data_9IN7
# 
_entry.id   9IN7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9IN7         pdb_00009in7 10.2210/pdb9in7/pdb 
WWPDB D_1300049191 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-12 
_pdbx_audit_revision_history.part_number         ? 
# 
_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             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IN7 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              valentin.gordeliy@gmail.com 
_pdbx_contact_author.name_first         Valentin 
_pdbx_contact_author.name_last          Gordeliy 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5782-5896 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bukhdruker, S.' 1 0000-0002-0157-532X 
'Zabelskii, D.'  2 0000-0001-6906-975X 
'Astashkin, R.'  3 0000-0001-9065-8225 
'Gordeliy, V.'   4 0000-0001-5782-5896 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Ion conducting and gating molecular mechanisms of channelrhodopsin revealed by true-atomic resolution structures of open and closed states
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zabelskii, D.'   1  ? 
primary 'Bukhdruker, S.'  2  ? 
primary 'Bukhalovich, S.' 3  ? 
primary 'Tsybrov, F.'     4  ? 
primary 'Lamm, G.H.U.'    5  ? 
primary 'Astashkin, R.'   6  ? 
primary 'Doroginin, D.'   7  ? 
primary 'Matveev, G.'     8  ? 
primary 'Sudarev, V.'     9  ? 
primary 'Kuzmin, A.'      10 ? 
primary 'Zinovev, E.'     11 ? 
primary 'Vlasova, A.'     12 ? 
primary 'Ryzhykau, Y.'    13 ? 
primary 'Ilyinsky, N.'    14 ? 
primary 'Gushchin, I.'    15 ? 
primary 'Bourenkov, G.'   16 ? 
primary 'Alekseev, A.'    17 ? 
primary 'Round, A.'       18 ? 
primary 'Wachtveitl, J.'  19 ? 
primary 'Bamberg, E.'     20 ? 
primary 'Gordeliy, V.'    21 ? 
# 
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 'Viral rhodopsin OLPVR1'                         28127.299 1   ? ? ? ? 
2 non-polymer syn 'SODIUM ION'                                     22.990    1   ? ? ? ? 
3 non-polymer syn RETINAL                                          284.436   1   ? ? ? ? 
4 non-polymer syn '(2S)-2,3-dihydroxypropyl (9Z)-hexadec-9-enoate' 328.487   1   ? ? ? ? 
5 non-polymer syn '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' 356.540   6   ? ? ? ? 
6 non-polymer syn EICOSANE                                         282.547   10  ? ? ? ? 
7 non-polymer syn GLYCEROL                                         92.094    3   ? ? ? ? 
8 water       nat water                                            18.015    146 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;(FME)DNIIMTAYISIFVQIITAIISVYGLFIPLNFKDIILREILILELIVQIIEFIFYIWLIITLQSINEDITYVRYFD
WVLTTPVMLLTTVYFFEYMNSDDGIRKKEINDRDYVYLFYICLSNFFMLLIGYLGETKQINKMLTLFGGSFFLFLTFYLL
YVKYTKENWMNYIVFYFMFLVWFLYGFAFMFPFSIKNQMYNILDIVSKNIYSIFIFIVILNQSYKLLLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDNIIMTAYISIFVQIITAIISVYGLFIPLNFKDIILREILILELIVQIIEFIFYIWLIITLQSINEDITYVRYFDWVLT
TPVMLLTTVYFFEYMNSDDGIRKKEINDRDYVYLFYICLSNFFMLLIGYLGETKQINKMLTLFGGSFFLFLTFYLLYVKY
TKENWMNYIVFYFMFLVWFLYGFAFMFPFSIKNQMYNILDIVSKNIYSIFIFIVILNQSYKLLLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SODIUM ION'                                     NA  
3 RETINAL                                          RET 
4 '(2S)-2,3-dihydroxypropyl (9Z)-hexadec-9-enoate' 97N 
5 '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' OLC 
6 EICOSANE                                         LFA 
7 GLYCEROL                                         GOL 
8 water                                            HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   FME n 
1 2   ASP n 
1 3   ASN n 
1 4   ILE n 
1 5   ILE n 
1 6   MET n 
1 7   THR n 
1 8   ALA n 
1 9   TYR n 
1 10  ILE n 
1 11  SER n 
1 12  ILE n 
1 13  PHE n 
1 14  VAL n 
1 15  GLN n 
1 16  ILE n 
1 17  ILE n 
1 18  THR n 
1 19  ALA n 
1 20  ILE n 
1 21  ILE n 
1 22  SER n 
1 23  VAL n 
1 24  TYR n 
1 25  GLY n 
1 26  LEU n 
1 27  PHE n 
1 28  ILE n 
1 29  PRO n 
1 30  LEU n 
1 31  ASN n 
1 32  PHE n 
1 33  LYS n 
1 34  ASP n 
1 35  ILE n 
1 36  ILE n 
1 37  LEU n 
1 38  ARG n 
1 39  GLU n 
1 40  ILE n 
1 41  LEU n 
1 42  ILE n 
1 43  LEU n 
1 44  GLU n 
1 45  LEU n 
1 46  ILE n 
1 47  VAL n 
1 48  GLN n 
1 49  ILE n 
1 50  ILE n 
1 51  GLU n 
1 52  PHE n 
1 53  ILE n 
1 54  PHE n 
1 55  TYR n 
1 56  ILE n 
1 57  TRP n 
1 58  LEU n 
1 59  ILE n 
1 60  ILE n 
1 61  THR n 
1 62  LEU n 
1 63  GLN n 
1 64  SER n 
1 65  ILE n 
1 66  ASN n 
1 67  GLU n 
1 68  ASP n 
1 69  ILE n 
1 70  THR n 
1 71  TYR n 
1 72  VAL n 
1 73  ARG n 
1 74  TYR n 
1 75  PHE n 
1 76  ASP n 
1 77  TRP n 
1 78  VAL n 
1 79  LEU n 
1 80  THR n 
1 81  THR n 
1 82  PRO n 
1 83  VAL n 
1 84  MET n 
1 85  LEU n 
1 86  LEU n 
1 87  THR n 
1 88  THR n 
1 89  VAL n 
1 90  TYR n 
1 91  PHE n 
1 92  PHE n 
1 93  GLU n 
1 94  TYR n 
1 95  MET n 
1 96  ASN n 
1 97  SER n 
1 98  ASP n 
1 99  ASP n 
1 100 GLY n 
1 101 ILE n 
1 102 ARG n 
1 103 LYS n 
1 104 LYS n 
1 105 GLU n 
1 106 ILE n 
1 107 ASN n 
1 108 ASP n 
1 109 ARG n 
1 110 ASP n 
1 111 TYR n 
1 112 VAL n 
1 113 TYR n 
1 114 LEU n 
1 115 PHE n 
1 116 TYR n 
1 117 ILE n 
1 118 CYS n 
1 119 LEU n 
1 120 SER n 
1 121 ASN n 
1 122 PHE n 
1 123 PHE n 
1 124 MET n 
1 125 LEU n 
1 126 LEU n 
1 127 ILE n 
1 128 GLY n 
1 129 TYR n 
1 130 LEU n 
1 131 GLY n 
1 132 GLU n 
1 133 THR n 
1 134 LYS n 
1 135 GLN n 
1 136 ILE n 
1 137 ASN n 
1 138 LYS n 
1 139 MET n 
1 140 LEU n 
1 141 THR n 
1 142 LEU n 
1 143 PHE n 
1 144 GLY n 
1 145 GLY n 
1 146 SER n 
1 147 PHE n 
1 148 PHE n 
1 149 LEU n 
1 150 PHE n 
1 151 LEU n 
1 152 THR n 
1 153 PHE n 
1 154 TYR n 
1 155 LEU n 
1 156 LEU n 
1 157 TYR n 
1 158 VAL n 
1 159 LYS n 
1 160 TYR n 
1 161 THR n 
1 162 LYS n 
1 163 GLU n 
1 164 ASN n 
1 165 TRP n 
1 166 MET n 
1 167 ASN n 
1 168 TYR n 
1 169 ILE n 
1 170 VAL n 
1 171 PHE n 
1 172 TYR n 
1 173 PHE n 
1 174 MET n 
1 175 PHE n 
1 176 LEU n 
1 177 VAL n 
1 178 TRP n 
1 179 PHE n 
1 180 LEU n 
1 181 TYR n 
1 182 GLY n 
1 183 PHE n 
1 184 ALA n 
1 185 PHE n 
1 186 MET n 
1 187 PHE n 
1 188 PRO n 
1 189 PHE n 
1 190 SER n 
1 191 ILE n 
1 192 LYS n 
1 193 ASN n 
1 194 GLN n 
1 195 MET n 
1 196 TYR n 
1 197 ASN n 
1 198 ILE n 
1 199 LEU n 
1 200 ASP n 
1 201 ILE n 
1 202 VAL n 
1 203 SER n 
1 204 LYS n 
1 205 ASN n 
1 206 ILE n 
1 207 TYR n 
1 208 SER n 
1 209 ILE n 
1 210 PHE n 
1 211 ILE n 
1 212 PHE n 
1 213 ILE n 
1 214 VAL n 
1 215 ILE n 
1 216 LEU n 
1 217 ASN n 
1 218 GLN n 
1 219 SER n 
1 220 TYR n 
1 221 LYS n 
1 222 LEU n 
1 223 LEU n 
1 224 LEU n 
1 225 GLU n 
1 226 HIS n 
1 227 HIS n 
1 228 HIS n 
1 229 HIS n 
1 230 HIS n 
1 231 HIS 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                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   231 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 162281038 
_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      'Organic Lake phycodnavirus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     938083 
_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 BL21(DE3)' 
_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               ? 
_entity_src_gen.pdbx_host_org_variant              C41 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
97N non-polymer         . '(2S)-2,3-dihydroxypropyl (9Z)-hexadec-9-enoate' ?                               'C19 H36 O4'     
328.487 
ALA 'L-peptide linking' y ALANINE                                          ?                               'C3 H7 N O2'     89.093 
ARG 'L-peptide linking' y ARGININE                                         ?                               'C6 H15 N4 O2 1' 
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                       ?                               'C4 H8 N2 O3'    
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                  ?                               'C4 H7 N O4'     
133.103 
CYS 'L-peptide linking' y CYSTEINE                                         ?                               'C3 H7 N O2 S'   
121.158 
FME 'L-peptide linking' n N-FORMYLMETHIONINE                               ?                               'C6 H11 N O3 S'  
177.221 
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 
GOL non-polymer         . GLYCEROL                                         'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094 
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 
LFA non-polymer         . EICOSANE                                         'LIPID FRAGMENT'                'C20 H42'        
282.547 
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 
NA  non-polymer         . 'SODIUM ION'                                     ?                               'Na 1'           22.990 
OLC non-polymer         . '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' 1-Oleoyl-R-glycerol             'C21 H40 O4'     
356.540 
PHE 'L-peptide linking' y PHENYLALANINE                                    ?                               'C9 H11 N O2'    
165.189 
PRO 'L-peptide linking' y PROLINE                                          ?                               'C5 H9 N O2'     
115.130 
RET non-polymer         . RETINAL                                          ?                               'C20 H28 O'      
284.436 
SER 'L-peptide linking' y SERINE                                           ?                               'C3 H7 N O3'     
105.093 
THR 'L-peptide linking' y THREONINE                                        ?                               'C4 H9 N O3'     
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                       ?                               'C11 H12 N2 O2'  
204.225 
TYR 'L-peptide linking' y TYROSINE                                         ?                               'C9 H11 N O3'    
181.189 
VAL 'L-peptide linking' y VALINE                                           ?                               'C5 H11 N O2'    
117.146 
# 
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   FME 1   1   1   FME FME A . n 
A 1 2   ASP 2   2   2   ASP ASP A . n 
A 1 3   ASN 3   3   3   ASN ASN A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   THR 7   7   7   THR THR A . n 
A 1 8   ALA 8   8   8   ALA ALA A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  PHE 13  13  13  PHE PHE A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  ILE 20  20  20  ILE ILE A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  VAL 23  23  23  VAL VAL A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  ILE 28  28  28  ILE ILE A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  ASN 31  31  31  ASN ASN A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  TRP 57  57  57  TRP TRP A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  TYR 74  74  74  TYR TYR A . n 
A 1 75  PHE 75  75  75  PHE PHE A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  TRP 77  77  77  TRP TRP 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  THR 80  80  80  THR THR A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  MET 84  84  84  MET MET A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  TYR 90  90  90  TYR TYR A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  MET 95  95  95  MET MET A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 LYS 103 103 103 LYS LYS A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 ASN 107 107 107 ASN ASN A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 TYR 111 111 111 TYR TYR A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 PHE 115 115 115 PHE PHE A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 CYS 118 118 118 CYS CYS A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 ASN 121 121 121 ASN ASN A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 PHE 123 123 123 PHE PHE A . n 
A 1 124 MET 124 124 124 MET MET A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 ILE 127 127 127 ILE ILE A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 TYR 129 129 129 TYR TYR A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 THR 133 133 133 THR THR A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 ASN 137 137 137 ASN ASN A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 MET 139 139 139 MET MET A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 PHE 143 143 143 PHE PHE A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 PHE 148 148 148 PHE PHE A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 TYR 160 160 160 TYR TYR A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 TRP 165 165 165 TRP TRP A . n 
A 1 166 MET 166 166 166 MET MET A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 TYR 168 168 168 TYR TYR A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 VAL 170 170 170 VAL VAL A . n 
A 1 171 PHE 171 171 171 PHE PHE A . n 
A 1 172 TYR 172 172 172 TYR TYR A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 MET 174 174 174 MET MET A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 TRP 178 178 178 TRP TRP A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 TYR 181 181 181 TYR TYR A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 PHE 183 183 183 PHE PHE A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 MET 186 186 186 MET MET A . n 
A 1 187 PHE 187 187 187 PHE PHE A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 ILE 191 191 191 ILE ILE A . n 
A 1 192 LYS 192 192 192 LYS LYS A . n 
A 1 193 ASN 193 193 193 ASN ASN A . n 
A 1 194 GLN 194 194 194 GLN GLN A . n 
A 1 195 MET 195 195 195 MET MET A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 ILE 206 206 206 ILE ILE A . n 
A 1 207 TYR 207 207 207 TYR TYR A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 PHE 210 210 210 PHE PHE A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 PHE 212 212 212 PHE PHE A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 ASN 217 217 217 ASN ASN A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 TYR 220 220 220 TYR TYR A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 GLU 225 225 ?   ?   ?   A . n 
A 1 226 HIS 226 226 ?   ?   ?   A . n 
A 1 227 HIS 227 227 ?   ?   ?   A . n 
A 1 228 HIS 228 228 ?   ?   ?   A . n 
A 1 229 HIS 229 229 ?   ?   ?   A . n 
A 1 230 HIS 230 230 ?   ?   ?   A . n 
A 1 231 HIS 231 231 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 NA  ? ? NA  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 RET ? ? RET ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 NA  1   301 292 NA  NA  A . 
C 3 RET 1   302 301 RET RET A . 
D 4 97N 1   303 303 97N 97N A . 
E 5 OLC 1   304 401 OLC OLC A . 
F 6 LFA 1   305 402 LFA LFA A . 
G 6 LFA 1   306 403 LFA LFA A . 
H 6 LFA 1   307 404 LFA LFA A . 
I 6 LFA 1   308 405 LFA LFA A . 
J 6 LFA 1   309 406 LFA LFA A . 
K 6 LFA 1   310 407 LFA LFA A . 
L 6 LFA 1   311 408 LFA LFA A . 
M 6 LFA 1   312 409 LFA LFA A . 
N 6 LFA 1   313 410 LFA LFA A . 
O 6 LFA 1   314 411 LFA LFA A . 
P 7 GOL 1   315 412 GOL GOL A . 
Q 7 GOL 1   316 413 GOL GOL A . 
R 7 GOL 1   317 414 GOL GOL A . 
S 5 OLC 1   318 415 OLC OLC A . 
T 5 OLC 1   319 416 OLC OLC A . 
U 5 OLC 1   320 417 OLC OLC A . 
V 5 OLC 1   321 418 OLC OLC A . 
W 5 OLC 1   322 419 OLC OLC A . 
X 8 HOH 1   401 513 HOH HOH A . 
X 8 HOH 2   402 534 HOH HOH A . 
X 8 HOH 3   403 560 HOH HOH A . 
X 8 HOH 4   404 625 HOH HOH A . 
X 8 HOH 5   405 523 HOH HOH A . 
X 8 HOH 6   406 585 HOH HOH A . 
X 8 HOH 7   407 524 HOH HOH A . 
X 8 HOH 8   408 530 HOH HOH A . 
X 8 HOH 9   409 515 HOH HOH A . 
X 8 HOH 10  410 605 HOH HOH A . 
X 8 HOH 11  411 567 HOH HOH A . 
X 8 HOH 12  412 635 HOH HOH A . 
X 8 HOH 13  413 526 HOH HOH A . 
X 8 HOH 14  414 584 HOH HOH A . 
X 8 HOH 15  415 537 HOH HOH A . 
X 8 HOH 16  416 547 HOH HOH A . 
X 8 HOH 17  417 566 HOH HOH A . 
X 8 HOH 18  418 631 HOH HOH A . 
X 8 HOH 19  419 512 HOH HOH A . 
X 8 HOH 20  420 542 HOH HOH A . 
X 8 HOH 21  421 505 HOH HOH A . 
X 8 HOH 22  422 620 HOH HOH A . 
X 8 HOH 23  423 626 HOH HOH A . 
X 8 HOH 24  424 504 HOH HOH A . 
X 8 HOH 25  425 545 HOH HOH A . 
X 8 HOH 26  426 582 HOH HOH A . 
X 8 HOH 27  427 561 HOH HOH A . 
X 8 HOH 28  428 618 HOH HOH A . 
X 8 HOH 29  429 521 HOH HOH A . 
X 8 HOH 30  430 552 HOH HOH A . 
X 8 HOH 31  431 592 HOH HOH A . 
X 8 HOH 32  432 645 HOH HOH A . 
X 8 HOH 33  433 580 HOH HOH A . 
X 8 HOH 34  434 506 HOH HOH A . 
X 8 HOH 35  435 507 HOH HOH A . 
X 8 HOH 36  436 629 HOH HOH A . 
X 8 HOH 37  437 533 HOH HOH A . 
X 8 HOH 38  438 558 HOH HOH A . 
X 8 HOH 39  439 514 HOH HOH A . 
X 8 HOH 40  440 607 HOH HOH A . 
X 8 HOH 41  441 503 HOH HOH A . 
X 8 HOH 42  442 637 HOH HOH A . 
X 8 HOH 43  443 529 HOH HOH A . 
X 8 HOH 44  444 590 HOH HOH A . 
X 8 HOH 45  445 541 HOH HOH A . 
X 8 HOH 46  446 627 HOH HOH A . 
X 8 HOH 47  447 509 HOH HOH A . 
X 8 HOH 48  448 510 HOH HOH A . 
X 8 HOH 49  449 549 HOH HOH A . 
X 8 HOH 50  450 586 HOH HOH A . 
X 8 HOH 51  451 522 HOH HOH A . 
X 8 HOH 52  452 538 HOH HOH A . 
X 8 HOH 53  453 610 HOH HOH A . 
X 8 HOH 54  454 519 HOH HOH A . 
X 8 HOH 55  455 564 HOH HOH A . 
X 8 HOH 56  456 516 HOH HOH A . 
X 8 HOH 57  457 520 HOH HOH A . 
X 8 HOH 58  458 525 HOH HOH A . 
X 8 HOH 59  459 644 HOH HOH A . 
X 8 HOH 60  460 556 HOH HOH A . 
X 8 HOH 61  461 577 HOH HOH A . 
X 8 HOH 62  462 532 HOH HOH A . 
X 8 HOH 63  463 608 HOH HOH A . 
X 8 HOH 64  464 617 HOH HOH A . 
X 8 HOH 65  465 508 HOH HOH A . 
X 8 HOH 66  466 517 HOH HOH A . 
X 8 HOH 67  467 502 HOH HOH A . 
X 8 HOH 68  468 619 HOH HOH A . 
X 8 HOH 69  469 643 HOH HOH A . 
X 8 HOH 70  470 571 HOH HOH A . 
X 8 HOH 71  471 576 HOH HOH A . 
X 8 HOH 72  472 624 HOH HOH A . 
X 8 HOH 73  473 575 HOH HOH A . 
X 8 HOH 74  474 630 HOH HOH A . 
X 8 HOH 75  475 511 HOH HOH A . 
X 8 HOH 76  476 518 HOH HOH A . 
X 8 HOH 77  477 572 HOH HOH A . 
X 8 HOH 78  478 634 HOH HOH A . 
X 8 HOH 79  479 599 HOH HOH A . 
X 8 HOH 80  480 555 HOH HOH A . 
X 8 HOH 81  481 594 HOH HOH A . 
X 8 HOH 82  482 611 HOH HOH A . 
X 8 HOH 83  483 574 HOH HOH A . 
X 8 HOH 84  484 550 HOH HOH A . 
X 8 HOH 85  485 578 HOH HOH A . 
X 8 HOH 86  486 589 HOH HOH A . 
X 8 HOH 87  487 604 HOH HOH A . 
X 8 HOH 88  488 531 HOH HOH A . 
X 8 HOH 89  489 573 HOH HOH A . 
X 8 HOH 90  490 563 HOH HOH A . 
X 8 HOH 91  491 614 HOH HOH A . 
X 8 HOH 92  492 565 HOH HOH A . 
X 8 HOH 93  493 536 HOH HOH A . 
X 8 HOH 94  494 587 HOH HOH A . 
X 8 HOH 95  495 539 HOH HOH A . 
X 8 HOH 96  496 597 HOH HOH A . 
X 8 HOH 97  497 609 HOH HOH A . 
X 8 HOH 98  498 551 HOH HOH A . 
X 8 HOH 99  499 528 HOH HOH A . 
X 8 HOH 100 500 535 HOH HOH A . 
X 8 HOH 101 501 557 HOH HOH A . 
X 8 HOH 102 502 606 HOH HOH A . 
X 8 HOH 103 503 546 HOH HOH A . 
X 8 HOH 104 504 527 HOH HOH A . 
X 8 HOH 105 505 595 HOH HOH A . 
X 8 HOH 106 506 553 HOH HOH A . 
X 8 HOH 107 507 596 HOH HOH A . 
X 8 HOH 108 508 591 HOH HOH A . 
X 8 HOH 109 509 501 HOH HOH A . 
X 8 HOH 110 510 543 HOH HOH A . 
X 8 HOH 111 511 593 HOH HOH A . 
X 8 HOH 112 512 559 HOH HOH A . 
X 8 HOH 113 513 641 HOH HOH A . 
X 8 HOH 114 514 601 HOH HOH A . 
X 8 HOH 115 515 583 HOH HOH A . 
X 8 HOH 116 516 579 HOH HOH A . 
X 8 HOH 117 517 646 HOH HOH A . 
X 8 HOH 118 518 613 HOH HOH A . 
X 8 HOH 119 519 554 HOH HOH A . 
X 8 HOH 120 520 544 HOH HOH A . 
X 8 HOH 121 521 628 HOH HOH A . 
X 8 HOH 122 522 588 HOH HOH A . 
X 8 HOH 123 523 548 HOH HOH A . 
X 8 HOH 124 524 642 HOH HOH A . 
X 8 HOH 125 525 569 HOH HOH A . 
X 8 HOH 126 526 622 HOH HOH A . 
X 8 HOH 127 527 598 HOH HOH A . 
X 8 HOH 128 528 616 HOH HOH A . 
X 8 HOH 129 529 568 HOH HOH A . 
X 8 HOH 130 530 562 HOH HOH A . 
X 8 HOH 131 531 621 HOH HOH A . 
X 8 HOH 132 532 640 HOH HOH A . 
X 8 HOH 133 533 639 HOH HOH A . 
X 8 HOH 134 534 600 HOH HOH A . 
X 8 HOH 135 535 615 HOH HOH A . 
X 8 HOH 136 536 570 HOH HOH A . 
X 8 HOH 137 537 540 HOH HOH A . 
X 8 HOH 138 538 632 HOH HOH A . 
X 8 HOH 139 539 602 HOH HOH A . 
X 8 HOH 140 540 638 HOH HOH A . 
X 8 HOH 141 541 581 HOH HOH A . 
X 8 HOH 142 542 612 HOH HOH A . 
X 8 HOH 143 543 603 HOH HOH A . 
X 8 HOH 144 544 623 HOH HOH A . 
X 8 HOH 145 545 636 HOH HOH A . 
X 8 HOH 146 546 633 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ILE 65  ? CG1 ? A ILE 65  CG1 
2   1 Y 1 A ILE 65  ? CG2 ? A ILE 65  CG2 
3   1 Y 1 A ILE 65  ? CD1 ? A ILE 65  CD1 
4   1 Y 1 A ASP 98  ? OD1 ? A ASP 98  OD1 
5   1 Y 1 A ASP 98  ? OD2 ? A ASP 98  OD2 
6   1 Y 1 A ASP 99  ? CG  ? A ASP 99  CG  
7   1 Y 1 A ASP 99  ? OD1 ? A ASP 99  OD1 
8   1 Y 1 A ASP 99  ? OD2 ? A ASP 99  OD2 
9   1 Y 1 A LEU 224 ? CG  ? A LEU 224 CG  
10  1 Y 1 A LEU 224 ? CD1 ? A LEU 224 CD1 
11  1 Y 1 A LEU 224 ? CD2 ? A LEU 224 CD2 
12  1 N 1 A OLC 304 ? C18 ? E OLC 1   C18 
13  1 N 1 A OLC 304 ? C17 ? E OLC 1   C17 
14  1 N 1 A OLC 304 ? C24 ? E OLC 1   C24 
15  1 N 1 A OLC 304 ? C16 ? E OLC 1   C16 
16  1 N 1 A OLC 304 ? C15 ? E OLC 1   C15 
17  1 N 1 A OLC 304 ? C21 ? E OLC 1   C21 
18  1 N 1 A OLC 304 ? C22 ? E OLC 1   C22 
19  1 N 1 A OLC 304 ? O25 ? E OLC 1   O25 
20  1 N 1 A OLC 304 ? O23 ? E OLC 1   O23 
21  1 N 1 A LFA 305 ? C13 ? F LFA 1   C13 
22  1 N 1 A LFA 305 ? C14 ? F LFA 1   C14 
23  1 N 1 A LFA 305 ? C15 ? F LFA 1   C15 
24  1 N 1 A LFA 305 ? C16 ? F LFA 1   C16 
25  1 N 1 A LFA 305 ? C17 ? F LFA 1   C17 
26  1 N 1 A LFA 305 ? C18 ? F LFA 1   C18 
27  1 N 1 A LFA 305 ? C19 ? F LFA 1   C19 
28  1 N 1 A LFA 305 ? C20 ? F LFA 1   C20 
29  1 N 1 A LFA 306 ? C1  ? G LFA 1   C1  
30  1 N 1 A LFA 306 ? C2  ? G LFA 1   C2  
31  1 N 1 A LFA 306 ? C3  ? G LFA 1   C3  
32  1 N 1 A LFA 306 ? C4  ? G LFA 1   C4  
33  1 N 1 A LFA 306 ? C5  ? G LFA 1   C5  
34  1 N 1 A LFA 306 ? C6  ? G LFA 1   C6  
35  1 N 1 A LFA 306 ? C7  ? G LFA 1   C7  
36  1 N 1 A LFA 307 ? C13 ? H LFA 1   C13 
37  1 N 1 A LFA 307 ? C14 ? H LFA 1   C14 
38  1 N 1 A LFA 307 ? C15 ? H LFA 1   C15 
39  1 N 1 A LFA 307 ? C16 ? H LFA 1   C16 
40  1 N 1 A LFA 307 ? C17 ? H LFA 1   C17 
41  1 N 1 A LFA 307 ? C18 ? H LFA 1   C18 
42  1 N 1 A LFA 307 ? C19 ? H LFA 1   C19 
43  1 N 1 A LFA 307 ? C20 ? H LFA 1   C20 
44  1 N 1 A LFA 308 ? C1  ? I LFA 1   C1  
45  1 N 1 A LFA 308 ? C2  ? I LFA 1   C2  
46  1 N 1 A LFA 308 ? C3  ? I LFA 1   C3  
47  1 N 1 A LFA 308 ? C4  ? I LFA 1   C4  
48  1 N 1 A LFA 308 ? C5  ? I LFA 1   C5  
49  1 N 1 A LFA 309 ? C1  ? J LFA 1   C1  
50  1 N 1 A LFA 309 ? C2  ? J LFA 1   C2  
51  1 N 1 A LFA 309 ? C3  ? J LFA 1   C3  
52  1 N 1 A LFA 309 ? C4  ? J LFA 1   C4  
53  1 N 1 A LFA 310 ? C6  ? K LFA 1   C6  
54  1 N 1 A LFA 310 ? C7  ? K LFA 1   C7  
55  1 N 1 A LFA 310 ? C8  ? K LFA 1   C8  
56  1 N 1 A LFA 310 ? C9  ? K LFA 1   C9  
57  1 N 1 A LFA 310 ? C10 ? K LFA 1   C10 
58  1 N 1 A LFA 310 ? C11 ? K LFA 1   C11 
59  1 N 1 A LFA 310 ? C12 ? K LFA 1   C12 
60  1 N 1 A LFA 310 ? C13 ? K LFA 1   C13 
61  1 N 1 A LFA 310 ? C14 ? K LFA 1   C14 
62  1 N 1 A LFA 310 ? C15 ? K LFA 1   C15 
63  1 N 1 A LFA 310 ? C16 ? K LFA 1   C16 
64  1 N 1 A LFA 310 ? C17 ? K LFA 1   C17 
65  1 N 1 A LFA 310 ? C18 ? K LFA 1   C18 
66  1 N 1 A LFA 310 ? C19 ? K LFA 1   C19 
67  1 N 1 A LFA 310 ? C20 ? K LFA 1   C20 
68  1 N 1 A LFA 311 ? C1  ? L LFA 1   C1  
69  1 N 1 A LFA 311 ? C2  ? L LFA 1   C2  
70  1 N 1 A LFA 311 ? C3  ? L LFA 1   C3  
71  1 N 1 A LFA 311 ? C4  ? L LFA 1   C4  
72  1 N 1 A LFA 311 ? C5  ? L LFA 1   C5  
73  1 N 1 A LFA 311 ? C6  ? L LFA 1   C6  
74  1 N 1 A LFA 311 ? C7  ? L LFA 1   C7  
75  1 N 1 A LFA 311 ? C8  ? L LFA 1   C8  
76  1 N 1 A LFA 311 ? C9  ? L LFA 1   C9  
77  1 N 1 A LFA 311 ? C10 ? L LFA 1   C10 
78  1 N 1 A LFA 311 ? C11 ? L LFA 1   C11 
79  1 N 1 A LFA 311 ? C12 ? L LFA 1   C12 
80  1 N 1 A LFA 311 ? C13 ? L LFA 1   C13 
81  1 N 1 A LFA 311 ? C14 ? L LFA 1   C14 
82  1 N 1 A LFA 311 ? C15 ? L LFA 1   C15 
83  1 N 1 A LFA 312 ? C1  ? M LFA 1   C1  
84  1 N 1 A LFA 312 ? C2  ? M LFA 1   C2  
85  1 N 1 A LFA 312 ? C3  ? M LFA 1   C3  
86  1 N 1 A LFA 312 ? C4  ? M LFA 1   C4  
87  1 N 1 A LFA 312 ? C5  ? M LFA 1   C5  
88  1 N 1 A LFA 312 ? C6  ? M LFA 1   C6  
89  1 N 1 A LFA 312 ? C7  ? M LFA 1   C7  
90  1 N 1 A LFA 312 ? C8  ? M LFA 1   C8  
91  1 N 1 A LFA 312 ? C9  ? M LFA 1   C9  
92  1 N 1 A LFA 312 ? C10 ? M LFA 1   C10 
93  1 N 1 A LFA 312 ? C11 ? M LFA 1   C11 
94  1 N 1 A LFA 312 ? C12 ? M LFA 1   C12 
95  1 N 1 A LFA 312 ? C13 ? M LFA 1   C13 
96  1 N 1 A LFA 312 ? C14 ? M LFA 1   C14 
97  1 N 1 A LFA 314 ? C1  ? O LFA 1   C1  
98  1 N 1 A LFA 314 ? C2  ? O LFA 1   C2  
99  1 N 1 A LFA 314 ? C3  ? O LFA 1   C3  
100 1 N 1 A LFA 314 ? C4  ? O LFA 1   C4  
101 1 N 1 A LFA 314 ? C5  ? O LFA 1   C5  
102 1 N 1 A LFA 314 ? C6  ? O LFA 1   C6  
103 1 N 1 A LFA 314 ? C7  ? O LFA 1   C7  
104 1 N 1 A LFA 314 ? C8  ? O LFA 1   C8  
105 1 N 1 A LFA 314 ? C9  ? O LFA 1   C9  
106 1 N 1 A LFA 314 ? C10 ? O LFA 1   C10 
107 1 N 1 A LFA 314 ? C11 ? O LFA 1   C11 
108 1 N 1 A LFA 314 ? C12 ? O LFA 1   C12 
109 1 N 1 A LFA 314 ? C13 ? O LFA 1   C13 
110 1 N 1 A LFA 314 ? C14 ? O LFA 1   C14 
111 1 N 1 A LFA 314 ? C15 ? O LFA 1   C15 
112 1 N 1 A OLC 318 ? C18 ? S OLC 1   C18 
113 1 N 1 A OLC 318 ? C10 ? S OLC 1   C10 
114 1 N 1 A OLC 318 ? C9  ? S OLC 1   C9  
115 1 N 1 A OLC 318 ? C17 ? S OLC 1   C17 
116 1 N 1 A OLC 318 ? C11 ? S OLC 1   C11 
117 1 N 1 A OLC 318 ? C8  ? S OLC 1   C8  
118 1 N 1 A OLC 318 ? C16 ? S OLC 1   C16 
119 1 N 1 A OLC 318 ? C12 ? S OLC 1   C12 
120 1 N 1 A OLC 318 ? C7  ? S OLC 1   C7  
121 1 N 1 A OLC 318 ? C15 ? S OLC 1   C15 
122 1 N 1 A OLC 318 ? C13 ? S OLC 1   C13 
123 1 N 1 A OLC 318 ? C6  ? S OLC 1   C6  
124 1 N 1 A OLC 318 ? C14 ? S OLC 1   C14 
125 1 N 1 A OLC 318 ? C5  ? S OLC 1   C5  
126 1 N 1 A OLC 319 ? C18 ? T OLC 1   C18 
127 1 N 1 A OLC 319 ? C17 ? T OLC 1   C17 
128 1 N 1 A OLC 319 ? C16 ? T OLC 1   C16 
129 1 N 1 A OLC 319 ? C12 ? T OLC 1   C12 
130 1 N 1 A OLC 319 ? C15 ? T OLC 1   C15 
131 1 N 1 A OLC 319 ? C13 ? T OLC 1   C13 
132 1 N 1 A OLC 319 ? C14 ? T OLC 1   C14 
133 1 N 1 A OLC 320 ? C18 ? U OLC 1   C18 
134 1 N 1 A OLC 320 ? C10 ? U OLC 1   C10 
135 1 N 1 A OLC 320 ? C9  ? U OLC 1   C9  
136 1 N 1 A OLC 320 ? C17 ? U OLC 1   C17 
137 1 N 1 A OLC 320 ? C11 ? U OLC 1   C11 
138 1 N 1 A OLC 320 ? C8  ? U OLC 1   C8  
139 1 N 1 A OLC 320 ? C24 ? U OLC 1   C24 
140 1 N 1 A OLC 320 ? C16 ? U OLC 1   C16 
141 1 N 1 A OLC 320 ? C12 ? U OLC 1   C12 
142 1 N 1 A OLC 320 ? C15 ? U OLC 1   C15 
143 1 N 1 A OLC 320 ? C13 ? U OLC 1   C13 
144 1 N 1 A OLC 320 ? C14 ? U OLC 1   C14 
145 1 N 1 A OLC 320 ? C21 ? U OLC 1   C21 
146 1 N 1 A OLC 320 ? C22 ? U OLC 1   C22 
147 1 N 1 A OLC 320 ? O25 ? U OLC 1   O25 
148 1 N 1 A OLC 320 ? O23 ? U OLC 1   O23 
149 1 N 1 A OLC 321 ? C18 ? V OLC 1   C18 
150 1 N 1 A OLC 321 ? C17 ? V OLC 1   C17 
151 1 N 1 A OLC 321 ? C24 ? V OLC 1   C24 
152 1 N 1 A OLC 321 ? C16 ? V OLC 1   C16 
153 1 N 1 A OLC 321 ? C15 ? V OLC 1   C15 
154 1 N 1 A OLC 321 ? C13 ? V OLC 1   C13 
155 1 N 1 A OLC 321 ? C14 ? V OLC 1   C14 
156 1 N 1 A OLC 321 ? O25 ? V OLC 1   O25 
157 1 N 1 A OLC 321 ? O23 ? V OLC 1   O23 
158 1 N 1 A OLC 322 ? C18 ? W OLC 1   C18 
159 1 N 1 A OLC 322 ? C17 ? W OLC 1   C17 
160 1 N 1 A OLC 322 ? C24 ? W OLC 1   C24 
161 1 N 1 A OLC 322 ? C16 ? W OLC 1   C16 
162 1 N 1 A OLC 322 ? C15 ? W OLC 1   C15 
163 1 N 1 A OLC 322 ? C21 ? W OLC 1   C21 
164 1 N 1 A OLC 322 ? C22 ? W OLC 1   C22 
165 1 N 1 A OLC 322 ? O25 ? W OLC 1   O25 
166 1 N 1 A OLC 322 ? O23 ? W OLC 1   O23 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? MxCuBE    ? ? ? 3           1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .           2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .           3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .           4 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.20.1_4487 5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IN7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.498 
_cell.length_a_esd                 ? 
_cell.length_b                     114.948 
_cell.length_b_esd                 ? 
_cell.length_c                     53.171 
_cell.length_c_esd                 ? 
_cell.volume                       284191.131 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9IN7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IN7 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.62 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.96 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM Tris, 900 mM NaCl, and 24% (w/v) PEG 6000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X CdTe 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-09-03 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8856 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8856 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          17.17 
_reflns.entry_id                                       9IN7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.13 
_reflns.d_resolution_low                               33.48 
_reflns.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.number_all                                     ? 
_reflns.number_obs                                     78116 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           94.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.022 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.13 
_reflns_shell.d_res_low                                     1.23 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3905 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               5.3 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               1.066 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.220 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          70.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               26.02 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9IN7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.13 
_refine.ls_d_res_low                             33.48 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     78045 
_refine.ls_number_reflns_R_free                  3898 
_refine.ls_number_reflns_R_work                  74147 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    72.44 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1530 
_refine.ls_R_factor_R_free                       0.1838 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1513 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      7AKY 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.0782 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.1208 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.13 
_refine_hist.d_res_low                        33.48 
_refine_hist.number_atoms_solvent             146 
_refine_hist.number_atoms_total               2317 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1914 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         257 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0087  ? 2467 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0616  ? 3292 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0856  ? 340  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0078  ? 386  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.8221 ? 961  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.13 1.14  . . 2   31   0.88  . . . . 0.2951 . . . . . . . . . . . 0.2565 
'X-RAY DIFFRACTION' 1.14 1.16  . . 6   120  3.41  . . . . 0.3320 . . . . . . . . . . . 0.1784 
'X-RAY DIFFRACTION' 1.16 1.17  . . 15  297  8.26  . . . . 0.3387 . . . . . . . . . . . 0.4533 
'X-RAY DIFFRACTION' 1.17 1.19  . . 33  606  16.89 . . . . 0.3236 . . . . . . . . . . . 0.3006 
'X-RAY DIFFRACTION' 1.19 1.21  . . 47  906  25.16 . . . . 0.3078 . . . . . . . . . . . 0.3350 
'X-RAY DIFFRACTION' 1.21 1.22  . . 69  1296 35.66 . . . . 0.3076 . . . . . . . . . . . 0.3630 
'X-RAY DIFFRACTION' 1.22 1.24  . . 82  1568 43.59 . . . . 0.3078 . . . . . . . . . . . 0.2912 
'X-RAY DIFFRACTION' 1.24 1.26  . . 96  1821 49.86 . . . . 0.2947 . . . . . . . . . . . 0.3094 
'X-RAY DIFFRACTION' 1.26 1.28  . . 111 2095 58.36 . . . . 0.2905 . . . . . . . . . . . 0.3155 
'X-RAY DIFFRACTION' 1.28 1.31  . . 128 2438 67.07 . . . . 0.2847 . . . . . . . . . . . 0.3137 
'X-RAY DIFFRACTION' 1.31 1.33  . . 144 2717 75.03 . . . . 0.2618 . . . . . . . . . . . 0.2837 
'X-RAY DIFFRACTION' 1.33 1.36  . . 157 2960 82.07 . . . . 0.2487 . . . . . . . . . . . 0.2907 
'X-RAY DIFFRACTION' 1.36 1.39  . . 167 3151 87.18 . . . . 0.2346 . . . . . . . . . . . 0.2975 
'X-RAY DIFFRACTION' 1.39 1.42  . . 170 3322 90.98 . . . . 0.2149 . . . . . . . . . . . 0.2869 
'X-RAY DIFFRACTION' 1.42 1.46  . . 205 3427 95.20 . . . . 0.1919 . . . . . . . . . . . 0.2534 
'X-RAY DIFFRACTION' 1.46 1.50  . . 198 3578 98.51 . . . . 0.1653 . . . . . . . . . . . 0.2470 
'X-RAY DIFFRACTION' 1.50 1.54  . . 192 3606 99.01 . . . . 0.1489 . . . . . . . . . . . 0.2301 
'X-RAY DIFFRACTION' 1.54 1.59  . . 201 3585 99.27 . . . . 0.1415 . . . . . . . . . . . 0.1759 
'X-RAY DIFFRACTION' 1.59 1.65  . . 193 3630 99.27 . . . . 0.1338 . . . . . . . . . . . 0.1890 
'X-RAY DIFFRACTION' 1.65 1.71  . . 164 3666 99.35 . . . . 0.1281 . . . . . . . . . . . 0.1866 
'X-RAY DIFFRACTION' 1.71 1.79  . . 165 3657 99.32 . . . . 0.1293 . . . . . . . . . . . 0.1662 
'X-RAY DIFFRACTION' 1.79 1.89  . . 180 3647 99.40 . . . . 0.1162 . . . . . . . . . . . 0.1695 
'X-RAY DIFFRACTION' 1.89 2.00  . . 195 3641 99.20 . . . . 0.1113 . . . . . . . . . . . 0.1541 
'X-RAY DIFFRACTION' 2.00 2.16  . . 179 3664 98.97 . . . . 0.1103 . . . . . . . . . . . 0.1343 
'X-RAY DIFFRACTION' 2.16 2.38  . . 189 3675 98.95 . . . . 0.1164 . . . . . . . . . . . 0.1438 
'X-RAY DIFFRACTION' 2.38 2.72  . . 211 3635 97.89 . . . . 0.1297 . . . . . . . . . . . 0.1597 
'X-RAY DIFFRACTION' 2.72 3.43  . . 183 3650 96.89 . . . . 0.1466 . . . . . . . . . . . 0.1559 
'X-RAY DIFFRACTION' 3.43 33.48 . . 216 3758 95.60 . . . . 0.1747 . . . . . . . . . . . 0.1995 
# 
_struct.entry_id                     9IN7 
_struct.title                        
'True-atomic resolution crystal structure of the closed state of the viral channelrhodopsin OLPVR1' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9IN7 
_struct_keywords.text            'rhodopsin, ChR2, open state, open channel, ChRMine, cation-conducting ChR, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 6 ? 
H N N 6 ? 
I N N 6 ? 
J N N 6 ? 
K N N 6 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
O N N 6 ? 
P N N 7 ? 
Q N N 7 ? 
R N N 7 ? 
S N N 5 ? 
T N N 5 ? 
U N N 5 ? 
V N N 5 ? 
W N N 5 ? 
X N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    F2Y337_9PHYC 
_struct_ref.pdbx_db_accession          F2Y337 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MDNIIMTAYISIFVQIITAIISVYGLFIPLNFKDIILREILILELIVQIIEFIFYIWLIITLQSINEDITYVRYFDWVLT
TPVMLLTTVYFFEYMNSDDGIRKKEINDRDYVYLFYICLSNFFMLLIGYLGETKQINKMLTLFGGSFFLFLTFYLLYVKY
TKENWMNYIVFYFMFLVWFLYGFAFMFPFSIKNQMYNILDIVSKNIYSIFIFIVILNQSYKLL
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9IN7 
_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                 223 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             F2Y337 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  223 
_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       223 
# 
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 9IN7 LEU A 224 ? UNP F2Y337 ? ? 'expression tag' 224 1 
1 9IN7 GLU A 225 ? UNP F2Y337 ? ? 'expression tag' 225 2 
1 9IN7 HIS A 226 ? UNP F2Y337 ? ? 'expression tag' 226 3 
1 9IN7 HIS A 227 ? UNP F2Y337 ? ? 'expression tag' 227 4 
1 9IN7 HIS A 228 ? UNP F2Y337 ? ? 'expression tag' 228 5 
1 9IN7 HIS A 229 ? UNP F2Y337 ? ? 'expression tag' 229 6 
1 9IN7 HIS A 230 ? UNP F2Y337 ? ? 'expression tag' 230 7 
1 9IN7 HIS A 231 ? UNP F2Y337 ? ? 'expression tag' 231 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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_
_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  AA1 FME A 1   ? LEU A 26  ? FME A 1   LEU A 26  1 ? 26 
HELX_P HELX_P2  AA2 ASN A 31  ? LYS A 33  ? ASN A 31  LYS A 33  5 ? 3  
HELX_P HELX_P3  AA3 ASP A 34  ? LEU A 62  ? ASP A 34  LEU A 62  1 ? 29 
HELX_P HELX_P4  AA4 GLN A 63  ? ILE A 65  ? GLN A 63  ILE A 65  5 ? 3  
HELX_P HELX_P5  AA5 ILE A 69  ? TYR A 71  ? ILE A 69  TYR A 71  5 ? 3  
HELX_P HELX_P6  AA6 VAL A 72  ? SER A 97  ? VAL A 72  SER A 97  1 ? 26 
HELX_P HELX_P7  AA7 ARG A 102 ? THR A 133 ? ARG A 102 THR A 133 1 ? 32 
HELX_P HELX_P8  AA8 ASN A 137 ? THR A 161 ? ASN A 137 THR A 161 1 ? 25 
HELX_P HELX_P9  AA9 ASN A 164 ? MET A 186 ? ASN A 164 MET A 186 1 ? 23 
HELX_P HELX_P10 AB1 PRO A 188 ? LYS A 204 ? PRO A 188 LYS A 204 1 ? 17 
HELX_P HELX_P11 AB2 LYS A 204 ? LEU A 224 ? LYS A 204 LEU A 224 1 ? 21 
# 
_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 
covale1 covale both ? A FME 1   C   ? ? ? 1_555 A ASP 2 N   ? ? A FME 1   A ASP 2   1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale2 covale one  ? A LYS 204 NZ  A ? ? 1_555 C RET . C15 A ? A LYS 204 A RET 302 1_555 ? ? ? ? ? ? ? 1.406 ? ? 
covale3 covale one  ? A LYS 204 NZ  B ? ? 1_555 C RET . C15 B ? A LYS 204 A RET 302 1_555 ? ? ? ? ? ? ? 1.419 ? ? 
metalc1 metalc ?    ? A ASP 68  OD2 ? ? ? 1_555 B NA  . NA  A ? A ASP 68  A NA  301 1_555 ? ? ? ? ? ? ? 2.695 ? ? 
metalc2 metalc ?    ? A GLU 132 O   ? ? ? 1_555 B NA  . NA  A ? A GLU 132 A NA  301 1_555 ? ? ? ? ? ? ? 2.548 ? ? 
metalc3 metalc ?    ? A GLU 132 OE2 ? ? ? 1_555 B NA  . NA  A ? A GLU 132 A NA  301 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
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 OD2 ? A ASP 68  ? A ASP 68  ? 1_555 NA A B NA . ? A NA 301 ? 1_555 O   ? A GLU 132 ? A GLU 132 ? 1_555 159.8 ? 
2 OD2 ? A ASP 68  ? A ASP 68  ? 1_555 NA A B NA . ? A NA 301 ? 1_555 OE2 ? A GLU 132 ? A GLU 132 ? 1_555 107.5 ? 
3 O   ? A GLU 132 ? A GLU 132 ? 1_555 NA A B NA . ? A NA 301 ? 1_555 OE2 ? A GLU 132 ? A GLU 132 ? 1_555 88.6  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 FME A 1 ? .   . .   . FME A 1   ? 1_555 .   . .   . .     .   .  MET 1 FME Formylation   'Named protein modification' 
2 RET C . A LYS A 204 A RET A 302 ? 1_555 LYS A 204 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like             
3 RET C . B LYS A 204 B RET A 302 ? 1_555 LYS A 204 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like             
# 
_pdbx_entry_details.entry_id                   9IN7 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              76 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              76 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              76 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                123.95 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            5.65 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    LYS 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     204 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    A 
_pdbx_validate_torsion.phi             -106.88 
_pdbx_validate_torsion.psi             -64.83 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    FME 
_pdbx_struct_mod_residue.label_seq_id     1 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     FME 
_pdbx_struct_mod_residue.auth_seq_id      1 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   MET 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 451 ? X HOH . 
2 1 A HOH 536 ? X HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x+1/2,y+1/2,-z 
4 -x,-y,z         
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       546 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.21 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 GLU 225 ? A GLU 225 
2 1 Y 1 A HIS 226 ? A HIS 226 
3 1 Y 1 A HIS 227 ? A HIS 227 
4 1 Y 1 A HIS 228 ? A HIS 228 
5 1 Y 1 A HIS 229 ? A HIS 229 
6 1 Y 1 A HIS 230 ? A HIS 230 
7 1 Y 1 A HIS 231 ? A HIS 231 
# 
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 
97N C    C  N N 1   
97N O    O  N N 2   
97N C1   C  N N 3   
97N O1   O  N N 4   
97N C2   C  N N 5   
97N O2   O  N N 6   
97N C3   C  N N 7   
97N O3   O  N N 8   
97N C4   C  N N 9   
97N C5   C  N N 10  
97N C6   C  N N 11  
97N C7   C  N N 12  
97N C8   C  N N 13  
97N C9   C  N N 14  
97N C10  C  N N 15  
97N C11  C  N N 16  
97N C12  C  N N 17  
97N C13  C  N N 18  
97N C14  C  N N 19  
97N C15  C  N N 20  
97N C16  C  N N 21  
97N C17  C  N S 22  
97N C18  C  N N 23  
97N H1   H  N N 24  
97N H2   H  N N 25  
97N H3   H  N N 26  
97N H4   H  N N 27  
97N H5   H  N N 28  
97N H6   H  N N 29  
97N H7   H  N N 30  
97N H8   H  N N 31  
97N H9   H  N N 32  
97N H10  H  N N 33  
97N H11  H  N N 34  
97N H12  H  N N 35  
97N H13  H  N N 36  
97N H14  H  N N 37  
97N H15  H  N N 38  
97N H16  H  N N 39  
97N H17  H  N N 40  
97N H18  H  N N 41  
97N H19  H  N N 42  
97N H20  H  N N 43  
97N H21  H  N N 44  
97N H22  H  N N 45  
97N H23  H  N N 46  
97N H24  H  N N 47  
97N H25  H  N N 48  
97N H26  H  N N 49  
97N H27  H  N N 50  
97N H28  H  N N 51  
97N H29  H  N N 52  
97N H30  H  N N 53  
97N H31  H  N N 54  
97N H32  H  N N 55  
97N H33  H  N N 56  
97N H34  H  N N 57  
97N H35  H  N N 58  
97N H36  H  N N 59  
ALA N    N  N N 60  
ALA CA   C  N S 61  
ALA C    C  N N 62  
ALA O    O  N N 63  
ALA CB   C  N N 64  
ALA OXT  O  N N 65  
ALA H    H  N N 66  
ALA H2   H  N N 67  
ALA HA   H  N N 68  
ALA HB1  H  N N 69  
ALA HB2  H  N N 70  
ALA HB3  H  N N 71  
ALA HXT  H  N N 72  
ARG N    N  N N 73  
ARG CA   C  N S 74  
ARG C    C  N N 75  
ARG O    O  N N 76  
ARG CB   C  N N 77  
ARG CG   C  N N 78  
ARG CD   C  N N 79  
ARG NE   N  N N 80  
ARG CZ   C  N N 81  
ARG NH1  N  N N 82  
ARG NH2  N  N N 83  
ARG OXT  O  N N 84  
ARG H    H  N N 85  
ARG H2   H  N N 86  
ARG HA   H  N N 87  
ARG HB2  H  N N 88  
ARG HB3  H  N N 89  
ARG HG2  H  N N 90  
ARG HG3  H  N N 91  
ARG HD2  H  N N 92  
ARG HD3  H  N N 93  
ARG HE   H  N N 94  
ARG HH11 H  N N 95  
ARG HH12 H  N N 96  
ARG HH21 H  N N 97  
ARG HH22 H  N N 98  
ARG HXT  H  N N 99  
ASN N    N  N N 100 
ASN CA   C  N S 101 
ASN C    C  N N 102 
ASN O    O  N N 103 
ASN CB   C  N N 104 
ASN CG   C  N N 105 
ASN OD1  O  N N 106 
ASN ND2  N  N N 107 
ASN OXT  O  N N 108 
ASN H    H  N N 109 
ASN H2   H  N N 110 
ASN HA   H  N N 111 
ASN HB2  H  N N 112 
ASN HB3  H  N N 113 
ASN HD21 H  N N 114 
ASN HD22 H  N N 115 
ASN HXT  H  N N 116 
ASP N    N  N N 117 
ASP CA   C  N S 118 
ASP C    C  N N 119 
ASP O    O  N N 120 
ASP CB   C  N N 121 
ASP CG   C  N N 122 
ASP OD1  O  N N 123 
ASP OD2  O  N N 124 
ASP OXT  O  N N 125 
ASP H    H  N N 126 
ASP H2   H  N N 127 
ASP HA   H  N N 128 
ASP HB2  H  N N 129 
ASP HB3  H  N N 130 
ASP HD2  H  N N 131 
ASP HXT  H  N N 132 
CYS N    N  N N 133 
CYS CA   C  N R 134 
CYS C    C  N N 135 
CYS O    O  N N 136 
CYS CB   C  N N 137 
CYS SG   S  N N 138 
CYS OXT  O  N N 139 
CYS H    H  N N 140 
CYS H2   H  N N 141 
CYS HA   H  N N 142 
CYS HB2  H  N N 143 
CYS HB3  H  N N 144 
CYS HG   H  N N 145 
CYS HXT  H  N N 146 
FME N    N  N N 147 
FME CN   C  N N 148 
FME O1   O  N N 149 
FME CA   C  N S 150 
FME CB   C  N N 151 
FME CG   C  N N 152 
FME SD   S  N N 153 
FME CE   C  N N 154 
FME C    C  N N 155 
FME O    O  N N 156 
FME OXT  O  N N 157 
FME H    H  N N 158 
FME HCN  H  N N 159 
FME HA   H  N N 160 
FME HB2  H  N N 161 
FME HB3  H  N N 162 
FME HG2  H  N N 163 
FME HG3  H  N N 164 
FME HE1  H  N N 165 
FME HE2  H  N N 166 
FME HE3  H  N N 167 
FME HXT  H  N N 168 
GLN N    N  N N 169 
GLN CA   C  N S 170 
GLN C    C  N N 171 
GLN O    O  N N 172 
GLN CB   C  N N 173 
GLN CG   C  N N 174 
GLN CD   C  N N 175 
GLN OE1  O  N N 176 
GLN NE2  N  N N 177 
GLN OXT  O  N N 178 
GLN H    H  N N 179 
GLN H2   H  N N 180 
GLN HA   H  N N 181 
GLN HB2  H  N N 182 
GLN HB3  H  N N 183 
GLN HG2  H  N N 184 
GLN HG3  H  N N 185 
GLN HE21 H  N N 186 
GLN HE22 H  N N 187 
GLN HXT  H  N N 188 
GLU N    N  N N 189 
GLU CA   C  N S 190 
GLU C    C  N N 191 
GLU O    O  N N 192 
GLU CB   C  N N 193 
GLU CG   C  N N 194 
GLU CD   C  N N 195 
GLU OE1  O  N N 196 
GLU OE2  O  N N 197 
GLU OXT  O  N N 198 
GLU H    H  N N 199 
GLU H2   H  N N 200 
GLU HA   H  N N 201 
GLU HB2  H  N N 202 
GLU HB3  H  N N 203 
GLU HG2  H  N N 204 
GLU HG3  H  N N 205 
GLU HE2  H  N N 206 
GLU HXT  H  N N 207 
GLY N    N  N N 208 
GLY CA   C  N N 209 
GLY C    C  N N 210 
GLY O    O  N N 211 
GLY OXT  O  N N 212 
GLY H    H  N N 213 
GLY H2   H  N N 214 
GLY HA2  H  N N 215 
GLY HA3  H  N N 216 
GLY HXT  H  N N 217 
GOL C1   C  N N 218 
GOL O1   O  N N 219 
GOL C2   C  N N 220 
GOL O2   O  N N 221 
GOL C3   C  N N 222 
GOL O3   O  N N 223 
GOL H11  H  N N 224 
GOL H12  H  N N 225 
GOL HO1  H  N N 226 
GOL H2   H  N N 227 
GOL HO2  H  N N 228 
GOL H31  H  N N 229 
GOL H32  H  N N 230 
GOL HO3  H  N N 231 
HIS N    N  N N 232 
HIS CA   C  N S 233 
HIS C    C  N N 234 
HIS O    O  N N 235 
HIS CB   C  N N 236 
HIS CG   C  Y N 237 
HIS ND1  N  Y N 238 
HIS CD2  C  Y N 239 
HIS CE1  C  Y N 240 
HIS NE2  N  Y N 241 
HIS OXT  O  N N 242 
HIS H    H  N N 243 
HIS H2   H  N N 244 
HIS HA   H  N N 245 
HIS HB2  H  N N 246 
HIS HB3  H  N N 247 
HIS HD1  H  N N 248 
HIS HD2  H  N N 249 
HIS HE1  H  N N 250 
HIS HE2  H  N N 251 
HIS HXT  H  N N 252 
HOH O    O  N N 253 
HOH H1   H  N N 254 
HOH H2   H  N N 255 
ILE N    N  N N 256 
ILE CA   C  N S 257 
ILE C    C  N N 258 
ILE O    O  N N 259 
ILE CB   C  N S 260 
ILE CG1  C  N N 261 
ILE CG2  C  N N 262 
ILE CD1  C  N N 263 
ILE OXT  O  N N 264 
ILE H    H  N N 265 
ILE H2   H  N N 266 
ILE HA   H  N N 267 
ILE HB   H  N N 268 
ILE HG12 H  N N 269 
ILE HG13 H  N N 270 
ILE HG21 H  N N 271 
ILE HG22 H  N N 272 
ILE HG23 H  N N 273 
ILE HD11 H  N N 274 
ILE HD12 H  N N 275 
ILE HD13 H  N N 276 
ILE HXT  H  N N 277 
LEU N    N  N N 278 
LEU CA   C  N S 279 
LEU C    C  N N 280 
LEU O    O  N N 281 
LEU CB   C  N N 282 
LEU CG   C  N N 283 
LEU CD1  C  N N 284 
LEU CD2  C  N N 285 
LEU OXT  O  N N 286 
LEU H    H  N N 287 
LEU H2   H  N N 288 
LEU HA   H  N N 289 
LEU HB2  H  N N 290 
LEU HB3  H  N N 291 
LEU HG   H  N N 292 
LEU HD11 H  N N 293 
LEU HD12 H  N N 294 
LEU HD13 H  N N 295 
LEU HD21 H  N N 296 
LEU HD22 H  N N 297 
LEU HD23 H  N N 298 
LEU HXT  H  N N 299 
LFA C1   C  N N 300 
LFA C2   C  N N 301 
LFA C3   C  N N 302 
LFA C4   C  N N 303 
LFA C5   C  N N 304 
LFA C6   C  N N 305 
LFA C7   C  N N 306 
LFA C8   C  N N 307 
LFA C9   C  N N 308 
LFA C10  C  N N 309 
LFA C11  C  N N 310 
LFA C12  C  N N 311 
LFA C13  C  N N 312 
LFA C14  C  N N 313 
LFA C15  C  N N 314 
LFA C16  C  N N 315 
LFA C17  C  N N 316 
LFA C18  C  N N 317 
LFA C19  C  N N 318 
LFA C20  C  N N 319 
LFA H11  H  N N 320 
LFA H12  H  N N 321 
LFA H13  H  N N 322 
LFA H21  H  N N 323 
LFA H22  H  N N 324 
LFA H31  H  N N 325 
LFA H32  H  N N 326 
LFA H41  H  N N 327 
LFA H42  H  N N 328 
LFA H51  H  N N 329 
LFA H52  H  N N 330 
LFA H61  H  N N 331 
LFA H62  H  N N 332 
LFA H71  H  N N 333 
LFA H72  H  N N 334 
LFA H81  H  N N 335 
LFA H82  H  N N 336 
LFA H91  H  N N 337 
LFA H92  H  N N 338 
LFA H101 H  N N 339 
LFA H102 H  N N 340 
LFA H111 H  N N 341 
LFA H112 H  N N 342 
LFA H121 H  N N 343 
LFA H122 H  N N 344 
LFA H131 H  N N 345 
LFA H132 H  N N 346 
LFA H141 H  N N 347 
LFA H142 H  N N 348 
LFA H151 H  N N 349 
LFA H152 H  N N 350 
LFA H161 H  N N 351 
LFA H162 H  N N 352 
LFA H171 H  N N 353 
LFA H172 H  N N 354 
LFA H181 H  N N 355 
LFA H182 H  N N 356 
LFA H191 H  N N 357 
LFA H192 H  N N 358 
LFA H201 H  N N 359 
LFA H202 H  N N 360 
LFA H203 H  N N 361 
LYS N    N  N N 362 
LYS CA   C  N S 363 
LYS C    C  N N 364 
LYS O    O  N N 365 
LYS CB   C  N N 366 
LYS CG   C  N N 367 
LYS CD   C  N N 368 
LYS CE   C  N N 369 
LYS NZ   N  N N 370 
LYS OXT  O  N N 371 
LYS H    H  N N 372 
LYS H2   H  N N 373 
LYS HA   H  N N 374 
LYS HB2  H  N N 375 
LYS HB3  H  N N 376 
LYS HG2  H  N N 377 
LYS HG3  H  N N 378 
LYS HD2  H  N N 379 
LYS HD3  H  N N 380 
LYS HE2  H  N N 381 
LYS HE3  H  N N 382 
LYS HZ1  H  N N 383 
LYS HZ2  H  N N 384 
LYS HZ3  H  N N 385 
LYS HXT  H  N N 386 
MET N    N  N N 387 
MET CA   C  N S 388 
MET C    C  N N 389 
MET O    O  N N 390 
MET CB   C  N N 391 
MET CG   C  N N 392 
MET SD   S  N N 393 
MET CE   C  N N 394 
MET OXT  O  N N 395 
MET H    H  N N 396 
MET H2   H  N N 397 
MET HA   H  N N 398 
MET HB2  H  N N 399 
MET HB3  H  N N 400 
MET HG2  H  N N 401 
MET HG3  H  N N 402 
MET HE1  H  N N 403 
MET HE2  H  N N 404 
MET HE3  H  N N 405 
MET HXT  H  N N 406 
NA  NA   NA N N 407 
OLC C18  C  N N 408 
OLC C10  C  N N 409 
OLC C9   C  N N 410 
OLC C17  C  N N 411 
OLC C11  C  N N 412 
OLC C8   C  N N 413 
OLC C24  C  N N 414 
OLC C16  C  N N 415 
OLC C12  C  N N 416 
OLC C7   C  N N 417 
OLC C15  C  N N 418 
OLC C13  C  N N 419 
OLC C6   C  N N 420 
OLC C14  C  N N 421 
OLC C5   C  N N 422 
OLC C4   C  N N 423 
OLC C3   C  N N 424 
OLC C2   C  N N 425 
OLC C21  C  N N 426 
OLC C1   C  N N 427 
OLC C22  C  N R 428 
OLC O19  O  N N 429 
OLC O25  O  N N 430 
OLC O23  O  N N 431 
OLC O20  O  N N 432 
OLC H18  H  N N 433 
OLC H18A H  N N 434 
OLC H18B H  N N 435 
OLC H10  H  N N 436 
OLC H9   H  N N 437 
OLC H17  H  N N 438 
OLC H17A H  N N 439 
OLC H11  H  N N 440 
OLC H11A H  N N 441 
OLC H8   H  N N 442 
OLC H8A  H  N N 443 
OLC H24  H  N N 444 
OLC H24A H  N N 445 
OLC H16  H  N N 446 
OLC H16A H  N N 447 
OLC H12  H  N N 448 
OLC H12A H  N N 449 
OLC H7   H  N N 450 
OLC H7A  H  N N 451 
OLC H15  H  N N 452 
OLC H15A H  N N 453 
OLC H13  H  N N 454 
OLC H13A H  N N 455 
OLC H6   H  N N 456 
OLC H6A  H  N N 457 
OLC H14  H  N N 458 
OLC H14A H  N N 459 
OLC H5   H  N N 460 
OLC H5A  H  N N 461 
OLC H4   H  N N 462 
OLC H4A  H  N N 463 
OLC H3   H  N N 464 
OLC H3A  H  N N 465 
OLC H2   H  N N 466 
OLC H2A  H  N N 467 
OLC H21  H  N N 468 
OLC H21A H  N N 469 
OLC H22  H  N N 470 
OLC HO25 H  N N 471 
OLC HO23 H  N N 472 
PHE N    N  N N 473 
PHE CA   C  N S 474 
PHE C    C  N N 475 
PHE O    O  N N 476 
PHE CB   C  N N 477 
PHE CG   C  Y N 478 
PHE CD1  C  Y N 479 
PHE CD2  C  Y N 480 
PHE CE1  C  Y N 481 
PHE CE2  C  Y N 482 
PHE CZ   C  Y N 483 
PHE OXT  O  N N 484 
PHE H    H  N N 485 
PHE H2   H  N N 486 
PHE HA   H  N N 487 
PHE HB2  H  N N 488 
PHE HB3  H  N N 489 
PHE HD1  H  N N 490 
PHE HD2  H  N N 491 
PHE HE1  H  N N 492 
PHE HE2  H  N N 493 
PHE HZ   H  N N 494 
PHE HXT  H  N N 495 
PRO N    N  N N 496 
PRO CA   C  N S 497 
PRO C    C  N N 498 
PRO O    O  N N 499 
PRO CB   C  N N 500 
PRO CG   C  N N 501 
PRO CD   C  N N 502 
PRO OXT  O  N N 503 
PRO H    H  N N 504 
PRO HA   H  N N 505 
PRO HB2  H  N N 506 
PRO HB3  H  N N 507 
PRO HG2  H  N N 508 
PRO HG3  H  N N 509 
PRO HD2  H  N N 510 
PRO HD3  H  N N 511 
PRO HXT  H  N N 512 
RET C1   C  N N 513 
RET C2   C  N N 514 
RET C3   C  N N 515 
RET C4   C  N N 516 
RET C5   C  N N 517 
RET C6   C  N N 518 
RET C7   C  N N 519 
RET C8   C  N N 520 
RET C9   C  N N 521 
RET C10  C  N N 522 
RET C11  C  N N 523 
RET C12  C  N N 524 
RET C13  C  N N 525 
RET C14  C  N N 526 
RET C15  C  N N 527 
RET O1   O  N N 528 
RET C16  C  N N 529 
RET C17  C  N N 530 
RET C18  C  N N 531 
RET C19  C  N N 532 
RET C20  C  N N 533 
RET H21  H  N N 534 
RET H22  H  N N 535 
RET H31  H  N N 536 
RET H32  H  N N 537 
RET H41  H  N N 538 
RET H42  H  N N 539 
RET H7   H  N N 540 
RET H8   H  N N 541 
RET H10  H  N N 542 
RET H11  H  N N 543 
RET H12  H  N N 544 
RET H14  H  N N 545 
RET H15  H  N N 546 
RET H161 H  N N 547 
RET H162 H  N N 548 
RET H163 H  N N 549 
RET H171 H  N N 550 
RET H172 H  N N 551 
RET H173 H  N N 552 
RET H181 H  N N 553 
RET H182 H  N N 554 
RET H183 H  N N 555 
RET H191 H  N N 556 
RET H192 H  N N 557 
RET H193 H  N N 558 
RET H201 H  N N 559 
RET H202 H  N N 560 
RET H203 H  N N 561 
SER N    N  N N 562 
SER CA   C  N S 563 
SER C    C  N N 564 
SER O    O  N N 565 
SER CB   C  N N 566 
SER OG   O  N N 567 
SER OXT  O  N N 568 
SER H    H  N N 569 
SER H2   H  N N 570 
SER HA   H  N N 571 
SER HB2  H  N N 572 
SER HB3  H  N N 573 
SER HG   H  N N 574 
SER HXT  H  N N 575 
THR N    N  N N 576 
THR CA   C  N S 577 
THR C    C  N N 578 
THR O    O  N N 579 
THR CB   C  N R 580 
THR OG1  O  N N 581 
THR CG2  C  N N 582 
THR OXT  O  N N 583 
THR H    H  N N 584 
THR H2   H  N N 585 
THR HA   H  N N 586 
THR HB   H  N N 587 
THR HG1  H  N N 588 
THR HG21 H  N N 589 
THR HG22 H  N N 590 
THR HG23 H  N N 591 
THR HXT  H  N N 592 
TRP N    N  N N 593 
TRP CA   C  N S 594 
TRP C    C  N N 595 
TRP O    O  N N 596 
TRP CB   C  N N 597 
TRP CG   C  Y N 598 
TRP CD1  C  Y N 599 
TRP CD2  C  Y N 600 
TRP NE1  N  Y N 601 
TRP CE2  C  Y N 602 
TRP CE3  C  Y N 603 
TRP CZ2  C  Y N 604 
TRP CZ3  C  Y N 605 
TRP CH2  C  Y N 606 
TRP OXT  O  N N 607 
TRP H    H  N N 608 
TRP H2   H  N N 609 
TRP HA   H  N N 610 
TRP HB2  H  N N 611 
TRP HB3  H  N N 612 
TRP HD1  H  N N 613 
TRP HE1  H  N N 614 
TRP HE3  H  N N 615 
TRP HZ2  H  N N 616 
TRP HZ3  H  N N 617 
TRP HH2  H  N N 618 
TRP HXT  H  N N 619 
TYR N    N  N N 620 
TYR CA   C  N S 621 
TYR C    C  N N 622 
TYR O    O  N N 623 
TYR CB   C  N N 624 
TYR CG   C  Y N 625 
TYR CD1  C  Y N 626 
TYR CD2  C  Y N 627 
TYR CE1  C  Y N 628 
TYR CE2  C  Y N 629 
TYR CZ   C  Y N 630 
TYR OH   O  N N 631 
TYR OXT  O  N N 632 
TYR H    H  N N 633 
TYR H2   H  N N 634 
TYR HA   H  N N 635 
TYR HB2  H  N N 636 
TYR HB3  H  N N 637 
TYR HD1  H  N N 638 
TYR HD2  H  N N 639 
TYR HE1  H  N N 640 
TYR HE2  H  N N 641 
TYR HH   H  N N 642 
TYR HXT  H  N N 643 
VAL N    N  N N 644 
VAL CA   C  N S 645 
VAL C    C  N N 646 
VAL O    O  N N 647 
VAL CB   C  N N 648 
VAL CG1  C  N N 649 
VAL CG2  C  N N 650 
VAL OXT  O  N N 651 
VAL H    H  N N 652 
VAL H2   H  N N 653 
VAL HA   H  N N 654 
VAL HB   H  N N 655 
VAL HG11 H  N N 656 
VAL HG12 H  N N 657 
VAL HG13 H  N N 658 
VAL HG21 H  N N 659 
VAL HG22 H  N N 660 
VAL HG23 H  N N 661 
VAL HXT  H  N N 662 
# 
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 
97N C   C1   sing N N 1   
97N C1  C2   sing N N 2   
97N C2  C3   sing N N 3   
97N C3  C4   sing N N 4   
97N C4  C5   sing N N 5   
97N C5  C6   sing N N 6   
97N C6  C7   doub N Z 7   
97N C7  C8   sing N N 8   
97N C8  C9   sing N N 9   
97N C9  C10  sing N N 10  
97N C10 C11  sing N N 11  
97N C11 C12  sing N N 12  
97N C12 C13  sing N N 13  
97N C13 C14  sing N N 14  
97N C14 C15  sing N N 15  
97N O   C15  doub N N 16  
97N C15 O1   sing N N 17  
97N O1  C16  sing N N 18  
97N O2  C17  sing N N 19  
97N C16 C17  sing N N 20  
97N C17 C18  sing N N 21  
97N C18 O3   sing N N 22  
97N C   H1   sing N N 23  
97N C   H2   sing N N 24  
97N C   H3   sing N N 25  
97N C1  H4   sing N N 26  
97N C1  H5   sing N N 27  
97N C2  H6   sing N N 28  
97N C2  H7   sing N N 29  
97N O2  H8   sing N N 30  
97N C3  H9   sing N N 31  
97N C3  H10  sing N N 32  
97N O3  H11  sing N N 33  
97N C4  H12  sing N N 34  
97N C4  H13  sing N N 35  
97N C5  H14  sing N N 36  
97N C5  H15  sing N N 37  
97N C6  H16  sing N N 38  
97N C7  H17  sing N N 39  
97N C8  H18  sing N N 40  
97N C8  H19  sing N N 41  
97N C9  H20  sing N N 42  
97N C9  H21  sing N N 43  
97N C10 H22  sing N N 44  
97N C10 H23  sing N N 45  
97N C11 H24  sing N N 46  
97N C11 H25  sing N N 47  
97N C12 H26  sing N N 48  
97N C12 H27  sing N N 49  
97N C13 H28  sing N N 50  
97N C13 H29  sing N N 51  
97N C14 H30  sing N N 52  
97N C14 H31  sing N N 53  
97N C16 H32  sing N N 54  
97N C16 H33  sing N N 55  
97N C17 H34  sing N N 56  
97N C18 H35  sing N N 57  
97N C18 H36  sing N N 58  
ALA N   CA   sing N N 59  
ALA N   H    sing N N 60  
ALA N   H2   sing N N 61  
ALA CA  C    sing N N 62  
ALA CA  CB   sing N N 63  
ALA CA  HA   sing N N 64  
ALA C   O    doub N N 65  
ALA C   OXT  sing N N 66  
ALA CB  HB1  sing N N 67  
ALA CB  HB2  sing N N 68  
ALA CB  HB3  sing N N 69  
ALA OXT HXT  sing N N 70  
ARG N   CA   sing N N 71  
ARG N   H    sing N N 72  
ARG N   H2   sing N N 73  
ARG CA  C    sing N N 74  
ARG CA  CB   sing N N 75  
ARG CA  HA   sing N N 76  
ARG C   O    doub N N 77  
ARG C   OXT  sing N N 78  
ARG CB  CG   sing N N 79  
ARG CB  HB2  sing N N 80  
ARG CB  HB3  sing N N 81  
ARG CG  CD   sing N N 82  
ARG CG  HG2  sing N N 83  
ARG CG  HG3  sing N N 84  
ARG CD  NE   sing N N 85  
ARG CD  HD2  sing N N 86  
ARG CD  HD3  sing N N 87  
ARG NE  CZ   sing N N 88  
ARG NE  HE   sing N N 89  
ARG CZ  NH1  sing N N 90  
ARG CZ  NH2  doub N N 91  
ARG NH1 HH11 sing N N 92  
ARG NH1 HH12 sing N N 93  
ARG NH2 HH21 sing N N 94  
ARG NH2 HH22 sing N N 95  
ARG OXT HXT  sing N N 96  
ASN N   CA   sing N N 97  
ASN N   H    sing N N 98  
ASN N   H2   sing N N 99  
ASN CA  C    sing N N 100 
ASN CA  CB   sing N N 101 
ASN CA  HA   sing N N 102 
ASN C   O    doub N N 103 
ASN C   OXT  sing N N 104 
ASN CB  CG   sing N N 105 
ASN CB  HB2  sing N N 106 
ASN CB  HB3  sing N N 107 
ASN CG  OD1  doub N N 108 
ASN CG  ND2  sing N N 109 
ASN ND2 HD21 sing N N 110 
ASN ND2 HD22 sing N N 111 
ASN OXT HXT  sing N N 112 
ASP N   CA   sing N N 113 
ASP N   H    sing N N 114 
ASP N   H2   sing N N 115 
ASP CA  C    sing N N 116 
ASP CA  CB   sing N N 117 
ASP CA  HA   sing N N 118 
ASP C   O    doub N N 119 
ASP C   OXT  sing N N 120 
ASP CB  CG   sing N N 121 
ASP CB  HB2  sing N N 122 
ASP CB  HB3  sing N N 123 
ASP CG  OD1  doub N N 124 
ASP CG  OD2  sing N N 125 
ASP OD2 HD2  sing N N 126 
ASP OXT HXT  sing N N 127 
CYS N   CA   sing N N 128 
CYS N   H    sing N N 129 
CYS N   H2   sing N N 130 
CYS CA  C    sing N N 131 
CYS CA  CB   sing N N 132 
CYS CA  HA   sing N N 133 
CYS C   O    doub N N 134 
CYS C   OXT  sing N N 135 
CYS CB  SG   sing N N 136 
CYS CB  HB2  sing N N 137 
CYS CB  HB3  sing N N 138 
CYS SG  HG   sing N N 139 
CYS OXT HXT  sing N N 140 
FME N   CN   sing N N 141 
FME N   CA   sing N N 142 
FME N   H    sing N N 143 
FME CN  O1   doub N N 144 
FME CN  HCN  sing N N 145 
FME CA  CB   sing N N 146 
FME CA  C    sing N N 147 
FME CA  HA   sing N N 148 
FME CB  CG   sing N N 149 
FME CB  HB2  sing N N 150 
FME CB  HB3  sing N N 151 
FME CG  SD   sing N N 152 
FME CG  HG2  sing N N 153 
FME CG  HG3  sing N N 154 
FME SD  CE   sing N N 155 
FME CE  HE1  sing N N 156 
FME CE  HE2  sing N N 157 
FME CE  HE3  sing N N 158 
FME C   O    doub N N 159 
FME C   OXT  sing N N 160 
FME OXT HXT  sing N N 161 
GLN N   CA   sing N N 162 
GLN N   H    sing N N 163 
GLN N   H2   sing N N 164 
GLN CA  C    sing N N 165 
GLN CA  CB   sing N N 166 
GLN CA  HA   sing N N 167 
GLN C   O    doub N N 168 
GLN C   OXT  sing N N 169 
GLN CB  CG   sing N N 170 
GLN CB  HB2  sing N N 171 
GLN CB  HB3  sing N N 172 
GLN CG  CD   sing N N 173 
GLN CG  HG2  sing N N 174 
GLN CG  HG3  sing N N 175 
GLN CD  OE1  doub N N 176 
GLN CD  NE2  sing N N 177 
GLN NE2 HE21 sing N N 178 
GLN NE2 HE22 sing N N 179 
GLN OXT HXT  sing N N 180 
GLU N   CA   sing N N 181 
GLU N   H    sing N N 182 
GLU N   H2   sing N N 183 
GLU CA  C    sing N N 184 
GLU CA  CB   sing N N 185 
GLU CA  HA   sing N N 186 
GLU C   O    doub N N 187 
GLU C   OXT  sing N N 188 
GLU CB  CG   sing N N 189 
GLU CB  HB2  sing N N 190 
GLU CB  HB3  sing N N 191 
GLU CG  CD   sing N N 192 
GLU CG  HG2  sing N N 193 
GLU CG  HG3  sing N N 194 
GLU CD  OE1  doub N N 195 
GLU CD  OE2  sing N N 196 
GLU OE2 HE2  sing N N 197 
GLU OXT HXT  sing N N 198 
GLY N   CA   sing N N 199 
GLY N   H    sing N N 200 
GLY N   H2   sing N N 201 
GLY CA  C    sing N N 202 
GLY CA  HA2  sing N N 203 
GLY CA  HA3  sing N N 204 
GLY C   O    doub N N 205 
GLY C   OXT  sing N N 206 
GLY OXT HXT  sing N N 207 
GOL C1  O1   sing N N 208 
GOL C1  C2   sing N N 209 
GOL C1  H11  sing N N 210 
GOL C1  H12  sing N N 211 
GOL O1  HO1  sing N N 212 
GOL C2  O2   sing N N 213 
GOL C2  C3   sing N N 214 
GOL C2  H2   sing N N 215 
GOL O2  HO2  sing N N 216 
GOL C3  O3   sing N N 217 
GOL C3  H31  sing N N 218 
GOL C3  H32  sing N N 219 
GOL O3  HO3  sing N N 220 
HIS N   CA   sing N N 221 
HIS N   H    sing N N 222 
HIS N   H2   sing N N 223 
HIS CA  C    sing N N 224 
HIS CA  CB   sing N N 225 
HIS CA  HA   sing N N 226 
HIS C   O    doub N N 227 
HIS C   OXT  sing N N 228 
HIS CB  CG   sing N N 229 
HIS CB  HB2  sing N N 230 
HIS CB  HB3  sing N N 231 
HIS CG  ND1  sing Y N 232 
HIS CG  CD2  doub Y N 233 
HIS ND1 CE1  doub Y N 234 
HIS ND1 HD1  sing N N 235 
HIS CD2 NE2  sing Y N 236 
HIS CD2 HD2  sing N N 237 
HIS CE1 NE2  sing Y N 238 
HIS CE1 HE1  sing N N 239 
HIS NE2 HE2  sing N N 240 
HIS OXT HXT  sing N N 241 
HOH O   H1   sing N N 242 
HOH O   H2   sing N N 243 
ILE N   CA   sing N N 244 
ILE N   H    sing N N 245 
ILE N   H2   sing N N 246 
ILE CA  C    sing N N 247 
ILE CA  CB   sing N N 248 
ILE CA  HA   sing N N 249 
ILE C   O    doub N N 250 
ILE C   OXT  sing N N 251 
ILE CB  CG1  sing N N 252 
ILE CB  CG2  sing N N 253 
ILE CB  HB   sing N N 254 
ILE CG1 CD1  sing N N 255 
ILE CG1 HG12 sing N N 256 
ILE CG1 HG13 sing N N 257 
ILE CG2 HG21 sing N N 258 
ILE CG2 HG22 sing N N 259 
ILE CG2 HG23 sing N N 260 
ILE CD1 HD11 sing N N 261 
ILE CD1 HD12 sing N N 262 
ILE CD1 HD13 sing N N 263 
ILE OXT HXT  sing N N 264 
LEU N   CA   sing N N 265 
LEU N   H    sing N N 266 
LEU N   H2   sing N N 267 
LEU CA  C    sing N N 268 
LEU CA  CB   sing N N 269 
LEU CA  HA   sing N N 270 
LEU C   O    doub N N 271 
LEU C   OXT  sing N N 272 
LEU CB  CG   sing N N 273 
LEU CB  HB2  sing N N 274 
LEU CB  HB3  sing N N 275 
LEU CG  CD1  sing N N 276 
LEU CG  CD2  sing N N 277 
LEU CG  HG   sing N N 278 
LEU CD1 HD11 sing N N 279 
LEU CD1 HD12 sing N N 280 
LEU CD1 HD13 sing N N 281 
LEU CD2 HD21 sing N N 282 
LEU CD2 HD22 sing N N 283 
LEU CD2 HD23 sing N N 284 
LEU OXT HXT  sing N N 285 
LFA C1  C2   sing N N 286 
LFA C1  H11  sing N N 287 
LFA C1  H12  sing N N 288 
LFA C1  H13  sing N N 289 
LFA C2  C3   sing N N 290 
LFA C2  H21  sing N N 291 
LFA C2  H22  sing N N 292 
LFA C3  C4   sing N N 293 
LFA C3  H31  sing N N 294 
LFA C3  H32  sing N N 295 
LFA C4  C5   sing N N 296 
LFA C4  H41  sing N N 297 
LFA C4  H42  sing N N 298 
LFA C5  C6   sing N N 299 
LFA C5  H51  sing N N 300 
LFA C5  H52  sing N N 301 
LFA C6  C7   sing N N 302 
LFA C6  H61  sing N N 303 
LFA C6  H62  sing N N 304 
LFA C7  C8   sing N N 305 
LFA C7  H71  sing N N 306 
LFA C7  H72  sing N N 307 
LFA C8  C9   sing N N 308 
LFA C8  H81  sing N N 309 
LFA C8  H82  sing N N 310 
LFA C9  C10  sing N N 311 
LFA C9  H91  sing N N 312 
LFA C9  H92  sing N N 313 
LFA C10 C11  sing N N 314 
LFA C10 H101 sing N N 315 
LFA C10 H102 sing N N 316 
LFA C11 C12  sing N N 317 
LFA C11 H111 sing N N 318 
LFA C11 H112 sing N N 319 
LFA C12 C13  sing N N 320 
LFA C12 H121 sing N N 321 
LFA C12 H122 sing N N 322 
LFA C13 C14  sing N N 323 
LFA C13 H131 sing N N 324 
LFA C13 H132 sing N N 325 
LFA C14 C15  sing N N 326 
LFA C14 H141 sing N N 327 
LFA C14 H142 sing N N 328 
LFA C15 C16  sing N N 329 
LFA C15 H151 sing N N 330 
LFA C15 H152 sing N N 331 
LFA C16 C17  sing N N 332 
LFA C16 H161 sing N N 333 
LFA C16 H162 sing N N 334 
LFA C17 C18  sing N N 335 
LFA C17 H171 sing N N 336 
LFA C17 H172 sing N N 337 
LFA C18 C19  sing N N 338 
LFA C18 H181 sing N N 339 
LFA C18 H182 sing N N 340 
LFA C19 C20  sing N N 341 
LFA C19 H191 sing N N 342 
LFA C19 H192 sing N N 343 
LFA C20 H201 sing N N 344 
LFA C20 H202 sing N N 345 
LFA C20 H203 sing N N 346 
LYS N   CA   sing N N 347 
LYS N   H    sing N N 348 
LYS N   H2   sing N N 349 
LYS CA  C    sing N N 350 
LYS CA  CB   sing N N 351 
LYS CA  HA   sing N N 352 
LYS C   O    doub N N 353 
LYS C   OXT  sing N N 354 
LYS CB  CG   sing N N 355 
LYS CB  HB2  sing N N 356 
LYS CB  HB3  sing N N 357 
LYS CG  CD   sing N N 358 
LYS CG  HG2  sing N N 359 
LYS CG  HG3  sing N N 360 
LYS CD  CE   sing N N 361 
LYS CD  HD2  sing N N 362 
LYS CD  HD3  sing N N 363 
LYS CE  NZ   sing N N 364 
LYS CE  HE2  sing N N 365 
LYS CE  HE3  sing N N 366 
LYS NZ  HZ1  sing N N 367 
LYS NZ  HZ2  sing N N 368 
LYS NZ  HZ3  sing N N 369 
LYS OXT HXT  sing N N 370 
MET N   CA   sing N N 371 
MET N   H    sing N N 372 
MET N   H2   sing N N 373 
MET CA  C    sing N N 374 
MET CA  CB   sing N N 375 
MET CA  HA   sing N N 376 
MET C   O    doub N N 377 
MET C   OXT  sing N N 378 
MET CB  CG   sing N N 379 
MET CB  HB2  sing N N 380 
MET CB  HB3  sing N N 381 
MET CG  SD   sing N N 382 
MET CG  HG2  sing N N 383 
MET CG  HG3  sing N N 384 
MET SD  CE   sing N N 385 
MET CE  HE1  sing N N 386 
MET CE  HE2  sing N N 387 
MET CE  HE3  sing N N 388 
MET OXT HXT  sing N N 389 
OLC C18 C17  sing N N 390 
OLC C10 C9   doub N N 391 
OLC C10 C11  sing N N 392 
OLC C9  C8   sing N N 393 
OLC C17 C16  sing N Z 394 
OLC C11 C12  sing N N 395 
OLC C8  C7   sing N N 396 
OLC C24 C22  sing N N 397 
OLC C24 O25  sing N N 398 
OLC C16 C15  sing N N 399 
OLC C12 C13  sing N N 400 
OLC C7  C6   sing N N 401 
OLC C15 C14  sing N N 402 
OLC C13 C14  sing N N 403 
OLC C6  C5   sing N N 404 
OLC C5  C4   sing N N 405 
OLC C4  C3   sing N N 406 
OLC C3  C2   sing N N 407 
OLC C2  C1   sing N N 408 
OLC C21 C22  sing N N 409 
OLC C21 O20  sing N N 410 
OLC C1  O19  doub N N 411 
OLC C1  O20  sing N N 412 
OLC C22 O23  sing N N 413 
OLC C18 H18  sing N N 414 
OLC C18 H18A sing N N 415 
OLC C18 H18B sing N N 416 
OLC C10 H10  sing N N 417 
OLC C9  H9   sing N N 418 
OLC C17 H17  sing N N 419 
OLC C17 H17A sing N N 420 
OLC C11 H11  sing N N 421 
OLC C11 H11A sing N N 422 
OLC C8  H8   sing N N 423 
OLC C8  H8A  sing N N 424 
OLC C24 H24  sing N N 425 
OLC C24 H24A sing N N 426 
OLC C16 H16  sing N N 427 
OLC C16 H16A sing N N 428 
OLC C12 H12  sing N N 429 
OLC C12 H12A sing N N 430 
OLC C7  H7   sing N N 431 
OLC C7  H7A  sing N N 432 
OLC C15 H15  sing N N 433 
OLC C15 H15A sing N N 434 
OLC C13 H13  sing N N 435 
OLC C13 H13A sing N N 436 
OLC C6  H6   sing N N 437 
OLC C6  H6A  sing N N 438 
OLC C14 H14  sing N N 439 
OLC C14 H14A sing N N 440 
OLC C5  H5   sing N N 441 
OLC C5  H5A  sing N N 442 
OLC C4  H4   sing N N 443 
OLC C4  H4A  sing N N 444 
OLC C3  H3   sing N N 445 
OLC C3  H3A  sing N N 446 
OLC C2  H2   sing N N 447 
OLC C2  H2A  sing N N 448 
OLC C21 H21  sing N N 449 
OLC C21 H21A sing N N 450 
OLC C22 H22  sing N N 451 
OLC O25 HO25 sing N N 452 
OLC O23 HO23 sing N N 453 
PHE N   CA   sing N N 454 
PHE N   H    sing N N 455 
PHE N   H2   sing N N 456 
PHE CA  C    sing N N 457 
PHE CA  CB   sing N N 458 
PHE CA  HA   sing N N 459 
PHE C   O    doub N N 460 
PHE C   OXT  sing N N 461 
PHE CB  CG   sing N N 462 
PHE CB  HB2  sing N N 463 
PHE CB  HB3  sing N N 464 
PHE CG  CD1  doub Y N 465 
PHE CG  CD2  sing Y N 466 
PHE CD1 CE1  sing Y N 467 
PHE CD1 HD1  sing N N 468 
PHE CD2 CE2  doub Y N 469 
PHE CD2 HD2  sing N N 470 
PHE CE1 CZ   doub Y N 471 
PHE CE1 HE1  sing N N 472 
PHE CE2 CZ   sing Y N 473 
PHE CE2 HE2  sing N N 474 
PHE CZ  HZ   sing N N 475 
PHE OXT HXT  sing N N 476 
PRO N   CA   sing N N 477 
PRO N   CD   sing N N 478 
PRO N   H    sing N N 479 
PRO CA  C    sing N N 480 
PRO CA  CB   sing N N 481 
PRO CA  HA   sing N N 482 
PRO C   O    doub N N 483 
PRO C   OXT  sing N N 484 
PRO CB  CG   sing N N 485 
PRO CB  HB2  sing N N 486 
PRO CB  HB3  sing N N 487 
PRO CG  CD   sing N N 488 
PRO CG  HG2  sing N N 489 
PRO CG  HG3  sing N N 490 
PRO CD  HD2  sing N N 491 
PRO CD  HD3  sing N N 492 
PRO OXT HXT  sing N N 493 
RET C1  C2   sing N N 494 
RET C1  C6   sing N N 495 
RET C1  C16  sing N N 496 
RET C1  C17  sing N N 497 
RET C2  C3   sing N N 498 
RET C2  H21  sing N N 499 
RET C2  H22  sing N N 500 
RET C3  C4   sing N N 501 
RET C3  H31  sing N N 502 
RET C3  H32  sing N N 503 
RET C4  C5   sing N N 504 
RET C4  H41  sing N N 505 
RET C4  H42  sing N N 506 
RET C5  C6   doub N N 507 
RET C5  C18  sing N N 508 
RET C6  C7   sing N N 509 
RET C7  C8   doub N E 510 
RET C7  H7   sing N N 511 
RET C8  C9   sing N N 512 
RET C8  H8   sing N N 513 
RET C9  C10  doub N E 514 
RET C9  C19  sing N N 515 
RET C10 C11  sing N N 516 
RET C10 H10  sing N N 517 
RET C11 C12  doub N E 518 
RET C11 H11  sing N N 519 
RET C12 C13  sing N N 520 
RET C12 H12  sing N N 521 
RET C13 C14  doub N E 522 
RET C13 C20  sing N N 523 
RET C14 C15  sing N N 524 
RET C14 H14  sing N N 525 
RET C15 O1   doub N N 526 
RET C15 H15  sing N N 527 
RET C16 H161 sing N N 528 
RET C16 H162 sing N N 529 
RET C16 H163 sing N N 530 
RET C17 H171 sing N N 531 
RET C17 H172 sing N N 532 
RET C17 H173 sing N N 533 
RET C18 H181 sing N N 534 
RET C18 H182 sing N N 535 
RET C18 H183 sing N N 536 
RET C19 H191 sing N N 537 
RET C19 H192 sing N N 538 
RET C19 H193 sing N N 539 
RET C20 H201 sing N N 540 
RET C20 H202 sing N N 541 
RET C20 H203 sing N N 542 
SER N   CA   sing N N 543 
SER N   H    sing N N 544 
SER N   H2   sing N N 545 
SER CA  C    sing N N 546 
SER CA  CB   sing N N 547 
SER CA  HA   sing N N 548 
SER C   O    doub N N 549 
SER C   OXT  sing N N 550 
SER CB  OG   sing N N 551 
SER CB  HB2  sing N N 552 
SER CB  HB3  sing N N 553 
SER OG  HG   sing N N 554 
SER OXT HXT  sing N N 555 
THR N   CA   sing N N 556 
THR N   H    sing N N 557 
THR N   H2   sing N N 558 
THR CA  C    sing N N 559 
THR CA  CB   sing N N 560 
THR CA  HA   sing N N 561 
THR C   O    doub N N 562 
THR C   OXT  sing N N 563 
THR CB  OG1  sing N N 564 
THR CB  CG2  sing N N 565 
THR CB  HB   sing N N 566 
THR OG1 HG1  sing N N 567 
THR CG2 HG21 sing N N 568 
THR CG2 HG22 sing N N 569 
THR CG2 HG23 sing N N 570 
THR OXT HXT  sing N N 571 
TRP N   CA   sing N N 572 
TRP N   H    sing N N 573 
TRP N   H2   sing N N 574 
TRP CA  C    sing N N 575 
TRP CA  CB   sing N N 576 
TRP CA  HA   sing N N 577 
TRP C   O    doub N N 578 
TRP C   OXT  sing N N 579 
TRP CB  CG   sing N N 580 
TRP CB  HB2  sing N N 581 
TRP CB  HB3  sing N N 582 
TRP CG  CD1  doub Y N 583 
TRP CG  CD2  sing Y N 584 
TRP CD1 NE1  sing Y N 585 
TRP CD1 HD1  sing N N 586 
TRP CD2 CE2  doub Y N 587 
TRP CD2 CE3  sing Y N 588 
TRP NE1 CE2  sing Y N 589 
TRP NE1 HE1  sing N N 590 
TRP CE2 CZ2  sing Y N 591 
TRP CE3 CZ3  doub Y N 592 
TRP CE3 HE3  sing N N 593 
TRP CZ2 CH2  doub Y N 594 
TRP CZ2 HZ2  sing N N 595 
TRP CZ3 CH2  sing Y N 596 
TRP CZ3 HZ3  sing N N 597 
TRP CH2 HH2  sing N N 598 
TRP OXT HXT  sing N N 599 
