173 ALA A CA  
1480 C  C   . ALA A 173 ? 0.3274 0.2890 0.1103 0.0368  -0.0610 0.0320  173 ALA A C   
1481 O  O   . ALA A 173 ? 0.3443 0.2303 0.1075 0.0482  -0.0195 0.0463  173 ALA A O   
1482 C  CB  . ALA A 173 ? 0.5041 0.2637 0.1328 0.0788  -0.0441 -0.0311 173 ALA A CB  
1483 N  N   A ASP A 174 ? 0.4759 0.3041 0.0989 0.0185  -0.0711 0.1287  174 ASP A N   
1484 N  N   B ASP A 174 ? 0.1615 0.2768 0.1121 -0.0496 -0.0078 0.0083  174 ASP A N   
1485 C  CA  A ASP A 174 ? 0.5788 0.2529 0.0490 0.0469  -0.0953 0.0295  174 ASP A CA  
1486 C  CA  B ASP A 174 ? 0.1981 0.2244 0.2068 -0.0527 -0.0057 -0.0456 174 ASP A CA  
1487 C  C   A ASP A 174 ? 0.5253 0.2509 0.2215 0.1369  -0.0439 0.1209  174 ASP A C   
1488 C  C   B ASP A 174 ? 0.0899 0.2858 0.2588 0.0252  0.0176  -0.0093 174 ASP A C   
1489 O  O   A ASP A 174 ? 0.3519 0.3185 0.1719 0.1491  -0.0781 -0.0206 174 ASP A O   
1490 O  O   B ASP A 174 ? 0.2201 0.2718 0.3156 -0.0307 -0.0108 -0.0081 174 ASP A O   
1491 C  CB  A ASP A 174 ? 0.5390 0.3849 0.1957 0.1263  -0.0667 0.1404  174 ASP A CB  
1492 C  CB  B ASP A 174 ? 0.3052 0.2782 0.2628 0.0588  -0.0586 -0.0041 174 ASP A CB  
1493 C  CG  A ASP A 174 ? 0.5091 0.3729 0.3109 -0.0193 -0.1015 0.0923  174 ASP A CG  
1494 C  CG  B ASP A 174 ? 0.3497 0.3458 0.2102 0.0762  -0.0724 0.0865  174 ASP A CG  
1495 O  OD1 A ASP A 174 ? 0.4298 0.3573 0.4257 -0.1433 -0.0305 0.2178  174 ASP A OD1 
1496 O  OD1 B ASP A 174 ? 0.2716 0.3213 0.2633 0.0864  -0.0908 0.0882  174 ASP A OD1 
1497 O  OD2 A ASP A 174 ? 0.4715 0.6402 0.3517 0.1652  -0.1405 -0.0272 174 ASP A OD2 
1498 O  OD2 B ASP A 174 ? 0.7638 0.6079 0.8374 -0.1377 -0.4577 -0.0644 174 ASP A OD2 
1499 N  N   . PHE A 175 ? 0.3943 0.3264 0.1712 0.0465  -0.0342 -0.0060 175 PHE A N   
1500 C  CA  . PHE A 175 ? 0.3844 0.2967 0.1836 0.0006  -0.0662 0.0412  175 PHE A CA  
1501 C  C   . PHE A 175 ? 0.3928 0.1957 0.2069 -0.0364 -0.1314 0.0472  175 PHE A C   
1502 O  O   . PHE A 175 ? 0.4677 0.2549 0.2029 0.1180  -0.1563 -0.0164 175 PHE A O   
1503 C  CB  . PHE A 175 ? 0.4741 0.2167 0.2145 0.0551  -0.0566 0.0684  175 PHE A CB  
1504 C  CG  . PHE A 175 ? 0.4530 0.2186 0.1896 0.0188  -0.1138 0.0041  175 PHE A CG  
1505 C  CD1 . PHE A 175 ? 0.4246 0.2149 0.2492 0.1114  -0.1018 -0.0216 175 PHE A CD1 
1506 C  CD2 . PHE A 175 ? 0.3177 0.2211 0.1908 0.0654  -0.0763 -0.0193 175 PHE A CD2 
1507 C  CE1 . PHE A 175 ? 0.4888 0.2174 0.1700 0.0653  -0.0593 0.0038  175 PHE A CE1 
1508 C  CE2 . PHE A 175 ? 0.4106 0.2048 0.2181 0.0678  -0.1024 0.0445  175 PHE A CE2 
1509 C  CZ  . PHE A 175 ? 0.3411 0.2125 0.2230 0.0529  -0.0592 0.0153  175 PHE A CZ  
1510 N  N   . THR A 176 ? 0.3736 0.2610 0.1511 0.0494  -0.0767 0.0582  176 THR A N   
1511 C  CA  . THR A 176 ? 0.3427 0.2369 0.1563 0.0190  -0.0566 0.0671  176 THR A CA  
1512 C  C   . THR A 176 ? 0.3213 0.2536 0.1295 0.0342  -0.0874 0.0604  176 THR A C   
1513 O  O   . THR A 176 ? 0.3540 0.2312 0.1450 0.0155  -0.0813 0.0644  176 THR A O   
1514 C  CB  . THR A 176 ? 0.3785 0.2547 0.2039 0.0179  -0.1142 0.0659  176 THR A CB  
1515 O  OG1 . THR A 176 ? 0.4734 0.3122 0.1752 0.0571  -0.0668 0.1027  176 THR A OG1 
1516 C  CG2 . THR A 176 ? 0.4758 0.2831 0.3887 0.0181  -0.1694 0.1668  176 THR A CG2 
1517 N  N   . ASN A 177 ? 0.2940 0.2384 0.1764 0.0322  -0.1039 0.0639  177 ASN A N   
1518 C  CA  . ASN A 177 ? 0.2894 0.2536 0.1225 0.0798  -0.0681 0.0238  177 ASN A CA  
1519 C  C   . ASN A 177 ? 0.2949 0.2856 0.1860 0.0551  -0.0817 0.0183  177 ASN A C   
1520 O  O   . ASN A 177 ? 0.3691 0.2822 0.2341 -0.0013 -0.1080 0.0797  177 ASN A O   
1521 C  CB  . ASN A 177 ? 0.2843 0.2186 0.1906 -0.0221 -0.0996 0.0675  177 ASN A CB  
1522 C  CG  . ASN A 177 ? 0.3353 0.2414 0.1808 0.0557  -0.0841 0.0482  177 ASN A CG  
1523 O  OD1 . ASN A 177 ? 0.3450 0.2926 0.2305 0.0776  0.0015  0.0649  177 ASN A OD1 
1524 N  ND2 . ASN A 177 ? 0.2906 0.2712 0.1425 0.0480  -0.0675 0.0505  177 ASN A ND2 
1525 N  N   . PHE A 178 ? 0.3091 0.2296 0.1179 0.0116  -0.0724 0.0456  178 PHE A N   
1526 C  CA  . PHE A 178 ? 0.3109 0.2285 0.1516 0.0012  -0.0784 0.0615  178 PHE A CA  
1527 C  C   . PHE A 178 ? 0.3018 0.2242 0.1601 0.0204  -0.0711 0.0723  178 PHE A C   
1528 O  O   . PHE A 178 ? 0.3118 0.2438 0.1395 0.0142  -0.0524 0.0373  178 PHE A O   
1529 C  CB  . PHE A 178 ? 0.3402 0.2449 0.1342 0.0522  -0.0308 0.0751  178 PHE A CB  
1530 C  CG  . PHE A 178 ? 0.3170 0.2361 0.1093 0.0099  -0.0102 0.0672  178 PHE A CG  
1531 C  CD1 . PHE A 178 ? 0.3431 0.2691 0.1351 0.0143  -0.0659 0.0579  178 PHE A CD1 
1532 C  CD2 . PHE A 178 ? 0.2536 0.1951 0.1420 0.0155  -0.0619 0.0228  178 PHE A CD2 
1533 C  CE1 . PHE A 178 ? 0.3070 0.1960 0.1419 0.0375  -0.0099 0.0337  178 PHE A CE1 
1534 C  CE2 . PHE A 178 ? 0.2628 0.2142 0.1529 0.0441  -0.0088 0.0463  178 PHE A CE2 
1535 C  CZ  . PHE A 178 ? 0.2606 0.2317 0.1341 0.0537  -0.0267 0.0684  178 PHE A CZ  
1536 N  N   . ASP A 179 ? 0.2467 0.2109 0.1202 0.0125  -0.0696 0.0335  179 ASP A N   
1537 C  CA  . ASP A 179 ? 0.2470 0.2242 0.1511 0.0445  -0.0636 0.0432  179 ASP A CA  
1538 C  C   . ASP A 179 ? 0.2475 0.2093 0.1337 0.0305  -0.0619 0.0108  179 ASP A C   
1539 O  O   . ASP A 179 ? 0.2044 0.2073 0.1445 0.0127  -0.0443 0.0121  179 ASP A O   
1540 C  CB  . ASP A 179 ? 0.2415 0.2849 0.1872 0.0250  -0.0777 0.0405  179 ASP A CB  
1541 C  CG  . ASP A 179 ? 0.2786 0.3179 0.2226 0.0599  -0.0575 0.0419  179 ASP A CG  
1542 O  OD1 . ASP A 179 ? 0.2461 0.2213 0.2026 0.0254  -0.0500 0.0357  179 ASP A OD1 
1543 O  OD2 . ASP A 179 ? 0.3014 0.5777 0.2581 -0.0251 -0.0571 -0.0375 179 ASP A OD2 
1544 N  N   . PRO A 180 ? 0.1984 0.1948 0.1359 0.0127  -0.0564 0.0221  180 PRO A N   
1545 C  CA  . PRO A 180 ? 0.2266 0.1921 0.1254 0.0183  -0.0553 0.0384  180 PRO A CA  
1546 C  C   . PRO A 180 ? 0.2084 0.1750 0.1310 0.0242  -0.0493 0.0100  180 PRO A C   
1547 O  O   . PRO A 180 ? 0.1835 0.1906 0.1254 0.0320  -0.0306 0.0243  180 PRO A O   
1548 C  CB  . PRO A 180 ? 0.2158 0.2019 0.1525 0.0109  -0.0615 0.0208  180 PRO A CB  
1549 C  CG  . PRO A 180 ? 0.2271 0.1893 0.1626 0.0212  -0.0806 0.0076  180 PRO A CG  
1550 C  CD  . PRO A 180 ? 0.2240 0.2314 0.1228 0.0003  -0.0557 0.0262  180 PRO A CD  
1551 N  N   . ARG A 181 ? 0.1872 0.1955 0.1348 0.0195  -0.0381 0.0211  181 ARG A N   
1552 C  CA  . ARG A 181 ? 0.1933 0.1872 0.1768 0.0381  -0.0308 -0.0129 181 ARG A CA  
1553 C  C   . ARG A 181 ? 0.1869 0.1933 0.1524 0.0449  -0.0641 0.0195  181 ARG A C   
1554 O  O   . ARG A 181 ? 0.2030 0.2357 0.1985 0.0306  -0.0428 0.0397  181 ARG A O   
1555 C  CB  . ARG A 181 ? 0.1829 0.2197 0.2183 0.0456  -0.0364 -0.0062 181 ARG A CB  
1556 C  CG  . ARG A 181 ? 0.2196 0.2134 0.2235 0.0395  -0.0317 -0.0295 181 ARG A CG  
1557 C  CD  . ARG A 181 ? 0.2136 0.2342 0.2931 0.0366  0.0491  0.0228  181 ARG A CD  
1558 N  NE  . ARG A 181 ? 0.2341 0.2229 0.2759 0.0034  -0.0044 0.0498  181 ARG A NE  
1559 C  CZ  . ARG A 181 ? 0.2773 0.3574 0.3337 0.0697  0.0716  0.0839  181 ARG A CZ  
1560 N  NH1 . ARG A 181 ? 0.1851 0.4002 0.5346 0.0527  0.0372  0.0841  181 ARG A NH1 
1561 N  NH2 . ARG A 181 ? 0.2558 0.3433 0.3395 0.0531  0.0055  0.0995  181 ARG A NH2 
1562 N  N   . GLY A 182 ? 0.1741 0.2059 0.1678 0.0156  -0.0595 0.0038  182 GLY A N   
1563 C  CA  . GLY A 182 ? 0.2319 0.1951 0.1757 0.0292  -0.0707 0.0126  182 GLY A CA  
1564 C  C   . GLY A 182 ? 0.2177 0.1960 0.1710 0.0254  -0.0445 0.0227  182 GLY A C   
1565 O  O   . GLY A 182 ? 0.2666 0.2106 0.2102 0.0405  -0.0758 0.0035  182 GLY A O   
1566 N  N   . LEU A 183 ? 0.1894 0.2071 0.1389 0.0447  -0.0573 -0.0097 183 LEU A N   
1567 C  CA  . LEU A 183 ? 0.1829 0.1793 0.1434 0.0270  -0.0447 0.0065  183 LEU A CA  
1568 C  C   . LEU A 183 ? 0.1884 0.1676 0.1477 0.0052  -0.0559 -0.0103 183 LEU A C   
1569 O  O   . LEU A 183 ? 0.1955 0.1662 0.1735 0.0318  -0.0370 0.0281  183 LEU A O   
1570 C  CB  . LEU A 183 ? 0.1595 0.2206 0.1365 0.0557  -0.0372 0.0410  183 LEU A CB  
1571 C  CG  . LEU A 183 ? 0.2129 0.2355 0.1292 0.0443  -0.0397 0.0390  183 LEU A CG  
1572 C  CD1 . LEU A 183 ? 0.2138 0.3260 0.1958 0.0307  -0.0718 0.0542  183 LEU A CD1 
1573 C  CD2 . LEU A 183 ? 0.2861 0.2393 0.1581 0.1058  -0.0078 0.0124  183 LEU A CD2 
1574 N  N   . LEU A 184 ? 0.1911 0.1574 0.1457 0.0136  -0.0299 0.0168  184 LEU A N   
1575 C  CA  . LEU A 184 ? 0.1942 0.1676 0.1425 -0.0151 -0.0408 0.0231  184 LEU A CA  
1576 C  C   . LEU A 184 ? 0.1987 0.1865 0.1772 -0.0267 -0.0829 0.0311  184 LEU A C   
1577 O  O   . LEU A 184 ? 0.2827 0.2402 0.2872 -0.0925 -0.1849 0.0697  184 LEU A O   
1578 C  CB  . LEU A 184 ? 0.1687 0.1741 0.1612 -0.0109 -0.0138 0.0000  184 LEU A CB  
1579 C  CG  . LEU A 184 ? 0.1635 0.1605 0.1757 0.0157  -0.0155 0.0035  184 LEU A CG  
1580 C  CD1 . LEU A 184 ? 0.1179 0.2332 0.2021 0.0284  0.0060  0.0094  184 LEU A CD1 
1581 C  CD2 . LEU A 184 ? 0.1421 0.2168 0.2330 0.0304  -0.0326 0.0207  184 LEU A CD2 
1582 N  N   . PRO A 185 ? 0.1842 0.1516 0.1606 -0.0034 -0.0384 0.0130  185 PRO A N   
1583 C  CA  . PRO A 185 ? 0.1903 0.1558 0.1603 0.0055  -0.0399 0.0274  185 PRO A CA  
1584 C  C   . PRO A 185 ? 0.1649 0.1465 0.1887 -0.0008 -0.0533 0.0162  185 PRO A C   
1585 O  O   . PRO A 185 ? 0.1116 0.1635 0.3116 -0.0041 -0.0579 0.0329  185 PRO A O   
1586 C  CB  . PRO A 185 ? 0.1437 0.1497 0.1723 0.0119  -0.0146 0.0281  185 PRO A CB  
1587 C  CG  . PRO A 185 ? 0.1209 0.1624 0.1454 0.0390  0.0046  0.0049  185 PRO A CG  
1588 C  CD  . PRO A 185 ? 0.1483 0.1412 0.1229 0.0057  -0.0260 0.0100  185 PRO A CD  
1589 N  N   A GLU A 186 ? 0.1398 0.1523 0.1815 0.0103  -0.0296 0.0186  186 GLU A N   
1590 N  N   B GLU A 186 ? 0.1281 0.2066 0.2231 -0.0458 -0.0785 0.0082  186 GLU A N   
1591 C  CA  A GLU A 186 ? 0.0878 0.1729 0.2248 -0.0317 -0.0296 -0.0249 186 GLU A CA  
1592 C  CA  B GLU A 186 ? 0.1574 0.1633 0.2351 -0.0353 -0.0527 0.0326  186 GLU A CA  
1593 C  C   A GLU A 186 ? 0.1394 0.1513 0.1800 -0.0155 -0.0205 0.0131  186 GLU A C   
1594 C  C   B GLU A 186 ? 0.1132 0.2032 0.2017 0.0000  -0.0109 0.0269  186 GLU A C   
1595 O  O   A GLU A 186 ? 0.1042 0.2129 0.1960 0.0118  -0.0121 -0.0013 186 GLU A O   
1596 O  O   B GLU A 186 ? 0.1477 0.2346 0.2190 0.0183  0.0093  0.0034  186 GLU A O   
1597 C  CB  A GLU A 186 ? 0.1407 0.1878 0.2125 -0.0186 -0.0298 0.0015  186 GLU A CB  
1598 C  CB  B GLU A 186 ? 0.1464 0.1590 0.2490 -0.0133 -0.0256 0.0212  186 GLU A CB  
1599 C  CG  A GLU A 186 ? 0.1777 0.1775 0.2601 -0.0603 -0.0646 -0.0006 186 GLU A CG  
1600 C  CG  B GLU A 186 ? 0.1599 0.2375 0.3713 0.0165  0.0176  0.0166  186 GLU A CG  
1601 C  CD  A GLU A 186 ? 0.1403 0.1847 0.2536 -0.0496 -0.0368 -0.0218 186 GLU A CD  
1602 C  CD  B GLU A 186 ? 0.2233 0.2213 0.3334 0.0654  -0.0136 0.0240  186 GLU A CD  
1603 O  OE1 A GLU A 186 ? 0.2106 0.2233 0.2506 -0.0183 -0.0732 -0.0208 186 GLU A OE1 
1604 O  OE1 B GLU A 186 ? 0.2039 0.2806 0.3519 0.0315  0.0151  -0.0375 186 GLU A OE1 
1605 O  OE2 A GLU A 186 ? 0.1784 0.1836 0.2856 -0.0399 -0.0315 0.0031  186 GLU A OE2 
1606 O  OE2 B GLU A 186 ? 0.3492 0.2231 0.3953 0.0001  0.0303  0.0775  186 GLU A OE2 
1607 N  N   . SER A 187 ? 0.0958 0.1892 0.2055 -0.0304 -0.0304 0.0115  187 SER A N   
1608 C  CA  . SER A 187 ? 0.1045 0.1908 0.1892 -0.0125 0.0046  0.0081  187 SER A CA  
1609 C  C   . SER A 187 ? 0.1046 0.1906 0.1673 -0.0164 0.0063  0.0115  187 SER A C   
1610 O  O   . SER A 187 ? 0.1149 0.2053 0.1896 -0.0195 0.0129  0.0057  187 SER A O   
1611 C  CB  . SER A 187 ? 0.1359 0.2021 0.1922 -0.0273 -0.0035 0.0146  187 SER A CB  
1612 O  OG  . SER A 187 ? 0.1419 0.2140 0.2050 -0.0087 0.0162  0.0273  187 SER A OG  
1613 N  N   . LEU A 188 ? 0.1168 0.1594 0.1910 -0.0142 -0.0013 -0.0049 188 LEU A N   
1614 C  CA  . LEU A 188 ? 0.1033 0.1708 0.2290 -0.0193 -0.0200 0.0093  188 LEU A CA  
1615 C  C   . LEU A 188 ? 0.0947 0.1755 0.1858 0.0032  -0.0035 -0.0113 188 LEU A C   
1616 O  O   . LEU A 188 ? 0.1441 0.2014 0.2195 -0.0337 0.0086  -0.0303 188 LEU A O   
1617 C  CB  . LEU A 188 ? 0.1054 0.1993 0.3138 -0.0295 -0.0331 0.0074  188 LEU A CB  
1618 C  CG  . LEU A 188 ? 0.1347 0.2075 0.3312 -0.0006 -0.0163 0.0529  188 LEU A CG  
1619 C  CD1 . LEU A 188 ? 0.1712 0.2280 0.4092 -0.0129 -0.0467 0.0549  188 LEU A CD1 
1620 C  CD2 . LEU A 188 ? 0.0701 0.2777 0.3271 0.0140  -0.0155 0.0671  188 LEU A CD2 
1621 N  N   . ASP A 189 ? 0.1037 0.1791 0.1588 0.0030  0.0082  -0.0049 189 ASP A N   
1622 C  CA  . ASP A 189 ? 0.1163 0.2087 0.1612 -0.0288 0.0244  -0.0003 189 ASP A CA  
1623 C  C   . ASP A 189 ? 0.1103 0.1464 0.1277 -0.0099 0.0130  -0.0130 189 ASP A C   
1624 O  O   . ASP A 189 ? 0.0992 0.1532 0.1288 -0.0136 0.0037  -0.0046 189 ASP A O   
1625 C  CB  . ASP A 189 ? 0.1989 0.2619 0.1563 -0.0876 0.0472  0.0175  189 ASP A CB  
1626 C  CG  . ASP A 189 ? 0.2169 0.3095 0.1721 -0.0886 -0.0399 0.0078  189 ASP A CG  
1627 O  OD1 . ASP A 189 ? 0.1639 0.4695 0.2739 -0.0732 0.0649  -0.0617 189 ASP A OD1 
1628 O  OD2 . ASP A 189 ? 0.2594 0.4989 0.3070 -0.1897 0.0248  0.0637  189 ASP A OD2 
1629 N  N   . TYR A 190 ? 0.1057 0.1588 0.1163 -0.0195 0.0197  -0.0098 190 TYR A N   
1630 C  CA  . TYR A 190 ? 0.0798 0.1642 0.1193 -0.0183 -0.0024 0.0120  190 TYR A CA  
1631 C  C   . TYR A 190 ? 0.1032 0.1348 0.0888 0.0017  0.0164  -0.0024 190 TYR A C   
1632 O  O   . TYR A 190 ? 0.1154 0.1533 0.0994 -0.0113 0.0182  -0.0034 190 TYR A O   