TYR N   CA   sing N N 600 
TYR N   H    sing N N 601 
TYR N   H2   sing N N 602 
TYR CA  C    sing N N 603 
TYR CA  CB   sing N N 604 
TYR CA  HA   sing N N 605 
TYR C   O    doub N N 606 
TYR C   OXT  sing N N 607 
TYR CB  CG   sing N N 608 
TYR CB  HB2  sing N N 609 
TYR CB  HB3  sing N N 610 
TYR CG  CD1  doub Y N 611 
TYR CG  CD2  sing Y N 612 
TYR CD1 CE1  sing Y N 613 
TYR CD1 HD1  sing N N 614 
TYR CD2 CE2  doub Y N 615 
TYR CD2 HD2  sing N N 616 
TYR CE1 CZ   doub Y N 617 
TYR CE1 HE1  sing N N 618 
TYR CE2 CZ   sing Y N 619 
TYR CE2 HE2  sing N N 620 
TYR CZ  OH   sing N N 621 
TYR OH  HH   sing N N 622 
TYR OXT HXT  sing N N 623 
VAL N   CA   sing N N 624 
VAL N   H    sing N N 625 
VAL N   H2   sing N N 626 
VAL CA  C    sing N N 627 
VAL CA  CB   sing N N 628 
VAL CA  HA   sing N N 629 
VAL C   O    doub N N 630 
VAL C   OXT  sing N N 631 
VAL CB  CG1  sing N N 632 
VAL CB  CG2  sing N N 633 
VAL CB  HB   sing N N 634 
VAL CG1 HG11 sing N N 635 
VAL CG1 HG12 sing N N 636 
VAL CG1 HG13 sing N N 637 
VAL CG2 HG21 sing N N 638 
VAL CG2 HG22 sing N N 639 
VAL CG2 HG23 sing N N 640 
VAL OXT HXT  sing N N 641 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Agence Nationale de la Recherche (ANR)' France ANR-15-CE11-0029-02 1 
'Agence Nationale de la Recherche (ANR)' France ANR-19-CE11-0026    2 
'Agence Nationale de la Recherche (ANR)' France ANR-11-LABX-0015-01 3 
# 
_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   7AKY 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 2' 
_space_group.name_Hall        'P 2 2ab' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9IN7 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.021506 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008700 
_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]   0.018807 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ?       ? 25.62398 1.50364  ?        ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ?       ? 19.97189 1.75589  ?        ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
NA ? ? 6.63511 3.01293 1.30238 ? 5.54423  0.54580  90.85902 ? 0.0 
;3-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ?       ? 15.80542 1.70748  ?        ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ?       ? 1.23737  29.19336 ?        ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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 
HETATM 1    N  N   . FME A 1 1   ? -2.86537  26.30732 -23.41622 1.000 39.32260 ? 1   FME A N   1 
HETATM 2    C  CN  . FME A 1 1   ? -4.06724  26.26115 -22.75708 1.000 41.49958 ? 1   FME A CN  1 
HETATM 3    O  O1  . FME A 1 1   ? -4.12910  26.27280 -21.52602 1.000 41.16484 ? 1   FME A O1  1 
HETATM 4    C  CA  . FME A 1 1   ? -1.58194  26.36323 -22.77330 1.000 41.36576 ? 1   FME A CA  1 
HETATM 5    C  CB  . FME A 1 1   ? -0.43540  26.39861 -23.80657 1.000 44.61384 ? 1   FME A CB  1 
HETATM 6    C  CG  . FME A 1 1   ? -0.34461  25.19301 -24.73978 0.500 44.79579 ? 1   FME A CG  1 
HETATM 7    S  SD  . FME A 1 1   ? -1.40867  23.79496 -24.38559 0.500 42.42995 ? 1   FME A SD  1 
HETATM 8    C  CE  . FME A 1 1   ? -0.31590  22.77276 -23.47137 0.500 45.18358 ? 1   FME A CE  1 
HETATM 9    C  C   . FME A 1 1   ? -1.43450  27.53076 -21.77110 1.000 40.68513 ? 1   FME A C   1 
HETATM 10   O  O   . FME A 1 1   ? -1.00896  27.37650 -20.61713 1.000 34.89032 ? 1   FME A O   1 
ATOM   11   N  N   . ASP A 1 2   ? -1.82627  28.72262 -22.22485 1.000 39.70736 ? 2   ASP A N   1 
ATOM   12   C  CA  . ASP A 1 2   ? -1.76445  29.94644 -21.41043 1.000 36.60508 ? 2   ASP A CA  1 
ATOM   13   C  C   . ASP A 1 2   ? -2.61556  29.87316 -20.13973 1.000 29.15280 ? 2   ASP A C   1 
ATOM   14   O  O   . ASP A 1 2   ? -2.20025  30.32854 -19.07648 1.000 29.90906 ? 2   ASP A O   1 
ATOM   15   C  CB  . ASP A 1 2   ? -2.18074  31.18122 -22.22229 1.000 42.79048 ? 2   ASP A CB  1 
ATOM   16   C  CG  . ASP A 1 2   ? -1.04611  31.74621 -23.06397 1.000 53.05633 ? 2   ASP A CG  1 
ATOM   17   O  OD1 . ASP A 1 2   ? 0.13411   31.44594 -22.76764 1.000 56.95230 ? 2   ASP A OD1 1 
ATOM   18   O  OD2 . ASP A 1 2   ? -1.34085  32.50467 -24.01680 1.000 56.10529 ? 2   ASP A OD2 1 
ATOM   19   N  N   . ASN A 1 3   ? -3.81889  29.31454 -20.24429 1.000 26.45482 ? 3   ASN A N   1 
ATOM   20   C  CA  . ASN A 1 3   ? -4.64551  29.22182 -19.04908 1.000 25.49435 ? 3   ASN A CA  1 
ATOM   21   C  C   . ASN A 1 3   ? -4.17094  28.13440 -18.10021 1.000 22.53082 ? 3   ASN A C   1 
ATOM   22   O  O   . ASN A 1 3   ? -4.36463  28.26517 -16.88804 1.000 20.19391 ? 3   ASN A O   1 
ATOM   23   C  CB  . ASN A 1 3   ? -6.09373  28.97170 -19.42791 1.000 33.16859 ? 3   ASN A CB  1 
ATOM   24   C  CG  . ASN A 1 3   ? -6.72744  30.16375 -20.06300 1.000 39.52449 ? 3   ASN A CG  1 
ATOM   25   O  OD1 . ASN A 1 3   ? -6.35485  31.30358 -19.78000 1.000 40.71467 ? 3   ASN A OD1 1 
ATOM   26   N  ND2 . ASN A 1 3   ? -7.68454  29.91733 -20.94298 1.000 39.26188 ? 3   ASN A ND2 1 
ATOM   27   N  N   . ILE A 1 4   ? -3.58260  27.04530 -18.61556 1.000 22.34905 ? 4   ILE A N   1 
ATOM   28   C  CA  . ILE A 1 4   ? -2.97155  26.07331 -17.71208 1.000 20.31475 ? 4   ILE A CA  1 
ATOM   29   C  C   . ILE A 1 4   ? -1.85657  26.73274 -16.93108 1.000 21.20101 ? 4   ILE A C   1 
ATOM   30   O  O   . ILE A 1 4   ? -1.74335  26.57509 -15.71818 1.000 23.01147 ? 4   ILE A O   1 
ATOM   31   C  CB  . ILE A 1 4   ? -2.45327  24.83475 -18.46441 1.000 22.07243 ? 4   ILE A CB  1 
ATOM   32   C  CG1 . ILE A 1 4   ? -3.56211  24.15452 -19.25434 1.000 24.09554 ? 4   ILE A CG1 1 
ATOM   33   C  CG2 . ILE A 1 4   ? -1.89391  23.85880 -17.43215 1.000 25.75616 ? 4   ILE A CG2 1 
ATOM   34   C  CD1 . ILE A 1 4   ? -2.99526  23.07585 -20.18445 1.000 29.08331 ? 4   ILE A CD1 1 
ATOM   35   N  N   . ILE A 1 5   ? -1.02066  27.49257 -17.61644 1.000 19.47800 ? 5   ILE A N   1 
ATOM   36   C  CA  . ILE A 1 5   ? 0.09141   28.15989 -16.94590 1.000 20.76234 ? 5   ILE A CA  1 
ATOM   37   C  C   . ILE A 1 5   ? -0.43741  29.18690 -15.95661 1.000 18.42102 ? 5   ILE A C   1 
ATOM   38   O  O   . ILE A 1 5   ? 0.06405   29.29605 -14.83060 1.000 20.40927 ? 5   ILE A O   1 
ATOM   39   C  CB  . ILE A 1 5   ? 1.01682   28.80582 -17.99210 1.000 25.89905 ? 5   ILE A CB  1 
ATOM   40   C  CG1 . ILE A 1 5   ? 1.72238   27.71445 -18.75641 1.000 30.98395 ? 5   ILE A CG1 1 
ATOM   41   C  CG2 . ILE A 1 5   ? 2.03597   29.71238 -17.32490 1.000 28.53850 ? 5   ILE A CG2 1 
ATOM   42   C  CD1 . ILE A 1 5   ? 2.95895   27.21400 -18.01711 1.000 40.25113 ? 5   ILE A CD1 1 
ATOM   43   N  N   . MET A 1 6   ? -1.42816  29.99144 -16.37530 1.000 19.32348 ? 6   MET A N   1 
ATOM   44   C  CA  . MET A 1 6   ? -1.92964  31.03877 -15.48862 1.000 20.39877 ? 6   MET A CA  1 
ATOM   45   C  C   . MET A 1 6   ? -2.49480  30.43894 -14.20659 1.000 19.05929 ? 6   MET A C   1 
ATOM   46   O  O   . MET A 1 6   ? -2.19828  30.90927 -13.10280 1.000 18.80095 ? 6   MET A O   1 
ATOM   47   C  CB  . MET A 1 6   ? -3.01129  31.85495 -16.18365 1.000 22.56977 ? 6   MET A CB  1 
ATOM   48   C  CG  . MET A 1 6   ? -3.60902  32.88671 -15.25540 1.000 30.11781 ? 6   MET A CG  1 
ATOM   49   S  SD  . MET A 1 6   ? -4.83941  33.87938 -16.08516 1.000 40.45587 ? 6   MET A SD  1 
ATOM   50   C  CE  . MET A 1 6   ? -3.86037  34.40991 -17.47700 1.000 42.72802 ? 6   MET A CE  1 
ATOM   51   N  N   . THR A 1 7   ? -3.30645  29.38215 -14.32555 1.000 17.51802 ? 7   THR A N   1 
ATOM   52   C  CA  . THR A 1 7   ? -3.85226  28.75613 -13.12888 1.000 16.88990 ? 7   THR A CA  1 
ATOM   53   C  C   . THR A 1 7   ? -2.75741  28.07748 -12.31609 1.000 16.47737 ? 7   THR A C   1 
ATOM   54   O  O   . THR A 1 7   ? -2.85537  28.02373 -11.08368 1.000 17.05469 ? 7   THR A O   1 
ATOM   55   C  CB  . THR A 1 7   ? -4.98995  27.78808 -13.46651 1.000 18.07892 ? 7   THR A CB  1 
ATOM   56   O  OG1 . THR A 1 7   ? -4.53398  26.77557 -14.37690 1.000 17.75031 ? 7   THR A OG1 1 
ATOM   57   C  CG2 . THR A 1 7   ? -6.21272  28.53959 -14.00950 1.000 18.19798 ? 7   THR A CG2 1 
ATOM   58   N  N   . ALA A 1 8   ? -1.70795  27.58195 -12.98162 1.000 17.23774 ? 8   ALA A N   1 
ATOM   59   C  CA  . ALA A 1 8   ? -0.55589  27.04293 -12.25790 1.000 16.72407 ? 8   ALA A CA  1 
ATOM   60   C  C   . ALA A 1 8   ? 0.12598   28.11826 -11.42717 1.000 17.11639 ? 8   ALA A C   1 
ATOM   61   O  O   . ALA A 1 8   ? 0.47066   27.88902 -10.25910 1.000 17.83585 ? 8   ALA A O   1 
ATOM   62   C  CB  . ALA A 1 8   ? 0.42987   26.34733 -13.19749 1.000 18.31556 ? 8   ALA A CB  1 
ATOM   63   N  N   . TYR A 1 9   ? 0.30850   29.31114 -12.00509 1.000 17.47819 ? 9   TYR A N   1 
ATOM   64   C  CA  . TYR A 1 9   ? 0.89044   30.40912 -11.25599 1.000 16.83954 ? 9   TYR A CA  1 
ATOM   65   C  C   . TYR A 1 9   ? 0.00317   30.83847 -10.09412 1.000 15.93452 ? 9   TYR A C   1 
ATOM   66   O  O   . TYR A 1 9   ? 0.51406   31.15361 -9.01990  1.000 17.07346 ? 9   TYR A O   1 
ATOM   67   C  CB  . TYR A 1 9   ? 1.15242   31.58622 -12.18811 1.000 19.22887 ? 9   TYR A CB  1 
ATOM   68   C  CG  . TYR A 1 9   ? 2.31429   31.45089 -13.13989 1.000 23.31644 ? 9   TYR A CG  1 
ATOM   69   C  CD1 . TYR A 1 9   ? 3.45844   30.77584 -12.78702 1.000 26.79752 ? 9   TYR A CD1 1 
ATOM   70   C  CD2 . TYR A 1 9   ? 2.25929   32.05052 -14.38442 1.000 24.33743 ? 9   TYR A CD2 1 
ATOM   71   C  CE1 . TYR A 1 9   ? 4.52337   30.65664 -13.66537 1.000 28.01018 ? 9   TYR A CE1 1 
ATOM   72   C  CE2 . TYR A 1 9   ? 3.32691   31.97353 -15.26300 1.000 27.23057 ? 9   TYR A CE2 1 
ATOM   73   C  CZ  . TYR A 1 9   ? 4.45208   31.25601 -14.89875 1.000 27.79844 ? 9   TYR A CZ  1 
ATOM   74   O  OH  . TYR A 1 9   ? 5.52148   31.14675 -15.75410 1.000 33.71201 ? 9   TYR A OH  1 
ATOM   75   N  N   . ILE A 1 10  ? -1.32428  30.89763 -10.28779 1.000 17.09501 ? 10  ILE A N   1 
ATOM   76   C  CA  . ILE A 1 10  ? -2.22355  31.22230 -9.17476  1.000 16.31788 ? 10  ILE A CA  1 
ATOM   77   C  C   . ILE A 1 10  ? -2.02625  30.22613 -8.03637  1.000 17.86064 ? 10  ILE A C   1 
ATOM   78   O  O   . ILE A 1 10  ? -1.89679  30.60132 -6.86121  1.000 17.30082 ? 10  ILE A O   1 
ATOM   79   C  CB  . ILE A 1 10  ? -3.69241  31.26405 -9.64675  1.000 18.00102 ? 10  ILE A CB  1 
ATOM   80   C  CG1 . ILE A 1 10  ? -3.88932  32.39862 -10.66602 1.000 18.96628 ? 10  ILE A CG1 1 
ATOM   81   C  CG2 . ILE A 1 10  ? -4.62697  31.46746 -8.48655  1.000 19.58160 ? 10  ILE A CG2 1 
ATOM   82   C  CD1 . ILE A 1 10  ? -5.25885  32.36819 -11.39032 1.000 22.85847 ? 10  ILE A CD1 1 
ATOM   83   N  N   . SER A 1 11  ? -1.98505  28.93218 -8.38313  1.000 17.07945 ? 11  SER A N   1 
ATOM   84   C  CA  . SER A 1 11  ? -1.78693  27.88279 -7.38908  1.000 15.57083 ? 11  SER A CA  1 
ATOM   85   C  C   . SER A 1 11  ? -0.44159  28.03764 -6.68665  1.000 15.60704 ? 11  SER A C   1 
ATOM   86   O  O   . SER A 1 11  ? -0.36062  27.94871 -5.46041  1.000 17.55851 ? 11  SER A O   1 
ATOM   87   C  CB  . SER A 1 11  ? -1.87108  26.53676 -8.10809  1.000 16.39298 ? 11  SER A CB  1 
ATOM   88   O  OG  . SER A 1 11  ? -1.98800  25.48326 -7.17300  1.000 16.73801 ? 11  SER A OG  1 
ATOM   89   N  N   . ILE A 1 12  ? 0.62822   28.27457 -7.45063  1.000 16.09438 ? 12  ILE A N   1 
ATOM   90   C  CA  . ILE A 1 12  ? 1.95138   28.47878 -6.85585  1.000 18.29730 ? 12  ILE A CA  1 
ATOM   91   C  C   . ILE A 1 12  ? 1.95461   29.68286 -5.92310  1.000 16.67632 ? 12  ILE A C   1 
ATOM   92   O  O   . ILE A 1 12  ? 2.56048   29.64811 -4.84410  1.000 17.78484 ? 12  ILE A O   1 
ATOM   93   C  CB  . ILE A 1 12  ? 2.99883   28.63263 -7.96588  1.000 17.88429 ? 12  ILE A CB  1 
ATOM   94   C  CG1 . ILE A 1 12  ? 3.19009   27.28354 -8.65357  1.000 19.57713 ? 12  ILE A CG1 1 
ATOM   95   C  CG2 . ILE A 1 12  ? 4.30003   29.21059 -7.42193  1.000 18.54271 ? 12  ILE A CG2 1 
ATOM   96   C  CD1 . ILE A 1 12  ? 3.91694   27.43495 -9.97461  1.000 20.92641 ? 12  ILE A CD1 1 
ATOM   97   N  N   . PHE A 1 13  ? 1.27868   30.77437 -6.31623  1.000 16.27501 ? 13  PHE A N   1 
ATOM   98   C  CA  . PHE A 1 13  ? 1.20773   31.97065 -5.48991  1.000 17.54482 ? 13  PHE A CA  1 
ATOM   99   C  C   . PHE A 1 13  ? 0.61379   31.62191 -4.13198  1.000 16.56032 ? 13  PHE A C   1 
ATOM   100  O  O   . PHE A 1 13  ? 1.18216   31.95099 -3.08157  1.000 18.18736 ? 13  PHE A O   1 
ATOM   101  C  CB  . PHE A 1 13  ? 0.33698   33.01391 -6.20936  1.000 18.45584 ? 13  PHE A CB  1 
ATOM   102  C  CG  . PHE A 1 13  ? 0.23335   34.34144 -5.48760  1.000 19.92417 ? 13  PHE A CG  1 
ATOM   103  C  CD1 . PHE A 1 13  ? -0.71634  34.53560 -4.50358  1.000 23.43263 ? 13  PHE A CD1 1 
ATOM   104  C  CD2 . PHE A 1 13  ? 1.03699   35.41084 -5.83160  1.000 24.28096 ? 13  PHE A CD2 1 
ATOM   105  C  CE1 . PHE A 1 13  ? -0.82739  35.73738 -3.82718  1.000 25.57404 ? 13  PHE A CE1 1 
ATOM   106  C  CE2 . PHE A 1 13  ? 0.92002   36.65401 -5.16278  1.000 22.45093 ? 13  PHE A CE2 1 
ATOM   107  C  CZ  . PHE A 1 13  ? -0.01380  36.80177 -4.16136  1.000 26.98269 ? 13  PHE A CZ  1 
ATOM   108  N  N   A VAL A 1 14  ? -0.52219  30.92545 -4.14118  0.500 17.04407 ? 14  VAL A N   1 
ATOM   109  N  N   B VAL A 1 14  ? -0.54433  30.97237 -4.12288  0.500 17.29286 ? 14  VAL A N   1 
ATOM   110  C  CA  A VAL A 1 14  ? -1.17577  30.54742 -2.89297  0.500 15.98793 ? 14  VAL A CA  1 
ATOM   111  C  CA  B VAL A 1 14  ? -1.12504  30.58748 -2.84091  0.500 17.12615 ? 14  VAL A CA  1 
ATOM   112  C  C   A VAL A 1 14  ? -0.33331  29.54540 -2.09911  0.500 16.63503 ? 14  VAL A C   1 
ATOM   113  C  C   B VAL A 1 14  ? -0.20114  29.63760 -2.08287  0.500 16.31556 ? 14  VAL A C   1 
ATOM   114  O  O   A VAL A 1 14  ? -0.34156  29.56084 -0.86382  0.500 16.91433 ? 14  VAL A O   1 
ATOM   115  O  O   B VAL A 1 14  ? -0.02137  29.77361 -0.86506  0.500 15.77431 ? 14  VAL A O   1 
ATOM   116  C  CB  A VAL A 1 14  ? -2.61440  30.06451 -3.13624  0.500 15.22115 ? 14  VAL A CB  1 
ATOM   117  C  CB  B VAL A 1 14  ? -2.54832  30.03586 -2.99713  0.500 16.80028 ? 14  VAL A CB  1 
ATOM   118  C  CG1 A VAL A 1 14  ? -3.36490  29.92902 -1.78698  0.500 16.65141 ? 14  VAL A CG1 1 
ATOM   119  C  CG1 B VAL A 1 14  ? -3.04192  29.46110 -1.65177  0.500 15.27870 ? 14  VAL A CG1 1 
ATOM   120  C  CG2 A VAL A 1 14  ? -3.34822  31.03272 -4.05332  0.500 15.02362 ? 14  VAL A CG2 1 
ATOM   121  C  CG2 B VAL A 1 14  ? -3.48159  31.15056 -3.47809  0.500 14.40176 ? 14  VAL A CG2 1 
ATOM   122  N  N   . GLN A 1 15  ? 0.40621   28.67445 -2.78580  1.000 16.60583 ? 15  GLN A N   1 
ATOM   123  C  CA  . GLN A 1 15  ? 1.28407   27.72385 -2.11133  1.000 16.82212 ? 15  GLN A CA  1 
ATOM   124  C  C   . GLN A 1 15  ? 2.38344   28.43961 -1.33310  1.000 17.68666 ? 15  GLN A C   1 
ATOM   125  O  O   . GLN A 1 15  ? 2.68406   28.08989 -0.19132  1.000 17.31309 ? 15  GLN A O   1 
ATOM   126  C  CB  . GLN A 1 15  ? 1.92880   26.79157 -3.13980  1.000 16.00603 ? 15  GLN A CB  1 
ATOM   127  C  CG  . GLN A 1 15  ? 0.94258   25.74648 -3.67264  1.000 16.96260 ? 15  GLN A CG  1 
ATOM   128  C  CD  . GLN A 1 15  ? 1.56192   24.95466 -4.76507  1.000 16.67413 ? 15  GLN A CD  1 
ATOM   129  O  OE1 . GLN A 1 15  ? 2.59838   24.30526 -4.58597  1.000 18.55665 ? 15  GLN A OE1 1 
ATOM   130  N  NE2 . GLN A 1 15  ? 0.91247   24.95801 -5.92893  1.000 17.09566 ? 15  GLN A NE2 1 
ATOM   131  N  N   . ILE A 1 16  ? 3.02710   29.41613 -1.96319  1.000 18.33487 ? 16  ILE A N   1 
ATOM   132  C  CA  . ILE A 1 16  ? 4.14275   30.09399 -1.33909  1.000 20.16966 ? 16  ILE A CA  1 
ATOM   133  C  C   . ILE A 1 16  ? 3.68562   30.83492 -0.09683  1.000 18.90342 ? 16  ILE A C   1 
ATOM   134  O  O   . ILE A 1 16  ? 4.32912   30.77025 0.95083   1.000 21.22527 ? 16  ILE A O   1 
ATOM   135  C  CB  . ILE A 1 16  ? 4.78738   31.05486 -2.34414  1.000 23.86768 ? 16  ILE A CB  1 
ATOM   136  C  CG1 . ILE A 1 16  ? 5.54768   30.30215 -3.43279  1.000 26.09497 ? 16  ILE A CG1 1 
ATOM   137  C  CG2 . ILE A 1 16  ? 5.59303   32.08346 -1.61222  1.000 28.33720 ? 16  ILE A CG2 1 
ATOM   138  C  CD1 . ILE A 1 16  ? 5.94460   31.27937 -4.56678  1.000 28.94886 ? 16  ILE A CD1 1 
ATOM   139  N  N   . ILE A 1 17  ? 2.58306   31.57540 -0.20112  1.000 19.11024 ? 17  ILE A N   1 
ATOM   140  C  CA  . ILE A 1 17  ? 2.11374   32.33516 0.95779   1.000 21.18922 ? 17  ILE A CA  1 
ATOM   141  C  C   . ILE A 1 17  ? 1.65746   31.38593 2.07190   1.000 18.31193 ? 17  ILE A C   1 
ATOM   142  O  O   . ILE A 1 17  ? 1.94976   31.59976 3.25696   1.000 20.33270 ? 17  ILE A O   1 
ATOM   143  C  CB  . ILE A 1 17  ? 1.02443   33.33770 0.53630   1.000 23.75541 ? 17  ILE A CB  1 
ATOM   144  C  CG1 . ILE A 1 17  ? 1.51583   34.22304 -0.62695  1.000 25.75827 ? 17  ILE A CG1 1 
ATOM   145  C  CG2 . ILE A 1 17  ? 0.59987   34.18897 1.70767   1.000 24.29092 ? 17  ILE A CG2 1 
ATOM   146  C  CD1 . ILE A 1 17  ? 2.76311   34.99842 -0.34818  1.000 29.59341 ? 17  ILE A CD1 1 
ATOM   147  N  N   A THR A 1 18  ? 0.97868   30.29961 1.69299   0.700 17.97551 ? 18  THR A N   1 
ATOM   148  N  N   B THR A 1 18  ? 0.93765   30.32540 1.71729   0.300 18.81445 ? 18  THR A N   1 
ATOM   149  C  CA  A THR A 1 18  ? 0.52369   29.31148 2.66682   0.700 17.41113 ? 18  THR A CA  1 
ATOM   150  C  CA  B THR A 1 18  ? 0.54082   29.36627 2.73945   0.300 19.51962 ? 18  THR A CA  1 
ATOM   151  C  C   A THR A 1 18  ? 1.68367   28.62431 3.36945   0.700 17.77472 ? 18  THR A C   1 
ATOM   152  C  C   B THR A 1 18  ? 1.75133   28.75331 3.42411   0.300 18.66425 ? 18  THR A C   1 
ATOM   153  O  O   A THR A 1 18  ? 1.59267   28.28942 4.55581   0.700 18.77553 ? 18  THR A O   1 
ATOM   154  O  O   B THR A 1 18  ? 1.77392   28.62475 4.65355   0.300 15.86349 ? 18  THR A O   1 
ATOM   155  C  CB  A THR A 1 18  ? -0.34248  28.26068 1.97129   0.700 17.36519 ? 18  THR A CB  1 
ATOM   156  C  CB  B THR A 1 18  ? -0.34778  28.28210 2.13993   0.300 21.32213 ? 18  THR A CB  1 
ATOM   157  O  OG1 A THR A 1 18  ? -1.47057  28.89882 1.36115   0.700 16.59182 ? 18  THR A OG1 1 
ATOM   158  O  OG1 B THR A 1 18  ? 0.27767   27.73754 0.98024   0.300 24.35405 ? 18  THR A OG1 1 
ATOM   159  C  CG2 A THR A 1 18  ? -0.85311  27.21186 2.98970   0.700 14.90501 ? 18  THR A CG2 1 
ATOM   160  C  CG2 B THR A 1 18  ? -1.66557  28.86179 1.73539   0.300 18.45210 ? 18  THR A CG2 1 
ATOM   161  N  N   . ALA A 1 19  ? 2.78241   28.39223 2.65403   1.000 18.30804 ? 19  ALA A N   1 
ATOM   162  C  CA  . ALA A 1 19  ? 3.94452   27.77118 3.27592   1.000 17.77719 ? 19  ALA A CA  1 
ATOM   163  C  C   . ALA A 1 19  ? 4.56402   28.70792 4.30826   1.000 18.29951 ? 19  ALA A C   1 
ATOM   164  O  O   . ALA A 1 19  ? 4.94474   28.27457 5.41001   1.000 17.38022 ? 19  ALA A O   1 
ATOM   165  C  CB  . ALA A 1 19  ? 4.97108   27.37817 2.21392   1.000 18.01426 ? 19  ALA A CB  1 
ATOM   166  N  N   . ILE A 1 20  ? 4.67619   29.99353 3.97125   1.000 17.66060 ? 20  ILE A N   1 
ATOM   167  C  CA  . ILE A 1 20  ? 5.21204   30.96350 4.93619   1.000 18.57187 ? 20  ILE A CA  1 
ATOM   168  C  C   . ILE A 1 20  ? 4.34667   30.99746 6.18589   1.000 17.17360 ? 20  ILE A C   1 
ATOM   169  O  O   . ILE A 1 20  ? 4.84379   30.91436 7.32075   1.000 19.16846 ? 20  ILE A O   1 
ATOM   170  C  CB  . ILE A 1 20  ? 5.32616   32.35392 4.28280   1.000 19.30002 ? 20  ILE A CB  1 
ATOM   171  C  CG1 . ILE A 1 20  ? 6.35436   32.30497 3.15119   1.000 20.86594 ? 20  ILE A CG1 1 
ATOM   172  C  CG2 . ILE A 1 20  ? 5.65167   33.43678 5.35717   1.000 19.83185 ? 20  ILE A CG2 1 
ATOM   173  C  CD1 . ILE A 1 20  ? 6.39536   33.56003 2.26090   1.000 23.84062 ? 20  ILE A CD1 1 
ATOM   174  N  N   . ILE A 1 21  ? 3.03580   31.11168 5.99588   1.000 19.33270 ? 21  ILE A N   1 
ATOM   175  C  CA  . ILE A 1 21  ? 2.11539   31.13757 7.12440   1.000 19.68580 ? 21  ILE A CA  1 
ATOM   176  C  C   . ILE A 1 21  ? 2.28069   29.88079 7.96715   1.000 19.21647 ? 21  ILE A C   1 
ATOM   177  O  O   . ILE A 1 21  ? 2.33701   29.93718 9.20319   1.000 18.84851 ? 21  ILE A O   1 
ATOM   178  C  CB  . ILE A 1 21  ? 0.67647   31.27351 6.60252   1.000 20.81219 ? 21  ILE A CB  1 
ATOM   179  C  CG1 . ILE A 1 21  ? 0.49153   32.66546 6.00371   1.000 23.74721 ? 21  ILE A CG1 1 
ATOM   180  C  CG2 . ILE A 1 21  ? -0.31642  31.01193 7.73002   1.000 23.75579 ? 21  ILE A CG2 1 
ATOM   181  C  CD1 . ILE A 1 21  ? -0.78354  32.79133 5.18838   1.000 25.18321 ? 21  ILE A CD1 1 
ATOM   182  N  N   . SER A 1 22  ? 2.36886   28.72646 7.30939   1.000 18.56895 ? 22  SER A N   1 
ATOM   183  C  CA  . SER A 1 22  ? 2.44887   27.46668 8.04041   1.000 18.66945 ? 22  SER A CA  1 
ATOM   184  C  C   . SER A 1 22  ? 3.73155   27.38080 8.85934   1.000 17.85333 ? 22  SER A C   1 
ATOM   185  O  O   . SER A 1 22  ? 3.71552   26.87835 9.98565   1.000 19.88991 ? 22  SER A O   1 
ATOM   186  C  CB  . SER A 1 22  ? 2.36196   26.29326 7.08116   1.000 20.78244 ? 22  SER A CB  1 
ATOM   187  O  OG  . SER A 1 22  ? 1.12092   26.27326 6.42273   1.000 22.66062 ? 22  SER A OG  1 
ATOM   188  N  N   . VAL A 1 23  ? 4.85451   27.85414 8.31683   1.000 16.75570 ? 23  VAL A N   1 
ATOM   189  C  CA  . VAL A 1 23  ? 6.10695   27.79353 9.06023   1.000 18.52999 ? 23  VAL A CA  1 
ATOM   190  C  C   . VAL A 1 23  ? 6.00498   28.60298 10.34693  1.000 19.22225 ? 23  VAL A C   1 
ATOM   191  O  O   . VAL A 1 23  ? 6.36332   28.11804 11.42373  1.000 18.22334 ? 23  VAL A O   1 
ATOM   192  C  CB  . VAL A 1 23  ? 7.29997   28.19632 8.17953   1.000 18.75222 ? 23  VAL A CB  1 
ATOM   193  C  CG1 . VAL A 1 23  ? 8.54279   28.37108 9.02795   1.000 20.72920 ? 23  VAL A CG1 1 
ATOM   194  C  CG2 . VAL A 1 23  ? 7.57556   27.10041 7.10342   1.000 18.69298 ? 23  VAL A CG2 1 
ATOM   195  N  N   . TYR A 1 24  ? 5.46489   29.82735 10.27163  1.000 17.70840 ? 24  TYR A N   1 
ATOM   196  C  CA  . TYR A 1 24  ? 5.25932   30.60113 11.49397  1.000 16.95887 ? 24  TYR A CA  1 
ATOM   197  C  C   . TYR A 1 24  ? 4.32322   29.87917 12.44538  1.000 17.53716 ? 24  TYR A C   1 
ATOM   198  O  O   . TYR A 1 24  ? 4.52970   29.87839 13.66269  1.000 19.26018 ? 24  TYR A O   1 
ATOM   199  C  CB  . TYR A 1 24  ? 4.74204   32.00543 11.16982  1.000 18.14575 ? 24  TYR A CB  1 
ATOM   200  C  CG  . TYR A 1 24  ? 5.82162   32.95021 10.72425  1.000 16.63406 ? 24  TYR A CG  1 
ATOM   201  C  CD1 . TYR A 1 24  ? 6.20699   32.99296 9.41055   1.000 17.46842 ? 24  TYR A CD1 1 
ATOM   202  C  CD2 . TYR A 1 24  ? 6.46474   33.79231 11.63184  1.000 17.11042 ? 24  TYR A CD2 1 
ATOM   203  C  CE1 . TYR A 1 24  ? 7.17705   33.83988 8.99790   1.000 17.49569 ? 24  TYR A CE1 1 
ATOM   204  C  CE2 . TYR A 1 24  ? 7.44530   34.63610 11.23249  1.000 17.19808 ? 24  TYR A CE2 1 
ATOM   205  C  CZ  . TYR A 1 24  ? 7.82009   34.66847 9.90691   1.000 18.79862 ? 24  TYR A CZ  1 
ATOM   206  O  OH  . TYR A 1 24  ? 8.81258   35.50247 9.47348   1.000 19.01768 ? 24  TYR A OH  1 
ATOM   207  N  N   . GLY A 1 25  ? 3.31266   29.21954 11.89945  1.000 17.66237 ? 25  GLY A N   1 
ATOM   208  C  CA  . GLY A 1 25  ? 2.36041   28.48741 12.71816  1.000 18.00063 ? 25  GLY A CA  1 
ATOM   209  C  C   . GLY A 1 25  ? 3.01663   27.42168 13.57328  1.000 19.24996 ? 25  GLY A C   1 
ATOM   210  O  O   . GLY A 1 25  ? 2.54133   27.12821 14.66524  1.000 19.80733 ? 25  GLY A O   1 
ATOM   211  N  N   . LEU A 1 26  ? 4.08349   26.80041 13.06857  1.000 18.28556 ? 26  LEU A N   1 
ATOM   212  C  CA  . LEU A 1 26  ? 4.78651   25.75857 13.80506  1.000 20.32295 ? 26  LEU A CA  1 
ATOM   213  C  C   . LEU A 1 26  ? 5.39031   26.26080 15.10136  1.000 20.38663 ? 26  LEU A C   1 
ATOM   214  O  O   . LEU A 1 26  ? 5.65138   25.45376 16.00293  1.000 23.84336 ? 26  LEU A O   1 
ATOM   215  C  CB  . LEU A 1 26  ? 5.92207   25.19955 12.97108  1.000 22.05114 ? 26  LEU A CB  1 
ATOM   216  C  CG  . LEU A 1 26  ? 5.45341   24.51783 11.69843  1.000 20.90903 ? 26  LEU A CG  1 
ATOM   217  C  CD1 . LEU A 1 26  ? 6.69965   24.02224 10.99561  1.000 24.36876 ? 26  LEU A CD1 1 
ATOM   218  C  CD2 . LEU A 1 26  ? 4.47532   23.36117 12.00200  1.000 26.83220 ? 26  LEU A CD2 1 
ATOM   219  N  N   . PHE A 1 27  ? 5.61233   27.55461 15.22444  1.000 21.12229 ? 27  PHE A N   1 
ATOM   220  C  CA  . PHE A 1 27  ? 6.26806   28.09985 16.39329  1.000 22.57402 ? 27  PHE A CA  1 
ATOM   221  C  C   . PHE A 1 27  ? 5.31759   28.79660 17.34608  1.000 22.92759 ? 27  PHE A C   1 
ATOM   222  O  O   . PHE A 1 27  ? 5.77127   29.36994 18.34775  1.000 23.78093 ? 27  PHE A O   1 
ATOM   223  C  CB  . PHE A 1 27  ? 7.39847   29.01662 15.95154  1.000 23.54101 ? 27  PHE A CB  1 
ATOM   224  C  CG  . PHE A 1 27  ? 8.45688   28.28311 15.18581  1.000 25.55079 ? 27  PHE A CG  1 
ATOM   225  C  CD1 . PHE A 1 27  ? 9.41686   27.53223 15.86056  1.000 27.75466 ? 27  PHE A CD1 1 
ATOM   226  C  CD2 . PHE A 1 27  ? 8.46129   28.28451 13.80768  1.000 23.83504 ? 27  PHE A CD2 1 
ATOM   227  C  CE1 . PHE A 1 27  ? 10.38557  26.82953 15.17351  1.000 33.37258 ? 27  PHE A CE1 1 
ATOM   228  C  CE2 . PHE A 1 27  ? 9.40936   27.58016 13.11425  1.000 26.21873 ? 27  PHE A CE2 1 
ATOM   229  C  CZ  . PHE A 1 27  ? 10.37439  26.83513 13.79704  1.000 30.05893 ? 27  PHE A CZ  1 
ATOM   230  N  N   . ILE A 1 28  ? 4.02292   28.76258 17.06673  1.000 19.83857 ? 28  ILE A N   1 
ATOM   231  C  CA  . ILE A 1 28  ? 3.05743   29.32842 18.01207  1.000 20.79268 ? 28  ILE A CA  1 
ATOM   232  C  C   . ILE A 1 28  ? 2.97379   28.40959 19.22899  1.000 22.11793 ? 28  ILE A C   1 
ATOM   233  O  O   . ILE A 1 28  ? 2.73710   27.20648 19.07220  1.000 22.91803 ? 28  ILE A O   1 
ATOM   234  C  CB  . ILE A 1 28  ? 1.69212   29.50481 17.33599  1.000 20.48680 ? 28  ILE A CB  1 
ATOM   235  C  CG1 . ILE A 1 28  ? 1.82580   30.54239 16.19658  1.000 19.69021 ? 28  ILE A CG1 1 
ATOM   236  C  CG2 . ILE A 1 28  ? 0.61272   29.86871 18.36908  1.000 20.99871 ? 28  ILE A CG2 1 
ATOM   237  C  CD1 . ILE A 1 28  ? 0.59124   30.68064 15.34870  1.000 21.45549 ? 28  ILE A CD1 1 
ATOM   238  N  N   . PRO A 1 29  ? 3.15891   28.91312 20.45264  1.000 24.11360 ? 29  PRO A N   1 
ATOM   239  C  CA  . PRO A 1 29  ? 3.04175   28.03421 21.63073  1.000 24.65325 ? 29  PRO A CA  1 
ATOM   240  C  C   . PRO A 1 29  ? 1.62168   27.52510 21.77390  1.000 24.60491 ? 29  PRO A C   1 
ATOM   241  O  O   . PRO A 1 29  ? 0.65939   28.20787 21.41166  1.000 24.51326 ? 29  PRO A O   1 
ATOM   242  C  CB  . PRO A 1 29  ? 3.40923   28.94653 22.80115  1.000 26.18604 ? 29  PRO A CB  1 
ATOM   243  C  CG  . PRO A 1 29  ? 3.18648   30.32609 22.31256  1.000 32.17117 ? 29  PRO A CG  1 
ATOM   244  C  CD  . PRO A 1 29  ? 3.43208   30.31857 20.82409  1.000 26.08878 ? 29  PRO A CD  1 
ATOM   245  N  N   . LEU A 1 30  ? 1.50289   26.29290 22.27285  1.000 22.06139 ? 30  LEU A N   1 
ATOM   246  C  CA  . LEU A 1 30  ? 0.23014   25.58246 22.34032  1.000 22.32472 ? 30  LEU A CA  1 
ATOM   247  C  C   . LEU A 1 30  ? -0.06754  25.10489 23.74568  1.000 21.49762 ? 30  LEU A C   1 
ATOM   248  O  O   . LEU A 1 30  ? 0.81715   24.62135 24.45861  1.000 26.40141 ? 30  LEU A O   1 
ATOM   249  C  CB  . LEU A 1 30  ? 0.26775   24.32980 21.47174  1.000 26.73861 ? 30  LEU A CB  1 
ATOM   250  C  CG  . LEU A 1 30  ? 0.51039   24.62085 20.00853  1.000 27.76618 ? 30  LEU A CG  1 
ATOM   251  C  CD1 . LEU A 1 30  ? 0.67644   23.30831 19.26641  1.000 34.06946 ? 30  LEU A CD1 1 
ATOM   252  C  CD2 . LEU A 1 30  ? -0.68674  25.37977 19.48499  1.000 28.87189 ? 30  LEU A CD2 1 
ATOM   253  N  N   . ASN A 1 31  ? -1.32306  25.22602 24.13520  1.000 20.89781 ? 31  ASN A N   1 
ATOM   254  C  CA  . ASN A 1 31  ? -1.80287  24.52224 25.30416  1.000 18.62968 ? 31  ASN A CA  1 
ATOM   255  C  C   . ASN A 1 31  ? -1.77632  23.01035 25.05860  1.000 19.70126 ? 31  ASN A C   1 
ATOM   256  O  O   . ASN A 1 31  ? -1.82624  22.54434 23.92140  1.000 20.20642 ? 31  ASN A O   1 
ATOM   257  C  CB  . ASN A 1 31  ? -3.24196  24.95938 25.58526  1.000 22.28529 ? 31  ASN A CB  1 
ATOM   258  C  CG  . ASN A 1 31  ? -3.33668  26.44222 25.91061  1.000 28.12474 ? 31  ASN A CG  1 
ATOM   259  O  OD1 . ASN A 1 31  ? -3.88062  27.25161 25.14100  1.000 35.62816 ? 31  ASN A OD1 1 
ATOM   260  N  ND2 . ASN A 1 31  ? -2.77386  26.81127 27.02448  1.000 30.42977 ? 31  ASN A ND2 1 
ATOM   261  N  N   . PHE A 1 32  ? -1.74283  22.24974 26.15748  1.000 22.24353 ? 32  PHE A N   1 
ATOM   262  C  CA  . PHE A 1 32  ? -1.69455  20.78642 26.10867  1.000 22.07571 ? 32  PHE A CA  1 
ATOM   263  C  C   . PHE A 1 32  ? -2.69875  20.20958 25.11908  1.000 19.50261 ? 32  PHE A C   1 
ATOM   264  O  O   . PHE A 1 32  ? -2.36235  19.34855 24.28957  1.000 21.59703 ? 32  PHE A O   1 
ATOM   265  C  CB  . PHE A 1 32  ? -1.99094  20.21827 27.49930  1.000 23.69091 ? 32  PHE A CB  1 
ATOM   266  C  CG  . PHE A 1 32  ? -2.24068  18.74384 27.50298  1.000 21.89997 ? 32  PHE A CG  1 
ATOM   267  C  CD1 . PHE A 1 32  ? -1.18565  17.84683 27.34023  1.000 24.75938 ? 32  PHE A CD1 1 
ATOM   268  C  CD2 . PHE A 1 32  ? -3.53064  18.24869 27.68815  1.000 24.38287 ? 32  PHE A CD2 1 
ATOM   269  C  CE1 . PHE A 1 32  ? -1.41319  16.48043 27.34338  1.000 27.74507 ? 32  PHE A CE1 1 
ATOM   270  C  CE2 . PHE A 1 32  ? -3.76973  16.88455 27.71319  1.000 26.86854 ? 32  PHE A CE2 1 
ATOM   271  C  CZ  . PHE A 1 32  ? -2.70563  15.98887 27.53149  1.000 29.09049 ? 32  PHE A CZ  1 
ATOM   272  N  N   . LYS A 1 33  ? -3.95582  20.64608 25.20214  1.000 19.03684 ? 33  LYS A N   1 
ATOM   273  C  CA  . LYS A 1 33  ? -4.97721  19.99654 24.39769  1.000 22.82123 ? 33  LYS A CA  1 
ATOM   274  C  C   . LYS A 1 33  ? -4.78041  20.23795 22.90672  1.000 19.93690 ? 33  LYS A C   1 
ATOM   275  O  O   . LYS A 1 33  ? -5.36571  19.52435 22.09877  1.000 20.77731 ? 33  LYS A O   1 
ATOM   276  C  CB  . LYS A 1 33  ? -6.37210  20.45708 24.82852  1.000 25.16785 ? 33  LYS A CB  1 
ATOM   277  C  CG  . LYS A 1 33  ? -6.68837  21.90269 24.51181  1.000 29.18499 ? 33  LYS A CG  1 
ATOM   278  C  CD  . LYS A 1 33  ? -8.07328  22.22177 25.05359  1.000 35.06195 ? 33  LYS A CD  1 
ATOM   279  C  CE  . LYS A 1 33  ? -8.49050  23.64351 24.77354  1.000 40.81866 ? 33  LYS A CE  1 
ATOM   280  N  NZ  . LYS A 1 33  ? -8.37558  24.03174 23.33461  1.000 43.07564 ? 33  LYS A NZ  1 
ATOM   281  N  N   . ASP A 1 34  ? -3.97749  21.22525 22.51834  1.000 18.21447 ? 34  ASP A N   1 
ATOM   282  C  CA  . ASP A 1 34  ? -3.89637  21.64465 21.12362  1.000 17.92971 ? 34  ASP A CA  1 
ATOM   283  C  C   . ASP A 1 34  ? -2.65527  21.15523 20.39655  1.000 17.48112 ? 34  ASP A C   1 
ATOM   284  O  O   . ASP A 1 34  ? -2.48298  21.46621 19.21186  1.000 18.72880 ? 34  ASP A O   1 
ATOM   285  C  CB  . ASP A 1 34  ? -3.95585  23.15931 21.06294  1.000 18.53216 ? 34  ASP A CB  1 
ATOM   286  C  CG  . ASP A 1 34  ? -5.24493  23.70102 21.63970  1.000 20.59719 ? 34  ASP A CG  1 
ATOM   287  O  OD1 . ASP A 1 34  ? -6.33169  23.13899 21.36702  1.000 22.26612 ? 34  ASP A OD1 1 
ATOM   288  O  OD2 . ASP A 1 34  ? -5.17536  24.70521 22.36984  1.000 21.99794 ? 34  ASP A OD2 1 
ATOM   289  N  N   . ILE A 1 35  ? -1.81073  20.37872 21.06492  1.000 17.10718 ? 35  ILE A N   1 
ATOM   290  C  CA  . ILE A 1 35  ? -0.54776  19.94154 20.48599  1.000 19.80461 ? 35  ILE A CA  1 
ATOM   291  C  C   . ILE A 1 35  ? -0.74675  19.24707 19.13770  1.000 19.12854 ? 35  ILE A C   1 
ATOM   292  O  O   . ILE A 1 35  ? 0.05606   19.41977 18.20808  1.000 18.51740 ? 35  ILE A O   1 
ATOM   293  C  CB  . ILE A 1 35  ? 0.20190   19.04856 21.49390  1.000 22.89150 ? 35  ILE A CB  1 
ATOM   294  C  CG1 . ILE A 1 35  ? 0.69200   19.85309 22.70803  1.000 25.67141 ? 35  ILE A CG1 1 
ATOM   295  C  CG2 . ILE A 1 35  ? 1.32215   18.36312 20.81249  1.000 24.18171 ? 35  ILE A CG2 1 
ATOM   296  C  CD1 . ILE A 1 35  ? 1.12219   18.96652 23.87812  1.000 31.35947 ? 35  ILE A CD1 1 
ATOM   297  N  N   . ILE A 1 36  ? -1.81118  18.46226 18.99236  1.000 17.73917 ? 36  ILE A N   1 
ATOM   298  C  CA  . ILE A 1 36  ? -2.01813  17.74771 17.73690  1.000 17.37749 ? 36  ILE A CA  1 
ATOM   299  C  C   . ILE A 1 36  ? -2.15054  18.69344 16.54232  1.000 17.39874 ? 36  ILE A C   1 
ATOM   300  O  O   . ILE A 1 36  ? -1.86746  18.30187 15.41154  1.000 16.26754 ? 36  ILE A O   1 
ATOM   301  C  CB  . ILE A 1 36  ? -3.24794  16.80825 17.86328  1.000 15.47313 ? 36  ILE A CB  1 
ATOM   302  C  CG1 . ILE A 1 36  ? -3.28564  15.76357 16.72637  1.000 17.50963 ? 36  ILE A CG1 1 
ATOM   303  C  CG2 . ILE A 1 36  ? -4.51357  17.57302 17.99971  1.000 17.37234 ? 36  ILE A CG2 1 
ATOM   304  C  CD1 . ILE A 1 36  ? -4.34672  14.69268 16.88853  1.000 17.61731 ? 36  ILE A CD1 1 
ATOM   305  N  N   . LEU A 1 37  ? -2.53754  19.94560 16.75144  1.000 17.37673 ? 37  LEU A N   1 
ATOM   306  C  CA  . LEU A 1 37  ? -2.65330  20.86775 15.61969  1.000 17.02608 ? 37  LEU A CA  1 
ATOM   307  C  C   . LEU A 1 37  ? -1.30481  21.10752 14.95896  1.000 15.69533 ? 37  LEU A C   1 
ATOM   308  O  O   . LEU A 1 37  ? -1.22025  21.27435 13.73791  1.000 16.21802 ? 37  LEU A O   1 
ATOM   309  C  CB  . LEU A 1 37  ? -3.25930  22.18370 16.07980  1.000 17.13751 ? 37  LEU A CB  1 
ATOM   310  C  CG  . LEU A 1 37  ? -4.70540  22.10583 16.56427  1.000 18.37457 ? 37  LEU A CG  1 
ATOM   311  C  CD1 . LEU A 1 37  ? -5.11788  23.43602 17.15037  1.000 20.06649 ? 37  LEU A CD1 1 
ATOM   312  C  CD2 . LEU A 1 37  ? -5.69636  21.65159 15.45409  1.000 20.89879 ? 37  LEU A CD2 1 
ATOM   313  N  N   . ARG A 1 38  ? -0.24342  21.18769 15.75483  1.000 16.38366 ? 38  ARG A N   1 
ATOM   314  C  CA  . ARG A 1 38  ? 1.09445   21.35854 15.19581  1.000 16.97103 ? 38  ARG A CA  1 
ATOM   315  C  C   . ARG A 1 38  ? 1.53826   20.09558 14.47988  1.000 16.63419 ? 38  ARG A C   1 
ATOM   316  O  O   . ARG A 1 38  ? 2.19267   20.16397 13.43046  1.000 17.69839 ? 38  ARG A O   1 
ATOM   317  C  CB  . ARG A 1 38  ? 2.09511   21.77273 16.27602  1.000 20.12810 ? 38  ARG A CB  1 
ATOM   318  C  CG  . ARG A 1 38  ? 3.49173   22.06280 15.73667  1.000 21.30499 ? 38  ARG A CG  1 
ATOM   319  C  CD  . ARG A 1 38  ? 4.45452   22.26651 16.88389  1.000 22.54475 ? 38  ARG A CD  1 
ATOM   320  N  NE  . ARG A 1 38  ? 4.07082   23.40484 17.70532  1.000 26.89711 ? 38  ARG A NE  1 
ATOM   321  C  CZ  . ARG A 1 38  ? 4.37933   23.54602 18.98754  1.000 32.62442 ? 38  ARG A CZ  1 
ATOM   322  N  NH1 . ARG A 1 38  ? 4.98281   22.58154 19.66421  1.000 34.48294 ? 38  ARG A NH1 1 
ATOM   323  N  NH2 . ARG A 1 38  ? 4.05316   24.67267 19.61002  1.000 34.63767 ? 38  ARG A NH2 1 
ATOM   324  N  N   . GLU A 1 39  ? 1.12791   18.92053 14.99099  1.000 16.27235 ? 39  GLU A N   1 
ATOM   325  C  CA  . GLU A 1 39  ? 1.41972   17.67117 14.28436  1.000 16.43476 ? 39  GLU A CA  1 
ATOM   326  C  C   . GLU A 1 39  ? 0.73868   17.64737 12.91570  1.000 16.18852 ? 39  GLU A C   1 
ATOM   327  O  O   . GLU A 1 39  ? 1.33006   17.21445 11.91518  1.000 17.45515 ? 39  GLU A O   1 
ATOM   328  C  CB  . GLU A 1 39  ? 0.95232   16.49230 15.14777  1.000 19.06412 ? 39  GLU A CB  1 
ATOM   329  C  CG  . GLU A 1 39  ? 1.66516   16.44055 16.51949  1.000 18.81788 ? 39  GLU A CG  1 
ATOM   330  C  CD  . GLU A 1 39  ? 1.22954   15.27324 17.38478  1.000 22.12117 ? 39  GLU A CD  1 
ATOM   331  O  OE1 . GLU A 1 39  ? 0.03290   14.91989 17.37885  1.000 20.30161 ? 39  GLU A OE1 1 
ATOM   332  O  OE2 . GLU A 1 39  ? 2.07899   14.69736 18.09775  1.000 26.15576 ? 39  GLU A OE2 1 
ATOM   333  N  N   . ILE A 1 40  ? -0.50177  18.12925 12.84365  1.000 15.95573 ? 40  ILE A N   1 
ATOM   334  C  CA  . ILE A 1 40  ? -1.20609  18.24639 11.57083  1.000 16.52641 ? 40  ILE A CA  1 
ATOM   335  C  C   . ILE A 1 40  ? -0.47836  19.21550 10.64909  1.000 16.58104 ? 40  ILE A C   1 
ATOM   336  O  O   . ILE A 1 40  ? -0.25641  18.93663 9.46737   1.000 15.92415 ? 40  ILE A O   1 
ATOM   337  C  CB  . ILE A 1 40  ? -2.64207  18.71026 11.83679  1.000 15.36897 ? 40  ILE A CB  1 
ATOM   338  C  CG1 . ILE A 1 40  ? -3.42183  17.56286 12.48674  1.000 16.76452 ? 40  ILE A CG1 1 
ATOM   339  C  CG2 . ILE A 1 40  ? -3.27720  19.19736 10.51365  1.000 17.24695 ? 40  ILE A CG2 1 
ATOM   340  C  CD1 . ILE A 1 40  ? -4.74989  17.99431 13.10354  1.000 18.03734 ? 40  ILE A CD1 1 
ATOM   341  N  N   . LEU A 1 41  ? -0.11448  20.38225 11.17363  1.000 17.25511 ? 41  LEU A N   1 
ATOM   342  C  CA  . LEU A 1 41  ? 0.48411   21.41392 10.33339  1.000 18.41216 ? 41  LEU A CA  1 
ATOM   343  C  C   . LEU A 1 41  ? 1.80240   20.95566 9.71773   1.000 17.06764 ? 41  LEU A C   1 
ATOM   344  O  O   . LEU A 1 41  ? 2.08580   21.25165 8.55598   1.000 17.53338 ? 41  LEU A O   1 
ATOM   345  C  CB  . LEU A 1 41  ? 0.62764   22.70477 11.13376  1.000 20.00867 ? 41  LEU A CB  1 
ATOM   346  C  CG  . LEU A 1 41  ? 0.92395   23.94668 10.31446  1.000 20.96709 ? 41  LEU A CG  1 
ATOM   347  C  CD1 . LEU A 1 41  ? -0.09804  24.13583 9.18547   1.000 21.07722 ? 41  LEU A CD1 1 
ATOM   348  C  CD2 . LEU A 1 41  ? 0.94040   25.16705 11.22618  1.000 21.21457 ? 41  LEU A CD2 1 
ATOM   349  N  N   A ILE A 1 42  ? 2.63368   20.26404 10.50011  0.500 16.49172 ? 42  ILE A N   1 
ATOM   350  N  N   B ILE A 1 42  ? 2.61125   20.19463 10.45247  0.500 16.58910 ? 42  ILE A N   1 
ATOM   351  C  CA  A ILE A 1 42  ? 3.86702   19.67992 9.97817   0.500 17.25847 ? 42  ILE A CA  1 
ATOM   352  C  CA  B ILE A 1 42  ? 3.87812   19.76809 9.86715   0.500 18.51243 ? 42  ILE A CA  1 
ATOM   353  C  C   A ILE A 1 42  ? 3.57248   18.80708 8.76611   0.500 17.80245 ? 42  ILE A C   1 
ATOM   354  C  C   B ILE A 1 42  ? 3.66413   18.71162 8.78622   0.500 17.97588 ? 42  ILE A C   1 
ATOM   355  O  O   A ILE A 1 42  ? 4.18334   18.95408 7.69911   0.500 17.74745 ? 42  ILE A O   1 
ATOM   356  O  O   B ILE A 1 42  ? 4.44712   18.62284 7.82817   0.500 16.90779 ? 42  ILE A O   1 
ATOM   357  C  CB  A ILE A 1 42  ? 4.59112   18.90354 11.09233  0.500 16.56567 ? 42  ILE A CB  1 
ATOM   358  C  CB  B ILE A 1 42  ? 4.87524   19.31420 10.94429  0.500 20.02599 ? 42  ILE A CB  1 
ATOM   359  C  CG1 A ILE A 1 42  ? 5.14265   19.90258 12.10688  0.500 17.59288 ? 42  ILE A CG1 1 
ATOM   360  C  CG1 B ILE A 1 42  ? 6.24634   19.03922 10.31164  0.500 22.66611 ? 42  ILE A CG1 1 
ATOM   361  C  CG2 A ILE A 1 42  ? 5.69884   17.99374 10.53587  0.500 21.06179 ? 42  ILE A CG2 1 
ATOM   362  C  CG2 B ILE A 1 42  ? 4.33278   18.10691 11.67671  0.500 18.50011 ? 42  ILE A CG2 1 
ATOM   363  C  CD1 A ILE A 1 42  ? 5.69644   19.29080 13.32462  0.500 22.12647 ? 42  ILE A CD1 1 
ATOM   364  C  CD1 B ILE A 1 42  ? 7.18902   18.22064 11.16846  0.500 28.30224 ? 42  ILE A CD1 1 
ATOM   365  N  N   . LEU A 1 43  ? 2.62258   17.88792 8.91224   1.000 16.47544 ? 43  LEU A N   1 
ATOM   366  C  CA  . LEU A 1 43  ? 2.28838   16.99458 7.81667   1.000 16.83828 ? 43  LEU A CA  1 
ATOM   367  C  C   . LEU A 1 43  ? 1.76370   17.75902 6.60109   1.000 16.35746 ? 43  LEU A C   1 
ATOM   368  O  O   . LEU A 1 43  ? 2.04647   17.37968 5.45646   1.000 16.33159 ? 43  LEU A O   1 
ATOM   369  C  CB  . LEU A 1 43  ? 1.27175   15.95333 8.29838   1.000 17.48945 ? 43  LEU A CB  1 
ATOM   370  C  CG  . LEU A 1 43  ? 1.91868   14.91158 9.23086   1.000 18.09336 ? 43  LEU A CG  1 
ATOM   371  C  CD1 . LEU A 1 43  ? 0.85446   14.13003 9.93820   1.000 24.14401 ? 43  LEU A CD1 1 
ATOM   372  C  CD2 . LEU A 1 43  ? 2.84198   13.95038 8.44486   1.000 22.37353 ? 43  LEU A CD2 1 
ATOM   373  N  N   A GLU A 1 44  ? 0.95806   18.80819 6.81514   0.700 16.62901 ? 44  GLU A N   1 
ATOM   374  N  N   B GLU A 1 44  ? 1.01343   18.84003 6.83641   0.300 16.89910 ? 44  GLU A N   1 
ATOM   375  C  CA  A GLU A 1 44  ? 0.47720   19.60031 5.68821   0.700 18.00960 ? 44  GLU A CA  1 
ATOM   376  C  CA  B GLU A 1 44  ? 0.54860   19.67142 5.73715   0.300 15.95967 ? 44  GLU A CA  1 
ATOM   377  C  C   A GLU A 1 44  ? 1.62764   20.26194 4.96052   0.700 16.55026 ? 44  GLU A C   1 
ATOM   378  C  C   B GLU A 1 44  ? 1.69685   20.40869 5.07469   0.300 14.42251 ? 44  GLU A C   1 
ATOM   379  O  O   A GLU A 1 44  ? 1.61912   20.34687 3.73106   0.700 15.76927 ? 44  GLU A O   1 
ATOM   380  O  O   B GLU A 1 44  ? 1.60607   20.74137 3.89351   0.300 17.06341 ? 44  GLU A O   1 
ATOM   381  C  CB  A GLU A 1 44  ? -0.48459  20.67619 6.17176   0.700 19.25178 ? 44  GLU A CB  1 
ATOM   382  C  CB  B GLU A 1 44  ? -0.49189  20.67350 6.22998   0.300 17.97767 ? 44  GLU A CB  1 
ATOM   383  C  CG  A GLU A 1 44  ? -1.83154  20.17372 6.63497   0.700 22.53311 ? 44  GLU A CG  1 
ATOM   384  C  CG  B GLU A 1 44  ? -1.76785  20.05522 6.76783   0.300 21.47248 ? 44  GLU A CG  1 
ATOM   385  C  CD  A GLU A 1 44  ? -2.60378  19.46831 5.53154   0.700 25.62635 ? 44  GLU A CD  1 
ATOM   386  C  CD  B GLU A 1 44  ? -2.75465  21.10229 7.24026   0.300 22.70297 ? 44  GLU A CD  1 
ATOM   387  O  OE1 A GLU A 1 44  ? -2.74410  20.03371 4.41913   0.700 26.50498 ? 44  GLU A OE1 1 
ATOM   388  O  OE1 B GLU A 1 44  ? -2.47718  21.75730 8.26776   0.300 23.19898 ? 44  GLU A OE1 1 
ATOM   389  O  OE2 A GLU A 1 44  ? -3.06762  18.33739 5.77862   0.700 29.71250 ? 44  GLU A OE2 1 
ATOM   390  O  OE2 B GLU A 1 44  ? -3.79618  21.28684 6.57630   0.300 23.32137 ? 44  GLU A OE2 1 
ATOM   391  N  N   A LEU A 1 45  ? 2.63152   20.72499 5.70234   0.500 16.02745 ? 45  LEU A N   1 
ATOM   392  N  N   B LEU A 1 45  ? 2.78263   20.66751 5.80260   0.500 16.63863 ? 45  LEU A N   1 
ATOM   393  C  CA  A LEU A 1 45  ? 3.82458   21.28996 5.08305   0.500 18.08469 ? 45  LEU A CA  1 
ATOM   394  C  CA  B LEU A 1 45  ? 3.93185   21.30693 5.17536   0.500 16.85987 ? 45  LEU A CA  1 
ATOM   395  C  C   A LEU A 1 45  ? 4.55095   20.25381 4.24136   0.500 17.96467 ? 45  LEU A C   1 
ATOM   396  C  C   B LEU A 1 45  ? 4.72690   20.30006 4.35652   0.500 16.49135 ? 45  LEU A C   1 
ATOM   397  O  O   A LEU A 1 45  ? 5.01418   20.56138 3.13360   0.500 18.71511 ? 45  LEU A O   1 
ATOM   398  O  O   B LEU A 1 45  ? 5.35980   20.66594 3.35515   0.500 17.61499 ? 45  LEU A O   1 
ATOM   399  C  CB  A LEU A 1 45  ? 4.76654   21.86017 6.14593   0.500 19.99214 ? 45  LEU A CB  1 
ATOM   400  C  CB  B LEU A 1 45  ? 4.80229   22.00797 6.22501   0.500 17.40165 ? 45  LEU A CB  1 
ATOM   401  C  CG  A LEU A 1 45  ? 4.42289   23.27809 6.58575   0.500 19.03245 ? 45  LEU A CG  1 
ATOM   402  C  CG  B LEU A 1 45  ? 5.88037   22.97944 5.75608   0.500 19.59524 ? 45  LEU A CG  1 
ATOM   403  C  CD1 A LEU A 1 45  ? 5.15379   23.66724 7.86875   0.500 20.05878 ? 45  LEU A CD1 1 
ATOM   404  C  CD1 B LEU A 1 45  ? 5.27418   24.10540 4.90836   0.500 19.87126 ? 45  LEU A CD1 1 
ATOM   405  C  CD2 A LEU A 1 45  ? 4.77979   24.26345 5.48535   0.500 15.81607 ? 45  LEU A CD2 1 
ATOM   406  C  CD2 B LEU A 1 45  ? 6.60418   23.53062 6.98020   0.500 24.40359 ? 45  LEU A CD2 1 
ATOM   407  N  N   . ILE A 1 46  ? 4.69122   19.03011 4.76292   1.000 17.78575 ? 46  ILE A N   1 
ATOM   408  C  CA  . ILE A 1 46  ? 5.29640   17.96132 3.97361   1.000 18.08930 ? 46  ILE A CA  1 
ATOM   409  C  C   . ILE A 1 46  ? 4.53125   17.74992 2.66314   1.000 18.01126 ? 46  ILE A C   1 
ATOM   410  O  O   . ILE A 1 46  ? 5.12569   17.60595 1.58833   1.000 18.43078 ? 46  ILE A O   1 
ATOM   411  C  CB  . ILE A 1 46  ? 5.39746   16.68196 4.81729   1.000 20.83414 ? 46  ILE A CB  1 
ATOM   412  C  CG1 . ILE A 1 46  ? 6.44668   16.88730 5.91632   1.000 23.95533 ? 46  ILE A CG1 1 
ATOM   413  C  CG2 . ILE A 1 46  ? 5.77028   15.48482 3.94357   1.000 24.00338 ? 46  ILE A CG2 1 
ATOM   414  C  CD1 . ILE A 1 46  ? 6.44637   15.81929 6.98375   1.000 24.59465 ? 46  ILE A CD1 1 
ATOM   415  N  N   . VAL A 1 47  ? 3.20099   17.72692 2.73405   1.000 15.72471 ? 47  VAL A N   1 
ATOM   416  C  CA  . VAL A 1 47  ? 2.37316   17.70804 1.53070   1.000 16.98841 ? 47  VAL A CA  1 
ATOM   417  C  C   . VAL A 1 47  ? 2.73770   18.85501 0.60065   1.000 16.82820 ? 47  VAL A C   1 
ATOM   418  O  O   . VAL A 1 47  ? 2.83728   18.66699 -0.62033  1.000 17.15158 ? 47  VAL A O   1 
ATOM   419  C  CB  . VAL A 1 47  ? 0.88227   17.72132 1.92419   1.000 15.39744 ? 47  VAL A CB  1 
ATOM   420  C  CG1 . VAL A 1 47  ? -0.00510  18.03508 0.70024   1.000 16.97688 ? 47  VAL A CG1 1 
ATOM   421  C  CG2 . VAL A 1 47  ? 0.47988   16.35968 2.52056   1.000 18.73001 ? 47  VAL A CG2 1 
ATOM   422  N  N   . GLN A 1 48  ? 2.93925   20.05951 1.15876   1.000 16.53157 ? 48  GLN A N   1 
ATOM   423  C  CA  . GLN A 1 48  ? 3.31928   21.20773 0.33478   1.000 17.31165 ? 48  GLN A CA  1 
ATOM   424  C  C   . GLN A 1 48  ? 4.65669   21.01607 -0.36229  1.000 19.06086 ? 48  GLN A C   1 
ATOM   425  O  O   . GLN A 1 48  ? 4.85250   21.54059 -1.45281  1.000 18.60264 ? 48  GLN A O   1 
ATOM   426  C  CB  . GLN A 1 48  ? 3.35489   22.47331 1.16851   1.000 21.29961 ? 48  GLN A CB  1 
ATOM   427  C  CG  . GLN A 1 48  ? 1.97191   23.04591 1.45702   1.000 19.82274 ? 48  GLN A CG  1 
ATOM   428  C  CD  . GLN A 1 48  ? 2.03110   24.54736 1.57414   1.000 19.33484 ? 48  GLN A CD  1 
ATOM   429  O  OE1 . GLN A 1 48  ? 1.85983   25.09145 2.66885   1.000 19.98316 ? 48  GLN A OE1 1 
ATOM   430  N  NE2 . GLN A 1 48  ? 2.26331   25.24622 0.43585   1.000 17.78834 ? 48  GLN A NE2 1 
ATOM   431  N  N   . ILE A 1 49  ? 5.61550   20.34340 0.26474   1.000 18.71323 ? 49  ILE A N   1 
ATOM   432  C  CA  . ILE A 1 49  ? 6.88587   20.09988 -0.42146  1.000 20.18784 ? 49  ILE A CA  1 
ATOM   433  C  C   . ILE A 1 49  ? 6.64906   19.30953 -1.69609  1.000 20.99861 ? 49  ILE A C   1 
ATOM   434  O  O   . ILE A 1 49  ? 7.14189   19.66987 -2.77689  1.000 19.22908 ? 49  ILE A O   1 
ATOM   435  C  CB  . ILE A 1 49  ? 7.88314   19.37975 0.49911   1.000 20.20536 ? 49  ILE A CB  1 
ATOM   436  C  CG1 . ILE A 1 49  ? 8.26159   20.30809 1.65655   1.000 23.61563 ? 49  ILE A CG1 1 
ATOM   437  C  CG2 . ILE A 1 49  ? 9.10430   18.92182 -0.30326  1.000 24.12116 ? 49  ILE A CG2 1 
ATOM   438  C  CD1 . ILE A 1 49  ? 8.98300   19.62775 2.80549   1.000 25.85501 ? 49  ILE A CD1 1 
ATOM   439  N  N   A ILE A 1 50  ? 5.90549   18.20856 -1.58730  0.500 17.67425 ? 50  ILE A N   1 
ATOM   440  N  N   B ILE A 1 50  ? 5.84180   18.25243 -1.60023  0.500 20.26422 ? 50  ILE A N   1 
ATOM   441  C  CA  A ILE A 1 50  ? 5.57472   17.40541 -2.76725  0.500 16.81407 ? 50  ILE A CA  1 
ATOM   442  C  CA  B ILE A 1 50  ? 5.57608   17.39259 -2.75551  0.500 19.28601 ? 50  ILE A CA  1 
ATOM   443  C  C   A ILE A 1 50  ? 4.83817   18.24733 -3.78949  0.500 18.19904 ? 50  ILE A C   1 
ATOM   444  C  C   B ILE A 1 50  ? 4.75735   18.13365 -3.80082  0.500 18.45102 ? 50  ILE A C   1 
ATOM   445  O  O   A ILE A 1 50  ? 5.23157   18.31106 -4.96004  0.500 17.09570 ? 50  ILE A O   1 
ATOM   446  O  O   B ILE A 1 50  ? 5.02539   18.02604 -5.00492  0.500 19.44913 ? 50  ILE A O   1 
ATOM   447  C  CB  A ILE A 1 50  ? 4.76567   16.15837 -2.37085  0.500 15.39674 ? 50  ILE A CB  1 
ATOM   448  C  CB  B ILE A 1 50  ? 4.90329   16.08421 -2.30000  0.500 20.16020 ? 50  ILE A CB  1 
ATOM   449  C  CG1 A ILE A 1 50  ? 5.65140   15.19565 -1.56396  0.500 20.27420 ? 50  ILE A CG1 1 
ATOM   450  C  CG1 B ILE A 1 50  ? 5.78761   15.36210 -1.27167  0.500 20.88363 ? 50  ILE A CG1 1 
ATOM   451  C  CG2 A ILE A 1 50  ? 4.18730   15.46038 -3.61806  0.500 15.32260 ? 50  ILE A CG2 1 
ATOM   452  C  CG2 B ILE A 1 50  ? 4.54838   15.17748 -3.50465  0.500 19.20815 ? 50  ILE A CG2 1 
ATOM   453  C  CD1 A ILE A 1 50  ? 4.90069   14.39067 -0.48130  0.500 23.04715 ? 50  ILE A CD1 1 
ATOM   454  C  CD1 B ILE A 1 50  ? 7.07547   14.81635 -1.82731  0.500 24.13292 ? 50  ILE A CD1 1 
ATOM   455  N  N   . GLU A 1 51  ? 3.76164   18.91151 -3.35498  1.000 17.03444 ? 51  GLU A N   1 
ATOM   456  C  CA  . GLU A 1 51  ? 2.94977   19.70355 -4.26475  1.000 18.11161 ? 51  GLU A CA  1 
ATOM   457  C  C   . GLU A 1 51  ? 3.79851   20.71617 -5.02558  1.000 17.24950 ? 51  GLU A C   1 
ATOM   458  O  O   . GLU A 1 51  ? 3.65946   20.86182 -6.24087  1.000 17.89911 ? 51  GLU A O   1 
ATOM   459  C  CB  . GLU A 1 51  ? 1.84608   20.43857 -3.48261  1.000 18.94492 ? 51  GLU A CB  1 
ATOM   460  C  CG  . GLU A 1 51  ? 0.87182   21.10066 -4.41846  1.000 18.18458 ? 51  GLU A CG  1 
ATOM   461  C  CD  . GLU A 1 51  ? -0.03015  22.09785 -3.78033  1.000 20.20143 ? 51  GLU A CD  1 
ATOM   462  O  OE1 . GLU A 1 51  ? 0.19264   22.48851 -2.60720  1.000 20.60166 ? 51  GLU A OE1 1 
ATOM   463  O  OE2 . GLU A 1 51  ? -0.97954  22.50078 -4.49228  1.000 22.38091 ? 51  GLU A OE2 1 
ATOM   464  N  N   . PHE A 1 52  ? 4.70764   21.38856 -4.33314  1.000 17.73482 ? 52  PHE A N   1 
ATOM   465  C  CA  . PHE A 1 52  ? 5.50180   22.41982 -4.95704  1.000 18.40501 ? 52  PHE A CA  1 
ATOM   466  C  C   . PHE A 1 52  ? 6.44816   21.82563 -5.99094  1.000 18.74448 ? 52  PHE A C   1 
ATOM   467  O  O   . PHE A 1 52  ? 6.62150   22.39531 -7.07793  1.000 19.63173 ? 52  PHE A O   1 
ATOM   468  C  CB  . PHE A 1 52  ? 6.25306   23.19687 -3.89009  1.000 19.41974 ? 52  PHE A CB  1 
ATOM   469  C  CG  . PHE A 1 52  ? 6.93762   24.41386 -4.41587  1.000 22.42765 ? 52  PHE A CG  1 
ATOM   470  C  CD1 . PHE A 1 52  ? 6.20743   25.53598 -4.80348  1.000 24.98941 ? 52  PHE A CD1 1 
ATOM   471  C  CD2 . PHE A 1 52  ? 8.32210   24.45572 -4.51076  1.000 26.56562 ? 52  PHE A CD2 1 
ATOM   472  C  CE1 . PHE A 1 52  ? 6.83582   26.66169 -5.28981  1.000 28.37180 ? 52  PHE A CE1 1 
ATOM   473  C  CE2 . PHE A 1 52  ? 8.96055   25.58437 -4.99748  1.000 29.17646 ? 52  PHE A CE2 1 
ATOM   474  C  CZ  . PHE A 1 52  ? 8.21987   26.69116 -5.37800  1.000 27.17415 ? 52  PHE A CZ  1 
ATOM   475  N  N   . ILE A 1 53  ? 7.07103   20.68429 -5.67656  1.000 19.22507 ? 53  ILE A N   1 
ATOM   476  C  CA  . ILE A 1 53  ? 7.93005   20.02851 -6.65663  1.000 20.03610 ? 53  ILE A CA  1 
ATOM   477  C  C   . ILE A 1 53  ? 7.13649   19.72580 -7.91888  1.000 17.89609 ? 53  ILE A C   1 
ATOM   478  O  O   . ILE A 1 53  ? 7.60411   19.97970 -9.04439  1.000 19.05117 ? 53  ILE A O   1 
ATOM   479  C  CB  . ILE A 1 53  ? 8.56573   18.75930 -6.06159  1.000 21.73065 ? 53  ILE A CB  1 
ATOM   480  C  CG1 . ILE A 1 53  ? 9.57480   19.12937 -4.96203  1.000 23.33635 ? 53  ILE A CG1 1 
ATOM   481  C  CG2 . ILE A 1 53  ? 9.26150   17.94903 -7.17746  1.000 22.80302 ? 53  ILE A CG2 1 
ATOM   482  C  CD1 . ILE A 1 53  ? 9.94220   17.97397 -4.07774  1.000 27.35659 ? 53  ILE A CD1 1 
ATOM   483  N  N   . PHE A 1 54  ? 5.90964   19.20990 -7.75529  1.000 17.43409 ? 54  PHE A N   1 
ATOM   484  C  CA  . PHE A 1 54  ? 5.06534   18.96919 -8.92346  1.000 18.38242 ? 54  PHE A CA  1 
ATOM   485  C  C   . PHE A 1 54  ? 4.83760   20.24455 -9.72856  1.000 18.36265 ? 54  PHE A C   1 
ATOM   486  O  O   . PHE A 1 54  ? 4.96026   20.23976 -10.96234 1.000 18.12770 ? 54  PHE A O   1 
ATOM   487  C  CB  . PHE A 1 54  ? 3.71820   18.33380 -8.57134  1.000 19.33571 ? 54  PHE A CB  1 
ATOM   488  C  CG  . PHE A 1 54  ? 2.80774   18.30719 -9.76339  1.000 18.34498 ? 54  PHE A CG  1 
ATOM   489  C  CD1 . PHE A 1 54  ? 2.93852   17.29858 -10.73115 1.000 18.34486 ? 54  PHE A CD1 1 
ATOM   490  C  CD2 . PHE A 1 54  ? 1.88975   19.33409 -9.99039  1.000 19.90247 ? 54  PHE A CD2 1 
ATOM   491  C  CE1 . PHE A 1 54  ? 2.14786   17.30262 -11.87643 1.000 18.49811 ? 54  PHE A CE1 1 
ATOM   492  C  CE2 . PHE A 1 54  ? 1.10387   19.34864 -11.13846 1.000 20.53229 ? 54  PHE A CE2 1 
ATOM   493  C  CZ  . PHE A 1 54  ? 1.24446   18.33341 -12.08191 1.000 19.26161 ? 54  PHE A CZ  1 
ATOM   494  N  N   . TYR A 1 55  ? 4.46076   21.33613 -9.05010  1.000 17.61206 ? 55  TYR A N   1 
ATOM   495  C  CA  . TYR A 1 55  ? 4.11847   22.56946 -9.76684  1.000 18.51096 ? 55  TYR A CA  1 
ATOM   496  C  C   . TYR A 1 55  ? 5.31281   23.17179 -10.48587 1.000 18.86366 ? 55  TYR A C   1 
ATOM   497  O  O   . TYR A 1 55  ? 5.15926   23.73864 -11.57938 1.000 19.01751 ? 55  TYR A O   1 
ATOM   498  C  CB  . TYR A 1 55  ? 3.37991   23.57294 -8.85413  1.000 16.04218 ? 55  TYR A CB  1 
ATOM   499  C  CG  . TYR A 1 55  ? 1.92143   23.20132 -8.83207  1.000 15.20591 ? 55  TYR A CG  1 
ATOM   500  C  CD1 . TYR A 1 55  ? 1.42198   22.27977 -7.91160  1.000 16.48905 ? 55  TYR A CD1 1 
ATOM   501  C  CD2 . TYR A 1 55  ? 1.06414   23.69905 -9.77522  1.000 18.20318 ? 55  TYR A CD2 1 
ATOM   502  C  CE1 . TYR A 1 55  ? 0.08151   21.89119 -7.92696  1.000 16.32398 ? 55  TYR A CE1 1 
ATOM   503  C  CE2 . TYR A 1 55  ? -0.26726  23.30687 -9.80807  1.000 20.47560 ? 55  TYR A CE2 1 
ATOM   504  C  CZ  . TYR A 1 55  ? -0.73638  22.38773 -8.88978  1.000 19.19167 ? 55  TYR A CZ  1 
ATOM   505  O  OH  . TYR A 1 55  ? -2.05966  22.01426 -9.01109  1.000 20.54652 ? 55  TYR A OH  1 
ATOM   506  N  N   . ILE A 1 56  ? 6.50579   23.10028 -9.87563  1.000 18.87372 ? 56  ILE A N   1 
ATOM   507  C  CA  . ILE A 1 56  ? 7.70032   23.58319 -10.57541 1.000 19.13424 ? 56  ILE A CA  1 
ATOM   508  C  C   . ILE A 1 56  ? 7.99731   22.70642 -11.78934 1.000 19.21772 ? 56  ILE A C   1 
ATOM   509  O  O   . ILE A 1 56  ? 8.29431   23.21123 -12.88335 1.000 20.14476 ? 56  ILE A O   1 
ATOM   510  C  CB  . ILE A 1 56  ? 8.90052   23.71221 -9.62949  1.000 20.55335 ? 56  ILE A CB  1 
ATOM   511  C  CG1 . ILE A 1 56  ? 8.56572   24.69920 -8.49659  1.000 24.55955 ? 56  ILE A CG1 1 
ATOM   512  C  CG2 . ILE A 1 56  ? 10.16034  24.13659 -10.40755 1.000 24.49352 ? 56  ILE A CG2 1 
ATOM   513  C  CD1 . ILE A 1 56  ? 7.90638   26.03281 -8.96580  1.000 27.16826 ? 56  ILE A CD1 1 
ATOM   514  N  N   . TRP A 1 57  ? 7.94642   21.38509 -11.61914 1.000 20.48603 ? 57  TRP A N   1 
ATOM   515  C  CA  . TRP A 1 57  ? 8.02474   20.46932 -12.75444 1.000 19.60708 ? 57  TRP A CA  1 
ATOM   516  C  C   . TRP A 1 57  ? 7.00028   20.83438 -13.83182 1.000 18.88289 ? 57  TRP A C   1 
ATOM   517  O  O   . TRP A 1 57  ? 7.31599   20.86267 -15.03050 1.000 20.61172 ? 57  TRP A O   1 
ATOM   518  C  CB  . TRP A 1 57  ? 7.79047   19.03098 -12.27468 1.000 20.51202 ? 57  TRP A CB  1 
ATOM   519  C  CG  . TRP A 1 57  ? 7.75349   18.08915 -13.42515 1.000 20.12397 ? 57  TRP A CG  1 
ATOM   520  C  CD1 . TRP A 1 57  ? 8.81772   17.46579 -13.99041 1.000 23.18229 ? 57  TRP A CD1 1 
ATOM   521  C  CD2 . TRP A 1 57  ? 6.59660   17.68393 -14.17513 1.000 20.22934 ? 57  TRP A CD2 1 
ATOM   522  N  NE1 . TRP A 1 57  ? 8.40287   16.69643 -15.05710 1.000 24.22176 ? 57  TRP A NE1 1 
ATOM   523  C  CE2 . TRP A 1 57  ? 7.04353   16.81659 -15.19357 1.000 22.29100 ? 57  TRP A CE2 1 
ATOM   524  C  CE3 . TRP A 1 57  ? 5.23022   17.97257 -14.08570 1.000 20.42249 ? 57  TRP A CE3 1 
ATOM   525  C  CZ2 . TRP A 1 57  ? 6.16873   16.23421 -16.12636 1.000 23.76854 ? 57  TRP A CZ2 1 
ATOM   526  C  CZ3 . TRP A 1 57  ? 4.35143   17.40886 -15.03495 1.000 23.64806 ? 57  TRP A CZ3 1 
ATOM   527  C  CH2 . TRP A 1 57  ? 4.83631   16.53831 -16.02708 1.000 24.20378 ? 57  TRP A CH2 1 
ATOM   528  N  N   . LEU A 1 58  ? 5.77254   21.14062 -13.41738 1.000 17.53344 ? 58  LEU A N   1 
ATOM   529  C  CA  . LEU A 1 58  ? 4.70566   21.43519 -14.37964 1.000 19.53745 ? 58  LEU A CA  1 
ATOM   530  C  C   . LEU A 1 58  ? 5.01331   22.69679 -15.18036 1.000 21.45888 ? 58  LEU A C   1 
ATOM   531  O  O   . LEU A 1 58  ? 4.91067   22.69886 -16.41118 1.000 22.13217 ? 58  LEU A O   1 
ATOM   532  C  CB  . LEU A 1 58  ? 3.34880   21.57488 -13.67981 1.000 19.34156 ? 58  LEU A CB  1 
ATOM   533  C  CG  . LEU A 1 58  ? 2.19985   21.94337 -14.62600 1.000 19.62210 ? 58  LEU A CG  1 
ATOM   534  C  CD1 . LEU A 1 58  ? 1.90693   20.80450 -15.59164 1.000 22.31041 ? 58  LEU A CD1 1 
ATOM   535  C  CD2 . LEU A 1 58  ? 0.96253   22.29803 -13.83428 1.000 20.79042 ? 58  LEU A CD2 1 
ATOM   536  N  N   . ILE A 1 59  ? 5.41013   23.78496 -14.50976 1.000 20.36978 ? 59  ILE A N   1 
ATOM   537  C  CA  . ILE A 1 59  ? 5.57473   25.01713 -15.27627 1.000 23.65621 ? 59  ILE A CA  1 
ATOM   538  C  C   . ILE A 1 59  ? 6.76714   24.91904 -16.20506 1.000 23.46526 ? 59  ILE A C   1 
ATOM   539  O  O   . ILE A 1 59  ? 6.74284   25.48544 -17.30284 1.000 25.14147 ? 59  ILE A O   1 
ATOM   540  C  CB  . ILE A 1 59  ? 5.59767   26.29567 -14.42486 1.000 23.83410 ? 59  ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 59  ? 6.71940   26.28471 -13.39927 1.000 23.57330 ? 59  ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 59  ? 4.26518   26.52239 -13.76465 1.000 24.75351 ? 59  ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 59  ? 6.90145   27.66147 -12.72179 1.000 25.79766 ? 59  ILE A CD1 1 
ATOM   544  N  N   . ILE A 1 60  ? 7.81537   24.18998 -15.80713 1.000 22.62652 ? 60  ILE A N   1 
ATOM   545  C  CA  . ILE A 1 60  ? 8.94785   23.94568 -16.69511 1.000 23.93350 ? 60  ILE A CA  1 
ATOM   546  C  C   . ILE A 1 60  ? 8.52234   23.08042 -17.86869 1.000 24.15370 ? 60  ILE A C   1 
ATOM   547  O  O   . ILE A 1 60  ? 8.86676   23.35925 -19.01933 1.000 27.80407 ? 60  ILE A O   1 
ATOM   548  C  CB  . ILE A 1 60  ? 10.10850  23.32263 -15.90726 1.000 24.26729 ? 60  ILE A CB  1 
ATOM   549  C  CG1 . ILE A 1 60  ? 10.64198  24.36337 -14.92040 1.000 23.28559 ? 60  ILE A CG1 1 
ATOM   550  C  CG2 . ILE A 1 60  ? 11.20733  22.77758 -16.83481 1.000 29.01659 ? 60  ILE A CG2 1 
ATOM   551  C  CD1 . ILE A 1 60  ? 11.66110  23.82488 -13.99410 1.000 25.98437 ? 60  ILE A CD1 1 
ATOM   552  N  N   . THR A 1 61  ? 7.75192   22.02669 -17.59396 1.000 24.54250 ? 61  THR A N   1 
ATOM   553  C  CA  . THR A 1 61  ? 7.38183   21.07571 -18.64291 1.000 27.22158 ? 61  THR A CA  1 
ATOM   554  C  C   . THR A 1 61  ? 6.40558   21.68582 -19.64504 1.000 27.54374 ? 61  THR A C   1 
ATOM   555  O  O   . THR A 1 61  ? 6.46185   21.37328 -20.84337 1.000 28.93492 ? 61  THR A O   1 
ATOM   556  C  CB  . THR A 1 61  ? 6.74949   19.84458 -17.99427 1.000 27.72769 ? 61  THR A CB  1 
ATOM   557  O  OG1 . THR A 1 61  ? 7.73081   19.18302 -17.18480 1.000 28.35220 ? 61  THR A OG1 1 
ATOM   558  C  CG2 . THR A 1 61  ? 6.25875   18.86267 -19.05267 1.000 31.50872 ? 61  THR A CG2 1 
ATOM   559  N  N   . LEU A 1 62  ? 5.51662   22.56678 -19.18495 1.000 28.92890 ? 62  LEU A N   1 
ATOM   560  C  CA  . LEU A 1 62  ? 4.52660   23.15984 -20.08669 1.000 30.55028 ? 62  LEU A CA  1 
ATOM   561  C  C   . LEU A 1 62  ? 5.14838   24.04391 -21.15519 1.000 36.28187 ? 62  LEU A C   1 
ATOM   562  O  O   . LEU A 1 62  ? 4.47748   24.36352 -22.14474 1.000 42.33313 ? 62  LEU A O   1 
ATOM   563  C  CB  . LEU A 1 62  ? 3.48913   23.96113 -19.29666 1.000 31.48103 ? 62  LEU A CB  1 
ATOM   564  C  CG  . LEU A 1 62  ? 2.44416   23.18317 -18.50335 1.000 31.21428 ? 62  LEU A CG  1 
ATOM   565  C  CD1 . LEU A 1 62  ? 1.65199   24.12086 -17.62248 1.000 33.64388 ? 62  LEU A CD1 1 
ATOM   566  C  CD2 . LEU A 1 62  ? 1.51396   22.44589 -19.44761 1.000 32.59672 ? 62  LEU A CD2 1 
ATOM   567  N  N   . GLN A 1 63  ? 6.39907   24.47159 -20.97447 1.000 36.43088 ? 63  GLN A N   1 
ATOM   568  C  CA  . GLN A 1 63  ? 7.07160   25.23388 -22.02094 1.000 40.32334 ? 63  GLN A CA  1 
ATOM   569  C  C   . GLN A 1 63  ? 7.08400   24.46829 -23.33708 1.000 45.50032 ? 63  GLN A C   1 
ATOM   570  O  O   . GLN A 1 63  ? 6.93320   25.06206 -24.41110 1.000 47.43560 ? 63  GLN A O   1 
ATOM   571  C  CB  . GLN A 1 63  ? 8.49967   25.55252 -21.58854 1.000 40.08384 ? 63  GLN A CB  1 
ATOM   572  C  CG  . GLN A 1 63  ? 8.58450   26.47410 -20.39825 1.000 41.84145 ? 63  GLN A CG  1 
ATOM   573  C  CD  . GLN A 1 63  ? 9.94448   26.40769 -19.72653 1.000 47.52083 ? 63  GLN A CD  1 
ATOM   574  O  OE1 . GLN A 1 63  ? 10.60873  25.36575 -19.74000 1.000 43.87910 ? 63  GLN A OE1 1 
ATOM   575  N  NE2 . GLN A 1 63  ? 10.36865  27.52182 -19.13947 1.000 54.03408 ? 63  GLN A NE2 1 
ATOM   576  N  N   . SER A 1 64  ? 7.25313   23.13969 -23.27410 1.000 47.27200 ? 64  SER A N   1 
ATOM   577  C  CA  . SER A 1 64  ? 7.33066   22.29383 -24.45817 1.000 52.77354 ? 64  SER A CA  1 
ATOM   578  C  C   . SER A 1 64  ? 6.48528   21.04248 -24.20997 1.000 54.43220 ? 64  SER A C   1 
ATOM   579  O  O   . SER A 1 64  ? 6.98659   19.92968 -24.07884 1.000 55.67132 ? 64  SER A O   1 
ATOM   580  C  CB  . SER A 1 64  ? 8.77801   21.93669 -24.79818 1.000 55.15535 ? 64  SER A CB  1 
ATOM   581  O  OG  . SER A 1 64  ? 9.38824   21.24389 -23.72608 1.000 57.63615 ? 64  SER A OG  1 
ATOM   582  N  N   . ILE A 1 65  ? 5.17460   21.23574 -24.14028 1.000 54.65537 ? 65  ILE A N   1 
ATOM   583  C  CA  . ILE A 1 65  ? 4.23534   20.14066 -23.93574 1.000 56.88633 ? 65  ILE A CA  1 
ATOM   584  C  C   . ILE A 1 65  ? 3.99016   19.45702 -25.27476 1.000 56.17302 ? 65  ILE A C   1 
ATOM   585  O  O   . ILE A 1 65  ? 3.59058   20.10196 -26.25001 1.000 56.37979 ? 65  ILE A O   1 
ATOM   586  C  CB  . ILE A 1 65  ? 2.91947   20.64420 -23.32349 1.000 56.38225 ? 65  ILE A CB  1 
ATOM   587  N  N   . ASN A 1 66  ? 4.23981   18.15077 -25.32436 1.000 56.21777 ? 66  ASN A N   1 
ATOM   588  C  CA  . ASN A 1 66  ? 3.92394   17.35350 -26.49548 1.000 57.42982 ? 66  ASN A CA  1 
ATOM   589  C  C   . ASN A 1 66  ? 3.02578   16.16753 -26.19678 1.000 55.45855 ? 66  ASN A C   1 
ATOM   590  O  O   . ASN A 1 66  ? 2.46285   15.59234 -27.13573 1.000 59.91035 ? 66  ASN A O   1 
ATOM   591  C  CB  . ASN A 1 66  ? 5.20352   16.84297 -27.17616 1.000 61.69110 ? 66  ASN A CB  1 
ATOM   592  C  CG  . ASN A 1 66  ? 5.00726   16.58644 -28.65747 1.000 65.09415 ? 66  ASN A CG  1 
ATOM   593  O  OD1 . ASN A 1 66  ? 4.46015   17.42842 -29.37820 1.000 66.01919 ? 66  ASN A OD1 1 
ATOM   594  N  ND2 . ASN A 1 66  ? 5.43920   15.41856 -29.11932 1.000 66.26084 ? 66  ASN A ND2 1 
ATOM   595  N  N   . GLU A 1 67  ? 2.87587   15.77974 -24.93478 1.000 46.55638 ? 67  GLU A N   1 
ATOM   596  C  CA  . GLU A 1 67  ? 1.96313   14.71172 -24.57518 1.000 40.92064 ? 67  GLU A CA  1 
ATOM   597  C  C   . GLU A 1 67  ? 1.01727   15.21420 -23.49571 1.000 33.77308 ? 67  GLU A C   1 
ATOM   598  O  O   . GLU A 1 67  ? 1.18987   16.27923 -22.89894 1.000 34.22692 ? 67  GLU A O   1 
ATOM   599  C  CB  . GLU A 1 67  ? 2.68597   13.43420 -24.10165 1.000 47.52054 ? 67  GLU A CB  1 
ATOM   600  C  CG  . GLU A 1 67  ? 3.08821   13.44646 -22.62246 1.000 51.88162 ? 67  GLU A CG  1 
ATOM   601  C  CD  . GLU A 1 67  ? 3.61277   12.10336 -22.10256 1.000 53.10882 ? 67  GLU A CD  1 
ATOM   602  O  OE1 . GLU A 1 67  ? 3.14159   11.03447 -22.55780 1.000 53.93831 ? 67  GLU A OE1 1 
ATOM   603  O  OE2 . GLU A 1 67  ? 4.49486   12.12432 -21.21523 1.000 48.83413 ? 67  GLU A OE2 1 
ATOM   604  N  N   . ASP A 1 68  ? -0.00729  14.43353 -23.25635 1.000 30.60655 ? 68  ASP A N   1 
ATOM   605  C  CA  . ASP A 1 68  ? -0.92750  14.75840 -22.19373 1.000 24.01183 ? 68  ASP A CA  1 
ATOM   606  C  C   . ASP A 1 68  ? -0.23021  14.38883 -20.88532 1.000 25.31475 ? 68  ASP A C   1 
ATOM   607  O  O   . ASP A 1 68  ? -0.10935  13.20198 -20.55492 1.000 29.23798 ? 68  ASP A O   1 
ATOM   608  C  CB  . ASP A 1 68  ? -2.17345  13.92539 -22.42207 1.000 27.95929 ? 68  ASP A CB  1 
ATOM   609  C  CG  . ASP A 1 68  ? -3.19790  14.15093 -21.39961 1.000 25.05058 ? 68  ASP A CG  1 
ATOM   610  O  OD1 . ASP A 1 68  ? -2.85408  14.61208 -20.28647 1.000 23.89319 ? 68  ASP A OD1 1 
ATOM   611  O  OD2 . ASP A 1 68  ? -4.36417  13.88260 -21.71232 1.000 32.98935 ? 68  ASP A OD2 1 
ATOM   612  N  N   . ILE A 1 69  ? 0.19731   15.39582 -20.10439 1.000 23.31201 ? 69  ILE A N   1 
ATOM   613  C  CA  . ILE A 1 69  ? 0.95718   15.14253 -18.87857 1.000 24.86441 ? 69  ILE A CA  1 
ATOM   614  C  C   . ILE A 1 69  ? 0.09606   15.01890 -17.62440 1.000 21.63375 ? 69  ILE A C   1 
ATOM   615  O  O   . ILE A 1 69  ? 0.63351   14.99563 -16.51028 1.000 20.20575 ? 69  ILE A O   1 
ATOM   616  C  CB  . ILE A 1 69  ? 2.07596   16.18641 -18.67256 1.000 29.74673 ? 69  ILE A CB  1 
ATOM   617  C  CG1 . ILE A 1 69  ? 1.56039   17.63688 -18.74861 1.000 31.65780 ? 69  ILE A CG1 1 
ATOM   618  C  CG2 . ILE A 1 69  ? 3.21015   15.96142 -19.68128 1.000 34.99600 ? 69  ILE A CG2 1 
ATOM   619  C  CD1 . ILE A 1 69  ? 0.53241   18.08516 -17.72841 1.000 33.99359 ? 69  ILE A CD1 1 
ATOM   620  N  N   . THR A 1 70  ? -1.22539  14.92006 -17.79007 1.000 20.00672 ? 70  THR A N   1 
ATOM   621  C  CA  . THR A 1 70  ? -2.11641  14.89139 -16.63725 1.000 17.10948 ? 70  THR A CA  1 
ATOM   622  C  C   . THR A 1 70  ? -1.75436  13.76567 -15.67020 1.000 17.57462 ? 70  THR A C   1 
ATOM   623  O  O   . THR A 1 70  ? -1.80835  13.93667 -14.45194 1.000 17.24322 ? 70  THR A O   1 
ATOM   624  C  CB  . THR A 1 70  ? -3.57422  14.78977 -17.06800 1.000 18.10276 ? 70  THR A CB  1 
ATOM   625  O  OG1 . THR A 1 70  ? -3.84967  15.71991 -18.13060 1.000 19.15656 ? 70  THR A OG1 1 
ATOM   626  C  CG2 . THR A 1 70  ? -4.52035  15.06055 -15.90289 1.000 20.25853 ? 70  THR A CG2 1 
ATOM   627  N  N   . TYR A 1 71  ? -1.36673  12.61164 -16.20294 1.000 17.44581 ? 71  TYR A N   1 
ATOM   628  C  CA  . TYR A 1 71  ? -1.06549  11.43524 -15.39052 1.000 18.34390 ? 71  TYR A CA  1 
ATOM   629  C  C   . TYR A 1 71  ? 0.04751   11.69298 -14.36897 1.000 18.40055 ? 71  TYR A C   1 
ATOM   630  O  O   . TYR A 1 71  ? 0.09792   11.00354 -13.33874 1.000 17.27956 ? 71  TYR A O   1 
ATOM   631  C  CB  . TYR A 1 71  ? -0.66410  10.24424 -16.29788 1.000 18.29336 ? 71  TYR A CB  1 
ATOM   632  C  CG  . TYR A 1 71  ? 0.71251   10.37502 -16.91347 1.000 21.46079 ? 71  TYR A CG  1 
ATOM   633  C  CD1 . TYR A 1 71  ? 0.90929   11.08682 -18.09363 1.000 23.81125 ? 71  TYR A CD1 1 
ATOM   634  C  CD2 . TYR A 1 71  ? 1.82205   9.76196  -16.32180 1.000 22.22147 ? 71  TYR A CD2 1 
ATOM   635  C  CE1 . TYR A 1 71  ? 2.17333   11.21290 -18.64257 1.000 25.13854 ? 71  TYR A CE1 1 
ATOM   636  C  CE2 . TYR A 1 71  ? 3.08350   9.89510  -16.85305 1.000 25.53701 ? 71  TYR A CE2 1 
ATOM   637  C  CZ  . TYR A 1 71  ? 3.25554   10.60194 -18.02204 1.000 26.83729 ? 71  TYR A CZ  1 
ATOM   638  O  OH  . TYR A 1 71  ? 4.51869   10.70802 -18.53283 1.000 30.89219 ? 71  TYR A OH  1 
ATOM   639  N  N   . VAL A 1 72  ? 0.93344   12.67151 -14.61053 1.000 17.88993 ? 72  VAL A N   1 
ATOM   640  C  CA  . VAL A 1 72  ? 2.03800   12.91860 -13.69063 1.000 16.83942 ? 72  VAL A CA  1 
ATOM   641  C  C   . VAL A 1 72  ? 1.50686   13.39276 -12.34624 1.000 17.27733 ? 72  VAL A C   1 
ATOM   642  O  O   . VAL A 1 72  ? 2.16165   13.18117 -11.31780 1.000 18.17002 ? 72  VAL A O   1 
ATOM   643  C  CB  . VAL A 1 72  ? 3.07546   13.87217 -14.32832 1.000 18.13714 ? 72  VAL A CB  1 
ATOM   644  C  CG1 . VAL A 1 72  ? 4.17947   14.23666 -13.35222 1.000 20.44032 ? 72  VAL A CG1 1 
ATOM   645  C  CG2 . VAL A 1 72  ? 3.67813   13.21833 -15.57123 1.000 20.79772 ? 72  VAL A CG2 1 
ATOM   646  N  N   . ARG A 1 73  ? 0.31911   13.99712 -12.32822 1.000 16.05365 ? 73  ARG A N   1 
ATOM   647  C  CA  . ARG A 1 73  ? -0.24439  14.41905 -11.05325 1.000 15.19553 ? 73  ARG A CA  1 
ATOM   648  C  C   . ARG A 1 73  ? -0.42438  13.25426 -10.09580 1.000 15.84185 ? 73  ARG A C   1 
ATOM   649  O  O   . ARG A 1 73  ? -0.38483  13.45843 -8.88066  1.000 16.32449 ? 73  ARG A O   1 
ATOM   650  C  CB  . ARG A 1 73  ? -1.60519  15.09255 -11.25484 1.000 15.07160 ? 73  ARG A CB  1 
ATOM   651  C  CG  . ARG A 1 73  ? -1.54111  16.38681 -12.04955 1.000 15.86124 ? 73  ARG A CG  1 
ATOM   652  C  CD  . ARG A 1 73  ? -2.92732  16.96996 -12.27413 1.000 16.92007 ? 73  ARG A CD  1 
ATOM   653  N  NE  . ARG A 1 73  ? -2.84485  18.13919 -13.15138 1.000 16.95319 ? 73  ARG A NE  1 
ATOM   654  C  CZ  . ARG A 1 73  ? -2.60398  19.38252 -12.73847 1.000 15.70651 ? 73  ARG A CZ  1 
ATOM   655  N  NH1 . ARG A 1 73  ? -2.51899  19.68373 -11.44520 1.000 17.09013 ? 73  ARG A NH1 1 
ATOM   656  N  NH2 . ARG A 1 73  ? -2.39257  20.33404 -13.64475 1.000 17.09984 ? 73  ARG A NH2 1 
ATOM   657  N  N   . TYR A 1 74  ? -0.64771  12.04061 -10.61295 1.000 15.94188 ? 74  TYR A N   1 
ATOM   658  C  CA  . TYR A 1 74  ? -0.83834  10.88229 -9.75448  1.000 16.27917 ? 74  TYR A CA  1 
ATOM   659  C  C   . TYR A 1 74  ? 0.39191   10.56025 -8.92050  1.000 15.47179 ? 74  TYR A C   1 
ATOM   660  O  O   . TYR A 1 74  ? 0.25456   9.99784  -7.83002  1.000 17.12523 ? 74  TYR A O   1 
ATOM   661  C  CB  . TYR A 1 74  ? -1.27901  9.67870  -10.60116 1.000 16.29350 ? 74  TYR A CB  1 
ATOM   662  C  CG  . TYR A 1 74  ? -2.69537  9.82696  -11.03096 1.000 16.78448 ? 74  TYR A CG  1 
ATOM   663  C  CD1 . TYR A 1 74  ? -3.03136  10.63601 -12.10624 1.000 17.66199 ? 74  TYR A CD1 1 
ATOM   664  C  CD2 . TYR A 1 74  ? -3.70709  9.16473  -10.35538 1.000 16.14536 ? 74  TYR A CD2 1 
ATOM   665  C  CE1 . TYR A 1 74  ? -4.36197  10.78188 -12.47845 1.000 17.62258 ? 74  TYR A CE1 1 
ATOM   666  C  CE2 . TYR A 1 74  ? -5.03213  9.29462  -10.72217 1.000 17.44588 ? 74  TYR A CE2 1 
ATOM   667  C  CZ  . TYR A 1 74  ? -5.34772  10.09335 -11.79072 1.000 17.69590 ? 74  TYR A CZ  1 
ATOM   668  O  OH  . TYR A 1 74  ? -6.66786  10.19653 -12.11792 1.000 17.27188 ? 74  TYR A OH  1 
ATOM   669  N  N   . PHE A 1 75  ? 1.59676   10.95357 -9.37361  1.000 15.73689 ? 75  PHE A N   1 
ATOM   670  C  CA  . PHE A 1 75  ? 2.81005   10.70768 -8.59468  1.000 17.40189 ? 75  PHE A CA  1 
ATOM   671  C  C   . PHE A 1 75  ? 2.88995   11.62213 -7.38391  1.000 17.67855 ? 75  PHE A C   1 
ATOM   672  O  O   . PHE A 1 75  ? 3.53024   11.26459 -6.37507  1.000 19.38972 ? 75  PHE A O   1 
ATOM   673  C  CB  . PHE A 1 75  ? 4.05415   10.85088 -9.47065  1.000 20.31029 ? 75  PHE A CB  1 
ATOM   674  C  CG  . PHE A 1 75  ? 4.03963   9.93691  -10.67850 1.000 22.54146 ? 75  PHE A CG  1 
ATOM   675  C  CD1 . PHE A 1 75  ? 3.67532   8.59361  -10.57740 1.000 30.02165 ? 75  PHE A CD1 1 
ATOM   676  C  CD2 . PHE A 1 75  ? 4.35775   10.42627 -11.90881 1.000 23.62486 ? 75  PHE A CD2 1 
ATOM   677  C  CE1 . PHE A 1 75  ? 3.63905   7.77268  -11.69551 1.000 33.75464 ? 75  PHE A CE1 1 
ATOM   678  C  CE2 . PHE A 1 75  ? 4.34457   9.60860  -13.00916 1.000 27.91272 ? 75  PHE A CE2 1 
ATOM   679  C  CZ  . PHE A 1 75  ? 3.97576   8.29059  -12.90702 1.000 30.52473 ? 75  PHE A CZ  1 
ATOM   680  N  N   . ASP A 1 76  ? 2.27522   12.81197 -7.47922  1.000 16.23262 ? 76  ASP A N   1 
ATOM   681  C  CA  . ASP A 1 76  ? 2.02563   13.64417 -6.31186  1.000 15.87894 ? 76  ASP A CA  1 
ATOM   682  C  C   . ASP A 1 76  ? 0.92525   13.02841 -5.46280  1.000 14.47351 ? 76  ASP A C   1 
ATOM   683  O  O   . ASP A 1 76  ? 1.13918   12.72705 -4.28790  1.000 16.17808 ? 76  ASP A O   1 
ATOM   684  C  CB  . ASP A 1 76  ? 1.70554   15.05127 -6.85484  1.000 17.32864 ? 76  ASP A CB  1 
ATOM   685  C  CG  . ASP A 1 76  ? 0.95414   15.98208 -5.90067  1.000 18.13120 ? 76  ASP A CG  1 
ATOM   686  O  OD1 . ASP A 1 76  ? 0.42687   15.60682 -4.82685  1.000 19.68908 ? 76  ASP A OD1 1 
ATOM   687  O  OD2 . ASP A 1 76  ? 0.85611   17.16586 -6.29299  1.000 20.36014 ? 76  ASP A OD2 1 
ATOM   688  N  N   . TRP A 1 77  ? -0.25030  12.79229 -6.05503  1.000 15.71258 ? 77  TRP A N   1 
ATOM   689  C  CA  . TRP A 1 77  ? -1.42786  12.39377 -5.28894  1.000 15.00779 ? 77  TRP A CA  1 
ATOM   690  C  C   . TRP A 1 77  ? -1.20046  11.10724 -4.49454  1.000 15.35710 ? 77  TRP A C   1 
ATOM   691  O  O   . TRP A 1 77  ? -1.70481  10.98603 -3.37833  1.000 15.04409 ? 77  TRP A O   1 
ATOM   692  C  CB  . TRP A 1 77  ? -2.64891  12.23562 -6.19469  1.000 14.68041 ? 77  TRP A CB  1 
ATOM   693  C  CG  . TRP A 1 77  ? -3.09209  13.45154 -6.89514  1.000 15.20620 ? 77  TRP A CG  1 
ATOM   694  C  CD1 . TRP A 1 77  ? -2.66400  14.75039 -6.69699  1.000 16.91263 ? 77  TRP A CD1 1 
ATOM   695  C  CD2 . TRP A 1 77  ? -4.03143  13.48906 -7.96504  1.000 15.81480 ? 77  TRP A CD2 1 
ATOM   696  N  NE1 . TRP A 1 77  ? -3.31222  15.58014 -7.57633  1.000 17.16801 ? 77  TRP A NE1 1 
ATOM   697  C  CE2 . TRP A 1 77  ? -4.15089  14.83517 -8.36984  1.000 17.28634 ? 77  TRP A CE2 1 
ATOM   698  C  CE3 . TRP A 1 77  ? -4.78207  12.50411 -8.63793  1.000 16.89676 ? 77  TRP A CE3 1 
ATOM   699  C  CZ2 . TRP A 1 77  ? -5.00088  15.23759 -9.40355  1.000 18.68692 ? 77  TRP A CZ2 1 
ATOM   700  C  CZ3 . TRP A 1 77  ? -5.64988  12.90011 -9.66485  1.000 18.50862 ? 77  TRP A CZ3 1 
ATOM   701  C  CH2 . TRP A 1 77  ? -5.74827  14.26524 -10.03275 1.000 19.06636 ? 77  TRP A CH2 1 
ATOM   702  N  N   . VAL A 1 78  ? -0.46584  10.14052 -5.04539  1.000 15.61357 ? 78  VAL A N   1 
ATOM   703  C  CA  . VAL A 1 78  ? -0.28183  8.87352  -4.33954  1.000 17.07246 ? 78  VAL A CA  1 
ATOM   704  C  C   . VAL A 1 78  ? 0.50151   9.06733  -3.03682  1.000 18.38718 ? 78  VAL A C   1 
ATOM   705  O  O   . VAL A 1 78  ? 0.40239   8.23964  -2.12665  1.000 16.85154 ? 78  VAL A O   1 
ATOM   706  C  CB  . VAL A 1 78  ? 0.35745   7.85185  -5.29991  1.000 16.69549 ? 78  VAL A CB  1 
ATOM   707  C  CG1 . VAL A 1 78  ? 1.82411   8.12672  -5.51923  1.000 18.43710 ? 78  VAL A CG1 1 
ATOM   708  C  CG2 . VAL A 1 78  ? 0.13937   6.42946  -4.81550  1.000 21.75027 ? 78  VAL A CG2 1 
ATOM   709  N  N   . LEU A 1 79  ? 1.28871   10.13500 -2.93132  1.000 17.57570 ? 79  LEU A N   1 
ATOM   710  C  CA  . LEU A 1 79  ? 2.00532   10.49949 -1.71742  1.000 16.55767 ? 79  LEU A CA  1 
ATOM   711  C  C   . LEU A 1 79  ? 1.20901   11.45082 -0.84337  1.000 16.03234 ? 79  LEU A C   1 
ATOM   712  O  O   . LEU A 1 79  ? 1.15868   11.27604 0.38239   1.000 18.19569 ? 79  LEU A O   1 
ATOM   713  C  CB  . LEU A 1 79  ? 3.33059   11.16473 -2.08006  1.000 18.09735 ? 79  LEU A CB  1 
ATOM   714  C  CG  . LEU A 1 79  ? 4.25339   10.29954 -2.95045  1.000 20.70886 ? 79  LEU A CG  1 
ATOM   715  C  CD1 . LEU A 1 79  ? 5.51600   11.07688 -3.25120  1.000 21.17775 ? 79  LEU A CD1 1 
ATOM   716  C  CD2 . LEU A 1 79  ? 4.57966   8.93967  -2.32378  1.000 24.30750 ? 79  LEU A CD2 1 
ATOM   717  N  N   . THR A 1 80  ? 0.56951   12.45055 -1.45648  1.000 15.78696 ? 80  THR A N   1 
ATOM   718  C  CA  . THR A 1 80  ? -0.01728  13.48966 -0.62403  1.000 14.59109 ? 80  THR A CA  1 
ATOM   719  C  C   . THR A 1 80  ? -1.38414  13.09279 -0.09429  1.000 14.04454 ? 80  THR A C   1 
ATOM   720  O  O   . THR A 1 80  ? -1.71546  13.41626 1.05059   1.000 15.18040 ? 80  THR A O   1 
ATOM   721  C  CB  . THR A 1 80  ? -0.12649  14.81920 -1.40300  1.000 15.27923 ? 80  THR A CB  1 
ATOM   722  O  OG1 . THR A 1 80  ? -0.88282  14.58008 -2.59102  1.000 15.70390 ? 80  THR A OG1 1 
ATOM   723  C  CG2 . THR A 1 80  ? 1.22454   15.38356 -1.72755  1.000 16.37915 ? 80  THR A CG2 1 
ATOM   724  N  N   . THR A 1 81  ? -2.21093  12.44158 -0.90741  1.000 15.27578 ? 81  THR A N   1 
ATOM   725  C  CA  . THR A 1 81  ? -3.56663  12.17395 -0.44503  1.000 16.02642 ? 81  THR A CA  1 
ATOM   726  C  C   . THR A 1 81  ? -3.63613  11.26266 0.77858   1.000 14.57751 ? 81  THR A C   1 
ATOM   727  O  O   . THR A 1 81  ? -4.48459  11.53904 1.64287   1.000 15.10884 ? 81  THR A O   1 
ATOM   728  C  CB  . THR A 1 81  ? -4.50616  11.71192 -1.57103  1.000 14.96218 ? 81  THR A CB  1 
ATOM   729  O  OG1 . THR A 1 81  ? -4.04849  10.47871 -2.13620  1.000 14.93520 ? 81  THR A OG1 1 
ATOM   730  C  CG2 . THR A 1 81  ? -4.64200  12.80725 -2.68842  1.000 16.20121 ? 81  THR A CG2 1 
ATOM   731  N  N   . PRO A 1 82  ? -2.82065  10.21787 0.93699   1.000 14.65113 ? 82  PRO A N   1 
ATOM   732  C  CA  . PRO A 1 82  ? -2.91545  9.47103  2.20336   1.000 16.53875 ? 82  PRO A CA  1 
ATOM   733  C  C   . PRO A 1 82  ? -2.54294  10.31983 3.40316   1.000 16.76596 ? 82  PRO A C   1 
ATOM   734  O  O   . PRO A 1 82  ? -3.15881  10.19120 4.46632   1.000 16.17638 ? 82  PRO A O   1 
ATOM   735  C  CB  . PRO A 1 82  ? -1.96583  8.28543  2.00599   1.000 17.36448 ? 82  PRO A CB  1 
ATOM   736  C  CG  . PRO A 1 82  ? -1.06827  8.68405  0.91263   1.000 17.49120 ? 82  PRO A CG  1 
ATOM   737  C  CD  . PRO A 1 82  ? -1.88780  9.55260  0.00326   1.000 15.66603 ? 82  PRO A CD  1 
ATOM   738  N  N   . VAL A 1 83  ? -1.55129  11.19233 3.25236   1.000 15.96983 ? 83  VAL A N   1 
ATOM   739  C  CA  . VAL A 1 83  ? -1.19166  12.08071 4.35703   1.000 15.62589 ? 83  VAL A CA  1 
ATOM   740  C  C   . VAL A 1 83  ? -2.37131  12.97921 4.70997   1.000 14.97091 ? 83  VAL A C   1 
ATOM   741  O  O   . VAL A 1 83  ? -2.64947  13.22711 5.89204   1.000 16.10110 ? 83  VAL A O   1 
ATOM   742  C  CB  . VAL A 1 83  ? 0.09084   12.87460 4.02356   1.000 17.53746 ? 83  VAL A CB  1 
ATOM   743  C  CG1 . VAL A 1 83  ? 0.43463   13.86945 5.13667   1.000 18.16659 ? 83  VAL A CG1 1 
ATOM   744  C  CG2 . VAL A 1 83  ? 1.26134   11.92944 3.78332   1.000 18.27904 ? 83  VAL A CG2 1 
ATOM   745  N  N   . MET A 1 84  ? -3.04353  13.52872 3.68679   1.000 15.19393 ? 84  MET A N   1 
ATOM   746  C  CA  . MET A 1 84  ? -4.16784  14.42955 3.91134   1.000 15.09431 ? 84  MET A CA  1 
ATOM   747  C  C   . MET A 1 84  ? -5.30669  13.69181 4.60038   1.000 14.99209 ? 84  MET A C   1 
ATOM   748  O  O   . MET A 1 84  ? -6.00066  14.26295 5.45154   1.000 15.83568 ? 84  MET A O   1 
ATOM   749  C  CB  . MET A 1 84  ? -4.63974  14.99154 2.57067   1.000 14.79380 ? 84  MET A CB  1 
ATOM   750  C  CG  . MET A 1 84  ? -3.59870  15.88372 1.94804   1.000 14.92923 ? 84  MET A CG  1 
ATOM   751  S  SD  . MET A 1 84  ? -3.97185  16.29173 0.22582   1.000 17.18666 ? 84  MET A SD  1 
ATOM   752  C  CE  . MET A 1 84  ? -5.36783  17.41782 0.42852   1.000 19.73501 ? 84  MET A CE  1 
ATOM   753  N  N   . LEU A 1 85  ? -5.51167  12.41264 4.24963   1.000 14.50651 ? 85  LEU A N   1 
ATOM   754  C  CA  . LEU A 1 85  ? -6.54443  11.63904 4.93199   1.000 15.59350 ? 85  LEU A CA  1 
ATOM   755  C  C   . LEU A 1 85  ? -6.16775  11.43361 6.40674   1.000 17.68607 ? 85  LEU A C   1 
ATOM   756  O  O   . LEU A 1 85  ? -7.00808  11.56219 7.30594   1.000 17.23317 ? 85  LEU A O   1 
ATOM   757  C  CB  . LEU A 1 85  ? -6.78582  10.29892 4.22923   1.000 15.49193 ? 85  LEU A CB  1 
ATOM   758  C  CG  . LEU A 1 85  ? -7.51082  10.45636 2.89603   1.000 14.85351 ? 85  LEU A CG  1 
ATOM   759  C  CD1 . LEU A 1 85  ? -7.31365  9.21489  2.06042   1.000 18.88498 ? 85  LEU A CD1 1 
ATOM   760  C  CD2 . LEU A 1 85  ? -9.00723  10.71790 3.08515   1.000 17.75080 ? 85  LEU A CD2 1 
ATOM   761  N  N   . LEU A 1 86  ? -4.89674  11.15083 6.67980   1.000 16.05598 ? 86  LEU A N   1 
ATOM   762  C  CA  . LEU A 1 86  ? -4.46318  11.00976 8.06010   1.000 18.20985 ? 86  LEU A CA  1 
ATOM   763  C  C   . LEU A 1 86  ? -4.65713  12.30880 8.82658   1.000 16.87408 ? 86  LEU A C   1 
ATOM   764  O  O   . LEU A 1 86  ? -5.15494  12.29435 9.94956   1.000 16.05686 ? 86  LEU A O   1 
ATOM   765  C  CB  . LEU A 1 86  ? -3.00318  10.56149 8.11033   1.000 20.37901 ? 86  LEU A CB  1 
ATOM   766  C  CG  . LEU A 1 86  ? -2.70462  9.12767  7.66788   1.000 23.94251 ? 86  LEU A CG  1 
ATOM   767  C  CD1 . LEU A 1 86  ? -1.18670  8.92771  7.75604   1.000 26.75512 ? 86  LEU A CD1 1 
ATOM   768  C  CD2 . LEU A 1 86  ? -3.45297  8.06506  8.50841   1.000 25.64372 ? 86  LEU A CD2 1 
ATOM   769  N  N   . THR A 1 87  ? -4.25275  13.44201 8.24484   1.000 17.03611 ? 87  THR A N   1 
ATOM   770  C  CA  . THR A 1 87  ? -4.40899  14.70193 8.96232   1.000 17.53765 ? 87  THR A CA  1 
ATOM   771  C  C   . THR A 1 87  ? -5.86614  15.02608 9.20983   1.000 15.90087 ? 87  THR A C   1 
ATOM   772  O  O   . THR A 1 87  ? -6.18872  15.62570 10.23132  1.000 17.32510 ? 87  THR A O   1 
ATOM   773  C  CB  . THR A 1 87  ? -3.69405  15.88933 8.31814   1.000 17.59416 ? 87  THR A CB  1 
ATOM   774  O  OG1 . THR A 1 87  ? -4.23430  16.14049 7.02748   1.000 20.49756 ? 87  THR A OG1 1 
ATOM   775  C  CG2 . THR A 1 87  ? -2.19336  15.67908 8.26362   1.000 20.01286 ? 87  THR A CG2 1 
ATOM   776  N  N   A THR A 1 88  ? -6.74061  14.67565 8.26165   0.500 16.67174 ? 88  THR A N   1 
ATOM   777  N  N   B THR A 1 88  ? -6.77179  14.60586 8.31758   0.500 17.17271 ? 88  THR A N   1 
ATOM   778  C  CA  A THR A 1 88  ? -8.17685  14.82897 8.46212   0.500 15.34221 ? 88  THR A CA  1 
ATOM   779  C  CA  B THR A 1 88  ? -8.18823  14.88925 8.54415   0.500 19.77818 ? 88  THR A CA  1 
ATOM   780  C  C   A THR A 1 88  ? -8.62374  14.02801 9.68171   0.500 14.50322 ? 88  THR A C   1 
ATOM   781  C  C   B THR A 1 88  ? -8.77044  13.97238 9.61246   0.500 16.74104 ? 88  THR A C   1 
ATOM   782  O  O   A THR A 1 88  ? -9.24915  14.56253 10.60515  0.500 12.37180 ? 88  THR A O   1 
ATOM   783  O  O   B THR A 1 88  ? -9.67148  14.37770 10.35554  0.500 17.17471 ? 88  THR A O   1 
ATOM   784  C  CB  A THR A 1 88  ? -8.91257  14.41497 7.17842   0.500 15.26280 ? 88  THR A CB  1 
ATOM   785  C  CB  B THR A 1 88  ? -8.98839  14.84286 7.23944   0.500 24.17223 ? 88  THR A CB  1 
ATOM   786  O  OG1 A THR A 1 88  ? -8.53883  15.30177 6.12460   0.500 16.05247 ? 88  THR A OG1 1 
ATOM   787  O  OG1 B THR A 1 88  ? -10.11997 15.72667 7.34381   0.500 29.82711 ? 88  THR A OG1 1 
ATOM   788  C  CG2 A THR A 1 88  ? -10.42646 14.51087 7.34695   0.500 16.51657 ? 88  THR A CG2 1 
ATOM   789  C  CG2 B THR A 1 88  ? -9.49544  13.44771 6.96369   0.500 23.40342 ? 88  THR A CG2 1 
ATOM   790  N  N   . VAL A 1 89  ? -8.25076  12.74814 9.72889   1.000 15.08009 ? 89  VAL A N   1 
ATOM   791  C  CA  . VAL A 1 89  ? -8.56236  11.91754 10.89132  1.000 15.11656 ? 89  VAL A CA  1 
ATOM   792  C  C   . VAL A 1 89  ? -8.08941  12.59256 12.17503  1.000 15.13946 ? 89  VAL A C   1 
ATOM   793  O  O   . VAL A 1 89  ? -8.83376  12.69210 13.16298  1.000 15.17514 ? 89  VAL A O   1 
ATOM   794  C  CB  . VAL A 1 89  ? -7.91474  10.52843 10.73985  1.000 16.25745 ? 89  VAL A CB  1 
ATOM   795  C  CG1 . VAL A 1 89  ? -8.04002  9.74735  12.07375  1.000 17.90247 ? 89  VAL A CG1 1 
ATOM   796  C  CG2 . VAL A 1 89  ? -8.58114  9.70714  9.63632   1.000 17.16677 ? 89  VAL A CG2 1 
ATOM   797  N  N   . TYR A 1 90  ? -6.84252  13.07517 12.18148  1.000 15.80896 ? 90  TYR A N   1 
ATOM   798  C  CA  . TYR A 1 90  ? -6.33397  13.74094 13.37978  1.000 14.38675 ? 90  TYR A CA  1 
ATOM   799  C  C   . TYR A 1 90  ? -7.20474  14.93823 13.73608  1.000 14.37084 ? 90  TYR A C   1 
ATOM   800  O  O   . TYR A 1 90  ? -7.45879  15.18611 14.91633  1.000 15.11490 ? 90  TYR A O   1 
ATOM   801  C  CB  . TYR A 1 90  ? -4.89140  14.18892 13.17660  1.000 15.79703 ? 90  TYR A CB  1 
ATOM   802  C  CG  . TYR A 1 90  ? -3.93202  13.06113 12.85605  1.000 16.54071 ? 90  TYR A CG  1 
ATOM   803  C  CD1 . TYR A 1 90  ? -4.22491  11.72664 13.18464  1.000 16.55812 ? 90  TYR A CD1 1 
ATOM   804  C  CD2 . TYR A 1 90  ? -2.73491  13.33820 12.18051  1.000 17.53973 ? 90  TYR A CD2 1 
ATOM   805  C  CE1 . TYR A 1 90  ? -3.35085  10.68833 12.87339  1.000 18.24917 ? 90  TYR A CE1 1 
ATOM   806  C  CE2 . TYR A 1 90  ? -1.88195  12.29861 11.82355  1.000 19.94062 ? 90  TYR A CE2 1 
ATOM   807  C  CZ  . TYR A 1 90  ? -2.18084  10.99247 12.19565  1.000 18.64377 ? 90  TYR A CZ  1 
ATOM   808  O  OH  . TYR A 1 90  ? -1.29364  10.01416 11.82201  1.000 23.26032 ? 90  TYR A OH  1 
ATOM   809  N  N   . PHE A 1 91  ? -7.61748  15.72881 12.74374  1.000 15.71564 ? 91  PHE A N   1 
ATOM   810  C  CA  . PHE A 1 91  ? -8.45305  16.88633 13.06348  1.000 14.52575 ? 91  PHE A CA  1 
ATOM   811  C  C   . PHE A 1 91  ? -9.82205  16.50956 13.61958  1.000 15.26022 ? 91  PHE A C   1 
ATOM   812  O  O   . PHE A 1 91  ? -10.29856 17.14156 14.57127  1.000 16.16539 ? 91  PHE A O   1 
ATOM   813  C  CB  . PHE A 1 91  ? -8.56946  17.83223 11.87516  1.000 15.87977 ? 91  PHE A CB  1 
ATOM   814  C  CG  . PHE A 1 91  ? -9.19727  19.12571 12.26816  1.000 16.29216 ? 91  PHE A CG  1 
ATOM   815  C  CD1 . PHE A 1 91  ? -8.47426  20.02804 13.03668  1.000 16.88089 ? 91  PHE A CD1 1 
ATOM   816  C  CD2 . PHE A 1 91  ? -10.54016 19.38876 11.99784  1.000 19.57631 ? 91  PHE A CD2 1 
ATOM   817  C  CE1 . PHE A 1 91  ? -9.06682  21.20072 13.49187  1.000 17.52002 ? 91  PHE A CE1 1 
ATOM   818  C  CE2 . PHE A 1 91  ? -11.12493 20.55833 12.44937  1.000 19.29147 ? 91  PHE A CE2 1 
ATOM   819  C  CZ  . PHE A 1 91  ? -10.38602 21.46744 13.21167  1.000 18.89813 ? 91  PHE A CZ  1 
ATOM   820  N  N   . PHE A 1 92  ? -10.47440 15.49875 13.04025  1.000 15.94560 ? 92  PHE A N   1 
ATOM   821  C  CA  . PHE A 1 92  ? -11.72703 15.03455 13.61410  1.000 16.33755 ? 92  PHE A CA  1 
ATOM   822  C  C   . PHE A 1 92  ? -11.53597 14.56249 15.04368  1.000 15.97864 ? 92  PHE A C   1 
ATOM   823  O  O   . PHE A 1 92  ? -12.34723 14.88640 15.92082  1.000 16.51627 ? 92  PHE A O   1 
ATOM   824  C  CB  . PHE A 1 92  ? -12.34287 13.92908 12.76220  1.000 17.11131 ? 92  PHE A CB  1 
ATOM   825  C  CG  . PHE A 1 92  ? -13.10777 14.44960 11.57770  1.000 17.28315 ? 92  PHE A CG  1 
ATOM   826  C  CD1 . PHE A 1 92  ? -14.30237 15.11795 11.73826  1.000 19.76341 ? 92  PHE A CD1 1 
ATOM   827  C  CD2 . PHE A 1 92  ? -12.61738 14.27566 10.29945  1.000 23.94300 ? 92  PHE A CD2 1 
ATOM   828  C  CE1 . PHE A 1 92  ? -14.99403 15.60009 10.63022  1.000 20.61377 ? 92  PHE A CE1 1 
ATOM   829  C  CE2 . PHE A 1 92  ? -13.31300 14.75238 9.18938   1.000 23.69968 ? 92  PHE A CE2 1 
ATOM   830  C  CZ  . PHE A 1 92  ? -14.49564 15.41500 9.36306   1.000 21.89015 ? 92  PHE A CZ  1 
ATOM   831  N  N   . GLU A 1 93  ? -10.45532 13.81527 15.30088  1.000 15.28292 ? 93  GLU A N   1 
ATOM   832  C  CA  . GLU A 1 93  ? -10.18119 13.34293 16.64829  1.000 16.66073 ? 93  GLU A CA  1 
ATOM   833  C  C   . GLU A 1 93  ? -9.97956  14.52608 17.57940  1.000 16.93590 ? 93  GLU A C   1 
ATOM   834  O  O   . GLU A 1 93  ? -10.51631 14.55024 18.68748  1.000 17.68411 ? 93  GLU A O   1 
ATOM   835  C  CB  . GLU A 1 93  ? -8.95907  12.43745 16.65136  1.000 16.33675 ? 93  GLU A CB  1 
ATOM   836  C  CG  . GLU A 1 93  ? -9.27951  11.06645 16.05052  1.000 18.12111 ? 93  GLU A CG  1 
ATOM   837  C  CD  . GLU A 1 93  ? -10.01663 10.18555 17.02102  1.000 22.72499 ? 93  GLU A CD  1 
ATOM   838  O  OE1 . GLU A 1 93  ? -9.37160  9.63939  17.91393  1.000 29.66780 ? 93  GLU A OE1 1 
ATOM   839  O  OE2 . GLU A 1 93  ? -11.24700 10.05289 16.90889  1.000 28.46269 ? 93  GLU A OE2 1 
ATOM   840  N  N   . TYR A 1 94  ? -9.24600  15.54273 17.12230  1.000 17.00183 ? 94  TYR A N   1 
ATOM   841  C  CA  . TYR A 1 94  ? -9.07265  16.76179 17.90265  1.000 16.64066 ? 94  TYR A CA  1 
ATOM   842  C  C   . TYR A 1 94  ? -10.41347 17.41128 18.21931  1.000 16.40698 ? 94  TYR A C   1 
ATOM   843  O  O   . TYR A 1 94  ? -10.68368 17.76929 19.37663  1.000 19.35943 ? 94  TYR A O   1 
ATOM   844  C  CB  . TYR A 1 94  ? -8.17709  17.71471 17.12401  1.000 17.75667 ? 94  TYR A CB  1 
ATOM   845  C  CG  . TYR A 1 94  ? -8.13125  19.09380 17.73151  1.000 18.18494 ? 94  TYR A CG  1 
ATOM   846  C  CD1 . TYR A 1 94  ? -7.45902  19.32684 18.93954  1.000 17.93389 ? 94  TYR A CD1 1 
ATOM   847  C  CD2 . TYR A 1 94  ? -8.74701  20.16772 17.09147  1.000 20.09229 ? 94  TYR A CD2 1 
ATOM   848  C  CE1 . TYR A 1 94  ? -7.41250  20.59736 19.49249  1.000 19.24611 ? 94  TYR A CE1 1 
ATOM   849  C  CE2 . TYR A 1 94  ? -8.71252  21.43553 17.64518  1.000 20.37239 ? 94  TYR A CE2 1 
ATOM   850  C  CZ  . TYR A 1 94  ? -8.06320  21.64556 18.85114  1.000 18.39022 ? 94  TYR A CZ  1 
ATOM   851  O  OH  . TYR A 1 94  ? -8.01744  22.92487 19.39291  1.000 21.93581 ? 94  TYR A OH  1 
ATOM   852  N  N   . MET A 1 95  ? -11.26149 17.59963 17.20651  1.000 17.98057 ? 95  MET A N   1 
ATOM   853  C  CA  . MET A 1 95  ? -12.54958 18.24790 17.44627  1.000 19.35798 ? 95  MET A CA  1 
ATOM   854  C  C   . MET A 1 95  ? -13.42989 17.43953 18.39047  1.000 19.05838 ? 95  MET A C   1 
ATOM   855  O  O   . MET A 1 95  ? -14.21667 18.01531 19.15447  1.000 22.36979 ? 95  MET A O   1 
ATOM   856  C  CB  . MET A 1 95  ? -13.33433 18.37198 16.13383  1.000 23.48009 ? 95  MET A CB  1 
ATOM   857  C  CG  . MET A 1 95  ? -12.98601 19.50558 15.22950  1.000 27.74092 ? 95  MET A CG  1 
ATOM   858  S  SD  . MET A 1 95  ? -14.38950 19.90719 14.11077  1.000 24.99667 ? 95  MET A SD  1 
ATOM   859  C  CE  . MET A 1 95  ? -14.49352 18.43225 13.15971  1.000 23.22458 ? 95  MET A CE  1 
ATOM   860  N  N   . ASN A 1 96  ? -13.35717 16.10705 18.32476  1.000 19.05101 ? 96  ASN A N   1 
ATOM   861  C  CA  . ASN A 1 96  ? -14.38846 15.25935 18.90447  1.000 20.16011 ? 96  ASN A CA  1 
ATOM   862  C  C   . ASN A 1 96  ? -13.99077 14.57888 20.20755  1.000 20.99453 ? 96  ASN A C   1 
ATOM   863  O  O   . ASN A 1 96  ? -14.85299 14.00714 20.87535  1.000 25.21030 ? 96  ASN A O   1 
ATOM   864  C  CB  . ASN A 1 96  ? -14.87424 14.21433 17.87843  1.000 19.82440 ? 96  ASN A CB  1 
ATOM   865  C  CG  . ASN A 1 96  ? -15.55874 14.86424 16.68826  1.000 18.23914 ? 96  ASN A CG  1 
ATOM   866  O  OD1 . ASN A 1 96  ? -16.13615 15.94913 16.80943  1.000 19.89229 ? 96  ASN A OD1 1 
ATOM   867  N  ND2 . ASN A 1 96  ? -15.50307 14.21410 15.52262  1.000 19.21020 ? 96  ASN A ND2 1 
ATOM   868  N  N   A SER A 1 97  ? -12.72703 14.63831 20.60622  0.500 22.02080 ? 97  SER A N   1 
ATOM   869  N  N   B SER A 1 97  ? -12.72094 14.61354 20.58732  0.500 23.64464 ? 97  SER A N   1 
ATOM   870  C  CA  A SER A 1 97  ? -12.27299 13.94187 21.80115  0.500 23.76534 ? 97  SER A CA  1 
ATOM   871  C  CA  B SER A 1 97  ? -12.28222 13.96086 21.80957  0.500 26.45567 ? 97  SER A CA  1 
ATOM   872  C  C   A SER A 1 97  ? -12.37691 14.88044 23.00156  0.500 28.66969 ? 97  SER A C   1 
ATOM   873  C  C   B SER A 1 97  ? -12.48288 14.91951 22.97426  0.500 29.41309 ? 97  SER A C   1 
ATOM   874  O  O   A SER A 1 97  ? -11.91597 16.02567 22.94629  0.500 31.37090 ? 97  SER A O   1 
ATOM   875  O  O   B SER A 1 97  ? -12.19253 16.11576 22.86546  0.500 30.75619 ? 97  SER A O   1 
ATOM   876  C  CB  A SER A 1 97  ? -10.83379 13.46761 21.60299  0.500 26.83784 ? 97  SER A CB  1 
ATOM   877  C  CB  B SER A 1 97  ? -10.81134 13.57410 21.70321  0.500 32.37197 ? 97  SER A CB  1 
ATOM   878  O  OG  A SER A 1 97  ? -10.71739 12.59040 20.48675  0.500 28.80459 ? 97  SER A OG  1 
ATOM   879  O  OG  B SER A 1 97  ? -10.00430 14.72877 21.60112  0.500 32.67805 ? 97  SER A OG  1 
ATOM   880  N  N   . ASP A 1 98  ? -12.98657 14.39236 24.08743  1.000 34.64746 ? 98  ASP A N   1 
ATOM   881  C  CA  . ASP A 1 98  ? -13.23540 15.24305 25.25201  1.000 35.03650 ? 98  ASP A CA  1 
ATOM   882  C  C   . ASP A 1 98  ? -11.93936 15.66004 25.92361  1.000 35.76593 ? 98  ASP A C   1 
ATOM   883  O  O   . ASP A 1 98  ? -11.87257 16.73363 26.53567  1.000 38.97581 ? 98  ASP A O   1 
ATOM   884  C  CB  . ASP A 1 98  ? -14.09923 14.49624 26.26336  1.000 40.61384 ? 98  ASP A CB  1 
ATOM   885  C  CG  . ASP A 1 98  ? -13.50620 13.15554 26.64777  1.000 41.91460 ? 98  ASP A CG  1 
ATOM   886  N  N   . ASP A 1 99  ? -10.91542 14.82628 25.82566  1.000 32.86539 ? 99  ASP A N   1 
ATOM   887  C  CA  . ASP A 1 99  ? -9.62080  15.06379 26.44244  1.000 33.09624 ? 99  ASP A CA  1 
ATOM   888  C  C   . ASP A 1 99  ? -8.57572  15.23705 25.34615  1.000 28.33920 ? 99  ASP A C   1 
ATOM   889  O  O   . ASP A 1 99  ? -8.80751  14.86356 24.19046  1.000 28.32179 ? 99  ASP A O   1 
ATOM   890  C  CB  . ASP A 1 99  ? -9.25122  13.86336 27.31917  1.000 39.29779 ? 99  ASP A CB  1 
ATOM   891  N  N   . GLY A 1 100 ? -7.42538  15.80332 25.71673  1.000 28.65679 ? 100 GLY A N   1 
ATOM   892  C  CA  . GLY A 1 100 ? -6.34109  15.96779 24.75904  1.000 24.20189 ? 100 GLY A CA  1 
ATOM   893  C  C   . GLY A 1 100 ? -5.94596  14.63912 24.12622  1.000 28.40957 ? 100 GLY A C   1 
ATOM   894  O  O   . GLY A 1 100 ? -5.85665  13.60916 24.79374  1.000 26.95169 ? 100 GLY A O   1 
ATOM   895  N  N   . ILE A 1 101 ? -5.70369  14.66358 22.81919  1.000 20.01464 ? 101 ILE A N   1 
ATOM   896  C  CA  . ILE A 1 101 ? -5.32046  13.47106 22.06849  1.000 17.45935 ? 101 ILE A CA  1 
ATOM   897  C  C   . ILE A 1 101 ? -4.22871  13.87444 21.08934  1.000 15.97080 ? 101 ILE A C   1 
ATOM   898  O  O   . ILE A 1 101 ? -4.22619  14.99000 20.54972  1.000 20.36822 ? 101 ILE A O   1 
ATOM   899  C  CB  . ILE A 1 101 ? -6.54019  12.83880 21.36461  1.000 20.84591 ? 101 ILE A CB  1 
ATOM   900  C  CG1 . ILE A 1 101 ? -6.16043  11.44922 20.81304  1.000 25.44162 ? 101 ILE A CG1 1 
ATOM   901  C  CG2 . ILE A 1 101 ? -7.10872  13.77244 20.27243  1.000 23.88299 ? 101 ILE A CG2 1 
ATOM   902  C  CD1 . ILE A 1 101 ? -7.28751  10.49208 20.63739  1.000 31.90018 ? 101 ILE A CD1 1 
ATOM   903  N  N   A ARG A 1 102 ? -3.30243  12.95320 20.85653  0.700 18.34980 ? 102 ARG A N   1 
ATOM   904  N  N   B ARG A 1 102 ? -3.30243  12.96390 20.83343  0.300 15.14618 ? 102 ARG A N   1 
ATOM   905  C  CA  A ARG A 1 102 ? -2.15536  13.17557 19.98439  0.700 20.58371 ? 102 ARG A CA  1 
ATOM   906  C  CA  B ARG A 1 102 ? -2.20298  13.25877 19.92719  0.300 13.96156 ? 102 ARG A CA  1 
ATOM   907  C  C   A ARG A 1 102 ? -2.16782  12.14182 18.86668  0.700 17.83458 ? 102 ARG A C   1 
ATOM   908  C  C   B ARG A 1 102 ? -1.99178  12.09141 18.97516  0.300 15.46910 ? 102 ARG A C   1 
ATOM   909  O  O   A ARG A 1 102 ? -2.84701  11.11650 18.93983  0.700 16.53643 ? 102 ARG A O   1 
ATOM   910  O  O   B ARG A 1 102 ? -2.35209  10.94894 19.27006  0.300 14.31746 ? 102 ARG A O   1 
ATOM   911  C  CB  A ARG A 1 102 ? -0.83019  13.02134 20.75130  0.700 26.44671 ? 102 ARG A CB  1 
ATOM   912  C  CB  B ARG A 1 102 ? -0.90555  13.56337 20.68504  0.300 14.90654 ? 102 ARG A CB  1 
ATOM   913  C  CG  A ARG A 1 102 ? -0.68682  13.88373 22.00119  0.700 31.03276 ? 102 ARG A CG  1 
ATOM   914  C  CG  B ARG A 1 102 ? -0.96047  14.84707 21.49029  0.300 12.94874 ? 102 ARG A CG  1 
ATOM   915  C  CD  A ARG A 1 102 ? -0.07202  15.22289 21.66413  0.700 30.29619 ? 102 ARG A CD  1 
ATOM   916  C  CD  B ARG A 1 102 ? 0.24178   14.92980 22.40334  0.300 15.62966 ? 102 ARG A CD  1 
ATOM   917  N  NE  A ARG A 1 102 ? 1.22131   15.10068 20.99344  0.700 32.22962 ? 102 ARG A NE  1 
ATOM   918  N  NE  B ARG A 1 102 ? 0.42239   13.70622 23.17518  0.300 20.25367 ? 102 ARG A NE  1 
ATOM   919  C  CZ  A ARG A 1 102 ? 2.39709   15.29365 21.57491  0.700 38.08573 ? 102 ARG A CZ  1 
ATOM   920  C  CZ  B ARG A 1 102 ? -0.28353  13.38033 24.24860  0.300 20.65860 ? 102 ARG A CZ  1 
ATOM   921  N  NH1 A ARG A 1 102 ? 2.49080   15.61239 22.85650  0.700 41.18731 ? 102 ARG A NH1 1 
ATOM   922  N  NH1 B ARG A 1 102 ? -1.25986  14.15331 24.69776  0.300 23.05832 ? 102 ARG A NH1 1 
ATOM   923  N  NH2 A ARG A 1 102 ? 3.50767   15.18825 20.84562  0.700 38.79530 ? 102 ARG A NH2 1 
ATOM   924  N  NH2 B ARG A 1 102 ? -0.00099  12.25352 24.89298  0.300 23.30562 ? 102 ARG A NH2 1 
ATOM   925  N  N   . LYS A 1 103 ? -1.37460  12.39831 17.82939  1.000 17.47028 ? 103 LYS A N   1 
ATOM   926  C  CA  . LYS A 1 103 ? -1.35494  11.45277 16.72642  1.000 18.56491 ? 103 LYS A CA  1 
ATOM   927  C  C   . LYS A 1 103 ? -0.78779  10.09583 17.10273  1.000 16.91658 ? 103 LYS A C   1 
ATOM   928  O  O   . LYS A 1 103 ? -1.22394  9.09276  16.54661  1.000 18.41525 ? 103 LYS A O   1 
ATOM   929  C  CB  . LYS A 1 103 ? -0.68333  12.01412 15.47670  1.000 23.22912 ? 103 LYS A CB  1 
ATOM   930  C  CG  . LYS A 1 103 ? 0.78424   11.89158 15.44994  1.000 23.64176 ? 103 LYS A CG  1 
ATOM   931  C  CD  . LYS A 1 103 ? 1.35385   12.40597 14.14567  1.000 25.92385 ? 103 LYS A CD  1 
ATOM   932  C  CE  . LYS A 1 103 ? 2.84662   12.23160 14.13720  1.000 26.51787 ? 103 LYS A CE  1 
ATOM   933  N  NZ  . LYS A 1 103 ? 3.40423   12.47650 12.77332  1.000 30.43939 ? 103 LYS A NZ  1 
ATOM   934  N  N   . LYS A 1 104 ? 0.17876   10.01657 18.01963  1.000 18.09699 ? 104 LYS A N   1 
ATOM   935  C  CA  . LYS A 1 104 ? 0.70407   8.69151  18.34323  1.000 19.97399 ? 104 LYS A CA  1 
ATOM   936  C  C   . LYS A 1 104 ? -0.38549  7.79234  18.92744  1.000 18.70179 ? 104 LYS A C   1 
ATOM   937  O  O   . LYS A 1 104 ? -0.46291  6.60186  18.59827  1.000 20.46952 ? 104 LYS A O   1 
ATOM   938  C  CB  . LYS A 1 104 ? 1.89682   8.80779  19.29527  1.000 22.75884 ? 104 LYS A CB  1 
ATOM   939  C  CG  . LYS A 1 104 ? 2.44551   7.45498  19.74323  1.000 28.92864 ? 104 LYS A CG  1 
ATOM   940  C  CD  . LYS A 1 104 ? 3.65498   7.65281  20.64581  1.000 34.08728 ? 104 LYS A CD  1 
ATOM   941  C  CE  . LYS A 1 104 ? 4.58787   6.45087  20.63786  1.000 39.54155 ? 104 LYS A CE  1 
ATOM   942  N  NZ  . LYS A 1 104 ? 3.90239   5.12920  20.66731  1.000 40.78858 ? 104 LYS A NZ  1 
ATOM   943  N  N   . GLU A 1 105 ? -1.21255  8.32998  19.83324  1.000 18.36177 ? 105 GLU A N   1 
ATOM   944  C  CA  . GLU A 1 105 ? -2.29911  7.52753  20.39848  1.000 19.80001 ? 105 GLU A CA  1 
ATOM   945  C  C   . GLU A 1 105 ? -3.26521  7.04743  19.31596  1.000 18.94173 ? 105 GLU A C   1 
ATOM   946  O  O   . GLU A 1 105 ? -3.65208  5.86450  19.29078  1.000 20.25001 ? 105 GLU A O   1 
ATOM   947  C  CB  . GLU A 1 105 ? -3.03746  8.34672  21.45123  1.000 21.42296 ? 105 GLU A CB  1 
ATOM   948  C  CG  . GLU A 1 105 ? -4.26979  7.64879  22.01680  1.000 23.62083 ? 105 GLU A CG  1 
ATOM   949  C  CD  . GLU A 1 105 ? -4.91886  8.40652  23.17078  1.000 32.10642 ? 105 GLU A CD  1 
ATOM   950  O  OE1 . GLU A 1 105 ? -4.29876  9.35697  23.69122  1.000 33.39777 ? 105 GLU A OE1 1 
ATOM   951  O  OE2 . GLU A 1 105 ? -6.06025  8.04977  23.55020  1.000 34.43059 ? 105 GLU A OE2 1 
ATOM   952  N  N   . ILE A 1 106 ? -3.58780  7.92194  18.35606  1.000 16.49631 ? 106 ILE A N   1 
ATOM   953  C  CA  . ILE A 1 106 ? -4.47720  7.56397  17.25699  1.000 18.43309 ? 106 ILE A CA  1 
ATOM   954  C  C   . ILE A 1 106 ? -3.84300  6.50999  16.36785  1.000 17.85137 ? 106 ILE A C   1 
ATOM   955  O  O   . ILE A 1 106 ? -4.46020  5.48790  16.05886  1.000 18.26920 ? 106 ILE A O   1 
ATOM   956  C  CB  . ILE A 1 106 ? -4.83457  8.82914  16.45956  1.000 16.31662 ? 106 ILE A CB  1 
ATOM   957  C  CG1 . ILE A 1 106 ? -5.61716  9.79106  17.34847  1.000 16.94194 ? 106 ILE A CG1 1 
ATOM   958  C  CG2 . ILE A 1 106 ? -5.68270  8.44069  15.20980  1.000 17.57200 ? 106 ILE A CG2 1 
ATOM   959  C  CD1 . ILE A 1 106 ? -5.72192  11.19156 16.77198  1.000 17.17961 ? 106 ILE A CD1 1 
ATOM   960  N  N   . ASN A 1 107 ? -2.59751  6.73764  15.96003  1.000 17.40487 ? 107 ASN A N   1 
ATOM   961  C  CA  . ASN A 1 107 ? -1.91368  5.80128  15.07855  1.000 17.62521 ? 107 ASN A CA  1 
ATOM   962  C  C   . ASN A 1 107 ? -1.77083  4.42931  15.73106  1.000 18.36431 ? 107 ASN A C   1 
ATOM   963  O  O   . ASN A 1 107 ? -2.00639  3.38600  15.10169  1.000 18.95450 ? 107 ASN A O   1 
ATOM   964  C  CB  . ASN A 1 107 ? -0.52381  6.33812  14.77268  1.000 18.01250 ? 107 ASN A CB  1 
ATOM   965  C  CG  . ASN A 1 107 ? -0.55272  7.51377  13.83206  1.000 17.07688 ? 107 ASN A CG  1 
ATOM   966  O  OD1 . ASN A 1 107 ? -1.55135  7.74019  13.13079  1.000 18.44958 ? 107 ASN A OD1 1 
ATOM   967  N  ND2 . ASN A 1 107 ? 0.54336   8.26405  13.79405  1.000 22.23152 ? 107 ASN A ND2 1 
ATOM   968  N  N   . ASP A 1 108 ? -1.34992  4.40766  16.99624  1.000 17.46851 ? 108 ASP A N   1 
ATOM   969  C  CA  . ASP A 1 108 ? -1.11110  3.13357  17.65047  1.000 18.93884 ? 108 ASP A CA  1 
ATOM   970  C  C   . ASP A 1 108 ? -2.40451  2.34853  17.81726  1.000 18.34960 ? 108 ASP A C   1 
ATOM   971  O  O   . ASP A 1 108 ? -2.38802  1.11097  17.80974  1.000 19.26892 ? 108 ASP A O   1 
ATOM   972  C  CB  . ASP A 1 108 ? -0.51430  3.36537  19.03000  1.000 18.69698 ? 108 ASP A CB  1 
ATOM   973  C  CG  . ASP A 1 108 ? 0.96209   3.75435  19.00411  1.000 21.04891 ? 108 ASP A CG  1 
ATOM   974  O  OD1 . ASP A 1 108 ? 1.62483   3.70078  17.94230  1.000 23.21470 ? 108 ASP A OD1 1 
ATOM   975  O  OD2 . ASP A 1 108 ? 1.45529   4.10933  20.08707  1.000 22.52156 ? 108 ASP A OD2 1 
ATOM   976  N  N   . ARG A 1 109 ? -3.51528  3.04701  18.01778  1.000 17.79076 ? 109 ARG A N   1 
ATOM   977  C  CA  . ARG A 1 109 ? -4.80607  2.40034  18.22233  1.000 19.70690 ? 109 ARG A CA  1 
ATOM   978  C  C   . ARG A 1 109 ? -5.45176  1.97988  16.90965  1.000 19.34641 ? 109 ARG A C   1 
ATOM   979  O  O   . ARG A 1 109 ? -6.00787  0.87737  16.81319  1.000 21.06241 ? 109 ARG A O   1 
ATOM   980  C  CB  . ARG A 1 109 ? -5.72945  3.36907  18.97003  1.000 20.36680 ? 109 ARG A CB  1 
ATOM   981  C  CG  . ARG A 1 109 ? -7.09615  2.83389  19.39833  1.000 22.85440 ? 109 ARG A CG  1 
ATOM   982  C  CD  . ARG A 1 109 ? -7.94595  3.98365  19.94113  1.000 22.57802 ? 109 ARG A CD  1 
ATOM   983  N  NE  . ARG A 1 109 ? -8.28381  4.89743  18.85697  1.000 23.99256 ? 109 ARG A NE  1 
ATOM   984  C  CZ  . ARG A 1 109 ? -8.59855  6.17308  19.01537  1.000 25.79989 ? 109 ARG A CZ  1 
ATOM   985  N  NH1 . ARG A 1 109 ? -8.63993  6.73247  20.21696  1.000 28.06787 ? 109 ARG A NH1 1 
ATOM   986  N  NH2 . ARG A 1 109 ? -8.86422  6.91265  17.94068  1.000 25.43276 ? 109 ARG A NH2 1 
ATOM   987  N  N   . ASP A 1 110 ? -5.36599  2.81278  15.87371  1.000 19.59258 ? 110 ASP A N   1 
ATOM   988  C  CA  . ASP A 1 110 ? -6.19695  2.67509  14.67583  1.000 17.46781 ? 110 ASP A CA  1 
ATOM   989  C  C   . ASP A 1 110 ? -5.42379  2.32320  13.41145  1.000 16.03448 ? 110 ASP A C   1 
ATOM   990  O  O   . ASP A 1 110 ? -6.00992  2.37751  12.32139  1.000 16.81194 ? 110 ASP A O   1 
ATOM   991  C  CB  . ASP A 1 110 ? -6.97176  3.97807  14.40986  1.000 17.52549 ? 110 ASP A CB  1 
ATOM   992  C  CG  . ASP A 1 110 ? -7.97966  4.31553  15.49028  1.000 20.89988 ? 110 ASP A CG  1 
ATOM   993  O  OD1 . ASP A 1 110 ? -8.27089  3.47255  16.37555  1.000 23.15708 ? 110 ASP A OD1 1 
ATOM   994  O  OD2 . ASP A 1 110 ? -8.48034  5.45468  15.43923  1.000 22.05688 ? 110 ASP A OD2 1 
ATOM   995  N  N   . TYR A 1 111 ? -4.16393  1.88391  13.52463  1.000 17.36711 ? 111 TYR A N   1 
ATOM   996  C  CA  . TYR A 1 111 ? -3.37145  1.67528  12.31232  1.000 17.63539 ? 111 TYR A CA  1 
ATOM   997  C  C   . TYR A 1 111 ? -4.05659  0.76210  11.30619  1.000 18.46448 ? 111 TYR A C   1 
ATOM   998  O  O   . TYR A 1 111 ? -3.94452  0.98050  10.10373  1.000 18.21456 ? 111 TYR A O   1 
ATOM   999  C  CB  . TYR A 1 111 ? -1.92386  1.25388  12.60813  1.000 17.59694 ? 111 TYR A CB  1 
ATOM   1000 C  CG  . TYR A 1 111 ? -1.80291  -0.05610 13.33398  1.000 18.30647 ? 111 TYR A CG  1 
ATOM   1001 C  CD1 . TYR A 1 111 ? -1.81515  -0.12782 14.72658  1.000 17.66634 ? 111 TYR A CD1 1 
ATOM   1002 C  CD2 . TYR A 1 111 ? -1.66490  -1.23979 12.62004  1.000 17.28946 ? 111 TYR A CD2 1 
ATOM   1003 C  CE1 . TYR A 1 111 ? -1.69505  -1.33750 15.38894  1.000 20.14130 ? 111 TYR A CE1 1 
ATOM   1004 C  CE2 . TYR A 1 111 ? -1.53458  -2.46361 13.29352  1.000 21.33848 ? 111 TYR A CE2 1 
ATOM   1005 C  CZ  . TYR A 1 111 ? -1.55387  -2.50800 14.66777  1.000 19.44798 ? 111 TYR A CZ  1 
ATOM   1006 O  OH  . TYR A 1 111 ? -1.43112  -3.71692 15.31599  1.000 20.53164 ? 111 TYR A OH  1 
ATOM   1007 N  N   . VAL A 1 112 ? -4.74186  -0.29339 11.75744  1.000 17.59091 ? 112 VAL A N   1 
ATOM   1008 C  CA  . VAL A 1 112 ? -5.39950  -1.17571 10.79231  1.000 18.83947 ? 112 VAL A CA  1 
ATOM   1009 C  C   . VAL A 1 112 ? -6.48897  -0.43308 10.02690  1.000 18.12491 ? 112 VAL A C   1 
ATOM   1010 O  O   . VAL A 1 112 ? -6.56769  -0.50391 8.79433   1.000 18.98943 ? 112 VAL A O   1 
ATOM   1011 C  CB  . VAL A 1 112 ? -5.95497  -2.43831 11.47275  1.000 21.26418 ? 112 VAL A CB  1 
ATOM   1012 C  CG1 . VAL A 1 112 ? -6.77741  -3.25130 10.45796  1.000 22.91354 ? 112 VAL A CG1 1 
ATOM   1013 C  CG2 . VAL A 1 112 ? -4.81942  -3.29324 12.01726  1.000 22.19211 ? 112 VAL A CG2 1 
ATOM   1014 N  N   . TYR A 1 113 ? -7.34352  0.29557  10.74324  1.000 18.30463 ? 113 TYR A N   1 
ATOM   1015 C  CA  . TYR A 1 113 ? -8.42716  1.00860  10.07400  1.000 18.15611 ? 113 TYR A CA  1 
ATOM   1016 C  C   . TYR A 1 113 ? -7.87673  2.10247  9.17492   1.000 19.20144 ? 113 TYR A C   1 
ATOM   1017 O  O   . TYR A 1 113 ? -8.38365  2.31938  8.06808   1.000 18.17354 ? 113 TYR A O   1 
ATOM   1018 C  CB  . TYR A 1 113 ? -9.37616  1.60601  11.10510  1.000 18.62236 ? 113 TYR A CB  1 
ATOM   1019 C  CG  . TYR A 1 113 ? -10.70921 2.02512  10.56755  1.000 17.36403 ? 113 TYR A CG  1 
ATOM   1020 C  CD1 . TYR A 1 113 ? -11.76246 1.13190  10.51722  1.000 20.98386 ? 113 TYR A CD1 1 
ATOM   1021 C  CD2 . TYR A 1 113 ? -10.93455 3.33249  10.15723  1.000 17.21377 ? 113 TYR A CD2 1 
ATOM   1022 C  CE1 . TYR A 1 113 ? -12.99613 1.50589  10.07157  1.000 20.81478 ? 113 TYR A CE1 1 
ATOM   1023 C  CE2 . TYR A 1 113 ? -12.17665 3.72792  9.70815   1.000 17.28238 ? 113 TYR A CE2 1 
ATOM   1024 C  CZ  . TYR A 1 113 ? -13.20891 2.79772  9.66399   1.000 18.03980 ? 113 TYR A CZ  1 
ATOM   1025 O  OH  . TYR A 1 113 ? -14.46758 3.13655  9.25906   1.000 20.58526 ? 113 TYR A OH  1 
ATOM   1026 N  N   . LEU A 1 114 ? -6.80796  2.75829  9.61327   1.000 17.11327 ? 114 LEU A N   1 
ATOM   1027 C  CA  . LEU A 1 114 ? -6.18403  3.79491  8.80413   1.000 16.83618 ? 114 LEU A CA  1 
ATOM   1028 C  C   . LEU A 1 114 ? -5.60640  3.19198  7.53094   1.000 18.54821 ? 114 LEU A C   1 
ATOM   1029 O  O   . LEU A 1 114 ? -5.69268  3.79041  6.44910   1.000 17.22525 ? 114 LEU A O   1 
ATOM   1030 C  CB  . LEU A 1 114 ? -5.09881  4.49342  9.61800   1.000 17.65218 ? 114 LEU A CB  1 
ATOM   1031 C  CG  . LEU A 1 114 ? -5.63911  5.31919  10.79164  1.000 17.46653 ? 114 LEU A CG  1 
ATOM   1032 C  CD1 . LEU A 1 114 ? -4.51339  5.81890  11.65287  1.000 21.16640 ? 114 LEU A CD1 1 
ATOM   1033 C  CD2 . LEU A 1 114 ? -6.49595  6.50272  10.33029  1.000 22.98543 ? 114 LEU A CD2 1 
ATOM   1034 N  N   . PHE A 1 115 ? -5.05523  1.97946  7.62730   1.000 18.42274 ? 115 PHE A N   1 
ATOM   1035 C  CA  . PHE A 1 115 ? -4.62633  1.27889  6.43189   1.000 18.49632 ? 115 PHE A CA  1 
ATOM   1036 C  C   . PHE A 1 115 ? -5.78874  1.02702  5.48039   1.000 17.58196 ? 115 PHE A C   1 
ATOM   1037 O  O   . PHE A 1 115 ? -5.63685  1.19972  4.26346   1.000 20.00978 ? 115 PHE A O   1 
ATOM   1038 C  CB  . PHE A 1 115 ? -3.93364  -0.02905 6.78848   1.000 20.51521 ? 115 PHE A CB  1 
ATOM   1039 C  CG  . PHE A 1 115 ? -3.55008  -0.80229 5.58803   1.000 26.72411 ? 115 PHE A CG  1 
ATOM   1040 C  CD1 . PHE A 1 115 ? -2.51752  -0.36031 4.77295   1.000 28.47540 ? 115 PHE A CD1 1 
ATOM   1041 C  CD2 . PHE A 1 115 ? -4.24245  -1.93784 5.22963   1.000 28.96514 ? 115 PHE A CD2 1 
ATOM   1042 C  CE1 . PHE A 1 115 ? -2.15769  -1.06972 3.64564   1.000 30.35804 ? 115 PHE A CE1 1 
ATOM   1043 C  CE2 . PHE A 1 115 ? -3.88223  -2.65660 4.09370   1.000 33.31244 ? 115 PHE A CE2 1 
ATOM   1044 C  CZ  . PHE A 1 115 ? -2.84394  -2.22113 3.31007   1.000 31.34912 ? 115 PHE A CZ  1 
ATOM   1045 N  N   . TYR A 1 116 ? -6.96550  0.62298  6.00717   1.000 18.96759 ? 116 TYR A N   1 
ATOM   1046 C  CA  . TYR A 1 116 ? -8.13167  0.42174  5.13554   1.000 18.96309 ? 116 TYR A CA  1 
ATOM   1047 C  C   . TYR A 1 116 ? -8.50229  1.69924  4.38652   1.000 19.56001 ? 116 TYR A C   1 
ATOM   1048 O  O   . TYR A 1 116 ? -8.79816  1.66124  3.18375   1.000 19.08429 ? 116 TYR A O   1 
ATOM   1049 C  CB  . TYR A 1 116 ? -9.35975  -0.02942 5.92062   1.000 22.90914 ? 116 TYR A CB  1 
ATOM   1050 C  CG  . TYR A 1 116 ? -9.29193  -1.34659 6.63198   1.000 28.23450 ? 116 TYR A CG  1 
ATOM   1051 C  CD1 . TYR A 1 116 ? -8.45218  -2.37022 6.21269   1.000 29.23011 ? 116 TYR A CD1 1 
ATOM   1052 C  CD2 . TYR A 1 116 ? -10.09762 -1.57261 7.74640   1.000 30.81500 ? 116 TYR A CD2 1 
ATOM   1053 C  CE1 . TYR A 1 116 ? -8.43932  -3.60141 6.89033   1.000 32.21734 ? 116 TYR A CE1 1 
ATOM   1054 C  CE2 . TYR A 1 116 ? -10.08152 -2.75964 8.40971   1.000 34.29117 ? 116 TYR A CE2 1 
ATOM   1055 C  CZ  . TYR A 1 116 ? -9.24399  -3.76521 7.98560   1.000 32.53764 ? 116 TYR A CZ  1 
ATOM   1056 O  OH  . TYR A 1 116 ? -9.22967  -4.94767 8.66206   1.000 37.97403 ? 116 TYR A OH  1 
ATOM   1057 N  N   . ILE A 1 117 ? -8.51400  2.83175  5.09329   1.000 17.89732 ? 117 ILE A N   1 
ATOM   1058 C  CA  . ILE A 1 117 ? -8.81563  4.10874  4.45746   1.000 18.81190 ? 117 ILE A CA  1 
ATOM   1059 C  C   . ILE A 1 117 ? -7.80483  4.37709  3.34965   1.000 18.74330 ? 117 ILE A C   1 
ATOM   1060 O  O   . ILE A 1 117 ? -8.16653  4.75371  2.22409   1.000 18.45964 ? 117 ILE A O   1 
ATOM   1061 C  CB  . ILE A 1 117 ? -8.81297  5.23081  5.51314   1.000 17.05573 ? 117 ILE A CB  1 
ATOM   1062 C  CG1 . ILE A 1 117 ? -10.01849 5.09263  6.43834   1.000 18.67458 ? 117 ILE A CG1 1 
ATOM   1063 C  CG2 . ILE A 1 117 ? -8.78469  6.61358  4.83876   1.000 19.41738 ? 117 ILE A CG2 1 
ATOM   1064 C  CD1 . ILE A 1 117 ? -9.96560  6.05027  7.62444   1.000 21.05391 ? 117 ILE A CD1 1 
ATOM   1065 N  N   A CYS A 1 118 ? -6.50933  4.19953  3.63794   0.700 18.46159 ? 118 CYS A N   1 
ATOM   1066 N  N   B CYS A 1 118 ? -6.51829  4.23973  3.68624   0.300 19.76918 ? 118 CYS A N   1 
ATOM   1067 C  CA  A CYS A 1 118 ? -5.49914  4.54060  2.63390   0.700 18.00105 ? 118 CYS A CA  1 
ATOM   1068 C  CA  B CYS A 1 118 ? -5.43843  4.47248  2.73810   0.300 19.59755 ? 118 CYS A CA  1 
ATOM   1069 C  C   A CYS A 1 118 ? -5.47615  3.52966  1.49241   0.700 19.27905 ? 118 CYS A C   1 
ATOM   1070 C  C   B CYS A 1 118 ? -5.57713  3.56516  1.52572   0.300 19.48904 ? 118 CYS A C   1 
ATOM   1071 O  O   A CYS A 1 118 ? -5.12309  3.87864  0.35690   0.700 17.57388 ? 118 CYS A O   1 
ATOM   1072 O  O   B CYS A 1 118 ? -5.43428  4.01324  0.38181   0.300 16.90860 ? 118 CYS A O   1 
ATOM   1073 C  CB  A CYS A 1 118 ? -4.12259  4.73471  3.28819   0.700 20.60320 ? 118 CYS A CB  1 
ATOM   1074 C  CB  B CYS A 1 118 ? -4.10453  4.22189  3.44651   0.300 22.86242 ? 118 CYS A CB  1 
ATOM   1075 S  SG  A CYS A 1 118 ? -4.03754  6.17213  4.37301   0.700 20.74829 ? 118 CYS A SG  1 
ATOM   1076 S  SG  B CYS A 1 118 ? -2.66062  4.58888  2.45945   0.300 26.81968 ? 118 CYS A SG  1 
ATOM   1077 N  N   . LEU A 1 119 ? -5.88113  2.28890  1.76498   1.000 18.96792 ? 119 LEU A N   1 
ATOM   1078 C  CA  . LEU A 1 119 ? -5.96181  1.31039  0.69047   1.000 19.36315 ? 119 LEU A CA  1 
ATOM   1079 C  C   . LEU A 1 119 ? -7.12840  1.60657  -0.24370  1.000 16.15555 ? 119 LEU A C   1 
ATOM   1080 O  O   . LEU A 1 119 ? -6.97133  1.54737  -1.46305  1.000 18.22480 ? 119 LEU A O   1 
ATOM   1081 C  CB  . LEU A 1 119 ? -6.07594  -0.07534 1.30578   1.000 21.20344 ? 119 LEU A CB  1 
ATOM   1082 C  CG  . LEU A 1 119 ? -6.13340  -1.17706 0.25550   1.000 21.17211 ? 119 LEU A CG  1 
ATOM   1083 C  CD1 . LEU A 1 119 ? -4.82146  -1.23559 -0.52544  1.000 25.52810 ? 119 LEU A CD1 1 
ATOM   1084 C  CD2 . LEU A 1 119 ? -6.43676  -2.50416 0.95660   1.000 26.30218 ? 119 LEU A CD2 1 
ATOM   1085 N  N   . SER A 1 120 ? -8.28841  1.97057  0.30843   1.000 17.29802 ? 120 SER A N   1 
ATOM   1086 C  CA  . SER A 1 120 ? -9.41157  2.40304  -0.51337  1.000 17.99980 ? 120 SER A CA  1 
ATOM   1087 C  C   . SER A 1 120 ? -9.00895  3.57331  -1.38482  1.000 16.36413 ? 120 SER A C   1 
ATOM   1088 O  O   . SER A 1 120 ? -9.27959  3.59292  -2.59167  1.000 17.19955 ? 120 SER A O   1 
ATOM   1089 C  CB  . SER A 1 120 ? -10.58645 2.79135  0.38687   1.000 17.49971 ? 120 SER A CB  1 
ATOM   1090 O  OG  . SER A 1 120 ? -11.68817 3.19835  -0.39023  1.000 18.48957 ? 120 SER A OG  1 
ATOM   1091 N  N   . ASN A 1 121 ? -8.32565  4.53918  -0.78485  1.000 17.03939 ? 121 ASN A N   1 
ATOM   1092 C  CA  . ASN A 1 121 ? -7.86997  5.71013  -1.51923  1.000 15.42735 ? 121 ASN A CA  1 
ATOM   1093 C  C   . ASN A 1 121 ? -6.87207  5.32155  -2.60705  1.000 16.59491 ? 121 ASN A C   1 
ATOM   1094 O  O   . ASN A 1 121 ? -6.90357  5.86668  -3.72460  1.000 16.47806 ? 121 ASN A O   1 
ATOM   1095 C  CB  . ASN A 1 121 ? -7.25937  6.70466  -0.51736  1.000 14.99924 ? 121 ASN A CB  1 
ATOM   1096 C  CG  . ASN A 1 121 ? -6.86420  7.99332  -1.17319  1.000 15.38391 ? 121 ASN A CG  1 
ATOM   1097 O  OD1 . ASN A 1 121 ? -7.73472  8.75948  -1.62098  1.000 16.02420 ? 121 ASN A OD1 1 
ATOM   1098 N  ND2 . ASN A 1 121 ? -5.58093  8.21034  -1.33585  1.000 16.53092 ? 121 ASN A ND2 1 
ATOM   1099 N  N   . PHE A 1 122 ? -5.99317  4.36654  -2.30943  1.000 17.16240 ? 122 PHE A N   1 
ATOM   1100 C  CA  . PHE A 1 122 ? -5.03290  3.93746  -3.30612  1.000 17.98818 ? 122 PHE A CA  1 
ATOM   1101 C  C   . PHE A 1 122 ? -5.73853  3.30812  -4.50399  1.000 17.80631 ? 122 PHE A C   1 
ATOM   1102 O  O   . PHE A 1 122 ? -5.37028  3.57757  -5.64959  1.000 18.27998 ? 122 PHE A O   1 
ATOM   1103 C  CB  . PHE A 1 122 ? -4.02299  2.96706  -2.69715  1.000 19.40360 ? 122 PHE A CB  1 
ATOM   1104 C  CG  . PHE A 1 122 ? -3.06922  2.43930  -3.70531  1.000 23.30284 ? 122 PHE A CG  1 
ATOM   1105 C  CD1 . PHE A 1 122 ? -2.06811  3.25671  -4.19140  1.000 25.97975 ? 122 PHE A CD1 1 
ATOM   1106 C  CD2 . PHE A 1 122 ? -3.21244  1.16212  -4.21210  1.000 25.96150 ? 122 PHE A CD2 1 
ATOM   1107 C  CE1 . PHE A 1 122 ? -1.20824  2.79809  -5.16768  1.000 25.80566 ? 122 PHE A CE1 1 
ATOM   1108 C  CE2 . PHE A 1 122 ? -2.34836  0.68543  -5.17921  1.000 27.69145 ? 122 PHE A CE2 1 
ATOM   1109 C  CZ  . PHE A 1 122 ? -1.34375  1.49803  -5.64571  1.000 27.24765 ? 122 PHE A CZ  1 
ATOM   1110 N  N   . PHE A 1 123 ? -6.76840  2.47957  -4.27092  1.000 16.73278 ? 123 PHE A N   1 
ATOM   1111 C  CA  . PHE A 1 123 ? -7.51210  1.90865  -5.39494  1.000 17.96186 ? 123 PHE A CA  1 
ATOM   1112 C  C   . PHE A 1 123 ? -8.19310  2.98831  -6.21374  1.000 18.65092 ? 123 PHE A C   1 
ATOM   1113 O  O   . PHE A 1 123 ? -8.23425  2.90041  -7.43832  1.000 19.11467 ? 123 PHE A O   1 
ATOM   1114 C  CB  . PHE A 1 123 ? -8.51804  0.86082  -4.92002  1.000 18.65425 ? 123 PHE A CB  1 
ATOM   1115 C  CG  . PHE A 1 123 ? -7.86839  -0.43078 -4.45883  1.000 23.32001 ? 123 PHE A CG  1 
ATOM   1116 C  CD1 . PHE A 1 123 ? -6.77699  -0.94668 -5.11999  1.000 32.24386 ? 123 PHE A CD1 1 
ATOM   1117 C  CD2 . PHE A 1 123 ? -8.32139  -1.09416 -3.33833  1.000 27.02151 ? 123 PHE A CD2 1 
ATOM   1118 C  CE1 . PHE A 1 123 ? -6.17048  -2.13580 -4.69161  1.000 36.08681 ? 123 PHE A CE1 1 
ATOM   1119 C  CE2 . PHE A 1 123 ? -7.71914  -2.26949 -2.90247  1.000 29.28247 ? 123 PHE A CE2 1 
ATOM   1120 C  CZ  . PHE A 1 123 ? -6.64084  -2.77967 -3.57643  1.000 33.12751 ? 123 PHE A CZ  1 
ATOM   1121 N  N   . MET A 1 124 ? -8.77349  3.99075  -5.56492  1.000 16.44614 ? 124 MET A N   1 
ATOM   1122 C  CA  . MET A 1 124 ? -9.32080  5.11828  -6.31613  1.000 17.66144 ? 124 MET A CA  1 
ATOM   1123 C  C   . MET A 1 124 ? -8.27340  5.70600  -7.25506  1.000 15.77745 ? 124 MET A C   1 
ATOM   1124 O  O   . MET A 1 124 ? -8.54401  5.95138  -8.43935  1.000 16.14238 ? 124 MET A O   1 
ATOM   1125 C  CB  . MET A 1 124 ? -9.80068  6.19764  -5.34042  1.000 17.45803 ? 124 MET A CB  1 
ATOM   1126 C  CG  . MET A 1 124 ? -10.42133 7.42840  -6.04480  1.000 16.90044 ? 124 MET A CG  1 
ATOM   1127 S  SD  . MET A 1 124 ? -10.59598 8.81155  -4.89407  1.000 17.36645 ? 124 MET A SD  1 
ATOM   1128 C  CE  . MET A 1 124 ? -8.86982  9.35307  -4.70846  1.000 15.63100 ? 124 MET A CE  1 
ATOM   1129 N  N   . LEU A 1 125 ? -7.07519  5.97224  -6.72324  1.000 17.28298 ? 125 LEU A N   1 
ATOM   1130 C  CA  . LEU A 1 125 ? -6.01170  6.58310  -7.52430  1.000 16.81220 ? 125 LEU A CA  1 
ATOM   1131 C  C   . LEU A 1 125 ? -5.55441  5.64719  -8.63895  1.000 16.90150 ? 125 LEU A C   1 
ATOM   1132 O  O   . LEU A 1 125 ? -5.26545  6.09067  -9.75825  1.000 17.68056 ? 125 LEU A O   1 
ATOM   1133 C  CB  . LEU A 1 125 ? -4.82435  6.95725  -6.63760  1.000 17.27954 ? 125 LEU A CB  1 
ATOM   1134 C  CG  . LEU A 1 125 ? -5.14363  8.07123  -5.66264  1.000 16.30851 ? 125 LEU A CG  1 
ATOM   1135 C  CD1 . LEU A 1 125 ? -3.87423  8.26283  -4.80082  1.000 16.95805 ? 125 LEU A CD1 1 
ATOM   1136 C  CD2 . LEU A 1 125 ? -5.48853  9.38296  -6.36880  1.000 16.70406 ? 125 LEU A CD2 1 
ATOM   1137 N  N   . LEU A 1 126 ? -5.39563  4.36578  -8.33036  1.000 17.43738 ? 126 LEU A N   1 
ATOM   1138 C  CA  . LEU A 1 126 ? -4.94874  3.42820  -9.34841  1.000 20.81228 ? 126 LEU A CA  1 
ATOM   1139 C  C   . LEU A 1 126 ? -5.94149  3.36571  -10.50291 1.000 19.32221 ? 126 LEU A C   1 
ATOM   1140 O  O   . LEU A 1 126 ? -5.54541  3.36837  -11.67986 1.000 18.69816 ? 126 LEU A O   1 
ATOM   1141 C  CB  . LEU A 1 126 ? -4.76756  2.06410  -8.68042  1.000 21.24957 ? 126 LEU A CB  1 
ATOM   1142 C  CG  . LEU A 1 126 ? -4.52447  0.93516  -9.66012  1.000 23.32395 ? 126 LEU A CG  1 
ATOM   1143 C  CD1 . LEU A 1 126 ? -3.24559  1.22533  -10.42706 1.000 27.49970 ? 126 LEU A CD1 1 
ATOM   1144 C  CD2 . LEU A 1 126 ? -4.40805  -0.34041 -8.85279  1.000 27.64637 ? 126 LEU A CD2 1 
ATOM   1145 N  N   . ILE A 1 127 ? -7.24169  3.32730  -10.18683 1.000 17.83882 ? 127 ILE A N   1 
ATOM   1146 C  CA  . ILE A 1 127 ? -8.27258  3.33219  -11.22967 1.000 18.14273 ? 127 ILE A CA  1 
ATOM   1147 C  C   . ILE A 1 127 ? -8.21236  4.61998  -12.03502 1.000 17.67241 ? 127 ILE A C   1 
ATOM   1148 O  O   . ILE A 1 127 ? -8.19790  4.59193  -13.27532 1.000 20.51995 ? 127 ILE A O   1 
ATOM   1149 C  CB  . ILE A 1 127 ? -9.65770  3.06997  -10.61761 1.000 20.54006 ? 127 ILE A CB  1 
ATOM   1150 C  CG1 . ILE A 1 127 ? -9.70934  1.62856  -10.09374 1.000 21.36614 ? 127 ILE A CG1 1 
ATOM   1151 C  CG2 . ILE A 1 127 ? -10.76845 3.33798  -11.63103 1.000 23.07078 ? 127 ILE A CG2 1 
ATOM   1152 C  CD1 . ILE A 1 127 ? -10.84908 1.38489  -9.12368  1.000 24.23919 ? 127 ILE A CD1 1 
ATOM   1153 N  N   . GLY A 1 128 ? -8.06572  5.75247  -11.35170 1.000 17.85842 ? 128 GLY A N   1 
ATOM   1154 C  CA  . GLY A 1 128 ? -7.90729  7.00891  -12.05985 1.000 17.64932 ? 128 GLY A CA  1 
ATOM   1155 C  C   . GLY A 1 128 ? -6.70322  7.00691  -12.97499 1.000 18.46311 ? 128 GLY A C   1 
ATOM   1156 O  O   . GLY A 1 128 ? -6.76285  7.51383  -14.09437 1.000 18.47435 ? 128 GLY A O   1 
ATOM   1157 N  N   . TYR A 1 129 ? -5.58191  6.48457  -12.49125 1.000 18.27051 ? 129 TYR A N   1 
ATOM   1158 C  CA  . TYR A 1 129 ? -4.36837  6.48557  -13.29312 1.000 18.12301 ? 129 TYR A CA  1 
ATOM   1159 C  C   . TYR A 1 129 ? -4.55416  5.64670  -14.55054 1.000 18.78993 ? 129 TYR A C   1 
ATOM   1160 O  O   . TYR A 1 129 ? -4.14801  6.05024  -15.64755 1.000 20.54435 ? 129 TYR A O   1 
ATOM   1161 C  CB  . TYR A 1 129 ? -3.21248  5.92610  -12.46320 1.000 19.54793 ? 129 TYR A CB  1 
ATOM   1162 C  CG  . TYR A 1 129 ? -1.90743  5.90432  -13.20766 1.000 20.22567 ? 129 TYR A CG  1 
ATOM   1163 C  CD1 . TYR A 1 129 ? -1.11983  7.04850  -13.28058 1.000 23.35521 ? 129 TYR A CD1 1 
ATOM   1164 C  CD2 . TYR A 1 129 ? -1.48317  4.75585  -13.86568 1.000 23.57884 ? 129 TYR A CD2 1 
ATOM   1165 C  CE1 . TYR A 1 129 ? 0.05545   7.06489  -13.97521 1.000 26.79926 ? 129 TYR A CE1 1 
ATOM   1166 C  CE2 . TYR A 1 129 ? -0.29193  4.75530  -14.55945 1.000 24.69357 ? 129 TYR A CE2 1 
ATOM   1167 C  CZ  . TYR A 1 129 ? 0.47491   5.92188  -14.59952 1.000 26.01079 ? 129 TYR A CZ  1 
ATOM   1168 O  OH  . TYR A 1 129 ? 1.66406   5.94141  -15.29562 1.000 33.14088 ? 129 TYR A OH  1 
ATOM   1169 N  N   . LEU A 1 130 ? -5.17054  4.47443  -14.40431 1.000 18.93985 ? 130 LEU A N   1 
ATOM   1170 C  CA  . LEU A 1 130 ? -5.50620  3.62593  -15.53837 1.000 19.89271 ? 130 LEU A CA  1 
ATOM   1171 C  C   . LEU A 1 130 ? -6.42155  4.34563  -16.50856 1.000 18.76198 ? 130 LEU A C   1 
ATOM   1172 O  O   . LEU A 1 130 ? -6.27134  4.20851  -17.72001 1.000 22.14187 ? 130 LEU A O   1 
ATOM   1173 C  CB  . LEU A 1 130 ? -6.16644  2.35601  -15.01831 1.000 22.74164 ? 130 LEU A CB  1 
ATOM   1174 C  CG  . LEU A 1 130 ? -5.20799  1.43387  -14.26646 1.000 25.41281 ? 130 LEU A CG  1 
ATOM   1175 C  CD1 . LEU A 1 130 ? -5.98691  0.28929  -13.62662 1.000 26.77721 ? 130 LEU A CD1 1 
ATOM   1176 C  CD2 . LEU A 1 130 ? -4.12019  0.88149  -15.20049 1.000 27.26652 ? 130 LEU A CD2 1 
ATOM   1177 N  N   . GLY A 1 131 ? -7.33387  5.15590  -16.00490 1.000 19.49628 ? 131 GLY A N   1 
ATOM   1178 C  CA  . GLY A 1 131 ? -8.21661  5.89476  -16.89241 1.000 19.26475 ? 131 GLY A CA  1 
ATOM   1179 C  C   . GLY A 1 131 ? -7.52849  7.06839  -17.55791 1.000 19.88482 ? 131 GLY A C   1 
ATOM   1180 O  O   . GLY A 1 131 ? -7.73748  7.36316  -18.73858 1.000 22.11940 ? 131 GLY A O   1 
ATOM   1181 N  N   . GLU A 1 132 ? -6.69986  7.75442  -16.77985 1.000 19.78795 ? 132 GLU A N   1 
ATOM   1182 C  CA  . GLU A 1 132 ? -6.00683  8.93294  -17.29017 1.000 20.41535 ? 132 GLU A CA  1 
ATOM   1183 C  C   . GLU A 1 132 ? -5.01832  8.55233  -18.37403 1.000 23.22589 ? 132 GLU A C   1 
ATOM   1184 O  O   . GLU A 1 132 ? -4.77307  9.34047  -19.29308 1.000 28.03120 ? 132 GLU A O   1 
ATOM   1185 C  CB  . GLU A 1 132 ? -5.30400  9.65167  -16.12133 1.000 23.45441 ? 132 GLU A CB  1 
ATOM   1186 C  CG  . GLU A 1 132 ? -4.77861  11.03978 -16.43589 1.000 23.35304 ? 132 GLU A CG  1 
ATOM   1187 C  CD  . GLU A 1 132 ? -5.83090  11.96161 -17.02196 1.000 18.25493 ? 132 GLU A CD  1 
ATOM   1188 O  OE1 . GLU A 1 132 ? -6.90257  12.20731 -16.38339 1.000 19.87061 ? 132 GLU A OE1 1 
ATOM   1189 O  OE2 . GLU A 1 132 ? -5.58111  12.42866 -18.15444 1.000 23.68890 ? 132 GLU A OE2 1 
ATOM   1190 N  N   . THR A 1 133 ? -4.42533  7.35759  -18.26260 1.000 23.18377 ? 133 THR A N   1 
ATOM   1191 C  CA  . THR A 1 133 ? -3.49817  6.83757  -19.25728 1.000 22.90031 ? 133 THR A CA  1 
ATOM   1192 C  C   . THR A 1 133 ? -4.20607  6.01269  -20.31826 1.000 25.76928 ? 133 THR A C   1 
ATOM   1193 O  O   . THR A 1 133 ? -3.53622  5.41542  -21.16262 1.000 29.81949 ? 133 THR A O   1 
ATOM   1194 C  CB  . THR A 1 133 ? -2.34751  6.03858  -18.61691 1.000 24.22566 ? 133 THR A CB  1 
ATOM   1195 O  OG1 . THR A 1 133 ? -2.86613  4.94468  -17.85181 1.000 23.25315 ? 133 THR A OG1 1 
ATOM   1196 C  CG2 . THR A 1 133 ? -1.51136  6.92343  -17.70224 1.000 25.25417 ? 133 THR A CG2 1 
ATOM   1197 N  N   . LYS A 1 134 ? -5.53915  5.94925  -20.27479 1.000 25.85850 ? 134 LYS A N   1 
ATOM   1198 C  CA  . LYS A 1 134 ? -6.36370  5.32432  -21.31257 1.000 27.49440 ? 134 LYS A CA  1 
ATOM   1199 C  C   . LYS A 1 134 ? -6.19775  3.81116  -21.37431 1.000 29.62443 ? 134 LYS A C   1 
ATOM   1200 O  O   . LYS A 1 134 ? -6.35290  3.20418  -22.43405 1.000 34.13648 ? 134 LYS A O   1 
ATOM   1201 C  CB  . LYS A 1 134 ? -6.20071  5.98147  -22.68981 1.000 30.27746 ? 134 LYS A CB  1 
ATOM   1202 C  CG  . LYS A 1 134 ? -6.49060  7.48234  -22.69693 1.000 34.43688 ? 134 LYS A CG  1 
ATOM   1203 C  CD  . LYS A 1 134 ? -6.36152  8.04113  -24.10650 1.000 42.23995 ? 134 LYS A CD  1 
ATOM   1204 C  CE  . LYS A 1 134 ? -6.55557  9.54785  -24.17845 1.000 42.41941 ? 134 LYS A CE  1 
ATOM   1205 N  NZ  . LYS A 1 134 ? -6.60907  10.02957 -25.60648 1.000 44.30629 ? 134 LYS A NZ  1 
ATOM   1206 N  N   A GLN A 1 135 ? -5.88392  3.18312  -20.24513 0.500 26.68386 ? 135 GLN A N   1 
ATOM   1207 N  N   B GLN A 1 135 ? -5.87236  3.20478  -20.23106 0.500 28.42163 ? 135 GLN A N   1 
ATOM   1208 C  CA  A GLN A 1 135 ? -5.85045  1.72998  -20.16427 0.500 28.69247 ? 135 GLN A CA  1 
ATOM   1209 C  CA  B GLN A 1 135 ? -5.83341  1.75332  -20.10686 0.500 30.65992 ? 135 GLN A CA  1 
ATOM   1210 C  C   A GLN A 1 135 ? -7.22121  1.13653  -19.87525 0.500 30.93122 ? 135 GLN A C   1 
ATOM   1211 C  C   B GLN A 1 135 ? -7.22981  1.17306  -19.93751 0.500 30.90177 ? 135 GLN A C   1 
ATOM   1212 O  O   A GLN A 1 135 ? -7.44918  -0.04200 -20.17675 0.500 35.39297 ? 135 GLN A O   1 
ATOM   1213 O  O   B GLN A 1 135 ? -7.48482  0.04260  -20.37282 0.500 33.99665 ? 135 GLN A O   1 
ATOM   1214 C  CB  A GLN A 1 135 ? -4.80743  1.27406  -19.13558 0.500 28.28741 ? 135 GLN A CB  1 
ATOM   1215 C  CB  B GLN A 1 135 ? -4.94138  1.34970  -18.92974 0.500 33.49966 ? 135 GLN A CB  1 
ATOM   1216 C  CG  A GLN A 1 135 ? -3.39699  1.74365  -19.47692 0.500 28.60474 ? 135 GLN A CG  1 
ATOM   1217 C  CG  B GLN A 1 135 ? -3.50716  1.82548  -19.05990 0.500 36.41050 ? 135 GLN A CG  1 
ATOM   1218 C  CD  A GLN A 1 135 ? -2.36546  1.42261  -18.40391 0.500 30.79633 ? 135 GLN A CD  1 
ATOM   1219 C  CD  B GLN A 1 135 ? -2.84107  1.31442  -20.31430 0.500 40.89082 ? 135 GLN A CD  1 
ATOM   1220 O  OE1 A GLN A 1 135 ? -1.79267  2.32831  -17.79188 0.500 32.71314 ? 135 GLN A OE1 1 
ATOM   1221 O  OE1 B GLN A 1 135 ? -2.97759  0.14519  -20.66962 0.500 41.67031 ? 135 GLN A OE1 1 
ATOM   1222 N  NE2 A GLN A 1 135 ? -2.08018  0.13481  -18.21509 0.500 35.69669 ? 135 GLN A NE2 1 
ATOM   1223 N  NE2 B GLN A 1 135 ? -2.12588  2.19721  -21.00614 0.500 43.51825 ? 135 GLN A NE2 1 
ATOM   1224 N  N   . ILE A 1 136 ? -8.13726  1.93388  -19.32045 1.000 30.42946 ? 136 ILE A N   1 
ATOM   1225 C  CA  . ILE A 1 136 ? -9.54110  1.57748  -19.19257 1.000 29.64483 ? 136 ILE A CA  1 
ATOM   1226 C  C   . ILE A 1 136 ? -10.35003 2.77616  -19.67125 1.000 28.32024 ? 136 ILE A C   1 
ATOM   1227 O  O   . ILE A 1 136 ? -9.83986  3.89635  -19.75421 1.000 30.23539 ? 136 ILE A O   1 
ATOM   1228 C  CB  . ILE A 1 136 ? -9.91690  1.19745  -17.74904 1.000 28.46827 ? 136 ILE A CB  1 
ATOM   1229 C  CG1 . ILE A 1 136 ? -9.63358  2.35632  -16.78924 1.000 25.84842 ? 136 ILE A CG1 1 
ATOM   1230 C  CG2 . ILE A 1 136 ? -9.12745  -0.04015 -17.30185 1.000 32.18679 ? 136 ILE A CG2 1 
ATOM   1231 C  CD1 . ILE A 1 136 ? -10.11639 2.07691  -15.34873 1.000 25.85027 ? 136 ILE A CD1 1 
ATOM   1232 N  N   . ASN A 1 137 ? -11.62201 2.53974  -19.98798 1.000 32.32143 ? 137 ASN A N   1 
ATOM   1233 C  CA  . ASN A 1 137 ? -12.42760 3.63692  -20.50630 1.000 32.72604 ? 137 ASN A CA  1 
ATOM   1234 C  C   . ASN A 1 137 ? -12.87432 4.59619  -19.40416 1.000 29.90491 ? 137 ASN A C   1 
ATOM   1235 O  O   . ASN A 1 137 ? -12.76611 4.32205  -18.20003 1.000 29.11491 ? 137 ASN A O   1 
ATOM   1236 C  CB  . ASN A 1 137 ? -13.62439 3.13958  -21.32013 1.000 34.91579 ? 137 ASN A CB  1 
ATOM   1237 C  CG  . ASN A 1 137 ? -14.65020 2.38914  -20.48726 1.000 39.32241 ? 137 ASN A CG  1 
ATOM   1238 O  OD1 . ASN A 1 137 ? -15.25817 2.94191  -19.57914 1.000 36.54694 ? 137 ASN A OD1 1 
ATOM   1239 N  ND2 . ASN A 1 137 ? -14.89424 1.13666  -20.84572 1.000 45.17892 ? 137 ASN A ND2 1 
ATOM   1240 N  N   . LYS A 1 138 ? -13.38471 5.75116  -19.84289 1.000 30.49731 ? 138 LYS A N   1 
ATOM   1241 C  CA  . LYS A 1 138 ? -13.69896 6.83331  -18.91352 1.000 30.26318 ? 138 LYS A CA  1 
ATOM   1242 C  C   . LYS A 1 138 ? -14.83995 6.45432  -17.98748 1.000 29.01853 ? 138 LYS A C   1 
ATOM   1243 O  O   . LYS A 1 138 ? -14.82396 6.80272  -16.80298 1.000 29.17098 ? 138 LYS A O   1 
ATOM   1244 C  CB  . LYS A 1 138 ? -14.05007 8.11143  -19.68258 1.000 32.36112 ? 138 LYS A CB  1 
ATOM   1245 C  CG  . LYS A 1 138 ? -12.83844 8.91394  -20.13996 1.000 36.85971 ? 138 LYS A CG  1 
ATOM   1246 C  CD  . LYS A 1 138 ? -13.25906 10.28115 -20.64140 1.000 42.67434 ? 138 LYS A CD  1 
ATOM   1247 C  CE  . LYS A 1 138 ? -12.04556 11.14367 -20.94834 1.000 47.55720 ? 138 LYS A CE  1 
ATOM   1248 N  NZ  . LYS A 1 138 ? -12.04009 12.40885 -20.15140 1.000 47.55280 ? 138 LYS A NZ  1 
ATOM   1249 N  N   . MET A 1 139 ? -15.83626 5.73787  -18.50387 1.000 30.47174 ? 139 MET A N   1 
ATOM   1250 C  CA  . MET A 1 139 ? -16.99173 5.37853  -17.69089 1.000 32.93087 ? 139 MET A CA  1 
ATOM   1251 C  C   . MET A 1 139 ? -16.58747 4.43630  -16.56721 1.000 29.70537 ? 139 MET A C   1 
ATOM   1252 O  O   . MET A 1 139 ? -16.96384 4.64363  -15.40951 1.000 28.38425 ? 139 MET A O   1 
ATOM   1253 C  CB  . MET A 1 139 ? -18.08504 4.77174  -18.57342 1.000 39.79837 ? 139 MET A CB  1 
ATOM   1254 C  CG  . MET A 1 139 ? -19.37604 4.43370  -17.85053 1.000 49.14184 ? 139 MET A CG  1 
ATOM   1255 S  SD  . MET A 1 139 ? -20.77976 4.20371  -18.98053 1.000 60.48261 ? 139 MET A SD  1 
ATOM   1256 C  CE  . MET A 1 139 ? -19.94307 3.92688  -20.54813 1.000 57.40272 ? 139 MET A CE  1 
ATOM   1257 N  N   . LEU A 1 140 ? -15.78718 3.41261  -16.88714 1.000 30.81434 ? 140 LEU A N   1 
ATOM   1258 C  CA  . LEU A 1 140 ? -15.27730 2.50967  -15.86153 1.000 26.87634 ? 140 LEU A CA  1 
ATOM   1259 C  C   . LEU A 1 140 ? -14.44721 3.26515  -14.82839 1.000 24.84111 ? 140 LEU A C   1 
ATOM   1260 O  O   . LEU A 1 140 ? -14.52731 2.97192  -13.63094 1.000 25.10998 ? 140 LEU A O   1 
ATOM   1261 C  CB  . LEU A 1 140 ? -14.42484 1.41459  -16.50634 1.000 28.97358 ? 140 LEU A CB  1 
ATOM   1262 C  CG  . LEU A 1 140 ? -13.87744 0.37165  -15.53470 1.000 32.85395 ? 140 LEU A CG  1 
ATOM   1263 C  CD1 . LEU A 1 140 ? -15.01880 -0.20278 -14.72360 1.000 35.73258 ? 140 LEU A CD1 1 
ATOM   1264 C  CD2 . LEU A 1 140 ? -13.13236 -0.73818 -16.28891 1.000 34.68985 ? 140 LEU A CD2 1 
ATOM   1265 N  N   . THR A 1 141 ? -13.63052 4.22695  -15.27521 1.000 24.23993 ? 141 THR A N   1 
ATOM   1266 C  CA  . THR A 1 141 ? -12.80615 5.01347  -14.36661 1.000 22.81887 ? 141 THR A CA  1 
ATOM   1267 C  C   . THR A 1 141 ? -13.68017 5.80401  -13.40811 1.000 22.73926 ? 141 THR A C   1 
ATOM   1268 O  O   . THR A 1 141 ? -13.43061 5.84356  -12.20358 1.000 22.06055 ? 141 THR A O   1 
ATOM   1269 C  CB  . THR A 1 141 ? -11.91147 5.96775  -15.16440 1.000 21.90313 ? 141 THR A CB  1 
ATOM   1270 O  OG1 . THR A 1 141 ? -11.14242 5.24056  -16.12226 1.000 23.76578 ? 141 THR A OG1 1 
ATOM   1271 C  CG2 . THR A 1 141 ? -10.92788 6.65555  -14.21091 1.000 21.68394 ? 141 THR A CG2 1 
ATOM   1272 N  N   . LEU A 1 142 ? -14.72453 6.43199  -13.93002 1.000 22.48685 ? 142 LEU A N   1 
ATOM   1273 C  CA  . LEU A 1 142 ? -15.56489 7.26852  -13.09134 1.000 23.40168 ? 142 LEU A CA  1 
ATOM   1274 C  C   . LEU A 1 142 ? -16.34224 6.43146  -12.09035 1.000 23.12059 ? 142 LEU A C   1 
ATOM   1275 O  O   . LEU A 1 142 ? -16.39306 6.77116  -10.90159 1.000 25.75493 ? 142 LEU A O   1 
ATOM   1276 C  CB  . LEU A 1 142 ? -16.51498 8.08047  -13.95575 1.000 26.65327 ? 142 LEU A CB  1 
ATOM   1277 C  CG  . LEU A 1 142 ? -15.84682 9.26634  -14.63548 1.000 31.70027 ? 142 LEU A CG  1 
ATOM   1278 C  CD1 . LEU A 1 142 ? -16.79214 9.80816  -15.66704 1.000 32.23914 ? 142 LEU A CD1 1 
ATOM   1279 C  CD2 . LEU A 1 142 ? -15.44399 10.36623 -13.63965 1.000 33.98268 ? 142 LEU A CD2 1 
ATOM   1280 N  N   A PHE A 1 143 ? -16.89081 5.29603  -12.52707 0.500 27.57033 ? 143 PHE A N   1 
ATOM   1281 N  N   B PHE A 1 143 ? -16.96167 5.34267  -12.55409 0.500 26.55378 ? 143 PHE A N   1 
ATOM   1282 C  CA  A PHE A 1 143 ? -17.68028 4.47307  -11.61260 0.500 29.33796 ? 143 PHE A CA  1 
ATOM   1283 C  CA  B PHE A 1 143 ? -17.66032 4.44142  -11.64256 0.500 26.69167 ? 143 PHE A CA  1 
ATOM   1284 C  C   A PHE A 1 143 ? -16.80552 3.74622  -10.59405 0.500 27.57950 ? 143 PHE A C   1 
ATOM   1285 C  C   B PHE A 1 143 ? -16.71298 3.90317  -10.58223 0.500 25.89043 ? 143 PHE A C   1 
ATOM   1286 O  O   A PHE A 1 143 ? -17.17340 3.64865  -9.41695  0.500 25.51973 ? 143 PHE A O   1 
ATOM   1287 O  O   B PHE A 1 143 ? -16.93155 4.08671  -9.37819  0.500 24.67108 ? 143 PHE A O   1 
ATOM   1288 C  CB  A PHE A 1 143 ? -18.56833 3.50054  -12.39133 0.500 32.85022 ? 143 PHE A CB  1 
ATOM   1289 C  CB  B PHE A 1 143 ? -18.28578 3.27711  -12.41642 0.500 27.80074 ? 143 PHE A CB  1 
ATOM   1290 C  CG  A PHE A 1 143 ? -19.86885 4.10442  -12.84894 0.500 37.00051 ? 143 PHE A CG  1 
ATOM   1291 C  CG  B PHE A 1 143 ? -18.81724 2.18676  -11.52673 0.500 33.75584 ? 143 PHE A CG  1 
ATOM   1292 C  CD1 A PHE A 1 143 ? -20.79750 4.56239  -11.92263 0.500 36.59775 ? 143 PHE A CD1 1 
ATOM   1293 C  CD1 B PHE A 1 143 ? -20.02107 2.34547  -10.86298 0.500 36.67040 ? 143 PHE A CD1 1 
ATOM   1294 C  CD2 A PHE A 1 143 ? -20.16731 4.21638  -14.19829 0.500 38.46837 ? 143 PHE A CD2 1 
ATOM   1295 C  CD2 B PHE A 1 143 ? -18.10273 1.01623  -11.33243 0.500 35.40832 ? 143 PHE A CD2 1 
ATOM   1296 C  CE1 A PHE A 1 143 ? -21.99875 5.11673  -12.33698 0.500 38.37726 ? 143 PHE A CE1 1 
ATOM   1297 C  CE1 B PHE A 1 143 ? -20.51003 1.35368  -10.03218 0.500 38.67073 ? 143 PHE A CE1 1 
ATOM   1298 C  CE2 A PHE A 1 143 ? -21.36618 4.77176  -14.61531 0.500 37.44912 ? 143 PHE A CE2 1 
ATOM   1299 C  CE2 B PHE A 1 143 ? -18.58437 0.01924  -10.50114 0.500 37.65953 ? 143 PHE A CE2 1 
ATOM   1300 C  CZ  A PHE A 1 143 ? -22.27876 5.22559  -13.68397 0.500 37.81415 ? 143 PHE A CZ  1 
ATOM   1301 C  CZ  B PHE A 1 143 ? -19.78851 0.18811  -9.85236  0.500 37.87603 ? 143 PHE A CZ  1 
ATOM   1302 N  N   . GLY A 1 144 ? -15.65352 3.21931  -11.02403 1.000 25.52715 ? 144 GLY A N   1 
ATOM   1303 C  CA  . GLY A 1 144 ? -14.75237 2.57203  -10.08509 1.000 24.64662 ? 144 GLY A CA  1 
ATOM   1304 C  C   . GLY A 1 144 ? -14.07462 3.56681  -9.16352  1.000 22.17850 ? 144 GLY A C   1 
ATOM   1305 O  O   . GLY A 1 144 ? -13.98212 3.33884  -7.95043  1.000 22.13808 ? 144 GLY A O   1 
ATOM   1306 N  N   . GLY A 1 145 ? -13.60352 4.68589  -9.71673  1.000 20.87298 ? 145 GLY A N   1 
ATOM   1307 C  CA  . GLY A 1 145 ? -12.95367 5.67710  -8.87044  1.000 19.39874 ? 145 GLY A CA  1 
ATOM   1308 C  C   . GLY A 1 145 ? -13.92579 6.28507  -7.88054  1.000 18.49987 ? 145 GLY A C   1 
ATOM   1309 O  O   . GLY A 1 145 ? -13.58932 6.50535  -6.71265  1.000 19.91429 ? 145 GLY A O   1 
ATOM   1310 N  N   . SER A 1 146 ? -15.16138 6.53086  -8.32056  1.000 20.18279 ? 146 SER A N   1 
ATOM   1311 C  CA  . SER A 1 146 ? -16.14694 7.09855  -7.41002  1.000 20.98822 ? 146 SER A CA  1 
ATOM   1312 C  C   . SER A 1 146 ? -16.54257 6.10203  -6.33653  1.000 19.12132 ? 146 SER A C   1 
ATOM   1313 O  O   . SER A 1 146 ? -16.74705 6.48702  -5.18022  1.000 19.60252 ? 146 SER A O   1 
ATOM   1314 C  CB  . SER A 1 146 ? -17.36350 7.59794  -8.17874  1.000 22.68974 ? 146 SER A CB  1 
ATOM   1315 O  OG  . SER A 1 146 ? -17.01409 8.67971  -9.01889  1.000 27.08042 ? 146 SER A OG  1 
ATOM   1316 N  N   . PHE A 1 147 ? -16.64901 4.81196  -6.68836  1.000 21.93539 ? 147 PHE A N   1 
ATOM   1317 C  CA  . PHE A 1 147 ? -16.90396 3.79966  -5.66573  1.000 20.87276 ? 147 PHE A CA  1 
ATOM   1318 C  C   . PHE A 1 147 ? -15.89634 3.90165  -4.51734  1.000 20.18910 ? 147 PHE A C   1 
ATOM   1319 O  O   . PHE A 1 147 ? -16.27257 3.94374  -3.34007  1.000 19.77066 ? 147 PHE A O   1 
ATOM   1320 C  CB  . PHE A 1 147 ? -16.86662 2.39246  -6.25716  1.000 23.34533 ? 147 PHE A CB  1 
ATOM   1321 C  CG  . PHE A 1 147 ? -16.99921 1.31806  -5.19940  1.000 22.86891 ? 147 PHE A CG  1 
ATOM   1322 C  CD1 . PHE A 1 147 ? -18.24661 0.92855  -4.73157  1.000 28.54735 ? 147 PHE A CD1 1 
ATOM   1323 C  CD2 . PHE A 1 147 ? -15.86651 0.75457  -4.62462  1.000 25.39081 ? 147 PHE A CD2 1 
ATOM   1324 C  CE1 . PHE A 1 147 ? -18.35937 -0.03048 -3.74968  1.000 32.19259 ? 147 PHE A CE1 1 
ATOM   1325 C  CE2 . PHE A 1 147 ? -15.97476 -0.20115 -3.63008  1.000 26.29868 ? 147 PHE A CE2 1 
ATOM   1326 C  CZ  . PHE A 1 147 ? -17.20939 -0.59628 -3.19621  1.000 28.78758 ? 147 PHE A CZ  1 
ATOM   1327 N  N   . PHE A 1 148 ? -14.60246 3.96226  -4.84413  1.000 17.71312 ? 148 PHE A N   1 
ATOM   1328 C  CA  . PHE A 1 148 ? -13.57029 4.00999  -3.81166  1.000 16.98042 ? 148 PHE A CA  1 
ATOM   1329 C  C   . PHE A 1 148 ? -13.53716 5.35258  -3.09695  1.000 17.29522 ? 148 PHE A C   1 
ATOM   1330 O  O   . PHE A 1 148 ? -13.26582 5.39680  -1.89707  1.000 17.31593 ? 148 PHE A O   1 
ATOM   1331 C  CB  . PHE A 1 148 ? -12.21922 3.55957  -4.35789  1.000 20.14726 ? 148 PHE A CB  1 
ATOM   1332 C  CG  . PHE A 1 148 ? -12.15914 2.07377  -4.52506  1.000 20.10647 ? 148 PHE A CG  1 
ATOM   1333 C  CD1 . PHE A 1 148 ? -12.02698 1.26582  -3.40587  1.000 19.72669 ? 148 PHE A CD1 1 
ATOM   1334 C  CD2 . PHE A 1 148 ? -12.24038 1.48802  -5.77042  1.000 22.32055 ? 148 PHE A CD2 1 
ATOM   1335 C  CE1 . PHE A 1 148 ? -12.00735 -0.12632 -3.51276  1.000 20.24225 ? 148 PHE A CE1 1 
ATOM   1336 C  CE2 . PHE A 1 148 ? -12.21679 0.10931  -5.91396  1.000 21.88893 ? 148 PHE A CE2 1 
ATOM   1337 C  CZ  . PHE A 1 148 ? -12.09648 -0.70626 -4.77528  1.000 21.72851 ? 148 PHE A CZ  1 
ATOM   1338 N  N   . LEU A 1 149 ? -13.80214 6.45611  -3.80095  1.000 17.11198 ? 149 LEU A N   1 
ATOM   1339 C  CA  . LEU A 1 149 ? -13.95434 7.74058  -3.11222  1.000 17.44874 ? 149 LEU A CA  1 
ATOM   1340 C  C   . LEU A 1 149 ? -15.03334 7.63807  -2.04272  1.000 17.20536 ? 149 LEU A C   1 
ATOM   1341 O  O   . LEU A 1 149 ? -14.82888 8.03753  -0.88299  1.000 17.62925 ? 149 LEU A O   1 
ATOM   1342 C  CB  . LEU A 1 149 ? -14.28907 8.83866  -4.11883  1.000 18.40336 ? 149 LEU A CB  1 
ATOM   1343 C  CG  . LEU A 1 149 ? -14.57066 10.19757 -3.47573  1.000 17.92273 ? 149 LEU A CG  1 
ATOM   1344 C  CD1 . LEU A 1 149 ? -13.24577 10.77628 -2.99338  1.000 21.06416 ? 149 LEU A CD1 1 
ATOM   1345 C  CD2 . LEU A 1 149 ? -15.26383 11.12985 -4.45651  1.000 23.35498 ? 149 LEU A CD2 1 
ATOM   1346 N  N   A PHE A 1 150 ? -16.20442 7.12961  -2.42152  0.500 17.56832 ? 150 PHE A N   1 
ATOM   1347 N  N   B PHE A 1 150 ? -16.18947 7.07672  -2.40988  0.500 18.31762 ? 150 PHE A N   1 
ATOM   1348 C  CA  A PHE A 1 150 ? -17.27883 6.95529  -1.45314  0.500 17.50756 ? 150 PHE A CA  1 
ATOM   1349 C  CA  B PHE A 1 150 ? -17.31022 6.94329  -1.48152  0.500 17.74855 ? 150 PHE A CA  1 
ATOM   1350 C  C   A PHE A 1 150 ? -16.82185 6.07743  -0.29924  0.500 18.33389 ? 150 PHE A C   1 
ATOM   1351 C  C   B PHE A 1 150 ? -17.00216 5.97056  -0.34731  0.500 18.16658 ? 150 PHE A C   1 
ATOM   1352 O  O   A PHE A 1 150 ? -17.01170 6.42157  0.87508   0.500 16.26904 ? 150 PHE A O   1 
ATOM   1353 O  O   B PHE A 1 150 ? -17.49841 6.14362  0.77226   0.500 17.69647 ? 150 PHE A O   1 
ATOM   1354 C  CB  A PHE A 1 150 ? -18.51677 6.36848  -2.13231  0.500 19.62239 ? 150 PHE A CB  1 
ATOM   1355 C  CB  B PHE A 1 150 ? -18.57131 6.51792  -2.23885  0.500 19.25290 ? 150 PHE A CB  1 
ATOM   1356 C  CG  A PHE A 1 150 ? -19.10677 7.25442  -3.19682  0.500 21.75039 ? 150 PHE A CG  1 
ATOM   1357 C  CG  B PHE A 1 150 ? -19.33601 7.66042  -2.85570  0.500 21.24782 ? 150 PHE A CG  1 
ATOM   1358 C  CD1 A PHE A 1 150 ? -18.78162 8.60624  -3.27557  0.500 24.06019 ? 150 PHE A CD1 1 
ATOM   1359 C  CD1 B PHE A 1 150 ? -18.78704 8.43017  -3.87580  0.500 22.24348 ? 150 PHE A CD1 1 
ATOM   1360 C  CD2 A PHE A 1 150 ? -19.99554 6.73590  -4.11355  0.500 23.90700 ? 150 PHE A CD2 1 
ATOM   1361 C  CD2 B PHE A 1 150 ? -20.61693 7.95732  -2.42352  0.500 24.45526 ? 150 PHE A CD2 1 
ATOM   1362 C  CE1 A PHE A 1 150 ? -19.33310 9.41568  -4.25775  0.500 26.27497 ? 150 PHE A CE1 1 
ATOM   1363 C  CE1 B PHE A 1 150 ? -19.51161 9.48327  -4.44883  0.500 22.09347 ? 150 PHE A CE1 1 
ATOM   1364 C  CE2 A PHE A 1 150 ? -20.54826 7.53336  -5.09567  0.500 26.39798 ? 150 PHE A CE2 1 
ATOM   1365 C  CE2 B PHE A 1 150 ? -21.34015 9.00184  -2.98822  0.500 29.67131 ? 150 PHE A CE2 1 
ATOM   1366 C  CZ  A PHE A 1 150 ? -20.21463 8.87526  -5.16954  0.500 27.50152 ? 150 PHE A CZ  1 
ATOM   1367 C  CZ  B PHE A 1 150 ? -20.78836 9.75778  -3.99637  0.500 27.25275 ? 150 PHE A CZ  1 
ATOM   1368 N  N   . LEU A 1 151 ? -16.20385 4.93594  -0.61985  1.000 18.76196 ? 151 LEU A N   1 
ATOM   1369 C  CA  . LEU A 1 151 ? -15.77535 4.02290  0.43082   1.000 18.67461 ? 151 LEU A CA  1 
ATOM   1370 C  C   . LEU A 1 151 ? -14.81546 4.71232  1.40351   1.000 18.05659 ? 151 LEU A C   1 
ATOM   1371 O  O   . LEU A 1 151 ? -14.96373 4.59959  2.62435   1.000 18.02227 ? 151 LEU A O   1 
ATOM   1372 C  CB  . LEU A 1 151 ? -15.15264 2.77036  -0.18280  1.000 19.24955 ? 151 LEU A CB  1 
ATOM   1373 C  CG  . LEU A 1 151 ? -14.65721 1.78142  0.87235   1.000 18.73007 ? 151 LEU A CG  1 
ATOM   1374 C  CD1 . LEU A 1 151 ? -15.74330 1.30363  1.82249   1.000 22.39484 ? 151 LEU A CD1 1 
ATOM   1375 C  CD2 . LEU A 1 151 ? -13.99351 0.61530  0.15770   1.000 22.59606 ? 151 LEU A CD2 1 
ATOM   1376 N  N   . THR A 1 152 ? -13.81505 5.41415  0.88097   1.000 16.41603 ? 152 THR A N   1 
ATOM   1377 C  CA  . THR A 1 152 ? -12.88849 6.14851  1.73370   1.000 15.30035 ? 152 THR A CA  1 
ATOM   1378 C  C   . THR A 1 152 ? -13.62974 7.09175  2.66303   1.000 16.76266 ? 152 THR A C   1 
ATOM   1379 O  O   . THR A 1 152 ? -13.39117 7.11559  3.88473   1.000 16.49955 ? 152 THR A O   1 
ATOM   1380 C  CB  . THR A 1 152 ? -11.92946 6.95460  0.85321   1.000 15.94876 ? 152 THR A CB  1 
ATOM   1381 O  OG1 . THR A 1 152 ? -11.18372 6.02785  0.08006   1.000 17.00583 ? 152 THR A OG1 1 
ATOM   1382 C  CG2 . THR A 1 152 ? -10.96844 7.81599  1.65959   1.000 17.36886 ? 152 THR A CG2 1 
ATOM   1383 N  N   . PHE A 1 153 ? -14.52974 7.89604  2.09239   1.000 16.98806 ? 153 PHE A N   1 
ATOM   1384 C  CA  . PHE A 1 153 ? -15.22175 8.89168  2.89606   1.000 16.66783 ? 153 PHE A CA  1 
ATOM   1385 C  C   . PHE A 1 153 ? -16.22320 8.26254  3.84305   1.000 17.44937 ? 153 PHE A C   1 
ATOM   1386 O  O   . PHE A 1 153 ? -16.43957 8.77822  4.94888   1.000 17.68863 ? 153 PHE A O   1 
ATOM   1387 C  CB  . PHE A 1 153 ? -15.80959 9.98912  2.00322   1.000 17.53635 ? 153 PHE A CB  1 
ATOM   1388 C  CG  . PHE A 1 153 ? -14.79159 11.03608 1.67851   1.000 17.09210 ? 153 PHE A CG  1 
ATOM   1389 C  CD1 . PHE A 1 153 ? -13.83613 10.82026 0.69384   1.000 17.91896 ? 153 PHE A CD1 1 
ATOM   1390 C  CD2 . PHE A 1 153 ? -14.72215 12.19938 2.45150   1.000 16.77289 ? 153 PHE A CD2 1 
ATOM   1391 C  CE1 . PHE A 1 153 ? -12.86467 11.78812 0.41672   1.000 18.87186 ? 153 PHE A CE1 1 
ATOM   1392 C  CE2 . PHE A 1 153 ? -13.77897 13.16983 2.18789   1.000 19.33629 ? 153 PHE A CE2 1 
ATOM   1393 C  CZ  . PHE A 1 153 ? -12.83409 12.96941 1.18186   1.000 19.01368 ? 153 PHE A CZ  1 
ATOM   1394 N  N   . TYR A 1 154 ? -16.82090 7.13976  3.44881   1.000 17.67575 ? 154 TYR A N   1 
ATOM   1395 C  CA  . TYR A 1 154 ? -17.69870 6.42585  4.36318   1.000 19.41504 ? 154 TYR A CA  1 