1633 C  CB  . TYR A 190 ? 0.1167 0.1488 0.1156 -0.0006 0.0063  -0.0038 190 TYR A CB  
1634 C  CG  . TYR A 190 ? 0.1089 0.1401 0.1240 -0.0057 0.0073  0.0132  190 TYR A CG  
1635 C  CD1 . TYR A 190 ? 0.1324 0.1401 0.1283 -0.0256 0.0092  0.0060  190 TYR A CD1 
1636 C  CD2 . TYR A 190 ? 0.1064 0.1497 0.1256 -0.0070 0.0127  0.0038  190 TYR A CD2 
1637 C  CE1 . TYR A 190 ? 0.1039 0.1574 0.1419 -0.0295 0.0252  -0.0021 190 TYR A CE1 
1638 C  CE2 . TYR A 190 ? 0.1353 0.1421 0.1462 -0.0021 0.0024  -0.0098 190 TYR A CE2 
1639 C  CZ  . TYR A 190 ? 0.1319 0.1342 0.1322 -0.0198 0.0083  0.0080  190 TYR A CZ  
1640 O  OH  . TYR A 190 ? 0.1579 0.1615 0.1651 0.0091  0.0038  -0.0280 190 TYR A OH  
1641 N  N   . TRP A 191 ? 0.0908 0.1097 0.0938 -0.0104 0.0049  0.0032  191 TRP A N   
1642 C  CA  . TRP A 191 ? 0.0996 0.1249 0.0909 -0.0073 0.0020  -0.0046 191 TRP A CA  
1643 C  C   . TRP A 191 ? 0.0882 0.1203 0.0824 -0.0015 0.0065  0.0035  191 TRP A C   
1644 O  O   . TRP A 191 ? 0.1225 0.1230 0.0860 -0.0240 0.0120  -0.0125 191 TRP A O   
1645 C  CB  . TRP A 191 ? 0.1256 0.1145 0.1360 0.0131  0.0167  -0.0020 191 TRP A CB  
1646 C  CG  . TRP A 191 ? 0.1077 0.1193 0.0964 0.0076  0.0081  0.0043  191 TRP A CG  
1647 C  CD1 . TRP A 191 ? 0.1552 0.1243 0.1070 0.0019  0.0147  0.0065  191 TRP A CD1 
1648 C  CD2 . TRP A 191 ? 0.0974 0.1331 0.1057 0.0032  0.0068  0.0027  191 TRP A CD2 
1649 N  NE1 . TRP A 191 ? 0.1563 0.1220 0.1324 -0.0063 0.0159  0.0176  191 TRP A NE1 
1650 C  CE2 . TRP A 191 ? 0.1420 0.1085 0.1308 0.0089  0.0037  -0.0024 191 TRP A CE2 
1651 C  CE3 . TRP A 191 ? 0.1082 0.1483 0.1233 0.0071  0.0015  -0.0182 191 TRP A CE3 
1652 C  CZ2 . TRP A 191 ? 0.1450 0.1305 0.1755 0.0091  -0.0052 0.0093  191 TRP A CZ2 
1653 C  CZ3 . TRP A 191 ? 0.1286 0.1509 0.1508 -0.0114 0.0023  -0.0152 191 TRP A CZ3 
1654 C  CH2 . TRP A 191 ? 0.1394 0.1366 0.1544 -0.0017 0.0023  -0.0195 191 TRP A CH2 
1655 N  N   . THR A 192 ? 0.0927 0.1170 0.0872 -0.0052 0.0074  -0.0049 192 THR A N   
1656 C  CA  . THR A 192 ? 0.1014 0.1032 0.0870 -0.0044 0.0071  -0.0071 192 THR A CA  
1657 C  C   . THR A 192 ? 0.0961 0.1073 0.0830 0.0104  0.0093  -0.0013 192 THR A C   
1658 O  O   . THR A 192 ? 0.1138 0.1353 0.0820 -0.0078 0.0076  -0.0041 192 THR A O   
1659 C  CB  . THR A 192 ? 0.1138 0.1030 0.1053 0.0120  0.0163  -0.0010 192 THR A CB  
1660 O  OG1 . THR A 192 ? 0.1059 0.1067 0.1111 0.0111  0.0115  -0.0124 192 THR A OG1 
1661 C  CG2 . THR A 192 ? 0.1138 0.1263 0.1158 0.0119  0.0172  -0.0115 192 THR A CG2 
1662 N  N   . TYR A 193 ? 0.0874 0.1124 0.0903 0.0003  0.0021  -0.0087 193 TYR A N   
1663 C  CA  . TYR A 193 ? 0.1066 0.1128 0.0784 -0.0019 0.0000  -0.0073 193 TYR A CA  
1664 C  C   . TYR A 193 ? 0.0909 0.1067 0.0798 0.0074  -0.0017 -0.0088 193 TYR A C   
1665 O  O   . TYR A 193 ? 0.0997 0.1055 0.0824 0.0066  0.0038  -0.0059 193 TYR A O   
1666 C  CB  . TYR A 193 ? 0.1080 0.1229 0.0810 0.0231  -0.0001 -0.0104 193 TYR A CB  
1667 C  CG  . TYR A 193 ? 0.0931 0.0992 0.0929 0.0181  -0.0060 -0.0065 193 TYR A CG  
1668 C  CD1 . TYR A 193 ? 0.1048 0.0910 0.0908 0.0179  -0.0048 -0.0077 193 TYR A CD1 
1669 C  CD2 . TYR A 193 ? 0.1012 0.0992 0.0933 0.0197  -0.0030 -0.0048 193 TYR A CD2 
1670 C  CE1 . TYR A 193 ? 0.0895 0.0894 0.0939 0.0172  -0.0060 -0.0031 193 TYR A CE1 
1671 C  CE2 . TYR A 193 ? 0.1027 0.1027 0.1028 0.0126  -0.0007 -0.0182 193 TYR A CE2 
1672 C  CZ  . TYR A 193 ? 0.0989 0.0915 0.0883 0.0176  -0.0041 -0.0062 193 TYR A CZ  
1673 O  OH  . TYR A 193 ? 0.0856 0.0969 0.0888 0.0068  0.0099  -0.0008 193 TYR A OH  
1674 N  N   . PRO A 194 ? 0.1012 0.1059 0.0901 -0.0003 -0.0041 -0.0177 194 PRO A N   
1675 C  CA  . PRO A 194 ? 0.0948 0.1012 0.1015 0.0085  0.0034  -0.0136 194 PRO A CA  
1676 C  C   . PRO A 194 ? 0.0899 0.0978 0.0850 0.0068  -0.0078 -0.0133 194 PRO A C   
1677 O  O   . PRO A 194 ? 0.1177 0.1068 0.0897 0.0163  -0.0097 -0.0126 194 PRO A O   
1678 C  CB  . PRO A 194 ? 0.1281 0.1386 0.0895 -0.0111 0.0024  -0.0204 194 PRO A CB  
1679 C  CG  . PRO A 194 ? 0.1444 0.1411 0.1075 -0.0205 -0.0100 -0.0249 194 PRO A CG  
1680 C  CD  . PRO A 194 ? 0.1215 0.1432 0.0908 -0.0174 -0.0017 -0.0196 194 PRO A CD  
1681 N  N   . GLY A 195 ? 0.0843 0.0974 0.0912 0.0080  -0.0024 -0.0137 195 GLY A N   
1682 C  CA  . GLY A 195 ? 0.0951 0.1041 0.0865 0.0063  0.0068  -0.0105 195 GLY A CA  
1683 C  C   . GLY A 195 ? 0.0865 0.0892 0.0987 0.0003  -0.0026 -0.0168 195 GLY A C   
1684 O  O   . GLY A 195 ? 0.1062 0.0952 0.1003 -0.0003 0.0080  -0.0108 195 GLY A O   
1685 N  N   . SER A 196 ? 0.0830 0.0926 0.0885 -0.0010 0.0000  -0.0104 196 SER A N   
1686 C  CA  . SER A 196 ? 0.0859 0.0974 0.0868 -0.0076 0.0099  -0.0102 196 SER A CA  
1687 C  C   . SER A 196 ? 0.0759 0.0760 0.0982 0.0017  0.0060  -0.0188 196 SER A C   
1688 O  O   . SER A 196 ? 0.0899 0.0973 0.0969 -0.0044 0.0026  -0.0217 196 SER A O   
1689 C  CB  . SER A 196 ? 0.0942 0.0886 0.1181 -0.0052 0.0019  -0.0250 196 SER A CB  
1690 O  OG  . SER A 196 ? 0.0825 0.0998 0.1084 -0.0046 0.0003  -0.0098 196 SER A OG  
1691 N  N   . LEU A 197 ? 0.0908 0.1001 0.0931 0.0037  0.0113  -0.0182 197 LEU A N   
1692 C  CA  . LEU A 197 ? 0.1222 0.0819 0.0974 0.0008  0.0043  -0.0124 197 LEU A CA  
1693 C  C   . LEU A 197 ? 0.1001 0.0910 0.1066 0.0044  0.0120  -0.0221 197 LEU A C   
1694 O  O   . LEU A 197 ? 0.0879 0.1041 0.1142 -0.0007 -0.0028 -0.0089 197 LEU A O   
1695 C  CB  . LEU A 197 ? 0.1590 0.1061 0.1053 0.0098  0.0300  -0.0034 197 LEU A CB  
1696 C  CG  . LEU A 197 ? 0.1884 0.1268 0.1373 0.0410  0.0204  0.0124  197 LEU A CG  
1697 C  CD1 . LEU A 197 ? 0.2176 0.1468 0.1550 -0.0113 0.0230  0.0119  197 LEU A CD1 
1698 C  CD2 . LEU A 197 ? 0.1756 0.2224 0.1992 0.0773  0.0485  0.0573  197 LEU A CD2 
1699 N  N   . THR A 198 ? 0.0913 0.1032 0.1018 0.0071  0.0027  -0.0216 198 THR A N   
1700 C  CA  . THR A 198 ? 0.0944 0.1111 0.1161 0.0010  0.0120  -0.0124 198 THR A CA  
1701 C  C   . THR A 198 ? 0.0601 0.1066 0.1317 -0.0044 -0.0019 -0.0162 198 THR A C   
1702 O  O   . THR A 198 ? 0.0906 0.1143 0.1411 0.0035  0.0076  -0.0320 198 THR A O   
1703 C  CB  . THR A 198 ? 0.0940 0.1111 0.0874 -0.0003 0.0000  -0.0187 198 THR A CB  
1704 O  OG1 . THR A 198 ? 0.1000 0.0980 0.0906 0.0005  0.0038  -0.0005 198 THR A OG1 
1705 C  CG2 . THR A 198 ? 0.1017 0.1067 0.1023 0.0131  0.0119  -0.0096 198 THR A CG2 
1706 N  N   . THR A 199 ? 0.1055 0.1358 0.1163 0.0023  0.0294  -0.0121 199 THR A N   
1707 C  CA  . THR A 199 ? 0.1082 0.1341 0.1535 -0.0049 0.0172  -0.0272 199 THR A CA  
1708 C  C   . THR A 199 ? 0.1143 0.1337 0.1242 0.0015  0.0311  -0.0155 199 THR A C   
1709 O  O   . THR A 199 ? 0.1079 0.1249 0.1430 -0.0108 0.0241  -0.0160 199 THR A O   
1710 C  CB  . THR A 199 ? 0.1371 0.1732 0.1405 -0.0085 0.0163  -0.0236 199 THR A CB  
1711 O  OG1 . THR A 199 ? 0.1796 0.1872 0.1791 -0.0171 -0.0277 -0.0097 199 THR A OG1 
1712 C  CG2 . THR A 199 ? 0.1978 0.1829 0.1914 -0.0211 0.0357  -0.0522 199 THR A CG2 
1713 N  N   . PRO A 200 ? 0.1251 0.1462 0.1407 -0.0041 0.0355  -0.0225 200 PRO A N   
1714 C  CA  . PRO A 200 ? 0.1342 0.1490 0.1594 -0.0299 0.0362  -0.0074 200 PRO A CA  
1715 C  C   . PRO A 200 ? 0.1396 0.1522 0.1493 -0.0271 0.0233  0.0013  200 PRO A C   
1716 O  O   . PRO A 200 ? 0.2014 0.1841 0.1425 -0.0063 0.0063  -0.0068 200 PRO A O   
1717 C  CB  . PRO A 200 ? 0.1328 0.2039 0.1893 -0.0195 0.0463  -0.0152 200 PRO A CB  
1718 C  CG  . PRO A 200 ? 0.1053 0.2113 0.1982 -0.0087 0.0351  -0.0489 200 PRO A CG  
1719 C  CD  . PRO A 200 ? 0.1001 0.1944 0.1777 0.0076  0.0223  -0.0450 200 PRO A CD  
1720 N  N   . PRO A 201 ? 0.1577 0.1518 0.1362 -0.0204 0.0171  0.0071  201 PRO A N   
1721 C  CA  . PRO A 201 ? 0.1585 0.1520 0.1358 -0.0199 0.0186  0.0087  201 PRO A CA  
1722 C  C   . PRO A 201 ? 0.1129 0.1308 0.1454 0.0103  0.0225  -0.0104 201 PRO A C   
1723 O  O   . PRO A 201 ? 0.1304 0.1420 0.1624 -0.0284 0.0073  -0.0160 201 PRO A O   
1724 C  CB  . PRO A 201 ? 0.2170 0.1684 0.1800 -0.0287 0.0399  0.0267  201 PRO A CB  
1725 C  CG  . PRO A 201 ? 0.2060 0.1434 0.2037 0.0115  0.0388  0.0238  201 PRO A CG  
1726 C  CD  . PRO A 201 ? 0.2208 0.1502 0.1665 0.0055  0.0216  0.0137  201 PRO A CD  
1727 N  N   . LEU A 202 ? 0.0983 0.1197 0.1395 -0.0091 0.0142  0.0065  202 LEU A N   
1728 C  CA  . LEU A 202 ? 0.1053 0.0960 0.1254 0.0133  0.0102  -0.0094 202 LEU A CA  
1729 C  C   . LEU A 202 ? 0.0888 0.1040 0.1342 -0.0153 0.0054  -0.0060 202 LEU A C   
1730 O  O   . LEU A 202 ? 0.1021 0.1156 0.1252 -0.0003 0.0055  -0.0197 202 LEU A O   
1731 C  CB  . LEU A 202 ? 0.0991 0.1136 0.1377 0.0065  0.0001  -0.0194 202 LEU A CB  
1732 C  CG  . LEU A 202 ? 0.0878 0.1256 0.1480 0.0109  0.0109  -0.0194 202 LEU A CG  
1733 C  CD1 . LEU A 202 ? 0.0926 0.1518 0.1902 0.0115  0.0098  -0.0324 202 LEU A CD1 
1734 C  CD2 . LEU A 202 ? 0.1231 0.1200 0.1482 -0.0065 -0.0046 -0.0219 202 LEU A CD2 
1735 N  N   . ALA A 203 ? 0.1039 0.1010 0.1420 -0.0105 0.0060  -0.0096 203 ALA A N   
1736 C  CA  . ALA A 203 ? 0.1107 0.1062 0.1437 -0.0031 0.0100  -0.0132 203 ALA A CA  
1737 C  C   . ALA A 203 ? 0.1136 0.1076 0.1290 -0.0186 0.0148  -0.0208 203 ALA A C   
1738 O  O   . ALA A 203 ? 0.1040 0.0960 0.1261 -0.0147 0.0008  -0.0126 203 ALA A O   
1739 C  CB  . ALA A 203 ? 0.1540 0.1185 0.1502 0.0185  0.0252  0.0093  203 ALA A CB  
1740 N  N   . GLU A 204 ? 0.0938 0.1084 0.1272 -0.0074 0.0124  -0.0142 204 GLU A N   
1741 C  CA  . GLU A 204 ? 0.1172 0.1145 0.1088 -0.0051 0.0000  -0.0258 204 GLU A CA  
1742 C  C   . GLU A 204 ? 0.1096 0.0994 0.1188 -0.0020 -0.0065 -0.0203 204 GLU A C   
1743 O  O   . GLU A 204 ? 0.1246 0.1481 0.1398 0.0159  -0.0055 -0.0342 204 GLU A O   
1744 C  CB  . GLU A 204 ? 0.1107 0.1359 0.1294 0.0129  -0.0187 -0.0229 204 GLU A CB  
1745 C  CG  . GLU A 204 ? 0.1395 0.1435 0.1421 0.0208  -0.0379 -0.0240 204 GLU A CG  
1746 C  CD  . GLU A 204 ? 0.1321 0.1323 0.1310 -0.0074 -0.0311 -0.0390 204 GLU A CD  
1747 O  OE1 . GLU A 204 ? 0.1617 0.1513 0.1628 0.0038  -0.0414 -0.0375 204 GLU A OE1 
1748 O  OE2 . GLU A 204 ? 0.1185 0.1405 0.1502 -0.0015 -0.0253 -0.0307 204 GLU A OE2 
1749 N  N   . CYS A 205 ? 0.0967 0.0912 0.1317 0.0017  -0.0035 -0.0132 205 CYS A N   
1750 C  CA  . CYS A 205 ? 0.0883 0.0987 0.1298 -0.0057 -0.0130 -0.0116 205 CYS A CA  
1751 C  C   . CYS A 205 ? 0.0915 0.1033 0.1100 -0.0010 -0.0062 -0.0015 205 CYS A C   
1752 O  O   . CYS A 205 ? 0.1161 0.1066 0.1544 0.0052  -0.0226 -0.0046 205 CYS A O   
1753 C  CB  . CYS A 205 ? 0.1026 0.1009 0.1319 -0.0068 0.0006  0.0005  205 CYS A CB  
1754 S  SG  . CYS A 205 ? 0.1489 0.1134 0.1301 0.0015  0.0026  -0.0051 205 CYS A SG  
1755 N  N   . VAL A 206 ? 0.0891 0.0847 0.1128 -0.0078 0.0035  -0.0171 206 VAL A N   
1756 C  CA  . VAL A 206 ? 0.0886 0.0897 0.1102 -0.0001 0.0077  -0.0037 206 VAL A CA  
1757 C  C   . VAL A 206 ? 0.0888 0.0860 0.1075 -0.0065 0.0031  -0.0077 206 VAL A C   
1758 O  O   . VAL A 206 ? 0.0949 0.1254 0.1100 -0.0003 0.0035  0.0052  206 VAL A O   
1759 C  CB  . VAL A 206 ? 0.0890 0.0897 0.1292 0.0007  0.0003  0.0017  206 VAL A CB  
1760 C  CG1 . VAL A 206 ? 0.0931 0.0929 0.1260 0.0098  -0.0046 -0.0115 206 VAL A CG1 
1761 C  CG2 . VAL A 206 ? 0.0956 0.1118 0.1222 0.0007  0.0187  0.0035  206 VAL A CG2 
1762 N  N   . THR A 207 ? 0.0815 0.0800 0.0997 -0.0027 0.0100  -0.0149 207 THR A N   
1763 C  CA  . THR A 207 ? 0.0913 0.1027 0.1064 0.0000  0.0111  -0.0078 207 THR A CA  
1764 C  C   . THR A 207 ? 0.0851 0.0917 0.0892 -0.0133 0.0103  -0.0109 207 THR A C   
1765 O  O   . THR A 207 ? 0.1012 0.0967 0.1008 0.0008  0.0034  -0.0003 207 THR A O   
1766 C  CB  . THR A 207 ? 0.1039 0.0931 0.1265 0.0017  0.0144  -0.0217 207 THR A CB  
1767 O  OG1 . THR A 207 ? 0.1088 0.1046 0.1197 0.0080  0.0111  -0.0237 207 THR A OG1 
1768 C  CG2 . THR A 207 ? 0.0994 0.1265 0.1339 -0.0071 0.0186  -0.0093 207 THR A CG2 
1769 N  N   . TRP A 208 ? 0.0886 0.0899 0.0920 0.0059  0.0054  -0.0040 208 TRP A N   
1770 C  CA  . TRP A 208 ? 0.0922 0.0794 0.0829 0.0034  0.0017  -0.0060 208 TRP A CA  
1771 C  C   . TRP A 208 ? 0.0915 0.0843 0.0727 0.0017  0.0087  -0.0093 208 TRP A C   
1772 O  O   . TRP A 208 ? 0.0945 0.0997 0.0816 -0.0020 0.0054  -0.0065 208 TRP A O   
1773 C  CB  . TRP A 208 ? 0.0842 0.1048 0.0900 0.0118  0.0041  0.0017  208 TRP A CB  
1774 C  CG  . TRP A 208 ? 0.0847 0.0773 0.0985 0.0104  0.0012  -0.0140 208 TRP A CG  
1775 C  CD1 . TRP A 208 ? 0.0888 0.1003 0.1030 0.0157  0.0043  -0.0038 208 TRP A CD1 
1776 C  CD2 . TRP A 208 ? 0.0860 0.0728 0.1041 0.0162  0.0003  -0.0071 208 TRP A CD2 
1777 N  NE1 . TRP A 208 ? 0.0852 0.0886 0.1152 0.0063  0.0062  -0.0089 208 TRP A NE1 
1778 C  CE2 . TRP A 208 ? 0.0842 0.0859 0.1015 0.0161  -0.0012 -0.0113 208 TRP A CE2 
1779 C  CE3 . TRP A 208 ? 0.1076 0.0781 0.0926 0.0049  -0.0142 -0.0126 208 TRP A CE3 
1780 C  CZ2 . TRP A 208 ? 0.0970 0.0996 0.1050 0.0234  0.0065  -0.0041 208 TRP A CZ2 
1781 C  CZ3 . TRP A 208 ? 0.0936 0.0944 0.1000 0.0148  0.0080  -0.0098 208 TRP A CZ3 
1782 C  CH2 . TRP A 208 ? 0.1049 0.1093 0.1019 0.0200  0.0109  -0.0078 208 TRP A CH2 
1783 N  N   . ILE A 209 ? 0.0839 0.0957 0.0870 0.0063  0.0005  -0.0010 209 ILE A N   
1784 C  CA  . ILE A 209 ? 0.0808 0.0860 0.1014 0.0020  -0.0102 -0.0135 209 ILE A CA  
1785 C  C   . ILE A 209 ? 0.0755 0.0951 0.0782 -0.0026 0.0024  -0.0023 209 ILE A C   