ATOM   1396 C  C   . TYR A 1 154 ? -16.90469 5.90294  5.55529   1.000 16.82709 ? 154 TYR A C   1 
ATOM   1397 O  O   . TYR A 1 154 ? -17.32528 6.04566  6.70680   1.000 18.52909 ? 154 TYR A O   1 
ATOM   1398 C  CB  . TYR A 1 154 ? -18.35593 5.25585  3.63654   1.000 20.17473 ? 154 TYR A CB  1 
ATOM   1399 C  CG  . TYR A 1 154 ? -19.19338 4.43165  4.56922   1.000 24.14947 ? 154 TYR A CG  1 
ATOM   1400 C  CD1 . TYR A 1 154 ? -20.43556 4.88666  4.99304   1.000 26.57838 ? 154 TYR A CD1 1 
ATOM   1401 C  CD2 . TYR A 1 154 ? -18.73559 3.21091  5.05647   1.000 29.91096 ? 154 TYR A CD2 1 
ATOM   1402 C  CE1 . TYR A 1 154 ? -21.20526 4.14392  5.85328   1.000 30.88026 ? 154 TYR A CE1 1 
ATOM   1403 C  CE2 . TYR A 1 154 ? -19.50284 2.46391  5.93425   1.000 32.65487 ? 154 TYR A CE2 1 
ATOM   1404 C  CZ  . TYR A 1 154 ? -20.73746 2.93853  6.32796   1.000 33.15579 ? 154 TYR A CZ  1 
ATOM   1405 O  OH  . TYR A 1 154 ? -21.52318 2.20559  7.19917   1.000 39.57014 ? 154 TYR A OH  1 
ATOM   1406 N  N   . LEU A 1 155 ? -15.75411 5.28282  5.29533   1.000 17.77008 ? 155 LEU A N   1 
ATOM   1407 C  CA  . LEU A 1 155 ? -14.91843 4.78037  6.38448   1.000 17.54042 ? 155 LEU A CA  1 
ATOM   1408 C  C   . LEU A 1 155 ? -14.51599 5.90641  7.32640   1.000 18.01794 ? 155 LEU A C   1 
ATOM   1409 O  O   . LEU A 1 155 ? -14.56333 5.74720  8.55476   1.000 17.06269 ? 155 LEU A O   1 
ATOM   1410 C  CB  . LEU A 1 155 ? -13.67110 4.09545  5.83754   1.000 17.97727 ? 155 LEU A CB  1 
ATOM   1411 C  CG  . LEU A 1 155 ? -13.96843 2.77676  5.12932   1.000 18.37497 ? 155 LEU A CG  1 
ATOM   1412 C  CD1 . LEU A 1 155 ? -12.69589 2.35741  4.41619   1.000 20.13830 ? 155 LEU A CD1 1 
ATOM   1413 C  CD2 . LEU A 1 155 ? -14.47626 1.68389  6.09049   1.000 23.41348 ? 155 LEU A CD2 1 
ATOM   1414 N  N   . LEU A 1 156 ? -14.14868 7.05348  6.76923   1.000 16.73301 ? 156 LEU A N   1 
ATOM   1415 C  CA  . LEU A 1 156 ? -13.82571 8.20558  7.59803   1.000 17.38712 ? 156 LEU A CA  1 
ATOM   1416 C  C   . LEU A 1 156 ? -15.02962 8.63762  8.43802   1.000 17.13673 ? 156 LEU A C   1 
ATOM   1417 O  O   . LEU A 1 156 ? -14.91827 8.88956  9.65184   1.000 18.00755 ? 156 LEU A O   1 
ATOM   1418 C  CB  . LEU A 1 156 ? -13.41120 9.33720  6.65732   1.000 19.30642 ? 156 LEU A CB  1 
ATOM   1419 C  CG  . LEU A 1 156 ? -13.15293 10.71359 7.22848   1.000 21.03428 ? 156 LEU A CG  1 
ATOM   1420 C  CD1 . LEU A 1 156 ? -12.00241 10.60303 8.23422   1.000 21.53066 ? 156 LEU A CD1 1 
ATOM   1421 C  CD2 . LEU A 1 156 ? -12.83462 11.65048 6.06181   1.000 23.17371 ? 156 LEU A CD2 1 
ATOM   1422 N  N   . TYR A 1 157 ? -16.20108 8.70602  7.81155   1.000 16.48020 ? 157 TYR A N   1 
ATOM   1423 C  CA  . TYR A 1 157 ? -17.37495 9.24241  8.47805   1.000 17.90769 ? 157 TYR A CA  1 
ATOM   1424 C  C   . TYR A 1 157 ? -17.76574 8.37650  9.65759   1.000 19.42983 ? 157 TYR A C   1 
ATOM   1425 O  O   . TYR A 1 157 ? -17.99500 8.88360  10.76908  1.000 20.03253 ? 157 TYR A O   1 
ATOM   1426 C  CB  . TYR A 1 157 ? -18.54101 9.29458  7.49693   1.000 18.97554 ? 157 TYR A CB  1 
ATOM   1427 C  CG  . TYR A 1 157 ? -19.71303 10.07631 8.05589   1.000 18.36383 ? 157 TYR A CG  1 
ATOM   1428 C  CD1 . TYR A 1 157 ? -20.66360 9.47060  8.87566   1.000 20.15133 ? 157 TYR A CD1 1 
ATOM   1429 C  CD2 . TYR A 1 157 ? -19.83153 11.43289 7.79932   1.000 21.29068 ? 157 TYR A CD2 1 
ATOM   1430 C  CE1 . TYR A 1 157 ? -21.70835 10.20073 9.41861   1.000 20.78715 ? 157 TYR A CE1 1 
ATOM   1431 C  CE2 . TYR A 1 157 ? -20.88643 12.18695 8.32606   1.000 20.34557 ? 157 TYR A CE2 1 
ATOM   1432 C  CZ  . TYR A 1 157 ? -21.82146 11.56254 9.13226   1.000 20.79103 ? 157 TYR A CZ  1 
ATOM   1433 O  OH  . TYR A 1 157 ? -22.85615 12.29280 9.65266   1.000 24.50846 ? 157 TYR A OH  1 
ATOM   1434 N  N   . VAL A 1 158 ? -17.88118 7.06232  9.42774   1.000 18.84327 ? 158 VAL A N   1 
ATOM   1435 C  CA  . VAL A 1 158 ? -18.46519 6.22172  10.45716  1.000 20.79969 ? 158 VAL A CA  1 
ATOM   1436 C  C   . VAL A 1 158 ? -17.54261 6.01938  11.64663  1.000 20.65146 ? 158 VAL A C   1 
ATOM   1437 O  O   . VAL A 1 158 ? -18.01526 5.65529  12.73259  1.000 25.52707 ? 158 VAL A O   1 
ATOM   1438 C  CB  . VAL A 1 158 ? -18.97335 4.88159  9.89916   1.000 20.25507 ? 158 VAL A CB  1 
ATOM   1439 C  CG1 . VAL A 1 158 ? -20.05737 5.09796  8.87865   1.000 24.90276 ? 158 VAL A CG1 1 
ATOM   1440 C  CG2 . VAL A 1 158 ? -17.85122 4.01795  9.36621   1.000 22.93590 ? 158 VAL A CG2 1 
ATOM   1441 N  N   . LYS A 1 159 ? -16.23684 6.21503  11.49326  1.000 18.74128 ? 159 LYS A N   1 
ATOM   1442 C  CA  . LYS A 1 159 ? -15.35808 6.04151  12.63938  1.000 19.77813 ? 159 LYS A CA  1 
ATOM   1443 C  C   . LYS A 1 159 ? -15.02644 7.34381  13.33893  1.000 20.47548 ? 159 LYS A C   1 
ATOM   1444 O  O   . LYS A 1 159 ? -14.93158 7.35818  14.56837  1.000 22.39016 ? 159 LYS A O   1 
ATOM   1445 C  CB  . LYS A 1 159 ? -14.06437 5.32373  12.23997  1.000 24.24916 ? 159 LYS A CB  1 
ATOM   1446 C  CG  . LYS A 1 159 ? -13.09955 5.08351  13.38748  1.000 29.63112 ? 159 LYS A CG  1 
ATOM   1447 C  CD  . LYS A 1 159 ? -12.27976 3.86063  13.12527  1.000 34.72035 ? 159 LYS A CD  1 
ATOM   1448 C  CE  . LYS A 1 159 ? -11.47210 3.40238  14.29975  1.000 32.57224 ? 159 LYS A CE  1 
ATOM   1449 N  NZ  . LYS A 1 159 ? -12.28316 2.46170  15.11917  1.000 33.97499 ? 159 LYS A NZ  1 
ATOM   1450 N  N   . TYR A 1 160 ? -14.91263 8.45222  12.61134  1.000 17.96704 ? 160 TYR A N   1 
ATOM   1451 C  CA  . TYR A 1 160 ? -14.27599 9.63190  13.17443  1.000 19.42040 ? 160 TYR A CA  1 
ATOM   1452 C  C   . TYR A 1 160 ? -15.16020 10.85249 13.32582  1.000 20.05159 ? 160 TYR A C   1 
ATOM   1453 O  O   . TYR A 1 160 ? -14.73009 11.80445 13.99074  1.000 20.78370 ? 160 TYR A O   1 
ATOM   1454 C  CB  . TYR A 1 160 ? -13.02434 10.01870 12.38163  1.000 16.98382 ? 160 TYR A CB  1 
ATOM   1455 C  CG  . TYR A 1 160 ? -11.97334 8.95648  12.51287  1.000 18.05727 ? 160 TYR A CG  1 
ATOM   1456 C  CD1 . TYR A 1 160 ? -11.36375 8.72760  13.73646  1.000 17.64634 ? 160 TYR A CD1 1 
ATOM   1457 C  CD2 . TYR A 1 160 ? -11.60864 8.16803  11.42032  1.000 17.49516 ? 160 TYR A CD2 1 
ATOM   1458 C  CE1 . TYR A 1 160 ? -10.38854 7.73895  13.85439  1.000 16.33582 ? 160 TYR A CE1 1 
ATOM   1459 C  CE2 . TYR A 1 160 ? -10.66813 7.17378  11.53891  1.000 16.84733 ? 160 TYR A CE2 1 
ATOM   1460 C  CZ  . TYR A 1 160 ? -10.04466 6.98212  12.74885  1.000 16.91540 ? 160 TYR A CZ  1 
ATOM   1461 O  OH  . TYR A 1 160 ? -9.09139  6.00866  12.88026  1.000 18.80587 ? 160 TYR A OH  1 
ATOM   1462 N  N   . THR A 1 161 ? -16.37253 10.89296 12.74802  1.000 18.84251 ? 161 THR A N   1 
ATOM   1463 C  CA  . THR A 1 161 ? -17.19296 12.08696 12.89649  1.000 18.57998 ? 161 THR A CA  1 
ATOM   1464 C  C   . THR A 1 161 ? -18.13545 11.98945 14.08257  1.000 19.31068 ? 161 THR A C   1 
ATOM   1465 O  O   . THR A 1 161 ? -18.38581 10.90851 14.64175  1.000 21.69576 ? 161 THR A O   1 
ATOM   1466 C  CB  . THR A 1 161 ? -18.00173 12.39545 11.63155  1.000 19.08937 ? 161 THR A CB  1 
ATOM   1467 O  OG1 . THR A 1 161 ? -19.00033 11.37999 11.41221  1.000 21.17457 ? 161 THR A OG1 1 
ATOM   1468 C  CG2 . THR A 1 161 ? -17.10707 12.52217 10.43407  1.000 19.58316 ? 161 THR A CG2 1 
ATOM   1469 N  N   A LYS A 1 162 ? -18.65411 13.14525 14.47136  0.500 17.93292 ? 162 LYS A N   1 
ATOM   1470 N  N   B LYS A 1 162 ? -18.68097 13.14318 14.45309  0.500 19.74386 ? 162 LYS A N   1 
ATOM   1471 C  CA  A LYS A 1 162 ? -19.81870 13.24931 15.33763  0.500 19.39908 ? 162 LYS A CA  1 
ATOM   1472 C  CA  B LYS A 1 162 ? -19.82118 13.23800 15.35321  0.500 20.24473 ? 162 LYS A CA  1 
ATOM   1473 C  C   A LYS A 1 162 ? -20.95227 13.92746 14.57180  0.500 19.53688 ? 162 LYS A C   1 
ATOM   1474 C  C   B LYS A 1 162 ? -20.91670 14.06815 14.68588  0.500 19.34528 ? 162 LYS A C   1 
ATOM   1475 O  O   A LYS A 1 162 ? -20.74946 14.49717 13.49603  0.500 21.54088 ? 162 LYS A O   1 
ATOM   1476 O  O   B LYS A 1 162 ? -20.65015 14.87069 13.78707  0.500 17.48839 ? 162 LYS A O   1 
ATOM   1477 C  CB  A LYS A 1 162 ? -19.49800 14.03961 16.61481  0.500 22.23304 ? 162 LYS A CB  1 
ATOM   1478 C  CB  B LYS A 1 162 ? -19.43811 13.86771 16.69847  0.500 24.13199 ? 162 LYS A CB  1 
ATOM   1479 C  CG  A LYS A 1 162 ? -18.65304 13.25728 17.61848  0.500 24.33160 ? 162 LYS A CG  1 
ATOM   1480 C  CG  B LYS A 1 162 ? -18.61893 12.95559 17.60847  0.500 26.85735 ? 162 LYS A CG  1 
ATOM   1481 C  CD  A LYS A 1 162 ? -18.29064 14.07386 18.86058  0.500 27.82563 ? 162 LYS A CD  1 
ATOM   1482 C  CD  B LYS A 1 162 ? -18.40073 13.60491 18.96779  0.500 26.91737 ? 162 LYS A CD  1 
ATOM   1483 C  CE  A LYS A 1 162 ? -19.49422 14.35573 19.74576  0.500 30.38825 ? 162 LYS A CE  1 
ATOM   1484 C  CE  B LYS A 1 162 ? -17.67513 12.68361 19.92708  0.500 28.24778 ? 162 LYS A CE  1 
ATOM   1485 N  NZ  A LYS A 1 162 ? -19.05199 14.90520 21.04807  0.500 32.63523 ? 162 LYS A NZ  1 
ATOM   1486 N  NZ  B LYS A 1 162 ? -17.42529 13.35830 21.23239  0.500 31.57422 ? 162 LYS A NZ  1 
ATOM   1487 N  N   . GLU A 1 163 ? -22.15678 13.86643 15.13816  1.000 20.44626 ? 163 GLU A N   1 
ATOM   1488 C  CA  . GLU A 1 163 ? -23.33086 14.43950 14.47132  1.000 21.19215 ? 163 GLU A CA  1 
ATOM   1489 C  C   . GLU A 1 163 ? -23.54627 15.88104 14.93592  1.000 21.41167 ? 163 GLU A C   1 
ATOM   1490 O  O   . GLU A 1 163 ? -24.37562 16.17295 15.80535  1.000 24.60735 ? 163 GLU A O   1 
ATOM   1491 C  CB  . GLU A 1 163 ? -24.55295 13.56487 14.69222  1.000 22.69226 ? 163 GLU A CB  1 
ATOM   1492 C  CG  . GLU A 1 163 ? -24.44102 12.18420 14.07215  1.000 23.90608 ? 163 GLU A CG  1 
ATOM   1493 C  CD  . GLU A 1 163 ? -24.42807 12.24108 12.55595  1.000 24.44047 ? 163 GLU A CD  1 
ATOM   1494 O  OE1 . GLU A 1 163 ? -25.14510 13.09706 11.97057  1.000 26.17594 ? 163 GLU A OE1 1 
ATOM   1495 O  OE2 . GLU A 1 163 ? -23.69943 11.43567 11.94583  1.000 25.49514 ? 163 GLU A OE2 1 
ATOM   1496 N  N   . ASN A 1 164 ? -22.79107 16.80665 14.33011  1.000 19.24197 ? 164 ASN A N   1 
ATOM   1497 C  CA  . ASN A 1 164 ? -22.95552 18.22867 14.64115  1.000 21.33676 ? 164 ASN A CA  1 
ATOM   1498 C  C   . ASN A 1 164 ? -22.44622 19.03719 13.45131  1.000 18.58708 ? 164 ASN A C   1 
ATOM   1499 O  O   . ASN A 1 164 ? -21.75801 18.50723 12.57966  1.000 17.95046 ? 164 ASN A O   1 
ATOM   1500 C  CB  . ASN A 1 164 ? -22.30492 18.63848 15.98092  1.000 21.30809 ? 164 ASN A CB  1 
ATOM   1501 C  CG  . ASN A 1 164 ? -20.80713 18.42072 16.01874  1.000 20.80043 ? 164 ASN A CG  1 
ATOM   1502 O  OD1 . ASN A 1 164 ? -20.10475 18.77589 15.09069  1.000 21.20636 ? 164 ASN A OD1 1 
ATOM   1503 N  ND2 . ASN A 1 164 ? -20.30875 17.83983 17.10599  1.000 22.90187 ? 164 ASN A ND2 1 
ATOM   1504 N  N   . TRP A 1 165 ? -22.79969 20.32723 13.42568  1.000 20.86773 ? 165 TRP A N   1 
ATOM   1505 C  CA  . TRP A 1 165 ? -22.53543 21.12736 12.23391  1.000 21.18766 ? 165 TRP A CA  1 
ATOM   1506 C  C   . TRP A 1 165 ? -21.05430 21.39883 12.00334  1.000 19.48051 ? 165 TRP A C   1 
ATOM   1507 O  O   . TRP A 1 165 ? -20.63660 21.52375 10.84396  1.000 20.50856 ? 165 TRP A O   1 
ATOM   1508 C  CB  . TRP A 1 165 ? -23.37234 22.40209 12.22787  1.000 21.50188 ? 165 TRP A CB  1 
ATOM   1509 C  CG  . TRP A 1 165 ? -24.76949 22.09092 11.76791  1.000 24.03321 ? 165 TRP A CG  1 
ATOM   1510 C  CD1 . TRP A 1 165 ? -25.84822 21.81020 12.55106  1.000 24.83873 ? 165 TRP A CD1 1 
ATOM   1511 C  CD2 . TRP A 1 165 ? -25.20344 21.92935 10.41152  1.000 25.63186 ? 165 TRP A CD2 1 
ATOM   1512 N  NE1 . TRP A 1 165 ? -26.94584 21.50672 11.76192  1.000 25.40665 ? 165 TRP A NE1 1 
ATOM   1513 C  CE2 . TRP A 1 165 ? -26.56968 21.56989 10.44562  1.000 26.16920 ? 165 TRP A CE2 1 
ATOM   1514 C  CE3 . TRP A 1 165 ? -24.57011 22.06469 9.16582   1.000 28.33071 ? 165 TRP A CE3 1 
ATOM   1515 C  CZ2 . TRP A 1 165 ? -27.32006 21.36923 9.28750   1.000 26.71899 ? 165 TRP A CZ2 1 
ATOM   1516 C  CZ3 . TRP A 1 165 ? -25.31873 21.85639 8.02028   1.000 26.84124 ? 165 TRP A CZ3 1 
ATOM   1517 C  CH2 . TRP A 1 165 ? -26.67858 21.50624 8.09105   1.000 29.04143 ? 165 TRP A CH2 1 
ATOM   1518 N  N   A MET A 1 166 ? -20.26026 21.53206 13.07426  0.500 19.31402 ? 166 MET A N   1 
ATOM   1519 N  N   B MET A 1 166 ? -20.23344 21.46963 13.05574  0.500 16.82202 ? 166 MET A N   1 
ATOM   1520 C  CA  A MET A 1 166 ? -18.81328 21.63229 12.90602  0.500 20.78281 ? 166 MET A CA  1 
ATOM   1521 C  CA  B MET A 1 166 ? -18.81068 21.67906 12.79887  0.500 16.50085 ? 166 MET A CA  1 
ATOM   1522 C  C   A MET A 1 166 ? -18.30424 20.45814 12.08329  0.500 19.02823 ? 166 MET A C   1 
ATOM   1523 C  C   B MET A 1 166 ? -18.17423 20.43854 12.17736  0.500 17.14614 ? 166 MET A C   1 
ATOM   1524 O  O   A MET A 1 166 ? -17.57249 20.62698 11.09654  0.500 16.85771 ? 166 MET A O   1 
ATOM   1525 O  O   B MET A 1 166 ? -17.19498 20.54889 11.42233  0.500 17.56321 ? 166 MET A O   1 
ATOM   1526 C  CB  A MET A 1 166 ? -18.12402 21.65454 14.27384  0.500 26.19624 ? 166 MET A CB  1 
ATOM   1527 C  CB  B MET A 1 166 ? -18.06780 22.10000 14.06275  0.500 17.75709 ? 166 MET A CB  1 
ATOM   1528 C  CG  A MET A 1 166 ? -17.96958 23.03307 14.85850  0.500 32.07931 ? 166 MET A CG  1 
ATOM   1529 C  CG  B MET A 1 166 ? -17.84729 20.98916 15.05170  0.500 21.59582 ? 166 MET A CG  1 
ATOM   1530 S  SD  A MET A 1 166 ? -17.37995 23.14222 16.56895  0.500 40.22092 ? 166 MET A SD  1 
ATOM   1531 S  SD  B MET A 1 166 ? -16.97012 21.61886 16.47692  0.500 29.22264 ? 166 MET A SD  1 
ATOM   1532 C  CE  A MET A 1 166 ? -16.04566 21.95049 16.53804  0.500 39.88096 ? 166 MET A CE  1 
ATOM   1533 C  CE  B MET A 1 166 ? -18.19534 22.75577 17.12735  0.500 31.68281 ? 166 MET A CE  1 
ATOM   1534 N  N   . ASN A 1 167 ? -18.72140 19.24978 12.45573  1.000 18.13820 ? 167 ASN A N   1 
ATOM   1535 C  CA  . ASN A 1 167 ? -18.28792 18.06125 11.72950  1.000 17.25577 ? 167 ASN A CA  1 
ATOM   1536 C  C   . ASN A 1 167 ? -18.81522 18.05615 10.30556  1.000 17.00551 ? 167 ASN A C   1 
ATOM   1537 O  O   . ASN A 1 167 ? -18.07406 17.72360 9.37468   1.000 18.13017 ? 167 ASN A O   1 
ATOM   1538 C  CB  . ASN A 1 167 ? -18.79093 16.81125 12.43435  1.000 17.48698 ? 167 ASN A CB  1 
ATOM   1539 C  CG  . ASN A 1 167 ? -17.86725 16.35798 13.53143  1.000 16.88478 ? 167 ASN A CG  1 
ATOM   1540 O  OD1 . ASN A 1 167 ? -17.13529 15.39609 13.36705  1.000 18.67581 ? 167 ASN A OD1 1 
ATOM   1541 N  ND2 . ASN A 1 167 ? -17.86253 17.07170 14.65463  1.000 17.75824 ? 167 ASN A ND2 1 
ATOM   1542 N  N   . TYR A 1 168 ? -20.07099 18.46899 10.10628  1.000 18.72716 ? 168 TYR A N   1 
ATOM   1543 C  CA  . TYR A 1 168 ? -20.62735 18.43432 8.75849   1.000 17.83577 ? 168 TYR A CA  1 
ATOM   1544 C  C   . TYR A 1 168 ? -19.87092 19.36769 7.83338   1.000 17.20100 ? 168 TYR A C   1 
ATOM   1545 O  O   . TYR A 1 168 ? -19.63154 19.03406 6.66725   1.000 17.87424 ? 168 TYR A O   1 
ATOM   1546 C  CB  . TYR A 1 168 ? -22.10984 18.80356 8.74969   1.000 19.22099 ? 168 TYR A CB  1 
ATOM   1547 C  CG  . TYR A 1 168 ? -22.98485 17.93196 9.60570   1.000 19.89323 ? 168 TYR A CG  1 
ATOM   1548 C  CD1 . TYR A 1 168 ? -22.69219 16.58429 9.82600   1.000 17.76908 ? 168 TYR A CD1 1 
ATOM   1549 C  CD2 . TYR A 1 168 ? -24.09715 18.46861 10.23319  1.000 21.12634 ? 168 TYR A CD2 1 
ATOM   1550 C  CE1 . TYR A 1 168 ? -23.51256 15.80281 10.67206  1.000 18.85609 ? 168 TYR A CE1 1 
ATOM   1551 C  CE2 . TYR A 1 168 ? -24.90402 17.72034 11.06571  1.000 22.77141 ? 168 TYR A CE2 1 
ATOM   1552 C  CZ  . TYR A 1 168 ? -24.62238 16.37508 11.28132  1.000 21.03868 ? 168 TYR A CZ  1 
ATOM   1553 O  OH  . TYR A 1 168 ? -25.44646 15.65083 12.10272  1.000 21.83397 ? 168 TYR A OH  1 
ATOM   1554 N  N   . ILE A 1 169 ? -19.53401 20.56176 8.31790   1.000 16.40504 ? 169 ILE A N   1 
ATOM   1555 C  CA  . ILE A 1 169 ? -18.76750 21.49416 7.48685   1.000 18.74433 ? 169 ILE A CA  1 
ATOM   1556 C  C   . ILE A 1 169 ? -17.46341 20.84669 7.02594   1.000 16.81970 ? 169 ILE A C   1 
ATOM   1557 O  O   . ILE A 1 169 ? -17.13410 20.81629 5.83059   1.000 17.91456 ? 169 ILE A O   1 
ATOM   1558 C  CB  . ILE A 1 169 ? -18.50487 22.80024 8.25341   1.000 18.90186 ? 169 ILE A CB  1 
ATOM   1559 C  CG1 . ILE A 1 169 ? -19.79835 23.61149 8.40235   1.000 19.17676 ? 169 ILE A CG1 1 
ATOM   1560 C  CG2 . ILE A 1 169 ? -17.45866 23.63206 7.51409   1.000 18.74206 ? 169 ILE A CG2 1 
ATOM   1561 C  CD1 . ILE A 1 169 ? -19.66709 24.70850 9.41947   1.000 20.34208 ? 169 ILE A CD1 1 
ATOM   1562 N  N   . VAL A 1 170 ? -16.67912 20.35047 7.97596   1.000 17.10599 ? 170 VAL A N   1 
ATOM   1563 C  CA  . VAL A 1 170 ? -15.36658 19.84156 7.61643   1.000 19.22358 ? 170 VAL A CA  1 
ATOM   1564 C  C   . VAL A 1 170 ? -15.51045 18.62246 6.72113   1.000 16.74366 ? 170 VAL A C   1 
ATOM   1565 O  O   . VAL A 1 170 ? -14.79629 18.47700 5.71601   1.000 19.67803 ? 170 VAL A O   1 
ATOM   1566 C  CB  . VAL A 1 170 ? -14.56239 19.54069 8.89547   1.000 19.39293 ? 170 VAL A CB  1 
ATOM   1567 C  CG1 . VAL A 1 170 ? -13.21890 18.92555 8.54854   1.000 22.25561 ? 170 VAL A CG1 1 
ATOM   1568 C  CG2 . VAL A 1 170 ? -14.31842 20.81126 9.67577   1.000 24.99112 ? 170 VAL A CG2 1 
ATOM   1569 N  N   . PHE A 1 171 ? -16.44337 17.72185 7.05737   1.000 15.73664 ? 171 PHE A N   1 
ATOM   1570 C  CA  . PHE A 1 171 ? -16.56191 16.48994 6.29704   1.000 16.04077 ? 171 PHE A CA  1 
ATOM   1571 C  C   . PHE A 1 171 ? -17.06478 16.75383 4.88105   1.000 16.09349 ? 171 PHE A C   1 
ATOM   1572 O  O   . PHE A 1 171 ? -16.46299 16.28023 3.89965   1.000 16.26684 ? 171 PHE A O   1 
ATOM   1573 C  CB  . PHE A 1 171 ? -17.47270 15.51247 7.02355   1.000 17.41859 ? 171 PHE A CB  1 
ATOM   1574 C  CG  . PHE A 1 171 ? -17.62484 14.21917 6.27235   1.000 15.50318 ? 171 PHE A CG  1 
ATOM   1575 C  CD1 . PHE A 1 171 ? -16.67502 13.20848 6.39788   1.000 18.35914 ? 171 PHE A CD1 1 
ATOM   1576 C  CD2 . PHE A 1 171 ? -18.66967 14.05596 5.36613   1.000 18.41879 ? 171 PHE A CD2 1 
ATOM   1577 C  CE1 . PHE A 1 171 ? -16.78754 12.01959 5.66552   1.000 20.71404 ? 171 PHE A CE1 1 
ATOM   1578 C  CE2 . PHE A 1 171 ? -18.80394 12.86713 4.61577   1.000 19.45698 ? 171 PHE A CE2 1 
ATOM   1579 C  CZ  . PHE A 1 171 ? -17.85453 11.86092 4.75574   1.000 21.32309 ? 171 PHE A CZ  1 
ATOM   1580 N  N   . TYR A 1 172 ? -18.18087 17.48102 4.74816   1.000 16.84743 ? 172 TYR A N   1 
ATOM   1581 C  CA  . TYR A 1 172 ? -18.80264 17.63289 3.44465   1.000 16.14161 ? 172 TYR A CA  1 
ATOM   1582 C  C   . TYR A 1 172 ? -18.02592 18.57913 2.53595   1.000 15.00242 ? 172 TYR A C   1 
ATOM   1583 O  O   . TYR A 1 172 ? -18.04747 18.40198 1.32424   1.000 16.82666 ? 172 TYR A O   1 
ATOM   1584 C  CB  . TYR A 1 172 ? -20.27489 17.98039 3.56368   1.000 17.75028 ? 172 TYR A CB  1 
ATOM   1585 C  CG  . TYR A 1 172 ? -21.06761 16.77935 4.01978   1.000 17.94410 ? 172 TYR A CG  1 
ATOM   1586 C  CD1 . TYR A 1 172 ? -21.28851 15.72115 3.15278   1.000 19.09149 ? 172 TYR A CD1 1 
ATOM   1587 C  CD2 . TYR A 1 172 ? -21.54226 16.68594 5.31754   1.000 18.23705 ? 172 TYR A CD2 1 
ATOM   1588 C  CE1 . TYR A 1 172 ? -21.98578 14.60874 3.55173   1.000 20.38171 ? 172 TYR A CE1 1 
ATOM   1589 C  CE2 . TYR A 1 172 ? -22.27074 15.57571 5.73409   1.000 20.33972 ? 172 TYR A CE2 1 
ATOM   1590 C  CZ  . TYR A 1 172 ? -22.46927 14.53595 4.83749   1.000 20.34895 ? 172 TYR A CZ  1 
ATOM   1591 O  OH  . TYR A 1 172 ? -23.17565 13.41403 5.20335   1.000 22.30797 ? 172 TYR A OH  1 
ATOM   1592 N  N   A PHE A 1 173 ? -17.46303 19.66255 3.07739   0.700 17.27695 ? 173 PHE A N   1 
ATOM   1593 N  N   B PHE A 1 173 ? -17.23839 19.50030 3.10939   0.300 13.58069 ? 173 PHE A N   1 
ATOM   1594 C  CA  A PHE A 1 173 ? -16.60841 20.50218 2.24932   0.700 14.72049 ? 173 PHE A CA  1 
ATOM   1595 C  CA  B PHE A 1 173 ? -16.36787 20.33139 2.28376   0.300 16.67069 ? 173 PHE A CA  1 
ATOM   1596 C  C   A PHE A 1 173 ? -15.54372 19.63944 1.57748   0.700 13.44889 ? 173 PHE A C   1 
ATOM   1597 C  C   B PHE A 1 173 ? -15.20102 19.52542 1.73886   0.300 17.59927 ? 173 PHE A C   1 
ATOM   1598 O  O   A PHE A 1 173 ? -15.37376 19.66116 0.35435   0.700 15.39956 ? 173 PHE A O   1 
ATOM   1599 O  O   B PHE A 1 173 ? -14.81138 19.70284 0.57837   0.300 14.39478 ? 173 PHE A O   1 
ATOM   1600 C  CB  A PHE A 1 173 ? -16.01214 21.60081 3.14461   0.700 19.30064 ? 173 PHE A CB  1 
ATOM   1601 C  CB  B PHE A 1 173 ? -15.87303 21.54889 3.06640   0.300 20.22575 ? 173 PHE A CB  1 
ATOM   1602 C  CG  A PHE A 1 173 ? -15.19379 22.66486 2.43006   0.700 21.36275 ? 173 PHE A CG  1 
ATOM   1603 C  CG  B PHE A 1 173 ? -14.95940 22.45746 2.27955   0.300 18.32139 ? 173 PHE A CG  1 
ATOM   1604 C  CD1 A PHE A 1 173 ? -15.05645 22.72394 1.05096   0.700 24.08162 ? 173 PHE A CD1 1 
ATOM   1605 C  CD1 B PHE A 1 173 ? -15.45701 23.25425 1.27162   0.300 19.40320 ? 173 PHE A CD1 1 
ATOM   1606 C  CD2 A PHE A 1 173 ? -14.55370 23.62382 3.19514   0.700 26.31868 ? 173 PHE A CD2 1 
ATOM   1607 C  CD2 B PHE A 1 173 ? -13.60830 22.51983 2.55523   0.300 23.00963 ? 173 PHE A CD2 1 
ATOM   1608 C  CE1 A PHE A 1 173 ? -14.28059 23.72313 0.45892   0.700 24.25846 ? 173 PHE A CE1 1 
ATOM   1609 C  CE1 B PHE A 1 173 ? -14.62917 24.12106 0.55847   0.300 22.04785 ? 173 PHE A CE1 1 
ATOM   1610 C  CE2 A PHE A 1 173 ? -13.79990 24.62177 2.62133   0.700 25.25348 ? 173 PHE A CE2 1 
ATOM   1611 C  CE2 B PHE A 1 173 ? -12.77276 23.37151 1.83167   0.300 25.42188 ? 173 PHE A CE2 1 
ATOM   1612 C  CZ  A PHE A 1 173 ? -13.66353 24.68035 1.24911   0.700 24.72431 ? 173 PHE A CZ  1 
ATOM   1613 C  CZ  B PHE A 1 173 ? -13.28878 24.16573 0.84370   0.300 23.89569 ? 173 PHE A CZ  1 
ATOM   1614 N  N   A MET A 1 174 ? -14.81138 18.86138 2.38354   0.600 14.34452 ? 174 MET A N   1 
ATOM   1615 N  N   B MET A 1 174 ? -14.63520 18.63637 2.56043   0.400 18.90761 ? 174 MET A N   1 
ATOM   1616 C  CA  A MET A 1 174 ? -13.74881 17.99738 1.86675   0.600 13.46670 ? 174 MET A CA  1 
ATOM   1617 C  CA  B MET A 1 174 ? -13.59388 17.74184 2.06781   0.400 18.38104 ? 174 MET A CA  1 
ATOM   1618 C  C   A MET A 1 174 ? -14.28765 16.98956 0.85353   0.600 13.43856 ? 174 MET A C   1 
ATOM   1619 C  C   B MET A 1 174 ? -14.14356 16.78209 1.01507   0.400 14.82324 ? 174 MET A C   1 
ATOM   1620 O  O   A MET A 1 174 ? -13.73642 16.83343 -0.24683  0.600 14.33809 ? 174 MET A O   1 
ATOM   1621 O  O   B MET A 1 174 ? -13.48735 16.51336 0.00259   0.400 15.06279 ? 174 MET A O   1 
ATOM   1622 C  CB  A MET A 1 174 ? -13.05760 17.26614 3.02277   0.600 13.32706 ? 174 MET A CB  1 
ATOM   1623 C  CB  B MET A 1 174 ? -12.95693 16.98103 3.23011   0.400 20.14792 ? 174 MET A CB  1 
ATOM   1624 C  CG  A MET A 1 174 ? -11.79720 16.50604 2.58441   0.600 11.42389 ? 174 MET A CG  1 
ATOM   1625 C  CG  B MET A 1 174 ? -11.67109 17.61966 3.72443   0.400 27.88934 ? 174 MET A CG  1 
ATOM   1626 S  SD  A MET A 1 174 ? -11.18100 15.49348 3.91344   0.600 14.92575 ? 174 MET A SD  1 
ATOM   1627 S  SD  B MET A 1 174 ? -10.69398 16.48625 4.73374   0.400 26.19700 ? 174 MET A SD  1 
ATOM   1628 C  CE  A MET A 1 174 ? -9.77457  14.73785 3.05967   0.600 15.55875 ? 174 MET A CE  1 
ATOM   1629 C  CE  B MET A 1 174 ? -10.97926 14.93393 3.89191   0.400 24.15332 ? 174 MET A CE  1 
ATOM   1630 N  N   . PHE A 1 175 ? -15.36758 16.28501 1.21909   1.000 14.71173 ? 175 PHE A N   1 
ATOM   1631 C  CA  . PHE A 1 175 ? -15.94476 15.28633 0.31671   1.000 14.41243 ? 175 PHE A CA  1 
ATOM   1632 C  C   . PHE A 1 175 ? -16.27685 15.92010 -1.04013  1.000 14.52686 ? 175 PHE A C   1 
ATOM   1633 O  O   . PHE A 1 175 ? -15.93566 15.37387 -2.08919  1.000 15.39269 ? 175 PHE A O   1 
ATOM   1634 C  CB  . PHE A 1 175 ? -17.19064 14.67874 0.98681   1.000 15.68231 ? 175 PHE A CB  1 
ATOM   1635 C  CG  . PHE A 1 175 ? -17.77390 13.48956 0.29984   1.000 18.20751 ? 175 PHE A CG  1 
ATOM   1636 C  CD1 . PHE A 1 175 ? -17.03957 12.68664 -0.54173  1.000 20.47247 ? 175 PHE A CD1 1 
ATOM   1637 C  CD2 . PHE A 1 175 ? -19.07403 13.09972 0.60442   1.000 24.99657 ? 175 PHE A CD2 1 
ATOM   1638 C  CE1 . PHE A 1 175 ? -17.61955 11.58135 -1.13601  1.000 21.43112 ? 175 PHE A CE1 1 
ATOM   1639 C  CE2 . PHE A 1 175 ? -19.64499 12.01138 0.02416   1.000 28.79576 ? 175 PHE A CE2 1 
ATOM   1640 C  CZ  . PHE A 1 175 ? -18.90869 11.24161 -0.84794  1.000 28.57078 ? 175 PHE A CZ  1 
ATOM   1641 N  N   . LEU A 1 176 ? -16.97156 17.06426 -1.02741  1.000 15.83182 ? 176 LEU A N   1 
ATOM   1642 C  CA  . LEU A 1 176 ? -17.30174 17.73562 -2.27960  1.000 16.41394 ? 176 LEU A CA  1 
ATOM   1643 C  C   . LEU A 1 176 ? -16.04368 18.09146 -3.07587  1.000 13.98599 ? 176 LEU A C   1 
ATOM   1644 O  O   . LEU A 1 176 ? -15.97245 17.82569 -4.28778  1.000 16.15732 ? 176 LEU A O   1 
ATOM   1645 C  CB  . LEU A 1 176 ? -18.12641 18.98673 -2.00344  1.000 16.75700 ? 176 LEU A CB  1 
ATOM   1646 C  CG  . LEU A 1 176 ? -18.43129 19.81576 -3.25374  1.000 18.79687 ? 176 LEU A CG  1 
ATOM   1647 C  CD1 . LEU A 1 176 ? -19.15671 19.01955 -4.35818  1.000 22.06336 ? 176 LEU A CD1 1 
ATOM   1648 C  CD2 . LEU A 1 176 ? -19.28431 21.02623 -2.84514  1.000 23.68715 ? 176 LEU A CD2 1 
ATOM   1649 N  N   . VAL A 1 177 ? -15.04347 18.70554 -2.42502  1.000 13.83742 ? 177 VAL A N   1 
ATOM   1650 C  CA  . VAL A 1 177 ? -13.82672 19.09120 -3.13508  1.000 13.89541 ? 177 VAL A CA  1 
ATOM   1651 C  C   . VAL A 1 177 ? -13.14959 17.87659 -3.75315  1.000 14.54838 ? 177 VAL A C   1 
ATOM   1652 O  O   . VAL A 1 177 ? -12.72432 17.90854 -4.91376  1.000 15.95769 ? 177 VAL A O   1 
ATOM   1653 C  CB  . VAL A 1 177 ? -12.88871 19.88107 -2.20892  1.000 14.08631 ? 177 VAL A CB  1 
ATOM   1654 C  CG1 . VAL A 1 177 ? -11.50086 20.06232 -2.79496  1.000 16.55236 ? 177 VAL A CG1 1 
ATOM   1655 C  CG2 . VAL A 1 177 ? -13.52353 21.26665 -1.90570  1.000 17.18790 ? 177 VAL A CG2 1 
ATOM   1656 N  N   . TRP A 1 178 ? -13.00397 16.79199 -2.98642  1.000 14.18752 ? 178 TRP A N   1 
ATOM   1657 C  CA  . TRP A 1 178 ? -12.36807 15.61847 -3.56643  1.000 14.34456 ? 178 TRP A CA  1 
ATOM   1658 C  C   . TRP A 1 178 ? -13.20085 15.02547 -4.70814  1.000 13.59087 ? 178 TRP A C   1 
ATOM   1659 O  O   . TRP A 1 178 ? -12.64788 14.65208 -5.75271  1.000 15.19896 ? 178 TRP A O   1 
ATOM   1660 C  CB  . TRP A 1 178 ? -12.07738 14.59548 -2.47608  1.000 14.48142 ? 178 TRP A CB  1 
ATOM   1661 C  CG  . TRP A 1 178 ? -10.89541 14.95233 -1.58484  1.000 13.51436 ? 178 TRP A CG  1 
ATOM   1662 C  CD1 . TRP A 1 178 ? -10.62688 16.18385 -1.04270  1.000 14.29595 ? 178 TRP A CD1 1 
ATOM   1663 C  CD2 . TRP A 1 178 ? -9.88075  14.06964 -1.13718  1.000 14.60172 ? 178 TRP A CD2 1 
ATOM   1664 N  NE1 . TRP A 1 178 ? -9.46811  16.10988 -0.29108  1.000 14.56708 ? 178 TRP A NE1 1 
ATOM   1665 C  CE2 . TRP A 1 178 ? -8.99489  14.82162 -0.33849  1.000 13.79788 ? 178 TRP A CE2 1 
ATOM   1666 C  CE3 . TRP A 1 178 ? -9.62430  12.70183 -1.33980  1.000 15.36753 ? 178 TRP A CE3 1 
ATOM   1667 C  CZ2 . TRP A 1 178 ? -7.85970  14.26654 0.23290   1.000 14.19877 ? 178 TRP A CZ2 1 
ATOM   1668 C  CZ3 . TRP A 1 178 ? -8.48567  12.15148 -0.76829  1.000 16.59259 ? 178 TRP A CZ3 1 
ATOM   1669 C  CH2 . TRP A 1 178 ? -7.64418  12.92830 0.04660   1.000 14.93102 ? 178 TRP A CH2 1 
ATOM   1670 N  N   . PHE A 1 179 ? -14.52650 15.01262 -4.56228  1.000 15.01701 ? 179 PHE A N   1 
ATOM   1671 C  CA  . PHE A 1 179 ? -15.38363 14.54652 -5.64675  1.000 15.13051 ? 179 PHE A CA  1 
ATOM   1672 C  C   . PHE A 1 179 ? -15.13980 15.35064 -6.92565  1.000 16.28792 ? 179 PHE A C   1 
ATOM   1673 O  O   . PHE A 1 179 ? -15.19758 14.81752 -8.04440  1.000 15.98489 ? 179 PHE A O   1 
ATOM   1674 C  CB  . PHE A 1 179 ? -16.83709 14.68225 -5.20708  1.000 18.18085 ? 179 PHE A CB  1 
ATOM   1675 C  CG  . PHE A 1 179 ? -17.81753 14.23374 -6.24610  1.000 24.52776 ? 179 PHE A CG  1 
ATOM   1676 C  CD1 . PHE A 1 179 ? -18.16571 12.89069 -6.34418  1.000 30.63657 ? 179 PHE A CD1 1 
ATOM   1677 C  CD2 . PHE A 1 179 ? -18.38187 15.13300 -7.14624  1.000 25.44161 ? 179 PHE A CD2 1 
ATOM   1678 C  CE1 . PHE A 1 179 ? -19.07559 12.45248 -7.30050  1.000 31.28967 ? 179 PHE A CE1 1 
ATOM   1679 C  CE2 . PHE A 1 179 ? -19.28681 14.69161 -8.11282  1.000 28.58726 ? 179 PHE A CE2 1 
ATOM   1680 C  CZ  . PHE A 1 179 ? -19.62718 13.35784 -8.17828  1.000 32.81646 ? 179 PHE A CZ  1 
ATOM   1681 N  N   . LEU A 1 180 ? -14.90421 16.65217 -6.78669  1.000 14.62620 ? 180 LEU A N   1 
ATOM   1682 C  CA  . LEU A 1 180 ? -14.67235 17.49897 -7.94805  1.000 15.06978 ? 180 LEU A CA  1 
ATOM   1683 C  C   . LEU A 1 180 ? -13.38643 17.15311 -8.71224  1.000 14.65765 ? 180 LEU A C   1 
ATOM   1684 O  O   . LEU A 1 180 ? -13.27729 17.51310 -9.88666  1.000 15.23699 ? 180 LEU A O   1 
ATOM   1685 C  CB  . LEU A 1 180 ? -14.68448 18.95916 -7.52240  1.000 15.26245 ? 180 LEU A CB  1 
ATOM   1686 C  CG  . LEU A 1 180 ? -16.11102 19.43168 -7.17573  1.000 16.47718 ? 180 LEU A CG  1 
ATOM   1687 C  CD1 . LEU A 1 180 ? -16.06932 20.76384 -6.41897  1.000 17.50778 ? 180 LEU A CD1 1 
ATOM   1688 C  CD2 . LEU A 1 180 ? -16.99813 19.53671 -8.45410  1.000 19.88950 ? 180 LEU A CD2 1 
ATOM   1689 N  N   . TYR A 1 181 ? -12.42057 16.43421 -8.11876  1.000 14.64476 ? 181 TYR A N   1 
ATOM   1690 C  CA  . TYR A 1 181 ? -11.32508 15.90346 -8.92035  1.000 13.59490 ? 181 TYR A CA  1 
ATOM   1691 C  C   . TYR A 1 181 ? -11.82954 14.84972 -9.89323  1.000 15.42272 ? 181 TYR A C   1 
ATOM   1692 O  O   . TYR A 1 181 ? -11.31384 14.73281 -11.00864 1.000 16.32211 ? 181 TYR A O   1 
ATOM   1693 C  CB  . TYR A 1 181 ? -10.21326 15.29984 -8.02730  1.000 14.77108 ? 181 TYR A CB  1 
ATOM   1694 C  CG  . TYR A 1 181 ? -9.32633  16.29966 -7.30378  1.000 14.92945 ? 181 TYR A CG  1 
ATOM   1695 C  CD1 . TYR A 1 181 ? -9.79066  17.01085 -6.18967  1.000 14.83164 ? 181 TYR A CD1 1 
ATOM   1696 C  CD2 . TYR A 1 181 ? -8.01297  16.52738 -7.72466  1.000 14.79591 ? 181 TYR A CD2 1 
ATOM   1697 C  CE1 . TYR A 1 181 ? -8.97679  17.90209 -5.54448  1.000 13.87993 ? 181 TYR A CE1 1 
ATOM   1698 C  CE2 . TYR A 1 181 ? -7.19711  17.45763 -7.07520  1.000 14.99826 ? 181 TYR A CE2 1 
ATOM   1699 C  CZ  . TYR A 1 181 ? -7.69867  18.12401 -5.99191  1.000 14.09467 ? 181 TYR A CZ  1 
ATOM   1700 O  OH  . TYR A 1 181 ? -6.89509  18.98693 -5.31241  1.000 14.43318 ? 181 TYR A OH  1 
ATOM   1701 N  N   . GLY A 1 182 ? -12.79786 14.03945 -9.47471  1.000 15.68984 ? 182 GLY A N   1 
ATOM   1702 C  CA  . GLY A 1 182 ? -13.42984 13.12390 -10.40597 1.000 17.29547 ? 182 GLY A CA  1 
ATOM   1703 C  C   . GLY A 1 182 ? -14.22147 13.83863 -11.48500 1.000 16.44177 ? 182 GLY A C   1 
ATOM   1704 O  O   . GLY A 1 182 ? -14.18977 13.44571 -12.66450 1.000 17.98256 ? 182 GLY A O   1 
ATOM   1705 N  N   . PHE A 1 183 ? -14.91098 14.92448 -11.11435 1.000 17.31816 ? 183 PHE A N   1 
ATOM   1706 C  CA  . PHE A 1 183 ? -15.60782 15.72757 -12.11180 1.000 17.18429 ? 183 PHE A CA  1 
ATOM   1707 C  C   . PHE A 1 183 ? -14.63231 16.25398 -13.16233 1.000 18.96259 ? 183 PHE A C   1 
ATOM   1708 O  O   . PHE A 1 183 ? -14.89977 16.18524 -14.36832 1.000 17.83255 ? 183 PHE A O   1 
ATOM   1709 C  CB  . PHE A 1 183 ? -16.35221 16.85837 -11.39375 1.000 19.19427 ? 183 PHE A CB  1 
ATOM   1710 C  CG  . PHE A 1 183 ? -17.21598 17.70488 -12.28378 1.000 20.71881 ? 183 PHE A CG  1 
ATOM   1711 C  CD1 . PHE A 1 183 ? -18.30457 17.16350 -12.94477 1.000 25.43095 ? 183 PHE A CD1 1 
ATOM   1712 C  CD2 . PHE A 1 183 ? -16.95551 19.05153 -12.42768 1.000 21.42259 ? 183 PHE A CD2 1 
ATOM   1713 C  CE1 . PHE A 1 183 ? -19.11067 17.96190 -13.74230 1.000 26.38522 ? 183 PHE A CE1 1 
ATOM   1714 C  CE2 . PHE A 1 183 ? -17.74057 19.84321 -13.23452 1.000 23.66494 ? 183 PHE A CE2 1 
ATOM   1715 C  CZ  . PHE A 1 183 ? -18.81933 19.29483 -13.89384 1.000 24.35194 ? 183 PHE A CZ  1 
ATOM   1716 N  N   . ALA A 1 184 ? -13.48290 16.76564 -12.71971 1.000 16.47658 ? 184 ALA A N   1 
ATOM   1717 C  CA  . ALA A 1 184 ? -12.46415 17.28888 -13.63394 1.000 16.58736 ? 184 ALA A CA  1 
ATOM   1718 C  C   . ALA A 1 184 ? -11.95865 16.24029 -14.62473 1.000 17.35327 ? 184 ALA A C   1 
ATOM   1719 O  O   . ALA A 1 184 ? -11.61925 16.58302 -15.76583 1.000 16.29364 ? 184 ALA A O   1 
ATOM   1720 C  CB  . ALA A 1 184 ? -11.29331 17.86182 -12.83439 1.000 15.26736 ? 184 ALA A CB  1 
ATOM   1721 N  N   . PHE A 1 185 ? -11.91301 14.97095 -14.21380 1.000 17.69995 ? 185 PHE A N   1 
ATOM   1722 C  CA  . PHE A 1 185 ? -11.39226 13.90402 -15.06481 1.000 16.10823 ? 185 PHE A CA  1 
ATOM   1723 C  C   . PHE A 1 185 ? -12.12471 13.84284 -16.39844 1.000 19.82749 ? 185 PHE A C   1 
ATOM   1724 O  O   . PHE A 1 185 ? -11.54946 13.40391 -17.39449 1.000 21.71071 ? 185 PHE A O   1 
ATOM   1725 C  CB  . PHE A 1 185 ? -11.51516 12.58500 -14.28286 1.000 17.10294 ? 185 PHE A CB  1 
ATOM   1726 C  CG  . PHE A 1 185 ? -11.20633 11.35956 -15.09150 1.000 18.93918 ? 185 PHE A CG  1 
ATOM   1727 C  CD1 . PHE A 1 185 ? -12.20466 10.71755 -15.79959 1.000 21.31751 ? 185 PHE A CD1 1 
ATOM   1728 C  CD2 . PHE A 1 185 ? -9.92006  10.85676 -15.12349 1.000 19.68023 ? 185 PHE A CD2 1 
ATOM   1729 C  CE1 . PHE A 1 185 ? -11.93652 9.62433  -16.54047 1.000 22.62890 ? 185 PHE A CE1 1 
ATOM   1730 C  CE2 . PHE A 1 185 ? -9.63051  9.73713  -15.88157 1.000 23.41341 ? 185 PHE A CE2 1 
ATOM   1731 C  CZ  . PHE A 1 185 ? -10.64513 9.13050  -16.60053 1.000 22.50158 ? 185 PHE A CZ  1 
ATOM   1732 N  N   A MET A 1 186 ? -13.39536 14.26508 -16.44174 0.500 18.64086 ? 186 MET A N   1 
ATOM   1733 N  N   B MET A 1 186 ? -13.38043 14.30839 -16.42515 0.500 21.67796 ? 186 MET A N   1 
ATOM   1734 C  CA  A MET A 1 186 ? -14.19145 14.18088 -17.66309 0.500 20.80556 ? 186 MET A CA  1 
ATOM   1735 C  CA  B MET A 1 186 ? -14.25142 14.25472 -17.59348 0.500 25.72669 ? 186 MET A CA  1 
ATOM   1736 C  C   A MET A 1 186 ? -13.81988 15.21680 -18.72810 0.500 20.34566 ? 186 MET A C   1 
ATOM   1737 C  C   B MET A 1 186 ? -13.87480 15.25340 -18.68755 0.500 22.65632 ? 186 MET A C   1 
ATOM   1738 O  O   A MET A 1 186 ? -14.20479 15.04623 -19.89122 0.500 25.22273 ? 186 MET A O   1 
ATOM   1739 O  O   B MET A 1 186 ? -14.30889 15.08574 -19.83295 0.500 28.12901 ? 186 MET A O   1 
ATOM   1740 C  CB  A MET A 1 186 ? -15.68631 14.36589 -17.34437 0.500 21.67118 ? 186 MET A CB  1 
ATOM   1741 C  CB  B MET A 1 186 ? -15.68506 14.57172 -17.14244 0.500 28.24570 ? 186 MET A CB  1 
ATOM   1742 C  CG  A MET A 1 186 ? -16.18593 13.55955 -16.15709 0.500 23.12093 ? 186 MET A CG  1 
ATOM   1743 C  CG  B MET A 1 186 ? -16.76281 14.08322 -18.09075 0.500 36.41226 ? 186 MET A CG  1 
ATOM   1744 S  SD  A MET A 1 186 ? -17.96564 13.70693 -15.89788 0.500 28.51917 ? 186 MET A SD  1 
ATOM   1745 S  SD  B MET A 1 186 ? -18.34400 13.87779 -17.25177 0.500 40.03449 ? 186 MET A SD  1 
ATOM   1746 C  CE  A MET A 1 186 ? -18.25331 15.44999 -16.15333 0.500 29.48119 ? 186 MET A CE  1 
ATOM   1747 C  CE  B MET A 1 186 ? -17.82345 13.18831 -15.68403 0.500 40.06879 ? 186 MET A CE  1 
ATOM   1748 N  N   . PHE A 1 187 ? -13.10039 16.26577 -18.37568 1.000 18.81583 ? 187 PHE A N   1 
ATOM   1749 C  CA  . PHE A 1 187 ? -12.92617 17.39592 -19.27244 1.000 20.01761 ? 187 PHE A CA  1 
ATOM   1750 C  C   . PHE A 1 187 ? -11.68652 17.24694 -20.14481 1.000 19.41068 ? 187 PHE A C   1 
ATOM   1751 O  O   . PHE A 1 187 ? -10.77006 16.49117 -19.81545 1.000 18.80525 ? 187 PHE A O   1 
ATOM   1752 C  CB  . PHE A 1 187 ? -12.86191 18.69467 -18.44778 1.000 18.75276 ? 187 PHE A CB  1 
ATOM   1753 C  CG  . PHE A 1 187 ? -14.20249 19.09977 -17.89381 1.000 19.18927 ? 187 PHE A CG  1 
ATOM   1754 C  CD1 . PHE A 1 187 ? -14.69212 18.51712 -16.74687 1.000 18.74241 ? 187 PHE A CD1 1 
ATOM   1755 C  CD2 . PHE A 1 187 ? -15.01654 19.99253 -18.58171 1.000 21.42110 ? 187 PHE A CD2 1 
ATOM   1756 C  CE1 . PHE A 1 187 ? -15.94325 18.84993 -16.26297 1.000 19.42641 ? 187 PHE A CE1 1 
ATOM   1757 C  CE2 . PHE A 1 187 ? -16.26879 20.33709 -18.09399 1.000 23.75039 ? 187 PHE A CE2 1 
ATOM   1758 C  CZ  . PHE A 1 187 ? -16.75686 19.76027 -16.95243 1.000 22.26543 ? 187 PHE A CZ  1 
ATOM   1759 N  N   . PRO A 1 188 ? -11.63555 17.94039 -21.28725 1.000 20.81098 ? 188 PRO A N   1 
ATOM   1760 C  CA  . PRO A 1 188 ? -10.42151 17.90038 -22.11053 1.000 20.35349 ? 188 PRO A CA  1 
ATOM   1761 C  C   . PRO A 1 188 ? -9.21500  18.45920 -21.37087 1.000 18.58565 ? 188 PRO A C   1 
ATOM   1762 O  O   . PRO A 1 188 ? -9.32125  19.20191 -20.38620 1.000 19.26455 ? 188 PRO A O   1 
ATOM   1763 C  CB  . PRO A 1 188 ? -10.75678 18.78383 -23.31968 1.000 25.71222 ? 188 PRO A CB  1 
ATOM   1764 C  CG  . PRO A 1 188 ? -12.22590 18.92753 -23.32495 1.000 27.07780 ? 188 PRO A CG  1 
ATOM   1765 C  CD  . PRO A 1 188 ? -12.66587 18.80653 -21.87100 1.000 23.63258 ? 188 PRO A CD  1 
ATOM   1766 N  N   . PHE A 1 189 ? -8.04271  18.13977 -21.92122 1.000 19.04288 ? 189 PHE A N   1 
ATOM   1767 C  CA  . PHE A 1 189 ? -6.73725  18.41964 -21.32231 1.000 18.49499 ? 189 PHE A CA  1 
ATOM   1768 C  C   . PHE A 1 189 ? -6.65654  19.77725 -20.62233 1.000 17.39029 ? 189 PHE A C   1 
ATOM   1769 O  O   . PHE A 1 189 ? -6.34041  19.86243 -19.42834 1.000 18.89020 ? 189 PHE A O   1 
ATOM   1770 C  CB  . PHE A 1 189 ? -5.65919  18.31254 -22.41301 1.000 19.27929 ? 189 PHE A CB  1 
ATOM   1771 C  CG  . PHE A 1 189 ? -4.27303  18.65225 -21.92352 1.000 19.14976 ? 189 PHE A CG  1 
ATOM   1772 C  CD1 . PHE A 1 189 ? -3.59143  17.79702 -21.05560 1.000 21.03848 ? 189 PHE A CD1 1 
ATOM   1773 C  CD2 . PHE A 1 189 ? -3.65841  19.82863 -22.30805 1.000 20.51828 ? 189 PHE A CD2 1 
ATOM   1774 C  CE1 . PHE A 1 189 ? -2.31613  18.12926 -20.60371 1.000 22.33327 ? 189 PHE A CE1 1 
ATOM   1775 C  CE2 . PHE A 1 189 ? -2.40175  20.15366 -21.87659 1.000 21.18663 ? 189 PHE A CE2 1 
ATOM   1776 C  CZ  . PHE A 1 189 ? -1.72238  19.31294 -21.00360 1.000 20.70114 ? 189 PHE A CZ  1 
ATOM   1777 N  N   . SER A 1 190 ? -6.89095  20.86159 -21.35832 1.000 17.66534 ? 190 SER A N   1 
ATOM   1778 C  CA  . SER A 1 190 ? -6.62526  22.17485 -20.77960 1.000 17.40341 ? 190 SER A CA  1 
ATOM   1779 C  C   . SER A 1 190 ? -7.57464  22.47916 -19.62361 1.000 18.52102 ? 190 SER A C   1 
ATOM   1780 O  O   . SER A 1 190 ? -7.13790  22.89678 -18.55471 1.000 18.20219 ? 190 SER A O   1 
ATOM   1781 C  CB  . SER A 1 190 ? -6.70183  23.25999 -21.85683 1.000 22.46576 ? 190 SER A CB  1 
ATOM   1782 O  OG  . SER A 1 190 ? -6.51815  24.52210 -21.24241 1.000 24.21199 ? 190 SER A OG  1 
ATOM   1783 N  N   . ILE A 1 191 ? -8.87585  22.26120 -19.81743 1.000 17.82745 ? 191 ILE A N   1 
ATOM   1784 C  CA  . ILE A 1 191 ? -9.87886  22.53527 -18.77958 1.000 16.63672 ? 191 ILE A CA  1 
ATOM   1785 C  C   . ILE A 1 191 ? -9.64915  21.66892 -17.55665 1.000 17.69006 ? 191 ILE A C   1 
ATOM   1786 O  O   . ILE A 1 191 ? -9.66235  22.15575 -16.41230 1.000 16.35916 ? 191 ILE A O   1 
ATOM   1787 C  CB  . ILE A 1 191 ? -11.29869 22.35051 -19.34271 1.000 19.53632 ? 191 ILE A CB  1 
ATOM   1788 C  CG1 . ILE A 1 191 ? -11.59318 23.41230 -20.41317 1.000 24.02466 ? 191 ILE A CG1 1 
ATOM   1789 C  CG2 . ILE A 1 191 ? -12.32186 22.40020 -18.22976 1.000 19.97754 ? 191 ILE A CG2 1 
ATOM   1790 C  CD1 . ILE A 1 191 ? -12.89232 23.17599 -21.14999 1.000 27.95266 ? 191 ILE A CD1 1 
ATOM   1791 N  N   . LYS A 1 192 ? -9.38711  20.38330 -17.78365 1.000 15.70337 ? 192 LYS A N   1 
ATOM   1792 C  CA  . LYS A 1 192 ? -9.13372  19.44883 -16.70464 1.000 16.01214 ? 192 LYS A CA  1 
ATOM   1793 C  C   . LYS A 1 192 ? -7.93707  19.89559 -15.87145 1.000 13.75596 ? 192 LYS A C   1 
ATOM   1794 O  O   . LYS A 1 192 ? -7.99444  19.88812 -14.63579 1.000 15.37437 ? 192 LYS A O   1 
ATOM   1795 C  CB  . LYS A 1 192 ? -8.89158  18.08019 -17.33239 1.000 17.48680 ? 192 LYS A CB  1 
ATOM   1796 C  CG  . LYS A 1 192 ? -8.30492  17.00037 -16.42006 1.000 17.29513 ? 192 LYS A CG  1 
ATOM   1797 C  CD  . LYS A 1 192 ? -8.38694  15.60953 -17.10957 1.000 18.24853 ? 192 LYS A CD  1 
ATOM   1798 C  CE  . LYS A 1 192 ? -7.58433  15.59491 -18.40938 1.000 20.56049 ? 192 LYS A CE  1 
ATOM   1799 N  NZ  . LYS A 1 192 ? -7.57770  14.22548 -19.01879 1.000 26.17042 ? 192 LYS A NZ  1 
ATOM   1800 N  N   . ASN A 1 193 ? -6.84130  20.30381 -16.52443 1.000 14.55058 ? 193 ASN A N   1 
ATOM   1801 C  CA  . ASN A 1 193 ? -5.64770  20.71875 -15.79829 1.000 15.70634 ? 193 ASN A CA  1 
ATOM   1802 C  C   . ASN A 1 193 ? -5.82662  22.04211 -15.08303 1.000 15.41308 ? 193 ASN A C   1 
ATOM   1803 O  O   . ASN A 1 193 ? -5.30614  22.21234 -13.97616 1.000 15.28893 ? 193 ASN A O   1 
ATOM   1804 C  CB  . ASN A 1 193 ? -4.40894  20.66577 -16.68929 1.000 15.80359 ? 193 ASN A CB  1 
ATOM   1805 C  CG  . ASN A 1 193 ? -3.91701  19.26574 -16.81818 1.000 16.99466 ? 193 ASN A CG  1 
ATOM   1806 O  OD1 . ASN A 1 193 ? -3.19028  18.78554 -15.96029 1.000 19.18510 ? 193 ASN A OD1 1 
ATOM   1807 N  ND2 . ASN A 1 193 ? -4.37995  18.55866 -17.84140 1.000 18.99823 ? 193 ASN A ND2 1 
ATOM   1808 N  N   . GLN A 1 194 ? -6.56275  22.97686 -15.68122 1.000 16.32258 ? 194 GLN A N   1 
ATOM   1809 C  CA  . GLN A 1 194 ? -6.94104  24.20048 -14.98348 1.000 14.39251 ? 194 GLN A CA  1 
ATOM   1810 C  C   . GLN A 1 194 ? -7.72393  23.87871 -13.72832 1.000 15.81375 ? 194 GLN A C   1 
ATOM   1811 O  O   . GLN A 1 194 ? -7.47207  24.45587 -12.66631 1.000 16.59598 ? 194 GLN A O   1 
ATOM   1812 C  CB  . GLN A 1 194 ? -7.74565  25.09635 -15.89998 1.000 17.10863 ? 194 GLN A CB  1 
ATOM   1813 C  CG  . GLN A 1 194 ? -6.91680  25.71381 -16.99952 1.000 17.57903 ? 194 GLN A CG  1 
ATOM   1814 C  CD  . GLN A 1 194 ? -7.81190  26.50999 -17.88921 1.000 21.15774 ? 194 GLN A CD  1 
ATOM   1815 O  OE1 . GLN A 1 194 ? -8.40586  27.50629 -17.45384 1.000 23.76107 ? 194 GLN A OE1 1 
ATOM   1816 N  NE2 . GLN A 1 194 ? -7.92152  26.09753 -19.14046 1.000 22.51814 ? 194 GLN A NE2 1 
ATOM   1817 N  N   A MET A 1 195 ? -8.65249  22.91838 -13.81988 0.500 16.03505 ? 195 MET A N   1 
ATOM   1818 N  N   B MET A 1 195 ? -8.70495  22.98032 -13.83263 0.500 17.28199 ? 195 MET A N   1 
ATOM   1819 C  CA  A MET A 1 195 ? -9.47411  22.54857 -12.67293 0.500 14.42050 ? 195 MET A CA  1 
ATOM   1820 C  CA  B MET A 1 195 ? -9.44984  22.56526 -12.65010 0.500 16.27134 ? 195 MET A CA  1 
ATOM   1821 C  C   A MET A 1 195 ? -8.63769  21.92198 -11.56218 0.500 13.72782 ? 195 MET A C   1 
ATOM   1822 C  C   B MET A 1 195 ? -8.52164  22.03922 -11.57187 0.500 15.93784 ? 195 MET A C   1 
ATOM   1823 O  O   A MET A 1 195 ? -8.84325  22.23049 -10.38333 0.500 14.00426 ? 195 MET A O   1 
ATOM   1824 O  O   B MET A 1 195 ? -8.55405  22.51955 -10.43177 0.500 13.98758 ? 195 MET A O   1 
ATOM   1825 C  CB  A MET A 1 195 ? -10.61074 21.61268 -13.10184 0.500 14.65268 ? 195 MET A CB  1 
ATOM   1826 C  CB  B MET A 1 195 ? -10.49280 21.51274 -13.00816 0.500 18.67335 ? 195 MET A CB  1 
ATOM   1827 C  CG  A MET A 1 195 ? -11.69422 22.24960 -13.97607 0.500 12.91960 ? 195 MET A CG  1 
ATOM   1828 C  CG  B MET A 1 195 ? -11.76375 22.12827 -13.50968 0.500 19.31874 ? 195 MET A CG  1 
ATOM   1829 S  SD  A MET A 1 195 ? -12.86764 20.97653 -14.52529 0.500 14.32488 ? 195 MET A SD  1 
ATOM   1830 S  SD  B MET A 1 195 ? -12.91698 20.83289 -13.96246 0.500 20.35442 ? 195 MET A SD  1 
ATOM   1831 C  CE  A MET A 1 195 ? -14.18916 21.98729 -15.19670 0.500 14.29467 ? 195 MET A CE  1 
ATOM   1832 C  CE  B MET A 1 195 ? -14.31443 21.82460 -14.48619 0.500 22.11451 ? 195 MET A CE  1 
ATOM   1833 N  N   . TYR A 1 196 ? -7.68895  21.04971 -11.91030 1.000 14.02008 ? 196 TYR A N   1 
ATOM   1834 C  CA  . TYR A 1 196 ? -6.81009  20.48007 -10.88483 1.000 14.92361 ? 196 TYR A CA  1 
ATOM   1835 C  C   . TYR A 1 196 ? -5.91902  21.55316 -10.25727 1.000 14.94433 ? 196 TYR A C   1 
ATOM   1836 O  O   . TYR A 1 196 ? -5.70779  21.53817 -9.04178  1.000 14.50178 ? 196 TYR A O   1 
ATOM   1837 C  CB  . TYR A 1 196 ? -5.95290  19.35878 -11.47632 1.000 15.00523 ? 196 TYR A CB  1 
ATOM   1838 C  CG  . TYR A 1 196 ? -6.74113  18.11328 -11.82557 1.000 14.98039 ? 196 TYR A CG  1 
ATOM   1839 C  CD1 . TYR A 1 196 ? -7.70654  17.63088 -10.95191 1.000 17.11385 ? 196 TYR A CD1 1 
ATOM   1840 C  CD2 . TYR A 1 196 ? -6.46209  17.38875 -12.98099 1.000 16.04542 ? 196 TYR A CD2 1 
ATOM   1841 C  CE1 . TYR A 1 196 ? -8.42118  16.48260 -11.22807 1.000 15.05154 ? 196 TYR A CE1 1 
ATOM   1842 C  CE2 . TYR A 1 196 ? -7.16455  16.22269 -13.27010 1.000 16.24230 ? 196 TYR A CE2 1 
ATOM   1843 C  CZ  . TYR A 1 196 ? -8.14535  15.77811 -12.40489 1.000 15.50200 ? 196 TYR A CZ  1 
ATOM   1844 O  OH  . TYR A 1 196 ? -8.85647  14.62547 -12.70006 1.000 17.27965 ? 196 TYR A OH  1 
ATOM   1845 N  N   . ASN A 1 197 ? -5.42225  22.49895 -11.05879 1.000 15.18215 ? 197 ASN A N   1 
ATOM   1846 C  CA  . ASN A 1 197 ? -4.51058  23.50999 -10.52196 1.000 15.78635 ? 197 ASN A CA  1 
ATOM   1847 C  C   . ASN A 1 197 ? -5.20737  24.33079 -9.43343  1.000 14.15110 ? 197 ASN A C   1 
ATOM   1848 O  O   . ASN A 1 197 ? -4.59459  24.67049 -8.41643  1.000 16.81804 ? 197 ASN A O   1 
ATOM   1849 C  CB  . ASN A 1 197 ? -4.05031  24.46932 -11.62718 1.000 15.79853 ? 197 ASN A CB  1 
ATOM   1850 C  CG  . ASN A 1 197 ? -3.06811  23.83556 -12.57490 1.000 16.56086 ? 197 ASN A CG  1 
ATOM   1851 O  OD1 . ASN A 1 197 ? -2.48616  22.78116 -12.29501 1.000 15.21533 ? 197 ASN A OD1 1 
ATOM   1852 N  ND2 . ASN A 1 197 ? -2.82530  24.50775 -13.70284 1.000 17.42330 ? 197 ASN A ND2 1 
ATOM   1853 N  N   A ILE A 1 198 ? -6.49273  24.61875 -9.62554  0.500 13.73875 ? 198 ILE A N   1 
ATOM   1854 N  N   B ILE A 1 198 ? -6.48737  24.66201 -9.62889  0.500 14.23078 ? 198 ILE A N   1 
ATOM   1855 C  CA  A ILE A 1 198 ? -7.26059  25.41888 -8.68816  0.500 14.24783 ? 198 ILE A CA  1 
ATOM   1856 C  CA  B ILE A 1 198 ? -7.23948  25.40659 -8.62493  0.500 16.44867 ? 198 ILE A CA  1 
ATOM   1857 C  C   A ILE A 1 198 ? -7.83864  24.56587 -7.55191  0.500 15.50975 ? 198 ILE A C   1 
ATOM   1858 C  C   B ILE A 1 198 ? -7.68672  24.49413 -7.49516  0.500 15.89450 ? 198 ILE A C   1 
ATOM   1859 O  O   A ILE A 1 198 ? -7.92891  25.03728 -6.40895  0.500 15.15397 ? 198 ILE A O   1 
ATOM   1860 O  O   B ILE A 1 198 ? -7.59578  24.86139 -6.31597  0.500 13.50502 ? 198 ILE A O   1 
ATOM   1861 C  CB  A ILE A 1 198 ? -8.35379  26.19022 -9.45416  0.500 13.35758 ? 198 ILE A CB  1 
ATOM   1862 C  CB  B ILE A 1 198 ? -8.44375  26.11567 -9.26750  0.500 18.72456 ? 198 ILE A CB  1 
ATOM   1863 C  CG1 A ILE A 1 198 ? -7.75212  27.02297 -10.58678 0.500 12.28698 ? 198 ILE A CG1 1 
ATOM   1864 C  CG1 B ILE A 1 198 ? -7.97773  27.15214 -10.28552 0.500 19.50869 ? 198 ILE A CG1 1 
ATOM   1865 C  CG2 A ILE A 1 198 ? -9.13080  27.10558 -8.50994  0.500 16.20626 ? 198 ILE A CG2 1 
ATOM   1866 C  CG2 B ILE A 1 198 ? -9.32873  26.74812 -8.18309  0.500 18.24203 ? 198 ILE A CG2 1 
ATOM   1867 C  CD1 A ILE A 1 198 ? -6.78786  28.07726 -10.07535 0.500 13.45001 ? 198 ILE A CD1 1 
ATOM   1868 C  CD1 B ILE A 1 198 ? -9.01016  27.44935 -11.32082 0.500 25.90037 ? 198 ILE A CD1 1 
ATOM   1869 N  N   . LEU A 1 199 ? -8.19879  23.30355 -7.83761  1.000 14.35371 ? 199 LEU A N   1 
ATOM   1870 C  CA  . LEU A 1 199 ? -8.69255  22.41126 -6.78877  1.000 14.58992 ? 199 LEU A CA  1 
ATOM   1871 C  C   . LEU A 1 199 ? -7.62230  22.16087 -5.75555  1.000 13.81759 ? 199 LEU A C   1 
ATOM   1872 O  O   . LEU A 1 199 ? -7.94284  22.09161 -4.56452  1.000 14.62118 ? 199 LEU A O   1 
ATOM   1873 C  CB  . LEU A 1 199 ? -9.15350  21.05933 -7.35886  1.000 14.58895 ? 199 LEU A CB  1 
ATOM   1874 C  CG  . LEU A 1 199 ? -10.52845 21.09946 -8.04883  1.000 14.69951 ? 199 LEU A CG  1 
ATOM   1875 C  CD1 . LEU A 1 199 ? -10.68570 19.82136 -8.90243  1.000 17.24536 ? 199 LEU A CD1 1 
ATOM   1876 C  CD2 . LEU A 1 199 ? -11.62495 21.15863 -7.00162  1.000 15.72190 ? 199 LEU A CD2 1 
ATOM   1877 N  N   . ASP A 1 200 ? -6.35071  22.09717 -6.17710  1.000 14.51991 ? 200 ASP A N   1 
ATOM   1878 C  CA  . ASP A 1 200 ? -5.26482  21.88968 -5.21684  1.000 14.88570 ? 200 ASP A CA  1 
ATOM   1879 C  C   . ASP A 1 200 ? -5.19326  23.02723 -4.19803  1.000 14.36819 ? 200 ASP A C   1 
ATOM   1880 O  O   . ASP A 1 200 ? -4.81727  22.80743 -3.04076  1.000 15.33277 ? 200 ASP A O   1 
ATOM   1881 C  CB  . ASP A 1 200 ? -3.93194  21.71729 -5.94833  1.000 14.39719 ? 200 ASP A CB  1 
ATOM   1882 C  CG  . ASP A 1 200 ? -3.77067  20.35074 -6.59790  1.000 14.02871 ? 200 ASP A CG  1 
ATOM   1883 O  OD1 . ASP A 1 200 ? -4.51954  19.38753 -6.31327  1.000 15.84184 ? 200 ASP A OD1 1 
ATOM   1884 O  OD2 . ASP A 1 200 ? -2.79806  20.20755 -7.35827  1.000 16.18392 ? 200 ASP A OD2 1 
ATOM   1885 N  N   . ILE A 1 201 ? -5.51816  24.24525 -4.62580  1.000 14.61041 ? 201 ILE A N   1 
ATOM   1886 C  CA  . ILE A 1 201 ? -5.50507  25.36903 -3.69291  1.000 15.27204 ? 201 ILE A CA  1 
ATOM   1887 C  C   . ILE A 1 201 ? -6.50613  25.10190 -2.58885  1.000 14.90276 ? 201 ILE A C   1 
ATOM   1888 O  O   . ILE A 1 201 ? -6.25627  25.39620 -1.41306  1.000 16.73295 ? 201 ILE A O   1 
ATOM   1889 C  CB  . ILE A 1 201 ? -5.85667  26.68231 -4.42190  1.000 16.17360 ? 201 ILE A CB  1 
ATOM   1890 C  CG1 . ILE A 1 201 ? -4.82935  27.04464 -5.48284  1.000 17.12557 ? 201 ILE A CG1 1 
ATOM   1891 C  CG2 . ILE A 1 201 ? -6.00778  27.80587 -3.37492  1.000 20.19158 ? 201 ILE A CG2 1 
ATOM   1892 C  CD1 . ILE A 1 201 ? -5.28735  28.18079 -6.38397  1.000 18.34001 ? 201 ILE A CD1 1 
ATOM   1893 N  N   . VAL A 1 202 ? -7.66890  24.55884 -2.94686  1.000 15.12170 ? 202 VAL A N   1 
ATOM   1894 C  CA  . VAL A 1 202 ? -8.73492  24.34810 -1.98292  1.000 15.39502 ? 202 VAL A CA  1 
ATOM   1895 C  C   . VAL A 1 202 ? -8.45497  23.12404 -1.11985  1.000 15.26698 ? 202 VAL A C   1 
ATOM   1896 O  O   . VAL A 1 202 ? -8.63062  23.17248 0.10452   1.000 17.65448 ? 202 VAL A O   1 
ATOM   1897 C  CB  . VAL A 1 202 ? -10.07410 24.21617 -2.72814  1.000 16.87218 ? 202 VAL A CB  1 
ATOM   1898 C  CG1 . VAL A 1 202 ? -11.18853 24.09276 -1.73689  1.000 19.71559 ? 202 VAL A CG1 1 
ATOM   1899 C  CG2 . VAL A 1 202 ? -10.30345 25.45515 -3.64829  1.000 18.76011 ? 202 VAL A CG2 1 
ATOM   1900 N  N   . SER A 1 203 ? -8.05723  22.00562 -1.73660  1.000 14.54025 ? 203 SER A N   1 
ATOM   1901 C  CA  . SER A 1 203 ? -7.88573  20.76512 -0.98418  1.000 15.08327 ? 203 SER A CA  1 
ATOM   1902 C  C   . SER A 1 203 ? -6.66914  20.82166 -0.08917  1.000 15.78555 ? 203 SER A C   1 
ATOM   1903 O  O   . SER A 1 203 ? -6.68911  20.25779 1.00288   1.000 15.64150 ? 203 SER A O   1 
ATOM   1904 C  CB  . SER A 1 203 ? -7.80559  19.55215 -1.93414  1.000 15.06628 ? 203 SER A CB  1 
ATOM   1905 O  OG  . SER A 1 203 ? -6.58103  19.57402 -2.64550  1.000 14.39866 ? 203 SER A OG  1 
ATOM   1906 N  N   A LYS A 1 204 ? -5.62819  21.54206 -0.47551  0.700 15.63791 ? 204 LYS A N   1 
ATOM   1907 N  N   B LYS A 1 204 ? -5.56681  21.37475 -0.59712  0.300 15.31884 ? 204 LYS A N   1 
ATOM   1908 C  CA  A LYS A 1 204 ? -4.40998  21.59105 0.32278   0.700 15.13400 ? 204 LYS A CA  1 
ATOM   1909 C  CA  B LYS A 1 204 ? -4.27008  21.40474 0.07346   0.300 13.47410 ? 204 LYS A CA  1 
ATOM   1910 C  C   A LYS A 1 204 ? -4.25059  22.92602 1.03488   0.700 14.96333 ? 204 LYS A C   1 
ATOM   1911 C  C   B LYS A 1 204 ? -4.04320  22.68717 0.86488   0.300 12.52898 ? 204 LYS A C   1 
ATOM   1912 O  O   A LYS A 1 204 ? -4.26063  22.96212 2.26863   0.700 12.55102 ? 204 LYS A O   1 
ATOM   1913 O  O   B LYS A 1 204 ? -3.67013  22.62955 2.04025   0.300 14.58693 ? 204 LYS A O   1 
ATOM   1914 C  CB  A LYS A 1 204 ? -3.16911  21.27946 -0.52843  0.700 15.79434 ? 204 LYS A CB  1 
ATOM   1915 C  CB  B LYS A 1 204 ? -3.12599  21.22012 -0.94758  0.300 14.22797 ? 204 LYS A CB  1 
ATOM   1916 C  CG  A LYS A 1 204 ? -3.20827  19.85194 -1.15278  0.700 15.40468 ? 204 LYS A CG  1 
ATOM   1917 C  CG  B LYS A 1 204 ? -2.96310  19.77196 -1.46318  0.300 12.97567 ? 204 LYS A CG  1 
ATOM   1918 C  CD  A LYS A 1 204 ? -1.98842  19.65687 -2.04337  0.700 17.15823 ? 204 LYS A CD  1 
ATOM   1919 C  CD  B LYS A 1 204 ? -1.75127  19.59266 -2.40095  0.300 15.64025 ? 204 LYS A CD  1 
ATOM   1920 C  CE  A LYS A 1 204 ? -1.80871  18.19861 -2.44883  0.700 16.24767 ? 204 LYS A CE  1 
ATOM   1921 C  CE  B LYS A 1 204 ? -1.66962  18.14941 -2.89806  0.300 20.93906 ? 204 LYS A CE  1 
ATOM   1922 N  NZ  A LYS A 1 204 ? -2.68481  17.80393 -3.58796  0.700 15.03832 ? 204 LYS A NZ  1 
ATOM   1923 N  NZ  B LYS A 1 204 ? -2.89292  17.47154 -2.42573  0.300 24.85973 ? 204 LYS A NZ  1 
ATOM   1924 N  N   A ASN A 1 205 ? -4.08045  24.02285 0.28814   0.700 15.64543 ? 205 ASN A N   1 
ATOM   1925 N  N   B ASN A 1 205 ? -4.27609  23.84974 0.25228   0.300 13.33905 ? 205 ASN A N   1 
ATOM   1926 C  CA  A ASN A 1 205 ? -3.69536  25.26498 0.93411   0.700 16.20545 ? 205 ASN A CA  1 
ATOM   1927 C  CA  B ASN A 1 205 ? -3.75932  25.09668 0.80721   0.300 14.42469 ? 205 ASN A CA  1 
ATOM   1928 C  C   A ASN A 1 205 ? -4.79597  25.77315 1.85089   0.700 16.62464 ? 205 ASN A C   1 
ATOM   1929 C  C   B ASN A 1 205 ? -4.76171  25.83698 1.69198   0.300 15.55769 ? 205 ASN A C   1 
ATOM   1930 O  O   A ASN A 1 205 ? -4.51363  26.20498 2.97876   0.700 14.94886 ? 205 ASN A O   1 
ATOM   1931 O  O   B ASN A 1 205 ? -4.35318  26.51571 2.64133   0.300 17.18143 ? 205 ASN A O   1 
ATOM   1932 C  CB  A ASN A 1 205 ? -3.34861  26.30997 -0.11700  0.700 16.49089 ? 205 ASN A CB  1 
ATOM   1933 C  CB  B ASN A 1 205 ? -3.22546  25.99140 -0.32191  0.300 13.56614 ? 205 ASN A CB  1 
ATOM   1934 C  CG  A ASN A 1 205 ? -2.30290  25.83358 -1.09653  0.700 17.33957 ? 205 ASN A CG  1 
ATOM   1935 C  CG  B ASN A 1 205 ? -2.07880  25.33584 -1.10238  0.300 15.19301 ? 205 ASN A CG  1 
ATOM   1936 O  OD1 A ASN A 1 205 ? -2.29324  26.29760 -2.22838  0.700 16.04662 ? 205 ASN A OD1 1 
ATOM   1937 O  OD1 B ASN A 1 205 ? -2.29644  24.74872 -2.15495  0.300 17.23286 ? 205 ASN A OD1 1 
ATOM   1938 N  ND2 A ASN A 1 205 ? -1.47122  24.83927 -0.70252  0.700 17.14939 ? 205 ASN A ND2 1 
ATOM   1939 N  ND2 B ASN A 1 205 ? -0.85495  25.44036 -0.58408  0.300 16.54646 ? 205 ASN A ND2 1 
ATOM   1940 N  N   . ILE A 1 206 ? -6.05813  25.71647 1.40364   1.000 16.50841 ? 206 ILE A N   1 
ATOM   1941 C  CA  . ILE A 1 206 ? -7.11394  26.21515 2.29142   1.000 16.83333 ? 206 ILE A CA  1 
ATOM   1942 C  C   . ILE A 1 206 ? -7.14530  25.42085 3.59567   1.000 17.52473 ? 206 ILE A C   1 
ATOM   1943 O  O   . ILE A 1 206 ? -7.37651  25.98089 4.67641   1.000 17.75102 ? 206 ILE A O   1 
ATOM   1944 C  CB  . ILE A 1 206 ? -8.48896  26.27443 1.59446   1.000 17.45732 ? 206 ILE A CB  1 
ATOM   1945 C  CG1 . ILE A 1 206 ? -8.47132  27.42424 0.59482   1.000 19.71190 ? 206 ILE A CG1 1 
ATOM   1946 C  CG2 . ILE A 1 206 ? -9.65559  26.41704 2.61362   1.000 19.70307 ? 206 ILE A CG2 1 
ATOM   1947 C  CD1 . ILE A 1 206 ? -9.79319  27.66923 -0.14376  1.000 27.35231 ? 206 ILE A CD1 1 
ATOM   1948 N  N   A TYR A 1 207 ? -6.85203  24.12309 3.52603   0.700 17.75895 ? 207 TYR A N   1 
ATOM   1949 N  N   B TYR A 1 207 ? -6.95852  24.09849 3.51469   0.300 17.60513 ? 207 TYR A N   1 
ATOM   1950 C  CA  A TYR A 1 207 ? -6.78258  23.32561 4.74038   0.700 17.59472 ? 207 TYR A CA  1 
ATOM   1951 C  CA  B TYR A 1 207 ? -6.93528  23.29533 4.73291   0.300 18.10557 ? 207 TYR A CA  1 
ATOM   1952 C  C   A TYR A 1 207 ? -5.69283  23.82954 5.67746   0.700 15.64826 ? 207 TYR A C   1 
ATOM   1953 C  C   B TYR A 1 207 ? -5.77752  23.69388 5.63385   0.300 16.79505 ? 207 TYR A C   1 
ATOM   1954 O  O   A TYR A 1 207 ? -5.94921  24.06946 6.86314   0.700 14.39327 ? 207 TYR A O   1 
ATOM   1955 O  O   B TYR A 1 207 ? -5.89402  23.61908 6.86214   0.300 17.20249 ? 207 TYR A O   1 
ATOM   1956 C  CB  A TYR A 1 207 ? -6.59262  21.85554 4.38277   0.700 19.47592 ? 207 TYR A CB  1 
ATOM   1957 C  CB  B TYR A 1 207 ? -6.86844  21.80034 4.40067   0.300 19.46526 ? 207 TYR A CB  1 
ATOM   1958 C  CG  A TYR A 1 207 ? -6.89642  20.96199 5.56615   0.700 21.41476 ? 207 TYR A CG  1 
ATOM   1959 C  CG  B TYR A 1 207 ? -7.46451  20.90235 5.48009   0.300 20.99332 ? 207 TYR A CG  1 
ATOM   1960 C  CD1 A TYR A 1 207 ? -8.21736  20.66261 5.92170   0.700 25.27241 ? 207 TYR A CD1 1 
ATOM   1961 C  CD1 B TYR A 1 207 ? -6.84937  20.75324 6.71795   0.300 21.41431 ? 207 TYR A CD1 1 
ATOM   1962 C  CD2 A TYR A 1 207 ? -5.88197  20.45988 6.36322   0.700 20.00955 ? 207 TYR A CD2 1 
ATOM   1963 C  CD2 B TYR A 1 207 ? -8.64217  20.19544 5.25526   0.300 22.67307 ? 207 TYR A CD2 1 
ATOM   1964 C  CE1 A TYR A 1 207 ? -8.51732  19.86266 7.01616   0.700 25.89053 ? 207 TYR A CE1 1 
ATOM   1965 C  CE1 B TYR A 1 207 ? -7.39061  19.94521 7.70468   0.300 22.14637 ? 207 TYR A CE1 1 
ATOM   1966 C  CE2 A TYR A 1 207 ? -6.17413  19.63685 7.45508   0.700 21.90091 ? 207 TYR A CE2 1 
ATOM   1967 C  CE2 B TYR A 1 207 ? -9.19006  19.38123 6.23132   0.300 22.03913 ? 207 TYR A CE2 1 
ATOM   1968 C  CZ  A TYR A 1 207 ? -7.48623  19.35382 7.78858   0.700 23.59693 ? 207 TYR A CZ  1 
ATOM   1969 C  CZ  B TYR A 1 207 ? -8.56723  19.25949 7.45483   0.300 21.13211 ? 207 TYR A CZ  1 
ATOM   1970 O  OH  A TYR A 1 207 ? -7.76399  18.56330 8.88715   0.700 23.59157 ? 207 TYR A OH  1 
ATOM   1971 O  OH  B TYR A 1 207 ? -9.12801  18.44392 8.41920   0.300 24.48794 ? 207 TYR A OH  1 
ATOM   1972 N  N   A SER A 1 208 ? -4.47316  24.02025 5.15437   0.500 14.36708 ? 208 SER A N   1 
ATOM   1973 N  N   B SER A 1 208 ? -4.66205  24.14023 5.04949   0.500 17.88586 ? 208 SER A N   1 
ATOM   1974 C  CA  A SER A 1 208 ? -3.38163  24.58397 5.94652   0.500 14.25208 ? 208 SER A CA  1 
ATOM   1975 C  CA  B SER A 1 208 ? -3.51617  24.52340 5.86425   0.500 20.05040 ? 208 SER A CA  1 
ATOM   1976 C  C   A SER A 1 208 ? -3.77463  25.91712 6.57526   0.500 14.68267 ? 208 SER A C   1 
ATOM   1977 C  C   B SER A 1 208 ? -3.71926  25.89441 6.50627   0.500 18.79259 ? 208 SER A C   1 
ATOM   1978 O  O   A SER A 1 208 ? -3.54368  26.14778 7.77073   0.500 13.70863 ? 208 SER A O   1 
ATOM   1979 O  O   B SER A 1 208 ? -3.29369  26.12075 7.64610   0.500 19.86745 ? 208 SER A O   1 
ATOM   1980 C  CB  A SER A 1 208 ? -2.14683  24.77082 5.07067   0.500 13.80160 ? 208 SER A CB  1 
ATOM   1981 C  CB  B SER A 1 208 ? -2.24100  24.49077 5.02705   0.500 23.68633 ? 208 SER A CB  1 
ATOM   1982 O  OG  A SER A 1 208 ? -1.62711  23.51938 4.67415   0.500 13.17293 ? 208 SER A OG  1 
ATOM   1983 O  OG  B SER A 1 208 ? -1.13165  24.83660 5.83038   0.500 29.44029 ? 208 SER A OG  1 
ATOM   1984 N  N   . ILE A 1 209 ? -4.36065  26.81847 5.78316   1.000 16.80597 ? 209 ILE A N   1 
ATOM   1985 C  CA  . ILE A 1 209 ? -4.73553  28.12190 6.33002   1.000 17.11198 ? 209 ILE A CA  1 
ATOM   1986 C  C   . ILE A 1 209 ? -5.74263  27.94804 7.46138   1.000 16.24820 ? 209 ILE A C   1 
ATOM   1987 O  O   . ILE A 1 209 ? -5.66211  28.61367 8.50563   1.000 17.10818 ? 209 ILE A O   1 
ATOM   1988 C  CB  . ILE A 1 209 ? -5.27299  29.02857 5.20839   1.000 18.42032 ? 209 ILE A CB  1 
ATOM   1989 C  CG1 . ILE A 1 209 ? -4.14788  29.34975 4.19771   1.000 19.97077 ? 209 ILE A CG1 1 
ATOM   1990 C  CG2 . ILE A 1 209 ? -5.79596  30.34959 5.83954   1.000 19.71235 ? 209 ILE A CG2 1 
ATOM   1991 C  CD1 . ILE A 1 209 ? -4.66065  29.91488 2.89417   1.000 25.60593 ? 209 ILE A CD1 1 
ATOM   1992 N  N   . PHE A 1 210 ? -6.71002  27.05366 7.26090   1.000 16.09972 ? 210 PHE A N   1 
ATOM   1993 C  CA  . PHE A 1 210 ? -7.67936  26.72166 8.29877   1.000 15.65417 ? 210 PHE A CA  1 
ATOM   1994 C  C   . PHE A 1 210 ? -6.99807  26.26518 9.58017   1.000 15.86670 ? 210 PHE A C   1 
ATOM   1995 O  O   . PHE A 1 210 ? -7.29940  26.77162 10.67449  1.000 16.07903 ? 210 PHE A O   1 
ATOM   1996 C  CB  . PHE A 1 210 ? -8.62918  25.65058 7.74955   1.000 16.68671 ? 210 PHE A CB  1 
ATOM   1997 C  CG  . PHE A 1 210 ? -9.49774  25.01743 8.78198   1.000 16.40476 ? 210 PHE A CG  1 
ATOM   1998 C  CD1 . PHE A 1 210 ? -10.53131 25.72857 9.40228   1.000 17.98010 ? 210 PHE A CD1 1 
ATOM   1999 C  CD2 . PHE A 1 210 ? -9.31536  23.67146 9.10301   1.000 18.18837 ? 210 PHE A CD2 1 
ATOM   2000 C  CE1 . PHE A 1 210 ? -11.35247 25.10334 10.34376  1.000 20.26555 ? 210 PHE A CE1 1 
ATOM   2001 C  CE2 . PHE A 1 210 ? -10.13033 23.03566 10.05891  1.000 19.53608 ? 210 PHE A CE2 1 
ATOM   2002 C  CZ  . PHE A 1 210 ? -11.14707 23.76465 10.66898  1.000 19.07247 ? 210 PHE A CZ  1 
ATOM   2003 N  N   . ILE A 1 211 ? -6.07509  25.30785 9.47237   1.000 14.89891 ? 211 ILE A N   1 
ATOM   2004 C  CA  . ILE A 1 211 ? -5.38718  24.79268 10.65987  1.000 15.92731 ? 211 ILE A CA  1 
ATOM   2005 C  C   . ILE A 1 211 ? -4.59921  25.92029 11.33192  1.000 16.51276 ? 211 ILE A C   1 
ATOM   2006 O  O   . ILE A 1 211 ? -4.58575  26.05562 12.55923  1.000 15.80599 ? 211 ILE A O   1 
ATOM   2007 C  CB  . ILE A 1 211 ? -4.48984  23.61142 10.26758  1.000 15.74280 ? 211 ILE A CB  1 
ATOM   2008 C  CG1 . ILE A 1 211 ? -5.33407  22.39170 9.81089   1.000 17.30216 ? 211 ILE A CG1 1 
ATOM   2009 C  CG2 . ILE A 1 211 ? -3.56580  23.23622 11.43814  1.000 17.06554 ? 211 ILE A CG2 1 
ATOM   2010 C  CD1 . ILE A 1 211 ? -6.23373  21.85177 10.90658  1.000 19.11340 ? 211 ILE A CD1 1 
ATOM   2011 N  N   . PHE A 1 212 ? -3.94958  26.75629 10.53969  1.000 16.51091 ? 212 PHE A N   1 
ATOM   2012 C  CA  . PHE A 1 212 ? -3.23750  27.90053 11.09780  1.000 16.37662 ? 212 PHE A CA  1 
ATOM   2013 C  C   . PHE A 1 212 ? -4.16190  28.81537 11.89367  1.000 17.18214 ? 212 PHE A C   1 
ATOM   2014 O  O   . PHE A 1 212 ? -3.80298  29.27817 12.99151  1.000 17.00620 ? 212 PHE A O   1 
ATOM   2015 C  CB  . PHE A 1 212 ? -2.57991  28.69445 9.96442   1.000 17.67864 ? 212 PHE A CB  1 
ATOM   2016 C  CG  . PHE A 1 212 ? -1.95379  29.98481 10.44010  1.000 16.64675 ? 212 PHE A CG  1 
ATOM   2017 C  CD1 . PHE A 1 212 ? -0.68486  29.98802 10.98835  1.000 18.38818 ? 212 PHE A CD1 1 
ATOM   2018 C  CD2 . PHE A 1 212 ? -2.65416  31.18702 10.39547  1.000 19.90455 ? 212 PHE A CD2 1 
ATOM   2019 C  CE1 . PHE A 1 212 ? -0.09598  31.16357 11.43912  1.000 20.22752 ? 212 PHE A CE1 1 
ATOM   2020 C  CE2 . PHE A 1 212 ? -2.08207  32.36780 10.85808  1.000 24.16754 ? 212 PHE A CE2 1 
ATOM   2021 C  CZ  . PHE A 1 212 ? -0.80234  32.35222 11.39603  1.000 24.04998 ? 212 PHE A CZ  1 
ATOM   2022 N  N   . ILE A 1 213 ? -5.33473  29.13314 11.33317  1.000 15.57785 ? 213 ILE A N   1 
ATOM   2023 C  CA  . ILE A 1 213 ? -6.27733  30.00481 12.03051  1.000 16.82409 ? 213 ILE A CA  1 
ATOM   2024 C  C   . ILE A 1 213 ? -6.76892  29.34580 13.32297  1.000 17.15140 ? 213 ILE A C   1 
ATOM   2025 O  O   . ILE A 1 213 ? -6.93831  30.01272 14.35051  1.000 17.01605 ? 213 ILE A O   1 
ATOM   2026 C  CB  . ILE A 1 213 ? -7.41670  30.44252 11.09522  1.000 17.24420 ? 213 ILE A CB  1 
ATOM   2027 C  CG1 . ILE A 1 213 ? -6.84489  31.30487 9.99590   1.000 19.69367 ? 213 ILE A CG1 1 
ATOM   2028 C  CG2 . ILE A 1 213 ? -8.50665  31.17983 11.87409  1.000 21.01013 ? 213 ILE A CG2 1 
ATOM   2029 C  CD1 . ILE A 1 213 ? -7.85275  31.54428 8.89319   1.000 21.30231 ? 213 ILE A CD1 1 
ATOM   2030 N  N   . VAL A 1 214 ? -7.04131  28.03326 13.28988  1.000 16.69078 ? 214 VAL A N   1 
ATOM   2031 C  CA  . VAL A 1 214 ? -7.42739  27.33304 14.51691  1.000 16.30088 ? 214 VAL A CA  1 
ATOM   2032 C  C   . VAL A 1 214 ? -6.31956  27.44119 15.56558  1.000 17.93706 ? 214 VAL A C   1 
ATOM   2033 O  O   . VAL A 1 214 ? -6.57315  27.75339 16.73549  1.000 17.63896 ? 214 VAL A O   1 
ATOM   2034 C  CB  . VAL A 1 214 ? -7.80141  25.86915 14.21718  1.000 17.64425 ? 214 VAL A CB  1 
ATOM   2035 C  CG1 . VAL A 1 214 ? -8.13183  25.12046 15.52579  1.000 18.19359 ? 214 VAL A CG1 1 
ATOM   2036 C  CG2 . VAL A 1 214 ? -9.01415  25.80154 13.27633  1.000 18.50727 ? 214 VAL A CG2 1 
ATOM   2037 N  N   . ILE A 1 215 ? -5.05882  27.22860 15.15596  1.000 16.55294 ? 215 ILE A N   1 
ATOM   2038 C  CA  . ILE A 1 215 ? -3.93594  27.37292 16.07120  1.000 17.66081 ? 215 ILE A CA  1 
ATOM   2039 C  C   . ILE A 1 215 ? -3.90044  28.78248 16.63975  1.000 16.80428 ? 215 ILE A C   1 
ATOM   2040 O  O   . ILE A 1 215 ? -3.74467  28.97984 17.84341  1.000 18.27140 ? 215 ILE A O   1 
ATOM   2041 C  CB  . ILE A 1 215 ? -2.61219  27.04387 15.35172  1.000 17.45752 ? 215 ILE A CB  1 
ATOM   2042 C  CG1 . ILE A 1 215 ? -2.51706  25.53226 15.09377  1.000 16.84930 ? 215 ILE A CG1 1 
ATOM   2043 C  CG2 . ILE A 1 215 ? -1.38996  27.53981 16.18577  1.000 18.31918 ? 215 ILE A CG2 1 
ATOM   2044 C  CD1 . ILE A 1 215 ? -1.30904  25.13878 14.19559  1.000 17.62470 ? 215 ILE A CD1 1 
ATOM   2045 N  N   . LEU A 1 216 ? -3.96770  29.78640 15.77342  1.000 16.82377 ? 216 LEU A N   1 
ATOM   2046 C  CA  . LEU A 1 216 ? -3.86597  31.15789 16.24002  1.000 19.20859 ? 216 LEU A CA  1 
ATOM   2047 C  C   . LEU A 1 216 ? -4.98917  31.47804 17.21867  1.000 19.74241 ? 216 LEU A C   1 
ATOM   2048 O  O   . LEU A 1 216 ? -4.74576  32.07272 18.28118  1.000 21.31399 ? 216 LEU A O   1 
ATOM   2049 C  CB  . LEU A 1 216 ? -3.88113  32.10044 15.03193  1.000 22.85444 ? 216 LEU A CB  1 
ATOM   2050 C  CG  . LEU A 1 216 ? -3.51659  33.54331 15.33555  1.000 26.01827 ? 216 LEU A CG  1 
ATOM   2051 C  CD1 . LEU A 1 216 ? -2.12109  33.66462 15.90654  1.000 32.33925 ? 216 LEU A CD1 1 
ATOM   2052 C  CD2 . LEU A 1 216 ? -3.67581  34.31496 14.04364  1.000 28.46889 ? 216 LEU A CD2 1 
ATOM   2053 N  N   . ASN A 1 217 ? -6.21740  31.04560 16.90149  1.000 19.27202 ? 217 ASN A N   1 
ATOM   2054 C  CA  . ASN A 1 217 ? -7.36465  31.26835 17.78566  1.000 21.86881 ? 217 ASN A CA  1 
ATOM   2055 C  C   . ASN A 1 217 ? -7.18841  30.57670 19.12999  1.000 23.81261 ? 217 ASN A C   1 
ATOM   2056 O  O   . ASN A 1 217 ? -7.48123  31.15335 20.18002  1.000 23.84825 ? 217 ASN A O   1 
ATOM   2057 C  CB  . ASN A 1 217 ? -8.63050  30.76701 17.08834  1.000 21.91399 ? 217 ASN A CB  1 
ATOM   2058 C  CG  . ASN A 1 217 ? -9.83483  30.80909 17.97134  1.000 28.95420 ? 217 ASN A CG  1 
ATOM   2059 O  OD1 . ASN A 1 217 ? -10.33687 29.77199 18.41673  1.000 34.89481 ? 217 ASN A OD1 1 
ATOM   2060 N  ND2 . ASN A 1 217 ? -10.29566 32.00714 18.26543  1.000 34.36817 ? 217 ASN A ND2 1 
ATOM   2061 N  N   . GLN A 1 218 ? -6.69929  29.34468 19.12509  1.000 20.73698 ? 218 GLN A N   1 
ATOM   2062 C  CA  . GLN A 1 218 ? -6.55520  28.63493 20.38818  1.000 24.46629 ? 218 GLN A CA  1 
ATOM   2063 C  C   . GLN A 1 218 ? -5.43645  29.21597 21.23288  1.000 26.44835 ? 218 GLN A C   1 
ATOM   2064 O  O   . GLN A 1 218 ? -5.50476  29.15929 22.46326  1.000 28.10870 ? 218 GLN A O   1 
ATOM   2065 C  CB  . GLN A 1 218 ? -6.25652  27.15697 20.11591  1.000 28.30237 ? 218 GLN A CB  1 
ATOM   2066 C  CG  . GLN A 1 218 ? -7.43025  26.43855 19.46587  1.000 28.16567 ? 218 GLN A CG  1 
ATOM   2067 C  CD  . GLN A 1 218 ? -8.63157  26.42849 20.37157  1.000 31.91758 ? 218 GLN A CD  1 
ATOM   2068 O  OE1 . GLN A 1 218 ? -8.59289  25.84797 21.44918  1.000 38.59526 ? 218 GLN A OE1 1 
ATOM   2069 N  NE2 . GLN A 1 218 ? -9.68454  27.10761 19.96777  1.000 38.55292 ? 218 GLN A NE2 1 
ATOM   2070 N  N   . SER A 1 219 ? -4.40218  29.76579 20.60631  1.000 27.93875 ? 219 SER A N   1 
ATOM   2071 C  CA  . SER A 1 219 ? -3.18210  30.09908 21.32622  1.000 30.73505 ? 219 SER A CA  1 
ATOM   2072 C  C   . SER A 1 219 ? -2.93199  31.58822 21.48419  1.000 39.68895 ? 219 SER A C   1 
ATOM   2073 O  O   . SER A 1 219 ? -1.87730  31.96001 22.00972  1.000 40.05816 ? 219 SER A O   1 
ATOM   2074 C  CB  . SER A 1 219 ? -1.97453  29.47635 20.62497  1.000 31.93100 ? 219 SER A CB  1 
ATOM   2075 O  OG  . SER A 1 219 ? -2.23080  28.12876 20.26282  1.000 37.48969 ? 219 SER A OG  1 
ATOM   2076 N  N   A TYR A 1 220 ? -3.85945  32.44759 21.05220  0.500 43.73381 ? 220 TYR A N   1 
ATOM   2077 N  N   B TYR A 1 220 ? -3.86664  32.44592 21.06216  0.500 43.81864 ? 220 TYR A N   1 
ATOM   2078 C  CA  A TYR A 1 220 ? -3.54915  33.87132 20.96117  0.500 52.19096 ? 220 TYR A CA  1 
ATOM   2079 C  CA  B TYR A 1 220 ? -3.56569  33.87249 20.95814  0.500 52.40289 ? 220 TYR A CA  1 
ATOM   2080 C  C   A TYR A 1 220 ? -3.15800  34.46094 22.30933  0.500 54.91794 ? 220 TYR A C   1 
ATOM   2081 C  C   B TYR A 1 220 ? -3.19003  34.48383 22.30282  0.500 55.20424 ? 220 TYR A C   1 
ATOM   2082 O  O   A TYR A 1 220 ? -2.29825  35.34752 22.36746  0.500 53.75299 ? 220 TYR A O   1 
ATOM   2083 O  O   B TYR A 1 220 ? -2.36731  35.40516 22.35224  0.500 54.36867 ? 220 TYR A O   1 
ATOM   2084 C  CB  A TYR A 1 220 ? -4.71185  34.65056 20.34829  0.500 58.11133 ? 220 TYR A CB  1 
ATOM   2085 C  CB  B TYR A 1 220 ? -4.72365  34.62909 20.30102  0.500 58.63992 ? 220 TYR A CB  1 
ATOM   2086 C  CG  A TYR A 1 220 ? -4.36620  36.09882 20.08527  0.500 63.48699 ? 220 TYR A CG  1 
ATOM   2087 C  CG  B TYR A 1 220 ? -5.95169  34.81027 21.16664  0.500 64.79178 ? 220 TYR A CG  1 
ATOM   2088 C  CD1 A TYR A 1 220 ? -3.56148  36.45382 19.01015  0.500 65.36550 ? 220 TYR A CD1 1 
ATOM   2089 C  CD1 B TYR A 1 220 ? -6.76028  33.73259 21.49522  0.500 67.13862 ? 220 TYR A CD1 1 
ATOM   2090 C  CD2 A TYR A 1 220 ? -4.83431  37.10959 20.91649  0.500 65.57985 ? 220 TYR A CD2 1 
ATOM   2091 C  CD2 B TYR A 1 220 ? -6.31694  36.06857 21.63312  0.500 67.38642 ? 220 TYR A CD2 1 
ATOM   2092 C  CE1 A TYR A 1 220 ? -3.23591  37.77423 18.76576  0.500 67.26793 ? 220 TYR A CE1 1 
ATOM   2093 C  CE1 B TYR A 1 220 ? -7.88979  33.89649 22.27571  0.500 69.09562 ? 220 TYR A CE1 1 
ATOM   2094 C  CE2 A TYR A 1 220 ? -4.51411  38.43372 20.67996  0.500 67.72682 ? 220 TYR A CE2 1 
ATOM   2095 C  CE2 B TYR A 1 220 ? -7.44571  36.24321 22.41255  0.500 68.84138 ? 220 TYR A CE2 1 
ATOM   2096 C  CZ  A TYR A 1 220 ? -3.71449  38.75976 19.60305  0.500 68.75140 ? 220 TYR A CZ  1 
ATOM   2097 C  CZ  B TYR A 1 220 ? -8.22673  35.15409 22.73211  0.500 69.94588 ? 220 TYR A CZ  1 
ATOM   2098 O  OH  A TYR A 1 220 ? -3.39337  40.07604 19.36307  0.500 70.22215 ? 220 TYR A OH  1 
ATOM   2099 O  OH  B TYR A 1 220 ? -9.34925  35.32198 23.50897  0.500 71.13677 ? 220 TYR A OH  1 
ATOM   2100 N  N   . LYS A 1 221 ? -3.76389  33.98031 23.39896  1.000 56.23925 ? 221 LYS A N   1 
ATOM   2101 C  CA  . LYS A 1 221 ? -3.39848  34.48296 24.72202  1.000 57.79975 ? 221 LYS A CA  1 
ATOM   2102 C  C   . LYS A 1 221 ? -1.95850  34.12787 25.07675  1.000 56.28741 ? 221 LYS A C   1 
ATOM   2103 O  O   . LYS A 1 221 ? -1.25135  34.92923 25.70019  1.000 54.44644 ? 221 LYS A O   1 
ATOM   2104 C  CB  . LYS A 1 221 ? -4.37335  33.96320 25.77878  1.000 61.31833 ? 221 LYS A CB  1 
ATOM   2105 C  CG  . LYS A 1 221 ? -5.75561  34.60333 25.73216  1.000 66.36687 ? 221 LYS A CG  1 
ATOM   2106 C  CD  . LYS A 1 221 ? -5.74671  36.00821 26.32463  1.000 70.63833 ? 221 LYS A CD  1 
ATOM   2107 C  CE  . LYS A 1 221 ? -5.67503  37.08613 25.24601  1.000 73.12133 ? 221 LYS A CE  1 
ATOM   2108 N  NZ  . LYS A 1 221 ? -5.50311  38.45649 25.81301  1.000 73.88304 ? 221 LYS A NZ  1 
ATOM   2109 N  N   . LEU A 1 222 ? -1.50361  32.93440 24.69274  1.000 55.29547 ? 222 LEU A N   1 
ATOM   2110 C  CA  . LEU A 1 222 ? -0.10308  32.58816 24.89807  1.000 59.15162 ? 222 LEU A CA  1 
ATOM   2111 C  C   . LEU A 1 222 ? 0.83200   33.44939 24.05835  1.000 63.76793 ? 222 LEU A C   1 
ATOM   2112 O  O   . LEU A 1 222 ? 2.00249   33.60218 24.42081  1.000 63.33905 ? 222 LEU A O   1 
ATOM   2113 C  CB  . LEU A 1 222 ? 0.13210   31.11153 24.58150  1.000 58.37638 ? 222 LEU A CB  1 
ATOM   2114 C  CG  . LEU A 1 222 ? -0.67996  30.08621 25.36917  1.000 57.30541 ? 222 LEU A CG  1 
ATOM   2115 C  CD1 . LEU A 1 222 ? -0.29739  28.68434 24.92476  1.000 54.15732 ? 222 LEU A CD1 1 
ATOM   2116 C  CD2 . LEU A 1 222 ? -0.45322  30.26099 26.86253  1.000 58.07120 ? 222 LEU A CD2 1 
ATOM   2117 N  N   . LEU A 1 223 ? 0.34375   34.01054 22.94845  1.000 66.22068 ? 223 LEU A N   1 
ATOM   2118 C  CA  . LEU A 1 223 ? 1.16820   34.87105 22.10436  1.000 69.09777 ? 223 LEU A CA  1 
ATOM   2119 C  C   . LEU A 1 223 ? 1.19342   36.30591 22.62054  1.000 73.08740 ? 223 LEU A C   1 
ATOM   2120 O  O   . LEU A 1 223 ? 2.26384   36.91298 22.74015  1.000 75.26986 ? 223 LEU A O   1 
ATOM   2121 C  CB  . LEU A 1 223 ? 0.64953   34.84495 20.66543  1.000 66.96678 ? 223 LEU A CB  1 
ATOM   2122 C  CG  . LEU A 1 223 ? 1.14009   33.73160 19.74773  1.000 65.65921 ? 223 LEU A CG  1 
ATOM   2123 C  CD1 . LEU A 1 223 ? 0.43381   33.82874 18.41288  1.000 65.41532 ? 223 LEU A CD1 1 
ATOM   2124 C  CD2 . LEU A 1 223 ? 2.64510   33.81601 19.56298  1.000 64.67481 ? 223 LEU A CD2 1 
ATOM   2125 N  N   . LEU A 1 224 ? 0.02466   36.86721 22.91262  1.000 74.87769 ? 224 LEU A N   1 
ATOM   2126 C  CA  . LEU A 1 224 ? -0.06994  38.24014 23.38767  1.000 76.41320 ? 224 LEU A CA  1 
ATOM   2127 C  C   . LEU A 1 224 ? 0.31354   38.32853 24.86013  1.000 78.33770 ? 224 LEU A C   1 
ATOM   2128 O  O   . LEU A 1 224 ? -0.00846  37.43979 25.65006  1.000 79.65462 ? 224 LEU A O   1 
ATOM   2129 C  CB  . LEU A 1 224 ? -1.48563  38.78167 23.17374  1.000 76.35990 ? 224 LEU A CB  1 
HETATM 2130 NA NA  A NA  B 2 .   ? -4.50307  11.75374 -20.06562 0.700 24.99152 ? 301 NA  A NA  1 
HETATM 2131 C  C1  A RET C 3 .   ? -10.02029 10.48508 -9.90483  0.700 16.73598 ? 302 RET A C1  1 
HETATM 2132 C  C1  B RET C 3 .   ? -9.94359  10.08374 -10.09014 0.300 14.16562 ? 302 RET A C1  1 
HETATM 2133 C  C2  A RET C 3 .   ? -10.63970 9.67264  -11.05657 0.700 20.01166 ? 302 RET A C2  1 
HETATM 2134 C  C2  B RET C 3 .   ? -10.61526 9.15466  -11.10670 0.300 13.50559 ? 302 RET A C2  1 
HETATM 2135 C  C3  A RET C 3 .   ? -11.66614 8.63194  -10.64690 0.700 24.78681 ? 302 RET A C3  1 
HETATM 2136 C  C3  B RET C 3 .   ? -12.01707 9.61231  -11.47568 0.300 12.29214 ? 302 RET A C3  1 
HETATM 2137 C  C4  A RET C 3 .   ? -12.78215 9.24866  -9.82231  0.700 21.85790 ? 302 RET A C4  1 
HETATM 2138 C  C4  B RET C 3 .   ? -12.90872 9.62091  -10.25220 0.300 13.45803 ? 302 RET A C4  1 
HETATM 2139 C  C5  A RET C 3 .   ? -12.30124 10.24819 -8.79806  0.700 19.04314 ? 302 RET A C5  1 
HETATM 2140 C  C5  B RET C 3 .   ? -12.23499 10.17218 -9.01756  0.300 13.41159 ? 302 RET A C5  1 
HETATM 2141 C  C6  A RET C 3 .   ? -11.03121 10.69564 -8.75128  0.700 14.30191 ? 302 RET A C6  1 
HETATM 2142 C  C6  B RET C 3 .   ? -10.90787 10.38622 -8.93460  0.300 14.89764 ? 302 RET A C6  1 
HETATM 2143 C  C7  A RET C 3 .   ? -10.58923 11.45880 -7.59691  0.700 14.37273 ? 302 RET A C7  1 
HETATM 2144 C  C7  B RET C 3 .   ? -10.35548 11.05887 -7.77189  0.300 14.52798 ? 302 RET A C7  1 
HETATM 2145 C  C8  A RET C 3 .   ? -9.37138  11.85436 -7.20550  0.700 15.19659 ? 302 RET A C8  1 
HETATM 2146 C  C8  B RET C 3 .   ? -9.41562  12.03789 -7.64742  0.300 12.65825 ? 302 RET A C8  1 
HETATM 2147 C  C9  A RET C 3 .   ? -9.06506  12.65258 -6.05265  0.700 15.10129 ? 302 RET A C9  1 
HETATM 2148 C  C9  B RET C 3 .   ? -9.01731  12.64276 -6.39750  0.300 14.49323 ? 302 RET A C9  1 
HETATM 2149 C  C10 A RET C 3 .   ? -7.92226  13.36926 -6.05147  0.700 15.46578 ? 302 RET A C10 1 
HETATM 2150 C  C10 B RET C 3 .   ? -7.79189  13.21253 -6.27908  0.300 16.83635 ? 302 RET A C10 1 
HETATM 2151 C  C11 A RET C 3 .   ? -7.44970  14.25471 -5.03388  0.700 12.03943 ? 302 RET A C11 1 
HETATM 2152 C  C11 B RET C 3 .   ? -7.25480  13.88033 -5.12557  0.300 17.07383 ? 302 RET A C11 1 
HETATM 2153 C  C12 A RET C 3 .   ? -6.29487  14.89866 -5.08582  0.700 14.36070 ? 302 RET A C12 1 
HETATM 2154 C  C12 B RET C 3 .   ? -6.56955  15.04043 -5.16450  0.300 19.09740 ? 302 RET A C12 1 
HETATM 2155 C  C13 A RET C 3 .   ? -5.79323  15.79193 -4.07002  0.700 15.05927 ? 302 RET A C13 1 
HETATM 2156 C  C13 B RET C 3 .   ? -6.03125  15.78110 -4.03367  0.300 15.87000 ? 302 RET A C13 1 
HETATM 2157 C  C14 A RET C 3 .   ? -4.65774  16.48051 -4.28339  0.700 12.54929 ? 302 RET A C14 1 
HETATM 2158 C  C14 B RET C 3 .   ? -4.70066  16.04598 -3.97430  0.300 19.29298 ? 302 RET A C14 1 
HETATM 2159 C  C15 A RET C 3 .   ? -3.97032  17.29434 -3.33364  0.700 15.12214 ? 302 RET A C15 1 
HETATM 2160 C  C15 B RET C 3 .   ? -3.99731  16.73101 -2.92119  0.300 19.65325 ? 302 RET A C15 1 
HETATM 2161 C  C16 A RET C 3 .   ? -8.79490  9.69416  -9.41345  0.700 18.72528 ? 302 RET A C16 1 
HETATM 2162 C  C16 B RET C 3 .   ? -8.67242  9.39936  -9.56479  0.300 14.83254 ? 302 RET A C16 1 
HETATM 2163 C  C17 A RET C 3 .   ? -9.53422  11.81865 -10.51682 0.700 15.00610 ? 302 RET A C17 1 
HETATM 2164 C  C17 B RET C 3 .   ? -9.54365  11.37676 -10.82113 0.300 14.97375 ? 302 RET A C17 1 
HETATM 2165 C  C18 A RET C 3 .   ? -13.31028 10.48195 -7.70333  0.700 22.09330 ? 302 RET A C18 1 
HETATM 2166 C  C18 B RET C 3 .   ? -13.19937 10.43576 -7.89387  0.300 15.64859 ? 302 RET A C18 1 
HETATM 2167 C  C19 A RET C 3 .   ? -10.07412 12.71668 -4.93580  0.700 15.35619 ? 302 RET A C19 1 
HETATM 2168 C  C19 B RET C 3 .   ? -10.02387 12.65059 -5.28026  0.300 17.77170 ? 302 RET A C19 1 
HETATM 2169 C  C20 A RET C 3 .   ? -6.54700  15.88292 -2.77100  0.700 15.92012 ? 302 RET A C20 1 
HETATM 2170 C  C20 B RET C 3 .   ? -6.99318  16.23176 -2.96671  0.300 17.77018 ? 302 RET A C20 1 
HETATM 2171 C  C   A 97N D 4 .   ? -12.42822 23.69996 15.99019  0.700 37.48528 ? 303 97N A C   1 
HETATM 2172 O  O   A 97N D 4 .   ? -13.10662 21.19397 5.41792   0.700 32.65987 ? 303 97N A O   1 
HETATM 2173 C  C1  A 97N D 4 .   ? -13.02989 24.60364 14.92039  0.700 37.23014 ? 303 97N A C1  1 
HETATM 2174 O  O1  A 97N D 4 .   ? -11.13557 21.73167 4.54684   0.700 28.34549 ? 303 97N A O1  1 
HETATM 2175 C  C2  A 97N D 4 .   ? -13.72395 23.85037 13.79855  0.700 34.84922 ? 303 97N A C2  1 
HETATM 2176 O  O2  A 97N D 4 .   ? -9.44011  21.60245 2.29373   0.700 23.40196 ? 303 97N A O2  1 
HETATM 2177 C  C3  A 97N D 4 .   ? -14.79371 24.66741 13.07738  0.700 34.21822 ? 303 97N A C3  1 
HETATM 2178 O  O3  A 97N D 4 .   ? -11.10253 19.50932 0.92607   0.700 24.92745 ? 303 97N A O3  1 
HETATM 2179 C  C4  A 97N D 4 .   ? -15.26605 23.96679 11.81793  0.700 33.31679 ? 303 97N A C4  1 
HETATM 2180 C  C5  A 97N D 4 .   ? -16.22477 24.75975 10.91033  0.700 32.45823 ? 303 97N A C5  1 
HETATM 2181 C  C6  A 97N D 4 .   ? -16.07415 26.24917 10.92601  0.700 35.75787 ? 303 97N A C6  1 
HETATM 2182 C  C7  A 97N D 4 .   ? -15.72227 27.09711 9.94815   0.700 34.02679 ? 303 97N A C7  1 
HETATM 2183 C  C8  A 97N D 4 .   ? -15.33598 26.83144 8.52923   0.700 32.74206 ? 303 97N A C8  1 
HETATM 2184 C  C9  A 97N D 4 .   ? -13.82769 26.71001 8.35185   0.700 35.85933 ? 303 97N A C9  1 
HETATM 2185 C  C10 A 97N D 4 .   ? -13.42271 26.76865 6.88299   0.700 39.86347 ? 303 97N A C10 1 
HETATM 2186 C  C11 A 97N D 4 .   ? -14.08389 25.65952 6.09467   0.700 40.24781 ? 303 97N A C11 1 
HETATM 2187 C  C12 A 97N D 4 .   ? -13.58954 24.30430 6.57027   0.700 40.79629 ? 303 97N A C12 1 
HETATM 2188 C  C13 A 97N D 4 .   ? -12.11528 24.14069 6.28202   0.700 36.12654 ? 303 97N A C13 1 
HETATM 2189 C  C14 A 97N D 4 .   ? -11.65974 22.73070 6.58390   0.700 31.55813 ? 303 97N A C14 1 
HETATM 2190 C  C15 A 97N D 4 .   ? -12.06673 21.79998 5.48666   0.700 31.82406 ? 303 97N A C15 1 
HETATM 2191 C  C16 A 97N D 4 .   ? -11.43711 20.89412 3.41297   0.700 27.38635 ? 303 97N A C16 1 
HETATM 2192 C  C17 A 97N D 4 .   ? -10.83733 21.56951 2.19155   0.700 24.98483 ? 303 97N A C17 1 
HETATM 2193 C  C18 A 97N D 4 .   ? -11.28666 20.90254 0.91024   0.700 22.49316 ? 303 97N A C18 1 
HETATM 2194 C  C10 . OLC E 5 .   ? 2.48359   35.12913 12.22085  1.000 37.99111 ? 304 OLC A C10 1 
HETATM 2195 C  C9  . OLC E 5 .   ? 1.72799   34.63286 13.16472  1.000 38.52058 ? 304 OLC A C9  1 
HETATM 2196 C  C11 . OLC E 5 .   ? 2.03865   35.14379 10.79379  1.000 36.96865 ? 304 OLC A C11 1 
HETATM 2197 C  C8  . OLC E 5 .   ? 2.10850   34.43357 14.59605  1.000 40.42681 ? 304 OLC A C8  1 
HETATM 2198 C  C12 . OLC E 5 .   ? 3.03217   35.67537 9.81317   1.000 37.24180 ? 304 OLC A C12 1 
HETATM 2199 C  C7  . OLC E 5 .   ? 3.56454   34.61026 14.84962  1.000 42.30091 ? 304 OLC A C7  1 
HETATM 2200 C  C13 . OLC E 5 .   ? 2.75920   35.17060 8.40698   1.000 40.34960 ? 304 OLC A C13 1 
HETATM 2201 C  C6  . OLC E 5 .   ? 4.12606   33.57928 15.81087  1.000 43.23199 ? 304 OLC A C6  1 
HETATM 2202 C  C14 . OLC E 5 .   ? 2.88276   36.20131 7.32161   1.000 39.89193 ? 304 OLC A C14 1 
HETATM 2203 C  C5  . OLC E 5 .   ? 5.59472   33.68379 16.10335  1.000 44.31479 ? 304 OLC A C5  1 
HETATM 2204 C  C4  . OLC E 5 .   ? 5.98738   32.74896 17.20859  1.000 48.18899 ? 304 OLC A C4  1 
HETATM 2205 C  C3  . OLC E 5 .   ? 7.41698   32.84803 17.69259  1.000 49.46424 ? 304 OLC A C3  1 
HETATM 2206 C  C2  . OLC E 5 .   ? 7.59677   32.14912 19.00573  1.000 51.38719 ? 304 OLC A C2  1 
HETATM 2207 C  C1  . OLC E 5 .   ? 6.90742   32.84898 20.14546  1.000 55.34742 ? 304 OLC A C1  1 
HETATM 2208 O  O19 . OLC E 5 .   ? 6.36282   33.92257 20.07604  1.000 57.98523 ? 304 OLC A O19 1 
HETATM 2209 O  O20 . OLC E 5 .   ? 6.98090   32.14222 21.26793  1.000 58.44630 ? 304 OLC A O20 1 
HETATM 2210 C  C1  . LFA F 6 .   ? 13.70785  27.54115 -4.76112  1.000 41.15776 ? 305 LFA A C1  1 
HETATM 2211 C  C2  . LFA F 6 .   ? 12.83971  28.25912 -5.76415  1.000 40.75005 ? 305 LFA A C2  1 
HETATM 2212 C  C3  . LFA F 6 .   ? 12.62093  27.45250 -7.01664  1.000 40.56433 ? 305 LFA A C3  1 
HETATM 2213 C  C4  . LFA F 6 .   ? 11.85776  28.18802 -8.08385  1.000 40.79225 ? 305 LFA A C4  1 
HETATM 2214 C  C5  . LFA F 6 .   ? 11.87121  27.54681 -9.45062  1.000 40.19873 ? 305 LFA A C5  1 
HETATM 2215 C  C6  . LFA F 6 .   ? 11.25223  28.41019 -10.52175 1.000 40.62349 ? 305 LFA A C6  1 
HETATM 2216 C  C7  . LFA F 6 .   ? 11.43144  27.91418 -11.92999 1.000 42.28800 ? 305 LFA A C7  1 
HETATM 2217 C  C8  . LFA F 6 .   ? 11.03581  28.91617 -12.98317 1.000 43.12543 ? 305 LFA A C8  1 
HETATM 2218 C  C9  . LFA F 6 .   ? 11.08913  28.39757 -14.39788 1.000 45.28641 ? 305 LFA A C9  1 
HETATM 2219 C  C10 . LFA F 6 .   ? 10.89758  29.46642 -15.44270 1.000 48.50288 ? 305 LFA A C10 1 
HETATM 2220 C  C11 . LFA F 6 .   ? 9.88947   29.12964 -16.51285 1.000 50.19570 ? 305 LFA A C11 1 
HETATM 2221 C  C12 . LFA F 6 .   ? 8.52251   28.76241 -15.99198 1.000 53.68510 ? 305 LFA A C12 1 
HETATM 2222 C  C8  . LFA G 6 .   ? 12.23241  11.04026 -10.19600 1.000 54.69061 ? 306 LFA A C8  1 
HETATM 2223 C  C9  . LFA G 6 .   ? 11.45846  10.60595 -8.97228  1.000 54.88521 ? 306 LFA A C9  1 
HETATM 2224 C  C10 . LFA G 6 .   ? 9.95551   10.69355 -9.11844  1.000 53.82739 ? 306 LFA A C10 1 
HETATM 2225 C  C11 . LFA G 6 .   ? 9.18062   10.21930 -7.91013  1.000 51.55873 ? 306 LFA A C11 1 
HETATM 2226 C  C12 . LFA G 6 .   ? 7.68643   10.19248 -8.11314  1.000 48.91957 ? 306 LFA A C12 1 
HETATM 2227 C  C13 . LFA G 6 .   ? 6.89634   9.53491  -6.99738  1.000 48.36894 ? 306 LFA A C13 1 
HETATM 2228 C  C14 . LFA G 6 .   ? 7.37568   8.14941  -6.63171  1.000 51.46898 ? 306 LFA A C14 1 
HETATM 2229 C  C15 . LFA G 6 .   ? 6.32651   7.23780  -6.03804  1.000 49.46761 ? 306 LFA A C15 1 
HETATM 2230 C  C16 . LFA G 6 .   ? 5.36255   6.67121  -7.05249  1.000 47.83833 ? 306 LFA A C16 1 
HETATM 2231 C  C17 . LFA G 6 .   ? 4.68764   5.38717  -6.63110  1.000 49.03862 ? 306 LFA A C17 1 
HETATM 2232 C  C18 . LFA G 6 .   ? 3.83800   4.75763  -7.70802  1.000 49.60545 ? 306 LFA A C18 1 
HETATM 2233 C  C19 . LFA G 6 .   ? 3.18515   3.45046  -7.33822  1.000 50.11096 ? 306 LFA A C19 1 
HETATM 2234 C  C20 . LFA G 6 .   ? 2.20680   3.53451  -6.19123  1.000 52.68962 ? 306 LFA A C20 1 
HETATM 2235 C  C1  . LFA H 6 .   ? -13.59655 24.65210 -5.87871  1.000 35.41941 ? 307 LFA A C1  1 
HETATM 2236 C  C2  . LFA H 6 .   ? -12.64731 25.27776 -6.86236  1.000 31.72940 ? 307 LFA A C2  1 
HETATM 2237 C  C3  . LFA H 6 .   ? -12.68309 24.66581 -8.23955  1.000 35.92111 ? 307 LFA A C3  1 
HETATM 2238 C  C4  . LFA H 6 .   ? -12.54236 25.65935 -9.35661  1.000 34.82003 ? 307 LFA A C4  1 
HETATM 2239 C  C5  . LFA H 6 .   ? -12.66066 25.09109 -10.75510 1.000 36.51692 ? 307 LFA A C5  1 
HETATM 2240 C  C6  . LFA H 6 .   ? -12.34612 26.08699 -11.84740 1.000 43.44004 ? 307 LFA A C6  1 
HETATM 2241 C  C7  . LFA H 6 .   ? -12.68008 25.60469 -13.23961 1.000 45.24435 ? 307 LFA A C7  1 
HETATM 2242 C  C8  . LFA H 6 .   ? -12.00633 26.36838 -14.35078 1.000 45.98718 ? 307 LFA A C8  1 
HETATM 2243 C  C9  . LFA H 6 .   ? -12.07381 25.67374 -15.68927 1.000 46.63686 ? 307 LFA A C9  1 
HETATM 2244 C  C10 . LFA H 6 .   ? -11.25226 26.32616 -16.77249 1.000 48.64815 ? 307 LFA A C10 1 
HETATM 2245 C  C11 . LFA H 6 .   ? -11.94969 27.42203 -17.53573 1.000 48.63679 ? 307 LFA A C11 1 
HETATM 2246 C  C12 . LFA H 6 .   ? -12.53044 26.97990 -18.85246 1.000 46.74078 ? 307 LFA A C12 1 
HETATM 2247 C  C6  . LFA I 6 .   ? 9.56847   14.10427 -4.16247  1.000 47.62425 ? 308 LFA A C6  1 
HETATM 2248 C  C7  . LFA I 6 .   ? 8.74966   14.38135 -5.40691  1.000 46.67412 ? 308 LFA A C7  1 
HETATM 2249 C  C8  . LFA I 6 .   ? 7.46570   13.59651 -5.48895  1.000 42.45445 ? 308 LFA A C8  1 
HETATM 2250 C  C9  . LFA I 6 .   ? 6.76980   13.62401 -6.82896  1.000 38.95207 ? 308 LFA A C9  1 
HETATM 2251 C  C10 . LFA I 6 .   ? 6.31993   14.98775 -7.29427  1.000 35.04969 ? 308 LFA A C10 1 
HETATM 2252 C  C11 . LFA I 6 .   ? 5.35062   14.95112 -8.45434  1.000 34.69467 ? 308 LFA A C11 1 
HETATM 2253 C  C12 . LFA I 6 .   ? 5.91505   14.55273 -9.78656  1.000 35.86741 ? 308 LFA A C12 1 
HETATM 2254 C  C13 . LFA I 6 .   ? 6.94971   15.48450 -10.35331 1.000 38.15022 ? 308 LFA A C13 1 
HETATM 2255 C  C14 . LFA I 6 .   ? 7.61545   14.95720 -11.59794 1.000 44.01818 ? 308 LFA A C14 1 
HETATM 2256 C  C15 . LFA I 6 .   ? 8.22538   13.58345 -11.44472 1.000 47.12728 ? 308 LFA A C15 1 
HETATM 2257 C  C16 . LFA I 6 .   ? 8.75628   13.00002 -12.73284 1.000 48.16612 ? 308 LFA A C16 1 
HETATM 2258 C  C17 . LFA I 6 .   ? 7.68484   12.53985 -13.69164 1.000 45.69761 ? 308 LFA A C17 1 
HETATM 2259 C  C18 . LFA I 6 .   ? 8.10015   12.56381 -15.13875 1.000 44.42606 ? 308 LFA A C18 1 
HETATM 2260 C  C19 . LFA I 6 .   ? 7.08359   12.07949 -16.13866 1.000 42.59019 ? 308 LFA A C19 1 
HETATM 2261 C  C20 . LFA I 6 .   ? 7.45920   12.39023 -17.56841 1.000 43.48846 ? 308 LFA A C20 1 
HETATM 2262 C  C5  . LFA J 6 .   ? -8.03841  -2.08551 -9.21748  1.000 53.10481 ? 309 LFA A C5  1 
HETATM 2263 C  C6  . LFA J 6 .   ? -8.10586  -2.70992 -7.84167  1.000 53.16376 ? 309 LFA A C6  1 
HETATM 2264 C  C7  . LFA J 6 .   ? -9.38273  -2.42358 -7.08566  1.000 50.97355 ? 309 LFA A C7  1 
HETATM 2265 C  C8  . LFA J 6 .   ? -10.38005 -3.55836 -7.06711  1.000 51.91588 ? 309 LFA A C8  1 
HETATM 2266 C  C9  . LFA J 6 .   ? -9.95999  -4.74841 -6.23413  1.000 52.98685 ? 309 LFA A C9  1 
HETATM 2267 C  C10 . LFA J 6 .   ? -9.80024  -4.44841 -4.76310  1.000 54.01714 ? 309 LFA A C10 1 
HETATM 2268 C  C11 . LFA J 6 .   ? -11.08645 -4.09900 -4.04513  1.000 54.30249 ? 309 LFA A C11 1 
HETATM 2269 C  C12 . LFA J 6 .   ? -10.88580 -3.30256 -2.76927  1.000 52.71725 ? 309 LFA A C12 1 
HETATM 2270 C  C13 . LFA J 6 .   ? -11.17187 -4.03389 -1.48351  1.000 51.51980 ? 309 LFA A C13 1 
HETATM 2271 C  C14 . LFA J 6 .   ? -10.60313 -3.34868 -0.25922  1.000 47.98337 ? 309 LFA A C14 1 
HETATM 2272 C  C15 . LFA J 6 .   ? -10.88155 -1.86979 -0.19137  1.000 45.61233 ? 309 LFA A C15 1 
HETATM 2273 C  C16 . LFA J 6 .   ? -10.25465 -1.18408 0.99530   1.000 41.16299 ? 309 LFA A C16 1 
HETATM 2274 C  C17 . LFA J 6 .   ? -10.69340 -1.74498 2.32551   1.000 44.52725 ? 309 LFA A C17 1 
HETATM 2275 C  C18 . LFA J 6 .   ? -12.18101 -1.63778 2.57812   1.000 46.66676 ? 309 LFA A C18 1 
HETATM 2276 C  C19 . LFA J 6 .   ? -12.74120 -2.40548 3.75187   1.000 48.50709 ? 309 LFA A C19 1 
HETATM 2277 C  C20 . LFA J 6 .   ? -12.35437 -1.92982 5.12850   1.000 46.99454 ? 309 LFA A C20 1 
HETATM 2278 C  C1  . LFA K 6 .   ? -20.08531 9.26146  2.72455   1.000 43.20068 ? 310 LFA A C1  1 
HETATM 2279 C  C2  . LFA K 6 .   ? -21.16071 9.94332  3.54384   1.000 41.88664 ? 310 LFA A C2  1 
HETATM 2280 C  C3  . LFA K 6 .   ? -21.59179 9.15398  4.75626   1.000 46.26654 ? 310 LFA A C3  1 
HETATM 2281 C  C4  . LFA K 6 .   ? -22.81583 9.67351  5.47435   1.000 44.92561 ? 310 LFA A C4  1 
HETATM 2282 C  C5  . LFA K 6 .   ? -23.34868 8.74867  6.54729   1.000 44.21459 ? 310 LFA A C5  1 
HETATM 2283 C  C16 . LFA L 6 .   ? 8.40191   24.34552 2.98273   1.000 44.52810 ? 311 LFA A C16 1 
HETATM 2284 C  C17 . LFA L 6 .   ? 7.56296   24.03216 1.76258   1.000 43.00172 ? 311 LFA A C17 1 
HETATM 2285 C  C18 . LFA L 6 .   ? 7.37051   25.19262 0.81807   1.000 43.06205 ? 311 LFA A C18 1 
HETATM 2286 C  C19 . LFA L 6 .   ? 6.42465   24.94919 -0.34011  1.000 35.75695 ? 311 LFA A C19 1 
HETATM 2287 C  C20 . LFA L 6 .   ? 6.24274   26.17751 -1.21916  1.000 33.49796 ? 311 LFA A C20 1 
HETATM 2288 C  C15 . LFA M 6 .   ? 12.01876  19.00102 -16.34858 1.000 39.20013 ? 312 LFA A C15 1 
HETATM 2289 C  C16 . LFA M 6 .   ? 12.52459  18.76990 -14.94967 1.000 39.03573 ? 312 LFA A C16 1 
HETATM 2290 C  C17 . LFA M 6 .   ? 11.96708  19.73649 -13.93921 1.000 36.21094 ? 312 LFA A C17 1 
HETATM 2291 C  C18 . LFA M 6 .   ? 12.17914  19.33044 -12.50185 1.000 39.62728 ? 312 LFA A C18 1 
HETATM 2292 C  C19 . LFA M 6 .   ? 11.76273  20.39326 -11.51863 1.000 38.63178 ? 312 LFA A C19 1 
HETATM 2293 C  C20 . LFA M 6 .   ? 11.88121  20.01037 -10.06229 1.000 37.81398 ? 312 LFA A C20 1 
HETATM 2294 C  C1  . LFA N 6 .   ? -14.69214 27.86721 0.31888   1.000 48.81859 ? 313 LFA A C1  1 
HETATM 2295 C  C2  . LFA N 6 .   ? -15.17352 28.12101 -1.08743  1.000 45.52930 ? 313 LFA A C2  1 
HETATM 2296 C  C3  . LFA N 6 .   ? -14.09983 27.95656 -2.12863  1.000 46.07883 ? 313 LFA A C3  1 
HETATM 2297 C  C4  . LFA N 6 .   ? -14.43046 28.47655 -3.50597  1.000 45.37611 ? 313 LFA A C4  1 
HETATM 2298 C  C5  . LFA N 6 .   ? -13.27563 28.36458 -4.47165  1.000 46.65664 ? 313 LFA A C5  1 
HETATM 2299 C  C6  . LFA N 6 .   ? -11.92889 28.47663 -3.78894  1.000 51.32563 ? 313 LFA A C6  1 
HETATM 2300 C  C7  . LFA N 6 .   ? -11.02066 29.56908 -4.29222  1.000 51.68162 ? 313 LFA A C7  1 
HETATM 2301 C  C8  . LFA N 6 .   ? -10.50307 29.35891 -5.68648  1.000 50.12814 ? 313 LFA A C8  1 
HETATM 2302 C  C9  . LFA N 6 .   ? -9.63327  30.48113 -6.18673  1.000 52.87173 ? 313 LFA A C9  1 
HETATM 2303 C  C10 . LFA N 6 .   ? -9.53147  30.54473 -7.68628  1.000 51.89439 ? 313 LFA A C10 1 
HETATM 2304 C  C11 . LFA N 6 .   ? -10.85939 30.69042 -8.38920  1.000 49.22233 ? 313 LFA A C11 1 
HETATM 2305 C  C12 . LFA N 6 .   ? -10.78006 30.44127 -9.87307  1.000 50.76978 ? 313 LFA A C12 1 
HETATM 2306 C  C13 . LFA N 6 .   ? -9.76619  31.30261 -10.56504 1.000 50.23109 ? 313 LFA A C13 1 
HETATM 2307 C  C14 . LFA N 6 .   ? -9.47389  30.92204 -11.98982 1.000 48.80482 ? 313 LFA A C14 1 
HETATM 2308 C  C15 . LFA N 6 .   ? -8.64946  31.94876 -12.71543 1.000 49.88149 ? 313 LFA A C15 1 
HETATM 2309 C  C16 . LFA N 6 .   ? -8.08310  31.48394 -14.02709 1.000 46.87792 ? 313 LFA A C16 1 
HETATM 2310 C  C17 . LFA N 6 .   ? -9.11655  31.04430 -15.02536 1.000 48.24503 ? 313 LFA A C17 1 
HETATM 2311 C  C18 . LFA N 6 .   ? -8.53309  30.58442 -16.33583 1.000 49.06160 ? 313 LFA A C18 1 
HETATM 2312 C  C19 . LFA N 6 .   ? -9.57033  30.40891 -17.40930 1.000 48.48563 ? 313 LFA A C19 1 
HETATM 2313 C  C20 . LFA N 6 .   ? -10.39246 31.66655 -17.59772 1.000 50.48346 ? 313 LFA A C20 1 
HETATM 2314 C  C16 . LFA O 6 .   ? 10.71231  22.35218 11.78214  1.000 53.33812 ? 314 LFA A C16 1 
HETATM 2315 C  C17 . LFA O 6 .   ? 9.74992   22.74543 12.87333  1.000 54.84442 ? 314 LFA A C17 1 
HETATM 2316 C  C18 . LFA O 6 .   ? 10.36227  22.80204 14.25024  1.000 55.99266 ? 314 LFA A C18 1 
HETATM 2317 C  C19 . LFA O 6 .   ? 9.40645   23.27250 15.31333  1.000 55.46005 ? 314 LFA A C19 1 
HETATM 2318 C  C20 . LFA O 6 .   ? 8.17298   22.40786 15.45037  1.000 54.57487 ? 314 LFA A C20 1 
HETATM 2319 C  C1  . GOL P 7 .   ? -0.01948  -1.15729 -15.60432 0.500 49.73495 ? 315 GOL A C1  1 
HETATM 2320 O  O1  . GOL P 7 .   ? -1.37478  -0.92974 -15.84169 0.500 51.02248 ? 315 GOL A O1  1 
HETATM 2321 C  C2  . GOL P 7 .   ? 0.54031   0.10226  -14.91963 0.500 49.04624 ? 315 GOL A C2  1 
HETATM 2322 O  O2  . GOL P 7 .   ? 0.03740   0.26437  -13.63192 0.500 51.43827 ? 315 GOL A O2  1 
HETATM 2323 C  C3  . GOL P 7 .   ? 0.11933   1.25186  -15.84693 0.500 47.01597 ? 315 GOL A C3  1 
HETATM 2324 O  O3  . GOL P 7 .   ? 1.27041   1.83880  -16.37762 0.500 44.59968 ? 315 GOL A O3  1 
HETATM 2325 C  C1  . GOL Q 7 .   ? -10.84267 22.96101 20.77180  1.000 66.87064 ? 316 GOL A C1  1 
HETATM 2326 O  O1  . GOL Q 7 .   ? -11.50330 22.99508 19.53840  1.000 68.32246 ? 316 GOL A O1  1 
HETATM 2327 C  C2  . GOL Q 7 .   ? -11.07218 21.56095 21.41180  1.000 64.23477 ? 316 GOL A C2  1 
HETATM 2328 O  O2  . GOL Q 7 .   ? -11.44980 20.59290 20.47742  1.000 57.36061 ? 316 GOL A O2  1 
HETATM 2329 C  C3  . GOL Q 7 .   ? -9.73329  21.21675 22.11783  1.000 64.84092 ? 316 GOL A C3  1 
HETATM 2330 O  O3  . GOL Q 7 .   ? -9.95497  20.09924 22.93541  1.000 64.26783 ? 316 GOL A O3  1 
HETATM 2331 C  C1  . GOL R 7 .   ? 1.76847   7.31648  -19.90346 1.000 62.74111 ? 317 GOL A C1  1 
HETATM 2332 O  O1  . GOL R 7 .   ? 2.80452   7.85541  -20.67735 1.000 62.86307 ? 317 GOL A O1  1 
HETATM 2333 C  C2  . GOL R 7 .   ? 2.42919   6.57075  -18.70574 1.000 63.40656 ? 317 GOL A C2  1 
HETATM 2334 O  O2  . GOL R 7 .   ? 3.78760   6.87817  -18.59336 1.000 64.09456 ? 317 GOL A O2  1 
HETATM 2335 C  C3  . GOL R 7 .   ? 2.16946   5.05167  -18.97456 1.000 63.44358 ? 317 GOL A C3  1 
HETATM 2336 O  O3  . GOL R 7 .   ? 2.07290   4.40092  -17.72645 1.000 61.59669 ? 317 GOL A O3  1 
HETATM 2337 C  C24 . OLC S 5 .   ? 2.04025   10.01636 10.11076  0.700 36.16589 ? 318 OLC A C24 1 
HETATM 2338 C  C4  . OLC S 5 .   ? -1.53775  3.86234  9.56769   0.700 36.68668 ? 318 OLC A C4  1 
HETATM 2339 C  C3  . OLC S 5 .   ? -0.61346  4.45686  10.61801  0.700 36.91443 ? 318 OLC A C3  1 
HETATM 2340 C  C2  . OLC S 5 .   ? -0.12206  5.80672  10.23003  0.700 38.11171 ? 318 OLC A C2  1 
HETATM 2341 C  C21 . OLC S 5 .   ? 2.82092   7.83768  11.07030  0.700 41.26289 ? 318 OLC A C21 1 
HETATM 2342 C  C1  . OLC S 5 .   ? 1.10726   6.23364  10.97020  0.700 40.92377 ? 318 OLC A C1  1 
HETATM 2343 C  C22 . OLC S 5 .   ? 3.21700   9.09719  10.33984  0.700 41.14466 ? 318 OLC A C22 1 
HETATM 2344 O  O19 . OLC S 5 .   ? 1.60347   5.66837  11.90542  0.700 41.81175 ? 318 OLC A O19 1 
HETATM 2345 O  O25 . OLC S 5 .   ? 1.46153   10.40115 11.35192  0.700 28.25288 ? 318 OLC A O25 1 
HETATM 2346 O  O23 . OLC S 5 .   ? 4.21553   9.77726  11.09786  0.700 45.56717 ? 318 OLC A O23 1 
HETATM 2347 O  O20 . OLC S 5 .   ? 1.61803   7.33959  10.44666  0.700 44.56059 ? 318 OLC A O20 1 
HETATM 2348 C  C10 . OLC T 5 .   ? 2.27926   40.73803 1.57460   1.000 48.33870 ? 319 OLC A C10 1 
HETATM 2349 C  C9  . OLC T 5 .   ? 1.42745   40.28805 0.67814   1.000 47.07627 ? 319 OLC A C9  1 
HETATM 2350 C  C11 . OLC T 5 .   ? 2.61874   42.16193 1.89626   1.000 47.03836 ? 319 OLC A C11 1 
HETATM 2351 C  C8  . OLC T 5 .   ? 1.18237   38.82932 0.43962   1.000 48.19749 ? 319 OLC A C8  1 
HETATM 2352 C  C24 . OLC T 5 .   ? -5.33943  39.36475 -9.99241  1.000 64.93900 ? 319 OLC A C24 1 
HETATM 2353 C  C7  . OLC T 5 .   ? 0.21427   38.52989 -0.65754  1.000 51.01144 ? 319 OLC A C7  1 
HETATM 2354 C  C6  . OLC T 5 .   ? -1.18202  39.09647 -0.44246  1.000 52.57222 ? 319 OLC A C6  1 
HETATM 2355 C  C5  . OLC T 5 .   ? -1.56760  40.16992 -1.42989  1.000 53.39948 ? 319 OLC A C5  1 
HETATM 2356 C  C4  . OLC T 5 .   ? -1.74817  39.68687 -2.84873  1.000 53.27100 ? 319 OLC A C4  1 
HETATM 2357 C  C3  . OLC T 5 .   ? -1.83003  40.81971 -3.85350  1.000 55.56375 ? 319 OLC A C3  1 
HETATM 2358 C  C2  . OLC T 5 .   ? -3.03293  40.74634 -4.73509  1.000 59.23182 ? 319 OLC A C2  1 
HETATM 2359 C  C21 . OLC T 5 .   ? -3.65317  39.39033 -8.09958  1.000 64.53609 ? 319 OLC A C21 1 
HETATM 2360 C  C1  . OLC T 5 .   ? -2.85226  39.86373 -5.93488  1.000 62.34515 ? 319 OLC A C1  1 
HETATM 2361 C  C22 . OLC T 5 .   ? -4.30498  40.16148 -9.22695  1.000 65.12964 ? 319 OLC A C22 1 
HETATM 2362 O  O19 . OLC T 5 .   ? -2.01091  39.01453 -6.05751  1.000 63.04602 ? 319 OLC A O19 1 
HETATM 2363 O  O25 . OLC T 5 .   ? -5.64608  39.97525 -11.24295 1.000 65.81285 ? 319 OLC A O25 1 
HETATM 2364 O  O23 . OLC T 5 .   ? -4.85519  41.38745 -8.74602  1.000 66.50616 ? 319 OLC A O23 1 
HETATM 2365 O  O20 . OLC T 5 .   ? -3.71694  40.17844 -6.89345  1.000 64.66033 ? 319 OLC A O20 1 
HETATM 2366 C  C7  . OLC U 5 .   ? -6.69044  35.62639 10.62054  1.000 54.81925 ? 320 OLC A C7  1 
HETATM 2367 C  C6  . OLC U 5 .   ? -7.42251  36.26519 11.79278  1.000 54.48461 ? 320 OLC A C6  1 
HETATM 2368 C  C5  . OLC U 5 .   ? -8.22375  35.29614 12.62365  1.000 54.71504 ? 320 OLC A C5  1 
HETATM 2369 C  C4  . OLC U 5 .   ? -7.42573  34.56067 13.66488  1.000 52.91801 ? 320 OLC A C4  1 
HETATM 2370 C  C3  . OLC U 5 .   ? -7.18506  35.34492 14.94282  1.000 53.97940 ? 320 OLC A C3  1 
HETATM 2371 C  C2  . OLC U 5 .   ? -8.02716  34.85111 16.07827  1.000 56.54481 ? 320 OLC A C2  1 
HETATM 2372 C  C1  . OLC U 5 .   ? -7.79004  35.58995 17.36406  1.000 60.69810 ? 320 OLC A C1  1 
HETATM 2373 O  O19 . OLC U 5 .   ? -7.00628  36.49212 17.50904  1.000 63.87268 ? 320 OLC A O19 1 
HETATM 2374 O  O20 . OLC U 5 .   ? -8.56012  35.12625 18.34433  1.000 62.05175 ? 320 OLC A O20 1 
HETATM 2375 C  C10 . OLC V 5 .   ? -16.21070 -3.31212 1.10306   1.000 53.58529 ? 321 OLC A C10 1 
HETATM 2376 C  C9  . OLC V 5 .   ? -17.20680 -2.50509 1.36996   1.000 55.49174 ? 321 OLC A C9  1 
HETATM 2377 C  C11 . OLC V 5 .   ? -15.30823 -3.22581 -0.08695  1.000 53.73791 ? 321 OLC A C11 1 
HETATM 2378 C  C8  . OLC V 5 .   ? -18.17366 -2.65050 2.50422   1.000 55.58538 ? 321 OLC A C8  1 
HETATM 2379 C  C12 . OLC V 5 .   ? -16.02274 -3.48855 -1.37612  1.000 54.37973 ? 321 OLC A C12 1 
HETATM 2380 C  C7  . OLC V 5 .   ? -18.23126 -1.48260 3.44234   1.000 54.88704 ? 321 OLC A C7  1 
HETATM 2381 C  C6  . OLC V 5 .   ? -17.27725 -1.56912 4.62708   1.000 53.35873 ? 321 OLC A C6  1 
HETATM 2382 C  C5  . OLC V 5 .   ? -17.81633 -0.92336 5.88202   1.000 54.60261 ? 321 OLC A C5  1 
HETATM 2383 C  C4  . OLC V 5 .   ? -16.89943 -0.98192 7.08055   1.000 55.51444 ? 321 OLC A C4  1 
HETATM 2384 C  C3  . OLC V 5 .   ? -17.47402 -0.29356 8.30892   1.000 57.74928 ? 321 OLC A C3  1 
HETATM 2385 C  C2  . OLC V 5 .   ? -16.50375 -0.21036 9.44972   1.000 59.11666 ? 321 OLC A C2  1 
HETATM 2386 C  C21 . OLC V 5 .   ? -16.34304 2.20667  12.24850  1.000 61.66782 ? 321 OLC A C21 1 
HETATM 2387 C  C1  . OLC V 5 .   ? -16.99636 0.65887  10.57343  1.000 60.88141 ? 321 OLC A C1  1 
HETATM 2388 C  C22 . OLC V 5 .   ? -16.62845 1.40292  13.49724  1.000 61.64811 ? 321 OLC A C22 1 
HETATM 2389 O  O19 . OLC V 5 .   ? -18.15182 0.77545  10.88869  1.000 62.53150 ? 321 OLC A O19 1 
HETATM 2390 O  O20 . OLC V 5 .   ? -15.99788 1.31064  11.16776  1.000 63.22130 ? 321 OLC A O20 1 
HETATM 2391 C  C10 . OLC W 5 .   ? -0.71784  -2.86191 -11.55619 1.000 44.87276 ? 322 OLC A C10 1 
HETATM 2392 C  C9  . OLC W 5 .   ? -1.75962  -2.25170 -12.03667 1.000 48.12863 ? 322 OLC A C9  1 
HETATM 2393 C  C11 . OLC W 5 .   ? -0.75592  -4.24707 -10.99198 1.000 44.26938 ? 322 OLC A C11 1 
HETATM 2394 C  C8  . OLC W 5 .   ? -3.12440  -2.86219 -12.06298 1.000 50.58093 ? 322 OLC A C8  1 
HETATM 2395 C  C12 . OLC W 5 .   ? 0.11494   -4.38801 -9.79467  1.000 41.88645 ? 322 OLC A C12 1 
HETATM 2396 C  C7  . OLC W 5 .   ? -3.53432  -3.25622 -13.44004 1.000 54.38953 ? 322 OLC A C7  1 
HETATM 2397 C  C13 . OLC W 5 .   ? 0.39085   -5.81861 -9.38919  1.000 37.03403 ? 322 OLC A C13 1 
HETATM 2398 C  C6  . OLC W 5 .   ? -4.94460  -3.81567 -13.55165 1.000 55.91037 ? 322 OLC A C6  1 
HETATM 2399 C  C14 . OLC W 5 .   ? 1.60106   -5.93727 -8.51098  1.000 33.27152 ? 322 OLC A C14 1 
HETATM 2400 C  C5  . OLC W 5 .   ? -5.30457  -4.20880 -14.95568 1.000 57.09631 ? 322 OLC A C5  1 
HETATM 2401 C  C4  . OLC W 5 .   ? -5.20699  -3.07513 -15.94170 1.000 58.90986 ? 322 OLC A C4  1 
HETATM 2402 C  C3  . OLC W 5 .   ? -5.17740  -3.51589 -17.39481 1.000 60.52194 ? 322 OLC A C3  1 
HETATM 2403 C  C2  . OLC W 5 .   ? -6.15129  -2.76230 -18.24167 1.000 62.78594 ? 322 OLC A C2  1 
HETATM 2404 C  C1  . OLC W 5 .   ? -7.57817  -3.18134 -18.02059 1.000 65.13126 ? 322 OLC A C1  1 
HETATM 2405 O  O19 . OLC W 5 .   ? -8.13485  -3.23660 -16.95280 1.000 66.98456 ? 322 OLC A O19 1 
HETATM 2406 O  O20 . OLC W 5 .   ? -8.17519  -3.48331 -19.16945 1.000 66.07315 ? 322 OLC A O20 1 
HETATM 2407 O  O   . HOH X 8 .   ? -2.22060  24.70047 -4.42713  1.000 20.01852 ? 401 HOH A O   1 
HETATM 2408 O  O   . HOH X 8 .   ? -6.33061  15.11033 -21.51644 1.000 26.94642 ? 402 HOH A O   1 
HETATM 2409 O  O   . HOH X 8 .   ? -10.32170 14.00784 -20.49915 1.000 41.63591 ? 403 HOH A O   1 
HETATM 2410 O  O   B HOH X 8 .   ? -3.03129  20.91856 3.60406   0.300 30.18727 ? 404 HOH A O   1 
HETATM 2411 O  O   . HOH X 8 .   ? -2.75840  11.20278 23.10346  1.000 25.85612 ? 405 HOH A O   1 
HETATM 2412 O  O   . HOH X 8 .   ? -13.97325 3.03606  16.84934  1.000 47.72273 ? 406 HOH A O   1 
HETATM 2413 O  O   A HOH X 8 .   ? -1.63879  17.99738 -5.88011  0.700 17.60513 ? 407 HOH A O   1 
HETATM 2414 O  O   B HOH X 8 .   ? -1.20084  18.87748 -5.78656  0.300 14.82225 ? 407 HOH A O   1 
HETATM 2415 O  O   . HOH X 8 .   ? -9.52394  17.21556 21.68938  1.000 27.31725 ? 408 HOH A O   1 
HETATM 2416 O  O   . HOH X 8 .   ? 1.04317   23.87410 4.93757   1.000 20.59232 ? 409 HOH A O   1 
HETATM 2417 O  O   . HOH X 8 .   ? -6.58578  25.83253 24.23194  1.000 55.48736 ? 410 HOH A O   1 
HETATM 2418 O  O   . HOH X 8 .   ? -6.41979  11.07507 24.74072  1.000 43.26893 ? 411 HOH A O   1 
HETATM 2419 O  O   . HOH X 8 .   ? -3.50736  31.70333 -25.22610 1.000 54.53563 ? 412 HOH A O   1 
HETATM 2420 O  O   . HOH X 8 .   ? -3.22767  26.45966 22.41056  1.000 24.22454 ? 413 HOH A O   1 
HETATM 2421 O  O   . HOH X 8 .   ? 9.68969   17.75946 -18.19083 1.000 57.78651 ? 414 HOH A O   1 
HETATM 2422 O  O   . HOH X 8 .   ? -13.44157 11.39846 16.36837  1.000 28.19383 ? 415 HOH A O   1 
HETATM 2423 O  O   . HOH X 8 .   ? -0.01909  4.96477  22.09068  1.000 35.15989 ? 416 HOH A O   1 
HETATM 2424 O  O   . HOH X 8 .   ? 4.24678   3.49368  18.02209  1.000 46.16997 ? 417 HOH A O   1 
HETATM 2425 O  O   . HOH X 8 .   ? -3.45790  28.93726 28.42160  1.000 51.20264 ? 418 HOH A O   1 
HETATM 2426 O  O   . HOH X 8 .   ? 2.05169   12.17141 18.87920  1.000 20.87257 ? 419 HOH A O   1 
HETATM 2427 O  O   . HOH X 8 .   ? -17.56909 17.85180 18.01581  1.000 33.19145 ? 420 HOH A O   1 
HETATM 2428 O  O   . HOH X 8 .   ? 9.44555   37.47058 11.16928  1.000 18.91930 ? 421 HOH A O   1 
HETATM 2429 O  O   . HOH X 8 .   ? -15.57018 13.00590 -20.97094 1.000 53.03485 ? 422 HOH A O   1 
HETATM 2430 O  O   . HOH X 8 .   ? -24.26143 13.52355 7.70673   1.000 27.55717 ? 423 HOH A O   1 
HETATM 2431 O  O   . HOH X 8 .   ? -7.09858  12.40132 -13.69991 1.000 19.75830 ? 424 HOH A O   1 
HETATM 2432 O  O   . HOH X 8 .   ? -10.02448 6.56995  -20.08632 1.000 30.96094 ? 425 HOH A O   1 
HETATM 2433 O  O   . HOH X 8 .   ? 10.29301  22.25361 -21.04318 1.000 51.56844 ? 426 HOH A O   1 
HETATM 2434 O  O   . HOH X 8 .   ? -6.92179  -0.82977 18.72712  1.000 39.46290 ? 427 HOH A O   1 
HETATM 2435 O  O   . HOH X 8 .   ? -17.87057 17.35195 20.77238  1.000 58.58512 ? 428 HOH A O   1 
HETATM 2436 O  O   . HOH X 8 .   ? -9.11195  12.18929 -18.03896 1.000 24.69894 ? 429 HOH A O   1 
HETATM 2437 O  O   . HOH X 8 .   ? -10.21038 9.22103  20.48036  1.000 34.64200 ? 430 HOH A O   1 
HETATM 2438 O  O   . HOH X 8 .   ? 7.40212   28.59384 20.39802  1.000 55.45701 ? 431 HOH A O   1 
HETATM 2439 O  O   . HOH X 8 .   ? -17.99962 9.44655  16.91812  1.000 65.06165 ? 432 HOH A O   1 
HETATM 2440 O  O   . HOH X 8 .   ? -12.63762 7.69937  17.08876  1.000 49.94680 ? 433 HOH A O   1 
HETATM 2441 O  O   . HOH X 8 .   ? 3.23430   23.83845 -1.96108  1.000 18.88786 ? 434 HOH A O   1 
HETATM 2442 O  O   . HOH X 8 .   ? -3.40494  17.50389 21.27060  1.000 19.20943 ? 435 HOH A O   1 
HETATM 2443 O  O   A HOH X 8 .   ? 7.02346   17.71595 -22.46204 0.700 48.49141 ? 436 HOH A O   1 
HETATM 2444 O  O   . HOH X 8 .   ? -6.73269  17.16474 21.80796  1.000 27.87301 ? 437 HOH A O   1 
HETATM 2445 O  O   . HOH X 8 .   ? -7.62683  5.96495  22.70124  1.000 35.75584 ? 438 HOH A O   1 
HETATM 2446 O  O   . HOH X 8 .   ? 2.31278   25.53810 16.89311  1.000 22.17145 ? 439 HOH A O   1 
HETATM 2447 O  O   A HOH X 8 .   ? -3.11614  13.64606 24.57177  0.700 45.47365 ? 440 HOH A O   1 
HETATM 2448 O  O   . HOH X 8 .   ? -10.35933 7.93918  -1.72332  1.000 17.60236 ? 441 HOH A O   1 
HETATM 2449 O  O   . HOH X 8 .   ? -6.77826  7.71838  -27.09087 1.000 54.41434 ? 442 HOH A O   1 
HETATM 2450 O  O   . HOH X 8 .   ? -5.01767  19.07357 3.19773   1.000 25.74641 ? 443 HOH A O   1 
HETATM 2451 O  O   . HOH X 8 .   ? 0.13233   10.87676 -22.01392 1.000 50.29369 ? 444 HOH A O   1 
HETATM 2452 O  O   . HOH X 8 .   ? -21.24758 10.69484 12.96452  1.000 26.95032 ? 445 HOH A O   1 
HETATM 2453 O  O   . HOH X 8 .   ? -26.12789 12.33907 9.50230   1.000 38.52380 ? 446 HOH A O   1 
HETATM 2454 O  O   . HOH X 8 .   ? -2.71323  18.05667 -9.10219  1.000 19.42753 ? 447 HOH A O   1 
HETATM 2455 O  O   . HOH X 8 .   ? -0.23517  17.14232 -8.84141  1.000 21.26452 ? 448 HOH A O   1 
HETATM 2456 O  O   . HOH X 8 .   ? -18.56291 8.29994  13.71836  1.000 38.47546 ? 449 HOH A O   1 
HETATM 2457 O  O   . HOH X 8 .   ? -4.10635  9.70913  26.43923  1.000 53.93476 ? 450 HOH A O   1 
HETATM 2458 O  O   . HOH X 8 .   ? 0.00000   -0.00000 18.69434  0.500 25.07156 ? 451 HOH A O   1 
HETATM 2459 O  O   . HOH X 8 .   ? -9.52272  1.10040  15.64384  1.000 28.93275 ? 452 HOH A O   1 
HETATM 2460 O  O   . HOH X 8 .   ? -27.22901 16.73876 13.94081  1.000 53.76822 ? 453 HOH A O   1 
HETATM 2461 O  O   . HOH X 8 .   ? -3.14138  4.24224  21.49267  1.000 24.98804 ? 454 HOH A O   1 
HETATM 2462 O  O   . HOH X 8 .   ? -7.41965  27.93605 24.07377  1.000 38.39885 ? 455 HOH A O   1 
HETATM 2463 O  O   . HOH X 8 .   ? -1.04072  23.54971 1.84516   1.000 21.92266 ? 456 HOH A O   1 
HETATM 2464 O  O   . HOH X 8 .   ? -1.31206  6.07311  -1.71031  1.000 23.91082 ? 457 HOH A O   1 
HETATM 2465 O  O   . HOH X 8 .   ? 3.28535   15.25920 12.53516  1.000 24.20664 ? 458 HOH A O   1 
HETATM 2466 O  O   . HOH X 8 .   ? -9.39945  30.61099 22.14366  1.000 63.45151 ? 459 HOH A O   1 
HETATM 2467 O  O   A HOH X 8 .   ? -3.38096  -5.51598 14.42626  0.500 26.79168 ? 460 HOH A O   1 
HETATM 2468 O  O   . HOH X 8 .   ? -5.56151  31.69828 23.64183  1.000 53.56929 ? 461 HOH A O   1 
HETATM 2469 O  O   . HOH X 8 .   ? -2.55371  16.58585 23.82064  1.000 27.30777 ? 462 HOH A O   1 
HETATM 2470 O  O   . HOH X 8 .   ? 3.72356   26.86917 -23.16993 1.000 65.16560 ? 463 HOH A O   1 
HETATM 2471 O  O   . HOH X 8 .   ? -14.93547 17.66528 21.84875  1.000 51.96845 ? 464 HOH A O   1 
HETATM 2472 O  O   . HOH X 8 .   ? -3.73153  6.25073  -0.25163  1.000 19.14785 ? 465 HOH A O   1 
HETATM 2473 O  O   . HOH X 8 .   ? -0.77097  20.86358 2.32375   1.000 23.12152 ? 466 HOH A O   1 
HETATM 2474 O  O   . HOH X 8 .   ? -8.62755  18.26273 1.50314   1.000 16.31161 ? 467 HOH A O   1 
HETATM 2475 O  O   . HOH X 8 .   ? -27.09399 15.50865 16.31840  1.000 55.88916 ? 468 HOH A O   1 
HETATM 2476 O  O   . HOH X 8 .   ? 2.39463   1.84523  21.53582  1.000 56.36762 ? 469 HOH A O   1 
HETATM 2477 O  O   . HOH X 8 .   ? -20.78743 5.65348  13.54036  1.000 55.93307 ? 470 HOH A O   1 
HETATM 2478 O  O   . HOH X 8 .   ? -14.62610 20.87501 19.33323  1.000 51.55656 ? 471 HOH A O   1 
HETATM 2479 O  O   . HOH X 8 .   ? 5.00447   3.00424  22.30272  1.000 57.84905 ? 472 HOH A O   1 
HETATM 2480 O  O   . HOH X 8 .   ? -3.96087  -1.15048 18.74323  1.000 53.53531 ? 473 HOH A O   1 
HETATM 2481 O  O   . HOH X 8 .   ? -14.20630 11.78331 23.65862  1.000 63.28510 ? 474 HOH A O   1 
HETATM 2482 O  O   . HOH X 8 .   ? -7.52212  20.94779 -24.21153 1.000 21.56703 ? 475 HOH A O   1 
HETATM 2483 O  O   . HOH X 8 .   ? -5.54685  -0.98267 14.58956  1.000 23.72540 ? 476 HOH A O   1 
HETATM 2484 O  O   . HOH X 8 .   ? 4.73200   14.27851 16.90830  1.000 53.99455 ? 477 HOH A O   1 
HETATM 2485 O  O   . HOH X 8 .   ? 6.38144   28.24123 -18.26581 1.000 62.97618 ? 478 HOH A O   1 
HETATM 2486 O  O   . HOH X 8 .   ? -8.21843  17.38513 4.04690   1.000 49.14751 ? 479 HOH A O   1 
HETATM 2487 O  O   . HOH X 8 .   ? -5.36277  28.99401 -22.75102 1.000 40.86633 ? 480 HOH A O   1 
HETATM 2488 O  O   . HOH X 8 .   ? -21.03342 21.97968 15.90245  1.000 28.41357 ? 481 HOH A O   1 
HETATM 2489 O  O   . HOH X 8 .   ? -24.03682 8.55516  12.58098  1.000 61.07461 ? 482 HOH A O   1 
HETATM 2490 O  O   . HOH X 8 .   ? -9.59142  27.13393 -21.36605 1.000 57.12154 ? 483 HOH A O   1 
HETATM 2491 O  O   . HOH X 8 .   ? -6.22387  17.23705 5.09346   1.000 35.11772 ? 484 HOH A O   1 
HETATM 2492 O  O   . HOH X 8 .   ? -12.05604 -0.42177 -20.13996 1.000 45.06069 ? 485 HOH A O   1 
HETATM 2493 O  O   . HOH X 8 .   ? -3.78531  10.07512 -22.02824 1.000 54.40431 ? 486 HOH A O   1 
HETATM 2494 O  O   . HOH X 8 .   ? -4.45163  30.05371 26.06468  1.000 51.44746 ? 487 HOH A O   1 
HETATM 2495 O  O   . HOH X 8 .   ? -8.63168  10.03587 -19.79511 1.000 24.91720 ? 488 HOH A O   1 
HETATM 2496 O  O   . HOH X 8 .   ? 10.10950  15.09483 -16.95500 1.000 48.10029 ? 489 HOH A O   1 
HETATM 2497 O  O   . HOH X 8 .   ? -13.41870 6.31141  -22.80706 1.000 41.73750 ? 490 HOH A O   1 
HETATM 2498 O  O   . HOH X 8 .   ? -17.81859 6.38320  15.65925  1.000 58.17451 ? 491 HOH A O   1 
HETATM 2499 O  O   . HOH X 8 .   ? -22.13722 16.74725 19.25040  1.000 45.35594 ? 492 HOH A O   1 
HETATM 2500 O  O   . HOH X 8 .   ? 2.28871   11.78872 21.74797  1.000 29.30540 ? 493 HOH A O   1 
HETATM 2501 O  O   . HOH X 8 .   ? -8.67419  11.87600 24.70447  1.000 63.08568 ? 494 HOH A O   1 
HETATM 2502 O  O   . HOH X 8 .   ? -22.54680 11.85463 17.37895  1.000 27.86922 ? 495 HOH A O   1 
HETATM 2503 O  O   . HOH X 8 .   ? -9.82191  19.06472 25.79311  1.000 35.50002 ? 496 HOH A O   1 
HETATM 2504 O  O   . HOH X 8 .   ? -13.16474 19.40240 22.69241  1.000 60.05865 ? 497 HOH A O   1 
HETATM 2505 O  O   . HOH X 8 .   ? 4.11933   24.76806 22.70294  1.000 35.02497 ? 498 HOH A O   1 
HETATM 2506 O  O   . HOH X 8 .   ? -2.48771  11.84378 -19.01809 1.000 25.84539 ? 499 HOH A O   1 
HETATM 2507 O  O   . HOH X 8 .   ? 2.99600   8.36104  15.64881  1.000 26.49756 ? 500 HOH A O   1 
HETATM 2508 O  O   . HOH X 8 .   ? -16.45896 5.52098  -21.51075 1.000 40.30449 ? 501 HOH A O   1 
HETATM 2509 O  O   . HOH X 8 .   ? 6.35338   11.87343 13.45297  1.000 63.24568 ? 502 HOH A O   1 
HETATM 2510 O  O   . HOH X 8 .   ? -0.14130  10.20834 22.09586  1.000 31.49845 ? 503 HOH A O   1 
HETATM 2511 O  O   . HOH X 8 .   ? -8.02807  -0.30057 13.75142  1.000 24.63136 ? 504 HOH A O   1 
HETATM 2512 O  O   . HOH X 8 .   ? -24.75603 21.13273 15.76694  1.000 28.61786 ? 505 HOH A O   1 
HETATM 2513 O  O   . HOH X 8 .   ? -6.52139  11.43496 -21.04712 1.000 33.55300 ? 506 HOH A O   1 
HETATM 2514 O  O   . HOH X 8 .   ? -7.80706  18.52473 27.41337  1.000 27.31217 ? 507 HOH A O   1 
HETATM 2515 O  O   . HOH X 8 .   ? -10.17396 28.23376 22.98256  1.000 53.25367 ? 508 HOH A O   1 
HETATM 2516 O  O   . HOH X 8 .   ? -4.98136  22.38390 27.85356  1.000 16.29671 ? 509 HOH A O   1 
HETATM 2517 O  O   . HOH X 8 .   ? -9.68910  22.18405 -23.06109 1.000 31.16694 ? 510 HOH A O   1 
HETATM 2518 O  O   . HOH X 8 .   ? -7.97666  15.92340 29.05243  1.000 26.77703 ? 511 HOH A O   1 
HETATM 2519 O  O   . HOH X 8 .   ? -21.42883 9.67126  15.58921  1.000 37.42856 ? 512 HOH A O   1 
HETATM 2520 O  O   . HOH X 8 .   ? -7.87786  12.27371 -23.29638 1.000 52.30618 ? 513 HOH A O   1 
HETATM 2521 O  O   . HOH X 8 .   ? -12.55286 15.04447 -23.02361 1.000 49.71551 ? 514 HOH A O   1 
HETATM 2522 O  O   . HOH X 8 .   ? -1.50483  9.51756  -20.54302 1.000 44.60964 ? 515 HOH A O   1 
HETATM 2523 O  O   . HOH X 8 .   ? -9.78103  10.32777 23.00017  1.000 44.72532 ? 516 HOH A O   1 
HETATM 2524 O  O   . HOH X 8 .   ? -10.80031 2.58183  -23.48079 1.000 69.57517 ? 517 HOH A O   1 
HETATM 2525 O  O   . HOH X 8 .   ? -20.78388 21.12921 18.52878  1.000 55.48378 ? 518 HOH A O   1 
HETATM 2526 O  O   . HOH X 8 .   ? -3.08012  1.48610  21.37727  1.000 38.51666 ? 519 HOH A O   1 
HETATM 2527 O  O   . HOH X 8 .   ? 0.27960   7.55768  23.11593  1.000 35.09092 ? 520 HOH A O   1 
HETATM 2528 O  O   B HOH X 8 .   ? -17.19296 20.03685 18.30484  0.500 46.69243 ? 521 HOH A O   1 
HETATM 2529 O  O   . HOH X 8 .   ? 4.73275   18.67870 16.16557  1.000 47.51690 ? 522 HOH A O   1 
HETATM 2530 O  O   . HOH X 8 .   ? -5.41558  -3.62954 15.44310  1.000 37.88386 ? 523 HOH A O   1 
HETATM 2531 O  O   . HOH X 8 .   ? -9.66369  -0.45949 17.86387  1.000 59.56284 ? 524 HOH A O   1 
HETATM 2532 O  O   . HOH X 8 .   ? -9.75709  -2.31578 12.70307  1.000 42.89125 ? 525 HOH A O   1 
HETATM 2533 O  O   . HOH X 8 .   ? -5.68915  4.01350  23.24556  1.000 52.69843 ? 526 HOH A O   1 
HETATM 2534 O  O   . HOH X 8 .   ? -0.08612  33.90705 -16.32379 1.000 37.76308 ? 527 HOH A O   1 
HETATM 2535 O  O   . HOH X 8 .   ? -15.41320 10.50135 17.85998  1.000 56.45594 ? 528 HOH A O   1 
HETATM 2536 O  O   . HOH X 8 .   ? -6.44450  24.95492 27.69183  1.000 42.74423 ? 529 HOH A O   1 
HETATM 2537 O  O   . HOH X 8 .   ? 4.16594   11.09337 17.45321  1.000 38.94636 ? 530 HOH A O   1 
HETATM 2538 O  O   . HOH X 8 .   ? -10.64208 7.13913  -22.69479 1.000 51.15818 ? 531 HOH A O   1 
HETATM 2539 O  O   . HOH X 8 .   ? -11.14107 21.42707 26.76425  1.000 57.31367 ? 532 HOH A O   1 
HETATM 2540 O  O   A HOH X 8 .   ? 0.19061   13.26587 25.52438  0.700 45.98417 ? 533 HOH A O   1 
HETATM 2541 O  O   . HOH X 8 .   ? -21.81639 7.41899  12.05426  1.000 53.87115 ? 534 HOH A O   1 
HETATM 2542 O  O   . HOH X 8 .   ? -20.47608 7.50300  16.22600  1.000 64.04234 ? 535 HOH A O   1 
HETATM 2543 O  O   . HOH X 8 .   ? 0.00000   0.00000  21.21699  0.500 42.32880 ? 536 HOH A O   1 
HETATM 2544 O  O   . HOH X 8 .   ? 4.98013   16.10636 14.63080  1.000 29.37924 ? 537 HOH A O   1 
HETATM 2545 O  O   . HOH X 8 .   ? 1.24155   35.75058 -22.63289 1.000 62.24834 ? 538 HOH A O   1 
HETATM 2546 O  O   . HOH X 8 .   ? -10.39883 1.07454  19.96709  1.000 63.99743 ? 539 HOH A O   1 
HETATM 2547 O  O   . HOH X 8 .   ? -7.81755  5.17543  -26.23474 1.000 58.96630 ? 540 HOH A O   1 
HETATM 2548 O  O   A HOH X 8 .   ? -4.32118  12.37017 29.04347  0.700 37.30058 ? 541 HOH A O   1 
HETATM 2549 O  O   B HOH X 8 .   ? -5.77842  13.17089 27.57756  0.300 27.26137 ? 541 HOH A O   1 
HETATM 2550 O  O   . HOH X 8 .   ? -25.47622 11.50255 17.51396  1.000 58.62970 ? 542 HOH A O   1 
HETATM 2551 O  O   . HOH X 8 .   ? 7.39662   15.59178 13.56704  1.000 55.43136 ? 543 HOH A O   1 
HETATM 2552 O  O   . HOH X 8 .   ? -7.36854  1.18507  22.59410  1.000 58.54450 ? 544 HOH A O   1 
HETATM 2553 O  O   A HOH X 8 .   ? -1.35805  12.23520 27.71976  0.700 39.19486 ? 545 HOH A O   1 
HETATM 2554 O  O   . HOH X 8 .   ? -18.65582 25.42698 18.91996  1.000 56.01166 ? 546 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   . FME A 1   ? 0.53491 0.55487 0.40430 -0.08250 -0.07433 0.05747  1   FME A N   
2    C  CN  . FME A 1   ? 0.58147 0.56926 0.42606 -0.05397 0.04282  0.06402  1   FME A CN  
3    O  O1  . FME A 1   ? 0.59021 0.58115 0.39271 -0.06173 -0.02386 0.09113  1   FME A O1  
4    C  CA  . FME A 1   ? 0.56849 0.54710 0.45613 -0.02995 0.00103  0.00597  1   FME A CA  
5    C  CB  . FME A 1   ? 0.61162 0.57445 0.50904 0.03944  0.07847  -0.04007 1   FME A CB  
6    C  CG  . FME A 1   ? 0.65271 0.60001 0.44932 0.02388  0.08512  -0.05487 1   FME A CG  
7    S  SD  . FME A 1   ? 0.65671 0.59190 0.36354 0.02418  0.05038  -0.05515 1   FME A SD  
8    C  CE  . FME A 1   ? 0.64021 0.60703 0.46953 0.02508  0.09774  -0.03657 1   FME A CE  
9    C  C   . FME A 1   ? 0.58935 0.51093 0.44557 -0.06638 -0.02041 0.05459  1   FME A C   
10   O  O   . FME A 1   ? 0.48677 0.48673 0.35218 -0.08229 0.00881  0.07243  1   FME A O   
11   N  N   . ASP A 2   ? 0.64820 0.50253 0.35797 -0.08571 0.06333  0.01711  2   ASP A N   
12   C  CA  . ASP A 2   ? 0.57681 0.48261 0.33140 -0.09918 0.07374  0.01421  2   ASP A CA  
13   C  C   . ASP A 2   ? 0.41665 0.41962 0.27140 -0.07109 0.05765  0.01575  2   ASP A C   
14   O  O   . ASP A 2   ? 0.52906 0.36194 0.24541 -0.03897 -0.04823 -0.00814 2   ASP A O   
15   C  CB  . ASP A 2   ? 0.64060 0.54206 0.44319 -0.07118 0.18212  0.07471  2   ASP A CB  
16   C  CG  . ASP A 2   ? 0.77946 0.62749 0.60895 -0.02703 0.02196  0.02714  2   ASP A CG  
17   O  OD1 . ASP A 2   ? 0.81966 0.66386 0.68041 -0.02475 -0.02100 0.00889  2   ASP A OD1 
18   O  OD2 . ASP A 2   ? 0.82737 0.65127 0.65311 -0.03548 -0.02805 0.00126  2   ASP A OD2 
19   N  N   . ASN A 3   ? 0.39714 0.36858 0.23944 -0.04617 -0.01308 0.03966  3   ASN A N   
20   C  CA  . ASN A 3   ? 0.40281 0.33377 0.23209 -0.02236 -0.09895 0.01826  3   ASN A CA  
21   C  C   . ASN A 3   ? 0.32708 0.28664 0.24235 -0.02186 -0.00803 0.03270  3   ASN A C   
22   O  O   . ASN A 3   ? 0.26235 0.27279 0.23213 -0.04789 0.01108  0.00913  3   ASN A O   
23   C  CB  . ASN A 3   ? 0.41319 0.41557 0.43149 0.01364  -0.19180 0.09631  3   ASN A CB  
24   C  CG  . ASN A 3   ? 0.49216 0.49167 0.51793 0.04183  -0.04363 0.13546  3   ASN A CG  
25   O  OD1 . ASN A 3   ? 0.53355 0.44571 0.56771 0.06736  0.09092  0.17827  3   ASN A OD1 
26   N  ND2 . ASN A 3   ? 0.41234 0.55604 0.52339 0.00380  -0.06030 0.12904  3   ASN A ND2 
27   N  N   . ILE A 4   ? 0.25754 0.28071 0.31091 -0.01994 0.00385  -0.00236 4   ILE A N   
28   C  CA  . ILE A 4   ? 0.25307 0.24383 0.27497 0.00649  0.01906  -0.01653 4   ILE A CA  
29   C  C   . ILE A 4   ? 0.30335 0.24092 0.26127 -0.09758 0.00211  -0.01962 4   ILE A C   
30   O  O   . ILE A 4   ? 0.40545 0.25197 0.21691 -0.04937 0.03221  0.00316  4   ILE A O   
31   C  CB  . ILE A 4   ? 0.26856 0.24479 0.32530 -0.05019 -0.00452 -0.04543 4   ILE A CB  
32   C  CG1 . ILE A 4   ? 0.22178 0.31577 0.37797 -0.05151 0.03295  -0.11633 4   ILE A CG1 
33   C  CG2 . ILE A 4   ? 0.38966 0.24194 0.34701 -0.00679 0.06325  -0.01109 4   ILE A CG2 
34   C  CD1 . ILE A 4   ? 0.30036 0.36933 0.43535 0.00308  0.03714  -0.16646 4   ILE A CD1 
35   N  N   . ILE A 5   ? 0.23491 0.26530 0.23986 -0.07181 0.01007  0.01747  5   ILE A N   
36   C  CA  . ILE A 5   ? 0.21668 0.31336 0.25884 -0.01185 0.09821  -0.01458 5   ILE A CA  
37   C  C   . ILE A 5   ? 0.20667 0.27303 0.22021 0.02582  0.02618  0.03831  5   ILE A C   
38   O  O   . ILE A 5   ? 0.27818 0.29635 0.20093 -0.05657 -0.00409 0.03240  5   ILE A O   
39   C  CB  . ILE A 5   ? 0.26689 0.40828 0.30888 -0.09781 0.09322  -0.06468 5   ILE A CB  
40   C  CG1 . ILE A 5   ? 0.28897 0.48252 0.40576 -0.01206 0.15798  0.01120  5   ILE A CG1 
41   C  CG2 . ILE A 5   ? 0.30108 0.42175 0.36150 -0.15134 0.06245  -0.03532 5   ILE A CG2 
42   C  CD1 . ILE A 5   ? 0.41708 0.54762 0.56466 0.08800  0.10524  0.02338  5   ILE A CD1 
43   N  N   . MET A 6   ? 0.25813 0.22719 0.24889 -0.03492 0.00099  0.01933  6   MET A N   
44   C  CA  . MET A 6   ? 0.33091 0.21865 0.22550 -0.06408 -0.02145 0.01129  6   MET A CA  
45   C  C   . MET A 6   ? 0.27480 0.22121 0.22816 -0.02277 -0.02027 0.03733  6   MET A C   
46   O  O   . MET A 6   ? 0.27078 0.21613 0.22744 -0.01788 -0.03995 0.01319  6   MET A O   
47   C  CB  . MET A 6   ? 0.36130 0.27249 0.22377 0.01460  -0.04547 0.00223  6   MET A CB  
48   C  CG  . MET A 6   ? 0.47888 0.31169 0.35377 0.10600  -0.14505 0.02675  6   MET A CG  
49   S  SD  . MET A 6   ? 0.59124 0.43229 0.51361 0.12692  -0.08628 0.05190  6   MET A SD  
50   C  CE  . MET A 6   ? 0.71463 0.43690 0.47194 0.05649  -0.06608 0.15932  6   MET A CE  
51   N  N   . THR A 7   ? 0.21783 0.20216 0.24561 -0.01790 -0.00408 0.03375  7   THR A N   
52   C  CA  . THR A 7   ? 0.23113 0.19595 0.21466 -0.01565 0.00499  0.01096  7   THR A CA  
53   C  C   . THR A 7   ? 0.20364 0.19152 0.23091 -0.00019 -0.01945 -0.00794 7   THR A C   
54   O  O   . THR A 7   ? 0.22871 0.22129 0.19801 -0.00886 -0.00185 0.00399  7   THR A O   
55   C  CB  . THR A 7   ? 0.22798 0.21733 0.24161 0.01270  0.03579  -0.01702 7   THR A CB  
56   O  OG1 . THR A 7   ? 0.22482 0.21676 0.23285 -0.02209 -0.01130 -0.01228 7   THR A OG1 
57   C  CG2 . THR A 7   ? 0.16445 0.23420 0.29279 0.03168  -0.00276 -0.00374 7   THR A CG2 
58   N  N   . ALA A 8   ? 0.20240 0.20637 0.24619 0.00563  -0.01158 0.01067  8   ALA A N   
59   C  CA  . ALA A 8   ? 0.19868 0.20930 0.22745 -0.00700 0.03746  0.01025  8   ALA A CA  
60   C  C   . ALA A 8   ? 0.21796 0.22015 0.21223 -0.05144 0.04738  -0.01142 8   ALA A C   
61   O  O   . ALA A 8   ? 0.25238 0.23922 0.18608 -0.02579 0.00126  -0.01174 8   ALA A O   
62   C  CB  . ALA A 8   ? 0.19096 0.23631 0.26863 0.01094  0.00940  -0.00678 8   ALA A CB  
63   N  N   . TYR A 9   ? 0.21006 0.20504 0.24899 -0.01642 -0.01050 0.00059  9   TYR A N   
64   C  CA  . TYR A 9   ? 0.19961 0.23273 0.20748 -0.04744 0.01832  0.01116  9   TYR A CA  
65   C  C   . TYR A 9   ? 0.18984 0.22211 0.19349 0.01332  -0.00092 0.03479  9   TYR A C   
66   O  O   . TYR A 9   ? 0.20167 0.23876 0.20828 -0.02626 -0.02519 0.00335  9   TYR A O   
67   C  CB  . TYR A 9   ? 0.26230 0.21314 0.25517 -0.06809 0.03896  0.01703  9   TYR A CB  
68   C  CG  . TYR A 9   ? 0.33665 0.26577 0.28349 -0.10524 0.02564  0.01076  9   TYR A CG  
69   C  CD1 . TYR A 9   ? 0.31542 0.29372 0.40905 -0.05930 0.12721  0.06781  9   TYR A CD1 
70   C  CD2 . TYR A 9   ? 0.30101 0.35814 0.26556 -0.06647 0.01606  0.05696  9   TYR A CD2 
71   C  CE1 . TYR A 9   ? 0.26320 0.35972 0.44134 -0.01613 0.10923  0.06271  9   TYR A CE1 
72   C  CE2 . TYR A 9   ? 0.28858 0.40858 0.33748 -0.05886 0.11000  -0.00771 9   TYR A CE2 
73   C  CZ  . TYR A 9   ? 0.24298 0.38575 0.42748 -0.06407 0.13736  0.00453  9   TYR A CZ  
74   O  OH  . TYR A 9   ? 0.36545 0.43597 0.47949 -0.14414 0.17639  -0.03528 9   TYR A OH  
75   N  N   . ILE A 10  ? 0.18739 0.21312 0.24901 0.01442  0.01415  0.01509  10  ILE A N   
76   C  CA  . ILE A 10  ? 0.16259 0.22129 0.23613 -0.00589 -0.00677 -0.00263 10  ILE A CA  
77   C  C   . ILE A 10  ? 0.23281 0.21573 0.23008 -0.00059 -0.05470 0.01758  10  ILE A C   
78   O  O   . ILE A 10  ? 0.19472 0.22980 0.23284 -0.01408 -0.03878 -0.01024 10  ILE A O   
79   C  CB  . ILE A 10  ? 0.21574 0.21444 0.25378 0.03448  -0.00777 0.03119  10  ILE A CB  
80   C  CG1 . ILE A 10  ? 0.21946 0.22770 0.27347 0.00957  -0.02383 0.02527  10  ILE A CG1 
81   C  CG2 . ILE A 10  ? 0.24465 0.20672 0.29264 0.00654  0.03348  0.00706  10  ILE A CG2 
82   C  CD1 . ILE A 10  ? 0.24178 0.27946 0.34728 0.01701  -0.08123 -0.00684 10  ILE A CD1 
83   N  N   . SER A 11  ? 0.22302 0.19607 0.22986 -0.03737 -0.01205 -0.00419 11  SER A N   
84   C  CA  . SER A 11  ? 0.14354 0.21622 0.23185 -0.01526 -0.00340 0.02627  11  SER A CA  
85   C  C   . SER A 11  ? 0.14083 0.21333 0.23884 -0.02092 0.01255  0.01297  11  SER A C   
86   O  O   . SER A 11  ? 0.23700 0.22893 0.20121 -0.01880 -0.02029 0.00447  11  SER A O   
87   C  CB  . SER A 11  ? 0.20484 0.20357 0.21444 -0.03146 -0.02930 0.00554  11  SER A CB  
88   O  OG  . SER A 11  ? 0.20417 0.22184 0.20996 0.01054  0.00540  0.01106  11  SER A OG  
89   N  N   . ILE A 12  ? 0.16334 0.20839 0.23979 -0.01672 0.01185  0.00347  12  ILE A N   
90   C  CA  . ILE A 12  ? 0.17291 0.27337 0.24894 -0.03223 0.02900  -0.02376 12  ILE A CA  
91   C  C   . ILE A 12  ? 0.16353 0.24507 0.22502 -0.00880 -0.00957 -0.03386 12  ILE A C   
92   O  O   . ILE A 12  ? 0.17735 0.27398 0.22442 -0.05610 -0.00896 0.00353  12  ILE A O   
93   C  CB  . ILE A 12  ? 0.15289 0.27133 0.25530 -0.01033 -0.00846 -0.03576 12  ILE A CB  
94   C  CG1 . ILE A 12  ? 0.23762 0.27858 0.22764 0.00591  0.02734  -0.00016 12  ILE A CG1 
95   C  CG2 . ILE A 12  ? 0.14921 0.28311 0.27222 -0.04016 -0.00736 -0.01911 12  ILE A CG2 
96   C  CD1 . ILE A 12  ? 0.27200 0.29462 0.22849 -0.04207 -0.00209 0.01805  12  ILE A CD1 
97   N  N   . PHE A 13  ? 0.18273 0.19840 0.23725 -0.02145 0.02250  -0.01192 13  PHE A N   
98   C  CA  . PHE A 13  ? 0.19874 0.20547 0.26241 -0.03592 0.01611  -0.01213 13  PHE A CA  
99   C  C   . PHE A 13  ? 0.17320 0.22306 0.23296 -0.02606 -0.00084 -0.03901 13  PHE A C   
100  O  O   . PHE A 13  ? 0.22627 0.23311 0.23166 -0.05426 -0.03039 -0.03409 13  PHE A O   
101  C  CB  . PHE A 13  ? 0.24815 0.21693 0.23616 -0.01088 0.02239  -0.03358 13  PHE A CB  
102  C  CG  . PHE A 13  ? 0.26614 0.24811 0.24278 -0.05824 -0.01705 -0.01596 13  PHE A CG  
103  C  CD1 . PHE A 13  ? 0.40029 0.27046 0.21959 -0.01457 0.07626  -0.01572 13  PHE A CD1 
104  C  CD2 . PHE A 13  ? 0.29310 0.28487 0.34459 -0.07315 0.01842  -0.09417 13  PHE A CD2 
105  C  CE1 . PHE A 13  ? 0.43445 0.26793 0.26931 -0.03708 -0.00453 -0.03311 13  PHE A CE1 
106  C  CE2 . PHE A 13  ? 0.29845 0.30605 0.24854 -0.06302 0.00006  -0.05514 13  PHE A CE2 
107  C  CZ  . PHE A 13  ? 0.45719 0.29117 0.27686 -0.02959 0.01522  -0.05913 13  PHE A CZ  
108  N  N   A VAL A 14  ? 0.21814 0.21201 0.21745 -0.02548 0.00767  0.00170  14  VAL A N   
109  N  N   B VAL A 14  ? 0.22418 0.22275 0.21012 -0.03979 -0.00681 0.01027  14  VAL A N   
110  C  CA  A VAL A 14  ? 0.19819 0.21285 0.19643 -0.01705 -0.00571 -0.00684 14  VAL A CA  
111  C  CA  B VAL A 14  ? 0.21789 0.22189 0.21094 -0.03428 0.01796  0.00570  14  VAL A CA  
112  C  C   A VAL A 14  ? 0.23768 0.19377 0.20061 -0.00649 -0.02493 0.00200  14  VAL A C   
113  C  C   B VAL A 14  ? 0.20077 0.21339 0.20575 -0.02268 0.00162  0.01209  14  VAL A C   
114  O  O   A VAL A 14  ? 0.23629 0.18896 0.21742 -0.00041 -0.07455 -0.00569 14  VAL A O   
115  O  O   B VAL A 14  ? 0.17539 0.23508 0.18889 -0.09172 0.02360  -0.00257 14  VAL A O   
116  C  CB  A VAL A 14  ? 0.13709 0.22796 0.21328 0.01028  -0.02793 0.02175  14  VAL A CB  
117  C  CB  B VAL A 14  ? 0.20057 0.20161 0.23615 -0.01668 -0.00046 -0.05736 14  VAL A CB  
118  C  CG1 A VAL A 14  ? 0.14879 0.21443 0.26946 0.04359  0.04143  0.06861  14  VAL A CG1 
119  C  CG1 B VAL A 14  ? 0.23491 0.16611 0.17950 -0.02870 0.02697  -0.04658 14  VAL A CG1 
120  C  CG2 A VAL A 14  ? 0.24170 0.18694 0.14219 0.01645  0.04111  -0.00213 14  VAL A CG2 
121  C  CG2 B VAL A 14  ? 0.17131 0.18971 0.18618 0.01596  0.02141  -0.05170 14  VAL A CG2 
122  N  N   . GLN A 15  ? 0.18505 0.21183 0.23407 -0.02967 -0.02919 0.00814  15  GLN A N   
123  C  CA  . GLN A 15  ? 0.17208 0.23093 0.23615 -0.02508 0.01356  -0.02409 15  GLN A CA  
124  C  C   . GLN A 15  ? 0.20438 0.24447 0.22316 -0.08322 0.00770  0.00097  15  GLN A C   
125  O  O   . GLN A 15  ? 0.22141 0.23214 0.20426 -0.03596 -0.01887 -0.00150 15  GLN A O   
126  C  CB  . GLN A 15  ? 0.15924 0.23444 0.21448 -0.02755 0.01423  -0.01120 15  GLN A CB  
127  C  CG  . GLN A 15  ? 0.20083 0.21639 0.22728 -0.05699 -0.02669 0.00982  15  GLN A CG  
128  C  CD  . GLN A 15  ? 0.19682 0.20787 0.22886 -0.01846 -0.00048 0.00644  15  GLN A CD  
129  O  OE1 . GLN A 15  ? 0.22021 0.23059 0.25427 0.00162  0.00791  0.00361  15  GLN A OE1 
130  N  NE2 . GLN A 15  ? 0.20632 0.23177 0.21146 -0.03203 -0.03693 -0.00538 15  GLN A NE2 
131  N  N   . ILE A 16  ? 0.23986 0.21868 0.23810 -0.07621 -0.00754 -0.01043 16  ILE A N   
132  C  CA  . ILE A 16  ? 0.24916 0.26046 0.25673 -0.10532 0.01505  -0.03015 16  ILE A CA  
133  C  C   . ILE A 16  ? 0.20682 0.22602 0.28540 -0.03675 -0.06023 0.00339  16  ILE A C   
134  O  O   . ILE A 16  ? 0.29258 0.23267 0.28121 -0.05598 -0.09056 -0.00855 16  ILE A O   
135  C  CB  . ILE A 16  ? 0.24754 0.37363 0.28569 -0.16915 0.00219  -0.05207 16  ILE A CB  
136  C  CG1 . ILE A 16  ? 0.23109 0.41470 0.34570 -0.13688 -0.04875 0.01849  16  ILE A CG1 
137  C  CG2 . ILE A 16  ? 0.30241 0.39701 0.37726 -0.09179 -0.07286 -0.01596 16  ILE A CG2 
138  C  CD1 . ILE A 16  ? 0.31988 0.45997 0.32008 -0.12301 0.06058  0.07877  16  ILE A CD1 
139  N  N   . ILE A 17  ? 0.24466 0.24074 0.24070 -0.03766 -0.01678 -0.02909 17  ILE A N   
140  C  CA  . ILE A 17  ? 0.29342 0.24475 0.26692 -0.02258 -0.01103 -0.02726 17  ILE A CA  
141  C  C   . ILE A 17  ? 0.22173 0.22801 0.24603 -0.03739 -0.02628 -0.01374 17  ILE A C   
142  O  O   . ILE A 17  ? 0.31151 0.22711 0.23393 -0.02267 -0.04553 -0.01401 17  ILE A O   
143  C  CB  . ILE A 17  ? 0.38792 0.24717 0.26750 -0.00178 -0.04688 0.00295  17  ILE A CB  
144  C  CG1 . ILE A 17  ? 0.35441 0.27830 0.34598 -0.03789 -0.09259 -0.05237 17  ILE A CG1 
145  C  CG2 . ILE A 17  ? 0.32680 0.29533 0.30082 0.00693  -0.08128 -0.05801 17  ILE A CG2 
146  C  CD1 . ILE A 17  ? 0.44352 0.32040 0.36050 -0.01016 -0.06312 0.01689  17  ILE A CD1 
147  N  N   A THR A 18  ? 0.24719 0.20426 0.23153 -0.02966 -0.02710 -0.02020 18  THR A N   
148  N  N   B THR A 18  ? 0.24544 0.23813 0.23130 -0.06324 -0.04322 -0.03472 18  THR A N   
149  C  CA  A THR A 18  ? 0.23599 0.19858 0.22697 0.00064  -0.06177 0.00931  18  THR A CA  
150  C  CA  B THR A 18  ? 0.25152 0.25789 0.23225 -0.05439 -0.05268 -0.03327 18  THR A CA  
151  C  C   A THR A 18  ? 0.25776 0.20505 0.21256 0.00346  -0.08259 -0.01699 18  THR A C   
152  C  C   B THR A 18  ? 0.21708 0.24716 0.24492 -0.03481 0.00203  -0.04524 18  THR A C   
153  O  O   A THR A 18  ? 0.26000 0.22834 0.22504 -0.05174 -0.09463 0.02910  18  THR A O   
154  O  O   B THR A 18  ? 0.12365 0.24769 0.23139 -0.07099 0.05805  -0.05670 18  THR A O   
155  C  CB  A THR A 18  ? 0.17314 0.22965 0.25701 0.00298  0.01688  -0.00074 18  THR A CB  
156  C  CB  B THR A 18  ? 0.29213 0.29571 0.22230 -0.04496 0.01422  -0.00584 18  THR A CB  
157  O  OG1 A THR A 18  ? 0.17516 0.22989 0.22537 0.00225  -0.00874 -0.00128 18  THR A OG1 
158  O  OG1 B THR A 18  ? 0.36169 0.30523 0.25842 -0.09760 0.03708  -0.01586 18  THR A OG1 
159  C  CG2 A THR A 18  ? 0.12122 0.22361 0.22149 -0.06492 0.01245  0.02447  18  THR A CG2 
160  C  CG2 B THR A 18  ? 0.25624 0.31627 0.12858 0.00398  0.02196  0.04453  18  THR A CG2 
161  N  N   . ALA A 19  ? 0.23317 0.21005 0.25240 -0.02354 0.00678  -0.01957 19  ALA A N   
162  C  CA  . ALA A 19  ? 0.18336 0.22273 0.26936 -0.02186 0.00067  -0.03657 19  ALA A CA  
163  C  C   . ALA A 19  ? 0.23634 0.23330 0.22566 -0.02835 -0.02659 -0.03393 19  ALA A C   
164  O  O   . ALA A 19  ? 0.19986 0.25061 0.20990 -0.02596 0.00581  -0.01821 19  ALA A O   
165  C  CB  . ALA A 19  ? 0.22624 0.24190 0.21633 0.02731  0.00511  -0.02633 19  ALA A CB  
166  N  N   . ILE A 20  ? 0.21287 0.21914 0.23901 -0.02852 -0.01392 -0.04519 20  ILE A N   
167  C  CA  . ILE A 20  ? 0.24519 0.22657 0.23389 -0.01583 -0.02529 -0.03544 20  ILE A CA  
168  C  C   . ILE A 20  ? 0.23534 0.22498 0.19220 -0.03650 0.00189  -0.03374 20  ILE A C   
169  O  O   . ILE A 20  ? 0.25625 0.26581 0.20626 -0.04801 -0.02933 -0.00791 20  ILE A O   
170  C  CB  . ILE A 20  ? 0.22775 0.23943 0.26614 -0.09469 -0.00013 -0.04032 20  ILE A CB  
171  C  CG1 . ILE A 20  ? 0.22855 0.26371 0.30055 -0.02965 0.09260  -0.00528 20  ILE A CG1 
172  C  CG2 . ILE A 20  ? 0.22589 0.25373 0.27390 -0.06443 -0.00137 -0.05810 20  ILE A CG2 
173  C  CD1 . ILE A 20  ? 0.31804 0.24995 0.33784 -0.02255 0.03558  0.01020  20  ILE A CD1 
174  N  N   . ILE A 21  ? 0.23350 0.26687 0.23418 -0.03604 0.01463  0.00655  21  ILE A N   
175  C  CA  . ILE A 21  ? 0.21730 0.28154 0.24912 -0.00551 -0.00067 0.01416  21  ILE A CA  
176  C  C   . ILE A 21  ? 0.22511 0.27685 0.22817 0.01934  -0.03943 -0.02770 21  ILE A C   
177  O  O   . ILE A 21  ? 0.21299 0.27763 0.22554 -0.00074 -0.01363 -0.00922 21  ILE A O   
178  C  CB  . ILE A 21  ? 0.19496 0.36320 0.23261 -0.00344 -0.00374 0.03528  21  ILE A CB  
179  C  CG1 . ILE A 21  ? 0.25448 0.38125 0.26656 0.05295  -0.02920 0.03154  21  ILE A CG1 
180  C  CG2 . ILE A 21  ? 0.23331 0.39594 0.27337 0.01649  0.00249  0.01818  21  ILE A CG2 
181  C  CD1 . ILE A 21  ? 0.28729 0.38022 0.28934 0.03191  0.03383  -0.01228 21  ILE A CD1 
182  N  N   . SER A 22  ? 0.19440 0.26452 0.24662 -0.05081 -0.01162 -0.02988 22  SER A N   
183  C  CA  . SER A 22  ? 0.19801 0.24769 0.26365 -0.02956 -0.05007 -0.01418 22  SER A CA  
184  C  C   . SER A 22  ? 0.15963 0.27064 0.24808 -0.01568 0.00820  -0.00960 22  SER A C   
185  O  O   . SER A 22  ? 0.22155 0.28599 0.24819 -0.07141 0.00682  0.00188  22  SER A O   
186  C  CB  . SER A 22  ? 0.25652 0.26971 0.26341 -0.01604 -0.09010 -0.03770 22  SER A CB  
187  O  OG  . SER A 22  ? 0.29212 0.30067 0.26821 -0.05296 -0.03123 -0.01017 22  SER A OG  
188  N  N   . VAL A 23  ? 0.15135 0.26694 0.21834 -0.02164 -0.01080 0.01074  23  VAL A N   
189  C  CA  . VAL A 23  ? 0.21431 0.25761 0.23213 -0.02024 0.01366  0.01567  23  VAL A CA  
190  C  C   . VAL A 23  ? 0.24841 0.24428 0.23767 -0.04815 0.02143  -0.01530 23  VAL A C   
191  O  O   . VAL A 23  ? 0.22220 0.24020 0.23000 -0.04737 -0.01256 -0.00062 23  VAL A O   
192  C  CB  . VAL A 23  ? 0.20515 0.28425 0.22310 -0.02453 0.01102  0.01244  23  VAL A CB  
193  C  CG1 . VAL A 23  ? 0.17385 0.33086 0.28290 -0.06425 -0.04937 0.01807  23  VAL A CG1 
194  C  CG2 . VAL A 23  ? 0.20557 0.26566 0.23902 0.00984  -0.00840 -0.02163 23  VAL A CG2 
195  N  N   . TYR A 24  ? 0.22511 0.23032 0.21740 -0.03133 -0.00623 -0.00356 24  TYR A N   
196  C  CA  . TYR A 24  ? 0.17578 0.24136 0.22722 -0.02438 -0.02121 -0.01193 24  TYR A CA  
197  C  C   . TYR A 24  ? 0.22172 0.24485 0.19976 -0.07426 0.04113  -0.00846 24  TYR A C   
198  O  O   . TYR A 24  ? 0.23778 0.26045 0.23358 -0.07518 -0.01813 0.00368  24  TYR A O   
199  C  CB  . TYR A 24  ? 0.22414 0.22041 0.24490 -0.02178 -0.04538 0.01645  24  TYR A CB  
200  C  CG  . TYR A 24  ? 0.14676 0.23215 0.25310 -0.04666 0.00141  0.00652  24  TYR A CG  
201  C  CD1 . TYR A 24  ? 0.21451 0.23893 0.21028 -0.06825 -0.02348 0.02872  24  TYR A CD1 
202  C  CD2 . TYR A 24  ? 0.16729 0.24100 0.24183 -0.04827 0.02858  -0.00891 24  TYR A CD2 
203  C  CE1 . TYR A 24  ? 0.23019 0.20538 0.22919 -0.04446 -0.00243 -0.03300 24  TYR A CE1 
204  C  CE2 . TYR A 24  ? 0.21275 0.22422 0.21648 -0.04189 0.02270  0.02541  24  TYR A CE2 
205  C  CZ  . TYR A 24  ? 0.29317 0.20883 0.21226 -0.07363 0.01803  0.00920  24  TYR A CZ  
206  O  OH  . TYR A 24  ? 0.27363 0.22514 0.22381 -0.06457 0.01228  0.01855  24  TYR A OH  
207  N  N   . GLY A 25  ? 0.17044 0.23256 0.26809 -0.06603 -0.01266 -0.01386 25  GLY A N   
208  C  CA  . GLY A 25  ? 0.17127 0.23692 0.27575 -0.05100 -0.00145 -0.01120 25  GLY A CA  
209  C  C   . GLY A 25  ? 0.24466 0.23424 0.25252 -0.02810 0.00271  -0.00327 25  GLY A C   
210  O  O   . GLY A 25  ? 0.25674 0.27497 0.22088 -0.05924 0.01370  0.00614  25  GLY A O   
211  N  N   . LEU A 26  ? 0.20857 0.23229 0.25391 -0.04926 -0.01068 0.01167  26  LEU A N   
212  C  CA  . LEU A 26  ? 0.24809 0.26670 0.25739 -0.02405 -0.02897 0.02816  26  LEU A CA  
213  C  C   . LEU A 26  ? 0.26926 0.28352 0.22183 -0.08630 0.03289  0.02021  26  LEU A C   
214  O  O   . LEU A 26  ? 0.33806 0.30866 0.25921 -0.12373 -0.03262 0.05023  26  LEU A O   
215  C  CB  . LEU A 26  ? 0.27197 0.28341 0.28246 0.00319  0.03706  0.02582  26  LEU A CB  
216  C  CG  . LEU A 26  ? 0.20539 0.29980 0.28926 0.00738  0.01943  0.02068  26  LEU A CG  
217  C  CD1 . LEU A 26  ? 0.27966 0.34193 0.30432 0.05290  0.07545  0.03947  26  LEU A CD1 
218  C  CD2 . LEU A 26  ? 0.34713 0.30035 0.37203 -0.03860 -0.01234 -0.02325 26  LEU A CD2 
219  N  N   . PHE A 27  ? 0.24416 0.30239 0.25600 -0.07514 -0.00182 -0.00139 27  PHE A N   
220  C  CA  . PHE A 27  ? 0.27016 0.32546 0.26208 -0.10785 -0.05081 0.02315  27  PHE A CA  
221  C  C   . PHE A 27  ? 0.28167 0.33628 0.25320 -0.11146 -0.03545 0.02410  27  PHE A C   
222  O  O   . PHE A 27  ? 0.26262 0.38549 0.25546 -0.11081 -0.03515 0.00284  27  PHE A O   
223  C  CB  . PHE A 27  ? 0.22017 0.36786 0.30642 -0.15151 -0.05438 0.02372  27  PHE A CB  
224  C  CG  . PHE A 27  ? 0.23553 0.41117 0.32411 -0.08081 0.02476  0.01074  27  PHE A CG  
225  C  CD1 . PHE A 27  ? 0.18707 0.45652 0.41095 0.00164  -0.01506 0.01516  27  PHE A CD1 
226  C  CD2 . PHE A 27  ? 0.17269 0.44368 0.28925 -0.08509 0.03885  0.02457  27  PHE A CD2 
227  C  CE1 . PHE A 27  ? 0.32377 0.49154 0.45270 0.00741  0.07105  0.02326  27  PHE A CE1 
228  C  CE2 . PHE A 27  ? 0.14314 0.47965 0.37341 -0.03138 -0.01692 0.00712  27  PHE A CE2 
229  C  CZ  . PHE A 27  ? 0.23098 0.49449 0.41663 0.02743  0.04190  0.04319  27  PHE A CZ  
230  N  N   . ILE A 28  ? 0.16672 0.32855 0.25850 -0.07567 0.00320  0.04131  28  ILE A N   
231  C  CA  . ILE A 28  ? 0.14111 0.32404 0.32488 -0.07294 0.07661  0.02020  28  ILE A CA  
232  C  C   . ILE A 28  ? 0.20876 0.32890 0.30273 -0.14912 0.00388  -0.01637 28  ILE A C   
233  O  O   . ILE A 28  ? 0.27311 0.32569 0.27198 -0.10663 -0.03352 0.00229  28  ILE A O   
234  C  CB  . ILE A 28  ? 0.22684 0.26651 0.28506 -0.06020 0.03645  0.00860  28  ILE A CB  
235  C  CG1 . ILE A 28  ? 0.22670 0.23996 0.28147 -0.03608 -0.04298 0.00758  28  ILE A CG1 
236  C  CG2 . ILE A 28  ? 0.25652 0.27439 0.26695 -0.03314 0.05065  -0.03002 28  ILE A CG2 
237  C  CD1 . ILE A 28  ? 0.25878 0.27995 0.27648 0.04694  0.00593  -0.00931 28  ILE A CD1 
238  N  N   . PRO A 29  ? 0.27866 0.36467 0.27288 -0.12754 -0.02333 -0.01598 29  PRO A N   
239  C  CA  . PRO A 29  ? 0.29669 0.39309 0.24693 -0.12760 -0.02340 0.01424  29  PRO A CA  
240  C  C   . PRO A 29  ? 0.30516 0.37161 0.25811 -0.08416 -0.01756 0.02259  29  PRO A C   
241  O  O   . PRO A 29  ? 0.27237 0.35971 0.29932 -0.08441 0.03164  0.01543  29  PRO A O   
242  C  CB  . PRO A 29  ? 0.35431 0.39811 0.24254 -0.14277 -0.00090 0.01227  29  PRO A CB  
243  C  CG  . PRO A 29  ? 0.54297 0.42102 0.25837 -0.12511 -0.03800 0.00073  29  PRO A CG  
244  C  CD  . PRO A 29  ? 0.34191 0.38234 0.26701 -0.15288 -0.01166 0.01672  29  PRO A CD  
245  N  N   . LEU A 30  ? 0.25725 0.32418 0.25680 -0.05685 -0.00278 0.05078  30  LEU A N   
246  C  CA  . LEU A 30  ? 0.28898 0.34367 0.21558 -0.06625 0.02372  0.01699  30  LEU A CA  
247  C  C   . LEU A 30  ? 0.24671 0.33355 0.23655 -0.04353 -0.03712 0.01656  30  LEU A C   
248  O  O   . LEU A 30  ? 0.32056 0.40449 0.27808 -0.07377 -0.03632 0.06006  30  LEU A O   
249  C  CB  . LEU A 30  ? 0.40596 0.35474 0.25525 -0.04094 0.10128  -0.01006 30  LEU A CB  
250  C  CG  . LEU A 30  ? 0.45197 0.33828 0.26474 -0.12250 0.08630  -0.02600 30  LEU A CG  
251  C  CD1 . LEU A 30  ? 0.54986 0.35301 0.39162 -0.11383 0.12976  -0.09440 30  LEU A CD1 
252  C  CD2 . LEU A 30  ? 0.49567 0.36491 0.23642 -0.03853 -0.08199 0.08173  30  LEU A CD2 
253  N  N   . ASN A 31  ? 0.29419 0.28518 0.21465 -0.06002 -0.00577 0.01837  31  ASN A N   
254  C  CA  . ASN A 31  ? 0.21336 0.26500 0.22948 -0.04269 0.00369  -0.01732 31  ASN A CA  
255  C  C   . ASN A 31  ? 0.27005 0.26299 0.21552 -0.02231 -0.02021 -0.00311 31  ASN A C   
256  O  O   . ASN A 31  ? 0.26719 0.28516 0.21540 -0.05941 -0.00521 -0.01582 31  ASN A O   
257  C  CB  . ASN A 31  ? 0.27240 0.27888 0.29546 -0.04216 0.07021  0.00397  31  ASN A CB  
258  C  CG  . ASN A 31  ? 0.46107 0.31944 0.28810 0.02123  0.01311  0.06955  31  ASN A CG  
259  O  OD1 . ASN A 31  ? 0.55795 0.36057 0.43519 0.05363  0.02056  0.00290  31  ASN A OD1 
260  N  ND2 . ASN A 31  ? 0.56523 0.34438 0.24658 -0.00411 0.05280  -0.02711 31  ASN A ND2 
261  N  N   . PHE A 32  ? 0.35138 0.26488 0.22889 -0.00155 -0.00843 0.02371  32  PHE A N   
262  C  CA  . PHE A 32  ? 0.37388 0.26928 0.19561 0.01375  -0.04172 0.02347  32  PHE A CA  
263  C  C   . PHE A 32  ? 0.30567 0.27738 0.15795 0.02285  -0.04116 0.02071  32  PHE A C   
264  O  O   . PHE A 32  ? 0.37170 0.25867 0.19022 0.00837  0.02183  -0.00629 32  PHE A O   
265  C  CB  . PHE A 32  ? 0.41843 0.28100 0.20072 -0.02555 -0.02101 0.02366  32  PHE A CB  
266  C  CG  . PHE A 32  ? 0.33446 0.29574 0.20190 0.01026  -0.03340 0.03654  32  PHE A CG  
267  C  CD1 . PHE A 32  ? 0.39096 0.29246 0.25732 0.08294  -0.06955 0.02879  32  PHE A CD1 
268  C  CD2 . PHE A 32  ? 0.44143 0.27791 0.20709 -0.05294 0.02059  0.03903  32  PHE A CD2 
269  C  CE1 . PHE A 32  ? 0.49632 0.29654 0.26133 0.07318  -0.04644 0.02532  32  PHE A CE1 
270  C  CE2 . PHE A 32  ? 0.52334 0.27570 0.22185 -0.02428 0.00755  0.04457  32  PHE A CE2 
271  C  CZ  . PHE A 32  ? 0.54674 0.29622 0.26235 0.02638  -0.06659 0.02660  32  PHE A CZ  
272  N  N   . LYS A 33  ? 0.20736 0.28380 0.23215 0.00410  -0.00781 0.02534  33  LYS A N   
273  C  CA  . LYS A 33  ? 0.28264 0.31841 0.26605 -0.03573 0.02720  0.00796  33  LYS A CA  
274  C  C   . LYS A 33  ? 0.29347 0.27091 0.19313 0.01980  0.01117  -0.01333 33  LYS A C   
275  O  O   . LYS A 33  ? 0.32486 0.25868 0.20590 -0.03788 -0.01187 -0.00480 33  LYS A O   
276  C  CB  . LYS A 33  ? 0.29845 0.36908 0.28874 -0.02662 0.02237  0.04204  33  LYS A CB  
277  C  CG  . LYS A 33  ? 0.33806 0.43890 0.33194 0.05346  0.07792  0.01257  33  LYS A CG  
278  C  CD  . LYS A 33  ? 0.40792 0.52003 0.40424 0.13276  0.14379  0.00694  33  LYS A CD  