1786 O  O   . ILE A 209 ? 0.1233 0.1001 0.0894 -0.0021 -0.0027 -0.0006 209 ILE A O   
1787 C  CB  . ILE A 209 ? 0.1057 0.1030 0.1188 0.0142  -0.0046 -0.0066 209 ILE A CB  
1788 C  CG1 . ILE A 209 ? 0.1059 0.1055 0.1500 0.0174  -0.0015 -0.0157 209 ILE A CG1 
1789 C  CG2 . ILE A 209 ? 0.0790 0.1389 0.1290 0.0091  -0.0017 -0.0065 209 ILE A CG2 
1790 C  CD1 . ILE A 209 ? 0.1489 0.1226 0.2165 0.0383  -0.0031 -0.0035 209 ILE A CD1 
1791 N  N   . VAL A 210 ? 0.0780 0.0899 0.0900 0.0068  0.0077  -0.0059 210 VAL A N   
1792 C  CA  . VAL A 210 ? 0.0838 0.1026 0.0820 -0.0010 0.0024  -0.0044 210 VAL A CA  
1793 C  C   . VAL A 210 ? 0.0851 0.1091 0.0741 0.0070  0.0115  0.0027  210 VAL A C   
1794 O  O   . VAL A 210 ? 0.1075 0.1076 0.0909 -0.0124 0.0168  0.0040  210 VAL A O   
1795 C  CB  . VAL A 210 ? 0.0886 0.1064 0.0944 0.0147  0.0031  -0.0015 210 VAL A CB  
1796 C  CG1 . VAL A 210 ? 0.1014 0.0961 0.1045 0.0037  -0.0037 -0.0057 210 VAL A CG1 
1797 C  CG2 . VAL A 210 ? 0.1057 0.1093 0.1256 -0.0031 0.0048  -0.0010 210 VAL A CG2 
1798 N  N   . LEU A 211 ? 0.0944 0.1186 0.0987 -0.0214 -0.0013 -0.0063 211 LEU A N   
1799 C  CA  . LEU A 211 ? 0.1017 0.1260 0.1005 -0.0225 0.0052  -0.0049 211 LEU A CA  
1800 C  C   . LEU A 211 ? 0.0944 0.1158 0.1037 -0.0216 0.0043  0.0031  211 LEU A C   
1801 O  O   . LEU A 211 ? 0.1193 0.1276 0.0942 -0.0037 0.0006  0.0006  211 LEU A O   
1802 C  CB  . LEU A 211 ? 0.1222 0.1252 0.1181 0.0020  -0.0013 0.0199  211 LEU A CB  
1803 C  CG  . LEU A 211 ? 0.0912 0.1416 0.1277 0.0037  -0.0063 0.0060  211 LEU A CG  
1804 C  CD1 . LEU A 211 ? 0.1335 0.1759 0.1497 0.0078  -0.0310 0.0142  211 LEU A CD1 
1805 C  CD2 . LEU A 211 ? 0.1235 0.1492 0.1481 0.0107  0.0124  0.0020  211 LEU A CD2 
1806 N  N   . LYS A 212 ? 0.1021 0.1240 0.1164 -0.0337 0.0060  0.0093  212 LYS A N   
1807 C  CA  . LYS A 212 ? 0.1150 0.1331 0.1118 -0.0168 0.0006  0.0333  212 LYS A CA  
1808 C  C   . LYS A 212 ? 0.1228 0.1161 0.1247 -0.0099 0.0080  0.0256  212 LYS A C   
1809 O  O   . LYS A 212 ? 0.1401 0.1368 0.1619 -0.0162 -0.0326 0.0199  212 LYS A O   
1810 C  CB  . LYS A 212 ? 0.1272 0.1608 0.1463 -0.0324 -0.0012 0.0152  212 LYS A CB  
1811 C  CG  . LYS A 212 ? 0.1967 0.1978 0.1664 -0.0324 0.0184  0.0706  212 LYS A CG  
1812 C  CD  . LYS A 212 ? 0.3253 0.2640 0.1800 -0.0687 0.0445  0.0509  212 LYS A CD  
1813 C  CE  . LYS A 212 ? 0.3467 0.3079 0.2486 -0.0952 -0.0107 0.1344  212 LYS A CE  
1814 N  NZ  . LYS A 212 ? 0.5780 0.3770 0.3346 -0.0094 0.0741  0.1703  212 LYS A NZ  
1815 N  N   . GLU A 213 ? 0.1046 0.1301 0.1190 -0.0242 0.0015  0.0104  213 GLU A N   
1816 C  CA  . GLU A 213 ? 0.1249 0.1243 0.1191 -0.0200 0.0070  0.0035  213 GLU A CA  
1817 C  C   . GLU A 213 ? 0.1281 0.1094 0.1199 -0.0179 -0.0068 -0.0006 213 GLU A C   
1818 O  O   . GLU A 213 ? 0.1058 0.1204 0.1353 -0.0008 -0.0096 0.0176  213 GLU A O   
1819 C  CB  . GLU A 213 ? 0.1140 0.1588 0.1304 -0.0247 -0.0015 -0.0082 213 GLU A CB  
1820 C  CG  . GLU A 213 ? 0.1403 0.1910 0.1808 -0.0450 -0.0187 -0.0182 213 GLU A CG  
1821 C  CD  . GLU A 213 ? 0.1822 0.2314 0.2513 -0.0741 -0.0185 -0.0364 213 GLU A CD  
1822 O  OE1 . GLU A 213 ? 0.1267 0.2109 0.2504 -0.0194 -0.0441 0.0203  213 GLU A OE1 
1823 O  OE2 . GLU A 213 ? 0.2962 0.5914 0.4072 -0.0502 -0.0540 -0.2764 213 GLU A OE2 
1824 N  N   . PRO A 214 ? 0.1247 0.1199 0.1233 -0.0138 0.0005  0.0035  214 PRO A N   
1825 C  CA  . PRO A 214 ? 0.1259 0.1371 0.1106 -0.0087 -0.0035 -0.0166 214 PRO A CA  
1826 C  C   . PRO A 214 ? 0.1380 0.1159 0.1319 -0.0263 -0.0032 -0.0203 214 PRO A C   
1827 O  O   . PRO A 214 ? 0.1523 0.1739 0.1371 -0.0326 -0.0113 0.0055  214 PRO A O   
1828 C  CB  . PRO A 214 ? 0.1502 0.1023 0.1281 -0.0085 -0.0007 -0.0019 214 PRO A CB  
1829 C  CG  . PRO A 214 ? 0.2485 0.1798 0.2308 0.0381  0.0590  0.0359  214 PRO A CG  
1830 C  CD  . PRO A 214 ? 0.1443 0.1177 0.1678 -0.0062 0.0372  0.0248  214 PRO A CD  
1831 N  N   . ILE A 215 ? 0.1191 0.1330 0.1202 -0.0103 -0.0078 -0.0152 215 ILE A N   
1832 C  CA  . ILE A 215 ? 0.1324 0.1371 0.1086 -0.0032 -0.0162 -0.0207 215 ILE A CA  
1833 C  C   . ILE A 215 ? 0.1283 0.1308 0.1308 0.0020  -0.0165 -0.0115 215 ILE A C   
1834 O  O   . ILE A 215 ? 0.1267 0.1161 0.1639 -0.0020 -0.0043 -0.0200 215 ILE A O   
1835 C  CB  . ILE A 215 ? 0.1439 0.1326 0.1307 0.0119  -0.0008 -0.0165 215 ILE A CB  
1836 C  CG1 . ILE A 215 ? 0.1595 0.1226 0.1234 0.0048  0.0024  0.0000  215 ILE A CG1 
1837 C  CG2 . ILE A 215 ? 0.1592 0.1444 0.1414 0.0186  -0.0104 -0.0264 215 ILE A CG2 
1838 C  CD1 . ILE A 215 ? 0.2073 0.1516 0.1447 -0.0065 -0.0085 0.0248  215 ILE A CD1 
1839 N  N   A SER A 216 ? 0.1298 0.1362 0.1313 -0.0119 -0.0171 -0.0023 216 SER A N   
1840 N  N   B SER A 216 ? 0.1518 0.1272 0.1304 0.0010  -0.0278 -0.0361 216 SER A N   
1841 C  CA  A SER A 216 ? 0.1585 0.1631 0.1206 -0.0148 0.0093  -0.0065 216 SER A CA  
1842 C  CA  B SER A 216 ? 0.1580 0.1333 0.1407 -0.0066 -0.0390 -0.0351 216 SER A CA  
1843 C  C   A SER A 216 ? 0.1507 0.1120 0.1152 0.0024  -0.0337 -0.0143 216 SER A C   
1844 C  C   B SER A 216 ? 0.1608 0.1297 0.1344 0.0057  -0.0294 -0.0306 216 SER A C   
1845 O  O   A SER A 216 ? 0.1389 0.1637 0.1482 0.0026  -0.0331 -0.0120 216 SER A O   
1846 O  O   B SER A 216 ? 0.1288 0.1631 0.1540 -0.0172 -0.0194 -0.0130 216 SER A O   
1847 C  CB  A SER A 216 ? 0.1933 0.0944 0.1806 0.0126  -0.0008 -0.0452 216 SER A CB  
1848 C  CB  B SER A 216 ? 0.2639 0.1199 0.1832 -0.0427 0.0758  0.0093  216 SER A CB  
1849 O  OG  A SER A 216 ? 0.2117 0.1739 0.1872 -0.0661 -0.0296 -0.0217 216 SER A OG  
1850 O  OG  B SER A 216 ? 0.2829 0.1703 0.2014 -0.0219 0.0283  -0.0285 216 SER A OG  
1851 N  N   . VAL A 217 ? 0.1474 0.1274 0.1303 -0.0214 -0.0111 -0.0206 217 VAL A N   
1852 C  CA  . VAL A 217 ? 0.1764 0.1237 0.1380 -0.0328 -0.0119 -0.0230 217 VAL A CA  
1853 C  C   . VAL A 217 ? 0.1658 0.1353 0.1228 -0.0282 -0.0082 -0.0059 217 VAL A C   
1854 O  O   . VAL A 217 ? 0.1698 0.1237 0.1447 -0.0282 -0.0276 -0.0151 217 VAL A O   
1855 C  CB  . VAL A 217 ? 0.1541 0.1269 0.1448 -0.0198 -0.0203 -0.0168 217 VAL A CB  
1856 C  CG1 . VAL A 217 ? 0.1800 0.1107 0.1583 -0.0178 -0.0238 -0.0178 217 VAL A CG1 
1857 C  CG2 . VAL A 217 ? 0.1694 0.1423 0.1894 -0.0160 -0.0298 -0.0299 217 VAL A CG2 
1858 N  N   . SER A 218 ? 0.1554 0.1319 0.1357 -0.0333 -0.0244 -0.0177 218 SER A N   
1859 C  CA  . SER A 218 ? 0.1692 0.1405 0.1544 -0.0438 -0.0239 -0.0564 218 SER A CA  
1860 C  C   . SER A 218 ? 0.1741 0.1073 0.1454 -0.0335 -0.0274 -0.0087 218 SER A C   
1861 O  O   . SER A 218 ? 0.1730 0.1249 0.1439 -0.0302 -0.0204 -0.0211 218 SER A O   
1862 C  CB  . SER A 218 ? 0.1843 0.1527 0.1547 -0.0511 -0.0129 -0.0212 218 SER A CB  
1863 O  OG  . SER A 218 ? 0.1976 0.1826 0.1261 -0.0507 -0.0297 -0.0096 218 SER A OG  
1864 N  N   A SER A 219 ? 0.2179 0.1098 0.1615 -0.0133 -0.0052 -0.0250 219 SER A N   
1865 N  N   B SER A 219 ? 0.2249 0.0913 0.1669 -0.0489 -0.0024 -0.0141 219 SER A N   
1866 C  CA  A SER A 219 ? 0.1929 0.1450 0.1883 -0.0057 -0.0115 -0.0386 219 SER A CA  
1867 C  CA  B SER A 219 ? 0.2238 0.1307 0.1827 -0.0340 0.0071  -0.0251 219 SER A CA  
1868 C  C   A SER A 219 ? 0.2054 0.1299 0.1915 -0.0049 -0.0251 -0.0183 219 SER A C   
1869 C  C   B SER A 219 ? 0.1832 0.1263 0.1884 -0.0148 -0.0097 0.0109  219 SER A C   
1870 O  O   A SER A 219 ? 0.2220 0.1418 0.1926 -0.0248 0.0197  0.0221  219 SER A O   
1871 O  O   B SER A 219 ? 0.1991 0.1475 0.2113 -0.0513 0.0049  -0.0337 219 SER A O   
1872 C  CB  A SER A 219 ? 0.2050 0.1687 0.2093 0.0260  -0.0142 -0.0640 219 SER A CB  
1873 C  CB  B SER A 219 ? 0.2526 0.1407 0.2274 -0.0518 0.0410  0.0185  219 SER A CB  
1874 O  OG  A SER A 219 ? 0.2152 0.1472 0.1960 0.0126  -0.0335 -0.0373 219 SER A OG  
1875 O  OG  B SER A 219 ? 0.3041 0.2285 0.3086 0.0091  -0.0671 -0.0256 219 SER A OG  
1876 N  N   . GLU A 220 ? 0.1834 0.1444 0.1768 -0.0350 -0.0111 -0.0299 220 GLU A N   
1877 C  CA  . GLU A 220 ? 0.2068 0.1536 0.1726 -0.0146 -0.0222 -0.0194 220 GLU A CA  
1878 C  C   . GLU A 220 ? 0.1705 0.1744 0.1484 -0.0384 -0.0076 -0.0198 220 GLU A C   
1879 O  O   . GLU A 220 ? 0.1978 0.1748 0.1676 -0.0159 0.0219  -0.0340 220 GLU A O   
1880 C  CB  . GLU A 220 ? 0.2441 0.2082 0.1682 -0.0467 -0.0562 -0.0562 220 GLU A CB  
1881 C  CG  . GLU A 220 ? 0.3508 0.2429 0.2260 -0.0786 -0.0443 -0.0710 220 GLU A CG  
1882 C  CD  . GLU A 220 ? 0.3318 0.2208 0.2224 -0.0952 -0.0377 -0.0901 220 GLU A CD  
1883 O  OE1 . GLU A 220 ? 0.2698 0.2109 0.2420 -0.0945 -0.0232 -0.0573 220 GLU A OE1 
1884 O  OE2 . GLU A 220 ? 0.6376 0.2808 0.4131 -0.2203 0.1054  -0.1268 220 GLU A OE2 
1885 N  N   . GLN A 221 ? 0.1773 0.1436 0.1341 -0.0331 -0.0098 -0.0256 221 GLN A N   
1886 C  CA  . GLN A 221 ? 0.1483 0.1331 0.1680 -0.0171 -0.0188 -0.0166 221 GLN A CA  
1887 C  C   . GLN A 221 ? 0.1446 0.1321 0.1342 -0.0208 -0.0249 -0.0034 221 GLN A C   
1888 O  O   . GLN A 221 ? 0.1763 0.1391 0.1425 -0.0179 0.0008  0.0115  221 GLN A O   
1889 C  CB  . GLN A 221 ? 0.1653 0.1535 0.1272 -0.0219 -0.0225 -0.0021 221 GLN A CB  
1890 C  CG  . GLN A 221 ? 0.1696 0.1710 0.1407 -0.0280 -0.0392 -0.0143 221 GLN A CG  
1891 C  CD  . GLN A 221 ? 0.1926 0.1459 0.1504 -0.0362 -0.0164 -0.0148 221 GLN A CD  
1892 O  OE1 . GLN A 221 ? 0.1867 0.1538 0.1392 -0.0218 -0.0167 -0.0038 221 GLN A OE1 
1893 N  NE2 . GLN A 221 ? 0.1766 0.1651 0.1820 -0.0175 -0.0262 -0.0005 221 GLN A NE2 
1894 N  N   A VAL A 222 ? 0.1793 0.1124 0.1447 -0.0305 -0.0313 -0.0031 222 VAL A N   
1895 N  N   B VAL A 222 ? 0.1567 0.1283 0.1544 -0.0193 -0.0194 0.0094  222 VAL A N   
1896 C  CA  A VAL A 222 ? 0.1684 0.1447 0.1405 -0.0147 -0.0071 0.0166  222 VAL A CA  
1897 C  CA  B VAL A 222 ? 0.1905 0.1732 0.1565 -0.0225 -0.0357 0.0204  222 VAL A CA  
1898 C  C   A VAL A 222 ? 0.1824 0.1251 0.1811 -0.0186 0.0192  0.0175  222 VAL A C   
1899 C  C   B VAL A 222 ? 0.2290 0.1411 0.1886 -0.0223 -0.0013 0.0258  222 VAL A C   
1900 O  O   A VAL A 222 ? 0.1644 0.1635 0.1653 -0.0230 -0.0068 0.0266  222 VAL A O   
1901 O  O   B VAL A 222 ? 0.2098 0.1711 0.1884 -0.0120 -0.0043 0.0397  222 VAL A O   
1902 C  CB  A VAL A 222 ? 0.2021 0.1536 0.1100 -0.0298 -0.0071 -0.0167 222 VAL A CB  
1903 C  CB  B VAL A 222 ? 0.1725 0.2452 0.1597 -0.0183 0.0401  0.0537  222 VAL A CB  
1904 C  CG1 A VAL A 222 ? 0.1905 0.1455 0.1477 -0.0272 0.0129  0.0434  222 VAL A CG1 
1905 C  CG1 B VAL A 222 ? 0.1714 0.2987 0.2300 0.0410  0.0081  0.0502  222 VAL A CG1 
1906 C  CG2 A VAL A 222 ? 0.2147 0.1295 0.1534 -0.0333 -0.0417 -0.0222 222 VAL A CG2 
1907 C  CG2 B VAL A 222 ? 0.1623 0.2255 0.1924 -0.0197 0.0204  -0.0043 222 VAL A CG2 
1908 N  N   . LEU A 223 ? 0.1951 0.1375 0.1985 -0.0247 0.0187  0.0054  223 LEU A N   
1909 C  CA  . LEU A 223 ? 0.2148 0.1586 0.2587 -0.0013 0.0342  -0.0276 223 LEU A CA  
1910 C  C   . LEU A 223 ? 0.1818 0.1552 0.1875 0.0023  0.0087  -0.0339 223 LEU A C   
1911 O  O   . LEU A 223 ? 0.1829 0.2060 0.2089 0.0005  0.0038  -0.0423 223 LEU A O   
1912 C  CB  . LEU A 223 ? 0.2379 0.1928 0.3337 -0.0390 0.0577  -0.0835 223 LEU A CB  
1913 C  CG  . LEU A 223 ? 0.3939 0.3641 0.4914 -0.0516 -0.0259 -0.0189 223 LEU A CG  
1914 C  CD1 . LEU A 223 ? 0.6714 0.2470 0.6263 -0.0311 -0.0816 -0.0854 223 LEU A CD1 
1915 C  CD2 . LEU A 223 ? 0.4002 0.2808 0.5138 -0.0292 -0.1509 -0.0261 223 LEU A CD2 
1916 N  N   . LYS A 224 ? 0.2190 0.1808 0.1581 -0.0256 -0.0082 -0.0350 224 LYS A N   
1917 C  CA  . LYS A 224 ? 0.2032 0.1836 0.1475 -0.0416 0.0142  -0.0198 224 LYS A CA  
1918 C  C   . LYS A 224 ? 0.1847 0.1660 0.1355 -0.0178 0.0115  -0.0240 224 LYS A C   
1919 O  O   . LYS A 224 ? 0.2035 0.1888 0.1116 -0.0337 0.0021  -0.0015 224 LYS A O   
1920 C  CB  . LYS A 224 ? 0.2788 0.3179 0.1802 0.0116  -0.0230 0.0383  224 LYS A CB  
1921 C  CG  . LYS A 224 ? 0.2089 0.3919 0.1712 -0.0028 -0.0234 0.0209  224 LYS A CG  
1922 C  CD  . LYS A 224 ? 0.2696 0.6750 0.3012 0.0131  -0.1150 0.0283  224 LYS A CD  
1923 C  CE  . LYS A 224 ? 0.5493 0.6604 0.3641 -0.0350 -0.2172 0.0115  224 LYS A CE  
1924 N  NZ  . LYS A 224 ? 0.6531 0.5497 0.3036 -0.1272 0.0458  -0.1406 224 LYS A NZ  
1925 N  N   . PHE A 225 ? 0.1766 0.1499 0.0996 -0.0144 -0.0052 0.0005  225 PHE A N   
1926 C  CA  . PHE A 225 ? 0.1604 0.1579 0.1048 -0.0230 0.0066  -0.0008 225 PHE A CA  
1927 C  C   . PHE A 225 ? 0.1748 0.1497 0.0798 -0.0294 0.0240  -0.0065 225 PHE A C   
1928 O  O   . PHE A 225 ? 0.1818 0.1328 0.1206 -0.0306 0.0168  0.0037  225 PHE A O   
1929 C  CB  . PHE A 225 ? 0.1836 0.1425 0.1159 -0.0186 0.0241  0.0028  225 PHE A CB  
1930 C  CG  . PHE A 225 ? 0.1764 0.1204 0.1362 -0.0331 0.0019  -0.0153 225 PHE A CG  
1931 C  CD1 . PHE A 225 ? 0.2147 0.1917 0.1337 0.0215  0.0223  -0.0151 225 PHE A CD1 
1932 C  CD2 . PHE A 225 ? 0.1824 0.1887 0.1434 -0.0282 -0.0152 -0.0379 225 PHE A CD2 
1933 C  CE1 . PHE A 225 ? 0.2196 0.1723 0.1484 0.0000  0.0131  0.0258  225 PHE A CE1 
1934 C  CE2 . PHE A 225 ? 0.1906 0.2314 0.2105 -0.0126 -0.0057 -0.0693 225 PHE A CE2 
1935 C  CZ  . PHE A 225 ? 0.1962 0.1729 0.2030 -0.0138 0.0083  -0.0697 225 PHE A CZ  
1936 N  N   . ARG A 226 ? 0.1457 0.1321 0.1168 -0.0175 0.0091  -0.0098 226 ARG A N   
1937 C  CA  . ARG A 226 ? 0.1605 0.1597 0.1136 -0.0266 0.0164  -0.0060 226 ARG A CA  
1938 C  C   . ARG A 226 ? 0.1942 0.1632 0.1303 -0.0182 0.0054  -0.0153 226 ARG A C   