279  C  CE  . LYS A 33  ? 0.49735 0.57866 0.47492 0.15375  0.12366  0.02086  33  LYS A CE  
280  N  NZ  . LYS A 33  ? 0.51128 0.60932 0.51608 0.15807  0.10130  0.05093  33  LYS A NZ  
281  N  N   . ASP A 34  ? 0.25173 0.24096 0.19938 0.00004  0.00484  0.00232  34  ASP A N   
282  C  CA  . ASP A 34  ? 0.28745 0.20871 0.18509 -0.00973 0.00502  0.00601  34  ASP A CA  
283  C  C   . ASP A 34  ? 0.22779 0.20258 0.23383 -0.01307 -0.03257 -0.01138 34  ASP A C   
284  O  O   . ASP A 34  ? 0.28034 0.23376 0.19751 -0.03340 -0.01015 0.00082  34  ASP A O   
285  C  CB  . ASP A 34  ? 0.26990 0.22003 0.21421 -0.02312 -0.01675 0.00059  34  ASP A CB  
286  C  CG  . ASP A 34  ? 0.25462 0.25190 0.27608 -0.01590 0.02309  0.00197  34  ASP A CG  
287  O  OD1 . ASP A 34  ? 0.24502 0.27778 0.32322 -0.00818 0.01103  -0.02280 34  ASP A OD1 
288  O  OD2 . ASP A 34  ? 0.28982 0.24764 0.29836 0.00400  0.00643  -0.02070 34  ASP A OD2 
289  N  N   . ILE A 35  ? 0.20964 0.21147 0.22889 0.00676  -0.02802 -0.00437 35  ILE A N   
290  C  CA  . ILE A 35  ? 0.27371 0.26387 0.21490 0.01770  -0.00355 -0.02055 35  ILE A CA  
291  C  C   . ILE A 35  ? 0.27558 0.20978 0.24143 -0.01089 -0.01114 0.01563  35  ILE A C   
292  O  O   . ILE A 35  ? 0.21498 0.26074 0.22786 -0.02970 0.00714  0.00030  35  ILE A O   
293  C  CB  . ILE A 35  ? 0.25319 0.36241 0.25417 0.07432  -0.03969 -0.06779 35  ILE A CB  
294  C  CG1 . ILE A 35  ? 0.28709 0.43589 0.25241 0.08536  -0.07088 -0.03554 35  ILE A CG1 
295  C  CG2 . ILE A 35  ? 0.18889 0.42221 0.30769 0.04155  -0.02799 -0.06431 35  ILE A CG2 
296  C  CD1 . ILE A 35  ? 0.36704 0.46803 0.35645 0.12755  -0.10311 -0.01413 35  ILE A CD1 
297  N  N   . ILE A 36  ? 0.26500 0.19576 0.21325 -0.01622 -0.01555 -0.01474 36  ILE A N   
298  C  CA  . ILE A 36  ? 0.21471 0.22815 0.21741 0.00035  -0.03498 0.00592  36  ILE A CA  
299  C  C   . ILE A 36  ? 0.21675 0.21393 0.23039 -0.01807 -0.00872 -0.02020 36  ILE A C   
300  O  O   . ILE A 36  ? 0.19729 0.20996 0.21084 -0.00608 0.00222  -0.00670 36  ILE A O   
301  C  CB  . ILE A 36  ? 0.15874 0.22956 0.19961 -0.03060 -0.01474 -0.01995 36  ILE A CB  
302  C  CG1 . ILE A 36  ? 0.24898 0.20879 0.20752 -0.04823 -0.02391 0.01104  36  ILE A CG1 
303  C  CG2 . ILE A 36  ? 0.17651 0.22093 0.26262 0.00900  -0.02775 0.02438  36  ILE A CG2 
304  C  CD1 . ILE A 36  ? 0.23474 0.18631 0.24833 -0.02599 -0.02602 0.01594  36  ILE A CD1 
305  N  N   . LEU A 37  ? 0.23951 0.20993 0.21080 -0.01560 0.02072  -0.00815 37  LEU A N   
306  C  CA  . LEU A 37  ? 0.22368 0.20473 0.21850 -0.03428 0.00053  0.01442  37  LEU A CA  
307  C  C   . LEU A 37  ? 0.17388 0.19627 0.22620 -0.04419 -0.02891 0.00790  37  LEU A C   
308  O  O   . LEU A 37  ? 0.21254 0.21610 0.18757 -0.01738 -0.00124 -0.00566 37  LEU A O   
309  C  CB  . LEU A 37  ? 0.22915 0.17297 0.24903 -0.01048 -0.00552 -0.01456 37  LEU A CB  
310  C  CG  . LEU A 37  ? 0.22817 0.23586 0.23412 0.00874  -0.00782 0.01263  37  LEU A CG  
311  C  CD1 . LEU A 37  ? 0.25455 0.25820 0.24969 0.07036  0.05153  -0.00556 37  LEU A CD1 
312  C  CD2 . LEU A 37  ? 0.20534 0.30888 0.27984 -0.00316 -0.02433 -0.00608 37  LEU A CD2 
313  N  N   . ARG A 38  ? 0.16121 0.24168 0.21961 -0.04189 -0.03148 -0.00576 38  ARG A N   
314  C  CA  . ARG A 38  ? 0.17911 0.22455 0.24116 -0.04492 -0.01849 -0.01714 38  ARG A CA  
315  C  C   . ARG A 38  ? 0.18432 0.24497 0.20273 -0.00806 -0.02224 -0.03247 38  ARG A C   
316  O  O   . ARG A 38  ? 0.20925 0.26673 0.19648 -0.01405 -0.00467 -0.02946 38  ARG A O   
317  C  CB  . ARG A 38  ? 0.20218 0.29728 0.26532 -0.06467 -0.03563 -0.02281 38  ARG A CB  
318  C  CG  . ARG A 38  ? 0.15087 0.34765 0.31097 -0.05261 0.01374  -0.01132 38  ARG A CG  
319  C  CD  . ARG A 38  ? 0.20747 0.35966 0.28946 -0.00029 -0.03131 -0.02385 38  ARG A CD  
320  N  NE  . ARG A 38  ? 0.33374 0.38358 0.30465 -0.07869 -0.11192 0.02453  38  ARG A NE  
321  C  CZ  . ARG A 38  ? 0.43261 0.41423 0.39274 -0.01279 -0.14100 -0.00914 38  ARG A CZ  
322  N  NH1 . ARG A 38  ? 0.49821 0.41901 0.39298 0.06780  -0.12473 0.00034  38  ARG A NH1 
323  N  NH2 . ARG A 38  ? 0.50719 0.44756 0.36133 -0.02746 -0.19666 -0.04775 38  ARG A NH2 
324  N  N   . GLU A 39  ? 0.18494 0.21248 0.22085 0.00237  -0.00984 -0.01439 39  GLU A N   
325  C  CA  . GLU A 39  ? 0.16061 0.23004 0.23379 0.01002  -0.02237 -0.00228 39  GLU A CA  
326  C  C   . GLU A 39  ? 0.17423 0.24814 0.19272 -0.00171 -0.02044 -0.01830 39  GLU A C   
327  O  O   . GLU A 39  ? 0.19682 0.26653 0.19986 0.01883  -0.02467 -0.01000 39  GLU A O   
328  C  CB  . GLU A 39  ? 0.24744 0.23497 0.24194 0.01254  -0.01453 0.02556  39  GLU A CB  
329  C  CG  . GLU A 39  ? 0.21573 0.26181 0.23745 0.03242  -0.08772 0.02659  39  GLU A CG  
330  C  CD  . GLU A 39  ? 0.28321 0.25138 0.30591 0.03459  -0.07280 0.01492  39  GLU A CD  
331  O  OE1 . GLU A 39  ? 0.23131 0.25868 0.28137 0.01324  0.00366  0.01224  39  GLU A OE1 
332  O  OE2 . GLU A 39  ? 0.36562 0.28787 0.34031 -0.02019 -0.10461 0.07024  39  GLU A OE2 
333  N  N   . ILE A 40  ? 0.16677 0.21288 0.22660 0.01037  -0.00704 0.00333  40  ILE A N   
334  C  CA  . ILE A 40  ? 0.21974 0.22075 0.18744 0.01584  -0.04357 0.01022  40  ILE A CA  
335  C  C   . ILE A 40  ? 0.18573 0.22688 0.21740 0.01867  -0.00334 -0.01410 40  ILE A C   
336  O  O   . ILE A 40  ? 0.14004 0.25082 0.21418 -0.00726 -0.00075 -0.00830 40  ILE A O   
337  C  CB  . ILE A 40  ? 0.15746 0.21813 0.20836 0.00741  -0.03644 -0.01039 40  ILE A CB  
338  C  CG1 . ILE A 40  ? 0.17854 0.22302 0.23542 -0.03033 0.01834  -0.00934 40  ILE A CG1 
339  C  CG2 . ILE A 40  ? 0.16923 0.22909 0.25699 -0.03617 -0.04658 0.00054  40  ILE A CG2 
340  C  CD1 . ILE A 40  ? 0.22404 0.22884 0.23245 -0.00691 -0.01273 -0.01569 40  ILE A CD1 
341  N  N   . LEU A 41  ? 0.24104 0.22185 0.19272 -0.01361 -0.00225 0.00065  41  LEU A N   
342  C  CA  . LEU A 41  ? 0.27529 0.22985 0.19443 -0.01326 0.01592  -0.02161 41  LEU A CA  
343  C  C   . LEU A 41  ? 0.21452 0.24904 0.18493 -0.02450 -0.02092 -0.02410 41  LEU A C   
344  O  O   . LEU A 41  ? 0.20696 0.25073 0.20849 -0.02174 0.01252  -0.01469 41  LEU A O   
345  C  CB  . LEU A 41  ? 0.30129 0.21787 0.24108 -0.04985 -0.01211 0.01300  41  LEU A CB  
346  C  CG  . LEU A 41  ? 0.31324 0.24329 0.24012 -0.06574 -0.06082 0.02168  41  LEU A CG  
347  C  CD1 . LEU A 41  ? 0.24420 0.24005 0.31659 -0.03860 -0.05427 -0.00446 41  LEU A CD1 
348  C  CD2 . LEU A 41  ? 0.28911 0.25519 0.26176 -0.07873 0.01907  -0.03660 41  LEU A CD2 
349  N  N   A ILE A 42  ? 0.13684 0.27547 0.21430 -0.01670 -0.02231 -0.01932 42  ILE A N   
350  N  N   B ILE A 42  ? 0.19305 0.25521 0.18205 -0.00229 -0.00349 -0.02781 42  ILE A N   
351  C  CA  A ILE A 42  ? 0.17820 0.26623 0.21131 -0.03347 0.00646  -0.01006 42  ILE A CA  
352  C  CA  B ILE A 42  ? 0.21611 0.26195 0.22533 0.00358  -0.05358 -0.02671 42  ILE A CA  
353  C  C   A ILE A 42  ? 0.21843 0.25245 0.20553 -0.01090 0.01951  0.00186  42  ILE A C   
354  C  C   B ILE A 42  ? 0.17626 0.26747 0.23927 -0.00952 -0.03232 -0.00018 42  ILE A C   
355  O  O   A ILE A 42  ? 0.28389 0.21791 0.17252 0.05262  -0.02742 0.00672  42  ILE A O   
356  O  O   B ILE A 42  ? 0.11935 0.27807 0.24500 -0.03133 -0.03058 0.02684  42  ILE A O   
357  C  CB  A ILE A 42  ? 0.09698 0.29771 0.23474 -0.02226 0.05223  -0.02603 42  ILE A CB  
358  C  CB  B ILE A 42  ? 0.18869 0.27902 0.29319 0.00886  -0.02973 -0.03984 42  ILE A CB  
359  C  CG1 A ILE A 42  ? 0.12698 0.31912 0.22235 -0.03325 -0.02829 -0.01245 42  ILE A CG1 
360  C  CG1 B ILE A 42  ? 0.21663 0.31622 0.32835 0.07539  -0.08786 -0.02684 42  ILE A CG1 
361  C  CG2 A ILE A 42  ? 0.17521 0.32516 0.29989 -0.04712 -0.05221 -0.01458 42  ILE A CG2 
362  C  CG2 B ILE A 42  ? 0.17679 0.23065 0.29548 0.04107  -0.00866 -0.01328 42  ILE A CG2 
363  C  CD1 A ILE A 42  ? 0.17290 0.30356 0.36425 0.07581  -0.07317 0.06887  42  ILE A CD1 
364  C  CD1 B ILE A 42  ? 0.24867 0.35930 0.46739 0.06037  -0.06130 -0.01372 42  ILE A CD1 
365  N  N   . LEU A 43  ? 0.18025 0.22684 0.21891 -0.01486 -0.02209 0.01266  43  LEU A N   
366  C  CA  . LEU A 43  ? 0.20504 0.22455 0.21018 -0.03635 -0.02846 0.00810  43  LEU A CA  
367  C  C   . LEU A 43  ? 0.16591 0.21880 0.23679 -0.00458 -0.03211 -0.01856 43  LEU A C   
368  O  O   . LEU A 43  ? 0.18208 0.22863 0.20981 -0.01002 0.00457  -0.01695 43  LEU A O   
369  C  CB  . LEU A 43  ? 0.20589 0.24118 0.21745 0.00289  -0.02891 0.01501  43  LEU A CB  
370  C  CG  . LEU A 43  ? 0.20211 0.25839 0.22697 -0.01095 -0.02786 0.04536  43  LEU A CG  
371  C  CD1 . LEU A 43  ? 0.30023 0.30181 0.31533 -0.05493 -0.00081 0.04631  43  LEU A CD1 
372  C  CD2 . LEU A 43  ? 0.25338 0.26874 0.32798 0.02664  0.02004  0.01985  43  LEU A CD2 
373  N  N   A GLU A 44  ? 0.20078 0.22255 0.20850 -0.00020 -0.01460 0.00468  44  GLU A N   
374  N  N   B GLU A 44  ? 0.19184 0.20715 0.24310 -0.01570 -0.05139 -0.00223 44  GLU A N   
375  C  CA  A GLU A 44  ? 0.21209 0.22581 0.24639 -0.00603 0.02241  0.02403  44  GLU A CA  
376  C  CA  B GLU A 44  ? 0.19662 0.19880 0.21098 -0.01239 -0.06609 -0.00939 44  GLU A CA  
377  C  C   A GLU A 44  ? 0.17373 0.21979 0.23531 -0.02705 -0.02725 -0.01168 44  GLU A C   
378  C  C   B GLU A 44  ? 0.19510 0.18595 0.16694 -0.01269 -0.05081 -0.04479 44  GLU A C   
379  O  O   A GLU A 44  ? 0.17247 0.21443 0.21225 -0.01814 0.02288  -0.04172 44  GLU A O   
380  O  O   B GLU A 44  ? 0.27105 0.18230 0.19498 0.02163  -0.09652 0.01567  44  GLU A O   
381  C  CB  A GLU A 44  ? 0.16901 0.27985 0.28262 0.03918  0.00535  0.03419  44  GLU A CB  
382  C  CB  B GLU A 44  ? 0.21631 0.21353 0.25323 -0.00952 -0.12185 -0.02201 44  GLU A CB  
383  C  CG  A GLU A 44  ? 0.24555 0.35953 0.25107 -0.00781 0.07110  0.05374  44  GLU A CG  
384  C  CG  B GLU A 44  ? 0.28773 0.23928 0.28885 0.01381  -0.10939 0.00105  44  GLU A CG  
385  C  CD  A GLU A 44  ? 0.27014 0.41745 0.28610 -0.03320 0.03875  0.05291  44  GLU A CD  
386  C  CD  B GLU A 44  ? 0.29339 0.26280 0.30642 0.03447  -0.08756 -0.00360 44  GLU A CD  
387  O  OE1 A GLU A 44  ? 0.29405 0.46216 0.25086 -0.05997 -0.02752 0.00055  44  GLU A OE1 
388  O  OE1 B GLU A 44  ? 0.33987 0.26050 0.28109 0.03079  -0.05207 0.01020  44  GLU A OE1 
389  O  OE2 A GLU A 44  ? 0.36854 0.43800 0.32240 0.00112  -0.06597 0.07358  44  GLU A OE2 
390  O  OE2 B GLU A 44  ? 0.21612 0.26927 0.40071 0.08300  0.00678  -0.00609 44  GLU A OE2 
391  N  N   A LEU A 45  ? 0.18976 0.21949 0.19972 -0.07355 -0.06532 -0.01352 45  LEU A N   
392  N  N   B LEU A 45  ? 0.16111 0.21957 0.25151 -0.01421 0.02926  0.01713  45  LEU A N   
393  C  CA  A LEU A 45  ? 0.23390 0.23563 0.21761 -0.05169 -0.04648 -0.01675 45  LEU A CA  
394  C  CA  B LEU A 45  ? 0.17133 0.24777 0.22150 -0.07829 -0.04635 0.01110  45  LEU A CA  
395  C  C   A LEU A 45  ? 0.17822 0.26751 0.23684 -0.03686 -0.01333 -0.00803 45  LEU A C   
396  C  C   B LEU A 45  ? 0.11618 0.27894 0.23147 -0.05066 -0.06476 -0.00742 45  LEU A C   
397  O  O   A LEU A 45  ? 0.21133 0.29271 0.20705 -0.09491 -0.06050 0.01058  45  LEU A O   
398  O  O   B LEU A 45  ? 0.13525 0.31866 0.21538 -0.05585 0.01385  -0.00625 45  LEU A O   
399  C  CB  A LEU A 45  ? 0.25674 0.25286 0.25001 -0.01548 -0.00698 -0.04249 45  LEU A CB  
400  C  CB  B LEU A 45  ? 0.13796 0.25518 0.26804 -0.08905 -0.04612 -0.02445 45  LEU A CB  
401  C  CG  A LEU A 45  ? 0.18360 0.27266 0.26689 -0.02119 0.04210  -0.03366 45  LEU A CG  
402  C  CG  B LEU A 45  ? 0.12575 0.32200 0.29678 -0.04294 -0.03251 -0.01363 45  LEU A CG  
403  C  CD1 A LEU A 45  ? 0.24440 0.26797 0.24978 -0.08435 -0.06113 -0.05289 45  LEU A CD1 
404  C  CD1 B LEU A 45  ? 0.12432 0.30065 0.33005 0.00409  0.05413  -0.00126 45  LEU A CD1 
405  C  CD2 A LEU A 45  ? 0.07055 0.25121 0.27917 -0.00656 -0.00909 -0.00178 45  LEU A CD2 
406  C  CD2 B LEU A 45  ? 0.29472 0.31569 0.31682 -0.09690 -0.09518 -0.05162 45  LEU A CD2 
407  N  N   . ILE A 46  ? 0.16769 0.27186 0.23623 -0.01256 -0.00960 -0.00828 46  ILE A N   
408  C  CA  . ILE A 46  ? 0.16776 0.28309 0.23646 0.02035  -0.03272 0.02901  46  ILE A CA  
409  C  C   . ILE A 46  ? 0.17495 0.26356 0.24584 0.00858  0.00966  0.00643  46  ILE A C   
410  O  O   . ILE A 46  ? 0.18922 0.26842 0.24265 0.02635  0.00362  0.01492  46  ILE A O   
411  C  CB  . ILE A 46  ? 0.23433 0.29789 0.25939 0.08937  -0.00921 0.03965  46  ILE A CB  
412  C  CG1 . ILE A 46  ? 0.32705 0.34175 0.24139 0.04794  -0.02206 0.06615  46  ILE A CG1 
413  C  CG2 . ILE A 46  ? 0.28470 0.30136 0.32595 0.11006  0.03755  0.00110  46  ILE A CG2 
414  C  CD1 . ILE A 46  ? 0.19974 0.41289 0.32186 0.06876  0.00388  0.05509  46  ILE A CD1 
415  N  N   . VAL A 47  ? 0.15740 0.23444 0.20563 -0.00266 0.00066  0.01171  47  VAL A N   
416  C  CA  . VAL A 47  ? 0.24033 0.23051 0.17465 -0.01543 0.00669  0.00652  47  VAL A CA  
417  C  C   . VAL A 47  ? 0.19344 0.22856 0.21739 -0.02619 -0.01771 -0.02035 47  VAL A C   
418  O  O   . VAL A 47  ? 0.18854 0.26909 0.19405 -0.01016 0.00135  0.00255  47  VAL A O   
419  C  CB  . VAL A 47  ? 0.17913 0.21282 0.19309 -0.01653 -0.00871 -0.00048 47  VAL A CB  
420  C  CG1 . VAL A 47  ? 0.23244 0.19806 0.21454 -0.02545 -0.03548 -0.01029 47  VAL A CG1 
421  C  CG2 . VAL A 47  ? 0.21259 0.23337 0.26569 -0.03384 -0.04163 -0.00972 47  VAL A CG2 
422  N  N   . GLN A 48  ? 0.19068 0.22454 0.21291 -0.02099 -0.02933 -0.00294 48  GLN A N   
423  C  CA  . GLN A 48  ? 0.20172 0.23335 0.22269 -0.05838 -0.02117 0.04112  48  GLN A CA  
424  C  C   . GLN A 48  ? 0.24980 0.22953 0.24490 -0.05560 0.01663  0.01889  48  GLN A C   
425  O  O   . GLN A 48  ? 0.25634 0.22999 0.22049 -0.02326 0.02914  0.00899  48  GLN A O   
426  C  CB  . GLN A 48  ? 0.30746 0.23221 0.26962 -0.01530 -0.08020 -0.00562 48  GLN A CB  
427  C  CG  . GLN A 48  ? 0.28836 0.22535 0.23946 -0.04014 -0.05683 -0.00714 48  GLN A CG  
428  C  CD  . GLN A 48  ? 0.28168 0.23356 0.21940 -0.05519 -0.00858 -0.00186 48  GLN A CD  
429  O  OE1 . GLN A 48  ? 0.28134 0.23373 0.24420 -0.03379 0.01074  -0.00293 48  GLN A OE1 
430  N  NE2 . GLN A 48  ? 0.19376 0.26284 0.21928 -0.04342 -0.00305 -0.00823 48  GLN A NE2 
431  N  N   . ILE A 49  ? 0.21169 0.28495 0.21438 -0.02319 -0.01387 0.00377  49  ILE A N   
432  C  CA  . ILE A 49  ? 0.21207 0.31713 0.23784 -0.02285 0.01833  -0.00783 49  ILE A CA  
433  C  C   . ILE A 49  ? 0.24592 0.27936 0.27257 -0.02056 -0.02117 0.04400  49  ILE A C   
434  O  O   . ILE A 49  ? 0.20278 0.28436 0.24348 -0.03339 0.00266  0.01790  49  ILE A O   
435  C  CB  . ILE A 49  ? 0.15316 0.38754 0.22701 0.00244  -0.02246 0.00201  49  ILE A CB  
436  C  CG1 . ILE A 49  ? 0.23203 0.39446 0.27080 -0.06589 -0.02509 0.04430  49  ILE A CG1 
437  C  CG2 . ILE A 49  ? 0.22509 0.42121 0.27020 -0.01260 -0.02556 0.04130  49  ILE A CG2 
438  C  CD1 . ILE A 49  ? 0.25991 0.41774 0.30473 -0.00429 -0.07502 0.01585  49  ILE A CD1 
439  N  N   A ILE A 50  ? 0.14285 0.26978 0.25892 0.00532  -0.03568 0.03332  50  ILE A N   
440  N  N   B ILE A 50  ? 0.23963 0.25243 0.27789 0.01339  0.00375  0.01752  50  ILE A N   
441  C  CA  A ILE A 50  ? 0.11641 0.26144 0.26101 0.01038  -0.05077 0.02618  50  ILE A CA  
442  C  CA  B ILE A 50  ? 0.19369 0.25598 0.28311 -0.00795 0.00852  -0.03850 50  ILE A CA  
443  C  C   A ILE A 50  ? 0.16072 0.24351 0.28725 0.02194  -0.00243 0.04524  50  ILE A C   
444  C  C   B ILE A 50  ? 0.18973 0.24916 0.26216 -0.04971 -0.02597 -0.07494 50  ILE A C   
445  O  O   A ILE A 50  ? 0.15264 0.25912 0.23780 0.01379  0.03674  0.06059  50  ILE A O   
446  O  O   B ILE A 50  ? 0.18843 0.28470 0.26586 -0.07829 -0.02955 -0.07320 50  ILE A O   
447  C  CB  A ILE A 50  ? 0.10225 0.23843 0.24432 -0.00116 -0.06635 0.04344  50  ILE A CB  
448  C  CB  B ILE A 50  ? 0.22220 0.23809 0.30570 0.02130  0.01521  -0.02295 50  ILE A CB  
449  C  CG1 A ILE A 50  ? 0.20295 0.26993 0.29744 -0.00469 -0.11854 0.03953  50  ILE A CG1 
450  C  CG1 B ILE A 50  ? 0.18370 0.28017 0.32962 0.02929  0.06544  -0.04358 50  ILE A CG1 
451  C  CG2 A ILE A 50  ? 0.09329 0.25795 0.23095 0.00855  0.01633  -0.01065 50  ILE A CG2 
452  C  CG2 B ILE A 50  ? 0.20551 0.22650 0.29781 0.02389  -0.06633 -0.01211 50  ILE A CG2 
453  C  CD1 A ILE A 50  ? 0.27159 0.28662 0.31747 -0.00961 -0.09931 0.02615  50  ILE A CD1 
454  C  CD1 B ILE A 50  ? 0.20162 0.32098 0.39434 0.01211  0.08260  -0.05805 50  ILE A CD1 
455  N  N   . GLU A 51  ? 0.18745 0.22668 0.23310 0.01680  -0.01499 0.01160  51  GLU A N   
456  C  CA  . GLU A 51  ? 0.16210 0.23990 0.28615 -0.03053 0.01797  0.01985  51  GLU A CA  
457  C  C   . GLU A 51  ? 0.15342 0.24325 0.25874 -0.01819 -0.01823 -0.01793 51  GLU A C   
458  O  O   . GLU A 51  ? 0.18999 0.26748 0.22261 0.00081  0.02196  0.00278  51  GLU A O   
459  C  CB  . GLU A 51  ? 0.19707 0.27539 0.24736 0.03489  -0.00150 0.01770  51  GLU A CB  
460  C  CG  . GLU A 51  ? 0.16383 0.26513 0.26198 0.04096  -0.01071 0.01024  51  GLU A CG  
461  C  CD  . GLU A 51  ? 0.16951 0.25626 0.34180 -0.04792 -0.04892 0.05836  51  GLU A CD  
462  O  OE1 . GLU A 51  ? 0.20018 0.24746 0.33513 -0.02194 0.02299  0.00197  51  GLU A OE1 
463  O  OE2 . GLU A 51  ? 0.16344 0.32068 0.36626 -0.01788 -0.04483 0.09880  51  GLU A OE2 
464  N  N   . PHE A 52  ? 0.20444 0.24209 0.22731 -0.02029 0.01954  0.00334  52  PHE A N   
465  C  CA  . PHE A 52  ? 0.22467 0.26846 0.20618 -0.02095 -0.00502 -0.03492 52  PHE A CA  
466  C  C   . PHE A 52  ? 0.18338 0.26933 0.25949 -0.03743 -0.00373 0.01436  52  PHE A C   
467  O  O   . PHE A 52  ? 0.23339 0.28394 0.22858 -0.01500 0.01393  0.00561  52  PHE A O   
468  C  CB  . PHE A 52  ? 0.25232 0.27885 0.20669 -0.03011 -0.01208 0.02903  52  PHE A CB  
469  C  CG  . PHE A 52  ? 0.28206 0.29722 0.27287 -0.08480 -0.05456 0.01567  52  PHE A CG  
470  C  CD1 . PHE A 52  ? 0.36360 0.28179 0.30409 -0.06573 -0.00802 0.01996  52  PHE A CD1 
471  C  CD2 . PHE A 52  ? 0.32949 0.35611 0.32377 -0.14176 -0.06486 0.01445  52  PHE A CD2 
472  C  CE1 . PHE A 52  ? 0.41953 0.32051 0.33795 -0.12364 0.01362  -0.01521 52  PHE A CE1 
473  C  CE2 . PHE A 52  ? 0.41486 0.38048 0.31324 -0.15722 -0.03356 0.03577  52  PHE A CE2 
474  C  CZ  . PHE A 52  ? 0.42250 0.32574 0.28426 -0.14621 0.00875  0.00343  52  PHE A CZ  
475  N  N   . ILE A 53  ? 0.20022 0.28519 0.24505 -0.00042 0.00465  0.01765  53  ILE A N   
476  C  CA  . ILE A 53  ? 0.17900 0.33137 0.25091 0.02513  -0.02577 0.00063  53  ILE A CA  
477  C  C   . ILE A 53  ? 0.12611 0.29983 0.25404 -0.01387 0.00877  -0.00045 53  ILE A C   
478  O  O   . ILE A 53  ? 0.17733 0.28819 0.25834 -0.02617 0.04354  0.00126  53  ILE A O   
479  C  CB  . ILE A 53  ? 0.18190 0.35533 0.28844 0.03293  0.04558  -0.00893 53  ILE A CB  
480  C  CG1 . ILE A 53  ? 0.21975 0.38224 0.28469 0.05067  0.02033  0.01388  53  ILE A CG1 
481  C  CG2 . ILE A 53  ? 0.20693 0.35358 0.30589 0.03044  0.05276  -0.03052 53  ILE A CG2 
482  C  CD1 . ILE A 53  ? 0.27305 0.41291 0.35347 0.06572  -0.05707 0.05337  53  ILE A CD1 
483  N  N   . PHE A 54  ? 0.14335 0.28315 0.23592 -0.02055 -0.00624 -0.00240 54  PHE A N   
484  C  CA  . PHE A 54  ? 0.17957 0.28052 0.23835 -0.01706 0.02247  0.02415  54  PHE A CA  
485  C  C   . PHE A 54  ? 0.15757 0.27622 0.26390 -0.00025 0.04020  0.00621  54  PHE A C   
486  O  O   . PHE A 54  ? 0.20547 0.26726 0.21603 -0.01066 0.03850  0.00188  54  PHE A O   
487  C  CB  . PHE A 54  ? 0.19665 0.30051 0.23752 -0.03276 0.00819  -0.02046 54  PHE A CB  
488  C  CG  . PHE A 54  ? 0.15923 0.27825 0.25954 -0.03426 0.00657  -0.05100 54  PHE A CG  
489  C  CD1 . PHE A 54  ? 0.16374 0.26458 0.26870 -0.05765 -0.01323 -0.00090 54  PHE A CD1 
490  C  CD2 . PHE A 54  ? 0.18794 0.27225 0.29601 -0.03446 0.08246  -0.01257 54  PHE A CD2 
491  C  CE1 . PHE A 54  ? 0.12856 0.25954 0.31475 -0.00805 -0.00939 0.01384  54  PHE A CE1 
492  C  CE2 . PHE A 54  ? 0.25910 0.24837 0.27266 -0.02638 0.03097  -0.01064 54  PHE A CE2 
493  C  CZ  . PHE A 54  ? 0.19715 0.27480 0.25990 -0.01976 0.02801  -0.01065 54  PHE A CZ  
494  N  N   . TYR A 55  ? 0.15487 0.24886 0.26545 -0.00766 0.03141  -0.01981 55  TYR A N   
495  C  CA  . TYR A 55  ? 0.21110 0.24286 0.24938 -0.02966 -0.00433 0.00267  55  TYR A CA  
496  C  C   . TYR A 55  ? 0.18030 0.28932 0.24710 -0.05859 0.01371  0.00070  55  TYR A C   
497  O  O   . TYR A 55  ? 0.19608 0.30405 0.22245 -0.04769 0.02865  0.01477  55  TYR A O   
498  C  CB  . TYR A 55  ? 0.13629 0.22323 0.25001 0.01159  0.01428  -0.02120 55  TYR A CB  
499  C  CG  . TYR A 55  ? 0.13604 0.23395 0.20776 -0.00080 -0.00027 -0.01514 55  TYR A CG  
500  C  CD1 . TYR A 55  ? 0.19848 0.23096 0.19707 -0.01626 0.03980  -0.00934 55  TYR A CD1 
501  C  CD2 . TYR A 55  ? 0.19903 0.25308 0.23953 0.01093  -0.00245 0.00537  55  TYR A CD2 
502  C  CE1 . TYR A 55  ? 0.18692 0.23259 0.20072 -0.00047 0.02301  -0.00377 55  TYR A CE1 
503  C  CE2 . TYR A 55  ? 0.18446 0.29041 0.30311 -0.00370 -0.02115 0.07268  55  TYR A CE2 
504  C  CZ  . TYR A 55  ? 0.22673 0.28274 0.21973 0.00375  -0.02537 0.06543  55  TYR A CZ  
505  O  OH  . TYR A 55  ? 0.18212 0.32513 0.27342 0.00480  -0.03407 0.07460  55  TYR A OH  
506  N  N   . ILE A 56  ? 0.14495 0.28727 0.28489 -0.07298 0.06838  -0.03048 56  ILE A N   
507  C  CA  . ILE A 56  ? 0.14758 0.31691 0.26253 -0.03087 0.04519  -0.03078 56  ILE A CA  
508  C  C   . ILE A 56  ? 0.19067 0.29569 0.24382 -0.01552 0.01676  -0.01554 56  ILE A C   
509  O  O   . ILE A 56  ? 0.18775 0.32104 0.25662 -0.04253 0.04456  0.00758  56  ILE A O   
510  C  CB  . ILE A 56  ? 0.15881 0.34665 0.27548 -0.10567 0.00791  -0.01611 56  ILE A CB  
511  C  CG1 . ILE A 56  ? 0.31715 0.33484 0.28116 -0.08226 -0.00551 -0.00694 56  ILE A CG1 
512  C  CG2 . ILE A 56  ? 0.15200 0.38939 0.38926 -0.10478 0.01490  0.02051  56  ILE A CG2 
513  C  CD1 . ILE A 56  ? 0.31484 0.37333 0.34409 -0.05832 -0.01045 -0.04084 56  ILE A CD1 
514  N  N   . TRP A 57  ? 0.24897 0.29546 0.23394 -0.00388 0.00291  -0.00999 57  TRP A N   
515  C  CA  . TRP A 57  ? 0.21573 0.29980 0.22945 -0.04270 -0.00836 -0.01110 57  TRP A CA  
516  C  C   . TRP A 57  ? 0.16367 0.31086 0.24293 -0.01437 0.05106  -0.02156 57  TRP A C   
517  O  O   . TRP A 57  ? 0.22045 0.33238 0.23032 -0.00824 0.05610  -0.01091 57  TRP A O   
518  C  CB  . TRP A 57  ? 0.24175 0.28738 0.25023 -0.02162 0.03484  0.00238  57  TRP A CB  
519  C  CG  . TRP A 57  ? 0.19766 0.30425 0.26271 -0.03682 0.06167  -0.01709 57  TRP A CG  
520  C  CD1 . TRP A 57  ? 0.27941 0.31379 0.28763 0.00570  0.00411  -0.04569 57  TRP A CD1 
521  C  CD2 . TRP A 57  ? 0.21136 0.28741 0.26985 -0.04029 0.07683  -0.02545 57  TRP A CD2 
522  N  NE1 . TRP A 57  ? 0.25834 0.33797 0.32400 -0.02152 0.02976  -0.05451 57  TRP A NE1 
523  C  CE2 . TRP A 57  ? 0.24153 0.31549 0.28994 -0.04343 0.01093  -0.00884 57  TRP A CE2 
524  C  CE3 . TRP A 57  ? 0.19539 0.25751 0.32306 -0.02931 0.04879  0.03050  57  TRP A CE3 
525  C  CZ2 . TRP A 57  ? 0.30364 0.32522 0.27424 -0.06486 -0.02462 0.02712  57  TRP A CZ2 
526  C  CZ3 . TRP A 57  ? 0.29373 0.26985 0.33494 0.03932  -0.05796 0.02547  57  TRP A CZ3 
527  C  CH2 . TRP A 57  ? 0.30224 0.29708 0.32031 0.03076  0.00083  -0.00617 57  TRP A CH2 
528  N  N   . LEU A 58  ? 0.11843 0.26873 0.27903 0.00876  0.03027  0.00278  58  LEU A N   
529  C  CA  . LEU A 58  ? 0.16556 0.30813 0.26865 -0.03290 0.03127  0.03401  58  LEU A CA  
530  C  C   . LEU A 58  ? 0.21039 0.31802 0.28694 -0.06491 0.04287  0.03622  58  LEU A C   
531  O  O   . LEU A 58  ? 0.24026 0.33146 0.26920 -0.00559 0.01380  0.03249  58  LEU A O   
532  C  CB  . LEU A 58  ? 0.18823 0.30275 0.24391 -0.02734 -0.00093 0.02018  58  LEU A CB  
533  C  CG  . LEU A 58  ? 0.19320 0.31164 0.24071 -0.04738 0.00607  -0.02119 58  LEU A CG  
534  C  CD1 . LEU A 58  ? 0.23682 0.34443 0.26644 -0.07548 0.01157  -0.03485 58  LEU A CD1 
535  C  CD2 . LEU A 58  ? 0.20977 0.32861 0.25156 -0.02426 0.03059  -0.02309 58  LEU A CD2 
536  N  N   . ILE A 59  ? 0.18027 0.30645 0.28724 -0.04955 0.03996  0.01209  59  ILE A N   
537  C  CA  . ILE A 59  ? 0.24195 0.30163 0.35525 -0.01661 0.08291  0.02554  59  ILE A CA  
538  C  C   . ILE A 59  ? 0.24857 0.31178 0.33123 -0.03013 0.06347  0.00444  59  ILE A C   
539  O  O   . ILE A 59  ? 0.31953 0.36084 0.27489 -0.02061 0.05755  0.05833  59  ILE A O   
540  C  CB  . ILE A 59  ? 0.26398 0.30111 0.34049 -0.03692 0.08794  0.02922  59  ILE A CB  
541  C  CG1 . ILE A 59  ? 0.26976 0.28082 0.34510 -0.04241 -0.01025 -0.00831 59  ILE A CG1 
542  C  CG2 . ILE A 59  ? 0.30676 0.33689 0.29687 -0.03704 0.10698  0.00464  59  ILE A CG2 
543  C  CD1 . ILE A 59  ? 0.28568 0.32277 0.37174 -0.03674 0.03341  -0.03037 59  ILE A CD1 
544  N  N   . ILE A 60  ? 0.26200 0.31376 0.28394 -0.02369 0.10298  -0.02062 60  ILE A N   
545  C  CA  . ILE A 60  ? 0.26947 0.33432 0.30557 0.00693  0.08766  0.02423  60  ILE A CA  
546  C  C   . ILE A 60  ? 0.25728 0.36994 0.29051 -0.02585 0.13150  -0.01150 60  ILE A C   
547  O  O   . ILE A 60  ? 0.39249 0.39341 0.27053 -0.08045 0.10753  -0.00116 60  ILE A O   
548  C  CB  . ILE A 60  ? 0.20347 0.37275 0.34582 0.02425  0.05960  -0.01885 60  ILE A CB  
549  C  CG1 . ILE A 60  ? 0.16889 0.36829 0.34757 -0.01091 0.07451  0.00210  60  ILE A CG1 
550  C  CG2 . ILE A 60  ? 0.29764 0.39542 0.40944 0.01673  0.14779  -0.02731 60  ILE A CG2 
551  C  CD1 . ILE A 60  ? 0.17905 0.37556 0.43268 0.02929  0.10132  0.03637  60  ILE A CD1 
552  N  N   . THR A 61  ? 0.30617 0.37199 0.25434 -0.07018 0.07116  -0.00576 61  THR A N   
553  C  CA  . THR A 61  ? 0.40751 0.36863 0.25816 -0.06859 0.06257  -0.01050 61  THR A CA  
554  C  C   . THR A 61  ? 0.36162 0.44357 0.24135 -0.09268 0.06577  0.02236  61  THR A C   
555  O  O   . THR A 61  ? 0.38668 0.46125 0.25146 -0.07738 0.04845  0.00073  61  THR A O   
556  C  CB  . THR A 61  ? 0.47197 0.36854 0.21302 -0.03401 0.01562  0.01443  61  THR A CB  
557  O  OG1 . THR A 61  ? 0.42192 0.39412 0.26122 -0.00063 0.04628  -0.00167 61  THR A OG1 
558  C  CG2 . THR A 61  ? 0.52072 0.37946 0.29701 -0.03614 -0.05110 0.01896  61  THR A CG2 
559  N  N   . LEU A 62  ? 0.33027 0.46789 0.30100 -0.09390 0.03149  0.08740  62  LEU A N   
560  C  CA  . LEU A 62  ? 0.33652 0.52508 0.29917 -0.07714 -0.01841 0.11061  62  LEU A CA  
561  C  C   . LEU A 62  ? 0.45292 0.57871 0.34692 -0.07407 -0.04936 0.14259  62  LEU A C   
562  O  O   . LEU A 62  ? 0.57439 0.61051 0.42357 -0.11540 -0.09608 0.16352  62  LEU A O   
563  C  CB  . LEU A 62  ? 0.30021 0.52284 0.37309 -0.07270 0.00900  0.08272  62  LEU A CB  
564  C  CG  . LEU A 62  ? 0.31741 0.51201 0.35659 -0.08074 0.00532  0.09064  62  LEU A CG  
565  C  CD1 . LEU A 62  ? 0.36505 0.50136 0.41190 -0.03385 0.02661  0.08993  62  LEU A CD1 
566  C  CD2 . LEU A 62  ? 0.33473 0.52554 0.37825 -0.10158 -0.01407 0.03893  62  LEU A CD2 
567  N  N   . GLN A 63  ? 0.40823 0.58536 0.39062 -0.09385 0.03816  0.17368  63  GLN A N   
568  C  CA  . GLN A 63  ? 0.51109 0.60721 0.41381 -0.08745 0.00232  0.17817  63  GLN A CA  
569  C  C   . GLN A 63  ? 0.59621 0.64328 0.48931 -0.04512 0.06130  0.18102  63  GLN A C   
570  O  O   . GLN A 63  ? 0.69479 0.64533 0.46221 -0.07286 0.03092  0.23653  63  GLN A O   
571  C  CB  . GLN A 63  ? 0.47227 0.62607 0.42466 -0.11259 0.03022  0.17674  63  GLN A CB  
572  C  CG  . GLN A 63  ? 0.49907 0.62933 0.46138 -0.10656 -0.05686 0.08435  63  GLN A CG  
573  C  CD  . GLN A 63  ? 0.55243 0.65636 0.59679 -0.07297 -0.11621 0.00915  63  GLN A CD  
574  O  OE1 . GLN A 63  ? 0.50011 0.65711 0.50999 -0.11236 -0.07118 -0.01603 63  GLN A OE1 
575  N  NE2 . GLN A 63  ? 0.65991 0.65461 0.73853 -0.00386 -0.13102 -0.00379 63  GLN A NE2 
576  N  N   . SER A 64  ? 0.61634 0.65943 0.52035 -0.03097 0.13834  0.08413  64  SER A N   
577  C  CA  . SER A 64  ? 0.71891 0.69251 0.59374 -0.01664 0.08724  0.01108  64  SER A CA  
578  C  C   . SER A 64  ? 0.75342 0.70404 0.61072 -0.02686 0.09335  -0.00775 64  SER A C   
579  O  O   . SER A 64  ? 0.77960 0.70808 0.62758 -0.02844 0.11027  0.03839  64  SER A O   
580  C  CB  . SER A 64  ? 0.75637 0.71025 0.62904 0.03911  0.02408  -0.00181 64  SER A CB  
581  O  OG  . SER A 64  ? 0.83293 0.72616 0.63082 0.06783  -0.02566 -0.00965 64  SER A OG  
582  N  N   . ILE A 65  ? 0.71994 0.71456 0.64215 -0.05105 0.09395  -0.04656 65  ILE A N   
583  C  CA  . ILE A 65  ? 0.76504 0.73066 0.66572 -0.03288 0.06564  -0.04571 65  ILE A CA  
584  C  C   . ILE A 65  ? 0.75475 0.74508 0.63449 -0.05355 0.04554  -0.04704 65  ILE A C   
585  O  O   . ILE A 65  ? 0.68958 0.75087 0.70172 -0.07435 0.02833  -0.09341 65  ILE A O   
586  C  CB  . ILE A 65  ? 0.70342 0.73724 0.70161 -0.01267 0.03075  -0.03217 65  ILE A CB  
587  N  N   . ASN A 66  ? 0.77104 0.74884 0.61614 -0.09437 0.04826  -0.01151 66  ASN A N   
588  C  CA  . ASN A 66  ? 0.76663 0.75490 0.66054 -0.09649 0.02284  0.03517  66  ASN A CA  
589  C  C   . ASN A 66  ? 0.72389 0.74909 0.63419 -0.10416 -0.00051 0.06027  66  ASN A C   
590  O  O   . ASN A 66  ? 0.77731 0.76066 0.73835 -0.13544 0.03095  0.05332  66  ASN A O   
591  C  CB  . ASN A 66  ? 0.80313 0.77978 0.76106 -0.06224 0.00104  0.05129  66  ASN A CB  
592  C  CG  . ASN A 66  ? 0.81716 0.79479 0.86133 -0.02750 -0.00353 0.04171  66  ASN A CG  
593  O  OD1 . ASN A 66  ? 0.79323 0.80880 0.90639 -0.00027 -0.02454 0.03429  66  ASN A OD1 
594  N  ND2 . ASN A 66  ? 0.82243 0.79618 0.89900 -0.01714 0.02653  0.04651  66  ASN A ND2 
595  N  N   . GLU A 67  ? 0.55878 0.71312 0.49703 -0.07376 0.04829  0.10402  67  GLU A N   
596  C  CA  . GLU A 67  ? 0.49941 0.69177 0.36362 0.02796  0.10916  0.10484  67  GLU A CA  
597  C  C   . GLU A 67  ? 0.34375 0.65036 0.28911 0.02186  -0.01690 0.10067  67  GLU A C   
598  O  O   . GLU A 67  ? 0.34072 0.68509 0.27466 0.04498  0.04248  0.11096  67  GLU A O   
599  C  CB  . GLU A 67  ? 0.61554 0.70772 0.48231 0.03909  0.07097  0.08329  67  GLU A CB  
600  C  CG  . GLU A 67  ? 0.67295 0.71419 0.58412 0.03661  0.00425  0.07753  67  GLU A CG  
601  C  CD  . GLU A 67  ? 0.68172 0.73138 0.60479 0.03076  0.02977  0.06434  67  GLU A CD  
602  O  OE1 . GLU A 67  ? 0.72293 0.72700 0.59948 0.03006  0.02616  0.02836  67  GLU A OE1 
603  O  OE2 . GLU A 67  ? 0.53964 0.73085 0.58499 0.04193  0.09582  0.09583  67  GLU A OE2 
604  N  N   . ASP A 68  ? 0.32990 0.58157 0.25144 0.09936  0.04153  0.05153  68  ASP A N   
605  C  CA  . ASP A 68  ? 0.21120 0.50081 0.20034 0.06552  0.03373  0.07177  68  ASP A CA  
606  C  C   . ASP A 68  ? 0.31141 0.45257 0.19786 0.07509  0.00240  0.04490  68  ASP A C   
607  O  O   . ASP A 68  ? 0.48941 0.41349 0.20801 0.14174  0.05287  0.03265  68  ASP A O   
608  C  CB  . ASP A 68  ? 0.33188 0.45429 0.27615 0.06456  -0.04601 0.02986  68  ASP A CB  
609  C  CG  . ASP A 68  ? 0.31245 0.37541 0.26395 0.09118  0.02481  0.04488  68  ASP A CG  
610  O  OD1 . ASP A 68  ? 0.34244 0.33165 0.23374 0.01920  -0.03662 -0.01307 68  ASP A OD1 
611  O  OD2 . ASP A 68  ? 0.49374 0.45233 0.30738 -0.03582 -0.01287 0.01173  68  ASP A OD2 
612  N  N   . ILE A 69  ? 0.23726 0.42535 0.22313 0.03153  0.00601  0.02973  69  ILE A N   
613  C  CA  . ILE A 69  ? 0.28128 0.42727 0.23618 0.06197  0.03431  0.06007  69  ILE A CA  
614  C  C   . ILE A 69  ? 0.26502 0.31234 0.24463 0.08845  -0.03632 0.01479  69  ILE A C   
615  O  O   . ILE A 69  ? 0.24690 0.28830 0.23252 0.02856  0.00874  0.01713  69  ILE A O   
616  C  CB  . ILE A 69  ? 0.37804 0.49607 0.25613 0.01105  -0.00747 0.03389  69  ILE A CB  
617  C  CG1 . ILE A 69  ? 0.44228 0.47025 0.29032 -0.04216 0.00295  0.03776  69  ILE A CG1 
618  C  CG2 . ILE A 69  ? 0.48834 0.55291 0.28844 -0.00400 0.11582  0.05739  69  ILE A CG2 
619  C  CD1 . ILE A 69  ? 0.52583 0.45511 0.31067 -0.04512 -0.07431 0.04394  69  ILE A CD1 
620  N  N   . THR A 70  ? 0.28517 0.23242 0.24257 0.06749  -0.01017 -0.01435 70  THR A N   
621  C  CA  . THR A 70  ? 0.17603 0.26328 0.21077 0.04982  -0.00402 -0.00505 70  THR A CA  
622  C  C   . THR A 70  ? 0.24847 0.25129 0.16799 0.04128  -0.03438 -0.00187 70  THR A C   
623  O  O   . THR A 70  ? 0.20085 0.24843 0.20588 0.03439  -0.01840 -0.00288 70  THR A O   
624  C  CB  . THR A 70  ? 0.14352 0.27237 0.27194 0.04715  -0.00012 0.00855  70  THR A CB  
625  O  OG1 . THR A 70  ? 0.25602 0.22353 0.24831 0.03170  -0.01913 0.00088  70  THR A OG1 
626  C  CG2 . THR A 70  ? 0.22666 0.29060 0.25248 0.04995  0.04224  0.04201  70  THR A CG2 
627  N  N   . TYR A 71  ? 0.21847 0.23065 0.21374 0.03599  0.00735  -0.02423 71  TYR A N   
628  C  CA  . TYR A 71  ? 0.26128 0.21739 0.21831 0.03613  -0.02315 -0.01991 71  TYR A CA  
629  C  C   . TYR A 71  ? 0.28542 0.20934 0.20438 0.03603  0.01312  -0.03186 71  TYR A C   
630  O  O   . TYR A 71  ? 0.22182 0.22046 0.21426 0.00939  0.01986  -0.00563 71  TYR A O   
631  C  CB  . TYR A 71  ? 0.22494 0.22178 0.24834 0.03265  -0.03292 -0.03498 71  TYR A CB  
632  C  CG  . TYR A 71  ? 0.29285 0.26293 0.25964 0.04427  0.05652  -0.02434 71  TYR A CG  
633  C  CD1 . TYR A 71  ? 0.39972 0.31493 0.19007 0.03323  0.05310  -0.01538 71  TYR A CD1 
634  C  CD2 . TYR A 71  ? 0.29798 0.27907 0.26726 0.08401  0.04811  -0.02735 71  TYR A CD2 
635  C  CE1 . TYR A 71  ? 0.36840 0.34803 0.23873 0.08021  0.05347  -0.03796 71  TYR A CE1 
636  C  CE2 . TYR A 71  ? 0.36922 0.33842 0.26265 0.02821  0.05204  -0.05124 71  TYR A CE2 
637  C  CZ  . TYR A 71  ? 0.29980 0.38357 0.33633 0.07202  0.09944  -0.05437 71  TYR A CZ  
638  O  OH  . TYR A 71  ? 0.27625 0.44608 0.45144 0.09725  0.12969  -0.03356 71  TYR A OH  
639  N  N   . VAL A 72  ? 0.20938 0.24670 0.22366 0.04264  -0.02090 -0.02756 72  VAL A N   
640  C  CA  . VAL A 72  ? 0.16672 0.25953 0.21358 -0.01289 0.02000  -0.01263 72  VAL A CA  
641  C  C   . VAL A 72  ? 0.18488 0.23166 0.23992 0.02264  0.02480  -0.00126 72  VAL A C   
642  O  O   . VAL A 72  ? 0.21860 0.24706 0.22472 0.03299  0.00266  -0.00480 72  VAL A O   
643  C  CB  . VAL A 72  ? 0.22740 0.24883 0.21290 0.00160  0.03808  -0.01781 72  VAL A CB  
644  C  CG1 . VAL A 72  ? 0.24307 0.26403 0.26953 -0.01546 0.01689  -0.04715 72  VAL A CG1 
645  C  CG2 . VAL A 72  ? 0.27133 0.29396 0.22492 0.06694  0.04813  0.00435  72  VAL A CG2 
646  N  N   . ARG A 73  ? 0.18873 0.21120 0.21004 0.02690  0.02301  -0.00161 73  ARG A N   
647  C  CA  . ARG A 73  ? 0.16956 0.21121 0.19659 0.00795  0.02326  -0.00146 73  ARG A CA  
648  C  C   . ARG A 73  ? 0.18938 0.19528 0.21726 0.02447  -0.00504 0.00683  73  ARG A C   
649  O  O   . ARG A 73  ? 0.20330 0.22636 0.19059 0.04583  -0.00196 -0.00841 73  ARG A O   
650  C  CB  . ARG A 73  ? 0.17403 0.20888 0.18974 0.04833  0.02691  -0.00679 73  ARG A CB  
651  C  CG  . ARG A 73  ? 0.16574 0.21393 0.22298 0.03515  0.01463  0.01734  73  ARG A CG  
652  C  CD  . ARG A 73  ? 0.16179 0.22939 0.25171 0.02572  -0.00830 0.01522  73  ARG A CD  
653  N  NE  . ARG A 73  ? 0.20170 0.17554 0.26691 0.00425  -0.01255 0.00676  73  ARG A NE  
654  C  CZ  . ARG A 73  ? 0.18377 0.21741 0.19559 -0.00155 0.02418  -0.00027 73  ARG A CZ  
655  N  NH1 . ARG A 73  ? 0.16629 0.24282 0.24024 0.02201  0.01061  -0.01730 73  ARG A NH1 
656  N  NH2 . ARG A 73  ? 0.19841 0.21826 0.23304 -0.01722 0.01835  0.00960  73  ARG A NH2 
657  N  N   . TYR A 74  ? 0.17633 0.18833 0.24106 0.03369  0.00898  0.00514  74  TYR A N   
658  C  CA  . TYR A 74  ? 0.19210 0.19564 0.23079 -0.00936 -0.01335 -0.00010 74  TYR A CA  
659  C  C   . TYR A 74  ? 0.12903 0.22879 0.23003 0.03295  0.02464  -0.04317 74  TYR A C   
660  O  O   . TYR A 74  ? 0.22523 0.23452 0.19092 0.03812  0.01460  -0.00884 74  TYR A O   
661  C  CB  . TYR A 74  ? 0.21581 0.19348 0.20979 0.02352  -0.01537 -0.01423 74  TYR A CB  
662  C  CG  . TYR A 74  ? 0.21601 0.21377 0.20795 0.04227  0.00005  -0.01180 74  TYR A CG  
663  C  CD1 . TYR A 74  ? 0.21639 0.23388 0.22081 -0.00033 0.00436  -0.00872 74  TYR A CD1 
664  C  CD2 . TYR A 74  ? 0.20263 0.19239 0.21843 0.01296  -0.00882 -0.02424 74  TYR A CD2 
665  C  CE1 . TYR A 74  ? 0.16008 0.25164 0.25786 0.00615  0.00372  -0.03567 74  TYR A CE1 
666  C  CE2 . TYR A 74  ? 0.21318 0.20939 0.24029 0.01428  -0.01758 -0.02631 74  TYR A CE2 
667  C  CZ  . TYR A 74  ? 0.17646 0.22557 0.27033 -0.00979 -0.03057 -0.02722 74  TYR A CZ  
668  O  OH  . TYR A 74  ? 0.22455 0.22149 0.21020 0.00685  0.00209  -0.02532 74  TYR A OH  
669  N  N   . PHE A 75  ? 0.10861 0.24166 0.24767 0.04674  0.00536  -0.02332 75  PHE A N   
670  C  CA  . PHE A 75  ? 0.14708 0.27880 0.23531 0.03663  0.01502  -0.00534 75  PHE A CA  
671  C  C   . PHE A 75  ? 0.19270 0.24560 0.23341 0.02299  -0.00122 -0.00629 75  PHE A C   
672  O  O   . PHE A 75  ? 0.22137 0.28037 0.23499 0.06587  -0.01578 -0.00105 75  PHE A O   
673  C  CB  . PHE A 75  ? 0.21224 0.30365 0.25581 0.02366  0.02295  0.01694  75  PHE A CB  
674  C  CG  . PHE A 75  ? 0.27935 0.30370 0.27343 0.10855  0.00379  -0.00305 75  PHE A CG  
675  C  CD1 . PHE A 75  ? 0.45868 0.36204 0.31996 0.09864  0.15576  -0.07825 75  PHE A CD1 
676  C  CD2 . PHE A 75  ? 0.33809 0.35025 0.20929 0.11100  -0.00055 -0.01620 75  PHE A CD2 
677  C  CE1 . PHE A 75  ? 0.54058 0.39212 0.34983 0.06188  0.04511  -0.08432 75  PHE A CE1 
678  C  CE2 . PHE A 75  ? 0.46467 0.39442 0.20147 0.07212  -0.00972 -0.03590 75  PHE A CE2 
679  C  CZ  . PHE A 75  ? 0.42880 0.40565 0.32535 0.07969  -0.13299 -0.06631 75  PHE A CZ  
680  N  N   . ASP A 76  ? 0.17498 0.22871 0.21308 0.02882  0.02155  -0.00712 76  ASP A N   
681  C  CA  . ASP A 76  ? 0.16859 0.22713 0.20761 0.03016  0.02224  -0.00176 76  ASP A CA  
682  C  C   . ASP A 76  ? 0.10374 0.21359 0.23260 0.00997  0.01891  -0.00195 76  ASP A C   
683  O  O   . ASP A 76  ? 0.19522 0.22534 0.19413 0.00819  -0.01366 0.01579  76  ASP A O   
684  C  CB  . ASP A 76  ? 0.20193 0.19688 0.25960 0.04663  0.00396  -0.00269 76  ASP A CB  
685  C  CG  . ASP A 76  ? 0.23653 0.21242 0.23996 -0.00782 -0.01521 0.01274  76  ASP A CG  
686  O  OD1 . ASP A 76  ? 0.26303 0.23803 0.24704 -0.03275 0.01588  0.00535  76  ASP A OD1 
687  O  OD2 . ASP A 76  ? 0.31480 0.22557 0.23322 0.04381  0.01291  -0.01594 76  ASP A OD2 
688  N  N   . TRP A 77  ? 0.11563 0.20950 0.27188 0.01652  0.01680  -0.01809 77  TRP A N   
689  C  CA  . TRP A 77  ? 0.14440 0.19163 0.23420 0.02788  -0.02852 -0.00672 77  TRP A CA  
690  C  C   . TRP A 77  ? 0.15708 0.19338 0.23303 0.02590  0.00851  -0.03217 77  TRP A C   
691  O  O   . TRP A 77  ? 0.18196 0.19824 0.19141 0.00292  0.00572  -0.00692 77  TRP A O   
692  C  CB  . TRP A 77  ? 0.15080 0.20691 0.20007 0.01258  -0.02623 0.02187  77  TRP A CB  
693  C  CG  . TRP A 77  ? 0.18342 0.19399 0.20036 0.04119  -0.00707 0.02392  77  TRP A CG  
694  C  CD1 . TRP A 77  ? 0.21919 0.18656 0.23685 0.04672  0.04350  0.01913  77  TRP A CD1 
695  C  CD2 . TRP A 77  ? 0.16787 0.22792 0.20510 0.05607  0.00438  0.00126  77  TRP A CD2 
696  N  NE1 . TRP A 77  ? 0.17542 0.19556 0.28132 -0.00240 0.05219  0.02972  77  TRP A NE1 
697  C  CE2 . TRP A 77  ? 0.16701 0.22958 0.26021 0.06039  0.00950  0.05054  77  TRP A CE2 
698  C  CE3 . TRP A 77  ? 0.18114 0.24331 0.21755 0.05565  -0.00910 -0.02858 77  TRP A CE3 
699  C  CZ2 . TRP A 77  ? 0.17083 0.29577 0.24341 0.06581  -0.00506 0.03951  77  TRP A CZ2 
700  C  CZ3 . TRP A 77  ? 0.23592 0.28617 0.18115 0.06971  -0.02004 0.00025  77  TRP A CZ3 
701  C  CH2 . TRP A 77  ? 0.17691 0.30809 0.23943 0.04580  0.02871  -0.00384 77  TRP A CH2 
702  N  N   . VAL A 78  ? 0.19516 0.18561 0.21248 0.03557  -0.01103 0.00149  78  VAL A N   
703  C  CA  . VAL A 78  ? 0.24454 0.20507 0.19907 0.05529  -0.00768 0.00115  78  VAL A CA  
704  C  C   . VAL A 78  ? 0.26714 0.19881 0.23267 0.05457  -0.02149 0.00731  78  VAL A C   
705  O  O   . VAL A 78  ? 0.19733 0.20305 0.23990 0.02887  -0.00893 0.00348  78  VAL A O   
706  C  CB  . VAL A 78  ? 0.20800 0.20566 0.22069 0.07707  0.00837  -0.00644 78  VAL A CB  
707  C  CG1 . VAL A 78  ? 0.22638 0.23345 0.24069 0.07132  0.02674  -0.00894 78  VAL A CG1 
708  C  CG2 . VAL A 78  ? 0.34754 0.21920 0.25968 0.03501  0.01766  0.01020  78  VAL A CG2 
709  N  N   . LEU A 79  ? 0.26102 0.21497 0.19181 0.06391  0.00870  -0.01499 79  LEU A N   
710  C  CA  . LEU A 79  ? 0.19655 0.24352 0.18905 0.03087  -0.00852 -0.00613 79  LEU A CA  
711  C  C   . LEU A 79  ? 0.18532 0.24451 0.17932 0.00217  -0.00484 -0.03190 79  LEU A C   
712  O  O   . LEU A 79  ? 0.24378 0.24078 0.20679 0.03127  -0.03027 -0.01345 79  LEU A O   
713  C  CB  . LEU A 79  ? 0.15025 0.26897 0.26840 0.04855  0.02190  -0.01627 79  LEU A CB  
714  C  CG  . LEU A 79  ? 0.21936 0.29486 0.27263 0.04000  0.02301  0.04639  79  LEU A CG  
715  C  CD1 . LEU A 79  ? 0.15687 0.30874 0.33905 0.01269  0.03954  0.02390  79  LEU A CD1 
716  C  CD2 . LEU A 79  ? 0.26199 0.30626 0.35532 0.10466  0.05249  0.08311  79  LEU A CD2 
717  N  N   . THR A 80  ? 0.15345 0.22249 0.22389 0.01518  -0.03964 -0.00844 80  THR A N   
718  C  CA  . THR A 80  ? 0.15459 0.20347 0.19633 0.00496  -0.00816 -0.02045 80  THR A CA  
719  C  C   . THR A 80  ? 0.14854 0.19141 0.19368 -0.00372 -0.01349 0.00011  80  THR A C   
720  O  O   . THR A 80  ? 0.19824 0.19688 0.18167 0.00669  0.00593  -0.00585 80  THR A O   
721  C  CB  . THR A 80  ? 0.17206 0.21100 0.19748 -0.02047 0.00224  0.00180  80  THR A CB  
722  O  OG1 . THR A 80  ? 0.19785 0.19858 0.20025 0.00643  0.00348  -0.00594 80  THR A OG1 
723  C  CG2 . THR A 80  ? 0.12430 0.24366 0.25437 0.02188  -0.01271 -0.00542 80  THR A CG2 
724  N  N   . THR A 81  ? 0.17509 0.18322 0.22210 -0.01088 -0.02022 0.00700  81  THR A N   
725  C  CA  . THR A 81  ? 0.20711 0.20529 0.19653 0.00718  -0.03597 -0.00544 81  THR A CA  
726  C  C   . THR A 81  ? 0.13417 0.18782 0.23189 0.05271  -0.00633 -0.02005 81  THR A C   
727  O  O   . THR A 81  ? 0.19250 0.17765 0.20392 0.00792  -0.00570 -0.01532 81  THR A O   
728  C  CB  . THR A 81  ? 0.19197 0.18638 0.19014 0.02875  -0.02467 -0.00800 81  THR A CB  
729  O  OG1 . THR A 81  ? 0.18437 0.16503 0.21807 0.01214  -0.00819 -0.01136 81  THR A OG1 
730  C  CG2 . THR A 81  ? 0.22228 0.18514 0.20815 0.04195  -0.04452 -0.00154 81  THR A CG2 
731  N  N   . PRO A 82  ? 0.14961 0.21532 0.19174 0.03099  0.01765  -0.00531 82  PRO A N   
732  C  CA  . PRO A 82  ? 0.22815 0.19905 0.20120 0.03004  0.00408  -0.03001 82  PRO A CA  
733  C  C   . PRO A 82  ? 0.26140 0.17835 0.19728 0.01434  -0.00055 0.02977  82  PRO A C   
734  O  O   . PRO A 82  ? 0.22845 0.20450 0.18169 -0.00021 -0.00883 0.01775  82  PRO A O   
735  C  CB  . PRO A 82  ? 0.25659 0.17759 0.22559 0.03225  0.00172  0.01772  82  PRO A CB  
736  C  CG  . PRO A 82  ? 0.24088 0.20839 0.21532 0.00332  0.01069  0.05208  82  PRO A CG  
737  C  CD  . PRO A 82  ? 0.19244 0.20442 0.19838 0.06562  0.01046  0.00026  82  PRO A CD  
738  N  N   . VAL A 83  ? 0.23723 0.18844 0.18112 0.00856  -0.00150 0.00891  83  VAL A N   
739  C  CA  . VAL A 83  ? 0.17276 0.21612 0.20483 0.01524  -0.01050 0.02039  83  VAL A CA  
740  C  C   . VAL A 83  ? 0.15897 0.20395 0.20590 0.01386  -0.03403 0.00017  83  VAL A C   
741  O  O   . VAL A 83  ? 0.20796 0.20655 0.19725 -0.01471 -0.02110 -0.00876 83  VAL A O   
742  C  CB  . VAL A 83  ? 0.21545 0.23352 0.21737 0.02110  -0.01627 0.00653  83  VAL A CB  
743  C  CG1 . VAL A 83  ? 0.23838 0.24562 0.20624 -0.02398 -0.02217 -0.02474 83  VAL A CG1 
744  C  CG2 . VAL A 83  ? 0.14482 0.26239 0.28731 -0.00267 -0.03410 -0.03498 83  VAL A CG2 
745  N  N   . MET A 84  ? 0.17088 0.19046 0.21596 0.00659  -0.03179 0.00048  84  MET A N   
746  C  CA  . MET A 84  ? 0.14844 0.20225 0.22283 0.00104  0.00431  0.00519  84  MET A CA  
747  C  C   . MET A 84  ? 0.17881 0.19574 0.19508 -0.01085 0.00821  0.00050  84  MET A C   
748  O  O   . MET A 84  ? 0.20329 0.20656 0.19183 -0.01496 0.02512  -0.01166 84  MET A O   
749  C  CB  . MET A 84  ? 0.18109 0.18320 0.19781 -0.00892 -0.01121 0.01617  84  MET A CB  
750  C  CG  . MET A 84  ? 0.19897 0.17999 0.18828 -0.03401 -0.02544 0.02080  84  MET A CG  
751  S  SD  . MET A 84  ? 0.20774 0.21775 0.22752 -0.00871 -0.00780 0.01002  84  MET A SD  
752  C  CE  . MET A 84  ? 0.19956 0.21586 0.33442 0.06379  0.00538  0.01098  84  MET A CE  
753  N  N   . LEU A 85  ? 0.16267 0.18162 0.20688 -0.02903 0.01676  0.00773  85  LEU A N   
754  C  CA  . LEU A 85  ? 0.20711 0.18727 0.19810 -0.04393 -0.01272 -0.01367 85  LEU A CA  
755  C  C   . LEU A 85  ? 0.25579 0.19483 0.22137 0.00866  -0.03240 -0.04734 85  LEU A C   
756  O  O   . LEU A 85  ? 0.24155 0.21446 0.19877 -0.02187 -0.01677 -0.03541 85  LEU A O   
757  C  CB  . LEU A 85  ? 0.18231 0.18613 0.22018 -0.02873 -0.00955 -0.03294 85  LEU A CB  
758  C  CG  . LEU A 85  ? 0.16591 0.20466 0.19379 -0.00878 -0.02855 -0.03086 85  LEU A CG  
759  C  CD1 . LEU A 85  ? 0.28429 0.21280 0.22046 -0.03264 -0.01196 -0.02746 85  LEU A CD1 
760  C  CD2 . LEU A 85  ? 0.25943 0.20420 0.21082 0.01408  -0.04588 -0.02864 85  LEU A CD2 
761  N  N   . LEU A 86  ? 0.22090 0.21287 0.17629 -0.01752 -0.00731 0.01360  86  LEU A N   
762  C  CA  . LEU A 86  ? 0.27827 0.22168 0.19194 0.00779  -0.05044 0.00789  86  LEU A CA  
763  C  C   . LEU A 86  ? 0.20477 0.22779 0.20858 0.00606  0.00989  0.01301  86  LEU A C   
764  O  O   . LEU A 86  ? 0.19151 0.22095 0.19763 0.00933  0.00385  0.00080  86  LEU A O   
765  C  CB  . LEU A 86  ? 0.28421 0.22740 0.26271 0.01912  -0.04837 -0.00268 86  LEU A CB  
766  C  CG  . LEU A 86  ? 0.33878 0.26809 0.30283 0.01681  0.01529  0.00343  86  LEU A CG  
767  C  CD1 . LEU A 86  ? 0.28053 0.28644 0.44960 0.07656  0.03592  0.00532  86  LEU A CD1 
768  C  CD2 . LEU A 86  ? 0.29927 0.28667 0.38841 0.02778  -0.00596 -0.02905 86  LEU A CD2 
769  N  N   . THR A 87  ? 0.21740 0.22286 0.20703 -0.03391 -0.00570 -0.02488 87  THR A N   
770  C  CA  . THR A 87  ? 0.22502 0.21869 0.22264 -0.02398 0.00289  -0.00274 87  THR A CA  
771  C  C   . THR A 87  ? 0.19476 0.19737 0.21202 -0.00548 0.00951  -0.01063 87  THR A C   
772  O  O   . THR A 87  ? 0.21516 0.24281 0.20031 -0.02280 0.03199  -0.03258 87  THR A O   
773  C  CB  . THR A 87  ? 0.19866 0.25801 0.21182 -0.00482 -0.00495 -0.02007 87  THR A CB  
774  O  OG1 . THR A 87  ? 0.32761 0.23611 0.21509 -0.00263 0.01407  -0.03149 87  THR A OG1 
775  C  CG2 . THR A 87  ? 0.11918 0.28822 0.35300 0.01323  0.00229  -0.05159 87  THR A CG2 
776  N  N   A THR A 88  ? 0.22558 0.19409 0.21378 0.01714  -0.01555 0.01913  88  THR A N   
777  N  N   B THR A 88  ? 0.20068 0.20248 0.24932 -0.02693 -0.03293 0.00087  88  THR A N   
778  C  CA  A THR A 88  ? 0.21838 0.21366 0.15090 0.01886  -0.02344 -0.00339 88  THR A CA  
779  C  CA  B THR A 88  ? 0.24615 0.24519 0.26014 -0.00503 -0.09527 0.01622  88  THR A CA  
780  C  C   A THR A 88  ? 0.17644 0.19740 0.17721 -0.01362 0.05061  0.00178  88  THR A C   
781  C  C   B THR A 88  ? 0.21054 0.20002 0.22552 -0.01384 -0.07114 0.01045  88  THR A C   
782  O  O   A THR A 88  ? 0.12030 0.20324 0.14654 -0.00436 -0.00762 -0.02976 88  THR A O   
783  O  O   B THR A 88  ? 0.25937 0.20183 0.19136 -0.05643 -0.09929 0.01270  88  THR A O   
784  C  CB  A THR A 88  ? 0.16835 0.21219 0.19938 -0.00020 0.01627  0.05257  88  THR A CB  
785  C  CB  B THR A 88  ? 0.32203 0.25959 0.33681 0.00516  -0.10987 0.01490  88  THR A CB  
786  O  OG1 A THR A 88  ? 0.14045 0.26433 0.20515 -0.01666 -0.02672 0.08432  88  THR A OG1 
787  O  OG1 B THR A 88  ? 0.45346 0.30233 0.37751 0.06683  -0.16313 0.00428  88  THR A OG1 
788  C  CG2 A THR A 88  ? 0.17659 0.22859 0.22237 -0.04512 0.00303  0.05103  88  THR A CG2 
789  C  CG2 B THR A 88  ? 0.30882 0.24417 0.33624 -0.01888 -0.11189 0.01001  88  THR A CG2 
790  N  N   . VAL A 89  ? 0.20606 0.17201 0.19490 0.00445  -0.02342 -0.00587 89  VAL A N   
791  C  CA  . VAL A 89  ? 0.20879 0.18941 0.17616 -0.01625 -0.01687 -0.00989 89  VAL A CA  
792  C  C   . VAL A 89  ? 0.17728 0.19748 0.20047 0.01199  0.02188  0.00488  89  VAL A C   
793  O  O   . VAL A 89  ? 0.19819 0.17677 0.20163 -0.01191 0.02186  -0.00548 89  VAL A O   
794  C  CB  . VAL A 89  ? 0.22652 0.19405 0.19714 -0.00394 0.00151  -0.00069 89  VAL A CB  
795  C  CG1 . VAL A 89  ? 0.26943 0.19941 0.21137 -0.00922 0.01611  0.01066  89  VAL A CG1 
796  C  CG2 . VAL A 89  ? 0.25516 0.19751 0.19959 -0.01711 -0.02039 -0.00962 89  VAL A CG2 
797  N  N   . TYR A 90  ? 0.22045 0.19078 0.18944 -0.00705 -0.03115 0.00568  90  TYR A N   
798  C  CA  . TYR A 90  ? 0.16155 0.18856 0.19652 0.00530  -0.01412 -0.01110 90  TYR A CA  
799  C  C   . TYR A 90  ? 0.16208 0.17256 0.21138 0.01033  -0.01914 -0.01722 90  TYR A C   
800  O  O   . TYR A 90  ? 0.18694 0.20531 0.18205 0.01043  -0.01467 -0.01580 90  TYR A O   
801  C  CB  . TYR A 90  ? 0.17586 0.22658 0.19777 0.03754  -0.02028 -0.00519 90  TYR A CB  
802  C  CG  . TYR A 90  ? 0.24632 0.19995 0.18220 0.00970  -0.03460 0.01307  90  TYR A CG  
803  C  CD1 . TYR A 90  ? 0.24272 0.21011 0.17631 0.03665  -0.02706 0.00420  90  TYR A CD1 
804  C  CD2 . TYR A 90  ? 0.20987 0.25121 0.20535 0.01061  -0.01491 0.00410  90  TYR A CD2 
805  C  CE1 . TYR A 90  ? 0.24790 0.25523 0.19026 0.04140  0.02098  0.00113  90  TYR A CE1 
806  C  CE2 . TYR A 90  ? 0.26243 0.22370 0.27153 0.07220  0.01381  0.05262  90  TYR A CE2 
807  C  CZ  . TYR A 90  ? 0.22268 0.25032 0.23538 0.07943  0.04527  0.04588  90  TYR A CZ  
808  O  OH  . TYR A 90  ? 0.27827 0.26636 0.33916 0.08291  0.11263  0.08375  90  TYR A OH  
809  N  N   . PHE A 91  ? 0.19747 0.17104 0.22861 0.02952  -0.02457 -0.00118 91  PHE A N   
810  C  CA  . PHE A 91  ? 0.14447 0.20129 0.20616 0.00319  0.00511  0.01641  91  PHE A CA  
811  C  C   . PHE A 91  ? 0.18811 0.18174 0.20997 -0.00349 -0.01645 0.01117  91  PHE A C   
812  O  O   . PHE A 91  ? 0.22454 0.19426 0.19541 0.00674  0.00068  -0.00947 91  PHE A O   
813  C  CB  . PHE A 91  ? 0.18399 0.20481 0.21456 0.01386  0.00290  0.02534  91  PHE A CB  
814  C  CG  . PHE A 91  ? 0.21514 0.18338 0.22051 0.01315  0.00160  0.02856  91  PHE A CG  
815  C  CD1 . PHE A 91  ? 0.23921 0.18411 0.21807 0.02665  -0.01681 0.00531  91  PHE A CD1 
816  C  CD2 . PHE A 91  ? 0.22210 0.19895 0.32275 0.02133  -0.03596 0.07022  91  PHE A CD2 
817  C  CE1 . PHE A 91  ? 0.20558 0.20327 0.25683 0.04266  0.00209  0.01821  91  PHE A CE1 
818  C  CE2 . PHE A 91  ? 0.20191 0.21334 0.31774 0.01647  -0.04192 0.06367  91  PHE A CE2 
819  C  CZ  . PHE A 91  ? 0.20058 0.25386 0.26360 0.03875  0.00784  0.03993  91  PHE A CZ  
820  N  N   . PHE A 92  ? 0.20018 0.19349 0.21219 0.00271  -0.01827 -0.00473 92  PHE A N   
821  C  CA  . PHE A 92  ? 0.18621 0.22630 0.20824 -0.01445 0.03350  -0.00602 92  PHE A CA  
822  C  C   . PHE A 92  ? 0.17524 0.20637 0.22551 0.00233  -0.01723 -0.00862 92  PHE A C   
823  O  O   . PHE A 92  ? 0.19606 0.22724 0.20425 -0.00643 0.01738  -0.00464 92  PHE A O   
824  C  CB  . PHE A 92  ? 0.19268 0.23675 0.22072 -0.02920 -0.00230 -0.02106 92  PHE A CB  
825  C  CG  . PHE A 92  ? 0.18327 0.26950 0.20391 -0.00419 -0.00706 -0.01838 92  PHE A CG  
826  C  CD1 . PHE A 92  ? 0.21405 0.24752 0.28935 0.03393  -0.04263 0.01189  92  PHE A CD1 
827  C  CD2 . PHE A 92  ? 0.28064 0.40129 0.22779 0.02385  -0.02694 -0.04573 92  PHE A CD2 
828  C  CE1 . PHE A 92  ? 0.21059 0.30714 0.26550 -0.01266 -0.01749 -0.00979 92  PHE A CE1 
829  C  CE2 . PHE A 92  ? 0.22217 0.44345 0.23486 0.05540  -0.03162 -0.03571 92  PHE A CE2 
830  C  CZ  . PHE A 92  ? 0.19772 0.35836 0.27565 0.03927  0.00351  0.02077  92  PHE A CZ  
831  N  N   . GLU A 93  ? 0.14757 0.21779 0.21532 -0.00057 -0.00524 0.01819  93  GLU A N   
832  C  CA  . GLU A 93  ? 0.21090 0.19899 0.22315 0.00254  -0.01386 0.02697  93  GLU A CA  
833  C  C   . GLU A 93  ? 0.22304 0.21343 0.20702 -0.00942 0.00901  -0.01582 93  GLU A C   
834  O  O   . GLU A 93  ? 0.21285 0.24803 0.21104 -0.01178 0.00328  0.00924  93  GLU A O   
835  C  CB  . GLU A 93  ? 0.19873 0.17548 0.24652 0.03011  -0.01925 0.02386  93  GLU A CB  
836  C  CG  . GLU A 93  ? 0.21049 0.20339 0.27464 0.00820  0.04144  0.01309  93  GLU A CG  
837  C  CD  . GLU A 93  ? 0.30554 0.29287 0.26503 0.03070  -0.01782 0.01299  93  GLU A CD  
838  O  OE1 . GLU A 93  ? 0.43317 0.35297 0.34110 -0.02510 -0.02797 0.05733  93  GLU A OE1 
839  O  OE2 . GLU A 93  ? 0.43368 0.37508 0.27269 -0.11067 0.00136  0.01985  93  GLU A OE2 
840  N  N   . TYR A 94  ? 0.21280 0.20345 0.22974 -0.00311 -0.02676 -0.01537 94  TYR A N   
841  C  CA  . TYR A 94  ? 0.15300 0.22454 0.25473 -0.01305 -0.05131 -0.00984 94  TYR A CA  
842  C  C   . TYR A 94  ? 0.16930 0.21561 0.23848 0.02069  -0.03359 0.00593  94  TYR A C   
843  O  O   . TYR A 94  ? 0.24215 0.26352 0.22990 0.01968  -0.00488 -0.04170 94  TYR A O   
844  C  CB  . TYR A 94  ? 0.26170 0.21457 0.19840 -0.09220 0.02371  -0.01847 94  TYR A CB  
845  C  CG  . TYR A 94  ? 0.25326 0.25468 0.18300 -0.03494 -0.01268 -0.00033 94  TYR A CG  
846  C  CD1 . TYR A 94  ? 0.20828 0.26653 0.20659 -0.00897 -0.00027 -0.03920 94  TYR A CD1 
847  C  CD2 . TYR A 94  ? 0.27642 0.25419 0.23280 -0.02852 0.00652  0.00798  94  TYR A CD2 
848  C  CE1 . TYR A 94  ? 0.23995 0.25703 0.23428 -0.01514 0.02714  -0.02203 94  TYR A CE1 
849  C  CE2 . TYR A 94  ? 0.27210 0.25208 0.24988 -0.06301 -0.00756 0.00270  94  TYR A CE2 
850  C  CZ  . TYR A 94  ? 0.24054 0.23313 0.22507 -0.03224 0.00590  -0.01799 94  TYR A CZ  
851  O  OH  . TYR A 94  ? 0.31921 0.22601 0.28824 -0.01508 0.04123  -0.01311 94  TYR A OH  
852  N  N   . MET A 95  ? 0.20298 0.21397 0.26622 0.01659  -0.04907 0.00134  95  MET A N   
853  C  CA  . MET A 95  ? 0.22176 0.27064 0.24311 -0.01170 -0.05174 -0.01840 95  MET A CA  
854  C  C   . MET A 95  ? 0.21289 0.30921 0.20203 0.03926  -0.01038 -0.02518 95  MET A C   
855  O  O   . MET A 95  ? 0.23800 0.33021 0.28174 0.03338  0.00746  -0.07514 95  MET A O   
856  C  CB  . MET A 95  ? 0.33237 0.28462 0.27515 0.04547  -0.08772 -0.02529 95  MET A CB  
857  C  CG  . MET A 95  ? 0.39987 0.31459 0.33957 0.03271  -0.01509 -0.03864 95  MET A CG  
858  S  SD  . MET A 95  ? 0.36587 0.29017 0.29372 0.04487  -0.03887 0.01931  95  MET A SD  
859  C  CE  . MET A 95  ? 0.36137 0.25012 0.27094 0.04591  0.00108  -0.01980 95  MET A CE  
860  N  N   . ASN A 96  ? 0.20887 0.26615 0.24883 0.01180  -0.00793 -0.00901 96  ASN A N   
861  C  CA  . ASN A 96  ? 0.23546 0.30297 0.22756 -0.00137 -0.00874 -0.01136 96  ASN A CA  
862  C  C   . ASN A 96  ? 0.19733 0.38445 0.21591 -0.00738 -0.00962 0.02046  96  ASN A C   
863  O  O   . ASN A 96  ? 0.26463 0.43324 0.26001 -0.04523 0.02666  0.03646  96  ASN A O   
864  C  CB  . ASN A 96  ? 0.19959 0.28892 0.26472 0.03387  -0.00998 -0.00196 96  ASN A CB  
865  C  CG  . ASN A 96  ? 0.18384 0.27468 0.23449 0.04283  0.02563  0.00023  96  ASN A CG  
866  O  OD1 . ASN A 96  ? 0.22182 0.28083 0.25317 0.00970  0.00758  -0.02318 96  ASN A OD1 
867  N  ND2 . ASN A 96  ? 0.21961 0.26611 0.24417 0.01596  0.03237  -0.03890 96  ASN A ND2 
868  N  N   A SER A 97  ? 0.21359 0.40543 0.21767 -0.00819 0.00043  0.02469  97  SER A N   
869  N  N   B SER A 97  ? 0.22842 0.40369 0.26628 -0.01068 -0.03849 -0.01607 97  SER A N   
870  C  CA  A SER A 97  ? 0.24770 0.41902 0.23625 -0.00764 -0.03825 0.10141  97  SER A CA  
871  C  CA  B SER A 97  ? 0.27828 0.42276 0.30415 -0.03701 -0.05781 0.02275  97  SER A CA  
872  C  C   A SER A 97  ? 0.37894 0.45595 0.25443 -0.01573 -0.04643 0.06496  97  SER A C   
873  C  C   B SER A 97  ? 0.38282 0.46451 0.27023 -0.03899 -0.06330 -0.00279 97  SER A C   
874  O  O   A SER A 97  ? 0.47717 0.43650 0.27828 -0.00114 -0.01364 0.05481  97  SER A O   
875  O  O   B SER A 97  ? 0.46861 0.45356 0.24642 -0.01727 -0.07166 -0.06595 97  SER A O   
876  C  CB  A SER A 97  ? 0.37418 0.43492 0.21062 0.04041  -0.04469 0.13463  97  SER A CB  
877  C  CB  B SER A 97  ? 0.42794 0.42742 0.37462 -0.04700 0.03898  0.04360  97  SER A CB  
878  O  OG  A SER A 97  ? 0.37965 0.43577 0.27902 0.08045  0.07924  0.10150  97  SER A OG  
879  O  OG  B SER A 97  ? 0.50071 0.40180 0.33911 -0.06257 0.07350  0.11223  97  SER A OG  
880  N  N   . ASP A 98  ? 0.52488 0.51427 0.27729 -0.05165 -0.03095 -0.00851 98  ASP A N   
881  C  CA  . ASP A 98  ? 0.49815 0.56400 0.26907 -0.05240 -0.07238 -0.02976 98  ASP A CA  
882  C  C   . ASP A 98  ? 0.44003 0.58953 0.32939 -0.04363 -0.03731 -0.04310 98  ASP A C   
883  O  O   . ASP A 98  ? 0.43454 0.60782 0.43855 -0.00831 -0.02335 -0.06673 98  ASP A O   
884  C  CB  . ASP A 98  ? 0.59651 0.56917 0.37746 -0.07804 0.04721  0.03329  98  ASP A CB  
885  C  CG  . ASP A 98  ? 0.64499 0.55562 0.39196 -0.09401 0.12666  0.04448  98  ASP A CG  
886  N  N   . ASP A 99  ? 0.40951 0.57058 0.26865 -0.03101 -0.03275 -0.02781 99  ASP A N   
887  C  CA  . ASP A 99  ? 0.34573 0.54906 0.36271 -0.01772 -0.04784 0.03635  99  ASP A CA  
888  C  C   . ASP A 99  ? 0.29141 0.47134 0.31401 -0.05583 0.02485  -0.00102 99  ASP A C   
889  O  O   . ASP A 99  ? 0.33698 0.45666 0.28246 0.00681  -0.03773 0.00063  99  ASP A O   
890  C  CB  . ASP A 99  ? 0.48002 0.55216 0.46095 -0.01787 -0.06183 0.11567  99  ASP A CB  
891  N  N   . GLY A 100 ? 0.32137 0.39290 0.37455 0.03469  0.01842  -0.07409 100 GLY A N   
892  C  CA  . GLY A 100 ? 0.37861 0.31750 0.22345 -0.00164 0.07596  -0.04901 100 GLY A CA  
893  C  C   . GLY A 100 ? 0.46890 0.29684 0.31369 -0.02160 0.04203  -0.02925 100 GLY A C   
894  O  O   . GLY A 100 ? 0.38498 0.33914 0.29992 0.03971  0.02185  0.00553  100 GLY A O   
895  N  N   . ILE A 101 ? 0.25072 0.25194 0.25780 0.01651  0.04563  -0.02779 101 ILE A N   
896  C  CA  . ILE A 101 ? 0.18793 0.25674 0.21871 0.00477  0.00780  -0.01379 101 ILE A CA  
897  C  C   . ILE A 101 ? 0.17987 0.22573 0.20122 0.02133  -0.00839 -0.01926 101 ILE A C   
898  O  O   . ILE A 101 ? 0.32245 0.20941 0.24204 0.02436  0.04174  -0.00301 101 ILE A O   
899  C  CB  . ILE A 101 ? 0.25032 0.29427 0.24746 0.00737  -0.01826 -0.05049 101 ILE A CB  
900  C  CG1 . ILE A 101 ? 0.29824 0.35253 0.31589 -0.10064 0.10503  -0.10409 101 ILE A CG1 
901  C  CG2 . ILE A 101 ? 0.20344 0.34946 0.35455 0.01522  -0.04118 -0.03847 101 ILE A CG2 
902  C  CD1 . ILE A 101 ? 0.47092 0.34735 0.39379 -0.11786 0.09020  -0.01393 101 ILE A CD1 
903  N  N   A ARG A 102 ? 0.21030 0.26902 0.21789 0.04672  0.01241  -0.02619 102 ARG A N   
904  N  N   B ARG A 102 ? 0.19491 0.18515 0.19542 0.05445  -0.01107 -0.04194 102 ARG A N   
905  C  CA  A ARG A 102 ? 0.20319 0.28829 0.29061 0.01028  0.03183  -0.05101 102 ARG A CA  
906  C  CA  B ARG A 102 ? 0.16901 0.16586 0.19560 0.03178  0.00913  -0.01824 102 ARG A CA  
907  C  C   A ARG A 102 ? 0.21167 0.22961 0.23634 0.01846  -0.02052 -0.02264 102 ARG A C   
908  C  C   B ARG A 102 ? 0.20334 0.17276 0.21166 0.05348  -0.00052 -0.00480 102 ARG A C   
909  O  O   A ARG A 102 ? 0.18985 0.21103 0.22743 0.02680  -0.05656 -0.00880 102 ARG A O   
910  O  O   B ARG A 102 ? 0.18486 0.16497 0.19417 0.05272  -0.02507 0.01887  102 ARG A O   
911  C  CB  A ARG A 102 ? 0.28479 0.33191 0.38816 0.01046  -0.05380 -0.09407 102 ARG A CB  
912  C  CB  B ARG A 102 ? 0.19623 0.15687 0.21328 -0.00214 -0.07111 -0.08354 102 ARG A CB  
913  C  CG  A ARG A 102 ? 0.35436 0.36327 0.46147 -0.03896 -0.01741 -0.08680 102 ARG A CG  
914  C  CG  B ARG A 102 ? 0.15877 0.16102 0.17220 0.01975  -0.03426 -0.04813 102 ARG A CG  
915  C  CD  A ARG A 102 ? 0.35170 0.36378 0.43564 -0.06016 0.08681  -0.11183 102 ARG A CD  
916  C  CD  B ARG A 102 ? 0.20084 0.21481 0.17821 0.00812  -0.08671 -0.01881 102 ARG A CD  
917  N  NE  A ARG A 102 ? 0.35915 0.40161 0.46382 -0.01213 0.05559  -0.07168 102 ARG A NE  
918  N  NE  B ARG A 102 ? 0.25191 0.28502 0.23262 0.02152  -0.12361 -0.04946 102 ARG A NE  
919  C  CZ  A ARG A 102 ? 0.47651 0.43071 0.53987 -0.02484 0.05302  -0.07747 102 ARG A CZ  
920  C  CZ  B ARG A 102 ? 0.25977 0.31521 0.20995 0.07195  -0.05565 -0.06948 102 ARG A CZ  
921  N  NH1 A ARG A 102 ? 0.59283 0.44496 0.52714 -0.00913 -0.01414 -0.06887 102 ARG A NH1 
922  N  NH1 B ARG A 102 ? 0.33955 0.32270 0.21386 0.15496  0.06498  -0.03444 102 ARG A NH1 
923  N  NH2 A ARG A 102 ? 0.39752 0.43323 0.64330 -0.01393 0.02168  -0.11922 102 ARG A NH2 
924  N  NH2 B ARG A 102 ? 0.31880 0.30718 0.25952 0.03994  -0.09344 -0.13053 102 ARG A NH2 
925  N  N   . LYS A 103 ? 0.22794 0.20052 0.23533 0.03028  -0.01800 -0.03204 103 LYS A N   
926  C  CA  . LYS A 103 ? 0.26223 0.21930 0.22386 0.04419  -0.00970 -0.00821 103 LYS A CA  
927  C  C   . LYS A 103 ? 0.18414 0.22746 0.23115 0.00737  0.00206  -0.00652 103 LYS A C   
928  O  O   . LYS A 103 ? 0.24356 0.22466 0.23147 0.01117  -0.00825 -0.03131 103 LYS A O   
929  C  CB  . LYS A 103 ? 0.34133 0.27941 0.26186 0.06470  0.04152  0.01761  103 LYS A CB  
930  C  CG  . LYS A 103 ? 0.30457 0.28853 0.30518 0.03285  0.04746  0.04656  103 LYS A CG  
931  C  CD  . LYS A 103 ? 0.32156 0.34284 0.32058 -0.02224 0.12937  0.00571  103 LYS A CD  
932  C  CE  . LYS A 103 ? 0.32998 0.36645 0.31113 -0.02339 0.08343  -0.01158 103 LYS A CE  
933  N  NZ  . LYS A 103 ? 0.43177 0.35590 0.36889 0.03204  0.11587  0.01677  103 LYS A NZ  
934  N  N   . LYS A 104 ? 0.20572 0.21862 0.26326 0.06925  -0.02964 -0.00557 104 LYS A N   
935  C  CA  . LYS A 104 ? 0.22431 0.25362 0.28099 0.04152  -0.08410 -0.01567 104 LYS A CA  
936  C  C   . LYS A 104 ? 0.25840 0.23190 0.22028 0.05587  -0.04281 -0.02980 104 LYS A C   
937  O  O   . LYS A 104 ? 0.34157 0.20510 0.23107 0.07641  -0.05601 -0.02951 104 LYS A O   
938  C  CB  . LYS A 104 ? 0.28670 0.27291 0.30512 0.09460  -0.03194 -0.00096 104 LYS A CB  
939  C  CG  . LYS A 104 ? 0.35555 0.30786 0.43575 0.08921  -0.15830 -0.00348 104 LYS A CG  
940  C  CD  . LYS A 104 ? 0.44203 0.34136 0.51177 0.09039  -0.18524 0.05225  104 LYS A CD  
941  C  CE  . LYS A 104 ? 0.49337 0.41059 0.59844 0.05297  -0.18304 0.02782  104 LYS A CE  
942  N  NZ  . LYS A 104 ? 0.46665 0.43236 0.65077 0.05973  -0.17420 0.03294  104 LYS A NZ  
943  N  N   . GLU A 105 ? 0.26253 0.21580 0.21933 0.04800  -0.01461 -0.01509 105 GLU A N   
944  C  CA  . GLU A 105 ? 0.36304 0.21111 0.17817 0.03036  -0.05685 -0.03354 105 GLU A CA  
945  C  C   . GLU A 105 ? 0.30004 0.20840 0.21126 0.05677  -0.00559 -0.00035 105 GLU A C   
946  O  O   . GLU A 105 ? 0.37166 0.20549 0.19226 0.05361  -0.01045 -0.02033 105 GLU A O   
947  C  CB  . GLU A 105 ? 0.35843 0.27100 0.18454 0.02917  0.00098  -0.02651 105 GLU A CB  
948  C  CG  . GLU A 105 ? 0.34085 0.29507 0.26157 0.04726  0.06838  0.01368  105 GLU A CG  
949  C  CD  . GLU A 105 ? 0.52732 0.36414 0.32844 -0.00456 0.12408  -0.01796 105 GLU A CD  
950  O  OE1 . GLU A 105 ? 0.61640 0.32391 0.32865 0.03052  0.11031  -0.04024 105 GLU A OE1 
951  O  OE2 . GLU A 105 ? 0.51912 0.42166 0.36742 -0.00564 0.10617  -0.05323 105 GLU A OE2 
952  N  N   . ILE A 106 ? 0.19242 0.21723 0.21714 0.03675  -0.00001 0.00135  106 ILE A N   
953  C  CA  . ILE A 106 ? 0.28227 0.20234 0.21576 0.00740  0.01286  -0.01053 106 ILE A CA  
954  C  C   . ILE A 106 ? 0.26129 0.20331 0.21367 0.00400  0.00098  0.00920  106 ILE A C   
955  O  O   . ILE A 106 ? 0.27064 0.19316 0.23035 0.01965  -0.00338 0.00774  106 ILE A O   
956  C  CB  . ILE A 106 ? 0.25772 0.18045 0.18178 0.01234  -0.02065 0.00230  106 ILE A CB  
957  C  CG1 . ILE A 106 ? 0.23594 0.17826 0.22951 0.01728  0.00720  0.00988  106 ILE A CG1 
958  C  CG2 . ILE A 106 ? 0.21114 0.20577 0.25075 0.01736  -0.00385 -0.01546 106 ILE A CG2 
959  C  CD1 . ILE A 106 ? 0.24252 0.18915 0.22107 0.02455  -0.01563 -0.00949 106 ILE A CD1 
960  N  N   . ASN A 107 ? 0.26794 0.19474 0.19862 0.04055  0.00467  0.00748  107 ASN A N   
961  C  CA  . ASN A 107 ? 0.26375 0.17996 0.22597 0.05350  0.02298  -0.01075 107 ASN A CA  
962  C  C   . ASN A 107 ? 0.28238 0.19333 0.22204 0.04331  -0.02374 -0.01117 107 ASN A C   
963  O  O   . ASN A 107 ? 0.29952 0.20298 0.21768 0.04338  -0.00362 -0.01254 107 ASN A O   
964  C  CB  . ASN A 107 ? 0.25688 0.19362 0.23390 0.03462  0.02266  0.00825  107 ASN A CB  
965  C  CG  . ASN A 107 ? 0.16083 0.23352 0.25449 0.05695  -0.03151 -0.00774 107 ASN A CG  
966  O  OD1 . ASN A 107 ? 0.24136 0.21939 0.24025 0.03838  0.02772  0.01166  107 ASN A OD1 
967  N  ND2 . ASN A 107 ? 0.28898 0.26214 0.29357 0.03905  0.04958  -0.00396 107 ASN A ND2 
968  N  N   . ASP A 108 ? 0.25535 0.20680 0.20158 0.05665  -0.01240 0.02292  108 ASP A N   
969  C  CA  . ASP A 108 ? 0.32754 0.17548 0.21657 0.03362  -0.05832 -0.01246 108 ASP A CA  
970  C  C   . ASP A 108 ? 0.27745 0.21041 0.20935 0.02193  -0.01384 -0.02227 108 ASP A C   
971  O  O   . ASP A 108 ? 0.29490 0.18872 0.24850 0.02077  0.01640  -0.01129 108 ASP A O   
972  C  CB  . ASP A 108 ? 0.26547 0.22523 0.21970 0.07054  -0.03275 -0.02440 108 ASP A CB  
973  C  CG  . ASP A 108 ? 0.29276 0.27021 0.23679 0.14070  -0.06147 -0.05756 108 ASP A CG  
974  O  OD1 . ASP A 108 ? 0.30987 0.27404 0.29814 0.05896  -0.02945 -0.06510 108 ASP A OD1 
975  O  OD2 . ASP A 108 ? 0.33556 0.26745 0.25270 0.07072  -0.05993 -0.02188 108 ASP A OD2 
976  N  N   . ARG A 109 ? 0.21699 0.23743 0.22155 0.02333  0.02486  0.03001  109 ARG A N   
977  C  CA  . ARG A 109 ? 0.28301 0.25015 0.21562 0.04261  0.03112  0.02833  109 ARG A CA  
978  C  C   . ARG A 109 ? 0.30518 0.22389 0.20600 0.02148  -0.00510 0.00762  109 ARG A C   
979  O  O   . ARG A 109 ? 0.32511 0.21614 0.25903 0.03533  -0.00488 0.01970  109 ARG A O   
980  C  CB  . ARG A 109 ? 0.28258 0.25709 0.23418 0.04093  -0.00725 0.02399  109 ARG A CB  
981  C  CG  . ARG A 109 ? 0.33276 0.28065 0.25495 0.04072  0.05603  0.05068  109 ARG A CG  
982  C  CD  . ARG A 109 ? 0.30636 0.27216 0.27934 0.07433  0.06117  0.06610  109 ARG A CD  
983  N  NE  . ARG A 109 ? 0.38903 0.25895 0.26363 0.06298  0.06376  0.07320  109 ARG A NE  
984  C  CZ  . ARG A 109 ? 0.39007 0.26083 0.32938 0.05484  0.06470  0.03829  109 ARG A CZ  
985  N  NH1 . ARG A 109 ? 0.46744 0.28336 0.31565 0.04450  0.08953  0.02641  109 ARG A NH1 
986  N  NH2 . ARG A 109 ? 0.35725 0.27448 0.33459 0.03195  0.06222  0.01617  109 ARG A NH2 
987  N  N   . ASP A 110 ? 0.31717 0.21670 0.21056 0.04244  -0.00929 0.02167  110 ASP A N   
988  C  CA  . ASP A 110 ? 0.24812 0.20748 0.20810 0.05203  0.01073  -0.01523 110 ASP A CA  
989  C  C   . ASP A 110 ? 0.21753 0.15440 0.23731 0.02171  -0.03066 0.01384  110 ASP A C   
990  O  O   . ASP A 110 ? 0.22714 0.19809 0.21355 0.03953  -0.02360 0.00219  110 ASP A O   
991  C  CB  . ASP A 110 ? 0.27056 0.18669 0.20864 0.03880  0.03057  -0.00256 110 ASP A CB  
992  C  CG  . ASP A 110 ? 0.31402 0.24084 0.23924 0.05192  0.02746  0.01613  110 ASP A CG  
993  O  OD1 . ASP A 110 ? 0.35416 0.26126 0.26445 0.02660  0.05221  0.03481  110 ASP A OD1 
994  O  OD2 . ASP A 110 ? 0.34155 0.24611 0.25040 0.04917  0.01358  0.01978  110 ASP A OD2 
995  N  N   . TYR A 111 ? 0.25991 0.17805 0.22191 0.03012  -0.00182 0.01686  111 TYR A N   
996  C  CA  . TYR A 111 ? 0.23661 0.19617 0.23729 0.00499  0.01556  -0.02598 111 TYR A CA  
997  C  C   . TYR A 111 ? 0.26397 0.17873 0.25887 0.01145  -0.02070 -0.02504 111 TYR A C   
998  O  O   . TYR A 111 ? 0.26402 0.21452 0.21353 0.01410  -0.02022 -0.01118 111 TYR A O   
999  C  CB  . TYR A 111 ? 0.23145 0.19522 0.24192 0.01544  -0.00768 0.00858  111 TYR A CB  
1000 C  CG  . TYR A 111 ? 0.27624 0.20661 0.21271 0.02474  -0.00417 -0.01447 111 TYR A CG  
1001 C  CD1 . TYR A 111 ? 0.20635 0.21499 0.24990 0.03003  -0.00615 -0.01490 111 TYR A CD1 
1002 C  CD2 . TYR A 111 ? 0.21943 0.19480 0.24269 0.03262  -0.02148 -0.01453 111 TYR A CD2 
1003 C  CE1 . TYR A 111 ? 0.27354 0.20865 0.28309 0.06130  -0.02508 -0.00554 111 TYR A CE1 
1004 C  CE2 . TYR A 111 ? 0.33554 0.22106 0.25416 0.06722  -0.08078 -0.01788 111 TYR A CE2 
1005 C  CZ  . TYR A 111 ? 0.26254 0.20563 0.27077 0.06448  -0.05489 -0.01680 111 TYR A CZ  
1006 O  OH  . TYR A 111 ? 0.30029 0.19282 0.28700 0.05782  0.00407  0.01550  111 TYR A OH  
1007 N  N   . VAL A 112 ? 0.24322 0.15728 0.26788 -0.00412 -0.03194 -0.01514 112 VAL A N   
1008 C  CA  . VAL A 112 ? 0.23791 0.17551 0.30239 0.00841  -0.03764 0.00131  112 VAL A CA  
1009 C  C   . VAL A 112 ? 0.26253 0.18637 0.23977 0.01153  0.00636  -0.00102 112 VAL A C   
1010 O  O   . VAL A 112 ? 0.31156 0.18903 0.22092 0.01149  -0.02029 0.00199  112 VAL A O   
1011 C  CB  . VAL A 112 ? 0.31483 0.17136 0.32176 -0.00626 -0.05183 0.01239  112 VAL A CB  
1012 C  CG1 . VAL A 112 ? 0.34557 0.16624 0.35879 -0.01887 -0.06933 0.02962  112 VAL A CG1 
1013 C  CG2 . VAL A 112 ? 0.32373 0.16756 0.35190 0.03541  -0.08461 0.00990  112 VAL A CG2 
1014 N  N   . TYR A 113 ? 0.24819 0.18479 0.26251 0.05056  0.00023  -0.00331 113 TYR A N   
1015 C  CA  . TYR A 113 ? 0.22330 0.19817 0.26838 0.03460  -0.00237 -0.00502 113 TYR A CA  
1016 C  C   . TYR A 113 ? 0.32131 0.18986 0.21840 -0.00651 -0.02811 -0.00166 113 TYR A C   
1017 O  O   . TYR A 113 ? 0.25347 0.23246 0.20458 -0.00917 -0.00100 -0.00342 113 TYR A O   
1018 C  CB  . TYR A 113 ? 0.24216 0.22827 0.23713 0.03709  0.01561  0.02548  113 TYR A CB  
1019 C  CG  . TYR A 113 ? 0.18084 0.22735 0.25156 0.00620  0.01487  0.01865  113 TYR A CG  
1020 C  CD1 . TYR A 113 ? 0.23424 0.25176 0.31129 -0.02559 0.01775  0.01724  113 TYR A CD1 
1021 C  CD2 . TYR A 113 ? 0.16937 0.21051 0.27417 0.03038  0.05134  0.01573  113 TYR A CD2 
1022 C  CE1 . TYR A 113 ? 0.27754 0.21480 0.29853 0.00218  -0.01997 0.00395  113 TYR A CE1 
1023 C  CE2 . TYR A 113 ? 0.14802 0.21155 0.29708 0.00916  -0.00118 -0.03168 113 TYR A CE2 
1024 C  CZ  . TYR A 113 ? 0.23519 0.21666 0.23358 0.00382  -0.02245 0.00130  113 TYR A CZ  
1025 O  OH  . TYR A 113 ? 0.24573 0.24004 0.29637 0.00011  -0.02334 0.03151  113 TYR A OH  
1026 N  N   . LEU A 114 ? 0.27267 0.15532 0.22223 0.00316  -0.01027 0.00677  114 LEU A N   
1027 C  CA  . LEU A 114 ? 0.21891 0.19966 0.22113 0.01241  0.01169  0.01023  114 LEU A CA  
1028 C  C   . LEU A 114 ? 0.26071 0.20303 0.24101 0.03475  0.01304  -0.00281 114 LEU A C   
1029 O  O   . LEU A 114 ? 0.24566 0.20064 0.20818 0.00217  -0.01457 0.00932  114 LEU A O   
1030 C  CB  . LEU A 114 ? 0.25536 0.19372 0.22163 -0.00653 0.00740  -0.02830 114 LEU A CB  
1031 C  CG  . LEU A 114 ? 0.23450 0.20010 0.22905 0.00698  0.00351  0.00860  114 LEU A CG  
1032 C  CD1 . LEU A 114 ? 0.32514 0.22282 0.25627 0.04105  -0.07694 -0.01711 114 LEU A CD1 
1033 C  CD2 . LEU A 114 ? 0.30469 0.20518 0.36347 0.03341  -0.02872 -0.01776 114 LEU A CD2 
1034 N  N   . PHE A 115 ? 0.25928 0.22771 0.21299 0.04218  0.00248  -0.03665 115 PHE A N   
1035 C  CA  . PHE A 115 ? 0.22196 0.21734 0.26347 0.06862  -0.01106 -0.03083 115 PHE A CA  