1939 O  O   . ARG A 226 ? 0.2009 0.1664 0.1434 -0.0210 0.0340  -0.0181 226 ARG A O   
1940 C  CB  . ARG A 226 ? 0.1727 0.1569 0.1161 0.0005  0.0041  0.0092  226 ARG A CB  
1941 C  CG  . ARG A 226 ? 0.2002 0.1342 0.1111 -0.0195 0.0164  -0.0006 226 ARG A CG  
1942 C  CD  . ARG A 226 ? 0.2424 0.1547 0.1333 0.0085  0.0167  0.0103  226 ARG A CD  
1943 N  NE  . ARG A 226 ? 0.1895 0.1369 0.1224 -0.0362 0.0003  -0.0043 226 ARG A NE  
1944 C  CZ  . ARG A 226 ? 0.2362 0.1448 0.1208 -0.0584 0.0052  -0.0093 226 ARG A CZ  
1945 N  NH1 . ARG A 226 ? 0.2597 0.2012 0.2054 -0.0741 -0.0203 -0.0619 226 ARG A NH1 
1946 N  NH2 . ARG A 226 ? 0.2416 0.1772 0.1538 -0.0476 0.0373  -0.0060 226 ARG A NH2 
1947 N  N   . LYS A 227 ? 0.1813 0.1585 0.1039 -0.0215 0.0218  -0.0278 227 LYS A N   
1948 C  CA  . LYS A 227 ? 0.2326 0.1764 0.0978 -0.0626 0.0206  -0.0281 227 LYS A CA  
1949 C  C   . LYS A 227 ? 0.1843 0.1545 0.1055 -0.0401 0.0186  -0.0223 227 LYS A C   
1950 O  O   . LYS A 227 ? 0.2795 0.1942 0.1094 -0.0443 0.0546  -0.0115 227 LYS A O   
1951 C  CB  . LYS A 227 ? 0.2327 0.2319 0.1297 -0.0798 0.0310  -0.0269 227 LYS A CB  
1952 C  CG  . LYS A 227 ? 0.2687 0.2150 0.2495 -0.0780 0.0212  -0.0593 227 LYS A CG  
1953 C  CD  . LYS A 227 ? 0.2669 0.3952 0.3447 -0.0175 -0.0292 -0.1730 227 LYS A CD  
1954 C  CE  . LYS A 227 ? 0.5170 0.5590 0.3648 -0.0803 0.0186  0.0182  227 LYS A CE  
1955 N  NZ  . LYS A 227 ? 0.8838 0.7350 0.4972 -0.2982 -0.1430 -0.1724 227 LYS A NZ  
1956 N  N   . LEU A 228 ? 0.1890 0.1369 0.1253 -0.0419 0.0068  -0.0283 228 LEU A N   
1957 C  CA  . LEU A 228 ? 0.2233 0.1549 0.0812 -0.0372 0.0133  -0.0068 228 LEU A CA  
1958 C  C   . LEU A 228 ? 0.2301 0.1887 0.1024 -0.0537 0.0555  -0.0397 228 LEU A C   
1959 O  O   . LEU A 228 ? 0.1888 0.1766 0.1360 -0.0410 0.0421  -0.0188 228 LEU A O   
1960 C  CB  . LEU A 228 ? 0.1908 0.1732 0.1067 -0.0264 0.0252  -0.0146 228 LEU A CB  
1961 C  CG  . LEU A 228 ? 0.2052 0.1464 0.1128 -0.0335 0.0146  -0.0054 228 LEU A CG  
1962 C  CD1 . LEU A 228 ? 0.2093 0.1728 0.1062 -0.0255 0.0219  -0.0165 228 LEU A CD1 
1963 C  CD2 . LEU A 228 ? 0.2605 0.2131 0.1504 -0.0255 0.0406  0.0447  228 LEU A CD2 
1964 N  N   . ASN A 229 ? 0.2366 0.1878 0.1172 -0.0690 0.0549  -0.0241 229 ASN A N   
1965 C  CA  . ASN A 229 ? 0.2337 0.2271 0.1158 -0.1010 0.0368  -0.0153 229 ASN A CA  
1966 C  C   . ASN A 229 ? 0.2520 0.2192 0.1425 -0.0533 0.0715  -0.0217 229 ASN A C   
1967 O  O   . ASN A 229 ? 0.2378 0.2240 0.1511 -0.0736 0.0370  -0.0273 229 ASN A O   
1968 C  CB  . ASN A 229 ? 0.2590 0.2357 0.1382 -0.0646 0.0705  -0.0289 229 ASN A CB  
1969 C  CG  . ASN A 229 ? 0.2761 0.2788 0.1143 -0.0640 0.0494  -0.0236 229 ASN A CG  
1970 O  OD1 . ASN A 229 ? 0.4368 0.3452 0.1335 -0.0741 0.1133  -0.0764 229 ASN A OD1 
1971 N  ND2 . ASN A 229 ? 0.2784 0.2177 0.1699 -0.0719 0.0671  -0.0557 229 ASN A ND2 
1972 N  N   . PHE A 230 ? 0.2235 0.2624 0.1421 -0.0951 0.0767  -0.0436 230 PHE A N   
1973 C  CA  . PHE A 230 ? 0.2545 0.2675 0.1797 -0.1234 0.0916  -0.0557 230 PHE A CA  
1974 C  C   . PHE A 230 ? 0.2301 0.2420 0.1881 -0.0856 0.0722  -0.0500 230 PHE A C   
1975 O  O   . PHE A 230 ? 0.2709 0.2398 0.1597 -0.1077 0.0694  -0.0410 230 PHE A O   
1976 C  CB  . PHE A 230 ? 0.2619 0.3181 0.1511 -0.1286 0.0918  -0.0505 230 PHE A CB  
1977 C  CG  . PHE A 230 ? 0.2199 0.2239 0.1868 -0.0803 0.0649  -0.0254 230 PHE A CG  
1978 C  CD1 . PHE A 230 ? 0.2068 0.2330 0.1358 -0.0643 0.0318  -0.0317 230 PHE A CD1 
1979 C  CD2 . PHE A 230 ? 0.1525 0.2443 0.1675 -0.0335 0.0480  -0.0329 230 PHE A CD2 
1980 C  CE1 . PHE A 230 ? 0.1843 0.2229 0.1781 -0.0722 0.0346  -0.0155 230 PHE A CE1 
1981 C  CE2 . PHE A 230 ? 0.2314 0.2228 0.1820 -0.0737 0.0649  -0.0298 230 PHE A CE2 
1982 C  CZ  . PHE A 230 ? 0.1861 0.2495 0.1283 -0.0434 0.0401  -0.0318 230 PHE A CZ  
1983 N  N   . ASN A 231 ? 0.2364 0.2813 0.1808 -0.1268 0.0951  -0.0705 231 ASN A N   
1984 C  CA  . ASN A 231 ? 0.2603 0.2964 0.1762 -0.1312 0.0877  -0.0648 231 ASN A CA  
1985 C  C   . ASN A 231 ? 0.2836 0.3355 0.1852 -0.1436 0.0885  -0.0615 231 ASN A C   
1986 O  O   . ASN A 231 ? 0.3285 0.2696 0.1667 -0.1332 0.1052  -0.0524 231 ASN A O   
1987 C  CB  . ASN A 231 ? 0.3185 0.3296 0.2696 -0.1604 0.1578  -0.0964 231 ASN A CB  
1988 C  CG  . ASN A 231 ? 0.3623 0.3488 0.2179 -0.1897 0.1211  -0.0714 231 ASN A CG  
1989 O  OD1 . ASN A 231 ? 0.2904 0.2901 0.2231 -0.1348 0.1289  -0.0890 231 ASN A OD1 
1990 N  ND2 . ASN A 231 ? 0.3873 0.3468 0.2267 -0.1349 0.1282  -0.0759 231 ASN A ND2 
1991 N  N   . GLY A 232 ? 0.3772 0.2657 0.2212 -0.1352 0.1416  -0.0590 232 GLY A N   
1992 C  CA  . GLY A 232 ? 0.4507 0.3258 0.1545 -0.1322 0.0895  0.0138  232 GLY A CA  
1993 C  C   . GLY A 232 ? 0.3100 0.3404 0.2594 -0.0373 -0.0278 0.0516  232 GLY A C   
1994 O  O   . GLY A 232 ? 0.3113 0.3585 0.2357 -0.1054 0.1465  -0.0093 232 GLY A O   
1995 N  N   . GLU A 233 ? 0.2508 0.2939 0.2019 -0.0702 0.0308  0.0388  233 GLU A N   
1996 C  CA  . GLU A 233 ? 0.2791 0.2237 0.2242 -0.0302 -0.0153 0.0326  233 GLU A CA  
1997 C  C   . GLU A 233 ? 0.2804 0.3928 0.3379 0.0006  -0.0293 -0.1736 233 GLU A C   
1998 O  O   . GLU A 233 ? 0.5378 0.4726 0.1888 -0.1659 0.1518  -0.0674 233 GLU A O   
1999 C  CB  . GLU A 233 ? 0.3055 0.3086 0.2445 0.0318  0.0513  0.0958  233 GLU A CB  
2000 C  CG  . GLU A 233 ? 0.2669 0.4582 0.1676 -0.0205 0.0307  0.0697  233 GLU A CG  
2001 C  CD  . GLU A 233 ? 0.6060 0.5029 0.3729 0.0612  -0.1642 -0.0120 233 GLU A CD  
2002 O  OE1 . GLU A 233 ? 0.5134 0.4117 0.3686 0.0080  0.0970  0.1604  233 GLU A OE1 
2003 O  OE2 . GLU A 233 ? 0.7315 0.5406 0.2587 -0.2065 0.0912  -0.0441 233 GLU A OE2 
2004 N  N   . GLY A 234 ? 0.7473 0.4036 0.5451 -0.0307 0.2212  -0.0237 234 GLY A N   
2005 C  CA  . GLY A 234 ? 0.5631 0.2813 0.6029 -0.0315 0.1186  -0.2728 234 GLY A CA  
2006 C  C   . GLY A 234 ? 1.2350 0.6827 0.3984 -0.0509 0.1062  0.2398  234 GLY A C   
2007 O  O   . GLY A 234 ? 1.6564 1.9228 0.2380 0.0346  0.4465  -0.2816 234 GLY A O   
2008 N  N   . GLU A 235 ? 0.5167 0.3682 0.2761 -0.0377 0.2093  -0.0366 235 GLU A N   
2009 C  CA  . GLU A 235 ? 0.5103 0.3420 0.2851 -0.1280 0.1762  -0.0715 235 GLU A CA  
2010 C  C   . GLU A 235 ? 0.2418 0.2508 0.2212 0.0109  0.0776  -0.0131 235 GLU A C   
2011 O  O   . GLU A 235 ? 0.3680 0.4774 0.2678 -0.1089 0.1421  -0.1146 235 GLU A O   
2012 C  CB  . GLU A 235 ? 0.6154 0.3966 0.4083 -0.1974 0.3600  -0.1651 235 GLU A CB  
2013 C  CG  . GLU A 235 ? 0.4257 0.4232 0.5113 -0.2124 0.2820  -0.1055 235 GLU A CG  
2014 C  CD  . GLU A 235 ? 0.7559 0.5163 0.5389 -0.1017 0.0860  -0.1753 235 GLU A CD  
2015 O  OE1 . GLU A 235 ? 0.6035 0.7419 0.9970 -0.0887 0.1757  0.1768  235 GLU A OE1 
2016 O  OE2 . GLU A 235 ? 0.6298 0.6122 0.7491 -0.1265 0.4555  -0.1026 235 GLU A OE2 
2017 N  N   . PRO A 236 ? 0.2700 0.4417 0.2881 -0.0141 0.0970  -0.0370 236 PRO A N   
2018 C  CA  . PRO A 236 ? 0.2696 0.4388 0.2624 -0.0195 0.0983  -0.0222 236 PRO A CA  
2019 C  C   . PRO A 236 ? 0.3842 0.4092 0.2549 -0.1601 0.1869  -0.0852 236 PRO A C   
2020 O  O   . PRO A 236 ? 0.3348 0.5080 0.2483 -0.1711 0.1632  -0.1370 236 PRO A O   
2021 C  CB  . PRO A 236 ? 0.2948 0.5655 0.3928 -0.0068 0.1596  0.0706  236 PRO A CB  
2022 C  CG  . PRO A 236 ? 0.3023 0.3761 0.3783 -0.0308 0.0879  -0.0505 236 PRO A CG  
2023 C  CD  . PRO A 236 ? 0.2529 0.3005 0.3249 0.0754  0.0544  0.0133  236 PRO A CD  
2024 N  N   . GLU A 237 ? 0.3671 0.3691 0.2221 -0.1186 0.1693  -0.1348 237 GLU A N   
2025 C  CA  . GLU A 237 ? 0.2919 0.3662 0.1498 -0.0584 0.0819  -0.0894 237 GLU A CA  
2026 C  C   . GLU A 237 ? 0.2518 0.3169 0.1698 -0.0914 0.0895  -0.0606 237 GLU A C   
2027 O  O   . GLU A 237 ? 0.2511 0.3923 0.2360 -0.0829 0.0636  -0.0829 237 GLU A O   
2028 C  CB  . GLU A 237 ? 0.3152 0.2248 0.2078 -0.0362 0.0445  -0.0443 237 GLU A CB  
2029 C  CG  . GLU A 237 ? 0.3014 0.3671 0.3416 -0.1023 0.0825  -0.1333 237 GLU A CG  
2030 C  CD  . GLU A 237 ? 0.3515 0.2969 0.2402 -0.0627 -0.0205 -0.0693 237 GLU A CD  
2031 O  OE1 . GLU A 237 ? 0.5303 0.4063 0.5963 0.0076  -0.1439 -0.3077 237 GLU A OE1 
2032 O  OE2 . GLU A 237 ? 0.3580 0.3219 0.2666 -0.0597 0.0883  -0.0803 237 GLU A OE2 
2033 N  N   . GLU A 238 ? 0.2213 0.3163 0.1851 -0.1077 0.1050  -0.0800 238 GLU A N   
2034 C  CA  . GLU A 238 ? 0.1856 0.3779 0.2141 -0.1193 0.0879  -0.0688 238 GLU A CA  
2035 C  C   . GLU A 238 ? 0.2025 0.2563 0.1448 -0.0771 0.0522  -0.0443 238 GLU A C   
2036 O  O   . GLU A 238 ? 0.2944 0.2330 0.1976 -0.0869 0.0806  -0.0390 238 GLU A O   
2037 C  CB  . GLU A 238 ? 0.2538 0.4273 0.2664 -0.1366 0.0890  -0.1066 238 GLU A CB  
2038 C  CG  . GLU A 238 ? 0.2623 0.7204 0.2978 -0.2187 0.0995  -0.0951 238 GLU A CG  
2039 C  CD  . GLU A 238 ? 0.3664 0.4451 0.2994 -0.1167 0.0625  -0.0679 238 GLU A CD  
2040 O  OE1 . GLU A 238 ? 0.2743 0.4156 0.2845 -0.1639 0.0741  -0.0524 238 GLU A OE1 
2041 O  OE2 . GLU A 238 ? 0.4220 0.1609 0.0662 -0.2318 0.1273  -0.0744 238 GLU A OE2 
2042 N  N   . LEU A 239 ? 0.1814 0.2251 0.1581 -0.0428 0.0681  -0.0450 239 LEU A N   
2043 C  CA  . LEU A 239 ? 0.1554 0.1904 0.1312 -0.0260 0.0350  -0.0201 239 LEU A CA  
2044 C  C   . LEU A 239 ? 0.1523 0.1685 0.1340 -0.0432 0.0399  -0.0057 239 LEU A C   
2045 O  O   . LEU A 239 ? 0.1856 0.2167 0.1409 -0.0241 0.0410  -0.0260 239 LEU A O   
2046 C  CB  . LEU A 239 ? 0.2326 0.1811 0.1795 -0.0052 0.0412  -0.0333 239 LEU A CB  
2047 C  CG  . LEU A 239 ? 0.2046 0.1940 0.2129 0.0015  0.0156  -0.0408 239 LEU A CG  
2048 C  CD1 . LEU A 239 ? 0.3176 0.1226 0.4266 -0.0035 -0.0155 -0.0348 239 LEU A CD1 
2049 C  CD2 . LEU A 239 ? 0.2542 0.2239 0.1951 0.0296  0.0331  -0.0658 239 LEU A CD2 
2050 N  N   . MET A 240 ? 0.1771 0.1807 0.1220 -0.0209 0.0533  -0.0104 240 MET A N   
2051 C  CA  . MET A 240 ? 0.1825 0.1680 0.0969 -0.0328 0.0500  -0.0078 240 MET A CA  
2052 C  C   . MET A 240 ? 0.1473 0.1551 0.1064 -0.0303 0.0259  -0.0291 240 MET A C   
2053 O  O   . MET A 240 ? 0.1520 0.1614 0.1080 -0.0256 0.0196  -0.0071 240 MET A O   
2054 C  CB  . MET A 240 ? 0.2215 0.1572 0.1364 -0.0351 0.0500  -0.0024 240 MET A CB  
2055 C  CG  . MET A 240 ? 0.2111 0.1890 0.1102 -0.0599 0.0535  -0.0091 240 MET A CG  
2056 S  SD  . MET A 240 ? 0.2291 0.1499 0.1576 -0.0430 0.0653  -0.0027 240 MET A SD  
2057 C  CE  . MET A 240 ? 0.2448 0.1578 0.1639 -0.0684 0.0632  -0.0093 240 MET A CE  
2058 N  N   . VAL A 241 ? 0.1676 0.1371 0.1028 -0.0234 0.0264  -0.0222 241 VAL A N   
2059 C  CA  . VAL A 241 ? 0.1601 0.1307 0.0976 -0.0082 0.0154  -0.0144 241 VAL A CA  
2060 C  C   . VAL A 241 ? 0.1179 0.1290 0.1238 -0.0052 0.0070  -0.0153 241 VAL A C   
2061 O  O   . VAL A 241 ? 0.1383 0.1651 0.1163 -0.0220 0.0261  -0.0227 241 VAL A O   
2062 C  CB  . VAL A 241 ? 0.1351 0.1509 0.1298 -0.0147 0.0126  -0.0570 241 VAL A CB  
2063 C  CG1 . VAL A 241 ? 0.1861 0.1789 0.1155 -0.0057 -0.0001 -0.0394 241 VAL A CG1 
2064 C  CG2 . VAL A 241 ? 0.1617 0.1605 0.1775 -0.0218 0.0255  -0.0434 241 VAL A CG2 
2065 N  N   . ASP A 242 ? 0.1238 0.1224 0.0952 -0.0104 0.0317  -0.0140 242 ASP A N   
2066 C  CA  . ASP A 242 ? 0.1330 0.1176 0.0992 0.0020  0.0184  -0.0250 242 ASP A CA  
2067 C  C   . ASP A 242 ? 0.1251 0.1283 0.0904 -0.0099 0.0193  -0.0167 242 ASP A C   
2068 O  O   . ASP A 242 ? 0.1488 0.1356 0.1396 -0.0126 0.0030  -0.0333 242 ASP A O   
2069 C  CB  . ASP A 242 ? 0.1427 0.1263 0.1258 0.0055  0.0110  -0.0082 242 ASP A CB  
2070 C  CG  . ASP A 242 ? 0.1439 0.1057 0.1384 0.0148  0.0269  -0.0179 242 ASP A CG  
2071 O  OD1 . ASP A 242 ? 0.1535 0.1170 0.1229 0.0024  0.0273  -0.0118 242 ASP A OD1 
2072 O  OD2 . ASP A 242 ? 0.1696 0.1347 0.1524 0.0183  0.0305  -0.0331 242 ASP A OD2 
2073 N  N   . ASN A 243 ? 0.1262 0.1116 0.0935 -0.0175 0.0366  -0.0147 243 ASN A N   
2074 C  CA  . ASN A 243 ? 0.1400 0.1023 0.1046 -0.0162 0.0288  -0.0205 243 ASN A CA  
2075 C  C   . ASN A 243 ? 0.1021 0.1136 0.0985 -0.0197 0.0118  -0.0074 243 ASN A C   
2076 O  O   . ASN A 243 ? 0.1412 0.1279 0.1014 0.0093  0.0225  0.0005  243 ASN A O   
2077 C  CB  . ASN A 243 ? 0.1324 0.1243 0.0910 -0.0258 0.0285  -0.0030 243 ASN A CB  
2078 C  CG  . ASN A 243 ? 0.1125 0.1075 0.0992 -0.0333 0.0304  -0.0017 243 ASN A CG  
2079 O  OD1 . ASN A 243 ? 0.1418 0.1256 0.1299 -0.0245 0.0137  0.0339  243 ASN A OD1 
2080 N  ND2 . ASN A 243 ? 0.1545 0.1459 0.1333 -0.0311 0.0043  0.0315  243 ASN A ND2 
2081 N  N   . TRP A 244 ? 0.1278 0.0985 0.0897 -0.0076 0.0143  -0.0172 244 TRP A N   
2082 C  CA  . TRP A 244 ? 0.1018 0.1033 0.0886 0.0110  0.0109  -0.0138 244 TRP A CA  
2083 C  C   . TRP A 244 ? 0.1055 0.0897 0.0978 -0.0087 0.0216  -0.0113 244 TRP A C   
2084 O  O   . TRP A 244 ? 0.1120 0.1252 0.1276 0.0097  0.0082  -0.0251 244 TRP A O   
2085 C  CB  . TRP A 244 ? 0.1234 0.0924 0.1015 -0.0003 0.0178  -0.0194 244 TRP A CB  
2086 C  CG  . TRP A 244 ? 0.1120 0.0863 0.0998 -0.0031 0.0199  -0.0146 244 TRP A CG  
2087 C  CD1 . TRP A 244 ? 0.1155 0.1057 0.0992 -0.0080 0.0182  -0.0046 244 TRP A CD1 
2088 C  CD2 . TRP A 244 ? 0.1014 0.0966 0.1100 -0.0054 0.0198  -0.0046 244 TRP A CD2 
2089 N  NE1 . TRP A 244 ? 0.1200 0.1112 0.1068 0.0043  0.0195  0.0020  244 TRP A NE1 
2090 C  CE2 . TRP A 244 ? 0.0988 0.1093 0.1154 0.0013  0.0188  -0.0086 244 TRP A CE2 
2091 C  CE3 . TRP A 244 ? 0.1281 0.1216 0.1106 -0.0040 0.0141  -0.0046 244 TRP A CE3 
2092 C  CZ2 . TRP A 244 ? 0.1254 0.1243 0.1332 0.0100  0.0161  -0.0062 244 TRP A CZ2 
2093 C  CZ3 . TRP A 244 ? 0.1365 0.1163 0.1276 0.0082  -0.0087 0.0030  244 TRP A CZ3 
2094 C  CH2 . TRP A 244 ? 0.1310 0.1425 0.1262 0.0207  0.0074  -0.0081 244 TRP A CH2 
2095 N  N   . ARG A 245 ? 0.1091 0.1091 0.0949 -0.0021 0.0184  -0.0208 245 ARG A N   
2096 C  CA  . ARG A 245 ? 0.0960 0.1001 0.1073 0.0023  0.0046  -0.0204 245 ARG A CA  
2097 C  C   . ARG A 245 ? 0.0851 0.0969 0.1080 0.0071  0.0041  -0.0245 245 ARG A C   
2098 O  O   . ARG A 245 ? 0.0944 0.1143 0.1156 0.0043  0.0092  -0.0210 245 ARG A O   
2099 C  CB  . ARG A 245 ? 0.1018 0.1233 0.1114 0.0035  0.0019  -0.0233 245 ARG A CB  
2100 C  CG  . ARG A 245 ? 0.0926 0.1046 0.1206 0.0008  0.0015  -0.0127 245 ARG A CG  
2101 C  CD  . ARG A 245 ? 0.0940 0.1197 0.1277 -0.0043 -0.0066 -0.0320 245 ARG A CD  
2102 N  NE  . ARG A 245 ? 0.1012 0.1152 0.1328 -0.0104 0.0007  -0.0271 245 ARG A NE  
2103 C  CZ  . ARG A 245 ? 0.0951 0.1233 0.1093 -0.0120 0.0118  -0.0233 245 ARG A CZ  
2104 N  NH1 . ARG A 245 ? 0.0979 0.1438 0.1339 -0.0196 0.0230  -0.0278 245 ARG A NH1 
2105 N  NH2 . ARG A 245 ? 0.0991 0.1474 0.1468 -0.0247 -0.0054 -0.0190 245 ARG A NH2 
2106 N  N   A PRO A 246 ? 0.0935 0.0985 0.1071 0.0109  0.0070  -0.0006 246 PRO A N   
2107 N  N   B PRO A 246 ? 0.1129 0.0988 0.1124 0.0226  -0.0005 -0.0126 246 PRO A N   
2108 C  CA  A PRO A 246 ? 0.1197 0.0961 0.1141 0.0068  0.0082  0.0010  246 PRO A CA  
2109 C  CA  B PRO A 246 ? 0.1127 0.1018 0.1224 0.0157  -0.0080 -0.0227 246 PRO A CA  
2110 C  C   A PRO A 246 ? 0.1093 0.0964 0.1129 0.0179  -0.0138 -0.0019 246 PRO A C   
2111 C  C   B PRO A 246 ? 0.1184 0.1032 0.1080 0.0188  -0.0118 -0.0071 246 PRO A C   
2112 O  O   A PRO A 246 ? 0.1181 0.1024 0.1052 0.0030  -0.0046 -0.0068 246 PRO A O   
2113 O  O   B PRO A 246 ? 0.1211 0.1057 0.1115 0.0171  0.0010  -0.0071 246 PRO A O   
2114 C  CB  A PRO A 246 ? 0.0966 0.1462 0.1396 0.0162  0.0040  -0.0111 246 PRO A CB  
2115 C  CB  B PRO A 246 ? 0.1306 0.0960 0.1008 0.0266  -0.0248 -0.0027 246 PRO A CB  
2116 C  CG  A PRO A 246 ? 0.1001 0.1409 0.1441 0.0005  0.0030  0.0285  246 PRO A CG  
2117 C  CG  B PRO A 246 ? 0.1766 0.1136 0.1935 0.0138  -0.0066 0.0386  246 PRO A CG  
2118 C  CD  A PRO A 246 ? 0.0870 0.1112 0.1527 0.0114  0.0098  -0.0046 246 PRO A CD  
2119 C  CD  B PRO A 246 ? 0.1164 0.1378 0.1262 0.0377  0.0074  -0.0017 246 PRO A CD  
2120 N  N   . ALA A 247 ? 0.1277 0.1109 0.1107 0.0103  -0.0027 -0.0057 247 ALA A N   
2121 C  CA  . ALA A 247 ? 0.1247 0.1186 0.1021 0.0040  -0.0052 -0.0089 247 ALA A CA  
2122 C  C   . ALA A 247 ? 0.1141 0.1240 0.1202 0.0350  0.0030  -0.0001 247 ALA A C   
2123 O  O   . ALA A 247 ? 0.1373 0.1233 0.1333 0.0372  -0.0093 -0.0026 247 ALA A O   
2124 C  CB  . ALA A 247 ? 0.1884 0.1197 0.1453 -0.0052 0.0285  0.0055  247 ALA A CB  
2125 N  N   . GLN A 248 ? 0.1240 0.1093 0.1111 0.0120  -0.0083 -0.0142 248 GLN A N   
2126 C  CA  . GLN A 248 ? 0.1195 0.1235 0.1071 0.0263  -0.0153 0.0008  248 GLN A CA  
2127 C  C   . GLN A 248 ? 0.1197 0.1209 0.1233 0.0040  -0.0031 -0.0076 248 GLN A C   
2128 O  O   . GLN A 248 ? 0.1289 0.1306 0.1190 0.0062  0.0015  -0.0006 248 GLN A O   
2129 C  CB  . GLN A 248 ? 0.1369 0.1351 0.1184 0.0024  -0.0219 -0.0080 248 GLN A CB  
2130 C  CG  . GLN A 248 ? 0.1313 0.1211 0.1328 0.0097  -0.0092 0.0005  248 GLN A CG  
2131 C  CD  . GLN A 248 ? 0.1269 0.1572 0.1342 -0.0078 -0.0110 -0.0017 248 GLN A CD  
2132 O  OE1 . GLN A 248 ? 0.1368 0.1948 0.1763 -0.0115 -0.0005 -0.0414 248 GLN A OE1 
2133 N  NE2 . GLN A 248 ? 0.1525 0.1504 0.1409 -0.0035 -0.0060 -0.0097 248 GLN A NE2 
2134 N  N   . PRO A 249 ? 0.1454 0.1547 0.1333 0.0346  -0.0277 -0.0068 249 PRO A N   
2135 C  CA  . PRO A 249 ? 0.1538 0.1793 0.1179 0.0372  -0.0217 -0.0019 249 PRO A CA  
2136 C  C   . PRO A 249 ? 0.1326 0.1561 0.1179 0.0207  -0.0298 -0.0032 249 PRO A C   
2137 O  O   . PRO A 249 ? 0.1347 0.1563 0.1386 0.0168  -0.0282 0.0028  249 PRO A O   
2138 C  CB  . PRO A 249 ? 0.1743 0.2361 0.1685 0.0744  -0.0513 -0.0294 249 PRO A CB  
2139 C  CG  . PRO A 249 ? 0.1870 0.2723 0.1420 0.0013  -0.0297 -0.0093 249 PRO A CG  
2140 C  CD  . PRO A 249 ? 0.1303 0.2102 0.1380 0.0263  -0.0339 -0.0087 249 PRO A CD  
2141 N  N   . LEU A 250 ? 0.1723 0.1529 0.1190 0.0280  -0.0263 -0.0020 250 LEU A N   
2142 C  CA  . LEU A 250 ? 0.1893 0.1299 0.1270 0.0082  -0.0041 -0.0041 250 LEU A CA  
2143 C  C   . LEU A 250 ? 0.1617 0.1411 0.1149 0.0204  -0.0309 0.0051  250 LEU A C   
2144 O  O   . LEU A 250 ? 0.1626 0.1405 0.1384 0.0261  -0.0425 -0.0054 250 LEU A O   
2145 C  CB  . LEU A 250 ? 0.1777 0.1419 0.1565 -0.0013 -0.0012 0.0012  250 LEU A CB  
2146 C  CG  . LEU A 250 ? 0.1687 0.1923 0.1502 -0.0219 0.0020  -0.0185 250 LEU A CG  
2147 C  CD1 . LEU A 250 ? 0.1574 0.1956 0.1556 -0.0043 -0.0203 -0.0399 250 LEU A CD1 
2148 C  CD2 . LEU A 250 ? 0.2680 0.2114 0.2324 -0.0494 0.0450  -0.0098 250 LEU A CD2 
2149 N  N   . LYS A 251 ? 0.1716 0.1472 0.1274 0.0524  -0.0432 -0.0110 251 LYS A N   
2150 C  CA  . LYS A 251 ? 0.1827 0.1592 0.1393 0.0397  -0.0482 -0.0223 251 LYS A CA  
2151 C  C   . LYS A 251 ? 0.2134 0.2160 0.1781 0.0200  -0.0535 -0.0071 251 LYS A C   
2152 O  O   . LYS A 251 ? 0.2669 0.2572 0.1586 -0.0248 -0.0083 -0.0335 251 LYS A O   
2153 C  CB  . LYS A 251 ? 0.1908 0.1960 0.1978 0.0071  -0.0627 -0.0252 251 LYS A CB  
2154 C  CG  . LYS A 251 ? 0.3224 0.2585 0.2378 -0.0143 0.0873  -0.0604 251 LYS A CG  
2155 C  CD  . LYS A 251 ? 0.2992 0.2705 0.2460 -0.0436 0.0491  -0.0680 251 LYS A CD  
2156 C  CE  . LYS A 251 ? 0.2615 0.3098 0.3770 0.0152  0.0304  0.0217  251 LYS A CE  
2157 N  NZ  . LYS A 251 ? 0.2104 0.4140 0.4442 0.0337  0.0483  0.0392  251 LYS A NZ  
2158 N  N   . ASN A 252 ? 0.1989 0.2116 0.1606 0.0333  -0.0621 -0.0511 252 ASN A N   
2159 C  CA  . ASN A 252 ? 0.1926 0.3111 0.1920 0.0379  -0.0236 -0.0706 252 ASN A CA  
2160 C  C   . ASN A 252 ? 0.2469 0.2802 0.2080 0.0520  -0.0397 -0.0467 252 ASN A C   
2161 O  O   . ASN A 252 ? 0.2834 0.2971 0.2667 0.0445  -0.0350 -0.0430 252 ASN A O   
2162 C  CB  . ASN A 252 ? 0.3738 0.4140 0.2109 -0.0051 -0.0230 -0.1557 252 ASN A CB  
2163 C  CG  . ASN A 252 ? 0.4548 0.3745 0.3779 0.0788  0.1042  -0.0705 252 ASN A CG  
2164 O  OD1 . ASN A 252 ? 0.5302 0.5149 0.2694 -0.1019 0.0807  -0.1010 252 ASN A OD1 
2165 N  ND2 . ASN A 252 ? 0.3529 0.3919 0.6319 0.0272  -0.1064 -0.2159 252 ASN A ND2 
2166 N  N   . ARG A 253 ? 0.1987 0.2673 0.1281 0.0280  -0.0244 0.0266  253 ARG A N   
2167 C  CA  . ARG A 253 ? 0.1486 0.1721 0.1206 0.0236  -0.0099 -0.0051 253 ARG A CA  
2168 C  C   . ARG A 253 ? 0.1615 0.1559 0.1199 0.0137  -0.0168 -0.0060 253 ARG A C   
2169 O  O   . ARG A 253 ? 0.2247 0.2050 0.2373 0.0538  0.0821  0.0511  253 ARG A O   
2170 C  CB  . ARG A 253 ? 0.1606 0.1592 0.1106 0.0138  -0.0019 -0.0146 253 ARG A CB  
2171 C  CG  . ARG A 253 ? 0.1572 0.1488 0.1145 0.0143  -0.0198 -0.0222 253 ARG A CG  
2172 C  CD  . ARG A 253 ? 0.1786 0.1136 0.1041 0.0080  -0.0021 -0.0313 253 ARG A CD  
2173 N  NE  . ARG A 253 ? 0.1421 0.1116 0.1053 0.0037  -0.0221 -0.0013 253 ARG A NE  
2174 C  CZ  . ARG A 253 ? 0.0973 0.1211 0.0983 -0.0115 -0.0131 -0.0148 253 ARG A CZ  
2175 N  NH1 . ARG A 253 ? 0.1246 0.1089 0.1076 -0.0024 -0.0218 -0.0007 253 ARG A NH1 
2176 N  NH2 . ARG A 253 ? 0.1084 0.1100 0.1120 0.0049  -0.0240 -0.0120 253 ARG A NH2 
2177 N  N   . GLN A 254 ? 0.1653 0.1906 0.1303 0.0000  -0.0006 -0.0318 254 GLN A N   
2178 C  CA  . GLN A 254 ? 0.1876 0.2177 0.1100 -0.0103 -0.0026 -0.0313 254 GLN A CA  
2179 C  C   . GLN A 254 ? 0.1748 0.1710 0.1344 0.0052  -0.0195 0.0052  254 GLN A C   
2180 O  O   . GLN A 254 ? 0.2211 0.1525 0.1928 -0.0136 -0.0220 -0.0170 254 GLN A O   
2181 C  CB  . GLN A 254 ? 0.2165 0.3930 0.1641 -0.0452 0.0324  -0.1296 254 GLN A CB  
2182 C  CG  . GLN A 254 ? 0.3063 0.5837 0.2174 0.0182  0.0819  -0.1589 254 GLN A CG  
2183 C  CD  . GLN A 254 ? 0.6201 0.9592 0.4875 -0.1256 0.0777  0.1636  254 GLN A CD  
2184 O  OE1 . GLN A 254 ? 1.0058 1.0518 0.8713 -0.0913 -0.0848 -0.3224 254 GLN A OE1 
2185 N  NE2 . GLN A 254 ? 0.5246 0.9585 0.6952 0.3296  0.0005  -0.3459 254 GLN A NE2 
2186 N  N   . ILE A 255 ? 0.1310 0.1547 0.1054 0.0115  -0.0111 -0.0027 255 ILE A N   
2187 C  CA  . ILE A 255 ? 0.1328 0.1281 0.1054 0.0143  -0.0044 -0.0006 255 ILE A CA  
2188 C  C   . ILE A 255 ? 0.1434 0.1200 0.1145 0.0005  0.0082  -0.0012 255 ILE A C   
2189 O  O   . ILE A 255 ? 0.1671 0.1736 0.1274 0.0076  0.0157  0.0320  255 ILE A O   
2190 C  CB  . ILE A 255 ? 0.1280 0.1493 0.1100 0.0188  0.0020  -0.0233 255 ILE A CB  
2191 C  CG1 . ILE A 255 ? 0.1384 0.1269 0.1396 0.0103  0.0051  -0.0146 255 ILE A CG1 
2192 C  CG2 . ILE A 255 ? 0.1486 0.1942 0.1159 0.0111  -0.0148 -0.0254 255 ILE A CG2 
2193 C  CD1 . ILE A 255 ? 0.1685 0.1420 0.1606 0.0031  0.0141  -0.0362 255 ILE A CD1 
2194 N  N   . LYS A 256 ? 0.1200 0.1378 0.0927 0.0015  0.0052  -0.0048 256 LYS A N   
2195 C  CA  . LYS A 256 ? 0.1292 0.1416 0.1067 0.0060  0.0119  -0.0099 256 LYS A CA  
2196 C  C   . LYS A 256 ? 0.1382 0.1439 0.0965 -0.0148 0.0085  0.0043  256 LYS A C   
2197 O  O   . LYS A 256 ? 0.1614 0.1870 0.0953 -0.0317 0.0142  0.0048  256 LYS A O   
2198 C  CB  . LYS A 256 ? 0.1626 0.1581 0.1416 0.0031  0.0335  -0.0265 256 LYS A CB  
2199 C  CG  . LYS A 256 ? 0.2242 0.1971 0.1552 -0.0379 0.0577  -0.0346 256 LYS A CG  
2200 C  CD  . LYS A 256 ? 0.3386 0.2506 0.3079 -0.0452 0.0939  -0.1191 256 LYS A CD  
2201 C  CE  . LYS A 256 ? 0.5080 0.4881 0.4255 -0.0976 0.0707  -0.2572 256 LYS A CE  
2202 N  NZ  . LYS A 256 ? 0.4580 0.4077 0.8019 -0.1803 0.2626  -0.3213 256 LYS A NZ  
2203 N  N   . ALA A 257 ? 0.1274 0.1709 0.1109 -0.0154 0.0253  0.0005  257 ALA A N   
2204 C  CA  . ALA A 257 ? 0.1295 0.1757 0.1386 -0.0287 0.0307  -0.0137 257 ALA A CA  
2205 C  C   . ALA A 257 ? 0.1154 0.1811 0.1206 -0.0300 0.0331  -0.0136 257 ALA A C   
2206 O  O   . ALA A 257 ? 0.1678 0.1903 0.1242 -0.0206 0.0383  -0.0331 257 ALA A O   
2207 C  CB  . ALA A 257 ? 0.1552 0.1775 0.1520 -0.0423 0.0250  -0.0003 257 ALA A CB  
2208 N  N   . SER A 258 ? 0.1228 0.1565 0.1238 -0.0136 0.0156  0.0005  258 SER A N   
2209 C  CA  . SER A 258 ? 0.1353 0.1784 0.1452 -0.0043 0.0339  -0.0023 258 SER A CA  
2210 C  C   . SER A 258 ? 0.1444 0.2060 0.1366 -0.0153 0.0447  -0.0073 258 SER A C   
2211 O  O   . SER A 258 ? 0.1274 0.2806 0.2158 -0.0188 0.0491  -0.0017 258 SER A O   
2212 C  CB  . SER A 258 ? 0.1389 0.1689 0.1594 0.0007  0.0080  0.0130  258 SER A CB  
2213 O  OG  . SER A 258 ? 0.1134 0.1888 0.1326 -0.0088 0.0221  -0.0044 258 SER A OG  
2214 N  N   . PHE A 259 ? 0.1349 0.2046 0.1547 -0.0175 0.0366  -0.0051 259 PHE A N   
2215 C  CA  . PHE A 259 ? 0.1741 0.2160 0.1885 -0.0502 0.0116  0.0203  259 PHE A CA  
2216 C  C   . PHE A 259 ? 0.2504 0.3208 0.1948 -0.0847 0.0297  0.0701  259 PHE A C   
2217 O  O   . PHE A 259 ? 0.3001 0.2949 0.1960 -0.0767 -0.0060 0.0619  259 PHE A O   
2218 C  CB  . PHE A 259 ? 0.1732 0.2386 0.2185 -0.0417 0.0253  -0.0165 259 PHE A CB  
2219 C  CG  . PHE A 259 ? 0.1531 0.1879 0.1649 -0.0208 -0.0038 0.0201  259 PHE A CG  
2220 C  CD1 . PHE A 259 ? 0.1736 0.1910 0.1547 -0.0392 0.0032  -0.0195 259 PHE A CD1 
2221 C  CD2 . PHE A 259 ? 0.2224 0.2292 0.2615 -0.0077 0.0417  0.0322  259 PHE A CD2 
2222 C  CE1 . PHE A 259 ? 0.1861 0.2215 0.2050 -0.0282 -0.0027 -0.0419 259 PHE A CE1 
2223 C  CE2 . PHE A 259 ? 0.2402 0.2450 0.3431 -0.0026 0.0182  0.0269  259 PHE A CE2 
2224 C  CZ  . PHE A 259 ? 0.2230 0.2357 0.2876 0.0046  0.0408  -0.0074 259 PHE A CZ  
2225 N  N   . LYS A 260 ? 0.3470 0.3804 0.2287 -0.1292 0.1041  0.0509  260 LYS A N   
2226 C  CA  . LYS A 260 ? 0.4444 0.4931 0.3274 -0.0013 0.1947  0.1546  260 LYS A CA  
2227 C  C   . LYS A 260 ? 0.4856 0.7390 0.3467 -0.0653 0.0728  0.2126  260 LYS A C   
2228 O  O   . LYS A 260 ? 0.5496 1.0575 0.9842 -0.0031 -0.1456 0.6812  260 LYS A O   
2229 C  CB  . LYS A 260 ? 0.5830 0.4095 0.4277 0.0395  0.0767  0.2056  260 LYS A CB  
2230 C  CG  . LYS A 260 ? 0.4365 0.5637 0.6999 -0.2151 0.1359  0.1932  260 LYS A CG  
2231 C  CD  . LYS A 260 ? 0.5971 0.5921 0.6252 -0.0125 0.0553  0.3802  260 LYS A CD  
2232 C  CE  . LYS A 260 ? 1.0372 0.9175 1.2875 0.4422  -0.4546 0.3323  260 LYS A CE  
2233 N  NZ  . LYS A 260 ? 1.3315 0.8482 1.0663 0.1957  0.4548  0.7612  260 LYS A NZ  
2234 O  OXT . LYS A 260 ? 0.4918 0.6949 0.9228 -0.0670 0.1142  -0.0762 260 LYS A OXT 
2235 ZN ZN  . ZN  B .   ? 0.1159 0.0863 0.0904 -0.0093 -0.0074 0.0000  301 ZN  A ZN  
2236 S  S   . DMS C .   ? 0.2215 0.2700 0.2520 -0.0096 0.0228  -0.0318 302 DMS A S   
2237 O  O   . DMS C .   ? 0.4241 0.2529 0.3750 0.0362  0.0927  -0.0993 302 DMS A O   
2238 C  C1  . DMS C .   ? 0.2172 0.2540 0.1752 -0.0003 0.0234  -0.0340 302 DMS A C1  
2239 C  C2  . DMS C .   ? 0.2037 0.2797 0.3172 -0.0219 0.0161  -0.0340 302 DMS A C2  
2240 N  N1  . BCN D .   ? 0.4629 0.5116 0.4849 0.0245  -0.0086 -0.1719 303 BCN A N1  
2241 C  C1  . BCN D .   ? 0.2718 0.2037 0.3684 -0.0663 0.0568  0.0057  303 BCN A C1  
2242 C  C2  . BCN D .   ? 0.7282 0.7006 0.5734 -0.2280 -0.0186 -0.1656 303 BCN A C2  
2243 O  O21 . BCN D .   ? 0.7642 1.6714 1.2101 -0.2791 0.3957  -0.0606 303 BCN A O21 
2244 O  O22 . BCN D .   ? 0.7906 0.4483 0.7013 -0.1333 0.1673  0.1554  303 BCN A O22 