1036 C  C   . PHE A 115 ? 0.22701 0.21222 0.22880 0.02914  -0.03622 0.00909  115 PHE A C   
1037 O  O   . PHE A 115 ? 0.29859 0.24825 0.21344 0.02240  -0.01256 0.02100  115 PHE A O   
1038 C  CB  . PHE A 115 ? 0.26566 0.24013 0.27369 0.08715  -0.00714 -0.04393 115 PHE A CB  
1039 C  CG  . PHE A 115 ? 0.42605 0.29711 0.29223 0.12751  0.00286  -0.02764 115 PHE A CG  
1040 C  CD1 . PHE A 115 ? 0.37839 0.34349 0.36006 0.12106  0.06728  -0.04662 115 PHE A CD1 
1041 C  CD2 . PHE A 115 ? 0.50406 0.28443 0.31205 0.15776  -0.04903 -0.06946 115 PHE A CD2 
1042 C  CE1 . PHE A 115 ? 0.44690 0.34416 0.36241 0.13720  0.00331  -0.02159 115 PHE A CE1 
1043 C  CE2 . PHE A 115 ? 0.55384 0.35090 0.36098 0.13703  -0.00673 -0.03718 115 PHE A CE2 
1044 C  CZ  . PHE A 115 ? 0.52690 0.35275 0.31148 0.12967  -0.03382 -0.02755 115 PHE A CZ  
1045 N  N   . TYR A 116 ? 0.28984 0.17148 0.25936 0.01306  -0.02720 -0.00503 116 TYR A N   
1046 C  CA  . TYR A 116 ? 0.28157 0.20825 0.23069 -0.00991 -0.00347 -0.01203 116 TYR A CA  
1047 C  C   . TYR A 116 ? 0.29852 0.21949 0.22518 0.03798  0.02455  0.00137  116 TYR A C   
1048 O  O   . TYR A 116 ? 0.28779 0.20345 0.23388 -0.01238 0.01111  0.01148  116 TYR A O   
1049 C  CB  . TYR A 116 ? 0.29809 0.22911 0.34324 -0.04094 0.04640  0.02136  116 TYR A CB  
1050 C  CG  . TYR A 116 ? 0.36762 0.26324 0.44192 -0.04503 -0.03510 0.06973  116 TYR A CG  
1051 C  CD1 . TYR A 116 ? 0.37769 0.20395 0.52898 -0.03689 -0.02041 0.04657  116 TYR A CD1 
1052 C  CD2 . TYR A 116 ? 0.39538 0.29274 0.48271 -0.07665 -0.01687 0.08076  116 TYR A CD2 
1053 C  CE1 . TYR A 116 ? 0.46793 0.26013 0.49605 -0.07009 -0.09962 0.11337  116 TYR A CE1 
1054 C  CE2 . TYR A 116 ? 0.47987 0.30091 0.52213 -0.09321 -0.06042 0.10416  116 TYR A CE2 
1055 C  CZ  . TYR A 116 ? 0.45464 0.25190 0.52974 -0.11388 -0.12969 0.12808  116 TYR A CZ  
1056 O  OH  . TYR A 116 ? 0.57840 0.31975 0.54469 -0.13840 -0.13473 0.17661  116 TYR A OH  
1057 N  N   . ILE A 117 ? 0.25806 0.18840 0.23355 0.01733  -0.00238 0.00027  117 ILE A N   
1058 C  CA  . ILE A 117 ? 0.28184 0.20630 0.22663 0.00286  -0.00810 0.00210  117 ILE A CA  
1059 C  C   . ILE A 117 ? 0.26645 0.21416 0.23155 -0.00888 0.00344  0.00304  117 ILE A C   
1060 O  O   . ILE A 117 ? 0.28504 0.19613 0.22021 -0.01349 -0.02165 0.00755  117 ILE A O   
1061 C  CB  . ILE A 117 ? 0.22652 0.20152 0.22000 0.01038  0.00961  -0.00432 117 ILE A CB  
1062 C  CG1 . ILE A 117 ? 0.26479 0.21502 0.22974 -0.02071 -0.00963 -0.03148 117 ILE A CG1 
1063 C  CG2 . ILE A 117 ? 0.31086 0.20025 0.22666 0.02074  -0.02092 0.02881  117 ILE A CG2 
1064 C  CD1 . ILE A 117 ? 0.35165 0.23039 0.21791 -0.02685 0.04292  -0.00135 117 ILE A CD1 
1065 N  N   A CYS A 118 ? 0.24798 0.23307 0.22040 -0.03207 -0.01795 -0.01513 118 CYS A N   
1066 N  N   B CYS A 118 ? 0.27190 0.23134 0.24789 -0.00564 0.01211  0.00078  118 CYS A N   
1067 C  CA  A CYS A 118 ? 0.19203 0.25240 0.23954 -0.03848 -0.00777 -0.05910 118 CYS A CA  
1068 C  CA  B CYS A 118 ? 0.22605 0.26318 0.25539 0.01241  -0.01141 -0.00209 118 CYS A CA  
1069 C  C   A CYS A 118 ? 0.24821 0.22595 0.25837 -0.02334 0.00110  0.00106  118 CYS A C   
1070 C  C   B CYS A 118 ? 0.27509 0.23593 0.22948 0.04233  0.00325  0.01189  118 CYS A C   
1071 O  O   A CYS A 118 ? 0.21903 0.21681 0.23188 -0.03315 -0.01511 -0.00207 118 CYS A O   
1072 O  O   B CYS A 118 ? 0.24391 0.23344 0.16511 0.08238  0.03540  0.04134  118 CYS A O   
1073 C  CB  A CYS A 118 ? 0.25122 0.27797 0.25364 -0.01009 0.03088  -0.05303 118 CYS A CB  
1074 C  CB  B CYS A 118 ? 0.26911 0.31883 0.28073 0.01100  0.00267  0.00549  118 CYS A CB  
1075 S  SG  A CYS A 118 ? 0.29603 0.26666 0.22565 -0.04819 0.00884  -0.00987 118 CYS A SG  
1076 S  SG  B CYS A 118 ? 0.41488 0.34110 0.26305 0.04140  -0.03125 0.04635  118 CYS A SG  
1077 N  N   . LEU A 119 ? 0.30072 0.20550 0.21448 0.00406  -0.02120 -0.02318 119 LEU A N   
1078 C  CA  . LEU A 119 ? 0.28662 0.19528 0.25381 0.03332  -0.02914 0.04201  119 LEU A CA  
1079 C  C   . LEU A 119 ? 0.22359 0.18028 0.20997 0.02597  0.00866  -0.01328 119 LEU A C   
1080 O  O   . LEU A 119 ? 0.28563 0.19062 0.21621 0.02717  -0.00367 -0.00907 119 LEU A O   
1081 C  CB  . LEU A 119 ? 0.37087 0.19363 0.24113 0.04457  -0.03240 -0.02026 119 LEU A CB  
1082 C  CG  . LEU A 119 ? 0.31367 0.22283 0.26795 0.02763  0.02034  0.00799  119 LEU A CG  
1083 C  CD1 . LEU A 119 ? 0.35903 0.26049 0.35043 0.04556  0.04814  -0.00905 119 LEU A CD1 
1084 C  CD2 . LEU A 119 ? 0.45687 0.20503 0.33746 0.01731  -0.03762 0.01675  119 LEU A CD2 
1085 N  N   . SER A 120 ? 0.23392 0.17876 0.24456 0.00424  0.01892  -0.00292 120 SER A N   
1086 C  CA  . SER A 120 ? 0.25905 0.18441 0.24045 0.00852  -0.01327 -0.01307 120 SER A CA  
1087 C  C   . SER A 120 ? 0.23571 0.17597 0.21008 0.00995  -0.05026 -0.01270 120 SER A C   
1088 O  O   . SER A 120 ? 0.23886 0.18748 0.22716 -0.00079 -0.03963 -0.01561 120 SER A O   
1089 C  CB  . SER A 120 ? 0.24348 0.19930 0.22214 -0.00812 -0.02553 0.01224  120 SER A CB  
1090 O  OG  . SER A 120 ? 0.25072 0.19865 0.25314 -0.01305 -0.01489 -0.01624 120 SER A OG  
1091 N  N   . ASN A 121 ? 0.26500 0.16727 0.21515 -0.01041 -0.02843 0.00177  121 ASN A N   
1092 C  CA  . ASN A 121 ? 0.22261 0.16378 0.19979 0.01658  -0.00202 -0.01254 121 ASN A CA  
1093 C  C   . ASN A 121 ? 0.24956 0.17645 0.20452 0.02171  -0.01345 -0.02524 121 ASN A C   
1094 O  O   . ASN A 121 ? 0.22858 0.20178 0.19572 0.00357  -0.00963 -0.02234 121 ASN A O   
1095 C  CB  . ASN A 121 ? 0.21535 0.15517 0.19939 -0.01128 0.00260  -0.02113 121 ASN A CB  
1096 C  CG  . ASN A 121 ? 0.22404 0.16812 0.19235 -0.03509 -0.01863 -0.02336 121 ASN A CG  
1097 O  OD1 . ASN A 121 ? 0.21194 0.19801 0.19890 0.00451  -0.01127 -0.00829 121 ASN A OD1 
1098 N  ND2 . ASN A 121 ? 0.22329 0.18734 0.21747 -0.02609 0.00161  -0.01040 121 ASN A ND2 
1099 N  N   . PHE A 122 ? 0.23103 0.19647 0.22460 0.00539  0.02047  -0.03646 122 PHE A N   
1100 C  CA  . PHE A 122 ? 0.24592 0.21045 0.22711 0.06471  0.00780  -0.01234 122 PHE A CA  
1101 C  C   . PHE A 122 ? 0.25738 0.18725 0.23193 -0.02333 -0.01809 -0.01110 122 PHE A C   
1102 O  O   . PHE A 122 ? 0.27744 0.20800 0.20912 0.02720  -0.01995 -0.00955 122 PHE A O   
1103 C  CB  . PHE A 122 ? 0.24806 0.24117 0.24802 0.06685  0.02658  0.02261  122 PHE A CB  
1104 C  CG  . PHE A 122 ? 0.30946 0.26408 0.31186 0.06719  -0.01734 0.02927  122 PHE A CG  
1105 C  CD1 . PHE A 122 ? 0.38485 0.30204 0.30022 0.06741  0.06401  -0.02926 122 PHE A CD1 
1106 C  CD2 . PHE A 122 ? 0.40853 0.29039 0.28750 0.09176  0.00916  0.01403  122 PHE A CD2 
1107 C  CE1 . PHE A 122 ? 0.35600 0.28952 0.33498 0.08116  0.04942  -0.01011 122 PHE A CE1 
1108 C  CE2 . PHE A 122 ? 0.38742 0.29977 0.36496 0.07131  0.06523  -0.01964 122 PHE A CE2 
1109 C  CZ  . PHE A 122 ? 0.36918 0.30063 0.36549 0.10509  0.10096  0.01708  122 PHE A CZ  
1110 N  N   . PHE A 123 ? 0.23363 0.18310 0.21904 -0.01067 -0.00533 -0.03047 123 PHE A N   
1111 C  CA  . PHE A 123 ? 0.25203 0.18658 0.24386 -0.04257 0.02091  -0.04307 123 PHE A CA  
1112 C  C   . PHE A 123 ? 0.29641 0.18559 0.22666 -0.00329 -0.03371 -0.04053 123 PHE A C   
1113 O  O   . PHE A 123 ? 0.33090 0.18850 0.20688 0.00073  -0.03593 -0.02557 123 PHE A O   
1114 C  CB  . PHE A 123 ? 0.25414 0.16903 0.28560 0.00529  0.01659  -0.03292 123 PHE A CB  
1115 C  CG  . PHE A 123 ? 0.43406 0.18183 0.27017 0.02226  0.06284  -0.05814 123 PHE A CG  
1116 C  CD1 . PHE A 123 ? 0.56953 0.19411 0.46148 0.05299  0.11858  0.01267  123 PHE A CD1 
1117 C  CD2 . PHE A 123 ? 0.51694 0.19978 0.30997 0.03572  -0.04759 0.00061  123 PHE A CD2 
1118 C  CE1 . PHE A 123 ? 0.60861 0.23332 0.52920 0.08695  0.11790  0.04272  123 PHE A CE1 
1119 C  CE2 . PHE A 123 ? 0.56050 0.19385 0.35825 0.01327  -0.03637 -0.00058 123 PHE A CE2 
1120 C  CZ  . PHE A 123 ? 0.56523 0.21731 0.47615 0.09056  0.06201  0.01074  123 PHE A CZ  
1121 N  N   . MET A 124 ? 0.25997 0.15903 0.20588 -0.00677 -0.01101 -0.00817 124 MET A N   
1122 C  CA  . MET A 124 ? 0.27558 0.18313 0.21235 0.01712  0.00642  -0.01225 124 MET A CA  
1123 C  C   . MET A 124 ? 0.23657 0.18569 0.17721 -0.00232 0.00774  -0.00157 124 MET A C   
1124 O  O   . MET A 124 ? 0.22960 0.18782 0.19592 -0.01327 -0.01849 -0.01455 124 MET A O   
1125 C  CB  . MET A 124 ? 0.24077 0.18318 0.23938 0.04161  -0.00426 -0.01213 124 MET A CB  
1126 C  CG  . MET A 124 ? 0.23149 0.18826 0.22239 0.04747  0.00676  -0.02088 124 MET A CG  
1127 S  SD  . MET A 124 ? 0.23127 0.20025 0.22833 0.00797  -0.00810 -0.00408 124 MET A SD  
1128 C  CE  . MET A 124 ? 0.13493 0.21452 0.24446 -0.01267 -0.00727 -0.00294 124 MET A CE  
1129 N  N   . LEU A 125 ? 0.23202 0.17423 0.25042 -0.02940 -0.01570 -0.02249 125 LEU A N   
1130 C  CA  . LEU A 125 ? 0.23561 0.17532 0.22786 0.00222  -0.04719 -0.01168 125 LEU A CA  
1131 C  C   . LEU A 125 ? 0.22487 0.18866 0.22864 0.01150  -0.00010 -0.04415 125 LEU A C   
1132 O  O   . LEU A 125 ? 0.27601 0.19761 0.19816 -0.00846 0.01194  -0.01311 125 LEU A O   
1133 C  CB  . LEU A 125 ? 0.22338 0.20617 0.22700 0.01172  -0.01314 -0.05518 125 LEU A CB  
1134 C  CG  . LEU A 125 ? 0.16255 0.20309 0.25401 0.00996  -0.00042 -0.02477 125 LEU A CG  
1135 C  CD1 . LEU A 125 ? 0.17371 0.22065 0.24997 0.00816  0.00353  -0.01197 125 LEU A CD1 
1136 C  CD2 . LEU A 125 ? 0.18198 0.20672 0.24597 -0.01943 -0.00822 -0.04840 125 LEU A CD2 
1137 N  N   . LEU A 126 ? 0.23885 0.19445 0.22924 0.04000  -0.00703 -0.04652 126 LEU A N   
1138 C  CA  . LEU A 126 ? 0.39271 0.20197 0.19609 0.04711  -0.01805 -0.00346 126 LEU A CA  
1139 C  C   . LEU A 126 ? 0.30951 0.18866 0.23599 0.00668  0.01256  -0.01417 126 LEU A C   
1140 O  O   . LEU A 126 ? 0.29961 0.20306 0.20778 0.02193  0.00271  -0.01061 126 LEU A O   
1141 C  CB  . LEU A 126 ? 0.37043 0.23744 0.19953 0.07477  -0.01248 -0.04402 126 LEU A CB  
1142 C  CG  . LEU A 126 ? 0.38759 0.25178 0.24684 0.08342  0.06242  0.01282  126 LEU A CG  
1143 C  CD1 . LEU A 126 ? 0.45982 0.26085 0.32420 0.14506  0.05543  -0.02434 126 LEU A CD1 
1144 C  CD2 . LEU A 126 ? 0.54602 0.24118 0.26324 0.04111  0.00500  -0.02334 126 LEU A CD2 
1145 N  N   . ILE A 127 ? 0.27942 0.18736 0.21101 0.00103  -0.02485 -0.03714 127 ILE A N   
1146 C  CA  . ILE A 127 ? 0.25295 0.23403 0.20236 -0.00246 -0.01406 -0.00555 127 ILE A CA  
1147 C  C   . ILE A 127 ? 0.23972 0.21176 0.22000 -0.00586 0.00031  -0.03131 127 ILE A C   
1148 O  O   . ILE A 127 ? 0.34136 0.24020 0.19810 0.01606  -0.01182 -0.04219 127 ILE A O   
1149 C  CB  . ILE A 127 ? 0.31407 0.26646 0.19990 -0.04823 -0.03398 -0.01712 127 ILE A CB  
1150 C  CG1 . ILE A 127 ? 0.31584 0.25448 0.24150 -0.03272 0.02441  -0.01682 127 ILE A CG1 
1151 C  CG2 . ILE A 127 ? 0.36143 0.28113 0.23403 -0.04786 -0.04985 -0.02534 127 ILE A CG2 
1152 C  CD1 . ILE A 127 ? 0.42000 0.24998 0.25100 -0.08482 -0.00188 -0.01445 127 ILE A CD1 
1153 N  N   . GLY A 128 ? 0.26131 0.17411 0.24312 0.00388  -0.03649 -0.03069 128 GLY A N   
1154 C  CA  . GLY A 128 ? 0.26555 0.20538 0.19967 0.01486  -0.00421 -0.03714 128 GLY A CA  
1155 C  C   . GLY A 128 ? 0.31158 0.19766 0.19227 0.01647  -0.00786 -0.02820 128 GLY A C   
1156 O  O   . GLY A 128 ? 0.29747 0.20183 0.20263 0.03116  -0.00512 -0.02318 128 GLY A O   
1157 N  N   . TYR A 129 ? 0.25356 0.19955 0.24108 0.04251  -0.01180 -0.03312 129 TYR A N   
1158 C  CA  . TYR A 129 ? 0.24672 0.22648 0.21540 0.03501  -0.00269 -0.01697 129 TYR A CA  
1159 C  C   . TYR A 129 ? 0.27572 0.21906 0.21916 0.03980  -0.00998 -0.01048 129 TYR A C   
1160 O  O   . TYR A 129 ? 0.33989 0.21898 0.22172 0.02980  -0.02144 -0.02949 129 TYR A O   
1161 C  CB  . TYR A 129 ? 0.29304 0.24942 0.20027 0.04949  -0.01835 -0.01608 129 TYR A CB  
1162 C  CG  . TYR A 129 ? 0.27698 0.26089 0.23061 0.05661  0.01405  0.01885  129 TYR A CG  
1163 C  CD1 . TYR A 129 ? 0.31969 0.29171 0.27599 0.01148  -0.00015 0.07448  129 TYR A CD1 
1164 C  CD2 . TYR A 129 ? 0.30333 0.32727 0.26529 0.08969  0.01068  0.00722  129 TYR A CD2 
1165 C  CE1 . TYR A 129 ? 0.37386 0.36826 0.27613 0.07258  -0.01995 0.06877  129 TYR A CE1 
1166 C  CE2 . TYR A 129 ? 0.23488 0.38508 0.31828 0.09848  0.03091  0.05927  129 TYR A CE2 
1167 C  CZ  . TYR A 129 ? 0.28813 0.42280 0.27736 0.10239  0.07653  0.07924  129 TYR A CZ  
1168 O  OH  . TYR A 129 ? 0.37578 0.51557 0.36786 0.10919  0.07771  0.10932  129 TYR A OH  
1169 N  N   . LEU A 130 ? 0.31629 0.21112 0.19221 0.02634  -0.00844 -0.03127 130 LEU A N   
1170 C  CA  . LEU A 130 ? 0.34796 0.21390 0.19397 0.04808  -0.01316 -0.03346 130 LEU A CA  
1171 C  C   . LEU A 130 ? 0.31743 0.20798 0.18746 0.01808  -0.03686 -0.03012 130 LEU A C   
1172 O  O   . LEU A 130 ? 0.38155 0.25568 0.20406 0.04605  -0.02730 -0.04011 130 LEU A O   
1173 C  CB  . LEU A 130 ? 0.43788 0.18644 0.23975 0.03558  0.01224  -0.00534 130 LEU A CB  
1174 C  CG  . LEU A 130 ? 0.49525 0.18996 0.28036 0.04047  -0.02258 -0.01218 130 LEU A CG  
1175 C  CD1 . LEU A 130 ? 0.52999 0.18991 0.29751 0.04814  -0.04926 -0.03642 130 LEU A CD1 
1176 C  CD2 . LEU A 130 ? 0.50018 0.23450 0.30132 0.10616  -0.03228 0.00610  130 LEU A CD2 
1177 N  N   . GLY A 131 ? 0.33691 0.18858 0.21528 0.04791  -0.04344 -0.01771 131 GLY A N   
1178 C  CA  . GLY A 131 ? 0.31836 0.17746 0.23616 0.00950  -0.04211 -0.03497 131 GLY A CA  
1179 C  C   . GLY A 131 ? 0.33977 0.21548 0.20028 0.02762  -0.02797 -0.00711 131 GLY A C   
1180 O  O   . GLY A 131 ? 0.36186 0.26982 0.20876 0.00289  -0.04741 0.00543  131 GLY A O   
1181 N  N   . GLU A 132 ? 0.28936 0.22229 0.24019 -0.00554 -0.04526 -0.00966 132 GLU A N   
1182 C  CA  . GLU A 132 ? 0.30120 0.24012 0.23437 -0.01515 -0.05198 0.01948  132 GLU A CA  
1183 C  C   . GLU A 132 ? 0.39271 0.27859 0.21118 -0.02372 -0.03075 0.03619  132 GLU A C   
1184 O  O   . GLU A 132 ? 0.48159 0.33200 0.25147 0.02525  0.05118  0.06246  132 GLU A O   
1185 C  CB  . GLU A 132 ? 0.33910 0.25138 0.30069 -0.05882 -0.07464 0.03000  132 GLU A CB  
1186 C  CG  . GLU A 132 ? 0.34998 0.26044 0.27688 0.04833  -0.07506 -0.00322 132 GLU A CG  
1187 C  CD  . GLU A 132 ? 0.19803 0.25558 0.24000 0.00763  -0.03187 0.01121  132 GLU A CD  
1188 O  OE1 . GLU A 132 ? 0.26899 0.25965 0.22635 0.00911  0.01889  0.03203  132 GLU A OE1 
1189 O  OE2 . GLU A 132 ? 0.35260 0.32029 0.22718 0.00484  -0.00739 -0.02895 132 GLU A OE2 
1190 N  N   . THR A 133 ? 0.35960 0.27802 0.24326 0.00787  0.00470  -0.01593 133 THR A N   
1191 C  CA  . THR A 133 ? 0.30722 0.34423 0.21866 0.04293  -0.07743 0.00772  133 THR A CA  
1192 C  C   . THR A 133 ? 0.39619 0.37648 0.20645 0.01399  0.03154  0.02289  133 THR A C   
1193 O  O   . THR A 133 ? 0.46337 0.42958 0.24006 0.03306  -0.00391 -0.05271 133 THR A O   
1194 C  CB  . THR A 133 ? 0.36747 0.32699 0.22600 0.03731  -0.00264 -0.03501 133 THR A CB  
1195 O  OG1 . THR A 133 ? 0.35562 0.29061 0.23729 0.05124  0.01523  -0.03003 133 THR A OG1 
1196 C  CG2 . THR A 133 ? 0.34086 0.34797 0.27071 0.03270  0.03512  -0.03516 133 THR A CG2 
1197 N  N   . LYS A 134 ? 0.42068 0.33946 0.22236 -0.01779 0.01722  0.02212  134 LYS A N   
1198 C  CA  . LYS A 134 ? 0.46632 0.36909 0.20926 0.00393  -0.02587 -0.00685 134 LYS A CA  
1199 C  C   . LYS A 134 ? 0.50437 0.36947 0.25175 0.02137  -0.00966 -0.06316 134 LYS A C   
1200 O  O   . LYS A 134 ? 0.64070 0.39685 0.25947 0.02608  -0.06437 -0.06388 134 LYS A O   
1201 C  CB  . LYS A 134 ? 0.47955 0.40687 0.26399 0.03150  -0.04975 0.02584  134 LYS A CB  
1202 C  CG  . LYS A 134 ? 0.55143 0.42635 0.33067 0.00687  -0.07773 0.13494  134 LYS A CG  
1203 C  CD  . LYS A 134 ? 0.66560 0.48169 0.45764 0.01160  -0.04050 0.11154  134 LYS A CD  
1204 C  CE  . LYS A 134 ? 0.69426 0.49470 0.42278 0.03097  0.02112  0.06965  134 LYS A CE  
1205 N  NZ  . LYS A 134 ? 0.72261 0.52292 0.43791 0.00407  0.11126  0.07372  134 LYS A NZ  
1206 N  N   A GLN A 135 ? 0.46040 0.33748 0.21599 0.06864  -0.00523 -0.07077 135 GLN A N   
1207 N  N   B GLN A 135 ? 0.46372 0.36196 0.25422 0.05344  -0.00569 -0.06498 135 GLN A N   
1208 C  CA  A GLN A 135 ? 0.47756 0.32398 0.28864 0.09989  -0.02403 -0.09107 135 GLN A CA  
1209 C  CA  B GLN A 135 ? 0.48830 0.36377 0.31287 0.06354  -0.00789 -0.08434 135 GLN A CA  
1210 C  C   A GLN A 135 ? 0.53214 0.32706 0.31604 0.05240  -0.02563 -0.12924 135 GLN A C   
1211 C  C   B GLN A 135 ? 0.53362 0.33928 0.30123 0.04027  -0.00957 -0.12908 135 GLN A C   
1212 O  O   A GLN A 135 ? 0.62170 0.34036 0.38271 0.03249  -0.04413 -0.14088 135 GLN A O   
1213 O  O   B GLN A 135 ? 0.61818 0.34116 0.33237 0.02621  -0.00798 -0.16247 135 GLN A O   
1214 C  CB  A GLN A 135 ? 0.47241 0.31406 0.28832 0.12908  -0.02920 -0.11743 135 GLN A CB  
1215 C  CB  B GLN A 135 ? 0.49207 0.39011 0.39066 0.04733  -0.03077 -0.07893 135 GLN A CB  
1216 C  CG  A GLN A 135 ? 0.50727 0.33518 0.24440 0.18150  -0.02423 -0.08006 135 GLN A CG  
1217 C  CG  B GLN A 135 ? 0.53174 0.41750 0.43419 0.05976  -0.00864 -0.06549 135 GLN A CG  
1218 C  CD  A GLN A 135 ? 0.48375 0.33893 0.34745 0.19412  0.02354  -0.09960 135 GLN A CD  
1219 C  CD  B GLN A 135 ? 0.60055 0.44395 0.50916 0.05762  0.03052  -0.05295 135 GLN A CD  
1220 O  OE1 A GLN A 135 ? 0.47276 0.43377 0.33642 0.24228  0.04310  -0.06415 135 GLN A OE1 
1221 O  OE1 B GLN A 135 ? 0.62264 0.43701 0.52364 0.07823  0.00900  -0.04887 135 GLN A OE1 
1222 N  NE2 A GLN A 135 ? 0.62018 0.27789 0.45824 0.14432  -0.06584 -0.12364 135 GLN A NE2 
1223 N  NE2 B GLN A 135 ? 0.63283 0.45415 0.56651 0.05144  0.06237  -0.05187 135 GLN A NE2 
1224 N  N   . ILE A 136 ? 0.52939 0.32613 0.30067 0.02377  -0.03382 -0.09882 136 ILE A N   
1225 C  CA  . ILE A 136 ? 0.54297 0.30633 0.27707 0.01607  -0.07250 -0.06771 136 ILE A CA  
1226 C  C   . ILE A 136 ? 0.50536 0.34862 0.22206 -0.02350 -0.08315 -0.05782 136 ILE A C   
1227 O  O   . ILE A 136 ? 0.54993 0.33505 0.26382 -0.05277 -0.04655 -0.04777 136 ILE A O   
1228 C  CB  . ILE A 136 ? 0.54311 0.24384 0.29471 -0.03924 -0.04463 -0.07873 136 ILE A CB  
1229 C  CG1 . ILE A 136 ? 0.46501 0.26535 0.25177 -0.01924 -0.02740 -0.02605 136 ILE A CG1 
1230 C  CG2 . ILE A 136 ? 0.67306 0.23615 0.31373 -0.03910 -0.04626 -0.04775 136 ILE A CG2 
1231 C  CD1 . ILE A 136 ? 0.41139 0.29457 0.27624 -0.00930 -0.00802 0.02300  136 ILE A CD1 
1232 N  N   . ASN A 137 ? 0.55706 0.41715 0.25386 -0.04956 -0.09479 -0.09318 137 ASN A N   
1233 C  CA  . ASN A 137 ? 0.52621 0.44076 0.27647 -0.04318 -0.11150 -0.10769 137 ASN A CA  
1234 C  C   . ASN A 137 ? 0.45176 0.43592 0.24858 -0.06589 -0.04565 -0.08894 137 ASN A C   
1235 O  O   . ASN A 137 ? 0.40973 0.45378 0.24272 -0.03551 -0.06188 -0.07288 137 ASN A O   
1236 C  CB  . ASN A 137 ? 0.50998 0.48963 0.32703 -0.03329 -0.12990 -0.13361 137 ASN A CB  
1237 C  CG  . ASN A 137 ? 0.56300 0.50689 0.42418 -0.08829 -0.10167 -0.15388 137 ASN A CG  
1238 O  OD1 . ASN A 137 ? 0.54671 0.50049 0.34142 -0.06528 -0.08016 -0.13160 137 ASN A OD1 
1239 N  ND2 . ASN A 137 ? 0.62072 0.52022 0.57565 -0.12651 0.00283  -0.15507 137 ASN A ND2 
1240 N  N   . LYS A 138 ? 0.42558 0.42833 0.30485 -0.08618 -0.06311 -0.04309 138 LYS A N   
1241 C  CA  . LYS A 138 ? 0.45707 0.41702 0.27578 -0.07072 -0.07320 0.01489  138 LYS A CA  
1242 C  C   . LYS A 138 ? 0.39046 0.41308 0.29903 -0.05770 -0.09246 0.04285  138 LYS A C   
1243 O  O   . LYS A 138 ? 0.40573 0.42896 0.27367 -0.01863 -0.08575 0.01301  138 LYS A O   
1244 C  CB  . LYS A 138 ? 0.47856 0.41154 0.33947 -0.07934 -0.09278 0.04426  138 LYS A CB  
1245 C  CG  . LYS A 138 ? 0.51654 0.44229 0.44167 -0.08850 -0.10438 0.03101  138 LYS A CG  
1246 C  CD  . LYS A 138 ? 0.57132 0.48639 0.56371 -0.08162 -0.06283 0.01677  138 LYS A CD  
1247 C  CE  . LYS A 138 ? 0.66717 0.51510 0.62469 -0.07919 -0.06466 -0.01061 138 LYS A CE  
1248 N  NZ  . LYS A 138 ? 0.69415 0.52658 0.58607 -0.07651 -0.08011 -0.05367 138 LYS A NZ  
1249 N  N   . MET A 139 ? 0.39754 0.46030 0.29995 -0.10493 -0.11238 0.00358  139 MET A N   
1250 C  CA  . MET A 139 ? 0.39757 0.48108 0.37258 -0.11120 -0.13419 -0.01386 139 MET A CA  
1251 C  C   . MET A 139 ? 0.37912 0.40499 0.34456 -0.07137 -0.08917 -0.02906 139 MET A C   
1252 O  O   . MET A 139 ? 0.28619 0.43619 0.35609 -0.06547 -0.08553 -0.04738 139 MET A O   
1253 C  CB  . MET A 139 ? 0.48629 0.57135 0.45452 -0.09612 -0.20323 -0.00965 139 MET A CB  
1254 C  CG  . MET A 139 ? 0.57682 0.67068 0.61966 -0.08219 -0.25175 -0.03521 139 MET A CG  
1255 S  SD  . MET A 139 ? 0.74389 0.76928 0.78489 -0.07447 -0.18098 -0.03579 139 MET A SD  
1256 C  CE  . MET A 139 ? 0.68074 0.77746 0.72284 -0.08411 -0.22479 -0.07088 139 MET A CE  
1257 N  N   . LEU A 140 ? 0.46343 0.38601 0.32137 -0.06876 -0.09254 -0.03611 140 LEU A N   
1258 C  CA  . LEU A 140 ? 0.36216 0.33815 0.32087 -0.08376 -0.04948 -0.06078 140 LEU A CA  
1259 C  C   . LEU A 140 ? 0.30399 0.32193 0.31793 -0.09294 -0.04938 -0.03622 140 LEU A C   
1260 O  O   . LEU A 140 ? 0.34790 0.32655 0.27961 -0.02907 -0.04859 -0.00132 140 LEU A O   
1261 C  CB  . LEU A 140 ? 0.40680 0.33966 0.35440 -0.10319 -0.04349 -0.06282 140 LEU A CB  
1262 C  CG  . LEU A 140 ? 0.44559 0.38257 0.42013 -0.11058 0.03450  -0.03226 140 LEU A CG  
1263 C  CD1 . LEU A 140 ? 0.43227 0.41311 0.51230 -0.10532 0.07301  -0.00079 140 LEU A CD1 
1264 C  CD2 . LEU A 140 ? 0.53104 0.37938 0.40764 -0.11171 0.02172  -0.00461 140 LEU A CD2 
1265 N  N   . THR A 141 ? 0.30510 0.28963 0.32627 -0.07342 -0.04688 -0.04263 141 THR A N   
1266 C  CA  . THR A 141 ? 0.29287 0.28692 0.28722 -0.07906 -0.01929 -0.05512 141 THR A CA  
1267 C  C   . THR A 141 ? 0.29876 0.30836 0.25687 -0.02474 -0.05211 -0.04674 141 THR A C   
1268 O  O   . THR A 141 ? 0.28391 0.32054 0.23375 -0.05936 -0.06241 -0.01685 141 THR A O   
1269 C  CB  . THR A 141 ? 0.29120 0.29353 0.24749 -0.07218 -0.02938 -0.03167 141 THR A CB  
1270 O  OG1 . THR A 141 ? 0.37009 0.28769 0.24521 -0.04214 -0.02064 -0.04873 141 THR A OG1 
1271 C  CG2 . THR A 141 ? 0.30190 0.29060 0.23140 -0.05933 -0.01940 -0.05738 141 THR A CG2 
1272 N  N   . LEU A 142 ? 0.28610 0.33851 0.22979 -0.04514 -0.06415 -0.02570 142 LEU A N   
1273 C  CA  . LEU A 142 ? 0.28304 0.36316 0.24296 -0.02819 -0.03398 -0.05436 142 LEU A CA  
1274 C  C   . LEU A 142 ? 0.19055 0.40727 0.28066 -0.09017 0.00649  -0.01311 142 LEU A C   
1275 O  O   . LEU A 142 ? 0.27925 0.43353 0.26579 0.05229  -0.04877 -0.01004 142 LEU A O   
1276 C  CB  . LEU A 142 ? 0.39301 0.36400 0.25569 -0.02281 -0.06976 -0.01293 142 LEU A CB  
1277 C  CG  . LEU A 142 ? 0.47880 0.35099 0.37467 -0.06187 -0.09936 -0.01805 142 LEU A CG  
1278 C  CD1 . LEU A 142 ? 0.48375 0.35490 0.38629 -0.06151 -0.11657 0.02812  142 LEU A CD1 
1279 C  CD2 . LEU A 142 ? 0.55334 0.33995 0.39790 -0.10114 -0.13728 -0.05290 142 LEU A CD2 
1280 N  N   A PHE A 143 ? 0.26903 0.43914 0.33938 -0.07842 -0.06358 0.00676  143 PHE A N   
1281 N  N   B PHE A 143 ? 0.26062 0.41540 0.33291 -0.08660 -0.09381 0.01137  143 PHE A N   
1282 C  CA  A PHE A 143 ? 0.33186 0.45511 0.32774 -0.08461 -0.06141 0.01513  143 PHE A CA  
1283 C  CA  B PHE A 143 ? 0.29626 0.40287 0.31504 -0.11139 -0.08445 0.00432  143 PHE A CA  
1284 C  C   A PHE A 143 ? 0.34321 0.40777 0.29691 -0.07726 -0.06994 0.00316  143 PHE A C   
1285 C  C   B PHE A 143 ? 0.32609 0.35661 0.30102 -0.09013 -0.06958 -0.02174 143 PHE A C   
1286 O  O   A PHE A 143 ? 0.31620 0.40130 0.25213 -0.11543 -0.07800 0.00635  143 PHE A O   
1287 O  O   B PHE A 143 ? 0.32085 0.30997 0.30657 -0.10101 -0.01991 -0.05415 143 PHE A O   
1288 C  CB  A PHE A 143 ? 0.38015 0.50267 0.36534 -0.06781 -0.08526 -0.00085 143 PHE A CB  
1289 C  CB  B PHE A 143 ? 0.31346 0.42350 0.31935 -0.12392 -0.11033 -0.00301 143 PHE A CB  
1290 C  CG  A PHE A 143 ? 0.42376 0.54718 0.43490 -0.01115 -0.02443 0.00898  143 PHE A CG  
1291 C  CG  B PHE A 143 ? 0.41884 0.44973 0.41399 -0.08344 -0.04450 0.01596  143 PHE A CG  
1292 C  CD1 A PHE A 143 ? 0.36498 0.56012 0.46545 0.01969  -0.01634 0.01252  143 PHE A CD1 
1293 C  CD1 B PHE A 143 ? 0.45836 0.45924 0.47571 -0.07400 -0.02941 0.02907  143 PHE A CD1 
1294 C  CD2 A PHE A 143 ? 0.42936 0.56414 0.46812 0.01698  -0.03345 -0.00185 143 PHE A CD2 
1295 C  CD2 B PHE A 143 ? 0.44093 0.45178 0.45265 -0.05901 0.01357  0.01975  143 PHE A CD2 
1296 C  CE1 A PHE A 143 ? 0.43076 0.56298 0.46442 0.03185  -0.05092 0.00587  143 PHE A CE1 
1297 C  CE1 B PHE A 143 ? 0.49943 0.46267 0.50722 -0.05076 0.00748  0.04204  143 PHE A CE1 
1298 C  CE2 A PHE A 143 ? 0.40981 0.56490 0.44819 0.04407  -0.05802 -0.00812 143 PHE A CE2 
1299 C  CE2 B PHE A 143 ? 0.45195 0.47899 0.49995 -0.03269 0.02812  0.02403  143 PHE A CE2 
1300 C  CZ  A PHE A 143 ? 0.43615 0.56457 0.43604 0.03814  -0.07729 0.00147  143 PHE A CZ  
1301 C  CZ  B PHE A 143 ? 0.45977 0.47202 0.50733 -0.04054 0.04247  0.03908  143 PHE A CZ  
1302 N  N   . GLY A 144 ? 0.31210 0.35985 0.29796 -0.06450 -0.07245 -0.03707 144 GLY A N   
1303 C  CA  . GLY A 144 ? 0.35868 0.28897 0.28881 -0.04081 -0.03176 -0.05700 144 GLY A CA  
1304 C  C   . GLY A 144 ? 0.34681 0.25448 0.24139 -0.06603 -0.03435 -0.03494 144 GLY A C   
1305 O  O   . GLY A 144 ? 0.34728 0.25637 0.23749 -0.01691 -0.00949 -0.03175 144 GLY A O   
1306 N  N   . GLY A 145 ? 0.26468 0.24615 0.28225 -0.05953 -0.04433 -0.01855 145 GLY A N   
1307 C  CA  . GLY A 145 ? 0.25000 0.23785 0.24922 -0.01711 0.00337  -0.02842 145 GLY A CA  
1308 C  C   . GLY A 145 ? 0.21289 0.25351 0.23651 -0.00653 -0.02133 0.01343  145 GLY A C   
1309 O  O   . GLY A 145 ? 0.25848 0.28626 0.21191 -0.00060 0.00210  -0.00139 145 GLY A O   
1310 N  N   . SER A 146 ? 0.20298 0.26521 0.29867 0.00695  -0.05364 -0.02488 146 SER A N   
1311 C  CA  . SER A 146 ? 0.22242 0.29912 0.27592 -0.01101 -0.02295 0.00342  146 SER A CA  
1312 C  C   . SER A 146 ? 0.21679 0.29506 0.21468 -0.08589 -0.06489 0.00093  146 SER A C   
1313 O  O   . SER A 146 ? 0.19303 0.31854 0.23324 -0.02226 -0.04164 -0.03084 146 SER A O   
1314 C  CB  . SER A 146 ? 0.18311 0.34007 0.33893 0.00647  -0.01432 0.04384  146 SER A CB  
1315 O  OG  . SER A 146 ? 0.31798 0.37289 0.33807 0.02722  -0.02681 0.06448  146 SER A OG  
1316 N  N   . PHE A 147 ? 0.24643 0.28407 0.30295 -0.05357 -0.04781 0.00167  147 PHE A N   
1317 C  CA  . PHE A 147 ? 0.23432 0.27729 0.28146 -0.05765 -0.04337 -0.04928 147 PHE A CA  
1318 C  C   . PHE A 147 ? 0.22284 0.24270 0.30155 -0.05735 -0.00017 -0.04292 147 PHE A C   
1319 O  O   . PHE A 147 ? 0.23273 0.26220 0.25626 -0.04245 -0.02027 -0.01563 147 PHE A O   
1320 C  CB  . PHE A 147 ? 0.29922 0.30301 0.28478 -0.11113 -0.01773 -0.03707 147 PHE A CB  
1321 C  CG  . PHE A 147 ? 0.30338 0.29991 0.26563 -0.13217 0.03516  -0.04405 147 PHE A CG  
1322 C  CD1 . PHE A 147 ? 0.42620 0.31888 0.33959 -0.12131 0.01269  0.00810  147 PHE A CD1 
1323 C  CD2 . PHE A 147 ? 0.35171 0.31111 0.30192 -0.09313 -0.05673 -0.02032 147 PHE A CD2 
1324 C  CE1 . PHE A 147 ? 0.41477 0.37057 0.43784 -0.10351 0.02510  0.03372  147 PHE A CE1 
1325 C  CE2 . PHE A 147 ? 0.32519 0.32408 0.34996 -0.15836 -0.01113 -0.02592 147 PHE A CE2 
1326 C  CZ  . PHE A 147 ? 0.32650 0.34736 0.41994 -0.10800 -0.03781 0.03038  147 PHE A CZ  
1327 N  N   . PHE A 148 ? 0.18412 0.22064 0.26825 -0.05026 -0.06012 0.00007  148 PHE A N   
1328 C  CA  . PHE A 148 ? 0.19100 0.21609 0.23809 -0.02802 -0.01777 -0.02050 148 PHE A CA  
1329 C  C   . PHE A 148 ? 0.19373 0.20280 0.26061 -0.03460 -0.03019 -0.01925 148 PHE A C   
1330 O  O   . PHE A 148 ? 0.19662 0.21743 0.24387 -0.02348 -0.02300 -0.01946 148 PHE A O   
1331 C  CB  . PHE A 148 ? 0.31935 0.20866 0.23750 -0.00432 -0.00322 -0.02016 148 PHE A CB  
1332 C  CG  . PHE A 148 ? 0.31742 0.19908 0.24746 -0.01955 0.01469  -0.01826 148 PHE A CG  
1333 C  CD1 . PHE A 148 ? 0.28521 0.19263 0.27168 -0.05790 0.00551  0.00011  148 PHE A CD1 
1334 C  CD2 . PHE A 148 ? 0.35311 0.21968 0.27529 0.02815  -0.00962 -0.04599 148 PHE A CD2 
1335 C  CE1 . PHE A 148 ? 0.30490 0.19646 0.26775 -0.04744 -0.00316 0.00901  148 PHE A CE1 
1336 C  CE2 . PHE A 148 ? 0.32495 0.23170 0.27503 0.04741  -0.01590 -0.01296 148 PHE A CE2 
1337 C  CZ  . PHE A 148 ? 0.33824 0.22280 0.26455 -0.02136 -0.01642 -0.02457 148 PHE A CZ  
1338 N  N   . LEU A 149 ? 0.22148 0.18733 0.24137 0.00250  -0.02785 -0.00118 149 LEU A N   
1339 C  CA  . LEU A 149 ? 0.24527 0.17740 0.24030 -0.00199 0.00613  -0.00826 149 LEU A CA  
1340 C  C   . LEU A 149 ? 0.20271 0.19528 0.25574 -0.01452 0.03703  0.00797  149 LEU A C   
1341 O  O   . LEU A 149 ? 0.23375 0.22292 0.21315 -0.02753 0.01789  -0.00410 149 LEU A O   
1342 C  CB  . LEU A 149 ? 0.27044 0.19255 0.23626 0.03583  -0.01745 -0.00020 149 LEU A CB  
1343 C  CG  . LEU A 149 ? 0.23098 0.17689 0.27311 0.01028  0.00104  0.01668  149 LEU A CG  
1344 C  CD1 . LEU A 149 ? 0.28184 0.20612 0.31239 -0.01451 0.07584  -0.02711 149 LEU A CD1 
1345 C  CD2 . LEU A 149 ? 0.34309 0.20811 0.33618 0.04099  -0.00087 -0.00068 149 LEU A CD2 
1346 N  N   A PHE A 150 ? 0.18955 0.18866 0.28931 -0.03357 -0.01675 0.00104  150 PHE A N   
1347 N  N   B PHE A 150 ? 0.19490 0.20037 0.30072 -0.02399 -0.00375 -0.00342 150 PHE A N   
1348 C  CA  A PHE A 150 ? 0.18763 0.24747 0.23011 -0.02012 -0.05143 0.02375  150 PHE A CA  
1349 C  CA  B PHE A 150 ? 0.17977 0.24760 0.24699 -0.03017 -0.01145 0.01822  150 PHE A CA  
1350 C  C   A PHE A 150 ? 0.20781 0.23558 0.25322 -0.07533 -0.03122 -0.01602 150 PHE A C   
1351 C  C   B PHE A 150 ? 0.14430 0.24351 0.30244 -0.06594 0.02554  0.01308  150 PHE A C   
1352 O  O   A PHE A 150 ? 0.17308 0.23379 0.21128 -0.10476 0.00218  -0.05826 150 PHE A O   
1353 O  O   B PHE A 150 ? 0.16216 0.23674 0.27348 -0.07359 -0.01362 0.00680  150 PHE A O   
1354 C  CB  A PHE A 150 ? 0.17465 0.29488 0.27603 0.01944  -0.02056 0.00167  150 PHE A CB  
1355 C  CB  B PHE A 150 ? 0.20211 0.28588 0.24353 -0.01893 0.00648  -0.01898 150 PHE A CB  
1356 C  CG  A PHE A 150 ? 0.17501 0.32043 0.33097 -0.00551 -0.04417 0.03162  150 PHE A CG  
1357 C  CG  B PHE A 150 ? 0.19701 0.30896 0.30135 -0.01299 -0.02588 -0.01200 150 PHE A CG  
1358 C  CD1 A PHE A 150 ? 0.27288 0.33545 0.30584 0.01740  -0.10062 -0.01907 150 PHE A CD1 
1359 C  CD1 B PHE A 150 ? 0.21298 0.34195 0.29022 0.05592  -0.01175 0.00623  150 PHE A CD1 
1360 C  CD2 A PHE A 150 ? 0.24998 0.33820 0.32018 -0.01240 -0.08715 0.05914  150 PHE A CD2 
1361 C  CD2 B PHE A 150 ? 0.23433 0.31267 0.38219 -0.01419 0.00232  -0.00133 150 PHE A CD2 
1362 C  CE1 A PHE A 150 ? 0.30353 0.35003 0.34477 -0.00166 -0.03206 -0.03162 150 PHE A CE1 
1363 C  CE1 B PHE A 150 ? 0.18751 0.34356 0.30838 0.07345  -0.04608 0.03529  150 PHE A CE1 
1364 C  CE2 A PHE A 150 ? 0.28373 0.36149 0.35778 -0.02701 -0.08429 0.05201  150 PHE A CE2 
1365 C  CE2 B PHE A 150 ? 0.35739 0.34403 0.42595 0.00496  0.00056  0.02770  150 PHE A CE2 
1366 C  CZ  A PHE A 150 ? 0.32805 0.34767 0.36921 0.00462  -0.08675 -0.01864 150 PHE A CZ  
1367 C  CZ  B PHE A 150 ? 0.30570 0.33479 0.39498 0.02238  -0.02772 0.04239  150 PHE A CZ  
1368 N  N   . LEU A 151 ? 0.18907 0.23109 0.29271 -0.06082 -0.00974 0.00768  151 LEU A N   
1369 C  CA  . LEU A 151 ? 0.19617 0.20586 0.30753 -0.06367 -0.00872 -0.01799 151 LEU A CA  
1370 C  C   . LEU A 151 ? 0.20836 0.20616 0.27155 -0.07913 0.02705  -0.01754 151 LEU A C   
1371 O  O   . LEU A 151 ? 0.23170 0.21182 0.24124 -0.02857 0.04002  -0.01163 151 LEU A O   
1372 C  CB  . LEU A 151 ? 0.27379 0.16874 0.28887 -0.00685 -0.01395 -0.01866 151 LEU A CB  
1373 C  CG  . LEU A 151 ? 0.25919 0.17324 0.27923 -0.01245 -0.01084 0.00493  151 LEU A CG  
1374 C  CD1 . LEU A 151 ? 0.32277 0.17696 0.35117 -0.08367 -0.02170 0.04306  151 LEU A CD1 
1375 C  CD2 . LEU A 151 ? 0.31936 0.18976 0.34943 -0.00274 -0.05533 0.01198  151 LEU A CD2 
1376 N  N   . THR A 152 ? 0.17709 0.16573 0.28091 -0.03330 -0.01913 0.00606  152 THR A N   
1377 C  CA  . THR A 152 ? 0.16664 0.17070 0.24400 -0.02902 -0.01258 -0.00875 152 THR A CA  
1378 C  C   . THR A 152 ? 0.19143 0.20222 0.24325 -0.03551 0.02626  -0.03538 152 THR A C   
1379 O  O   . THR A 152 ? 0.19588 0.21558 0.21545 -0.02587 0.01875  -0.02142 152 THR A O   
1380 C  CB  . THR A 152 ? 0.19609 0.19193 0.21796 -0.04466 -0.00726 -0.01424 152 THR A CB  
1381 O  OG1 . THR A 152 ? 0.22476 0.17718 0.24420 -0.00016 0.00042  -0.01721 152 THR A OG1 
1382 C  CG2 . THR A 152 ? 0.23164 0.21760 0.21070 -0.02263 -0.01628 0.00229  152 THR A CG2 
1383 N  N   . PHE A 153 ? 0.18740 0.18925 0.26881 0.00348  0.01283  -0.00769 153 PHE A N   
1384 C  CA  . PHE A 153 ? 0.20358 0.18591 0.24381 0.00501  0.02179  0.01160  153 PHE A CA  
1385 C  C   . PHE A 153 ? 0.20684 0.19290 0.26326 -0.02157 -0.01387 -0.01239 153 PHE A C   
1386 O  O   . PHE A 153 ? 0.22807 0.20749 0.23652 -0.00144 0.00483  0.00566  153 PHE A O   
1387 C  CB  . PHE A 153 ? 0.20536 0.21011 0.25084 0.02163  0.01174  0.02794  153 PHE A CB  
1388 C  CG  . PHE A 153 ? 0.23139 0.19342 0.22462 -0.01076 0.01898  0.00898  153 PHE A CG  
1389 C  CD1 . PHE A 153 ? 0.25311 0.21133 0.21640 -0.00052 0.03013  0.02610  153 PHE A CD1 
1390 C  CD2 . PHE A 153 ? 0.21699 0.19310 0.22720 0.00764  -0.01018 -0.01956 153 PHE A CD2 
1391 C  CE1 . PHE A 153 ? 0.25615 0.20972 0.25117 -0.00201 0.04256  0.00564  153 PHE A CE1 
1392 C  CE2 . PHE A 153 ? 0.26512 0.19960 0.26997 -0.01167 -0.00632 -0.01354 153 PHE A CE2 
1393 C  CZ  . PHE A 153 ? 0.28204 0.22047 0.21992 -0.00847 0.01607  0.02286  153 PHE A CZ  
1394 N  N   . TYR A 154 ? 0.19179 0.21070 0.26911 -0.03123 0.02348  -0.00390 154 TYR A N   
1395 C  CA  . TYR A 154 ? 0.19004 0.25852 0.28912 -0.06942 -0.02029 0.01303  154 TYR A CA  
1396 C  C   . TYR A 154 ? 0.17138 0.23855 0.22942 -0.01493 -0.00334 -0.01287 154 TYR A C   
1397 O  O   . TYR A 154 ? 0.22158 0.23293 0.24951 -0.01832 0.01677  0.00657  154 TYR A O   
1398 C  CB  . TYR A 154 ? 0.19114 0.30334 0.27207 -0.09223 0.02559  -0.00068 154 TYR A CB  
1399 C  CG  . TYR A 154 ? 0.23721 0.36357 0.31679 -0.10597 0.01970  -0.01831 154 TYR A CG  
1400 C  CD1 . TYR A 154 ? 0.25514 0.42556 0.32916 -0.09597 0.04113  0.01164  154 TYR A CD1 
1401 C  CD2 . TYR A 154 ? 0.45024 0.37783 0.30842 -0.18973 0.03972  0.02008  154 TYR A CD2 
1402 C  CE1 . TYR A 154 ? 0.32099 0.46775 0.38457 -0.18071 0.04323  0.03131  154 TYR A CE1 
1403 C  CE2 . TYR A 154 ? 0.47810 0.42861 0.33402 -0.23453 0.02344  0.02194  154 TYR A CE2 
1404 C  CZ  . TYR A 154 ? 0.40615 0.46692 0.38670 -0.22264 0.09583  0.04191  154 TYR A CZ  
1405 O  OH  . TYR A 154 ? 0.55729 0.52868 0.41752 -0.22774 0.09073  0.02795  154 TYR A OH  
1406 N  N   . LEU A 155 ? 0.19615 0.19668 0.28235 -0.00781 0.01675  0.00416  155 LEU A N   
1407 C  CA  . LEU A 155 ? 0.22392 0.19411 0.24842 0.00889  0.01153  0.01987  155 LEU A CA  
1408 C  C   . LEU A 155 ? 0.24919 0.19246 0.24295 -0.00815 0.04922  0.00535  155 LEU A C   
1409 O  O   . LEU A 155 ? 0.18029 0.20436 0.26366 -0.00885 0.05240  0.00787  155 LEU A O   
1410 C  CB  . LEU A 155 ? 0.22470 0.20963 0.24872 0.02158  0.00415  -0.00535 155 LEU A CB  
1411 C  CG  . LEU A 155 ? 0.21231 0.21038 0.27547 -0.02455 0.04416  -0.00828 155 LEU A CG  
1412 C  CD1 . LEU A 155 ? 0.26200 0.25331 0.24985 -0.02091 0.00153  -0.00166 155 LEU A CD1 
1413 C  CD2 . LEU A 155 ? 0.39716 0.24038 0.25206 -0.02383 0.03873  0.01558  155 LEU A CD2 
1414 N  N   . LEU A 156 ? 0.19366 0.20271 0.23941 -0.02567 0.01429  0.01486  156 LEU A N   
1415 C  CA  . LEU A 156 ? 0.22405 0.18747 0.24912 -0.00542 0.01967  -0.00590 156 LEU A CA  
1416 C  C   . LEU A 156 ? 0.19902 0.20264 0.24947 0.00942  -0.01457 -0.02180 156 LEU A C   
1417 O  O   . LEU A 156 ? 0.21161 0.23633 0.23627 0.00356  0.00619  0.00548  156 LEU A O   
1418 C  CB  . LEU A 156 ? 0.22690 0.19260 0.31406 -0.01304 -0.02558 0.00425  156 LEU A CB  
1419 C  CG  . LEU A 156 ? 0.22138 0.25275 0.32508 -0.00694 0.01360  0.00331  156 LEU A CG  
1420 C  CD1 . LEU A 156 ? 0.15816 0.29838 0.36153 -0.01296 -0.02504 0.02021  156 LEU A CD1 
1421 C  CD2 . LEU A 156 ? 0.34948 0.26435 0.26667 -0.06236 0.02984  0.05910  156 LEU A CD2 
1422 N  N   . TYR A 157 ? 0.15725 0.20931 0.25961 -0.00522 0.00499  0.01000  157 TYR A N   
1423 C  CA  . TYR A 157 ? 0.14671 0.24468 0.28903 -0.00007 -0.02620 0.00865  157 TYR A CA  
1424 C  C   . TYR A 157 ? 0.21812 0.22916 0.29096 -0.02859 0.01902  0.01169  157 TYR A C   
1425 O  O   . TYR A 157 ? 0.22604 0.25117 0.28394 0.01308  0.02885  0.01515  157 TYR A O   
1426 C  CB  . TYR A 157 ? 0.14596 0.24831 0.32672 0.02863  0.02473  -0.02521 157 TYR A CB  
1427 C  CG  . TYR A 157 ? 0.15775 0.25959 0.28041 -0.01027 0.00640  0.01670  157 TYR A CG  
1428 C  CD1 . TYR A 157 ? 0.17338 0.31810 0.27418 -0.02656 0.00461  -0.01497 157 TYR A CD1 
1429 C  CD2 . TYR A 157 ? 0.25127 0.24697 0.31071 0.04719  -0.01543 -0.01327 157 TYR A CD2 
1430 C  CE1 . TYR A 157 ? 0.19181 0.30582 0.29218 -0.00439 0.01285  -0.03132 157 TYR A CE1 
1431 C  CE2 . TYR A 157 ? 0.18080 0.27692 0.31532 -0.00329 0.01132  0.00045  157 TYR A CE2 
1432 C  CZ  . TYR A 157 ? 0.18035 0.29818 0.31144 -0.01552 0.05671  -0.03878 157 TYR A CZ  
1433 O  OH  . TYR A 157 ? 0.27051 0.33141 0.32929 0.03617  0.07300  -0.01412 157 TYR A OH  
1434 N  N   . VAL A 158 ? 0.21511 0.22227 0.27857 -0.03394 0.01472  0.01578  158 VAL A N   
1435 C  CA  . VAL A 158 ? 0.25111 0.24005 0.29913 -0.03740 0.02610  0.01807  158 VAL A CA  
1436 C  C   . VAL A 158 ? 0.19914 0.29059 0.29493 -0.01424 0.01662  0.03661  158 VAL A C   
1437 O  O   . VAL A 158 ? 0.27197 0.42381 0.27413 0.00373  0.03716  0.05741  158 VAL A O   
1438 C  CB  . VAL A 158 ? 0.19346 0.29710 0.27904 -0.06331 0.02951  0.01081  158 VAL A CB  
1439 C  CG1 . VAL A 158 ? 0.25131 0.35277 0.34211 -0.06560 0.03033  -0.00949 158 VAL A CG1 
1440 C  CG2 . VAL A 158 ? 0.28022 0.29445 0.29678 -0.03148 0.10903  0.02788  158 VAL A CG2 
1441 N  N   . LYS A 159 ? 0.19147 0.23620 0.28442 -0.03011 -0.01897 0.02135  159 LYS A N   
1442 C  CA  . LYS A 159 ? 0.26078 0.21374 0.27696 -0.03526 -0.01801 0.03759  159 LYS A CA  
1443 C  C   . LYS A 159 ? 0.30271 0.21531 0.25995 -0.00602 0.06313  0.02639  159 LYS A C   
1444 O  O   . LYS A 159 ? 0.30949 0.27212 0.26912 -0.03092 0.03308  0.03189  159 LYS A O   
1445 C  CB  . LYS A 159 ? 0.33965 0.21015 0.37155 -0.01259 -0.03673 0.02433  159 LYS A CB  
1446 C  CG  . LYS A 159 ? 0.37052 0.30407 0.45126 0.03662  -0.14564 0.01986  159 LYS A CG  
1447 C  CD  . LYS A 159 ? 0.50188 0.37347 0.44386 0.01392  -0.10595 -0.01706 159 LYS A CD  
1448 C  CE  . LYS A 159 ? 0.46813 0.38356 0.38590 0.04653  -0.03079 0.07373  159 LYS A CE  
1449 N  NZ  . LYS A 159 ? 0.48406 0.40774 0.39910 0.01231  0.00933  0.09679  159 LYS A NZ  
1450 N  N   . TYR A 160 ? 0.21217 0.22330 0.24720 0.00233  0.01226  0.00455  160 TYR A N   
1451 C  CA  . TYR A 160 ? 0.22845 0.21495 0.29450 0.00825  0.02675  0.01313  160 TYR A CA  
1452 C  C   . TYR A 160 ? 0.18177 0.23101 0.34909 0.02623  0.07767  0.06415  160 TYR A C   
1453 O  O   . TYR A 160 ? 0.20903 0.22851 0.35214 0.00498  0.02409  -0.00797 160 TYR A O   
1454 C  CB  . TYR A 160 ? 0.17126 0.22091 0.25314 -0.00584 -0.00123 0.01157  160 TYR A CB  
1455 C  CG  . TYR A 160 ? 0.23429 0.20209 0.24972 -0.01396 0.00179  0.02048  160 TYR A CG  
1456 C  CD1 . TYR A 160 ? 0.20247 0.21480 0.25321 0.01744  0.00598  0.01662  160 TYR A CD1 
1457 C  CD2 . TYR A 160 ? 0.20667 0.18675 0.27131 0.01075  0.03334  0.02436  160 TYR A CD2 
1458 C  CE1 . TYR A 160 ? 0.15031 0.21820 0.25217 0.02264  0.02868  -0.00556 160 TYR A CE1 
1459 C  CE2 . TYR A 160 ? 0.22770 0.19202 0.22041 0.00476  0.01495  0.01973  160 TYR A CE2 
1460 C  CZ  . TYR A 160 ? 0.21692 0.20058 0.22521 0.02798  0.01592  -0.00975 160 TYR A CZ  
1461 O  OH  . TYR A 160 ? 0.26194 0.20760 0.24499 0.01150  0.02441  -0.00388 160 TYR A OH  
1462 N  N   . THR A 161 ? 0.15701 0.23961 0.31931 0.04222  0.03582  0.05927  161 THR A N   
1463 C  CA  . THR A 161 ? 0.17440 0.26129 0.27026 0.05291  0.02896  0.04646  161 THR A CA  
1464 C  C   . THR A 161 ? 0.18156 0.24123 0.31093 -0.03135 -0.01975 0.00409  161 THR A C   
1465 O  O   . THR A 161 ? 0.25857 0.24412 0.32164 -0.02277 0.02849  0.01706  161 THR A O   
1466 C  CB  . THR A 161 ? 0.21505 0.27778 0.23248 0.01830  -0.00597 0.02878  161 THR A CB  
1467 O  OG1 . THR A 161 ? 0.20442 0.29669 0.30342 -0.00511 -0.00490 -0.02814 161 THR A OG1 
1468 C  CG2 . THR A 161 ? 0.20619 0.27202 0.26586 0.01818  0.02755  0.01953  161 THR A CG2 
1469 N  N   A LYS A 162 ? 0.12840 0.27042 0.28255 0.07131  -0.01083 -0.04117 162 LYS A N   
1470 N  N   B LYS A 162 ? 0.20429 0.26614 0.27975 0.00193  0.00944  -0.01132 162 LYS A N   
1471 C  CA  A LYS A 162 ? 0.16992 0.29471 0.27245 0.05459  0.03793  0.00113  162 LYS A CA  
1472 C  CA  B LYS A 162 ? 0.19847 0.27774 0.29299 -0.03451 0.01882  0.01056  162 LYS A CA  
1473 C  C   A LYS A 162 ? 0.17972 0.28815 0.27444 0.06785  0.09151  0.01960  162 LYS A C   
1474 C  C   B LYS A 162 ? 0.19325 0.25849 0.28329 -0.04604 0.02679  0.00078  162 LYS A C   
1475 O  O   A LYS A 162 ? 0.25838 0.28904 0.27103 0.08794  0.07694  -0.02211 162 LYS A O   
1476 O  O   B LYS A 162 ? 0.19143 0.23371 0.23935 -0.07390 0.01727  0.00564  162 LYS A O   
1477 C  CB  A LYS A 162 ? 0.25780 0.34179 0.24517 0.00732  -0.00479 0.01105  162 LYS A CB  
1478 C  CB  B LYS A 162 ? 0.26770 0.34523 0.30397 0.00392  0.01326  0.01279  162 LYS A CB  
1479 C  CG  A LYS A 162 ? 0.28684 0.36353 0.27411 -0.06844 -0.06365 -0.01782 162 LYS A CG  
1480 C  CG  B LYS A 162 ? 0.32326 0.38871 0.30849 0.00897  0.00262  0.01643  162 LYS A CG  
1481 C  CD  A LYS A 162 ? 0.29163 0.40140 0.36421 -0.08528 -0.00393 -0.02958 162 LYS A CD  
1482 C  CD  B LYS A 162 ? 0.26999 0.43888 0.31387 -0.00486 0.07596  0.04674  162 LYS A CD  
1483 C  CE  A LYS A 162 ? 0.31946 0.43062 0.40453 -0.08210 -0.04162 -0.06151 162 LYS A CE  
1484 C  CE  B LYS A 162 ? 0.32896 0.46206 0.28227 -0.04245 0.04799  0.06406  162 LYS A CE  
1485 N  NZ  A LYS A 162 ? 0.37487 0.43051 0.43461 -0.05382 -0.03427 -0.10347 162 LYS A NZ  
1486 N  NZ  B LYS A 162 ? 0.35046 0.48974 0.35947 -0.03409 0.02747  0.04067  162 LYS A NZ  
1487 N  N   . GLU A 163 ? 0.20513 0.28572 0.28601 0.00469  0.05949  0.01315  163 GLU A N   
1488 C  CA  . GLU A 163 ? 0.18209 0.28292 0.34020 -0.06795 0.05632  -0.00152 163 GLU A CA  
1489 C  C   . GLU A 163 ? 0.19711 0.27414 0.34229 -0.04546 0.04652  -0.02270 163 GLU A C   
1490 O  O   . GLU A 163 ? 0.23733 0.31891 0.37873 -0.02832 0.08393  -0.01173 163 GLU A O   
1491 C  CB  . GLU A 163 ? 0.21363 0.28062 0.36795 -0.05938 0.07303  -0.00786 163 GLU A CB  
1492 C  CG  . GLU A 163 ? 0.28788 0.30071 0.31974 -0.04793 0.04464  -0.03675 163 GLU A CG  
1493 C  CD  . GLU A 163 ? 0.28207 0.32609 0.32047 -0.00488 0.02949  -0.03601 163 GLU A CD  
1494 O  OE1 . GLU A 163 ? 0.25991 0.33285 0.40181 -0.01857 0.01384  0.00371  163 GLU A OE1 
1495 O  OE2 . GLU A 163 ? 0.28486 0.34564 0.33819 0.00625  0.05386  -0.01123 163 GLU A OE2 
1496 N  N   . ASN A 164 ? 0.18691 0.24847 0.29573 -0.03308 0.02272  -0.04102 164 ASN A N   
1497 C  CA  . ASN A 164 ? 0.25092 0.24722 0.31256 0.01673  -0.02486 -0.02519 164 ASN A CA  
1498 C  C   . ASN A 164 ? 0.20473 0.22061 0.28089 0.03442  0.00067  -0.02762 164 ASN A C   
1499 O  O   . ASN A 164 ? 0.17935 0.23433 0.26837 0.02787  0.04418  -0.02746 164 ASN A O   
1500 C  CB  . ASN A 164 ? 0.24383 0.28091 0.28487 0.05762  -0.04778 -0.03302 164 ASN A CB  
1501 C  CG  . ASN A 164 ? 0.27176 0.27630 0.24226 0.08376  -0.04960 -0.04257 164 ASN A CG  
1502 O  OD1 . ASN A 164 ? 0.27487 0.29924 0.23164 0.01908  0.04388  -0.01178 164 ASN A OD1 
1503 N  ND2 . ASN A 164 ? 0.26896 0.34981 0.25139 0.04967  0.06087  0.02074  164 ASN A ND2 
1504 N  N   . TRP A 165 ? 0.24328 0.24578 0.30382 0.02786  0.00108  -0.02434 165 TRP A N   
1505 C  CA  . TRP A 165 ? 0.23851 0.24401 0.32252 0.04818  0.02193  0.00259  165 TRP A CA  
1506 C  C   . TRP A 165 ? 0.22414 0.24047 0.27557 0.02788  0.00022  -0.02136 165 TRP A C   
1507 O  O   . TRP A 165 ? 0.28208 0.25788 0.23927 0.03037  0.05053  -0.00038 165 TRP A O   
1508 C  CB  . TRP A 165 ? 0.24108 0.24173 0.33416 0.04088  0.04021  -0.00051 165 TRP A CB  
1509 C  CG  . TRP A 165 ? 0.21970 0.27779 0.41566 0.04803  0.03395  -0.01561 165 TRP A CG  
1510 C  CD1 . TRP A 165 ? 0.19986 0.27527 0.46864 0.07096  0.01967  0.02389  165 TRP A CD1 
1511 C  CD2 . TRP A 165 ? 0.32987 0.29359 0.35043 0.06108  0.03101  0.00993  165 TRP A CD2 
1512 N  NE1 . TRP A 165 ? 0.26517 0.32092 0.37925 0.01557  0.00512  0.03250  165 TRP A NE1 
1513 C  CE2 . TRP A 165 ? 0.32363 0.31059 0.36008 0.05763  -0.03427 0.02045  165 TRP A CE2 
1514 C  CE3 . TRP A 165 ? 0.42706 0.32014 0.32925 0.09843  -0.02452 0.04925  165 TRP A CE3 
1515 C  CZ2 . TRP A 165 ? 0.34263 0.34117 0.33139 0.03304  -0.09766 0.02502  165 TRP A CZ2 
1516 C  CZ3 . TRP A 165 ? 0.32060 0.34971 0.34953 0.07190  0.00969  0.05250  165 TRP A CZ3 
1517 C  CH2 . TRP A 165 ? 0.38572 0.34089 0.37684 0.04886  -0.03085 0.00564  165 TRP A CH2 
1518 N  N   A MET A 166 ? 0.19419 0.22779 0.31186 -0.01183 -0.00296 0.00648  166 MET A N   
1519 N  N   B MET A 166 ? 0.19228 0.20556 0.24132 0.03670  0.03623  -0.01938 166 MET A N   
1520 C  CA  A MET A 166 ? 0.24005 0.25571 0.29390 0.01179  -0.02581 -0.04542 166 MET A CA  
1521 C  CA  B MET A 166 ? 0.16604 0.22921 0.23171 0.01876  -0.00751 -0.04950 166 MET A CA  
1522 C  C   A MET A 166 ? 0.23435 0.22789 0.26075 0.00044  0.03069  -0.03860 166 MET A C   
1523 C  C   B MET A 166 ? 0.18530 0.22473 0.24145 -0.01309 0.02182  -0.03069 166 MET A C   
1524 O  O   A MET A 166 ? 0.19406 0.23767 0.20879 0.01513  -0.01474 -0.02213 166 MET A O   
1525 O  O   B MET A 166 ? 0.16307 0.24508 0.25917 -0.01535 0.01863  -0.00964 166 MET A O   
1526 C  CB  A MET A 166 ? 0.37270 0.30136 0.32128 0.02953  -0.04657 -0.05882 166 MET A CB  
1527 C  CB  B MET A 166 ? 0.22963 0.24382 0.20123 -0.02500 -0.02215 -0.04365 166 MET A CB  
1528 C  CG  A MET A 166 ? 0.52647 0.36985 0.32255 -0.00279 -0.08075 -0.04797 166 MET A CG  
1529 C  CG  B MET A 166 ? 0.22419 0.31856 0.27780 -0.00823 -0.09548 -0.03483 166 MET A CG  
1530 S  SD  A MET A 166 ? 0.64015 0.43690 0.45116 -0.02335 -0.03728 -0.06982 166 MET A SD  
1531 S  SD  B MET A 166 ? 0.42961 0.34882 0.33190 -0.01989 -0.13596 -0.06938 166 MET A SD  
1532 C  CE  A MET A 166 ? 0.58457 0.45515 0.47558 -0.02163 -0.02694 -0.07040 166 MET A CE  
1533 C  CE  B MET A 166 ? 0.45411 0.38451 0.36519 0.00298  0.00190  -0.05227 166 MET A CE  
1534 N  N   . ASN A 167 ? 0.21488 0.20991 0.26438 0.00976  0.03393  -0.02139 167 ASN A N   
1535 C  CA  . ASN A 167 ? 0.20252 0.21476 0.23836 -0.00409 0.01354  0.00381  167 ASN A CA  
1536 C  C   . ASN A 167 ? 0.17701 0.24069 0.22843 0.01575  0.02927  0.01599  167 ASN A C   
1537 O  O   . ASN A 167 ? 0.20677 0.25541 0.22668 0.00645  0.04484  -0.00511 167 ASN A O   
1538 C  CB  . ASN A 167 ? 0.19117 0.22720 0.24606 -0.00146 0.01167  0.02257  167 ASN A CB  
1539 C  CG  . ASN A 167 ? 0.17730 0.23284 0.23140 -0.00517 0.01970  -0.00336 167 ASN A CG  
1540 O  OD1 . ASN A 167 ? 0.26905 0.22264 0.21791 0.00134  0.00865  -0.02648 167 ASN A OD1 
1541 N  ND2 . ASN A 167 ? 0.20395 0.24139 0.22939 0.02599  0.02563  -0.00405 167 ASN A ND2 
1542 N  N   . TYR A 168 ? 0.21986 0.23229 0.25940 0.02596  0.02400  -0.00208 168 TYR A N   
1543 C  CA  . TYR A 168 ? 0.16584 0.25053 0.26131 -0.02275 0.01159  -0.01928 168 TYR A CA  
1544 C  C   . TYR A 168 ? 0.17663 0.24225 0.23469 -0.03121 -0.01806 -0.04997 168 TYR A C   
1545 O  O   . TYR A 168 ? 0.19624 0.25553 0.22737 0.00073  -0.02741 -0.03546 168 TYR A O   
1546 C  CB  . TYR A 168 ? 0.15083 0.28259 0.29689 -0.01642 -0.00053 -0.01708 168 TYR A CB  
1547 C  CG  . TYR A 168 ? 0.23679 0.26922 0.24984 0.04049  -0.00409 -0.01854 168 TYR A CG  
1548 C  CD1 . TYR A 168 ? 0.15423 0.29108 0.22983 -0.01188 0.01120  -0.00348 168 TYR A CD1 
1549 C  CD2 . TYR A 168 ? 0.18931 0.30522 0.30818 -0.04101 0.04658  -0.03710 168 TYR A CD2 
1550 C  CE1 . TYR A 168 ? 0.13751 0.33610 0.24284 -0.02006 0.04512  -0.03031 168 TYR A CE1 
1551 C  CE2 . TYR A 168 ? 0.22535 0.30912 0.33073 -0.02910 0.03431  -0.01793 168 TYR A CE2 
1552 C  CZ  . TYR A 168 ? 0.20802 0.31790 0.27346 -0.04942 0.06564  0.00864  168 TYR A CZ  
1553 O  OH  . TYR A 168 ? 0.18824 0.35007 0.29129 -0.02866 0.03856  -0.00553 168 TYR A OH  
1554 N  N   . ILE A 169 ? 0.15982 0.21823 0.24526 -0.00557 -0.01686 -0.01803 169 ILE A N   
1555 C  CA  . ILE A 169 ? 0.21747 0.22739 0.26734 -0.03369 0.02519  -0.00504 169 ILE A CA  
1556 C  C   . ILE A 169 ? 0.16596 0.26355 0.20956 -0.01253 -0.01235 -0.01316 169 ILE A C   
1557 O  O   . ILE A 169 ? 0.21626 0.24529 0.21912 0.01406  0.00831  -0.01900 169 ILE A O   
1558 C  CB  . ILE A 169 ? 0.23065 0.21926 0.26827 -0.01443 0.02317  -0.00893 169 ILE A CB  
1559 C  CG1 . ILE A 169 ? 0.23580 0.23832 0.25451 0.01072  -0.01409 -0.01427 169 ILE A CG1 
1560 C  CG2 . ILE A 169 ? 0.20258 0.21981 0.28972 0.01477  0.01640  -0.00653 169 ILE A CG2 
1561 C  CD1 . ILE A 169 ? 0.26401 0.25504 0.25386 0.02704  -0.03189 -0.00744 169 ILE A CD1 
1562 N  N   . VAL A 170 ? 0.17682 0.24726 0.22587 0.01689  -0.00251 -0.00434 170 VAL A N   
1563 C  CA  . VAL A 170 ? 0.14227 0.25645 0.33169 0.01562  -0.02206 -0.01750 170 VAL A CA  
1564 C  C   . VAL A 170 ? 0.11781 0.25015 0.26822 0.02789  0.03832  -0.00224 170 VAL A C   
1565 O  O   . VAL A 170 ? 0.18182 0.24680 0.31906 0.02150  0.07775  -0.00823 170 VAL A O   
1566 C  CB  . VAL A 170 ? 0.16090 0.29560 0.28035 0.04460  -0.04445 -0.00244 170 VAL A CB  
1567 C  CG1 . VAL A 170 ? 0.15717 0.33983 0.34861 0.04431  -0.05081 0.00308  170 VAL A CG1 
1568 C  CG2 . VAL A 170 ? 0.30219 0.33958 0.30778 -0.00504 -0.06033 -0.02241 170 VAL A CG2 
1569 N  N   . PHE A 171 ? 0.17306 0.21599 0.20887 0.03434  -0.02011 -0.01230 171 PHE A N   
1570 C  CA  . PHE A 171 ? 0.17911 0.24304 0.18733 0.00742  -0.00940 0.02238  171 PHE A CA  
1571 C  C   . PHE A 171 ? 0.17187 0.22902 0.21059 0.01752  0.01836  -0.00736 171 PHE A C   
1572 O  O   . PHE A 171 ? 0.16063 0.22464 0.23279 0.01661  0.00856  0.00363  171 PHE A O   
1573 C  CB  . PHE A 171 ? 0.20890 0.23161 0.22132 -0.02456 0.00623  -0.00061 171 PHE A CB  
1574 C  CG  . PHE A 171 ? 0.16685 0.20760 0.21461 0.00841  0.00684  0.01699  171 PHE A CG  
1575 C  CD1 . PHE A 171 ? 0.19341 0.22242 0.28174 0.02521  0.06068  0.02993  171 PHE A CD1 
1576 C  CD2 . PHE A 171 ? 0.23710 0.21438 0.24835 -0.01318 0.00259  0.00657  171 PHE A CD2 
1577 C  CE1 . PHE A 171 ? 0.26655 0.23876 0.28173 -0.00442 0.08664  0.01636  171 PHE A CE1 
1578 C  CE2 . PHE A 171 ? 0.23584 0.22308 0.28036 0.00337  0.03516  -0.02409 171 PHE A CE2 
1579 C  CZ  . PHE A 171 ? 0.27751 0.23817 0.29450 0.02813  0.08323  -0.00369 171 PHE A CZ  
1580 N  N   . TYR A 172 ? 0.17394 0.23662 0.22957 0.01545  -0.01035 -0.00172 172 TYR A N   
1581 C  CA  . TYR A 172 ? 0.17480 0.23972 0.19878 0.01905  0.01294  -0.01099 172 TYR A CA  
1582 C  C   . TYR A 172 ? 0.12368 0.22799 0.21835 0.02219  0.01659  0.00763  172 TYR A C   
1583 O  O   . TYR A 172 ? 0.20865 0.23546 0.19522 0.03319  0.00509  -0.01334 172 TYR A O   
1584 C  CB  . TYR A 172 ? 0.13890 0.25217 0.28336 0.01008  0.01159  -0.02655 172 TYR A CB  
1585 C  CG  . TYR A 172 ? 0.15584 0.27704 0.24892 0.00713  0.01546  -0.04299 172 TYR A CG  
1586 C  CD1 . TYR A 172 ? 0.16312 0.26909 0.29318 -0.02204 -0.03262 -0.01604 172 TYR A CD1 
1587 C  CD2 . TYR A 172 ? 0.17037 0.26511 0.25744 -0.03018 0.02834  -0.03500 172 TYR A CD2 
1588 C  CE1 . TYR A 172 ? 0.20971 0.27375 0.29095 -0.03662 0.01147  -0.04111 172 TYR A CE1 
1589 C  CE2 . TYR A 172 ? 0.18577 0.27090 0.31615 -0.02110 -0.02033 -0.03718 172 TYR A CE2 
1590 C  CZ  . TYR A 172 ? 0.19865 0.26921 0.30531 -0.04058 -0.03380 -0.01499 172 TYR A CZ  
1591 O  OH  . TYR A 172 ? 0.22750 0.30848 0.31162 -0.04669 -0.02025 -0.00893 172 TYR A OH  
1592 N  N   A PHE A 173 ? 0.23250 0.18776 0.23618 0.06474  0.00557  0.00859  173 PHE A N   
1593 N  N   B PHE A 173 ? 0.06642 0.20551 0.24407 -0.02668 -0.00785 -0.00255 173 PHE A N   
1594 C  CA  A PHE A 173 ? 0.15056 0.17315 0.23560 0.03118  0.05318  0.00850  173 PHE A CA  
1595 C  CA  B PHE A 173 ? 0.16077 0.24961 0.22302 -0.03641 -0.00242 -0.00690 173 PHE A CA  
1596 C  C   A PHE A 173 ? 0.07198 0.20012 0.23890 0.03070  -0.00086 -0.03277 173 PHE A C   
1597 C  C   B PHE A 173 ? 0.19717 0.23083 0.24069 -0.00835 0.03837  0.00975  173 PHE A C   
1598 O  O   A PHE A 173 ? 0.15052 0.22823 0.20637 -0.00182 -0.02120 -0.04241 173 PHE A O   
1599 O  O   B PHE A 173 ? 0.10858 0.25321 0.18515 0.06680  0.01941  0.02397  173 PHE A O   
1600 C  CB  A PHE A 173 ? 0.33098 0.16829 0.23407 -0.01061 0.06760  -0.00974 173 PHE A CB  
1601 C  CB  B PHE A 173 ? 0.29893 0.25284 0.21672 -0.08350 -0.02639 -0.03538 173 PHE A CB  
1602 C  CG  A PHE A 173 ? 0.32478 0.20060 0.28630 0.05328  0.03710  -0.02899 173 PHE A CG  
1603 C  CG  B PHE A 173 ? 0.29224 0.24864 0.15525 -0.08273 -0.02886 -0.07577 173 PHE A CG  
1604 C  CD1 A PHE A 173 ? 0.31003 0.21240 0.39256 0.04614  0.10236  0.00969  173 PHE A CD1 
1605 C  CD1 B PHE A 173 ? 0.26824 0.25939 0.20960 -0.10059 -0.02998 -0.09112 173 PHE A CD1 
1606 C  CD2 A PHE A 173 ? 0.34515 0.25794 0.39690 0.02084  -0.09332 0.01575  173 PHE A CD2 
1607 C  CD2 B PHE A 173 ? 0.28544 0.29502 0.29380 -0.11257 0.05081  -0.07196 173 PHE A CD2 
1608 C  CE1 A PHE A 173 ? 0.24627 0.28665 0.38879 0.00467  0.11718  -0.01275 173 PHE A CE1 
1609 C  CE1 B PHE A 173 ? 0.29678 0.26809 0.27285 -0.10017 -0.06481 -0.10333 173 PHE A CE1 
1610 C  CE2 A PHE A 173 ? 0.37579 0.28852 0.29521 0.03564  -0.05545 0.04420  173 PHE A CE2 
1611 C  CE2 B PHE A 173 ? 0.38116 0.28350 0.30126 -0.06810 0.03640  -0.08076 173 PHE A CE2 
1612 C  CZ  A PHE A 173 ? 0.34767 0.30858 0.28316 0.02457  0.05887  0.00473  173 PHE A CZ  
1613 C  CZ  B PHE A 173 ? 0.36885 0.29173 0.24735 -0.09351 -0.03908 -0.12460 173 PHE A CZ  
1614 N  N   A MET A 174 ? 0.10989 0.20154 0.23360 0.07332  -0.03392 0.01903  174 MET A N   
1615 N  N   B MET A 174 ? 0.22484 0.20354 0.29002 -0.08768 -0.05171 -0.00940 174 MET A N   
1616 C  CA  A MET A 174 ? 0.11163 0.18174 0.21830 0.07379  -0.03033 0.01872  174 MET A CA  
1617 C  CA  B MET A 174 ? 0.20948 0.21374 0.27518 -0.06899 -0.07261 -0.00557 174 MET A CA  
1618 C  C   A MET A 174 ? 0.11281 0.19613 0.20167 0.02152  0.01171  0.02006  174 MET A C   
1619 C  C   B MET A 174 ? 0.10075 0.19670 0.26577 -0.03522 -0.03426 -0.02117 174 MET A C   
1620 O  O   A MET A 174 ? 0.15563 0.22629 0.16286 0.04832  0.00136  0.01038  174 MET A O   
1621 O  O   B MET A 174 ? 0.09639 0.19844 0.27749 -0.04883 -0.03536 0.02135  174 MET A O   
1622 C  CB  A MET A 174 ? 0.11676 0.19782 0.19179 0.06831  -0.02138 0.04714  174 MET A CB  
1623 C  CB  B MET A 174 ? 0.23712 0.23852 0.28989 -0.02744 -0.11782 -0.00962 174 MET A CB  
1624 C  CG  A MET A 174 ? 0.10673 0.17256 0.15476 0.06753  -0.02992 0.01432  174 MET A CG  
1625 C  CG  B MET A 174 ? 0.36138 0.28862 0.40967 0.01757  -0.04112 0.01456  174 MET A CG  
1626 S  SD  A MET A 174 ? 0.16625 0.21561 0.18525 0.06161  -0.01029 -0.00813 174 MET A SD  
1627 S  SD  B MET A 174 ? 0.26806 0.29499 0.43231 0.06358  -0.06786 0.05510  174 MET A SD  
1628 C  CE  A MET A 174 ? 0.13681 0.24475 0.20960 0.09835  0.02097  0.02645  174 MET A CE  
1629 C  CE  B MET A 174 ? 0.25051 0.25432 0.41288 0.02214  -0.10258 0.13621  174 MET A CE  
1630 N  N   . PHE A 175 ? 0.10799 0.19715 0.25384 -0.01816 -0.03607 -0.00356 175 PHE A N   
1631 C  CA  . PHE A 175 ? 0.08528 0.19995 0.26237 -0.02901 -0.02967 -0.01765 175 PHE A CA  
1632 C  C   . PHE A 175 ? 0.13911 0.21944 0.19341 0.03045  0.01092  0.02391  175 PHE A C   
1633 O  O   . PHE A 175 ? 0.12716 0.24972 0.20798 -0.00830 0.01384  -0.00556 175 PHE A O   
1634 C  CB  . PHE A 175 ? 0.10764 0.22288 0.26533 -0.07141 0.00279  -0.03151 175 PHE A CB  
1635 C  CG  . PHE A 175 ? 0.19752 0.26059 0.23369 -0.07048 0.05577  -0.01631 175 PHE A CG  
1636 C  CD1 . PHE A 175 ? 0.27414 0.26244 0.24129 -0.00734 0.01055  -0.05426 175 PHE A CD1 
1637 C  CD2 . PHE A 175 ? 0.28902 0.29654 0.36419 -0.08333 0.06070  -0.08169 175 PHE A CD2 
1638 C  CE1 . PHE A 175 ? 0.20587 0.28864 0.31978 -0.03312 0.05163  -0.02447 175 PHE A CE1 
1639 C  CE2 . PHE A 175 ? 0.32854 0.32735 0.43821 -0.11695 -0.03800 -0.10779 175 PHE A CE2 
1640 C  CZ  . PHE A 175 ? 0.35649 0.31591 0.41316 -0.05733 0.05973  -0.10294 175 PHE A CZ  
1641 N  N   . LEU A 176 ? 0.16768 0.21005 0.22380 0.02581  -0.01808 0.02012  176 LEU A N   
1642 C  CA  . LEU A 176 ? 0.15371 0.23556 0.23439 0.00986  -0.02526 -0.00888 176 LEU A CA  
1643 C  C   . LEU A 176 ? 0.09384 0.18879 0.24877 -0.01011 0.01588  -0.01923 176 LEU A C   
1644 O  O   . LEU A 176 ? 0.19880 0.21275 0.20235 0.01755  0.00170  -0.02048 176 LEU A O   
1645 C  CB  . LEU A 176 ? 0.14701 0.24827 0.24140 0.03573  -0.00770 0.01580  176 LEU A CB  
1646 C  CG  . LEU A 176 ? 0.13340 0.26864 0.31215 0.05343  -0.03520 -0.00028 176 LEU A CG  
1647 C  CD1 . LEU A 176 ? 0.26692 0.28067 0.29072 0.04683  -0.05313 0.00972  176 LEU A CD1 
1648 C  CD2 . LEU A 176 ? 0.27582 0.28306 0.34112 0.09582  0.01505  0.02787  176 LEU A CD2 
1649 N  N   . VAL A 177 ? 0.10201 0.20219 0.22156 -0.01129 -0.01040 -0.00540 177 VAL A N   
1650 C  CA  . VAL A 177 ? 0.09304 0.20035 0.23457 -0.00010 -0.03326 -0.02054 177 VAL A CA  
1651 C  C   . VAL A 177 ? 0.17893 0.17398 0.19986 0.02000  -0.04938 -0.01621 177 VAL A C   
1652 O  O   . VAL A 177 ? 0.19471 0.21572 0.19589 0.00032  -0.01026 -0.00874 177 VAL A O   
1653 C  CB  . VAL A 177 ? 0.11162 0.20031 0.22328 0.00433  0.00148  -0.02635 177 VAL A CB  
1654 C  CG1 . VAL A 177 ? 0.15995 0.24540 0.22357 -0.01367 0.02281  -0.01788 177 VAL A CG1 
1655 C  CG2 . VAL A 177 ? 0.20537 0.19466 0.25303 0.03463  -0.00088 -0.01614 177 VAL A CG2 
1656 N  N   . TRP A 178 ? 0.14343 0.17210 0.22353 0.02730  -0.02437 -0.01231 178 TRP A N   
1657 C  CA  . TRP A 178 ? 0.16059 0.17918 0.20526 0.04387  -0.03146 -0.00059 178 TRP A CA  
1658 C  C   . TRP A 178 ? 0.09143 0.20860 0.21637 0.02106  -0.01225 0.00078  178 TRP A C   
1659 O  O   . TRP A 178 ? 0.18302 0.19864 0.19584 0.02453  0.01357  -0.00805 178 TRP A O   
1660 C  CB  . TRP A 178 ? 0.13853 0.18910 0.22260 0.00628  -0.01292 0.01302  178 TRP A CB  
1661 C  CG  . TRP A 178 ? 0.12742 0.19024 0.19582 -0.00847 -0.01457 0.00275  178 TRP A CG  
1662 C  CD1 . TRP A 178 ? 0.15728 0.20008 0.18581 0.00798  -0.00059 0.00905  178 TRP A CD1 
1663 C  CD2 . TRP A 178 ? 0.15813 0.19204 0.20463 -0.01331 -0.01761 0.01386  178 TRP A CD2 
1664 N  NE1 . TRP A 178 ? 0.16037 0.20414 0.18898 0.03086  -0.00628 0.01207  178 TRP A NE1 
1665 C  CE2 . TRP A 178 ? 0.09854 0.20366 0.22205 0.02775  -0.01001 0.02904  178 TRP A CE2 
1666 C  CE3 . TRP A 178 ? 0.17730 0.19472 0.21187 0.03230  0.02020  0.01881  178 TRP A CE3 
1667 C  CZ2 . TRP A 178 ? 0.15518 0.19013 0.19417 0.01787  -0.00571 0.01616  178 TRP A CZ2 
1668 C  CZ3 . TRP A 178 ? 0.22187 0.19241 0.21616 0.01268  -0.00797 0.00138  178 TRP A CZ3 
1669 C  CH2 . TRP A 178 ? 0.17225 0.18185 0.21322 0.00184  0.03453  0.00224  178 TRP A CH2 
1670 N  N   . PHE A 179 ? 0.14342 0.20139 0.22576 -0.00049 -0.03451 -0.02193 179 PHE A N   
1671 C  CA  . PHE A 179 ? 0.14423 0.20349 0.22717 -0.00177 -0.01174 -0.00464 179 PHE A CA  
1672 C  C   . PHE A 179 ? 0.19063 0.21283 0.21540 0.03905  -0.01660 -0.01735 179 PHE A C   
1673 O  O   . PHE A 179 ? 0.17444 0.22756 0.20535 -0.01142 -0.01507 -0.02185 179 PHE A O   
1674 C  CB  . PHE A 179 ? 0.16493 0.28033 0.24553 -0.00652 -0.01225 -0.01667 179 PHE A CB  
1675 C  CG  . PHE A 179 ? 0.26222 0.36649 0.30323 0.01060  -0.02352 -0.03341 179 PHE A CG  
1676 C  CD1 . PHE A 179 ? 0.36964 0.39636 0.39805 -0.09915 -0.15557 0.01422  179 PHE A CD1 
1677 C  CD2 . PHE A 179 ? 0.23680 0.41919 0.31068 0.01788  -0.10674 0.01057  179 PHE A CD2 
1678 C  CE1 . PHE A 179 ? 0.35401 0.44420 0.39065 -0.07491 -0.12435 0.00772  179 PHE A CE1 
1679 C  CE2 . PHE A 179 ? 0.24572 0.46185 0.37862 -0.04868 -0.11163 -0.03221 179 PHE A CE2 
1680 C  CZ  . PHE A 179 ? 0.36725 0.46119 0.41844 -0.03538 -0.09445 0.01397  179 PHE A CZ  
1681 N  N   . LEU A 180 ? 0.16149 0.19874 0.19550 0.00294  -0.01837 0.00216  180 LEU A N   
1682 C  CA  . LEU A 180 ? 0.18462 0.18671 0.20126 0.01839  -0.03751 -0.00498 180 LEU A CA  
1683 C  C   . LEU A 180 ? 0.14820 0.19655 0.21218 0.03031  0.00122  -0.04458 180 LEU A C   
1684 O  O   . LEU A 180 ? 0.17622 0.21167 0.19105 0.01969  -0.01077 -0.02424 180 LEU A O   
1685 C  CB  . LEU A 180 ? 0.17593 0.18226 0.22171 0.04721  -0.00445 -0.00659 180 LEU A CB  
1686 C  CG  . LEU A 180 ? 0.20250 0.22080 0.20276 0.04267  -0.00088 -0.00869 180 LEU A CG  
1687 C  CD1 . LEU A 180 ? 0.20346 0.22649 0.23527 0.03279  0.00335  -0.00833 180 LEU A CD1 
1688 C  CD2 . LEU A 180 ? 0.15754 0.26749 0.33068 0.01078  -0.07395 -0.00301 180 LEU A CD2 
1689 N  N   . TYR A 181 ? 0.12349 0.19654 0.23640 0.01523  -0.01786 -0.01659 181 TYR A N   
1690 C  CA  . TYR A 181 ? 0.11616 0.19401 0.20637 0.02569  -0.01491 -0.00995 181 TYR A CA  
1691 C  C   . TYR A 181 ? 0.17751 0.18165 0.22683 -0.00552 0.00783  -0.03063 181 TYR A C   
1692 O  O   . TYR A 181 ? 0.20385 0.20105 0.21527 0.00229  -0.00955 -0.00811 181 TYR A O   
1693 C  CB  . TYR A 181 ? 0.14862 0.18922 0.22339 0.02295  -0.03595 -0.00839 181 TYR A CB  
1694 C  CG  . TYR A 181 ? 0.20092 0.16922 0.19711 -0.00124 -0.02626 -0.00247 181 TYR A CG  
1695 C  CD1 . TYR A 181 ? 0.18295 0.17505 0.20554 -0.00802 -0.04324 -0.00107 181 TYR A CD1 
1696 C  CD2 . TYR A 181 ? 0.15893 0.18165 0.22160 -0.01837 -0.00401 0.00672  181 TYR A CD2 
1697 C  CE1 . TYR A 181 ? 0.14161 0.18738 0.19837 -0.02335 0.00024  0.01530  181 TYR A CE1 
1698 C  CE2 . TYR A 181 ? 0.22313 0.16099 0.18575 -0.01817 -0.01711 -0.00568 181 TYR A CE2 
1699 C  CZ  . TYR A 181 ? 0.18531 0.18403 0.16619 -0.00012 0.00047  -0.01224 181 TYR A CZ  
1700 O  OH  . TYR A 181 ? 0.17040 0.18208 0.19592 -0.00111 -0.02106 -0.01451 181 TYR A OH  
1701 N  N   . GLY A 182 ? 0.18259 0.18630 0.22726 -0.00235 -0.00495 -0.02316 182 GLY A N   
1702 C  CA  . GLY A 182 ? 0.22909 0.20460 0.22346 -0.01434 -0.00258 -0.03044 182 GLY A CA  
1703 C  C   . GLY A 182 ? 0.19313 0.21793 0.21365 0.01438  0.00922  -0.00785 182 GLY A C   
1704 O  O   . GLY A 182 ? 0.22277 0.23866 0.22183 0.00214  -0.01608 -0.03621 182 GLY A O   
1705 N  N   . PHE A 183 ? 0.17847 0.21982 0.25973 0.02102  -0.04004 -0.03014 183 PHE A N   
1706 C  CA  . PHE A 183 ? 0.16598 0.23982 0.24713 0.03462  -0.06250 -0.03711 183 PHE A CA  
1707 C  C   . PHE A 183 ? 0.24846 0.24045 0.23159 0.05584  -0.00725 -0.02460 183 PHE A C   
1708 O  O   . PHE A 183 ? 0.20009 0.26891 0.20856 0.04200  -0.03048 -0.00814 183 PHE A O   
1709 C  CB  . PHE A 183 ? 0.18601 0.25663 0.28666 0.07574  -0.03326 -0.03763 183 PHE A CB  
1710 C  CG  . PHE A 183 ? 0.20130 0.28223 0.30369 0.04904  -0.04820 -0.02869 183 PHE A CG  
1711 C  CD1 . PHE A 183 ? 0.18826 0.32031 0.45769 0.06241  -0.06798 -0.02476 183 PHE A CD1 
1712 C  CD2 . PHE A 183 ? 0.29024 0.29135 0.23237 0.11240  -0.03537 -0.04228 183 PHE A CD2 
1713 C  CE1 . PHE A 183 ? 0.29886 0.31540 0.38826 0.04507  -0.13983 -0.04120 183 PHE A CE1 
1714 C  CE2 . PHE A 183 ? 0.27880 0.33207 0.28829 0.08464  -0.02044 -0.05264 183 PHE A CE2 
1715 C  CZ  . PHE A 183 ? 0.26689 0.33372 0.32465 0.02266  -0.07040 -0.08069 183 PHE A CZ  
1716 N  N   . ALA A 184 ? 0.13788 0.23613 0.25202 0.01158  -0.01602 -0.01832 184 ALA A N   
1717 C  CA  . ALA A 184 ? 0.20966 0.21010 0.21048 0.01510  0.00390  -0.01673 184 ALA A CA  
1718 C  C   . ALA A 184 ? 0.22913 0.21115 0.21907 0.02017  -0.03744 -0.00913 184 ALA A C   
1719 O  O   . ALA A 184 ? 0.18299 0.23405 0.20204 0.00284  -0.02967 -0.00961 184 ALA A O   
1720 C  CB  . ALA A 184 ? 0.17510 0.20689 0.19809 0.01754  -0.02874 -0.00606 184 ALA A CB  
1721 N  N   . PHE A 185 ? 0.24541 0.20843 0.21867 0.03921  -0.01042 -0.02093 185 PHE A N   
1722 C  CA  . PHE A 185 ? 0.20940 0.20605 0.19658 0.00667  -0.03372 0.00367  185 PHE A CA  
1723 C  C   . PHE A 185 ? 0.27483 0.23524 0.24328 0.01407  -0.02478 -0.01347 185 PHE A C   
1724 O  O   . PHE A 185 ? 0.37024 0.25165 0.20301 0.00271  -0.02143 -0.03693 185 PHE A O   
1725 C  CB  . PHE A 185 ? 0.20632 0.21883 0.22468 0.02016  -0.01625 0.00171  185 PHE A CB  
1726 C  CG  . PHE A 185 ? 0.23212 0.23538 0.25211 0.01045  -0.01273 -0.02250 185 PHE A CG  
1727 C  CD1 . PHE A 185 ? 0.29290 0.21878 0.29829 0.01295  -0.03672 0.00198  185 PHE A CD1 
1728 C  CD2 . PHE A 185 ? 0.22072 0.20711 0.31993 -0.01253 0.05075  0.00491  185 PHE A CD2 
1729 C  CE1 . PHE A 185 ? 0.32264 0.22095 0.31621 -0.00343 -0.07515 -0.02580 185 PHE A CE1 
1730 C  CE2 . PHE A 185 ? 0.35528 0.19670 0.33763 0.01674  0.06862  -0.05345 185 PHE A CE2 
1731 C  CZ  . PHE A 185 ? 0.34109 0.19544 0.31843 0.01669  0.01226  -0.05368 185 PHE A CZ  
1732 N  N   A MET A 186 ? 0.20793 0.23576 0.26457 -0.00285 -0.06637 0.00336  186 MET A N   
1733 N  N   B MET A 186 ? 0.28302 0.25572 0.28493 0.02760  -0.02927 -0.01029 186 MET A N   
1734 C  CA  A MET A 186 ? 0.19731 0.31719 0.27602 -0.06841 -0.08940 0.04922  186 MET A CA  
1735 C  CA  B MET A 186 ? 0.33955 0.33149 0.30646 -0.01353 -0.03225 -0.00374 186 MET A CA  
1736 C  C   A MET A 186 ? 0.23516 0.28076 0.25712 -0.06099 -0.08687 0.01651  186 MET A C   
1737 C  C   B MET A 186 ? 0.29584 0.28273 0.28226 -0.02023 -0.06542 0.01753  186 MET A C   
1738 O  O   A MET A 186 ? 0.37080 0.32620 0.26135 -0.08613 -0.15009 -0.03854 186 MET A O   
1739 O  O   B MET A 186 ? 0.44060 0.30465 0.32352 -0.01572 -0.04936 0.02384  186 MET A O   
1740 C  CB  A MET A 186 ? 0.15059 0.35623 0.31658 -0.08232 -0.07299 0.03806  186 MET A CB  
1741 C  CB  B MET A 186 ? 0.38612 0.41945 0.26764 -0.01342 0.02420  -0.08106 186 MET A CB  
1742 C  CG  A MET A 186 ? 0.14197 0.43991 0.29661 -0.06022 -0.01983 0.03487  186 MET A CG  
1743 C  CG  B MET A 186 ? 0.44178 0.50239 0.43933 -0.00534 0.00656  -0.02082 186 MET A CG  
1744 S  SD  A MET A 186 ? 0.23982 0.50870 0.33508 -0.09369 -0.04684 0.04336  186 MET A SD  
1745 S  SD  B MET A 186 ? 0.42410 0.58777 0.50926 0.05861  -0.00328 0.00838  186 MET A SD  
1746 C  CE  A MET A 186 ? 0.17382 0.48435 0.46198 -0.08272 -0.09137 -0.00311 186 MET A CE  
1747 C  CE  B MET A 186 ? 0.43885 0.57463 0.50894 0.08615  -0.00550 0.01481  186 MET A CE  
1748 N  N   . PHE A 187 ? 0.21301 0.25267 0.24924 -0.04180 -0.04116 -0.01854 187 PHE A N   
1749 C  CA  . PHE A 187 ? 0.29702 0.23389 0.22967 -0.00893 -0.03283 -0.00832 187 PHE A CA  
1750 C  C   . PHE A 187 ? 0.27542 0.24548 0.21662 -0.03512 -0.03625 -0.02946 187 PHE A C   
1751 O  O   . PHE A 187 ? 0.23373 0.25460 0.22619 0.01112  -0.04139 -0.01551 187 PHE A O   
1752 C  CB  . PHE A 187 ? 0.27635 0.22332 0.21284 0.01947  -0.04162 -0.01240 187 PHE A CB  
1753 C  CG  . PHE A 187 ? 0.23344 0.26207 0.23359 0.03146  0.00199  0.00278  187 PHE A CG  
1754 C  CD1 . PHE A 187 ? 0.20247 0.26553 0.24413 0.04745  0.00938  -0.01795 187 PHE A CD1 
1755 C  CD2 . PHE A 187 ? 0.22525 0.29703 0.29162 -0.00237 -0.06567 -0.00538 187 PHE A CD2 
1756 C  CE1 . PHE A 187 ? 0.19612 0.29247 0.24953 0.02152  -0.02909 -0.03622 187 PHE A CE1 
1757 C  CE2 . PHE A 187 ? 0.27908 0.33703 0.28630 0.03740  -0.11297 0.01686  187 PHE A CE2 
1758 C  CZ  . PHE A 187 ? 0.27463 0.31125 0.26011 0.00551  -0.10941 -0.02192 187 PHE A CZ  
1759 N  N   . PRO A 188 ? 0.28801 0.29463 0.20808 -0.06147 -0.05236 -0.01465 188 PRO A N   
1760 C  CA  . PRO A 188 ? 0.18693 0.32226 0.26415 -0.04892 -0.03066 0.00046  188 PRO A CA  
1761 C  C   . PRO A 188 ? 0.25234 0.25404 0.19978 -0.03145 -0.04088 0.01299  188 PRO A C   
1762 O  O   . PRO A 188 ? 0.26513 0.26434 0.20250 -0.02235 -0.03110 -0.02511 188 PRO A O   
1763 C  CB  . PRO A 188 ? 0.30535 0.39203 0.27956 -0.04800 -0.09534 0.01459  188 PRO A CB  
1764 C  CG  . PRO A 188 ? 0.37088 0.39597 0.26199 -0.02971 0.00297  0.07542  188 PRO A CG  
1765 C  CD  . PRO A 188 ? 0.31947 0.35573 0.22274 -0.02344 -0.06418 0.03548  188 PRO A CD  
1766 N  N   . PHE A 189 ? 0.25440 0.24347 0.22567 0.00537  0.00411  0.00495  189 PHE A N   
1767 C  CA  . PHE A 189 ? 0.22598 0.24825 0.22849 -0.00117 0.02597  -0.01525 189 PHE A CA  
1768 C  C   . PHE A 189 ? 0.22821 0.19807 0.23447 0.02550  -0.01485 -0.00778 189 PHE A C   
1769 O  O   . PHE A 189 ? 0.29399 0.24242 0.18133 0.02804  -0.02606 -0.01558 189 PHE A O   
1770 C  CB  . PHE A 189 ? 0.25543 0.28850 0.18860 0.02056  0.00910  -0.02098 189 PHE A CB  
1771 C  CG  . PHE A 189 ? 0.25260 0.25597 0.21904 0.00667  -0.01614 -0.01933 189 PHE A CG  
1772 C  CD1 . PHE A 189 ? 0.27572 0.28333 0.24032 0.04163  0.07866  -0.00404 189 PHE A CD1 
1773 C  CD2 . PHE A 189 ? 0.27692 0.27841 0.22428 -0.03471 0.02693  -0.04432 189 PHE A CD2 
1774 C  CE1 . PHE A 189 ? 0.24491 0.28057 0.32308 -0.00780 0.06108  -0.00418 189 PHE A CE1 
1775 C  CE2 . PHE A 189 ? 0.26915 0.29765 0.23819 -0.01664 -0.03089 -0.02543 189 PHE A CE2 
1776 C  CZ  . PHE A 189 ? 0.20785 0.27695 0.30175 -0.02337 0.00776  -0.00687 189 PHE A CZ  
1777 N  N   . SER A 190 ? 0.25384 0.19300 0.22435 0.02678  0.00061  -0.00147 190 SER A N   
1778 C  CA  . SER A 190 ? 0.25056 0.20099 0.20970 -0.01641 -0.00190 0.00302  190 SER A CA  
1779 C  C   . SER A 190 ? 0.29476 0.21006 0.19889 0.01062  0.03456  -0.01506 190 SER A C   
1780 O  O   . SER A 190 ? 0.26610 0.22762 0.19789 -0.01285 -0.00567 -0.01699 190 SER A O   
1781 C  CB  . SER A 190 ? 0.41494 0.22882 0.20984 -0.01697 -0.02558 0.00961  190 SER A CB  
1782 O  OG  . SER A 190 ? 0.41040 0.27295 0.23660 -0.02611 -0.02239 -0.01788 190 SER A OG  
1783 N  N   . ILE A 191 ? 0.23820 0.22496 0.21420 -0.00015 0.02430  0.01975  191 ILE A N   
1784 C  CA  . ILE A 191 ? 0.17423 0.25134 0.20655 0.03748  -0.00293 0.02041  191 ILE A CA  
1785 C  C   . ILE A 191 ? 0.25016 0.21143 0.21056 -0.00258 -0.00989 0.00451  191 ILE A C   
1786 O  O   . ILE A 191 ? 0.21467 0.20953 0.19737 0.02551  -0.02868 -0.00995 191 ILE A O   
1787 C  CB  . ILE A 191 ? 0.24355 0.28667 0.21208 0.03690  -0.01052 0.02892  191 ILE A CB  
1788 C  CG1 . ILE A 191 ? 0.31631 0.34126 0.25526 0.05865  -0.09088 0.00979  191 ILE A CG1 
1789 C  CG2 . ILE A 191 ? 0.23426 0.24038 0.28442 -0.00833 -0.04467 -0.00945 191 ILE A CG2 
1790 C  CD1 . ILE A 191 ? 0.41725 0.36239 0.28243 0.03592  -0.08511 -0.02814 191 ILE A CD1 
1791 N  N   . LYS A 192 ? 0.19379 0.19922 0.20364 0.03791  -0.02470 -0.00045 192 LYS A N   