2245 C  C3  . BCN D .   ? 0.2346 0.4900 0.3867 -0.0636 -0.0151 0.0494  303 BCN A C3  
2246 C  C4  . BCN D .   ? 0.4260 0.6759 0.3147 0.0073  0.0417  0.0225  303 BCN A C4  
2247 O  O4  . BCN D .   ? 0.6762 0.7789 0.4194 0.2542  -0.0217 -0.0560 303 BCN A O4  
2248 C  C5  . BCN D .   ? 0.3021 0.3431 0.4045 -0.1146 0.0719  0.0697  303 BCN A C5  
2249 C  C6  . BCN D .   ? 0.6024 0.4607 0.6057 0.1154  0.0984  -0.1538 303 BCN A C6  
2250 O  O6  . BCN D .   ? 0.3713 0.3391 0.5246 -0.1032 0.1365  -0.0436 303 BCN A O6  
2251 F  F18 . V90 E .   ? 0.4767 0.3248 0.2472 0.0623  -0.0355 0.0430  304 V90 A F18 
2252 C  C5  . V90 E .   ? 0.4180 0.3073 0.1199 -0.0947 -0.0065 0.0476  304 V90 A C5  
2253 C  C6  . V90 E .   ? 0.4864 0.3079 0.1531 -0.0094 -0.0847 -0.0430 304 V90 A C6  
2254 S  S12 . V90 E .   ? 0.4444 0.3971 0.1958 -0.0348 -0.0153 -0.0359 304 V90 A S12 
2255 C  C13 . V90 E .   ? 0.3222 0.3249 0.3725 -0.0878 0.0623  0.0087  304 V90 A C13 
2256 C  C14 . V90 E .   ? 0.4230 0.3982 0.4097 -0.1301 -0.0983 0.0355  304 V90 A C14 
2257 O  O15 . V90 E .   ? 0.9846 0.5029 0.6802 -0.2280 0.2018  0.1425  304 V90 A O15 
2258 C  C1  . V90 E .   ? 0.4938 0.3517 0.1459 0.0516  -0.0441 -0.0320 304 V90 A C1  
2259 F  F17 . V90 E .   ? 0.4192 0.2558 0.3133 -0.0304 0.0467  -0.0553 304 V90 A F17 
2260 C  C4  . V90 E .   ? 0.2885 0.2653 0.1743 -0.0234 -0.0267 0.0256  304 V90 A C4  
2261 C  C3  . V90 E .   ? 0.3452 0.2673 0.1992 -0.0082 -0.1177 0.0167  304 V90 A C3  
2262 S  S8  . V90 E .   ? 0.2996 0.2125 0.2308 -0.0129 -0.0474 -0.0196 304 V90 A S8  
2263 O  O10 . V90 E .   ? 0.2186 0.2527 0.3806 0.0441  -0.0215 0.0041  304 V90 A O10 
2264 N  N11 . V90 E .   ? 0.2469 0.1362 0.2452 -0.0606 -0.1036 0.0644  304 V90 A N11 
2265 O  O9  . V90 E .   ? 0.2748 0.1850 0.1687 -0.0425 -0.0515 -0.0186 304 V90 A O9  
2266 C  C2  . V90 E .   ? 0.1454 0.3634 0.1813 -0.0155 0.0173  -0.0549 304 V90 A C2  
2267 F  F16 . V90 E .   ? 0.4863 0.2323 0.2423 0.0024  -0.0923 -0.0085 304 V90 A F16 
2268 N  N7  . V90 E .   ? 0.3059 0.1923 0.3201 -0.0277 -0.0549 0.0615  304 V90 A N7  
2269 C  C19 . V90 E .   ? 0.3034 0.2737 0.6783 -0.0419 -0.0575 -0.0283 304 V90 A C19 
2270 C  C26 . V90 E .   ? 0.2856 0.3943 0.3759 -0.1129 -0.0619 0.0208  304 V90 A C26 
2271 C  C25 . V90 E .   ? 0.4770 0.2734 0.4905 -0.0381 0.0491  0.0482  304 V90 A C25 
2272 C  C24 . V90 E .   ? 0.5020 0.2781 0.4404 -0.0306 0.0082  0.0001  304 V90 A C24 
2273 C  C23 . V90 E .   ? 0.3826 0.5473 0.5126 -0.0052 0.0092  0.1138  304 V90 A C23 
2274 C  C22 . V90 E .   ? 0.3772 0.3057 0.4954 -0.0364 0.0954  0.0197  304 V90 A C22 
2275 C  C21 . V90 E .   ? 0.3824 0.3691 0.3655 -0.1396 0.1665  -0.1759 304 V90 A C21 
2276 C  C20 . V90 E .   ? 0.3023 0.2824 0.3677 0.0148  0.0439  -0.0355 304 V90 A C20 
2277 O  O   . HOH F .   ? 0.1221 0.1220 0.1040 -0.0105 0.0129  -0.0065 401 HOH A O   
2278 O  O   . HOH F .   ? 0.2045 0.2030 0.2424 -0.0083 -0.0914 -0.0544 402 HOH A O   
2279 O  O   . HOH F .   ? 0.1182 0.1315 0.1242 -0.0126 0.0286  -0.0153 403 HOH A O   
2280 O  O   . HOH F .   ? 0.0915 0.2064 0.2020 0.0115  0.0088  -0.0348 404 HOH A O   
2281 O  O   . HOH F .   ? 0.1254 0.1136 0.1364 0.0131  -0.0074 -0.0063 405 HOH A O   
2282 O  O   . HOH F .   ? 0.1299 0.1068 0.1212 0.0076  -0.0026 -0.0151 406 HOH A O   
2283 O  O   . HOH F .   ? 0.1335 0.1290 0.1075 0.0285  -0.0007 -0.0062 407 HOH A O   
2284 O  O   . HOH F .   ? 0.1896 0.1319 0.1565 -0.0137 0.0063  0.0041  408 HOH A O   
2285 O  O   . HOH F .   ? 0.1283 0.1531 0.1290 0.0097  -0.0255 0.0207  409 HOH A O   
2286 O  O   . HOH F .   ? 0.1462 0.1233 0.1271 -0.0081 0.0181  -0.0163 410 HOH A O   
2287 O  O   . HOH F .   ? 0.1513 0.1312 0.1450 0.0342  -0.0118 0.0131  411 HOH A O   
2288 O  O   . HOH F .   ? 0.1360 0.1132 0.1493 -0.0020 0.0034  -0.0088 412 HOH A O   
2289 O  O   . HOH F .   ? 0.1788 0.1511 0.1671 0.0208  0.0048  0.0164  413 HOH A O   
2290 O  O   . HOH F .   ? 0.2545 0.1100 0.2196 0.0288  0.0037  -0.0188 414 HOH A O   
2291 O  O   . HOH F .   ? 0.1315 0.2016 0.2824 -0.0320 -0.0049 -0.0165 415 HOH A O   
2292 O  O   . HOH F .   ? 0.1947 0.1606 0.1745 0.0285  0.0070  0.0184  416 HOH A O   
2293 O  O   . HOH F .   ? 0.1132 0.1732 0.1942 -0.0015 -0.0010 -0.0537 417 HOH A O   
2294 O  O   . HOH F .   ? 0.2985 0.3587 0.2275 0.1322  -0.0518 -0.0059 418 HOH A O   
2295 O  O   . HOH F .   ? 0.3287 0.1896 0.2687 0.0485  0.0280  0.0399  419 HOH A O   
2296 O  O   . HOH F .   ? 0.1910 0.3393 0.2669 0.0612  -0.0273 0.0005  420 HOH A O   
2297 O  O   . HOH F .   ? 0.1493 0.1766 0.2210 -0.0024 0.0028  0.0060  421 HOH A O   
2298 O  O   . HOH F .   ? 0.3889 0.3583 0.2395 0.0068  0.0322  0.1247  422 HOH A O   
2299 O  O   . HOH F .   ? 0.1718 0.1454 0.1757 -0.0126 0.0203  -0.0130 423 HOH A O   
2300 O  O   . HOH F .   ? 0.4293 0.2572 0.2285 0.0693  -0.1270 0.0373  424 HOH A O   
2301 O  O   . HOH F .   ? 0.2078 0.1109 0.1662 -0.0197 -0.0091 -0.0046 425 HOH A O   
2302 O  O   . HOH F .   ? 0.1735 0.1628 0.2093 -0.0046 -0.0410 -0.0509 426 HOH A O   
2303 O  O   . HOH F .   ? 0.1396 0.2057 0.1835 -0.0104 -0.0582 0.0443  427 HOH A O   
2304 O  O   . HOH F .   ? 0.2069 0.1215 0.1721 -0.0133 0.0103  0.0063  428 HOH A O   
2305 O  O   . HOH F .   ? 0.1813 0.2142 0.2078 0.0266  0.0425  -0.0307 429 HOH A O   
2306 O  O   . HOH F .   ? 0.2953 0.2497 0.2517 0.0727  -0.0670 -0.0516 430 HOH A O   
2307 O  O   . HOH F .   ? 0.2908 0.1965 0.2195 0.0245  -0.0452 0.0286  431 HOH A O   
2308 O  O   . HOH F .   ? 0.2937 0.1364 0.3147 -0.0173 0.0870  0.0082  432 HOH A O   
2309 O  O   . HOH F .   ? 0.4368 0.3127 0.2160 -0.0032 -0.1094 0.0003  433 HOH A O   
2310 O  O   . HOH F .   ? 0.2680 0.2213 0.2032 0.0174  -0.0346 -0.0715 434 HOH A O   
2311 O  O   . HOH F .   ? 0.3878 0.2421 0.1795 0.0798  0.0277  -0.0008 435 HOH A O   
2312 O  O   . HOH F .   ? 0.2549 0.1480 0.2028 0.0223  -0.0282 0.0040  436 HOH A O   
2313 O  O   . HOH F .   ? 0.2041 0.2305 0.2752 0.0619  -0.0373 -0.0208 437 HOH A O   
2314 O  O   . HOH F .   ? 0.4878 0.3783 0.1197 -0.0483 0.0015  -0.0041 438 HOH A O   
2315 O  O   . HOH F .   ? 0.3948 0.3016 0.5461 0.0324  -0.1679 -0.0491 439 HOH A O   
2316 O  O   . HOH F .   ? 0.3048 0.2831 0.4419 0.1017  0.0115  0.0401  440 HOH A O   
2317 O  O   . HOH F .   ? 0.2037 0.2233 0.3625 -0.0511 -0.0071 0.0377  441 HOH A O   
2318 O  O   . HOH F .   ? 0.2111 0.3194 0.2497 0.0421  0.0775  -0.0186 442 HOH A O   
2319 O  O   . HOH F .   ? 0.1902 0.2346 0.2224 0.0649  -0.0507 0.0087  443 HOH A O   
2320 O  O   . HOH F .   ? 0.2955 0.1905 0.2301 -0.0784 0.0161  -0.0496 444 HOH A O   
2321 O  O   . HOH F .   ? 0.3064 0.1906 0.2143 -0.0754 -0.0697 -0.0135 445 HOH A O   
2322 O  O   . HOH F .   ? 0.3583 0.1818 0.3133 0.0581  -0.0575 -0.0027 446 HOH A O   
2323 O  O   . HOH F .   ? 0.2615 0.1856 0.2149 0.0146  -0.0204 0.0199  447 HOH A O   
2324 O  O   . HOH F .   ? 0.2122 0.2157 0.1887 0.0176  -0.0259 -0.0310 448 HOH A O   
2325 O  O   . HOH F .   ? 0.3050 0.3526 0.5220 -0.0635 0.0130  0.0291  449 HOH A O   
2326 O  O   . HOH F .   ? 0.2768 0.2345 0.2894 0.0753  -0.1371 -0.0175 450 HOH A O   
2327 O  O   . HOH F .   ? 0.1525 0.3625 0.3240 -0.0151 -0.0089 0.0020  451 HOH A O   
2328 O  O   . HOH F .   ? 0.2784 0.2179 0.2235 0.0242  0.0212  0.1049  452 HOH A O   
2329 O  O   . HOH F .   ? 0.1691 0.1790 0.2764 -0.0461 0.0060  -0.0100 453 HOH A O   
2330 O  O   . HOH F .   ? 0.2732 0.2255 0.3531 -0.0637 0.1058  -0.0110 454 HOH A O   
2331 O  O   . HOH F .   ? 0.1368 0.1716 0.2088 -0.0428 -0.0146 -0.0286 455 HOH A O   
2332 O  O   . HOH F .   ? 0.3759 0.2452 0.1493 -0.0087 0.0007  -0.0055 456 HOH A O   
2333 O  O   . HOH F .   ? 0.2339 0.4041 0.3219 0.0632  0.0617  0.1221  457 HOH A O   
2334 O  O   . HOH F .   ? 0.4111 0.1944 0.2269 0.0692  -0.1291 0.0324  458 HOH A O   
2335 O  O   . HOH F .   ? 0.2766 0.2933 0.4370 -0.0189 -0.0264 0.0693  459 HOH A O   
2336 O  O   . HOH F .   ? 0.4180 0.2063 0.2294 0.0274  -0.1235 -0.0292 460 HOH A O   
2337 O  O   . HOH F .   ? 0.4896 0.4539 0.1477 -0.0074 0.0320  0.0450  461 HOH A O   
2338 O  O   . HOH F .   ? 0.2298 0.2635 0.1680 -0.0114 0.0041  -0.0423 462 HOH A O   
2339 O  O   . HOH F .   ? 0.2569 0.3183 0.2551 -0.0260 -0.0027 -0.0675 463 HOH A O   
2340 O  O   . HOH F .   ? 0.3926 0.1872 0.1872 -0.0608 0.0054  0.0505  464 HOH A O   
2341 O  O   . HOH F .   ? 0.3048 0.2637 0.2439 0.0340  -0.0684 0.0458  465 HOH A O   
2342 O  O   . HOH F .   ? 0.3201 0.2917 0.2061 0.1222  -0.0359 0.0286  466 HOH A O   
2343 O  O   . HOH F .   ? 0.3061 0.2714 0.2924 -0.0595 -0.0034 -0.0913 467 HOH A O   
2344 O  O   . HOH F .   ? 0.1985 0.1931 0.1721 -0.0167 -0.0162 0.0013  468 HOH A O   
2345 O  O   . HOH F .   ? 0.2545 0.2019 0.1387 0.0035  -0.0038 -0.0141 469 HOH A O   
2346 O  O   . HOH F .   ? 0.2924 0.1762 0.2662 -0.0317 -0.0467 0.0326  470 HOH A O   
2347 O  O   . HOH F .   ? 0.3186 0.2949 0.3666 -0.0164 -0.0223 -0.0498 471 HOH A O   
2348 O  O   . HOH F .   ? 0.2694 0.2188 0.2339 0.0114  0.0089  0.0397  472 HOH A O   
2349 O  O   . HOH F .   ? 0.5242 0.3312 0.2023 0.0388  0.0785  0.0130  473 HOH A O   
2350 O  O   . HOH F .   ? 0.2431 0.4077 0.1532 0.1159  -0.0656 0.0046  474 HOH A O   
2351 O  O   . HOH F .   ? 0.4842 0.3892 0.3152 -0.0847 -0.1820 -0.0104 475 HOH A O   
2352 O  O   . HOH F .   ? 0.3368 0.3528 0.3743 -0.0952 0.1050  -0.1136 476 HOH A O   
2353 O  O   . HOH F .   ? 0.4189 0.3255 0.3424 -0.1282 0.1393  -0.1444 477 HOH A O   
2354 O  O   . HOH F .   ? 0.1939 0.1635 0.3111 -0.0038 0.0421  -0.0394 478 HOH A O   
2355 O  O   . HOH F .   ? 0.1588 0.3519 0.1721 0.0037  0.0324  -0.0381 479 HOH A O   
2356 O  O   . HOH F .   ? 0.2840 0.1446 0.1809 0.0434  -0.0337 -0.0126 480 HOH A O   
2357 O  O   . HOH F .   ? 0.2617 0.4438 0.3179 0.0478  0.0054  0.1498  481 HOH A O   
2358 O  O   . HOH F .   ? 0.2179 0.2197 0.2066 0.0151  0.0518  -0.0238 482 HOH A O   
2359 O  O   . HOH F .   ? 0.2082 0.2093 0.3287 0.0175  0.0115  -0.0328 483 HOH A O   
2360 O  O   . HOH F .   ? 0.6104 0.4280 0.1973 -0.2380 0.0390  -0.0443 484 HOH A O   
2361 O  O   . HOH F .   ? 0.2651 0.3474 0.4564 0.0209  0.0927  0.1252  485 HOH A O   
2362 O  O   . HOH F .   ? 0.2097 0.2091 0.2820 0.0379  0.0502  0.0333  486 HOH A O   
2363 O  O   . HOH F .   ? 0.2851 0.2948 0.2658 0.0732  0.0847  -0.0093 487 HOH A O   
2364 O  O   . HOH F .   ? 0.3309 0.2529 0.4041 -0.0487 -0.0366 -0.0653 488 HOH A O   
2365 O  O   . HOH F .   ? 0.2422 0.2156 0.2079 0.0003  -0.0221 0.0759  489 HOH A O   
2366 O  O   . HOH F .   ? 0.3779 0.3217 0.2212 -0.0996 0.1023  -0.0973 490 HOH A O   
2367 O  O   . HOH F .   ? 0.2524 0.2254 0.2544 0.0252  -0.0282 -0.0052 491 HOH A O   
2368 O  O   . HOH F .   ? 0.2903 0.2957 0.3427 0.1186  -0.0740 0.0452  492 HOH A O   
2369 O  O   . HOH F .   ? 0.3111 0.3160 0.2915 0.0113  0.0878  -0.1198 493 HOH A O   
2370 O  O   . HOH F .   ? 0.3427 0.5228 0.7069 0.0790  0.2152  0.0421  494 HOH A O   
2371 O  O   . HOH F .   ? 0.4435 0.2352 0.1971 -0.0318 -0.0399 -0.0231 495 HOH A O   
2372 O  O   . HOH F .   ? 0.2872 0.1536 0.2089 -0.0288 0.0078  0.0157  496 HOH A O   
2373 O  O   . HOH F .   ? 0.2978 0.2930 0.3172 0.0838  0.0727  0.0024  497 HOH A O   
2374 O  O   . HOH F .   ? 0.1613 0.3093 0.3140 0.0640  0.0644  0.0227  498 HOH A O   
2375 O  O   . HOH F .   ? 0.3170 0.3118 0.2213 -0.0008 0.0500  -0.0958 499 HOH A O   
2376 O  O   . HOH F .   ? 0.2764 0.5318 0.5687 -0.0370 0.1523  -0.1754 500 HOH A O   
2377 O  O   . HOH F .   ? 0.3975 0.2416 0.2831 -0.0359 0.0372  -0.0142 501 HOH A O   
2378 O  O   . HOH F .   ? 0.2685 0.4065 0.2235 -0.0010 -0.0028 0.0000  502 HOH A O   
2379 O  O   . HOH F .   ? 0.5475 0.3950 0.1922 -0.1090 0.0456  0.1298  503 HOH A O   
2380 O  O   . HOH F .   ? 0.5691 0.7107 0.2910 -0.2522 0.0953  -0.0693 504 HOH A O   
2381 O  O   . HOH F .   ? 0.2475 0.1808 0.2484 -0.0073 -0.0320 0.0318  505 HOH A O   
2382 O  O   . HOH F .   ? 0.3273 0.2134 0.3310 -0.0001 0.0935  0.0167  506 HOH A O   
2383 O  O   . HOH F .   ? 0.2402 0.2307 0.3208 -0.0174 -0.0156 -0.0485 507 HOH A O   
2384 O  O   . HOH F .   ? 0.4907 0.4018 0.5476 -0.1040 0.1967  -0.1756 508 HOH A O   
2385 O  O   . HOH F .   ? 0.3686 0.1719 0.3639 0.0054  0.0175  -0.0798 509 HOH A O   
2386 O  O   . HOH F .   ? 0.3711 0.3398 0.3424 -0.0520 0.1437  -0.0331 510 HOH A O   
2387 O  O   . HOH F .   ? 0.3553 0.1809 0.3213 0.0315  -0.0013 0.0645  511 HOH A O   
2388 O  O   . HOH F .   ? 0.4550 0.3565 0.2635 0.1094  -0.0509 0.0436  512 HOH A O   
2389 O  O   . HOH F .   ? 0.3885 0.3456 0.2312 0.0623  0.0326  0.0615  513 HOH A O   
2390 O  O   . HOH F .   ? 0.4751 0.4097 0.4832 -0.0593 -0.1890 -0.1615 514 HOH A O   
2391 O  O   . HOH F .   ? 0.4853 0.2856 0.2915 -0.0588 -0.1138 -0.1001 515 HOH A O   
2392 O  O   . HOH F .   ? 0.3549 0.2272 0.2504 -0.0085 -0.0604 0.0216  516 HOH A O   
2393 O  O   . HOH F .   ? 0.6776 0.2037 0.3628 -0.0184 0.0537  0.0516  517 HOH A O   
2394 O  O   . HOH F .   ? 0.2413 0.2231 0.2203 -0.0342 -0.0361 -0.0019 518 HOH A O   
2395 O  O   . HOH F .   ? 0.3497 0.4068 0.3874 -0.0555 0.0073  0.1617  519 HOH A O   
2396 O  O   . HOH F .   ? 0.3515 0.3151 0.1975 0.0296  0.0430  -0.0456 520 HOH A O   
2397 O  O   . HOH F .   ? 0.2558 0.3411 0.3810 -0.0432 0.1509  0.0003  521 HOH A O   
2398 O  O   . HOH F .   ? 0.4361 0.2912 0.2389 -0.0952 0.0535  -0.0855 522 HOH A O   
2399 O  O   . HOH F .   ? 0.1958 0.3122 0.2427 -0.0353 -0.0238 0.0216  523 HOH A O   
2400 O  O   . HOH F .   ? 0.1693 0.3440 0.3815 -0.0153 -0.0232 -0.0452 524 HOH A O   
2401 O  O   . HOH F .   ? 0.4936 0.3770 0.2587 -0.0430 -0.0639 0.0610  525 HOH A O   
2402 O  O   . HOH F .   ? 0.6941 0.3235 0.1592 -0.0178 0.0469  0.0160  526 HOH A O   
2403 O  O   . HOH F .   ? 0.1938 0.3402 0.3285 0.0104  0.0478  -0.0155 527 HOH A O   
2404 O  O   . HOH F .   ? 0.2856 0.2556 0.2973 -0.0375 0.0000  -0.0666 528 HOH A O   
2405 O  O   . HOH F .   ? 0.1553 0.3842 0.4036 0.0586  0.0140  0.0764  529 HOH A O   
2406 O  O   . HOH F .   ? 0.2838 0.2782 0.3249 0.0575  -0.0531 -0.0115 530 HOH A O   
2407 O  O   . HOH F .   ? 0.4183 0.4239 0.2398 0.1661  0.0546  -0.0412 531 HOH A O   
2408 O  O   . HOH F .   ? 0.3046 0.5059 0.3634 -0.0531 -0.1225 0.0496  532 HOH A O   
2409 O  O   . HOH F .   ? 0.4063 0.3215 0.3454 0.0562  -0.0403 -0.0298 533 HOH A O   
2410 O  O   . HOH F .   ? 0.3682 0.3368 0.9591 -0.1296 -0.2764 0.1159  534 HOH A O   
2411 O  O   . HOH F .   ? 0.5388 0.3607 0.2953 0.1143  0.1366  -0.0877 535 HOH A O   
2412 O  O   . HOH F .   ? 0.5906 0.3765 0.2545 0.0403  0.0439  0.0381  536 HOH A O   
2413 O  O   . HOH F .   ? 0.4070 0.2660 0.2276 0.0399  -0.0172 0.0399  537 HOH A O   
2414 O  O   . HOH F .   ? 0.3646 0.2714 0.3580 0.0829  -0.0230 0.0205  538 HOH A O   
2415 O  O   . HOH F .   ? 1.0859 0.9910 0.1244 -0.1040 0.2313  0.1929  539 HOH A O   
2416 O  O   . HOH F .   ? 0.3546 0.3716 0.4429 0.0015  -0.0421 0.0320  540 HOH A O   
2417 O  O   . HOH F .   ? 0.3625 0.2700 0.2552 -0.0076 0.0199  0.0138  541 HOH A O   
2418 O  O   . HOH F .   ? 0.5554 0.6768 0.6310 -0.2971 0.0756  -0.0542 542 HOH A O   
2419 O  O   . HOH F .   ? 0.2964 0.4140 0.3763 -0.0661 0.0832  -0.0379 543 HOH A O   
2420 O  O   . HOH F .   ? 0.2858 0.6549 0.4758 0.0172  0.1572  0.1694  544 HOH A O   
2421 O  O   . HOH F .   ? 0.2930 0.3544 0.7570 0.0251  -0.0555 -0.0397 545 HOH A O   
2422 O  O   . HOH F .   ? 0.2500 0.4780 0.2610 -0.0612 -0.0776 0.0234  546 HOH A O   
2423 O  O   . HOH F .   ? 0.2178 0.3138 0.3847 0.0361  0.0738  0.0498  547 HOH A O   
2424 O  O   . HOH F .   ? 0.2619 0.3883 0.2989 -0.0766 0.0700  -0.1416 548 HOH A O   
2425 O  O   . HOH F .   ? 0.4641 0.3774 0.3109 0.0115  -0.0024 -0.1115 549 HOH A O   
2426 O  O   . HOH F .   ? 0.3032 0.5008 0.7134 0.1501  0.0608  0.1335  550 HOH A O   
2427 O  O   . HOH F .   ? 0.4442 0.3465 0.4120 -0.0081 0.1064  -0.1083 551 HOH A O   
2428 O  O   . HOH F .   ? 0.2142 0.3289 0.3111 -0.0208 0.0395  -0.0689 552 HOH A O   
2429 O  O   . HOH F .   ? 0.3433 0.2096 0.2942 -0.0348 -0.0304 -0.0621 553 HOH A O   
2430 O  O   . HOH F .   ? 0.2822 0.5006 0.3578 -0.1331 0.0491  0.0803  554 HOH A O   
2431 O  O   . HOH F .   ? 0.2903 0.3336 0.2982 0.0147  -0.0156 -0.1045 555 HOH A O   
2432 O  O   . HOH F .   ? 0.4526 0.6277 0.4230 -0.0008 -0.0697 0.3030  556 HOH A O   
2433 O  O   . HOH F .   ? 0.4025 0.2615 0.4712 0.0040  -0.1283 -0.0351 557 HOH A O   
2434 O  O   . HOH F .   ? 0.8956 0.2660 0.4318 -0.0307 0.2500  0.0282  558 HOH A O   
2435 O  O   . HOH F .   ? 0.2240 0.3472 0.2834 0.0077  -0.0194 -0.0329 559 HOH A O   
2436 O  O   . HOH F .   ? 0.2064 0.4989 0.4013 -0.0706 -0.0639 -0.0298 560 HOH A O   
2437 O  O   . HOH F .   ? 0.4675 0.2226 0.4165 0.1067  -0.0364 -0.0077 561 HOH A O   
2438 O  O   . HOH F .   ? 0.3361 0.2615 0.2606 -0.0419 -0.0262 0.0630  562 HOH A O   
2439 O  O   . HOH F .   ? 0.4974 0.2800 0.4445 -0.0516 0.1611  -0.0839 563 HOH A O   
2440 O  O   . HOH F .   ? 0.5254 0.3098 0.4537 0.0021  -0.1617 0.0819  564 HOH A O   
2441 O  O   . HOH F .   ? 0.3278 0.2752 0.5834 -0.0208 0.0702  0.0705  565 HOH A O   
2442 O  O   . HOH F .   ? 0.2594 0.3749 0.3707 0.0322  -0.0318 0.0109  566 HOH A O   
2443 O  O   . HOH F .   ? 0.3659 0.3695 0.6699 -0.0614 0.0127  -0.0329 567 HOH A O   
2444 O  O   . HOH F .   ? 0.6446 0.3727 0.4790 -0.0681 0.0270  -0.1024 568 HOH A O   
2445 O  O   . HOH F .   ? 0.3801 0.2838 0.7325 -0.0679 0.1045  -0.0328 569 HOH A O   
2446 O  O   . HOH F .   ? 0.2415 0.2820 0.2454 0.0260  -0.0335 0.0148  570 HOH A O   
2447 O  O   . HOH F .   ? 0.4481 0.3280 0.5807 0.0927  -0.2506 -0.0390 571 HOH A O   
2448 O  O   . HOH F .   ? 0.2632 0.1344 0.2978 -0.0283 -0.0249 -0.0137 572 HOH A O   
2449 O  O   . HOH F .   ? 0.4077 0.4788 0.2500 -0.0364 -0.1361 0.1483  573 HOH A O   
2450 O  O   . HOH F .   ? 0.3452 0.4004 0.4616 0.1756  -0.0962 -0.0917 574 HOH A O   
2451 O  O   . HOH F .   ? 0.2109 0.3686 0.2409 0.0619  -0.0043 0.0944  575 HOH A O   
2452 O  O   . HOH F .   ? 0.4097 0.3064 0.2536 -0.0657 0.0819  0.0489  576 HOH A O   
2453 O  O   . HOH F .   ? 0.3587 0.6434 0.3944 0.0522  0.1174  -0.0355 577 HOH A O   
2454 O  O   . HOH F .   ? 0.2858 0.5282 0.4198 -0.0868 0.0230  -0.1695 578 HOH A O   
2455 O  O   . HOH F .   ? 0.4408 0.4652 0.3720 0.1599  -0.1764 -0.1903 579 HOH A O   
2456 O  O   . HOH F .   ? 0.5508 0.4507 0.5212 0.0697  0.2361  -0.1615 580 HOH A O   
2457 O  O   . HOH F .   ? 1.0144 0.5400 0.3781 -0.1465 0.0315  -0.0197 581 HOH A O   
2458 O  O   . HOH F .   ? 0.1631 0.3874 0.5928 -0.0469 -0.0231 0.0188  582 HOH A O   
2459 O  O   . HOH F .   ? 0.7828 0.5939 0.7897 -0.3840 -0.0154 -0.2504 583 HOH A O   
2460 O  O   . HOH F .   ? 0.6226 0.3792 0.2649 -0.1721 0.0659  -0.0509 584 HOH A O   
2461 O  O   . HOH F .   ? 0.5192 0.3882 0.2939 -0.1014 -0.0485 -0.0434 585 HOH A O   
2462 O  O   . HOH F .   ? 0.2594 0.2461 0.1787 0.0146  0.0113  -0.0535 586 HOH A O   
2463 O  O   . HOH F .   ? 0.2843 0.2278 0.1838 -0.0469 0.0051  -0.0249 587 HOH A O   
2464 O  O   . HOH F .   ? 0.5236 0.6186 0.4503 -0.0313 0.2137  -0.0961 588 HOH A O   
2465 O  O   . HOH F .   ? 0.4269 0.6385 0.3980 0.2237  0.0104  0.1152  589 HOH A O   
2466 O  O   . HOH F .   ? 0.3375 0.4849 0.7027 -0.0144 0.0537  0.0913  590 HOH A O   
2467 O  O   . HOH F .   ? 0.3546 0.2276 0.4751 -0.0071 -0.0060 -0.0105 591 HOH A O   
2468 O  O   . HOH F .   ? 0.2996 0.2915 0.3145 -0.0089 0.0048  0.0219  592 HOH A O   
2469 O  O   . HOH F .   ? 0.3720 0.2822 0.4566 0.1099  -0.0006 -0.1037 593 HOH A O   
2470 O  O   . HOH F .   ? 0.2951 0.5857 0.6115 0.1252  0.1009  -0.0728 594 HOH A O   
2471 O  O   . HOH F .   ? 0.2053 0.5030 0.6499 -0.0277 -0.0751 0.0003  595 HOH A O   
2472 O  O   . HOH F .   ? 0.4435 0.5357 0.3811 -0.0351 0.0467  -0.0768 596 HOH A O   
2473 O  O   . HOH F .   ? 0.2109 0.5295 0.5390 -0.1412 -0.0873 0.0037  597 HOH A O   
2474 O  O   . HOH F .   ? 0.5806 0.3100 0.2635 0.0353  0.0041  -0.1459 598 HOH A O   
2475 O  O   . HOH F .   ? 0.3359 0.5295 0.5153 0.0531  0.1097  0.0741  599 HOH A O   
2476 O  O   . HOH F .   ? 0.3704 0.3657 0.4751 0.1544  0.0311  -0.0296 600 HOH A O   
2477 O  O   . HOH F .   ? 0.7513 0.8260 0.2066 -0.3431 -0.0428 -0.0766 601 HOH A O   
2478 O  O   . HOH F .   ? 0.3474 0.4878 0.2276 0.0811  -0.0177 0.0270  602 HOH A O   
2479 O  O   . HOH F .   ? 0.3264 0.2386 0.1596 0.0059  -0.0293 0.0165  603 HOH A O   
2480 O  O   . HOH F .   ? 0.5357 0.3907 0.3528 -0.0146 -0.1252 0.0007  604 HOH A O   
2481 O  O   . HOH F .   ? 0.3600 0.2827 0.3039 0.0149  0.0741  0.0643  605 HOH A O   
2482 O  O   . HOH F .   ? 0.2533 0.2707 0.1944 -0.0406 0.0443  0.0588  606 HOH A O   
2483 O  O   . HOH F .   ? 0.5726 0.3941 0.7469 -0.2228 -0.3503 0.2363  607 HOH A O   
2484 O  O   . HOH F .   ? 0.4020 0.4370 0.2515 0.0711  0.0109  0.0421  608 HOH A O   
2485 O  O   . HOH F .   ? 0.3449 0.4907 0.3352 -0.0820 -0.0239 -0.0379 609 HOH A O   
2486 O  O   . HOH F .   ? 0.2448 0.7074 0.2820 0.0747  0.0423  0.0934  610 HOH A O   
2487 O  O   . HOH F .   ? 0.3592 0.4203 0.3156 0.1400  0.1230  -0.0057 611 HOH A O   
2488 O  O   . HOH F .   ? 0.1316 0.3777 0.4977 0.0154  0.0294  -0.0527 612 HOH A O   
2489 O  O   . HOH F .   ? 0.1921 0.3610 0.5756 -0.0038 0.0135  0.0904  613 HOH A O   
2490 O  O   . HOH F .   ? 0.4009 0.3567 0.4228 0.1544  -0.0179 0.0571  614 HOH A O   
2491 O  O   . HOH F .   ? 0.5224 0.4618 0.2615 -0.0206 0.0091  -0.0991 615 HOH A O   
2492 O  O   . HOH F .   ? 0.4208 0.3614 0.3258 0.0903  -0.0799 -0.0848 616 HOH A O   
2493 O  O   . HOH F .   ? 0.2978 0.3648 0.2723 0.0307  0.0487  0.0008  617 HOH A O   
2494 O  O   . HOH F .   ? 0.3553 0.2500 0.3258 0.0035  -0.0960 0.0366  618 HOH A O   
2495 O  O   . HOH F .   ? 0.6442 0.2249 0.5212 0.1568  -0.0661 0.0432  619 HOH A O   
2496 O  O   . HOH F .   ? 0.2395 0.3014 0.4706 0.0155  -0.0515 0.0108  620 HOH A O   
2497 O  O   . HOH F .   ? 0.7903 0.3350 0.4946 -0.1923 0.0054  0.0716  621 HOH A O   
2498 O  O   . HOH F .   ? 0.5067 0.2657 0.4763 -0.0034 -0.0480 -0.0502 622 HOH A O   
2499 O  O   . HOH F .   ? 0.7516 0.3831 0.2779 0.1926  -0.1907 0.0866  623 HOH A O   
2500 O  O   . HOH F .   ? 0.5249 0.5731 0.4135 0.1893  -0.0904 0.1400  624 HOH A O   
2501 O  O   . HOH F .   ? 0.9312 0.6999 0.9039 0.0265  0.0472  0.4147  625 HOH A O   
2502 O  O   . HOH F .   ? 0.3630 0.4652 0.3688 -0.0579 0.1597  0.0086  626 HOH A O   
2503 O  O   . HOH F .   ? 0.4928 0.3605 0.3271 -0.0021 -0.1049 0.1050  627 HOH A O   
2504 O  O   . HOH F .   ? 0.4560 0.2976 0.6980 -0.0549 -0.1765 0.0208  628 HOH A O   
2505 O  O   . HOH F .   ? 0.5892 0.5248 0.5098 -0.0006 -0.1159 -0.1608 629 HOH A O   
2506 O  O   . HOH F .   ? 0.5432 0.4384 0.3551 0.0947  0.0416  -0.1439 630 HOH A O   
2507 O  O   . HOH F .   ? 0.4106 0.3668 0.7258 0.0728  0.0077  -0.0340 631 HOH A O   
2508 O  O   . HOH F .   ? 0.2851 0.1924 0.4765 0.0153  -0.0489 -0.0120 632 HOH A O   
2509 O  O   . HOH F .   ? 0.2664 0.2415 0.3312 0.0436  -0.0020 -0.0408 633 HOH A O   
2510 O  O   . HOH F .   ? 0.5138 0.1615 0.3513 -0.0287 -0.0046 -0.0175 634 HOH A O   
2511 O  O   . HOH F .   ? 0.3522 0.1951 0.3582 0.0304  -0.0568 -0.0026 635 HOH A O   
2512 O  O   . HOH F .   ? 0.2856 0.3567 0.3456 -0.0133 -0.0608 0.0005  636 HOH A O   
2513 O  O   . HOH F .   ? 0.4011 0.3610 0.7271 -0.0487 0.1251  0.1439  637 HOH A O   
2514 O  O   . HOH F .   ? 0.3549 0.2231 0.5555 0.0974  0.1580  0.0890  638 HOH A O   
2515 O  O   . HOH F .   ? 0.4061 0.3213 0.3828 0.0187  -0.0204 0.0577  639 HOH A O   
2516 O  O   . HOH F .   ? 0.4115 0.5217 0.3944 -0.1685 0.0096  0.0364  640 HOH A O   
2517 O  O   . HOH F .   ? 0.4762 0.4149 0.4551 -0.0860 0.2004  -0.0467 641 HOH A O   
2518 O  O   . HOH F .   ? 0.4882 0.3140 0.4322 -0.2092 0.0646  0.0471  642 HOH A O   
2519 O  O   . HOH F .   ? 0.3443 0.2490 0.4142 -0.0120 -0.0146 -0.0485 643 HOH A O   
2520 O  O   . HOH F .   ? 0.2554 0.3086 0.2194 -0.0146 -0.0015 -0.0125 644 HOH A O   
2521 O  O   . HOH F .   ? 0.4169 0.5536 0.7961 -0.1581 0.2154  -0.1798 645 HOH A O   
2522 O  O   . HOH F .   ? 0.6288 0.2809 0.4106 -0.2150 -0.2694 -0.0342 646 HOH A O   
2523 O  O   . HOH F .   ? 0.3883 0.2287 0.3705 -0.0007 0.0401  -0.0688 647 HOH A O   
2524 O  O   . HOH F .   ? 0.4377 0.4964 0.3251 -0.0357 -0.0899 -0.0744 648 HOH A O   
2525 O  O   . HOH F .   ? 0.4138 0.6007 0.3122 -0.0802 0.0675  -0.1526 649 HOH A O   
2526 O  O   . HOH F .   ? 0.4187 0.5105 0.5429 0.0908  -0.1729 0.1455  650 HOH A O   
2527 O  O   . HOH F .   ? 0.4027 0.3847 0.2694 -0.0292 -0.0681 -0.0296 651 HOH A O   
2528 O  O   . HOH F .   ? 0.4917 0.3939 0.7196 -0.1168 -0.3352 0.2257  652 HOH A O   
2529 O  O   . HOH F .   ? 0.5088 0.7955 0.3792 -0.1563 0.1017  0.1033  653 HOH A O   
2530 O  O   . HOH F .   ? 0.5360 0.3095 0.3039 0.1062  0.0388  -0.0142 654 HOH A O   
2531 O  O   . HOH F .   ? 0.5018 0.4447 0.4059 -0.0463 -0.0597 -0.0930 655 HOH A O   
2532 O  O   . HOH F .   ? 0.4733 0.5340 0.5324 -0.1665 -0.0878 0.0096  656 HOH A O   
2533 O  O   . HOH F .   ? 0.4902 0.4156 0.6159 -0.0051 0.0136  -0.1832 657 HOH A O   
2534 O  O   . HOH F .   ? 0.5381 0.3506 0.8949 0.0914  -0.1416 -0.1203 658 HOH A O   
2535 O  O   . HOH F .   ? 0.6186 0.4881 0.3267 -0.0575 0.1361  -0.0887 659 HOH A O   
2536 O  O   . HOH F .   ? 0.4932 0.3361 0.1527 -0.2012 0.0769  0.0353  660 HOH A O   
2537 O  O   . HOH F .   ? 0.3018 0.2736 0.8845 -0.0903 0.2319  -0.0081 661 HOH A O   
2538 O  O   . HOH F .   ? 1.6875 1.6497 0.5356 0.4268  0.1076  0.2093  662 HOH A O   
2539 O  O   . HOH F .   ? 0.2897 0.6707 0.4196 -0.0063 -0.0790 0.0573  663 HOH A O   
2540 O  O   . HOH F .   ? 0.5582 0.3434 0.2897 0.0049  -0.0649 0.0006  664 HOH A O   
2541 O  O   . HOH F .   ? 0.5806 0.5899 0.3016 -0.2840 -0.0522 0.0147  665 HOH A O   
2542 O  O   . HOH F .   ? 0.2759 0.7042 0.4535 -0.0560 0.1348  0.0304  666 HOH A O   
2543 O  O   . HOH F .   ? 0.1303 0.6967 0.3720 0.1001  -0.0447 -0.2286 667 HOH A O   
2544 O  O   . HOH F .   ? 0.6136 0.3054 0.3878 -0.0284 -0.0333 0.1286  668 HOH A O   
2545 O  O   . HOH F .   ? 0.4296 0.8676 0.2831 0.1039  -0.1049 0.0593  669 HOH A O   
2546 O  O   . HOH F .   ? 0.3659 0.3885 0.4924 -0.0854 -0.0239 0.1053  670 HOH A O   
2547 O  O   . HOH F .   ? 0.7597 0.5612 0.2673 0.0197  -0.0076 0.0923  671 HOH A O   
2548 O  O   . HOH F .   ? 0.2431 0.2522 0.3404 0.1066  -0.0898 -0.1235 672 HOH A O   
2549 O  O   . HOH F .   ? 0.2838 0.1838 0.3555 0.0040  0.0333  -0.0388 673 HOH A O   
2550 O  O   . HOH F .   ? 0.4706 0.2684 0.4372 -0.0531 -0.0228 0.0604  674 HOH A O   
2551 O  O   . HOH F .   ? 0.4266 0.3210 0.2660 -0.0427 0.0276  -0.0020 675 HOH A O   
2552 O  O   . HOH F .   ? 0.2323 0.5644 0.4564 0.0417  0.0383  -0.0566 676 HOH A O   
2553 O  O   . HOH F .   ? 0.3106 0.5864 0.5544 -0.0551 -0.2082 0.0308  677 HOH A O   
2554 O  O   . HOH F .   ? 0.4632 0.6097 0.5088 -0.1688 -0.0153 0.2289  678 HOH A O   
2555 O  O   . HOH F .   ? 1.0946 0.2369 0.2870 -0.2752 -0.2551 0.0851  679 HOH A O   
2556 O  O   . HOH F .   ? 0.3828 0.4040 0.5336 0.0326  -0.1162 0.0450  680 HOH A O   
2557 O  O   . HOH F .   ? 0.3707 0.4156 0.3533 -0.1018 0.0052  -0.0170 681 HOH A O   
2558 O  O   . HOH F .   ? 0.5949 0.3774 0.2563 -0.1244 -0.0716 -0.0747 682 HOH A O   
2559 O  O   . HOH F .   ? 0.3876 0.1486 0.2563 0.0168  -0.1123 -0.0731 683 HOH A O   
2560 O  O   . HOH F .   ? 0.4587 0.2452 0.3910 0.0803  -0.0183 -0.0122 684 HOH A O   
2561 O  O   . HOH F .   ? 0.2861 0.4456 0.4946 -0.0859 -0.0896 -0.0952 685 HOH A O   
2562 O  O   . HOH F .   ? 0.2984 0.3186 0.3488 0.0668  0.0372  0.0008  686 HOH A O   
2563 O  O   . HOH F .   ? 0.7578 0.5116 0.1757 -0.1268 0.0182  0.0524  687 HOH A O   
2564 O  O   . HOH F .   ? 0.2921 0.2718 0.3149 -0.0370 0.1042  0.0606  688 HOH A O   
2565 O  O   . HOH F .   ? 0.2495 0.4738 0.3045 0.0076  0.0197  -0.0130 689 HOH A O   
2566 O  O   . HOH F .   ? 0.3456 0.3779 0.4232 0.0329  -0.0287 0.0656  690 HOH A O   
2567 O  O   . HOH F .   ? 0.2856 0.3700 0.6650 -0.1299 0.0308  0.1884  691 HOH A O   
2568 O  O   . HOH F .   ? 0.6575 0.5052 0.5314 0.3440  -0.0702 -0.1992 692 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   3   HIS HIS 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 126 126 127 LYS LYS A . n 
A 1 127 TYR 127 127 128 TYR TYR A . n 
A 1 128 GLY 128 128 129 GLY GLY A . n 
A 1 129 ASP 129 129 130 ASP ASP A . n 
A 1 130 VAL 130 130 131 VAL VAL A . n 
A 1 131 GLY 131 131 132 GLY GLY A . n 
A 1 132 LYS 132 132 133 LYS LYS A . n 
A 1 133 ALA 133 133 134 ALA ALA A . n 
A 1 134 LEU 134 134 135 LEU LEU A . n 
A 1 135 GLN 135 135 136 GLN GLN A . n 
A 1 136 GLN 136 136 137 GLN GLN A . n 
A 1 137 PRO 137 137 138 PRO PRO A . n 
A 1 138 ASP 138 138 139 ASP ASP A . n 
A 1 139 GLY 139 139 140 GLY GLY A . n 
A 1 140 LEU 140 140 141 LEU LEU A . n 
A 1 141 ALA 141 141 142 ALA ALA A . n 
A 1 142 VAL 142 142 143 VAL VAL A . n 
A 1 143 LEU 143 143 144 LEU LEU A . n 
A 1 144 GLY 144 144 145 GLY GLY A . n 
A 1 145 ILE 145 145 146 ILE ILE A . n 
A 1 146 PHE 146 146 147 PHE PHE A . n 
A 1 147 LEU 147 147 148 LEU LEU A . n 
A 1 148 LYS 148 148 149 LYS LYS A . n 
A 1 149 VAL 149 149 150 VAL VAL A . n 
A 1 150 GLY 150 150 151 GLY GLY A . n 
A 1 151 SER 151 151 152 SER SER A . n 
A 1 152 ALA 152 152 153 ALA ALA A . n 
A 1 153 LYS 153 153 154 LYS LYS A . n 
A 1 154 PRO 154 154 155 PRO PRO A . n 
A 1 155 GLY 155 155 156 GLY GLY A . n 
A 1 156 LEU 156 156 157 LEU LEU A . n 
A 1 157 GLN 157 157 158 GLN GLN A . n 
A 1 158 LYS 158 158 159 LYS LYS A . n 
A 1 159 VAL 159 159 160 VAL VAL A . n 
A 1 160 VAL 160 160 161 VAL VAL A . n 
A 1 161 ASP 161 161 162 ASP ASP A . n 
A 1 162 VAL 162 162 163 VAL VAL A . n 
A 1 163 LEU 163 163 164 LEU LEU A . n 
A 1 164 ASP 164 164 165 ASP ASP A . n 
A 1 165 SER 165 165 166 SER SER A . n 
A 1 166 ILE 166 166 167 ILE ILE A . n 
A 1 167 LYS 167 167 168 LYS LYS A . n 
A 1 168 THR 168 168 169 THR THR A . n 
A 1 169 LYS 169 169 170 LYS LYS A . n 
A 1 170 GLY 170 170 171 GLY GLY A . n 
A 1 171 LYS 171 171 172 LYS LYS A . n 
A 1 172 SER 172 172 173 SER SER A . n 
A 1 173 ALA 173 173 174 ALA ALA A . n 
A 1 174 ASP 174 174 175 ASP ASP A . n 
A 1 175 PHE 175 175 176 PHE PHE A . n 
A 1 176 THR 176 176 177 THR THR A . n 
A 1 177 ASN 177 177 178 ASN ASN A . n 
A 1 178 PHE 178 178 179 PHE PHE A . n 
A 1 179 ASP 179 179 180 ASP ASP A . n 
A 1 180 PRO 180 180 181 PRO PRO A . n 
A 1 181 ARG 181 181 182 ARG ARG A . n 
A 1 182 GLY 182 182 183 GLY GLY A . n 
A 1 183 LEU 183 183 184 LEU LEU A . n 
A 1 184 LEU 184 184 185 LEU LEU A . n 
A 1 185 PRO 185 185 186 PRO PRO A . n 
A 1 186 GLU 186 186 187 GLU GLU A . n 
A 1 187 SER 187 187 188 SER SER A . n 
A 1 188 LEU 188 188 189 LEU LEU A . n 
A 1 189 ASP 189 189 190 ASP ASP A . n 
A 1 190 TYR 190 190 191 TYR TYR A . n 
A 1 191 TRP 191 191 192 TRP TRP A . n 
A 1 192 THR 192 192 193 THR THR A . n 
A 1 193 TYR 193 193 194 TYR TYR A . n 
A 1 194 PRO 194 194 195 PRO PRO A . n 
A 1 195 GLY 195 195 196 GLY GLY A . n 
A 1 196 SER 196 196 197 SER SER A . n 
A 1 197 LEU 197 197 198 LEU LEU A . n 
A 1 198 THR 198 198 199 THR THR A . n 
A 1 199 THR 199 199 200 THR THR A . n 
A 1 200 PRO 200 200 201 PRO PRO A . n 
A 1 201 PRO 201 201 202 PRO PRO A . n 
A 1 202 LEU 202 202 203 LEU LEU A . n 
A 1 203 ALA 203 203 204 ALA ALA A . n 
A 1 204 GLU 204 204 205 GLU GLU A . n 
A 1 205 CYS 205 205 206 CYS CYS A . n 
A 1 206 VAL 206 206 207 VAL VAL A . n 
A 1 207 THR 207 207 208 THR THR A . n 
A 1 208 TRP 208 208 209 TRP TRP A . n 
A 1 209 ILE 209 209 210 ILE ILE A . n 
A 1 210 VAL 210 210 211 VAL VAL A . n 
A 1 211 LEU 211 211 212 LEU LEU A . n 
A 1 212 LYS 212 212 213 LYS LYS A . n 
A 1 213 GLU 213 213 214 GLU GLU A . n 
A 1 214 PRO 214 214 215 PRO PRO A . n 
A 1 215 ILE 215 215 216 ILE ILE A . n 
A 1 216 SER 216 216 217 SER SER A . n 
A 1 217 VAL 217 217 218 VAL VAL A . n 
A 1 218 SER 218 218 219 SER SER A . n 
A 1 219 SER 219 219 220 SER SER A . n 
A 1 220 GLU 220 220 221 GLU GLU A . n 
A 1 221 GLN 221 221 222 GLN GLN A . n 
A 1 222 VAL 222 222 223 VAL VAL A . n 
A 1 223 LEU 223 223 224 LEU LEU A . n 
A 1 224 LYS 224 224 225 LYS LYS A . n 
A 1 225 PHE 225 225 226 PHE PHE A . n 
A 1 226 ARG 226 226 227 ARG ARG A . n 
A 1 227 LYS 227 227 228 LYS LYS A . n 
A 1 228 LEU 228 228 229 LEU LEU A . n 
A 1 229 ASN 229 229 230 ASN ASN A . n 
A 1 230 PHE 230 230 231 PHE PHE A . n 
A 1 231 ASN 231 231 232 ASN ASN A . n 
A 1 232 GLY 232 232 233 GLY GLY A . n 
A 1 233 GLU 233 233 234 GLU GLU A . n 
A 1 234 GLY 234 234 235 GLY GLY A . n 
A 1 235 GLU 235 235 236 GLU GLU A . n 
A 1 236 PRO 236 236 237 PRO PRO A . n 
A 1 237 GLU 237 237 238 GLU GLU A . n 
A 1 238 GLU 238 238 239 GLU GLU A . n 
A 1 239 LEU 239 239 240 LEU LEU A . n 
A 1 240 MET 240 240 241 MET MET A . n 
A 1 241 VAL 241 241 242 VAL VAL A . n 
A 1 242 ASP 242 242 243 ASP ASP A . n 
A 1 243 ASN 243 243 244 ASN ASN A . n 
A 1 244 TRP 244 244 245 TRP TRP A . n 
A 1 245 ARG 245 245 246 ARG ARG A . n 
A 1 246 PRO 246 246 247 PRO PRO A . n 
A 1 247 ALA 247 247 248 ALA ALA A . n 
A 1 248 GLN 248 248 249 GLN GLN A . n 
A 1 249 PRO 249 249 250 PRO PRO A . n 
A 1 250 LEU 250 250 251 LEU LEU A . n 
A 1 251 LYS 251 251 252 LYS LYS A . n 
A 1 252 ASN 252 252 253 ASN ASN A . n 
A 1 253 ARG 253 253 254 ARG ARG A . n 
A 1 254 GLN 254 254 255 GLN GLN A . n 
A 1 255 ILE 255 255 256 ILE ILE A . n 
A 1 256 LYS 256 256 257 LYS LYS A . n 
A 1 257 ALA 257 257 258 ALA ALA A . n 
A 1 258 SER 258 258 259 SER SER A . n 
A 1 259 PHE 259 259 260 PHE PHE A . n 
A 1 260 LYS 260 260 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 DMS 1   302 1   DMS DMS A . 
D 4 BCN 1   303 2   BCN BCN A . 
E 5 V90 1   304 1   V90 V90 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 . 
# 
_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_555 104.7 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 112.7 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.6  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 ? E V90 .   ? A V90 304 ? 1_555 112.6 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 ? E V90 .   ? A V90 304 ? 1_555 117.6 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 ? E V90 .   ? A V90 304 ? 1_555 109.9 ? 
# 
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_sheet                  
10 3 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
2  3 'Structure model' '_database_2.pdbx_DOI'                        
3  3 'Structure model' '_database_2.pdbx_database_accession'         
4  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
5  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
16 3 'Structure model' '_pdbx_struct_conn_angle.value'               
17 3 'Structure model' '_struct_conn.pdbx_dist_value'                
18 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
19 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
20 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
21 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
22 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
23 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
24 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
25 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
26 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
27 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
28 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
29 3 'Structure model' '_struct_ref_seq_dif.details'                 
30 3 'Structure model' '_struct_sheet.number_strands'                
31 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
32 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
33 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 
# 
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  ? ? -144.71 54.45   
2 1 SER A 65  ? B -158.84 -159.26 
3 1 LYS A 76  ? A -81.38  -89.59  
4 1 GLU A 106 ? ? -92.19  -60.52  
5 1 LYS A 111 ? ? 73.28   -4.45   
6 1 PHE A 175 ? ? -161.06 69.13   
7 1 ASN A 243 ? ? -99.87  51.50   
8 1 LYS A 251 ? ? 54.64   -138.70 
# 
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 
# 
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 
V90 F18  F  N N 406 
V90 C5   C  Y N 407 
V90 C6   C  Y N 408 
V90 S12  S  N N 409 
V90 C13  C  N N 410 
V90 C14  C  N N 411 
V90 O15  O  N N 412 
V90 C1   C  Y N 413 
V90 F17  F  N N 414 
V90 C4   C  Y N 415 
V90 C3   C  Y N 416 
V90 S8   S  N N 417 
V90 O10  O  N N 418 
V90 N11  N  N N 419 
V90 O9   O  N N 420 
V90 C2   C  Y N 421 
V90 F16  F  N N 422 
V90 N7   N  N N 423 
V90 C19  C  N N 424 
V90 C26  C  N N 425 
V90 C25  C  N N 426 
V90 C24  C  N N 427 
V90 C23  C  N N 428 
V90 C22  C  N N 429 
V90 C21  C  N N 430 
V90 C20  C  N N 431 
V90 H1   H  N N 432 
V90 H2   H  N N 433 
V90 H3   H  N N 434 
V90 H4   H  N N 435 
V90 H5   H  N N 436 
V90 H6   H  N N 437 
V90 H7   H  N N 438 
V90 H8   H  N N 439 
V90 H9   H  N N 440 
V90 H10  H  N N 441 
V90 H11  H  N N 442 
V90 H12  H  N N 443 
V90 H13  H  N N 444 
V90 H14  H  N N 445 
V90 H15  H  N N 446 
V90 H16  H  N N 447 
V90 H17  H  N N 448 
V90 H18  H  N N 449 
V90 H19  H  N N 450 
V90 H20  H  N N 451 
V90 H21  H  N N 452 
V90 H22  H  N N 453 
V90 H23  H  N N 454 
VAL N    N  N N 455 
VAL CA   C  N S 456 
VAL C    C  N N 457 
VAL O    O  N N 458 
VAL CB   C  N N 459 
VAL CG1  C  N N 460 
VAL CG2  C  N N 461 
VAL OXT  O  N N 462 
VAL H    H  N N 463 
VAL H2   H  N N 464 
VAL HA   H  N N 465 
VAL HB   H  N N 466 
VAL HG11 H  N N 467 
VAL HG12 H  N N 468 
VAL HG13 H  N N 469 
VAL HG21 H  N N 470 
VAL HG22 H  N N 471 
VAL HG23 H  N N 472 
VAL HXT  H  N N 473 
ZN  ZN   ZN N N 474 
# 
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 
V90 C22 C23  sing N N 390 
V90 C22 C21  sing N N 391 
V90 C23 C24  sing N N 392 
V90 C24 C25  sing N N 393 
V90 O15 C14  sing N N 394 
V90 C21 C20  sing N N 395 
V90 C14 C13  sing N N 396 
V90 C25 C26  sing N N 397 
V90 C20 C19  sing N N 398 
V90 C13 S12  sing N N 399 
V90 C26 C19  sing N N 400 
V90 C19 N7   sing N N 401 
V90 F18 C5   sing N N 402 
V90 S12 C6   sing N N 403 
V90 C5  C6   doub Y N 404 
V90 C5  C4   sing Y N 405 
V90 N7  C4   sing N N 406 
V90 C6  C1   sing Y N 407 
V90 C4  C3   doub Y N 408 
V90 C1  F17  sing N N 409 
V90 C1  C2   doub Y N 410 
V90 C3  C2   sing Y N 411 
V90 C3  S8   sing N N 412 
V90 N11 S8   sing N N 413 
V90 C2  F16  sing N N 414 
V90 O10 S8   doub N N 415 
V90 S8  O9   doub N N 416 
V90 C13 H1   sing N N 417 
V90 C13 H2   sing N N 418 
V90 C14 H3   sing N N 419 
V90 C14 H4   sing N N 420 
V90 O15 H5   sing N N 421 
V90 N11 H6   sing N N 422 
V90 N11 H7   sing N N 423 
V90 N7  H8   sing N N 424 
V90 C19 H9   sing N N 425 
V90 C26 H10  sing N N 426 
V90 C26 H11  sing N N 427 
V90 C25 H12  sing N N 428 
V90 C25 H13  sing N N 429 
V90 C24 H14  sing N N 430 
V90 C24 H15  sing N N 431 
V90 C23 H16  sing N N 432 
V90 C23 H17  sing N N 433 
V90 C22 H18  sing N N 434 
V90 C22 H19  sing N N 435 
V90 C21 H20  sing N N 436 
V90 C21 H21  sing N N 437 
V90 C20 H22  sing N N 438 
V90 C20 H23  sing N N 439 
VAL N   CA   sing N N 440 
VAL N   H    sing N N 441 
VAL N   H2   sing N N 442 
VAL CA  C    sing N N 443 
VAL CA  CB   sing N N 444 
VAL CA  HA   sing N N 445 
VAL C   O    doub N N 446 
VAL C   OXT  sing N N 447 
VAL CB  CG1  sing N N 448 
VAL CB  CG2  sing N N 449 
VAL CB  HB   sing N N 450 
VAL CG1 HG11 sing N N 451 
VAL CG1 HG12 sing N N 452 
VAL CG1 HG13 sing N N 453 
VAL CG2 HG21 sing N N 454 
VAL CG2 HG22 sing N N 455 
VAL CG2 HG23 sing N N 456 
VAL OXT HXT  sing N N 457 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                           ZN  
3 'DIMETHYL SULFOXIDE'                                                                 DMS 
4 BICINE                                                                               BCN 
5 '2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' V90 
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' 
# 