1792 C  CA  . LYS A 192 ? 0.19376 0.17812 0.23650 0.03092  -0.03807 -0.02188 192 LYS A CA  
1793 C  C   . LYS A 192 ? 0.11979 0.18972 0.21315 -0.01794 -0.00885 -0.00045 192 LYS A C   
1794 O  O   . LYS A 192 ? 0.19884 0.20294 0.18237 -0.00288 -0.01230 -0.02510 192 LYS A O   
1795 C  CB  . LYS A 192 ? 0.24198 0.19968 0.22276 0.03872  -0.03136 0.00074  192 LYS A CB  
1796 C  CG  . LYS A 192 ? 0.23574 0.16176 0.25964 0.00892  -0.02694 0.00540  192 LYS A CG  
1797 C  CD  . LYS A 192 ? 0.24877 0.19719 0.24740 0.02767  -0.00940 -0.00232 192 LYS A CD  
1798 C  CE  . LYS A 192 ? 0.29085 0.21493 0.27542 0.01871  -0.01506 -0.04439 192 LYS A CE  
1799 N  NZ  . LYS A 192 ? 0.39058 0.23787 0.36591 0.05289  -0.13047 -0.09156 192 LYS A NZ  
1800 N  N   . ASN A 193 ? 0.15011 0.18225 0.22050 -0.00990 -0.00803 -0.01414 193 ASN A N   
1801 C  CA  . ASN A 193 ? 0.17482 0.19797 0.22398 0.01331  -0.01440 -0.00050 193 ASN A CA  
1802 C  C   . ASN A 193 ? 0.17137 0.18635 0.22791 -0.01109 -0.00945 -0.01895 193 ASN A C   
1803 O  O   . ASN A 193 ? 0.18022 0.19963 0.20106 -0.01030 -0.00977 -0.00550 193 ASN A O   
1804 C  CB  . ASN A 193 ? 0.17691 0.21151 0.21204 0.02293  0.03040  -0.02276 193 ASN A CB  
1805 C  CG  . ASN A 193 ? 0.21142 0.21248 0.22182 0.00843  0.01475  -0.00098 193 ASN A CG  
1806 O  OD1 . ASN A 193 ? 0.27646 0.24407 0.20841 0.02136  -0.04356 -0.00453 193 ASN A OD1 
1807 N  ND2 . ASN A 193 ? 0.26912 0.22511 0.22762 0.00414  -0.01523 -0.02097 193 ASN A ND2 
1808 N  N   . GLN A 194 ? 0.20918 0.17298 0.23803 0.00620  -0.00863 -0.01328 194 GLN A N   
1809 C  CA  . GLN A 194 ? 0.17626 0.16955 0.20105 -0.00918 -0.00901 0.01214  194 GLN A CA  
1810 C  C   . GLN A 194 ? 0.24580 0.16866 0.18638 0.01757  -0.00110 -0.00198 194 GLN A C   
1811 O  O   . GLN A 194 ? 0.24183 0.19022 0.19853 0.00195  -0.02373 -0.03373 194 GLN A O   
1812 C  CB  . GLN A 194 ? 0.26476 0.20006 0.18524 -0.00260 -0.01127 0.03069  194 GLN A CB  
1813 C  CG  . GLN A 194 ? 0.23703 0.20617 0.22472 0.01748  -0.03556 0.02048  194 GLN A CG  
1814 C  CD  . GLN A 194 ? 0.32825 0.22956 0.24609 0.00641  0.00709  0.01945  194 GLN A CD  
1815 O  OE1 . GLN A 194 ? 0.33466 0.27461 0.29354 0.06644  0.01653  0.04353  194 GLN A OE1 
1816 N  NE2 . GLN A 194 ? 0.35772 0.24223 0.25564 0.04072  -0.03744 0.03543  194 GLN A NE2 
1817 N  N   A MET A 195 ? 0.26897 0.17395 0.16634 0.00560  -0.01972 0.00293  195 MET A N   
1818 N  N   B MET A 195 ? 0.23689 0.17763 0.24212 0.01808  -0.04287 0.00859  195 MET A N   
1819 C  CA  A MET A 195 ? 0.16956 0.18117 0.19718 0.01227  -0.00752 0.00886  195 MET A CA  
1820 C  CA  B MET A 195 ? 0.18876 0.19263 0.23685 0.01793  -0.03352 0.01473  195 MET A CA  
1821 C  C   A MET A 195 ? 0.15072 0.17673 0.19414 0.03350  -0.06165 -0.03688 195 MET A C   
1822 C  C   B MET A 195 ? 0.19663 0.17862 0.23032 0.03384  -0.01921 -0.00396 195 MET A C   
1823 O  O   A MET A 195 ? 0.14673 0.18131 0.20406 0.01535  -0.03625 -0.03642 195 MET A O   
1824 O  O   B MET A 195 ? 0.15132 0.19915 0.18100 -0.01871 0.00077  0.01072  195 MET A O   
1825 C  CB  A MET A 195 ? 0.16434 0.20274 0.18966 0.01373  -0.01191 -0.00059 195 MET A CB  
1826 C  CB  B MET A 195 ? 0.26224 0.22519 0.22207 0.00562  -0.05389 -0.01419 195 MET A CB  
1827 C  CG  A MET A 195 ? 0.15012 0.19707 0.14369 0.03410  -0.04665 -0.00588 195 MET A CG  
1828 C  CG  B MET A 195 ? 0.29232 0.25573 0.18597 0.00533  -0.01337 -0.01768 195 MET A CG  
1829 S  SD  A MET A 195 ? 0.16262 0.23040 0.15127 0.00761  -0.02056 -0.02451 195 MET A SD  
1830 S  SD  B MET A 195 ? 0.27224 0.28465 0.21648 0.08109  -0.10408 -0.03022 195 MET A SD  
1831 C  CE  A MET A 195 ? 0.12048 0.25322 0.16943 0.07096  -0.02843 0.03694  195 MET A CE  
1832 C  CE  B MET A 195 ? 0.32616 0.29034 0.22376 0.04212  -0.00962 0.01502  195 MET A CE  
1833 N  N   . TYR A 196 ? 0.17450 0.17243 0.18576 0.00727  -0.00579 0.00508  196 TYR A N   
1834 C  CA  . TYR A 196 ? 0.17453 0.19082 0.20168 0.02416  -0.02667 0.00078  196 TYR A CA  
1835 C  C   . TYR A 196 ? 0.17994 0.16790 0.21998 0.00506  -0.04088 -0.00828 196 TYR A C   
1836 O  O   . TYR A 196 ? 0.17817 0.18129 0.19154 0.00496  -0.02638 0.00126  196 TYR A O   
1837 C  CB  . TYR A 196 ? 0.18377 0.16864 0.21772 -0.00504 -0.01241 -0.01158 196 TYR A CB  
1838 C  CG  . TYR A 196 ? 0.18750 0.19139 0.19029 0.00290  -0.00487 0.00533  196 TYR A CG  
1839 C  CD1 . TYR A 196 ? 0.21047 0.19895 0.24083 -0.02925 -0.03705 0.00300  196 TYR A CD1 
1840 C  CD2 . TYR A 196 ? 0.21650 0.18752 0.20563 -0.02004 -0.02175 0.00026  196 TYR A CD2 
1841 C  CE1 . TYR A 196 ? 0.15367 0.19553 0.22269 0.02875  -0.00720 0.00304  196 TYR A CE1 
1842 C  CE2 . TYR A 196 ? 0.18441 0.20309 0.22964 -0.02129 -0.05056 0.01479  196 TYR A CE2 
1843 C  CZ  . TYR A 196 ? 0.16317 0.19350 0.23233 -0.00784 -0.03009 0.01493  196 TYR A CZ  
1844 O  OH  . TYR A 196 ? 0.24611 0.18202 0.22841 -0.01754 -0.05520 0.00594  196 TYR A OH  
1845 N  N   . ASN A 197 ? 0.18622 0.16979 0.22084 -0.02157 0.01000  0.01326  197 ASN A N   
1846 C  CA  . ASN A 197 ? 0.19800 0.18266 0.21915 -0.01483 0.01971  -0.01215 197 ASN A CA  
1847 C  C   . ASN A 197 ? 0.14852 0.20949 0.17967 0.01950  -0.00042 0.01127  197 ASN A C   
1848 O  O   . ASN A 197 ? 0.23066 0.22089 0.18746 0.00350  -0.02810 -0.00914 197 ASN A O   
1849 C  CB  . ASN A 197 ? 0.16842 0.19337 0.23848 -0.03326 0.02581  -0.00794 197 ASN A CB  
1850 C  CG  . ASN A 197 ? 0.21312 0.19422 0.22189 -0.00282 0.00200  0.01482  197 ASN A CG  
1851 O  OD1 . ASN A 197 ? 0.14002 0.20602 0.23207 -0.00888 -0.01090 0.00704  197 ASN A OD1 
1852 N  ND2 . ASN A 197 ? 0.22445 0.22284 0.21471 -0.02754 0.00584  0.00419  197 ASN A ND2 
1853 N  N   A ILE A 198 ? 0.12485 0.16942 0.22774 -0.00496 0.01354  0.00930  198 ILE A N   
1854 N  N   B ILE A 198 ? 0.16161 0.17861 0.20049 0.02703  -0.00244 -0.01750 198 ILE A N   
1855 C  CA  A ILE A 198 ? 0.15848 0.17606 0.20681 0.00558  -0.01310 0.01139  198 ILE A CA  
1856 C  CA  B ILE A 198 ? 0.22395 0.17870 0.22233 0.04679  0.01109  0.00347  198 ILE A CA  
1857 C  C   A ILE A 198 ? 0.17425 0.18282 0.23223 -0.01718 -0.03755 -0.01983 198 ILE A C   
1858 C  C   B ILE A 198 ? 0.23000 0.17458 0.19934 -0.00495 -0.01121 -0.03432 198 ILE A C   
1859 O  O   A ILE A 198 ? 0.17505 0.16938 0.23135 0.00713  -0.04163 0.02668  198 ILE A O   
1860 O  O   B ILE A 198 ? 0.16326 0.16708 0.18280 0.02964  -0.03290 -0.04849 198 ILE A O   
1861 C  CB  A ILE A 198 ? 0.14109 0.19903 0.16742 0.01937  0.00869  0.01224  198 ILE A CB  
1862 C  CB  B ILE A 198 ? 0.30491 0.19669 0.20985 0.08714  -0.01312 -0.02283 198 ILE A CB  
1863 C  CG1 A ILE A 198 ? 0.07560 0.20197 0.18928 -0.03054 -0.02754 -0.00296 198 ILE A CG1 
1864 C  CG1 B ILE A 198 ? 0.29539 0.25811 0.18774 0.07579  0.01182  -0.07106 198 ILE A CG1 
1865 C  CG2 A ILE A 198 ? 0.20578 0.22547 0.18451 0.01296  0.09273  0.05879  198 ILE A CG2 
1866 C  CG2 B ILE A 198 ? 0.30033 0.21164 0.18115 0.08936  -0.00173 -0.02583 198 ILE A CG2 
1867 C  CD1 A ILE A 198 ? 0.13871 0.19011 0.18222 -0.00370 0.00475  0.01071  198 ILE A CD1 
1868 C  CD1 B ILE A 198 ? 0.37164 0.27500 0.33745 0.05906  0.05356  -0.03826 198 ILE A CD1 
1869 N  N   . LEU A 199 ? 0.16912 0.17583 0.20042 0.00318  0.01470  0.00675  199 LEU A N   
1870 C  CA  . LEU A 199 ? 0.17001 0.17983 0.20452 -0.01796 0.00582  0.00110  199 LEU A CA  
1871 C  C   . LEU A 199 ? 0.14927 0.21000 0.16574 0.00391  -0.01371 -0.00746 199 LEU A C   
1872 O  O   . LEU A 199 ? 0.18015 0.19305 0.18234 -0.00002 -0.00056 -0.00340 199 LEU A O   
1873 C  CB  . LEU A 199 ? 0.15763 0.20274 0.19394 0.01193  -0.01282 -0.00329 199 LEU A CB  
1874 C  CG  . LEU A 199 ? 0.13429 0.20665 0.21758 -0.01198 -0.02452 0.01327  199 LEU A CG  
1875 C  CD1 . LEU A 199 ? 0.19602 0.22314 0.23608 -0.04758 -0.05241 -0.03843 199 LEU A CD1 
1876 C  CD2 . LEU A 199 ? 0.13222 0.25515 0.20999 -0.01713 -0.00309 -0.00640 199 LEU A CD2 
1877 N  N   . ASP A 200 ? 0.12958 0.20225 0.21986 -0.00523 -0.00410 -0.00533 200 ASP A N   
1878 C  CA  . ASP A 200 ? 0.13787 0.22315 0.20457 -0.02840 -0.00677 0.01429  200 ASP A CA  
1879 C  C   . ASP A 200 ? 0.16315 0.19115 0.19163 -0.02447 0.00514  -0.02180 200 ASP A C   
1880 O  O   . ASP A 200 ? 0.18618 0.21755 0.17884 -0.01085 -0.01926 -0.01588 200 ASP A O   
1881 C  CB  . ASP A 200 ? 0.13479 0.21862 0.19362 -0.01617 -0.01847 0.00461  200 ASP A CB  
1882 C  CG  . ASP A 200 ? 0.11243 0.20190 0.21869 0.01440  0.00769  0.03649  200 ASP A CG  
1883 O  OD1 . ASP A 200 ? 0.17263 0.22671 0.20258 -0.01229 0.00839  -0.00067 200 ASP A OD1 
1884 O  OD2 . ASP A 200 ? 0.11535 0.25129 0.24828 0.01616  -0.00613 -0.01511 200 ASP A OD2 
1885 N  N   . ILE A 201 ? 0.14334 0.17813 0.23365 -0.02809 -0.00303 -0.01252 201 ILE A N   
1886 C  CA  . ILE A 201 ? 0.18331 0.19297 0.20398 0.00198  0.02312  -0.01068 201 ILE A CA  
1887 C  C   . ILE A 201 ? 0.15413 0.19173 0.22038 -0.00348 0.03476  -0.00099 201 ILE A C   
1888 O  O   . ILE A 201 ? 0.21484 0.22850 0.19243 -0.01503 0.00028  -0.00946 201 ILE A O   
1889 C  CB  . ILE A 201 ? 0.21808 0.18254 0.21391 -0.00645 0.00703  -0.01949 201 ILE A CB  
1890 C  CG1 . ILE A 201 ? 0.22863 0.22281 0.19925 0.00044  -0.00044 0.03300  201 ILE A CG1 
1891 C  CG2 . ILE A 201 ? 0.33712 0.20427 0.22579 0.00621  -0.03557 -0.03444 201 ILE A CG2 
1892 C  CD1 . ILE A 201 ? 0.23816 0.24209 0.21659 -0.01923 -0.00074 0.02797  201 ILE A CD1 
1893 N  N   . VAL A 202 ? 0.17267 0.19080 0.21109 -0.00964 0.00513  -0.02189 202 VAL A N   
1894 C  CA  . VAL A 202 ? 0.17348 0.18631 0.22514 -0.02147 0.00769  -0.03082 202 VAL A CA  
1895 C  C   . VAL A 202 ? 0.19193 0.16488 0.22326 -0.00124 0.03731  0.00266  202 VAL A C   
1896 O  O   . VAL A 202 ? 0.25014 0.21106 0.20959 0.01312  0.06701  -0.00901 202 VAL A O   
1897 C  CB  . VAL A 202 ? 0.15595 0.20918 0.27594 -0.01490 0.03385  -0.00947 202 VAL A CB  
1898 C  CG1 . VAL A 202 ? 0.20163 0.23085 0.31661 -0.00874 0.03355  0.00877  202 VAL A CG1 
1899 C  CG2 . VAL A 202 ? 0.18410 0.21061 0.31810 -0.02316 -0.03973 0.02324  202 VAL A CG2 
1900 N  N   . SER A 203 ? 0.14518 0.17139 0.23590 -0.01386 0.01167  -0.01952 203 SER A N   
1901 C  CA  . SER A 203 ? 0.15560 0.18283 0.23466 -0.02559 -0.02349 0.00314  203 SER A CA  
1902 C  C   . SER A 203 ? 0.18522 0.18305 0.23150 0.00480  -0.01945 -0.00193 203 SER A C   
1903 O  O   . SER A 203 ? 0.18499 0.18642 0.22290 -0.00182 -0.00856 -0.00515 203 SER A O   
1904 C  CB  . SER A 203 ? 0.19998 0.16427 0.20820 0.00421  0.02117  -0.02228 203 SER A CB  
1905 O  OG  . SER A 203 ? 0.13075 0.20386 0.21247 -0.00267 0.01606  -0.00214 203 SER A OG  
1906 N  N   A LYS A 204 ? 0.17238 0.18776 0.23403 -0.01216 -0.02795 -0.04516 204 LYS A N   
1907 N  N   B LYS A 204 ? 0.15337 0.18056 0.24812 -0.00160 -0.04050 -0.00968 204 LYS A N   
1908 C  CA  A LYS A 204 ? 0.18163 0.20008 0.19332 -0.01728 0.00494  -0.04449 204 LYS A CA  
1909 C  CA  B LYS A 204 ? 0.13424 0.16545 0.21226 0.01649  -0.01249 -0.03929 204 LYS A CA  
1910 C  C   A LYS A 204 ? 0.20520 0.18513 0.17821 0.02365  0.01270  0.01283  204 LYS A C   
1911 C  C   B LYS A 204 ? 0.08660 0.18880 0.20064 0.01500  -0.05806 -0.03489 204 LYS A C   
1912 O  O   A LYS A 204 ? 0.12439 0.18883 0.16366 0.00681  -0.00087 -0.02362 204 LYS A O   
1913 O  O   B LYS A 204 ? 0.10083 0.20213 0.25127 0.06540  0.01036  -0.01014 204 LYS A O   
1914 C  CB  A LYS A 204 ? 0.22254 0.18898 0.18859 -0.00366 -0.03396 -0.03506 204 LYS A CB  
1915 C  CB  B LYS A 204 ? 0.13184 0.18086 0.22790 -0.00778 0.05760  -0.01115 204 LYS A CB  
1916 C  CG  A LYS A 204 ? 0.17086 0.18615 0.22829 -0.00221 0.05433  -0.01698 204 LYS A CG  
1917 C  CG  B LYS A 204 ? 0.11194 0.17718 0.20390 0.02149  -0.02748 0.04724  204 LYS A CG  
1918 C  CD  A LYS A 204 ? 0.22993 0.20876 0.21325 0.03323  0.04059  -0.03038 204 LYS A CD  
1919 C  CD  B LYS A 204 ? 0.14990 0.17585 0.26851 -0.07218 0.04146  0.04262  204 LYS A CD  
1920 C  CE  A LYS A 204 ? 0.20091 0.22626 0.19016 -0.05399 -0.01516 0.00615  204 LYS A CE  
1921 C  CE  B LYS A 204 ? 0.25814 0.17574 0.36171 -0.04396 -0.03258 0.06859  204 LYS A CE  
1922 N  NZ  A LYS A 204 ? 0.13177 0.21336 0.22626 -0.03145 -0.01304 -0.01152 204 LYS A NZ  
1923 N  NZ  B LYS A 204 ? 0.32514 0.17045 0.44896 0.04854  -0.02174 0.06999  204 LYS A NZ  
1924 N  N   A ASN A 205 ? 0.21880 0.20240 0.17326 0.01690  0.01471  0.01164  205 ASN A N   
1925 N  N   B ASN A 205 ? 0.09004 0.20798 0.20881 -0.03862 -0.04744 -0.02805 205 ASN A N   
1926 C  CA  A ASN A 205 ? 0.20512 0.20287 0.20775 -0.02899 0.01258  -0.00835 205 ASN A CA  
1927 C  CA  B ASN A 205 ? 0.14782 0.22279 0.17746 -0.05303 -0.02421 -0.01169 205 ASN A CA  
1928 C  C   A ASN A 205 ? 0.19833 0.22818 0.20515 0.01101  -0.00672 0.00332  205 ASN A C   
1929 C  C   B ASN A 205 ? 0.21749 0.21517 0.15847 -0.03083 -0.02328 0.00989  205 ASN A C   
1930 O  O   A ASN A 205 ? 0.20605 0.20959 0.15235 -0.01305 -0.00897 0.01752  205 ASN A O   
1931 O  O   B ASN A 205 ? 0.26570 0.19164 0.19548 -0.06215 -0.03470 0.02361  205 ASN A O   
1932 C  CB  A ASN A 205 ? 0.22304 0.17133 0.23222 -0.02638 0.05079  0.01780  205 ASN A CB  
1933 C  CB  B ASN A 205 ? 0.15845 0.22116 0.13585 -0.02909 -0.03765 -0.03752 205 ASN A CB  
1934 C  CG  A ASN A 205 ? 0.23445 0.18232 0.24206 -0.01539 0.00935  -0.00620 205 ASN A CG  
1935 C  CG  B ASN A 205 ? 0.11204 0.27791 0.18731 0.02267  -0.01199 0.01351  205 ASN A CG  
1936 O  OD1 A ASN A 205 ? 0.20467 0.19418 0.21085 0.00621  0.02563  0.00214  205 ASN A OD1 
1937 O  OD1 B ASN A 205 ? 0.15984 0.26345 0.23148 -0.00414 -0.01183 -0.01030 205 ASN A OD1 
1938 N  ND2 A ASN A 205 ? 0.19241 0.17386 0.28532 -0.08568 -0.01162 -0.01889 205 ASN A ND2 
1939 N  ND2 B ASN A 205 ? 0.10727 0.29825 0.22317 0.03208  0.03529  0.07738  205 ASN A ND2 
1940 N  N   . ILE A 206 ? 0.18581 0.22037 0.22107 0.02573  0.00077  -0.02966 206 ILE A N   
1941 C  CA  . ILE A 206 ? 0.20144 0.19843 0.23971 -0.02488 -0.02359 -0.01074 206 ILE A CA  
1942 C  C   . ILE A 206 ? 0.24330 0.21091 0.21165 -0.00965 -0.04148 -0.00677 206 ILE A C   
1943 O  O   . ILE A 206 ? 0.22115 0.25055 0.20276 0.01792  -0.04488 -0.02128 206 ILE A O   
1944 C  CB  . ILE A 206 ? 0.15810 0.23457 0.27063 0.00146  -0.03416 -0.00896 206 ILE A CB  
1945 C  CG1 . ILE A 206 ? 0.26769 0.24886 0.23241 0.04592  -0.03651 0.00217  206 ILE A CG1 
1946 C  CG2 . ILE A 206 ? 0.18372 0.28018 0.28473 0.04785  0.02902  -0.04885 206 ILE A CG2 
1947 C  CD1 . ILE A 206 ? 0.40644 0.34017 0.29265 0.02256  -0.09007 -0.05014 206 ILE A CD1 
1948 N  N   A TYR A 207 ? 0.20544 0.20458 0.26474 -0.00582 0.00735  0.03729  207 TYR A N   
1949 N  N   B TYR A 207 ? 0.21326 0.19465 0.26100 -0.00351 -0.03108 0.01059  207 TYR A N   
1950 C  CA  A TYR A 207 ? 0.20927 0.19574 0.26351 -0.04406 0.00604  0.01319  207 TYR A CA  
1951 C  CA  B TYR A 207 ? 0.22655 0.19483 0.26655 -0.02270 -0.07389 -0.01145 207 TYR A CA  
1952 C  C   A TYR A 207 ? 0.17538 0.17442 0.24477 -0.03379 0.01911  0.01661  207 TYR A C   
1953 C  C   B TYR A 207 ? 0.22343 0.15880 0.25591 -0.03415 -0.03158 0.00293  207 TYR A C   
1954 O  O   A TYR A 207 ? 0.15046 0.19157 0.20485 -0.02047 0.00963  -0.01016 207 TYR A O   
1955 O  O   B TYR A 207 ? 0.28112 0.12957 0.24293 0.02772  -0.01452 0.01769  207 TYR A O   
1956 C  CB  A TYR A 207 ? 0.25880 0.19539 0.28581 -0.04473 0.00100  0.02416  207 TYR A CB  
1957 C  CB  B TYR A 207 ? 0.22977 0.20628 0.30354 0.01180  -0.11158 -0.01664 207 TYR A CB  
1958 C  CG  A TYR A 207 ? 0.27561 0.23247 0.30559 -0.06623 -0.12048 0.03054  207 TYR A CG  
1959 C  CG  B TYR A 207 ? 0.26479 0.21720 0.31566 -0.06578 -0.08659 -0.02644 207 TYR A CG  
1960 C  CD1 A TYR A 207 ? 0.33686 0.29950 0.32387 -0.06050 -0.01415 0.08077  207 TYR A CD1 
1961 C  CD1 B TYR A 207 ? 0.27068 0.22976 0.31321 -0.05741 -0.13571 -0.01266 207 TYR A CD1 
1962 C  CD2 A TYR A 207 ? 0.21471 0.27250 0.27307 0.00893  0.02795  0.01475  207 TYR A CD2 
1963 C  CD2 B TYR A 207 ? 0.30750 0.25595 0.29802 -0.09521 -0.01815 -0.00206 207 TYR A CD2 
1964 C  CE1 A TYR A 207 ? 0.28333 0.30802 0.39238 -0.04033 -0.02355 0.08963  207 TYR A CE1 
1965 C  CE1 B TYR A 207 ? 0.26745 0.25155 0.32246 -0.06593 -0.16170 0.01656  207 TYR A CE1 
1966 C  CE2 A TYR A 207 ? 0.24191 0.28141 0.30881 -0.01749 -0.04883 0.09262  207 TYR A CE2 
1967 C  CE2 B TYR A 207 ? 0.34073 0.25252 0.24414 -0.04296 -0.13669 0.00662  207 TYR A CE2 
1968 C  CZ  A TYR A 207 ? 0.31232 0.29634 0.28791 -0.01248 0.01574  0.10209  207 TYR A CZ  
1969 C  CZ  B TYR A 207 ? 0.31386 0.25636 0.23270 -0.02049 -0.13071 0.01705  207 TYR A CZ  
1970 O  OH  A TYR A 207 ? 0.27928 0.31480 0.30230 0.06422  0.05830  0.01610  207 TYR A OH  
1971 O  OH  B TYR A 207 ? 0.33759 0.28868 0.30417 0.08174  -0.09769 0.04864  207 TYR A OH  
1972 N  N   A SER A 208 ? 0.18593 0.18025 0.17970 -0.03310 0.00847  -0.02400 208 SER A N   
1973 N  N   B SER A 208 ? 0.21638 0.21164 0.25156 -0.05624 -0.05191 0.00579  208 SER A N   
1974 C  CA  A SER A 208 ? 0.16379 0.18945 0.18828 0.01215  0.02516  -0.02254 208 SER A CA  
1975 C  CA  B SER A 208 ? 0.24404 0.26216 0.25563 -0.02868 -0.05769 -0.01193 208 SER A CA  
1976 C  C   A SER A 208 ? 0.15187 0.18310 0.22290 -0.04111 0.04407  -0.01472 208 SER A C   
1977 C  C   B SER A 208 ? 0.23444 0.23158 0.24800 -0.01118 -0.04937 -0.01283 208 SER A C   
1978 O  O   A SER A 208 ? 0.14183 0.20946 0.16958 -0.04090 0.03429  -0.01808 208 SER A O   
1979 O  O   B SER A 208 ? 0.23019 0.26414 0.26054 0.02205  -0.10033 -0.02194 208 SER A O   
1980 C  CB  A SER A 208 ? 0.10252 0.21402 0.20786 -0.01515 0.00631  0.00101  208 SER A CB  
1981 C  CB  B SER A 208 ? 0.23345 0.34786 0.31866 -0.07860 -0.05431 -0.00679 208 SER A CB  
1982 O  OG  A SER A 208 ? 0.13682 0.16761 0.19608 0.01391  -0.01455 -0.03203 208 SER A OG  
1983 O  OG  B SER A 208 ? 0.28862 0.40198 0.42800 -0.08727 0.02572  -0.03022 208 SER A OG  
1984 N  N   . ILE A 209 ? 0.19223 0.19680 0.24952 -0.02191 0.00236  0.00049  209 ILE A N   
1985 C  CA  . ILE A 209 ? 0.21459 0.19269 0.24289 -0.01408 -0.00576 0.02500  209 ILE A CA  
1986 C  C   . ILE A 209 ? 0.17795 0.19657 0.24284 -0.03186 -0.03122 0.02595  209 ILE A C   
1987 O  O   . ILE A 209 ? 0.24237 0.21134 0.19632 0.00412  -0.03212 -0.01705 209 ILE A O   
1988 C  CB  . ILE A 209 ? 0.29134 0.18991 0.21863 -0.00270 0.00647  0.02713  209 ILE A CB  
1989 C  CG1 . ILE A 209 ? 0.31449 0.20581 0.23849 -0.02085 -0.01276 0.01354  209 ILE A CG1 
1990 C  CG2 . ILE A 209 ? 0.30585 0.18799 0.25514 0.00459  0.00028  0.00064  209 ILE A CG2 
1991 C  CD1 . ILE A 209 ? 0.42913 0.22922 0.31455 0.00386  -0.02941 0.03805  209 ILE A CD1 
1992 N  N   . PHE A 210 ? 0.19294 0.19673 0.22205 -0.00454 0.00604  0.01993  210 PHE A N   
1993 C  CA  . PHE A 210 ? 0.20067 0.20431 0.18980 -0.01035 -0.01802 0.02052  210 PHE A CA  
1994 C  C   . PHE A 210 ? 0.16161 0.21803 0.22322 0.03624  -0.00261 0.01797  210 PHE A C   
1995 O  O   . PHE A 210 ? 0.18328 0.23126 0.19639 -0.00675 -0.00208 -0.00586 210 PHE A O   
1996 C  CB  . PHE A 210 ? 0.17233 0.22629 0.23540 -0.01745 -0.01379 -0.00277 210 PHE A CB  
1997 C  CG  . PHE A 210 ? 0.13078 0.23815 0.25437 0.00039  -0.03447 0.02339  210 PHE A CG  
1998 C  CD1 . PHE A 210 ? 0.10013 0.29996 0.28307 -0.01070 -0.01542 0.03140  210 PHE A CD1 
1999 C  CD2 . PHE A 210 ? 0.18099 0.23630 0.27379 -0.01992 -0.01941 0.03222  210 PHE A CD2 
2000 C  CE1 . PHE A 210 ? 0.16600 0.27829 0.32571 0.04846  0.00249  0.00838  210 PHE A CE1 
2001 C  CE2 . PHE A 210 ? 0.19530 0.24180 0.30519 0.01074  0.00082  0.00861  210 PHE A CE2 
2002 C  CZ  . PHE A 210 ? 0.14422 0.26094 0.31950 0.01836  0.01786  0.00343  210 PHE A CZ  
2003 N  N   . ILE A 211 ? 0.13890 0.21636 0.21083 0.00249  -0.01596 0.01052  211 ILE A N   
2004 C  CA  . ILE A 211 ? 0.19576 0.18626 0.22315 -0.01017 -0.02371 0.02486  211 ILE A CA  
2005 C  C   . ILE A 211 ? 0.17624 0.20694 0.24424 -0.02962 0.01147  -0.00943 211 ILE A C   
2006 O  O   . ILE A 211 ? 0.17480 0.22629 0.19947 0.00763  -0.02699 -0.00511 211 ILE A O   
2007 C  CB  . ILE A 211 ? 0.19092 0.18937 0.21786 0.00726  -0.02164 0.00647  211 ILE A CB  
2008 C  CG1 . ILE A 211 ? 0.21597 0.20350 0.23793 -0.05128 0.01193  0.02146  211 ILE A CG1 
2009 C  CG2 . ILE A 211 ? 0.19432 0.21968 0.23441 -0.01793 -0.02073 -0.00270 211 ILE A CG2 
2010 C  CD1 . ILE A 211 ? 0.22901 0.22752 0.26969 -0.03824 0.00449  0.01844  211 ILE A CD1 
2011 N  N   . PHE A 212 ? 0.16351 0.20460 0.25922 -0.01329 -0.01642 0.00074  212 PHE A N   
2012 C  CA  . PHE A 212 ? 0.18370 0.21404 0.22449 -0.00159 -0.01863 -0.00228 212 PHE A CA  
2013 C  C   . PHE A 212 ? 0.19601 0.21977 0.23707 -0.00599 -0.03991 -0.00347 212 PHE A C   
2014 O  O   . PHE A 212 ? 0.19244 0.24192 0.21180 -0.02209 -0.04018 -0.00486 212 PHE A O   
2015 C  CB  . PHE A 212 ? 0.20970 0.21155 0.25045 -0.03333 -0.00979 -0.01540 212 PHE A CB  
2016 C  CG  . PHE A 212 ? 0.18251 0.21682 0.23317 0.00855  -0.00218 -0.02202 212 PHE A CG  
2017 C  CD1 . PHE A 212 ? 0.21405 0.26221 0.22241 -0.01520 -0.00673 -0.02450 212 PHE A CD1 
2018 C  CD2 . PHE A 212 ? 0.26769 0.20375 0.28484 -0.00794 0.03864  -0.01390 212 PHE A CD2 
2019 C  CE1 . PHE A 212 ? 0.27397 0.26826 0.22633 -0.03821 -0.02912 -0.02890 212 PHE A CE1 
2020 C  CE2 . PHE A 212 ? 0.35851 0.24293 0.31682 -0.04669 0.03705  -0.03968 212 PHE A CE2 
2021 C  CZ  . PHE A 212 ? 0.32920 0.24945 0.33514 -0.03903 0.00908  -0.01940 212 PHE A CZ  
2022 N  N   . ILE A 213 ? 0.16596 0.20688 0.21904 -0.00533 0.00943  -0.00195 213 ILE A N   
2023 C  CA  . ILE A 213 ? 0.18980 0.23628 0.21315 0.01919  -0.01841 -0.00830 213 ILE A CA  
2024 C  C   . ILE A 213 ? 0.22944 0.23454 0.18770 0.02525  0.00695  -0.00328 213 ILE A C   
2025 O  O   . ILE A 213 ? 0.22354 0.23350 0.18949 0.01551  0.00429  -0.00904 213 ILE A O   
2026 C  CB  . ILE A 213 ? 0.19834 0.23821 0.21865 0.02466  -0.04252 0.02180  213 ILE A CB  
2027 C  CG1 . ILE A 213 ? 0.30473 0.23454 0.20900 0.02150  -0.05062 0.03622  213 ILE A CG1 
2028 C  CG2 . ILE A 213 ? 0.25757 0.24681 0.29391 0.06589  -0.01839 -0.03453 213 ILE A CG2 
2029 C  CD1 . ILE A 213 ? 0.29228 0.28003 0.23709 0.02403  -0.00481 0.03745  213 ILE A CD1 
2030 N  N   . VAL A 214 ? 0.23831 0.19796 0.19790 -0.00372 -0.00222 0.01325  214 VAL A N   
2031 C  CA  . VAL A 214 ? 0.20093 0.21003 0.20840 -0.02122 -0.01522 0.01824  214 VAL A CA  
2032 C  C   . VAL A 214 ? 0.24664 0.23983 0.19505 -0.00523 -0.03050 0.01098  214 VAL A C   
2033 O  O   . VAL A 214 ? 0.23705 0.24767 0.18548 0.00307  -0.00989 -0.00021 214 VAL A O   
2034 C  CB  . VAL A 214 ? 0.17858 0.21230 0.27953 -0.05098 -0.01952 0.00749  214 VAL A CB  
2035 C  CG1 . VAL A 214 ? 0.19582 0.25012 0.24534 -0.01073 -0.02199 0.04705  214 VAL A CG1 
2036 C  CG2 . VAL A 214 ? 0.16852 0.27166 0.26301 -0.02873 -0.01135 0.00261  214 VAL A CG2 
2037 N  N   . ILE A 215 ? 0.17203 0.24017 0.21675 -0.02266 -0.02406 -0.00162 215 ILE A N   
2038 C  CA  . ILE A 215 ? 0.20518 0.24308 0.22277 -0.01314 -0.02522 -0.00739 215 ILE A CA  
2039 C  C   . ILE A 215 ? 0.19780 0.21952 0.22116 0.00743  -0.03338 0.00274  215 ILE A C   
2040 O  O   . ILE A 215 ? 0.23230 0.25459 0.20733 -0.00429 -0.03847 -0.02075 215 ILE A O   
2041 C  CB  . ILE A 215 ? 0.16976 0.24124 0.25231 -0.02298 -0.02726 0.00573  215 ILE A CB  
2042 C  CG1 . ILE A 215 ? 0.16276 0.20819 0.26925 -0.04766 -0.05246 0.01702  215 ILE A CG1 
2043 C  CG2 . ILE A 215 ? 0.17593 0.25373 0.26639 -0.01993 -0.04620 -0.02865 215 ILE A CG2 
2044 C  CD1 . ILE A 215 ? 0.16447 0.23401 0.27118 -0.01069 0.02843  0.00052  215 ILE A CD1 
2045 N  N   . LEU A 216 ? 0.20980 0.20514 0.22429 -0.00466 -0.01825 -0.00734 216 LEU A N   
2046 C  CA  . LEU A 216 ? 0.25744 0.23437 0.23803 -0.00938 0.00175  -0.00803 216 LEU A CA  
2047 C  C   . LEU A 216 ? 0.28753 0.25760 0.20500 -0.01006 -0.02082 -0.01353 216 LEU A C   
2048 O  O   . LEU A 216 ? 0.31672 0.26189 0.23123 0.00941  -0.04493 -0.04365 216 LEU A O   
2049 C  CB  . LEU A 216 ? 0.33918 0.23191 0.29727 -0.02066 -0.05994 -0.01105 216 LEU A CB  
2050 C  CG  . LEU A 216 ? 0.31621 0.28441 0.38796 -0.08310 -0.11266 0.04516  216 LEU A CG  
2051 C  CD1 . LEU A 216 ? 0.34858 0.30751 0.57266 -0.14312 -0.15670 0.05994  216 LEU A CD1 
2052 C  CD2 . LEU A 216 ? 0.40919 0.28149 0.39102 -0.00100 0.02394  0.10141  216 LEU A CD2 
2053 N  N   . ASN A 217 ? 0.25169 0.23793 0.24263 0.01557  -0.01957 -0.01170 217 ASN A N   
2054 C  CA  . ASN A 217 ? 0.27275 0.27689 0.28127 -0.01542 -0.02063 -0.01736 217 ASN A CA  
2055 C  C   . ASN A 217 ? 0.31546 0.31524 0.27407 0.02331  0.01995  -0.03718 217 ASN A C   
2056 O  O   . ASN A 217 ? 0.33081 0.31464 0.26068 0.02702  0.02239  -0.01922 217 ASN A O   
2057 C  CB  . ASN A 217 ? 0.21025 0.39230 0.23008 0.02280  -0.02164 -0.03834 217 ASN A CB  
2058 C  CG  . ASN A 217 ? 0.33790 0.44024 0.32199 0.02363  0.01922  -0.03423 217 ASN A CG  
2059 O  OD1 . ASN A 217 ? 0.40732 0.46773 0.45079 -0.04263 0.06466  -0.06231 217 ASN A OD1 
2060 N  ND2 . ASN A 217 ? 0.46443 0.46584 0.37557 0.09567  0.02379  -0.02283 217 ASN A ND2 
2061 N  N   . GLN A 218 ? 0.21073 0.36494 0.21224 -0.00990 -0.00898 0.01402  218 GLN A N   
2062 C  CA  . GLN A 218 ? 0.28071 0.44041 0.20849 0.05871  0.00001  -0.01626 218 GLN A CA  
2063 C  C   . GLN A 218 ? 0.33065 0.49415 0.18012 0.14202  -0.02091 -0.05718 218 GLN A C   
2064 O  O   . GLN A 218 ? 0.38672 0.48556 0.19572 0.02553  0.00950  -0.00997 218 GLN A O   
2065 C  CB  . GLN A 218 ? 0.42996 0.43703 0.20837 0.01479  0.02173  0.02927  218 GLN A CB  
2066 C  CG  . GLN A 218 ? 0.40002 0.44478 0.22536 -0.00241 -0.00249 0.04166  218 GLN A CG  
2067 C  CD  . GLN A 218 ? 0.43577 0.50519 0.27176 -0.07838 -0.02047 0.07856  218 GLN A CD  
2068 O  OE1 . GLN A 218 ? 0.53826 0.53490 0.39328 -0.11162 0.07769  0.06928  218 GLN A OE1 
2069 N  NE2 . GLN A 218 ? 0.53027 0.55601 0.37856 -0.06949 -0.00243 0.07901  218 GLN A NE2 
2070 N  N   . SER A 219 ? 0.28195 0.58099 0.19861 0.11726  0.00538  -0.04729 219 SER A N   
2071 C  CA  . SER A 219 ? 0.23781 0.67779 0.25219 0.04945  -0.04270 -0.04416 219 SER A CA  
2072 C  C   . SER A 219 ? 0.40755 0.75272 0.34773 -0.00653 -0.11560 -0.17873 219 SER A C   
2073 O  O   . SER A 219 ? 0.36508 0.76664 0.39031 -0.04215 -0.13404 -0.15762 219 SER A O   
2074 C  CB  . SER A 219 ? 0.24602 0.71243 0.25478 -0.00617 0.02051  -0.11363 219 SER A CB  
2075 O  OG  . SER A 219 ? 0.35966 0.73221 0.33257 -0.01651 0.03079  -0.02118 219 SER A OG  
2076 N  N   A TYR A 220 ? 0.46795 0.79254 0.40119 -0.00705 -0.17519 -0.18091 220 TYR A N   
2077 N  N   B TYR A 220 ? 0.47214 0.79723 0.39554 -0.00702 -0.17254 -0.18042 220 TYR A N   
2078 C  CA  A TYR A 220 ? 0.60882 0.84671 0.52749 0.00385  -0.13306 -0.13394 220 TYR A CA  
2079 C  CA  B TYR A 220 ? 0.62222 0.84870 0.52015 0.00325  -0.12495 -0.12758 220 TYR A CA  
2080 C  C   A TYR A 220 ? 0.65581 0.86897 0.56185 0.00306  -0.09023 -0.10223 220 TYR A C   
2081 C  C   B TYR A 220 ? 0.66586 0.87208 0.55957 -0.00056 -0.08729 -0.09707 220 TYR A C   
2082 O  O   A TYR A 220 ? 0.64285 0.87270 0.52681 0.00546  -0.04768 -0.06949 220 TYR A O   
2083 O  O   B TYR A 220 ? 0.66123 0.87747 0.52706 -0.00443 -0.04792 -0.06105 220 TYR A O   
2084 C  CB  A TYR A 220 ? 0.69991 0.88393 0.62412 0.01540  -0.09183 -0.10700 220 TYR A CB  
2085 C  CB  B TYR A 220 ? 0.72316 0.89248 0.61240 0.01621  -0.07982 -0.09655 220 TYR A CB  
2086 C  CG  A TYR A 220 ? 0.75037 0.92213 0.73972 0.00816  -0.06216 -0.06094 220 TYR A CG  
2087 C  CG  B TYR A 220 ? 0.79654 0.93465 0.73061 0.01110  -0.04056 -0.04949 220 TYR A CG  
2088 C  CD1 A TYR A 220 ? 0.76056 0.93482 0.78821 0.00663  -0.03294 -0.04898 220 TYR A CD1 
2089 C  CD1 B TYR A 220 ? 0.83261 0.94860 0.76976 0.01085  -0.02010 -0.04047 220 TYR A CD1 
2090 C  CD2 A TYR A 220 ? 0.78364 0.93404 0.77405 -0.00230 -0.05660 -0.04709 220 TYR A CD2 
2091 C  CD2 B TYR A 220 ? 0.83491 0.94934 0.77612 0.01039  -0.02852 -0.03244 220 TYR A CD2 
2092 C  CE1 A TYR A 220 ? 0.78855 0.94466 0.82266 -0.00043 -0.01418 -0.03913 220 TYR A CE1 
2093 C  CE1 B TYR A 220 ? 0.85561 0.96165 0.80807 0.01079  -0.00283 -0.02823 220 TYR A CE1 
2094 C  CE2 A TYR A 220 ? 0.81732 0.94462 0.81137 -0.00197 -0.03573 -0.03829 220 TYR A CE2 
2095 C  CE2 B TYR A 220 ? 0.85232 0.95958 0.80376 0.01039  -0.00464 -0.02230 220 TYR A CE2 
2096 C  CZ  A TYR A 220 ? 0.82476 0.95019 0.83729 -0.00463 -0.01241 -0.03348 220 TYR A CZ  
2097 C  CZ  B TYR A 220 ? 0.86524 0.96693 0.82545 0.01591  -0.00078 -0.02071 220 TYR A CZ  
2098 O  OH  A TYR A 220 ? 0.85414 0.95573 0.85825 -0.00435 0.00354  -0.02760 220 TYR A OH  
2099 O  OH  B TYR A 220 ? 0.87814 0.97143 0.85330 0.02536  -0.01123 -0.01842 220 TYR A OH  
2100 N  N   . LYS A 221 ? 0.66602 0.88648 0.58433 -0.01354 -0.09996 -0.09912 221 LYS A N   
2101 C  CA  . LYS A 221 ? 0.67300 0.91942 0.60371 -0.02115 -0.04438 -0.09138 221 LYS A CA  
2102 C  C   . LYS A 221 ? 0.62149 0.92662 0.59055 -0.03255 -0.02923 -0.09679 221 LYS A C   
2103 O  O   . LYS A 221 ? 0.55352 0.91917 0.59602 -0.03154 -0.09526 -0.14625 221 LYS A O   
2104 C  CB  . LYS A 221 ? 0.70643 0.94339 0.68000 -0.02861 0.00243  -0.07153 221 LYS A CB  
2105 C  CG  . LYS A 221 ? 0.78922 0.96762 0.76480 -0.02257 0.00743  -0.06462 221 LYS A CG  
2106 C  CD  . LYS A 221 ? 0.85740 0.99493 0.83160 -0.00900 0.01925  -0.05414 221 LYS A CD  
2107 C  CE  . LYS A 221 ? 0.89759 1.01170 0.86899 0.00504  0.00152  -0.05567 221 LYS A CE  
2108 N  NZ  . LYS A 221 ? 0.91049 1.01706 0.87967 0.00540  -0.02182 -0.06590 221 LYS A NZ  
2109 N  N   . LEU A 222 ? 0.60031 0.93087 0.56980 -0.03748 -0.04628 -0.08020 222 LEU A N   
2110 C  CA  . LEU A 222 ? 0.64948 0.94516 0.65286 -0.03414 -0.05772 -0.04010 222 LEU A CA  
2111 C  C   . LEU A 222 ? 0.72347 0.95370 0.74572 -0.02451 -0.08376 -0.02281 222 LEU A C   
2112 O  O   . LEU A 222 ? 0.69884 0.95121 0.75655 -0.03411 -0.12242 -0.02988 222 LEU A O   
2113 C  CB  . LEU A 222 ? 0.61953 0.95509 0.64341 -0.04177 -0.04931 -0.02329 222 LEU A CB  
2114 C  CG  . LEU A 222 ? 0.58953 0.95936 0.62845 -0.05174 -0.01310 -0.01745 222 LEU A CG  
2115 C  CD1 . LEU A 222 ? 0.48900 0.95360 0.61514 -0.06505 0.04826  -0.02635 222 LEU A CD1 
2116 C  CD2 . LEU A 222 ? 0.60415 0.96503 0.63726 -0.02371 -0.00506 -0.01501 222 LEU A CD2 
2117 N  N   . LEU A 223 ? 0.77921 0.96185 0.77502 -0.02589 -0.09099 0.00138  223 LEU A N   
2118 C  CA  . LEU A 223 ? 0.84178 0.97359 0.81002 -0.02458 -0.08887 0.02085  223 LEU A CA  
2119 C  C   . LEU A 223 ? 0.91265 0.99006 0.87428 -0.04147 -0.06893 0.02865  223 LEU A C   
2120 O  O   . LEU A 223 ? 0.95560 1.00131 0.90300 -0.05755 -0.05850 0.03783  223 LEU A O   
2121 C  CB  . LEU A 223 ? 0.82002 0.95583 0.76858 -0.02060 -0.10630 0.03524  223 LEU A CB  
2122 C  CG  . LEU A 223 ? 0.80863 0.93458 0.75154 -0.02077 -0.11302 0.05297  223 LEU A CG  
2123 C  CD1 . LEU A 223 ? 0.79740 0.92748 0.76060 -0.00565 -0.11469 0.06144  223 LEU A CD1 
2124 C  CD2 . LEU A 223 ? 0.81308 0.92802 0.71624 -0.03018 -0.08439 0.06448  223 LEU A CD2 
2125 N  N   . LEU A 224 ? 0.95204 0.99121 0.90176 -0.02895 -0.03421 0.01942  224 LEU A N   
2126 C  CA  . LEU A 224 ? 0.98836 0.98983 0.92516 -0.02318 0.00123  0.00662  224 LEU A CA  
2127 C  C   . LEU A 224 ? 1.02447 0.99109 0.96092 -0.02131 0.02174  -0.00336 224 LEU A C   
2128 O  O   . LEU A 224 ? 1.04255 0.98898 0.99498 -0.02546 0.04922  -0.00629 224 LEU A O   
2129 C  CB  . LEU A 224 ? 0.97937 0.99032 0.93164 -0.02872 0.01712  0.00401  224 LEU A CB  
2130 NA NA  A NA  B .   ? 0.33964 0.30539 0.30453 0.07343  0.03383  0.00697  301 NA  A NA  
2131 C  C1  A RET C .   ? 0.22089 0.17332 0.24168 0.03312  0.05674  -0.01532 302 RET A C1  
2132 C  C1  B RET C .   ? 0.21138 0.13812 0.18873 0.00603  -0.03071 -0.06203 302 RET A C1  
2133 C  C2  A RET C .   ? 0.31505 0.20958 0.23571 -0.05137 -0.03453 -0.04431 302 RET A C2  
2134 C  C2  B RET C .   ? 0.14617 0.13053 0.23645 -0.04360 -0.05058 -0.04724 302 RET A C2  
2135 C  C3  A RET C .   ? 0.38400 0.25917 0.29862 -0.05698 -0.03280 -0.04805 302 RET A C3  
2136 C  C3  B RET C .   ? 0.13063 0.14108 0.19534 -0.02715 -0.01043 -0.01034 302 RET A C3  
2137 C  C4  A RET C .   ? 0.27106 0.26764 0.29180 -0.03248 -0.01420 -0.05844 302 RET A C4  
2138 C  C4  B RET C .   ? 0.14876 0.12444 0.23815 -0.06615 -0.04153 -0.00053 302 RET A C4  
2139 C  C5  A RET C .   ? 0.18381 0.25452 0.28522 0.02515  -0.03600 -0.06243 302 RET A C5  
2140 C  C5  B RET C .   ? 0.11620 0.15922 0.23416 -0.03957 0.04293  0.02047  302 RET A C5  
2141 C  C6  A RET C .   ? 0.10413 0.18198 0.25730 0.01638  -0.05363 -0.03353 302 RET A C6  
2142 C  C6  B RET C .   ? 0.19474 0.13913 0.23218 -0.01680 -0.01888 -0.01133 302 RET A C6  
2143 C  C7  A RET C .   ? 0.17916 0.15961 0.20733 0.02207  -0.07406 -0.02419 302 RET A C7  
2144 C  C7  B RET C .   ? 0.18237 0.15648 0.21314 -0.02452 -0.02278 -0.02558 302 RET A C7  
2145 C  C8  A RET C .   ? 0.22645 0.18485 0.16609 0.02783  -0.05101 0.00472  302 RET A C8  
2146 C  C8  B RET C .   ? 0.18202 0.16990 0.12904 -0.03229 -0.06683 -0.03673 302 RET A C8  
2147 C  C9  A RET C .   ? 0.18436 0.19575 0.19367 0.04352  -0.00552 0.02382  302 RET A C9  
2148 C  C9  B RET C .   ? 0.17440 0.19929 0.17698 0.02023  0.00477  -0.06343 302 RET A C9  
2149 C  C10 A RET C .   ? 0.22467 0.18235 0.18061 0.02627  0.04937  -0.00768 302 RET A C10 
2150 C  C10 B RET C .   ? 0.22383 0.19398 0.22190 0.07519  -0.07010 -0.10140 302 RET A C10 
2151 C  C11 A RET C .   ? 0.12353 0.15904 0.17488 0.01532  -0.00182 -0.00122 302 RET A C11 
2152 C  C11 B RET C .   ? 0.19357 0.21221 0.24295 0.08980  -0.08362 -0.05772 302 RET A C11 
2153 C  C12 A RET C .   ? 0.18583 0.16918 0.19063 -0.03807 -0.03087 -0.01799 302 RET A C12 
2154 C  C12 B RET C .   ? 0.25031 0.17926 0.29605 0.05775  -0.01033 -0.02907 302 RET A C12 
2155 C  C13 A RET C .   ? 0.15833 0.21760 0.19625 -0.02505 0.01684  -0.00158 302 RET A C13 
2156 C  C13 B RET C .   ? 0.21335 0.14420 0.24544 0.05834  -0.03135 0.03006  302 RET A C13 
2157 C  C14 A RET C .   ? 0.11232 0.17466 0.18984 0.00209  -0.02778 0.02407  302 RET A C14 
2158 C  C14 B RET C .   ? 0.21119 0.19404 0.32782 0.04618  -0.05945 0.00606  302 RET A C14 
2159 C  C15 A RET C .   ? 0.22604 0.17950 0.16903 0.01855  -0.07530 -0.00557 302 RET A C15 
2160 C  C15 B RET C .   ? 0.22420 0.16376 0.35877 0.05948  -0.09339 0.03329  302 RET A C15 
2161 C  C16 A RET C .   ? 0.24840 0.17392 0.28915 0.02450  0.06964  -0.00860 302 RET A C16 
2162 C  C16 B RET C .   ? 0.24299 0.15436 0.16622 0.05081  -0.10330 -0.05841 302 RET A C16 
2163 C  C17 A RET C .   ? 0.21134 0.14534 0.21348 -0.00674 0.06044  -0.00926 302 RET A C17 
2164 C  C17 B RET C .   ? 0.21169 0.12032 0.23693 0.01917  -0.03818 -0.08506 302 RET A C17 
2165 C  C18 A RET C .   ? 0.21976 0.29518 0.32451 0.08869  -0.00261 -0.05865 302 RET A C18 
2166 C  C18 B RET C .   ? 0.09540 0.20636 0.29282 -0.02310 0.04442  0.03500  302 RET A C18 
2167 C  C19 A RET C .   ? 0.15396 0.21723 0.21227 0.00309  0.03314  0.00340  302 RET A C19 
2168 C  C19 B RET C .   ? 0.25082 0.22678 0.19764 -0.02942 0.00941  -0.07579 302 RET A C19 
2169 C  C20 A RET C .   ? 0.15007 0.25523 0.19959 0.06028  -0.00894 0.02522  302 RET A C20 
2170 C  C20 B RET C .   ? 0.32947 0.11672 0.22899 0.03421  -0.02581 0.05885  302 RET A C20 
2171 C  C   A 97N D .   ? 0.42705 0.41157 0.58565 0.13410  0.09902  -0.08080 303 97N A C   
2172 O  O   A 97N D .   ? 0.34334 0.48241 0.41518 -0.13014 0.10065  0.01645  303 97N A O   
2173 C  C1  A 97N D .   ? 0.41319 0.42014 0.58124 0.11158  0.10948  -0.08023 303 97N A C1  
2174 O  O1  A 97N D .   ? 0.25426 0.45437 0.36837 -0.11679 -0.04860 -0.02637 303 97N A O1  
2175 C  C2  A 97N D .   ? 0.36788 0.41238 0.54385 0.08518  0.08573  -0.07209 303 97N A C2  
2176 O  O2  A 97N D .   ? 0.21874 0.37575 0.29468 -0.06450 -0.03792 0.02908  303 97N A O2  
2177 C  C3  A 97N D .   ? 0.36276 0.41840 0.51897 0.03792  0.05086  -0.09160 303 97N A C3  
2178 O  O3  A 97N D .   ? 0.32232 0.28303 0.34178 -0.10796 -0.03379 0.07310  303 97N A O3  
2179 C  C4  A 97N D .   ? 0.35876 0.41873 0.48840 -0.02660 0.02595  -0.10311 303 97N A C4  
2180 C  C5  A 97N D .   ? 0.27300 0.45338 0.50688 -0.02162 -0.09998 -0.06814 303 97N A C5  
2181 C  C6  A 97N D .   ? 0.38336 0.47520 0.50007 0.00798  -0.03698 -0.05137 303 97N A C6  
2182 C  C7  A 97N D .   ? 0.33301 0.50316 0.45670 0.07902  -0.11444 -0.04937 303 97N A C7  
2183 C  C8  A 97N D .   ? 0.23416 0.51011 0.49978 0.07939  -0.13719 -0.07807 303 97N A C8  
2184 C  C9  A 97N D .   ? 0.36976 0.53782 0.45491 0.08273  -0.03245 -0.07426 303 97N A C9  
2185 C  C10 A 97N D .   ? 0.45421 0.54535 0.51508 0.05185  -0.00814 -0.03639 303 97N A C10 
2186 C  C11 A 97N D .   ? 0.48436 0.52621 0.51867 0.00737  0.03464  -0.04836 303 97N A C11 
2187 C  C12 A 97N D .   ? 0.50234 0.53044 0.51729 -0.05578 0.03251  -0.04681 303 97N A C12 
2188 C  C13 A 97N D .   ? 0.40736 0.50683 0.45846 -0.10791 -0.09112 -0.04427 303 97N A C13 
2189 C  C14 A 97N D .   ? 0.37993 0.47429 0.34485 -0.18492 -0.06323 -0.02421 303 97N A C14 
2190 C  C15 A 97N D .   ? 0.33159 0.46736 0.41022 -0.13728 0.01313  -0.02714 303 97N A C15 
2191 C  C16 A 97N D .   ? 0.27980 0.42060 0.34016 -0.14704 -0.06379 0.00686  303 97N A C16 
2192 C  C17 A 97N D .   ? 0.27495 0.38712 0.28724 -0.12550 -0.03368 0.04572  303 97N A C17 
2193 C  C18 A 97N D .   ? 0.22080 0.29676 0.33708 -0.09007 -0.06612 0.10080  303 97N A C18 
2194 C  C10 . OLC E .   ? 0.36517 0.56183 0.51649 -0.19750 -0.03269 0.04410  304 OLC A C10 
2195 C  C9  . OLC E .   ? 0.38045 0.57566 0.50750 -0.16859 0.02523  0.04921  304 OLC A C9  
2196 C  C11 . OLC E .   ? 0.32026 0.54900 0.53539 -0.13296 -0.05972 0.09837  304 OLC A C11 
2197 C  C8  . OLC E .   ? 0.39001 0.56959 0.57644 -0.19283 0.12559  0.06139  304 OLC A C8  
2198 C  C12 . OLC E .   ? 0.32372 0.55246 0.53883 -0.11004 0.03491  0.09829  304 OLC A C12 
2199 C  C7  . OLC E .   ? 0.40009 0.58336 0.62379 -0.17772 0.18664  0.04456  304 OLC A C7  
2200 C  C13 . OLC E .   ? 0.37733 0.56917 0.58660 -0.15052 0.00825  0.06908  304 OLC A C13 
2201 C  C6  . OLC E .   ? 0.44254 0.57130 0.62878 -0.16300 0.10863  0.04424  304 OLC A C6  
2202 C  C14 . OLC E .   ? 0.30943 0.60869 0.59759 -0.15206 0.16647  0.07220  304 OLC A C14 
2203 C  C5  . OLC E .   ? 0.47549 0.57926 0.62901 -0.12896 -0.01605 0.03014  304 OLC A C5  
2204 C  C4  . OLC E .   ? 0.51958 0.59596 0.71542 -0.14320 -0.01531 0.05158  304 OLC A C4  
2205 C  C3  . OLC E .   ? 0.52919 0.61172 0.73850 -0.16269 -0.05579 0.06314  304 OLC A C3  
2206 C  C2  . OLC E .   ? 0.56240 0.62137 0.76871 -0.17932 -0.09146 0.07854  304 OLC A C2  
2207 C  C1  . OLC E .   ? 0.63190 0.63707 0.83399 -0.15551 -0.04482 0.11526  304 OLC A C1  
2208 O  O19 . OLC E .   ? 0.66327 0.66637 0.87354 -0.08314 -0.02038 0.11438  304 OLC A O19 
2209 O  O20 . OLC E .   ? 0.69527 0.63827 0.88716 -0.21657 0.00159  0.13321  304 OLC A O20 
2210 C  C1  . LFA F .   ? 0.47748 0.44836 0.63797 0.01034  -0.08491 -0.12112 305 LFA A C1  
2211 C  C2  . LFA F .   ? 0.49576 0.42787 0.62468 0.04524  0.00706  -0.06666 305 LFA A C2  
2212 C  C3  . LFA F .   ? 0.45156 0.43968 0.65002 0.06048  0.09948  -0.01933 305 LFA A C3  
2213 C  C4  . LFA F .   ? 0.44126 0.42828 0.68038 0.06929  0.06794  0.00931  305 LFA A C4  
2214 C  C5  . LFA F .   ? 0.41766 0.42268 0.68702 -0.00530 0.03251  -0.00687 305 LFA A C5  
2215 C  C6  . LFA F .   ? 0.42947 0.42589 0.68814 -0.04213 -0.00636 -0.02908 305 LFA A C6  
2216 C  C7  . LFA F .   ? 0.51118 0.43090 0.66467 -0.02093 0.05217  -0.03922 305 LFA A C7  
2217 C  C8  . LFA F .   ? 0.57450 0.43066 0.63341 -0.03601 0.07231  -0.07313 305 LFA A C8  
2218 C  C9  . LFA F .   ? 0.64214 0.43330 0.64524 -0.02682 0.07744  -0.10303 305 LFA A C9  
2219 C  C10 . LFA F .   ? 0.68778 0.49269 0.66242 -0.04169 0.06037  -0.11117 305 LFA A C10 
2220 C  C11 . LFA F .   ? 0.65554 0.52462 0.72704 -0.08924 0.09836  -0.07731 305 LFA A C11 
2221 C  C12 . LFA F .   ? 0.71667 0.55993 0.76319 -0.10248 0.14526  -0.03510 305 LFA A C12 
2222 C  C8  . LFA G .   ? 0.69923 0.64571 0.73305 -0.09471 0.11005  -0.03353 306 LFA A C8  
2223 C  C9  . LFA G .   ? 0.68917 0.65278 0.74344 -0.07147 0.09882  -0.04710 306 LFA A C9  
2224 C  C10 . LFA G .   ? 0.65873 0.64689 0.73958 -0.07382 0.06642  -0.03590 306 LFA A C10 
2225 C  C11 . LFA G .   ? 0.60601 0.63625 0.71674 -0.05280 0.06914  -0.02074 306 LFA A C11 
2226 C  C12 . LFA G .   ? 0.52909 0.63198 0.69765 -0.02274 -0.01331 -0.02444 306 LFA A C12 
2227 C  C13 . LFA G .   ? 0.55991 0.62965 0.64824 0.03202  -0.02484 -0.03657 306 LFA A C13 
2228 C  C14 . LFA G .   ? 0.62158 0.64141 0.69260 -0.00986 -0.02306 -0.02381 306 LFA A C14 
2229 C  C15 . LFA G .   ? 0.53379 0.64550 0.70025 -0.00904 -0.01967 -0.02819 306 LFA A C15 
2230 C  C16 . LFA G .   ? 0.43824 0.65200 0.72741 0.02311  0.00409  -0.01984 306 LFA A C16 
2231 C  C17 . LFA G .   ? 0.48492 0.64422 0.73411 0.05696  -0.01133 -0.03176 306 LFA A C17 
2232 C  C18 . LFA G .   ? 0.49946 0.64469 0.74063 0.05429  0.01343  -0.04473 306 LFA A C18 
2233 C  C19 . LFA G .   ? 0.52701 0.64246 0.73453 0.04901  0.06986  -0.04920 306 LFA A C19 
2234 C  C20 . LFA G .   ? 0.58322 0.64500 0.77375 0.01548  0.09933  -0.03397 306 LFA A C20 
2235 C  C1  . LFA H .   ? 0.29748 0.54246 0.50584 -0.04066 -0.01094 0.03630  307 LFA A C1  
2236 C  C2  . LFA H .   ? 0.37668 0.50898 0.31991 -0.05346 -0.10158 0.04916  307 LFA A C2  
2237 C  C3  . LFA H .   ? 0.44827 0.48371 0.43286 -0.08364 -0.10427 -0.03416 307 LFA A C3  
2238 C  C4  . LFA H .   ? 0.47374 0.44929 0.39998 -0.11719 -0.05223 -0.06168 307 LFA A C4  
2239 C  C5  . LFA H .   ? 0.52207 0.42340 0.44200 -0.11467 0.00766  -0.06821 307 LFA A C5  
2240 C  C6  . LFA H .   ? 0.68351 0.46322 0.50379 -0.03138 -0.01860 -0.03707 307 LFA A C6  
2241 C  C7  . LFA H .   ? 0.71240 0.46211 0.54457 -0.01146 -0.03524 -0.00888 307 LFA A C7  
2242 C  C8  . LFA H .   ? 0.67100 0.48699 0.58932 0.01626  0.01773  0.02697  307 LFA A C8  
2243 C  C9  . LFA H .   ? 0.62386 0.49860 0.64953 0.02058  0.02219  0.02081  307 LFA A C9  
2244 C  C10 . LFA H .   ? 0.64510 0.50281 0.70050 0.02187  -0.00667 0.00036  307 LFA A C10 
2245 C  C11 . LFA H .   ? 0.61368 0.51074 0.72356 0.03726  -0.04378 -0.04047 307 LFA A C11 
2246 C  C12 . LFA H .   ? 0.56767 0.49298 0.71529 0.00423  -0.07185 -0.08936 307 LFA A C12 
2247 C  C6  . LFA I .   ? 0.61015 0.56688 0.63248 -0.07078 -0.01873 0.02899  308 LFA A C6  
2248 C  C7  . LFA I .   ? 0.59215 0.56129 0.61996 -0.06947 0.02349  0.01064  308 LFA A C7  
2249 C  C8  . LFA I .   ? 0.49664 0.54168 0.57475 -0.04011 0.17868  0.01862  308 LFA A C8  
2250 C  C9  . LFA I .   ? 0.42900 0.50836 0.54264 -0.00673 0.10775  0.02721  308 LFA A C9  
2251 C  C10 . LFA I .   ? 0.33160 0.46179 0.53835 0.05638  0.11733  -0.00742 308 LFA A C10 
2252 C  C11 . LFA I .   ? 0.32086 0.44972 0.54766 0.04787  0.01830  -0.03547 308 LFA A C11 
2253 C  C12 . LFA I .   ? 0.34438 0.47571 0.54271 0.02682  -0.12064 -0.02958 308 LFA A C12 
2254 C  C13 . LFA I .   ? 0.49764 0.48900 0.46290 0.03028  -0.13771 -0.00246 308 LFA A C13 
2255 C  C14 . LFA I .   ? 0.58709 0.54504 0.54036 0.02491  -0.05949 -0.00358 308 LFA A C14 
2256 C  C15 . LFA I .   ? 0.64209 0.58196 0.56657 0.01451  0.02671  -0.02676 308 LFA A C15 
2257 C  C16 . LFA I .   ? 0.61479 0.61285 0.60246 -0.01062 0.06704  -0.05309 308 LFA A C16 
2258 C  C17 . LFA I .   ? 0.53068 0.62887 0.57675 -0.02669 0.06132  -0.06170 308 LFA A C17 
2259 C  C18 . LFA I .   ? 0.47368 0.63803 0.57627 -0.04657 0.10334  -0.05712 308 LFA A C18 
2260 C  C19 . LFA I .   ? 0.41389 0.63540 0.56895 -0.06639 0.14043  -0.05587 308 LFA A C19 
2261 C  C20 . LFA I .   ? 0.42706 0.63652 0.58878 -0.12630 0.10457  -0.05463 308 LFA A C20 
2262 C  C5  . LFA J .   ? 0.72260 0.64948 0.64567 0.04846  -0.05954 -0.03362 309 LFA A C5  
2263 C  C6  . LFA J .   ? 0.71529 0.64976 0.65493 0.04466  -0.02311 -0.04575 309 LFA A C6  
2264 C  C7  . LFA J .   ? 0.63199 0.64441 0.66036 0.07032  0.01489  -0.03603 309 LFA A C7  
2265 C  C8  . LFA J .   ? 0.66658 0.64930 0.65668 0.08643  0.02505  -0.02601 309 LFA A C8  
2266 C  C9  . LFA J .   ? 0.68515 0.66511 0.66300 0.08022  0.02705  -0.02206 309 LFA A C9  
2267 C  C10 . LFA J .   ? 0.69502 0.66261 0.69478 0.05681  0.02503  -0.05427 309 LFA A C10 
2268 C  C11 . LFA J .   ? 0.69560 0.66132 0.70633 0.04342  0.02424  -0.05601 309 LFA A C11 
2269 C  C12 . LFA J .   ? 0.69007 0.65093 0.66201 0.02256  -0.01238 -0.04738 309 LFA A C12 
2270 C  C13 . LFA J .   ? 0.67919 0.64211 0.63622 0.00539  -0.03454 -0.04911 309 LFA A C13 
2271 C  C14 . LFA J .   ? 0.59948 0.60482 0.61885 -0.00093 -0.03198 -0.04360 309 LFA A C14 
2272 C  C15 . LFA J .   ? 0.55625 0.58810 0.58871 0.00493  -0.05887 0.01263  309 LFA A C15 
2273 C  C16 . LFA J .   ? 0.45086 0.55241 0.56074 -0.03894 -0.12879 0.00935  309 LFA A C16 
2274 C  C17 . LFA J .   ? 0.52918 0.55525 0.60740 -0.05164 -0.11376 -0.02300 309 LFA A C17 
2275 C  C18 . LFA J .   ? 0.59691 0.53659 0.63963 -0.06289 -0.02753 -0.00887 309 LFA A C18 
2276 C  C19 . LFA J .   ? 0.66202 0.52867 0.65236 -0.09575 -0.01886 -0.00234 309 LFA A C19 
2277 C  C20 . LFA J .   ? 0.61941 0.52630 0.63987 -0.12304 -0.04235 0.00265  309 LFA A C20 
2278 C  C1  . LFA K .   ? 0.33396 0.66648 0.64099 0.00164  -0.08556 0.04463  310 LFA A C1  
2279 C  C2  . LFA K .   ? 0.27594 0.66281 0.65275 -0.02413 -0.13884 0.02123  310 LFA A C2  
2280 C  C3  . LFA K .   ? 0.45430 0.67414 0.62948 -0.01107 -0.08744 -0.00264 310 LFA A C3  
2281 C  C4  . LFA K .   ? 0.43146 0.66022 0.61529 -0.01257 -0.10936 -0.02484 310 LFA A C4  
2282 C  C5  . LFA K .   ? 0.43653 0.66652 0.57690 -0.01485 -0.20918 -0.05705 310 LFA A C5  
2283 C  C16 . LFA L .   ? 0.57820 0.48163 0.63204 0.01929  0.05492  0.03666  311 LFA A C16 
2284 C  C17 . LFA L .   ? 0.56052 0.47250 0.60085 -0.01656 0.07585  0.04619  311 LFA A C17 
2285 C  C18 . LFA L .   ? 0.55487 0.50110 0.58019 -0.05051 0.04618  0.02877  311 LFA A C18 
2286 C  C19 . LFA L .   ? 0.45730 0.46666 0.43465 -0.12331 0.04591  0.00489  311 LFA A C19 
2287 C  C20 . LFA L .   ? 0.47945 0.42412 0.36920 -0.16219 0.15723  -0.01922 311 LFA A C20 
2288 C  C15 . LFA M .   ? 0.39770 0.54255 0.54918 0.01028  0.08558  0.04912  312 LFA A C15 
2289 C  C16 . LFA M .   ? 0.37164 0.55314 0.55840 0.01924  0.13655  -0.00883 312 LFA A C16 
2290 C  C17 . LFA M .   ? 0.27565 0.55829 0.54190 0.01422  0.11087  -0.01196 312 LFA A C17 
2291 C  C18 . LFA M .   ? 0.37669 0.57665 0.55231 -0.00537 -0.03550 0.00724  312 LFA A C18 
2292 C  C19 . LFA M .   ? 0.35261 0.57953 0.53569 0.02758  -0.02748 0.02850  312 LFA A C19 
2293 C  C20 . LFA M .   ? 0.29470 0.59679 0.54528 0.02489  -0.01685 0.06925  312 LFA A C20 
2294 C  C1  . LFA N .   ? 0.53405 0.60624 0.71460 -0.01448 0.06776  0.10261  313 LFA A C1  
2295 C  C2  . LFA N .   ? 0.46433 0.60058 0.66500 -0.00466 0.03370  0.09483  313 LFA A C2  
2296 C  C3  . LFA N .   ? 0.47999 0.60672 0.66407 -0.03111 0.02730  0.10216  313 LFA A C3  
2297 C  C4  . LFA N .   ? 0.46403 0.61607 0.64399 -0.02850 -0.01091 0.11668  313 LFA A C4  
2298 C  C5  . LFA N .   ? 0.46325 0.63297 0.67652 0.02143  -0.05710 0.12839  313 LFA A C5  
2299 C  C6  . LFA N .   ? 0.59843 0.64037 0.71135 0.00888  -0.03795 0.10158  313 LFA A C6  
2300 C  C7  . LFA N .   ? 0.67325 0.61739 0.67303 -0.02479 0.05270  0.09664  313 LFA A C7  
2301 C  C8  . LFA N .   ? 0.63699 0.61441 0.65325 -0.03325 0.15949  0.05538  313 LFA A C8  
2302 C  C9  . LFA N .   ? 0.69771 0.61166 0.69952 -0.00454 0.08471  0.01017  313 LFA A C9  
2303 C  C10 . LFA N .   ? 0.67369 0.60491 0.69315 0.04244  0.05041  -0.02261 313 LFA A C10 
2304 C  C11 . LFA N .   ? 0.61901 0.58873 0.66248 0.07165  -0.01399 -0.01105 313 LFA A C11 
2305 C  C12 . LFA N .   ? 0.65889 0.57952 0.69062 0.09335  -0.02975 0.03394  313 LFA A C12 
2306 C  C13 . LFA N .   ? 0.64108 0.57893 0.68854 0.11181  0.02575  0.03257  313 LFA A C13 
2307 C  C14 . LFA N .   ? 0.61579 0.56734 0.67123 0.14252  0.00763  0.01531  313 LFA A C14 
2308 C  C15 . LFA N .   ? 0.64599 0.60470 0.64458 0.15906  -0.00312 0.01520  313 LFA A C15 
2309 C  C16 . LFA N .   ? 0.60137 0.60514 0.57464 0.18033  -0.12915 0.02806  313 LFA A C16 
2310 C  C17 . LFA N .   ? 0.56468 0.63641 0.63201 0.11098  -0.08813 0.01914  313 LFA A C17 
2311 C  C18 . LFA N .   ? 0.60303 0.64521 0.61588 0.09733  -0.08180 0.04704  313 LFA A C18 
2312 C  C19 . LFA N .   ? 0.58715 0.64180 0.61328 0.14574  -0.10717 0.13665  313 LFA A C19 
2313 C  C20 . LFA N .   ? 0.62404 0.64525 0.64885 0.14742  -0.06794 0.15438  313 LFA A C20 
2314 C  C16 . LFA O .   ? 0.62992 0.66984 0.72684 0.10961  0.11097  0.00662  314 LFA A C16 
2315 C  C17 . LFA O .   ? 0.68738 0.66529 0.73117 0.10313  0.05322  0.02238  314 LFA A C17 
2316 C  C18 . LFA O .   ? 0.71730 0.66130 0.74887 0.08727  0.07423  0.05820  314 LFA A C18 
2317 C  C19 . LFA O .   ? 0.67638 0.65312 0.77772 0.06376  0.10015  0.08054  314 LFA A C19 
2318 C  C20 . LFA O .   ? 0.63378 0.65474 0.78507 0.03919  0.12003  0.09937  314 LFA A C20 
2319 C  C1  . GOL P .   ? 0.53053 0.62792 0.73125 0.03815  0.06480  0.00502  315 GOL A C1  
2320 O  O1  . GOL P .   ? 0.55822 0.63718 0.74322 0.05007  0.03003  0.00875  315 GOL A O1  
2321 C  C2  . GOL P .   ? 0.51044 0.61918 0.73391 0.05105  0.07544  -0.00239 315 GOL A C2  
2322 O  O2  . GOL P .   ? 0.54829 0.63332 0.77281 0.04827  0.06126  0.00962  315 GOL A O2  
2323 C  C3  . GOL P .   ? 0.49616 0.59159 0.69864 0.11045  0.04349  -0.04118 315 GOL A C3  
2324 O  O3  . GOL P .   ? 0.47523 0.56870 0.65065 0.18777  0.10094  -0.08112 315 GOL A O3  
2325 C  C1  . GOL Q .   ? 0.76489 0.90890 0.86700 -0.01167 0.09947  -0.09654 316 GOL A C1  
2326 O  O1  . GOL Q .   ? 0.73844 0.92518 0.93232 0.00093  0.14393  -0.06885 316 GOL A O1  
2327 C  C2  . GOL Q .   ? 0.76383 0.88967 0.78712 -0.00161 0.08315  -0.13249 316 GOL A C2  
2328 O  O2  . GOL Q .   ? 0.68341 0.84869 0.64734 0.07714  0.18843  -0.20138 316 GOL A O2  
2329 C  C3  . GOL Q .   ? 0.76783 0.89946 0.79637 -0.04733 0.01192  -0.10021 316 GOL A C3  
2330 O  O3  . GOL Q .   ? 0.75930 0.90491 0.77767 -0.06449 0.00879  -0.09303 316 GOL A O3  
2331 C  C1  . GOL R .   ? 0.73172 0.80276 0.84940 -0.07338 0.03727  0.08352  317 GOL A C1  
2332 O  O1  . GOL R .   ? 0.74663 0.80162 0.84026 -0.08802 0.04642  0.09463  317 GOL A O1  
2333 C  C2  . GOL R .   ? 0.72867 0.80498 0.87551 -0.05022 0.02562  0.08956  317 GOL A C2  
2334 O  O2  . GOL R .   ? 0.75090 0.80113 0.88327 -0.02709 0.06143  0.08872  317 GOL A O2  
2335 C  C3  . GOL R .   ? 0.71215 0.81560 0.88281 -0.04366 0.01906  0.09477  317 GOL A C3  
2336 O  O3  . GOL R .   ? 0.65681 0.81816 0.86543 -0.04356 0.06406  0.09323  317 GOL A O3  
2337 C  C24 . OLC S .   ? 0.44563 0.45529 0.47321 0.01745  0.00236  -0.03832 318 OLC A C24 
2338 C  C4  . OLC S .   ? 0.41537 0.51800 0.46055 0.06211  -0.07219 0.07627  318 OLC A C4  
2339 C  C3  . OLC S .   ? 0.46200 0.49855 0.44203 0.05413  -0.04145 0.06826  318 OLC A C3  
2340 C  C2  . OLC S .   ? 0.51362 0.47875 0.45571 0.02581  0.03490  0.02766  318 OLC A C2  
2341 C  C21 . OLC S .   ? 0.61315 0.47606 0.47859 -0.01211 -0.01615 -0.00744 318 OLC A C21 
2342 C  C1  . OLC S .   ? 0.63843 0.46103 0.45545 0.04839  0.02888  0.01081  318 OLC A C1  
2343 C  C22 . OLC S .   ? 0.57435 0.47105 0.51792 -0.00425 0.01082  -0.03820 318 OLC A C22 
2344 O  O19 . OLC S .   ? 0.67148 0.42746 0.48972 0.11498  0.01243  -0.03830 318 OLC A O19 
2345 O  O25 . OLC S .   ? 0.30651 0.39770 0.36927 0.05072  0.07078  -0.06624 318 OLC A O25 
2346 O  O23 . OLC S .   ? 0.63662 0.49279 0.60194 -0.01287 0.03759  -0.06637 318 OLC A O23 
2347 O  O20 . OLC S .   ? 0.70878 0.47147 0.51285 0.01331  -0.01246 0.02672  318 OLC A O20 
2348 C  C10 . OLC T .   ? 0.55180 0.71337 0.57147 0.10432  0.05410  0.09590  319 OLC A C10 
2349 C  C9  . OLC T .   ? 0.51098 0.71988 0.55782 0.11568  -0.02294 0.08322  319 OLC A C9  
2350 C  C11 . OLC T .   ? 0.52271 0.70085 0.56368 0.03709  0.13992  0.13588  319 OLC A C11 
2351 C  C8  . OLC T .   ? 0.54580 0.73556 0.54993 0.11496  -0.02772 0.07106  319 OLC A C8  
2352 C  C24 . OLC T .   ? 0.78577 0.80189 0.87973 0.07554  -0.06962 0.05865  319 OLC A C24 
2353 C  C7  . OLC T .   ? 0.61737 0.75282 0.56802 0.10531  0.03098  0.04980  319 OLC A C7  
2354 C  C6  . OLC T .   ? 0.61799 0.76892 0.61059 0.09987  0.03480  0.04628  319 OLC A C6  
2355 C  C5  . OLC T .   ? 0.59829 0.78269 0.64796 0.07271  0.02726  0.04673  319 OLC A C5  
2356 C  C4  . OLC T .   ? 0.56027 0.78789 0.67589 0.05659  0.02830  0.03674  319 OLC A C4  
2357 C  C3  . OLC T .   ? 0.61538 0.79145 0.70434 0.03557  -0.00481 0.04500  319 OLC A C3  
2358 C  C2  . OLC T .   ? 0.70140 0.79387 0.75528 0.03046  0.00190  0.03746  319 OLC A C2  
2359 C  C21 . OLC T .   ? 0.82256 0.79694 0.83258 0.06740  -0.01033 0.02397  319 OLC A C21 
2360 C  C1  . OLC T .   ? 0.77128 0.78648 0.81107 0.04675  0.01041  0.04466  319 OLC A C1  
2361 C  C22 . OLC T .   ? 0.81023 0.79862 0.86578 0.08030  -0.03207 0.03278  319 OLC A C22 
2362 O  O19 . OLC T .   ? 0.77897 0.77657 0.83992 0.04254  0.01953  0.05224  319 OLC A O19 
2363 O  O25 . OLC T .   ? 0.79169 0.80901 0.89989 0.05504  -0.05969 0.08613  319 OLC A O25 
2364 O  O23 . OLC T .   ? 0.83734 0.79996 0.88963 0.06532  -0.03689 0.02094  319 OLC A O23 
2365 O  O20 . OLC T .   ? 0.83363 0.80041 0.82276 0.05756  -0.01595 0.03103  319 OLC A O20 
2366 C  C7  . OLC U .   ? 0.62485 0.66774 0.79029 0.01341  -0.01118 0.01322  320 OLC A C7  
2367 C  C6  . OLC U .   ? 0.60047 0.67569 0.79401 0.00194  0.03083  0.02050  320 OLC A C6  
2368 C  C5  . OLC U .   ? 0.61607 0.67223 0.79062 -0.00849 0.01867  0.01038  320 OLC A C5  
2369 C  C4  . OLC U .   ? 0.56227 0.68292 0.76545 -0.02505 -0.00836 -0.00879 320 OLC A C4  
2370 C  C3  . OLC U .   ? 0.58850 0.68787 0.77460 -0.02068 0.01238  -0.00696 320 OLC A C3  
2371 C  C2  . OLC U .   ? 0.66014 0.70255 0.78576 -0.03670 -0.02466 0.00073  320 OLC A C2  
2372 C  C1  . OLC U .   ? 0.74852 0.71535 0.84238 -0.06235 -0.05425 0.01977  320 OLC A C1  
2373 O  O19 . OLC U .   ? 0.80752 0.73345 0.88591 -0.05473 -0.04886 0.04451  320 OLC A O19 
2374 O  O20 . OLC U .   ? 0.76963 0.71614 0.87192 -0.06847 -0.10248 0.01010  320 OLC A O20 
2375 C  C10 . OLC V .   ? 0.69616 0.65708 0.68276 -0.00616 0.06250  0.00184  321 OLC A C10 
2376 C  C9  . OLC V .   ? 0.72728 0.66751 0.71365 -0.04395 0.10778  0.01515  321 OLC A C9  
2377 C  C11 . OLC V .   ? 0.72866 0.64660 0.66654 0.01652  0.01547  0.00169  321 OLC A C11 
2378 C  C8  . OLC V .   ? 0.71831 0.68534 0.70834 -0.07322 0.11259  0.00792  321 OLC A C8  
2379 C  C12 . OLC V .   ? 0.76188 0.64579 0.65851 0.03841  0.01278  0.00856  321 OLC A C12 
2380 C  C7  . OLC V .   ? 0.68300 0.68347 0.71899 -0.13094 0.06236  0.00063  321 OLC A C7  
2381 C  C6  . OLC V .   ? 0.61614 0.69109 0.72016 -0.15652 0.03570  -0.00779 321 OLC A C6  
2382 C  C5  . OLC V .   ? 0.64569 0.69876 0.73019 -0.15554 0.03976  -0.01709 321 OLC A C5  
2383 C  C4  . OLC V .   ? 0.66123 0.70414 0.74392 -0.14455 0.04419  -0.00628 321 OLC A C4  
2384 C  C3  . OLC V .   ? 0.68349 0.71837 0.79235 -0.14176 0.01286  -0.00048 321 OLC A C3  
2385 C  C2  . OLC V .   ? 0.68218 0.72639 0.83760 -0.12987 -0.02033 0.01228  321 OLC A C2  
2386 C  C21 . OLC V .   ? 0.71519 0.76839 0.85952 -0.06894 0.00511  0.01750  321 OLC A C21 
2387 C  C1  . OLC V .   ? 0.68858 0.73350 0.89113 -0.11978 0.01508  0.03329  321 OLC A C1  
2388 C  C22 . OLC V .   ? 0.72404 0.78705 0.83125 -0.06531 -0.01819 0.01996  321 OLC A C22 
2389 O  O19 . OLC V .   ? 0.72611 0.72160 0.92820 -0.13517 0.05450  0.07326  321 OLC A O19 
2390 O  O20 . OLC V .   ? 0.72883 0.76309 0.91020 -0.07382 0.01543  0.02286  321 OLC A O20 
2391 C  C10 . OLC W .   ? 0.58061 0.59184 0.53251 0.18795  -0.12888 0.05817  322 OLC A C10 
2392 C  C9  . OLC W .   ? 0.60570 0.62570 0.59727 0.18774  -0.07711 0.00949  322 OLC A C9  
2393 C  C11 . OLC W .   ? 0.58934 0.55970 0.53300 0.18103  -0.11411 0.07162  322 OLC A C11 
2394 C  C8  . OLC W .   ? 0.64813 0.65229 0.62142 0.14398  -0.09714 -0.01354 322 OLC A C8  
2395 C  C12 . OLC W .   ? 0.58119 0.52368 0.48663 0.18031  -0.01641 0.07345  322 OLC A C12 
2396 C  C7  . OLC W .   ? 0.71510 0.67337 0.67809 0.09768  -0.02358 -0.02920 322 OLC A C7  
2397 C  C13 . OLC W .   ? 0.49990 0.46973 0.43750 0.22301  -0.00291 0.01547  322 OLC A C13 
2398 C  C6  . OLC W .   ? 0.73773 0.69311 0.69349 0.06174  -0.03718 -0.03162 322 OLC A C6  
2399 C  C14 . OLC W .   ? 0.46314 0.47425 0.32677 0.18364  0.01843  0.03607  322 OLC A C14 
2400 C  C5  . OLC W .   ? 0.75807 0.70990 0.70144 0.04659  -0.02474 -0.00510 322 OLC A C5  
2401 C  C4  . OLC W .   ? 0.78711 0.71028 0.74091 0.02625  -0.01205 -0.00118 322 OLC A C4  
2402 C  C3  . OLC W .   ? 0.79987 0.72687 0.77281 0.01693  -0.00517 0.01639  322 OLC A C3  
2403 C  C2  . OLC W .   ? 0.82540 0.73423 0.82595 0.01814  -0.00622 0.01211  322 OLC A C2  
2404 C  C1  . OLC W .   ? 0.86703 0.74434 0.86333 0.02692  -0.01184 -0.00375 322 OLC A C1  
2405 O  O19 . OLC W .   ? 0.90916 0.74731 0.88863 0.05011  -0.04199 0.00793  322 OLC A O19 
2406 O  O20 . OLC W .   ? 0.89228 0.74802 0.87018 0.01553  0.00132  -0.03282 322 OLC A O20 
2407 O  O   . HOH X .   ? 0.24691 0.27002 0.24369 -0.00164 0.01333  0.02496  401 HOH A O   
2408 O  O   . HOH X .   ? 0.44997 0.27340 0.30047 0.01641  -0.04076 -0.06329 402 HOH A O   
2409 O  O   . HOH X .   ? 0.66033 0.33758 0.58406 0.15252  -0.26795 -0.11678 403 HOH A O   
2410 O  O   B HOH X .   ? 0.33725 0.49460 0.31513 0.07297  -0.08685 0.16653  404 HOH A O   
2411 O  O   . HOH X .   ? 0.48302 0.25469 0.24470 0.08446  -0.04757 -0.01811 405 HOH A O   
2412 O  O   . HOH X .   ? 0.59451 0.74492 0.47381 -0.02285 -0.12593 0.10069  406 HOH A O   
2413 O  O   A HOH X .   ? 0.22506 0.21900 0.22485 -0.03314 0.02020  0.01443  407 HOH A O   
2414 O  O   B HOH X .   ? 0.11196 0.16348 0.28774 -0.03984 0.06490  -0.03114 407 HOH A O   
2415 O  O   . HOH X .   ? 0.36748 0.44185 0.22861 0.02841  -0.01272 -0.00969 408 HOH A O   
2416 O  O   . HOH X .   ? 0.25318 0.25424 0.27500 -0.03388 -0.01238 0.02136  409 HOH A O   
2417 O  O   . HOH X .   ? 0.50180 0.69954 0.90693 0.16261  0.19077  -0.21474 410 HOH A O   
2418 O  O   . HOH X .   ? 0.87492 0.38975 0.37934 0.13446  0.19252  0.07095  411 HOH A O   
2419 O  O   . HOH X .   ? 0.69930 0.68464 0.68817 0.03868  0.17017  0.12006  412 HOH A O   
2420 O  O   . HOH X .   ? 0.34008 0.27203 0.30831 0.00555  -0.03694 0.00061  413 HOH A O   
2421 O  O   . HOH X .   ? 0.64858 0.99303 0.55402 0.25103  0.26972  0.08494  414 HOH A O   
2422 O  O   . HOH X .   ? 0.37746 0.32615 0.36763 0.00056  -0.02831 -0.08903 415 HOH A O   
2423 O  O   . HOH X .   ? 0.57124 0.48121 0.28347 0.16027  -0.03365 -0.03095 416 HOH A O   
2424 O  O   . HOH X .   ? 0.49038 0.75294 0.51093 -0.20954 0.04871  -0.20565 417 HOH A O   
2425 O  O   . HOH X .   ? 0.99834 0.59934 0.34778 0.17384  -0.02459 0.00283  418 HOH A O   
2426 O  O   . HOH X .   ? 0.20736 0.28248 0.30323 0.01662  -0.03784 0.00072  419 HOH A O   
2427 O  O   . HOH X .   ? 0.38295 0.49645 0.38172 0.18473  -0.06314 -0.16814 420 HOH A O   
2428 O  O   . HOH X .   ? 0.23671 0.24647 0.23567 -0.07294 0.01499  -0.01057 421 HOH A O   
2429 O  O   . HOH X .   ? 0.77477 0.55250 0.68781 -0.25866 -0.24592 -0.10555 422 HOH A O   
2430 O  O   . HOH X .   ? 0.30185 0.34684 0.39836 -0.01179 -0.01983 -0.00247 423 HOH A O   
2431 O  O   . HOH X .   ? 0.29360 0.21207 0.24506 0.03593  -0.03030 -0.01242 424 HOH A O   
2432 O  O   . HOH X .   ? 0.37966 0.42830 0.36842 -0.00751 -0.09811 0.00228  425 HOH A O   
2433 O  O   . HOH X .   ? 0.62064 0.56564 0.77308 -0.00876 0.20131  -0.05249 426 HOH A O   
2434 O  O   . HOH X .   ? 0.65992 0.39796 0.44152 -0.10068 0.12552  0.07810  427 HOH A O   
2435 O  O   . HOH X .   ? 0.95341 0.86483 0.40772 0.21769  0.07110  -0.12555 428 HOH A O   
2436 O  O   . HOH X .   ? 0.35700 0.32306 0.25838 0.04328  0.00822  -0.01161 429 HOH A O   
2437 O  O   . HOH X .   ? 0.62998 0.35677 0.32948 -0.05508 0.09656  0.03288  430 HOH A O   
2438 O  O   . HOH X .   ? 0.78179 0.78823 0.53709 0.22237  -0.22187 0.07377  431 HOH A O   
2439 O  O   . HOH X .   ? 0.87194 0.83519 0.76492 0.03224  -0.17565 0.26221  432 HOH A O   
2440 O  O   . HOH X .   ? 0.51019 0.53395 0.85362 0.01366  0.23326  0.20748  433 HOH A O   
2441 O  O   . HOH X .   ? 0.24672 0.23357 0.23737 -0.02547 -0.01188 -0.01389 434 HOH A O   
2442 O  O   . HOH X .   ? 0.25261 0.25890 0.21836 -0.02285 0.00429  0.00112  435 HOH A O   
2443 O  O   A HOH X .   ? 0.60320 0.80899 0.43026 0.13161  0.15534  -0.00548 436 HOH A O   
2444 O  O   . HOH X .   ? 0.29977 0.25605 0.50323 -0.01920 -0.02373 0.06840  437 HOH A O   
2445 O  O   . HOH X .   ? 0.43164 0.56661 0.36030 0.00304  0.06491  -0.00772 438 HOH A O   
2446 O  O   . HOH X .   ? 0.26503 0.31791 0.25948 -0.10006 -0.01551 0.04172  439 HOH A O   
2447 O  O   A HOH X .   ? 0.77324 0.58415 0.37041 -0.01952 0.11098  -0.23161 440 HOH A O   
2448 O  O   . HOH X .   ? 0.24127 0.19123 0.23631 0.01340  0.00369  0.00516  441 HOH A O   
2449 O  O   . HOH X .   ? 0.77119 0.77253 0.52379 -0.17388 0.19212  -0.01411 442 HOH A O   
2450 O  O   . HOH X .   ? 0.39308 0.31114 0.27402 0.06713  0.00126  -0.00472 443 HOH A O   
2451 O  O   . HOH X .   ? 0.89582 0.58794 0.42717 -0.08616 -0.03237 -0.01854 444 HOH A O   
2452 O  O   . HOH X .   ? 0.24972 0.45075 0.32352 0.01387  0.02123  0.04532  445 HOH A O   
2453 O  O   . HOH X .   ? 0.41430 0.60848 0.44096 -0.15314 -0.00888 -0.04059 446 HOH A O   
2454 O  O   . HOH X .   ? 0.27219 0.21538 0.25059 -0.00359 -0.01388 -0.00782 447 HOH A O   
2455 O  O   . HOH X .   ? 0.25161 0.30804 0.24831 0.02022  -0.01464 -0.00527 448 HOH A O   
2456 O  O   . HOH X .   ? 0.53401 0.25366 0.67422 -0.04796 0.27355  -0.06189 449 HOH A O   
2457 O  O   . HOH X .   ? 0.80570 0.68901 0.55456 -0.16533 -0.03389 -0.20018 450 HOH A O   
2458 O  O   . HOH X .   ? 0.36147 0.22773 0.36341 0.08838  0.00000  0.00000  451 HOH A O   
2459 O  O   . HOH X .   ? 0.30176 0.31692 0.48063 -0.01445 0.02679  0.07683  452 HOH A O   
2460 O  O   . HOH X .   ? 0.47713 0.82125 0.74457 0.19796  0.25458  -0.00826 453 HOH A O   
2461 O  O   . HOH X .   ? 0.45853 0.26846 0.22244 0.08825  -0.01948 0.01376  454 HOH A O   
2462 O  O   . HOH X .   ? 0.41958 0.66684 0.37257 0.10252  0.07978  0.03289  455 HOH A O   
2463 O  O   . HOH X .   ? 0.24964 0.28324 0.30009 0.00320  -0.00770 0.02928  456 HOH A O   
2464 O  O   . HOH X .   ? 0.31456 0.27927 0.31468 -0.00847 0.09186  -0.04131 457 HOH A O   
2465 O  O   . HOH X .   ? 0.30619 0.33464 0.27891 0.09677  -0.01649 0.00706  458 HOH A O   
2466 O  O   . HOH X .   ? 0.67946 1.05919 0.67222 0.20541  0.35203  0.08726  459 HOH A O   
2467 O  O   A HOH X .   ? 0.31942 0.24923 0.44932 -0.06878 -0.11443 0.08338  460 HOH A O   
2468 O  O   . HOH X .   ? 0.77023 0.55318 0.71198 -0.23231 0.41627  -0.21815 461 HOH A O   
2469 O  O   . HOH X .   ? 0.51018 0.28223 0.24515 0.07924  0.02446  -0.00450 462 HOH A O   
2470 O  O   . HOH X .   ? 1.05447 0.62178 0.79975 0.15646  0.00852  0.01693  463 HOH A O   
2471 O  O   . HOH X .   ? 0.82679 0.63249 0.51528 -0.07402 0.05732  -0.18497 464 HOH A O   
2472 O  O   . HOH X .   ? 0.23447 0.22723 0.26583 0.03269  -0.01653 0.01657  465 HOH A O   
2473 O  O   . HOH X .   ? 0.33059 0.24916 0.29877 0.01188  -0.07518 0.00571  466 HOH A O   
2474 O  O   . HOH X .   ? 0.17257 0.22055 0.22665 0.01165  0.00953  -0.01362 467 HOH A O   
2475 O  O   . HOH X .   ? 0.45593 0.88238 0.78522 0.07729  0.32461  -0.01522 468 HOH A O   
2476 O  O   . HOH X .   ? 0.82680 0.76374 0.55118 0.22858  -0.17903 0.19235  469 HOH A O   
2477 O  O   . HOH X .   ? 0.61907 0.94377 0.56236 0.15230  0.18248  0.28786  470 HOH A O   
2478 O  O   . HOH X .   ? 0.76700 0.52434 0.66758 0.25445  -0.08568 -0.24984 471 HOH A O   
2479 O  O   . HOH X .   ? 0.73868 0.73203 0.72729 0.24059  -0.26705 0.11440  472 HOH A O   
2480 O  O   . HOH X .   ? 0.90830 0.34516 0.78064 0.04700  0.23639  0.17788  473 HOH A O   
2481 O  O   . HOH X .   ? 0.79564 0.78507 0.82384 -0.22058 0.21155  0.33418  474 HOH A O   
2482 O  O   . HOH X .   ? 0.31375 0.32083 0.18486 -0.03305 -0.02506 0.00606  475 HOH A O   
2483 O  O   . HOH X .   ? 0.39113 0.23480 0.27552 -0.04376 -0.02345 0.02322  476 HOH A O   
2484 O  O   . HOH X .   ? 0.53014 0.81791 0.70349 -0.11362 -0.23767 0.20017  477 HOH A O   
2485 O  O   . HOH X .   ? 0.91857 0.63120 0.84304 0.27729  0.05119  0.24873  478 HOH A O   
2486 O  O   . HOH X .   ? 0.58824 0.71458 0.56456 -0.23582 -0.05735 0.31989  479 HOH A O   
2487 O  O   . HOH X .   ? 0.55474 0.58154 0.41645 -0.08361 -0.17563 0.05000  480 HOH A O   
2488 O  O   . HOH X .   ? 0.43776 0.33969 0.30213 0.07616  0.08067  -0.02396 481 HOH A O   
2489 O  O   . HOH X .   ? 0.83343 0.65169 0.83543 -0.20319 -0.06881 0.15540  482 HOH A O   
2490 O  O   . HOH X .   ? 0.89923 0.67939 0.59173 0.09780  -0.30850 0.20715  483 HOH A O   
2491 O  O   . HOH X .   ? 0.49017 0.36844 0.47571 0.01501  0.01049  0.06600  484 HOH A O   
2492 O  O   . HOH X .   ? 0.63978 0.46116 0.61116 -0.07494 -0.05337 -0.10700 485 HOH A O   
2493 O  O   . HOH X .   ? 0.79970 0.73988 0.52754 -0.12201 0.28438  -0.22497 486 HOH A O   
2494 O  O   . HOH X .   ? 0.66487 0.50682 0.78308 0.12848  -0.19202 -0.20811 487 HOH A O   
2495 O  O   . HOH X .   ? 0.33012 0.31543 0.30120 0.05459  -0.00096 0.01682  488 HOH A O   
2496 O  O   . HOH X .   ? 0.64508 0.53535 0.64717 0.04478  0.28164  -0.15783 489 HOH A O   
2497 O  O   . HOH X .   ? 0.70064 0.62697 0.25823 -0.07668 -0.10518 0.02652  490 HOH A O   
2498 O  O   . HOH X .   ? 0.73160 0.93091 0.54785 -0.02992 0.21322  -0.03977 491 HOH A O   
2499 O  O   . HOH X .   ? 0.50373 0.79128 0.42831 0.10129  0.18742  0.23296  492 HOH A O   
2500 O  O   . HOH X .   ? 0.43927 0.38374 0.29046 0.04522  -0.06799 -0.02226 493 HOH A O   
2501 O  O   . HOH X .   ? 1.07680 0.64728 0.67289 -0.03172 0.06355  0.25228  494 HOH A O   
2502 O  O   . HOH X .   ? 0.33694 0.36103 0.36094 -0.03423 0.04772  0.05502  495 HOH A O   
2503 O  O   . HOH X .   ? 0.40069 0.46672 0.48143 0.01872  0.05610  -0.12734 496 HOH A O   
2504 O  O   . HOH X .   ? 0.66216 0.96197 0.65782 0.03637  -0.09552 0.14247  497 HOH A O   
2505 O  O   . HOH X .   ? 0.34247 0.57096 0.41736 0.01013  -0.10907 -0.01229 498 HOH A O   
2506 O  O   . HOH X .   ? 0.39710 0.29430 0.29061 0.04196  -0.10493 0.02786  499 HOH A O   
2507 O  O   . HOH X .   ? 0.36929 0.29867 0.33883 0.05772  0.01392  -0.04511 500 HOH A O   
2508 O  O   . HOH X .   ? 0.47913 0.68340 0.36886 -0.03292 -0.14925 0.00724  501 HOH A O   
2509 O  O   . HOH X .   ? 0.53757 1.03777 0.82771 0.24168  -0.06525 -0.13875 502 HOH A O   
2510 O  O   . HOH X .   ? 0.40861 0.34114 0.44705 0.05812  -0.03380 -0.11031 503 HOH A O   
2511 O  O   . HOH X .   ? 0.38562 0.23918 0.31107 -0.02145 -0.05029 0.04530  504 HOH A O   
2512 O  O   . HOH X .   ? 0.30772 0.47008 0.30955 0.15241  0.01621  -0.04050 505 HOH A O   
2513 O  O   . HOH X .   ? 0.52245 0.43436 0.31804 -0.01614 0.06537  -0.04586 506 HOH A O   
2514 O  O   . HOH X .   ? 0.39019 0.34570 0.30185 -0.01798 0.09503  0.01530  507 HOH A O   
2515 O  O   . HOH X .   ? 0.62926 0.71140 0.68273 -0.02006 0.32417  -0.03063 508 HOH A O   
2516 O  O   . HOH X .   ? 0.22677 0.22638 0.16606 0.01372  0.06245  -0.01080 509 HOH A O   
2517 O  O   . HOH X .   ? 0.27113 0.39091 0.52216 -0.02669 -0.02149 -0.07446 510 HOH A O   
2518 O  O   . HOH X .   ? 0.35082 0.36473 0.30185 0.00042  -0.05459 -0.07879 511 HOH A O   
2519 O  O   . HOH X .   ? 0.54533 0.50325 0.37354 -0.05228 0.04070  0.03477  512 HOH A O   
2520 O  O   . HOH X .   ? 0.86478 0.40492 0.71770 -0.04640 -0.24478 0.14635  513 HOH A O   
2521 O  O   . HOH X .   ? 0.88495 0.48128 0.52273 -0.11979 -0.31663 -0.03650 514 HOH A O   
2522 O  O   . HOH X .   ? 0.81412 0.47458 0.40626 -0.03999 0.04227  -0.04536 515 HOH A O   
2523 O  O   . HOH X .   ? 0.63970 0.44220 0.61746 0.01765  0.18646  -0.03705 516 HOH A O   
2524 O  O   . HOH X .   ? 0.94535 0.98967 0.70852 -0.05660 0.02578  0.09335  517 HOH A O   
2525 O  O   . HOH X .   ? 0.82371 0.61377 0.67065 0.08235  -0.23790 0.00974  518 HOH A O   
2526 O  O   . HOH X .   ? 0.71512 0.39017 0.35817 -0.01974 0.10414  0.00296  519 HOH A O   
2527 O  O   . HOH X .   ? 0.56323 0.46554 0.30453 0.19992  -0.05707 -0.08574 520 HOH A O   
2528 O  O   B HOH X .   ? 0.49867 0.58337 0.69206 0.05970  0.02437  -0.11514 521 HOH A O   
2529 O  O   . HOH X .   ? 0.59399 0.47566 0.73577 -0.00445 0.12596  -0.07646 522 HOH A O   
2530 O  O   . HOH X .   ? 0.69304 0.32368 0.42269 -0.06594 -0.12737 0.12147  523 HOH A O   
2531 O  O   . HOH X .   ? 0.83384 0.81896 0.61032 -0.01418 0.03113  0.05378  524 HOH A O   
2532 O  O   . HOH X .   ? 0.54887 0.48332 0.59748 -0.24403 0.04040  -0.06678 525 HOH A O   
2533 O  O   . HOH X .   ? 0.85376 0.60254 0.54601 0.28268  -0.07635 0.10460  526 HOH A O   
2534 O  O   . HOH X .   ? 0.49232 0.48098 0.46152 -0.11324 -0.04218 0.13646  527 HOH A O   
2535 O  O   . HOH X .   ? 0.51638 0.78406 0.84463 -0.08925 0.14758  0.18934  528 HOH A O   
2536 O  O   . HOH X .   ? 0.49942 0.45564 0.66902 0.14061  0.14826  0.09200  529 HOH A O   
2537 O  O   . HOH X .   ? 0.36314 0.51102 0.60562 0.13901  0.17559  0.07437  530 HOH A O   
2538 O  O   . HOH X .   ? 0.65308 0.87615 0.41454 0.07977  -0.02592 0.10026  531 HOH A O   
2539 O  O   . HOH X .   ? 0.52989 0.88219 0.76557 0.18597  0.08743  0.09419  532 HOH A O   
2540 O  O   A HOH X .   ? 0.60919 0.75770 0.38029 0.10974  -0.18978 -0.11948 533 HOH A O   
2541 O  O   . HOH X .   ? 0.71485 0.63079 0.70121 0.26514  0.32154  0.21110  534 HOH A O   
2542 O  O   . HOH X .   ? 0.85866 0.82457 0.75009 0.05409  0.23078  -0.05090 535 HOH A O   
2543 O  O   . HOH X .   ? 0.90523 0.31678 0.38629 0.05329  0.00000  -0.00000 536 HOH A O   
2544 O  O   . HOH X .   ? 0.32282 0.45484 0.33862 0.02391  -0.06224 0.02887  537 HOH A O   
2545 O  O   . HOH X .   ? 0.61062 1.02424 0.73030 -0.05214 0.13611  0.33348  538 HOH A O   
2546 O  O   . HOH X .   ? 0.78384 0.58998 1.05779 -0.22419 0.25525  -0.01875 539 HOH A O   
2547 O  O   . HOH X .   ? 0.76409 0.96395 0.51241 -0.15541 -0.20776 -0.06094 540 HOH A O   
2548 O  O   A HOH X .   ? 0.64678 0.36630 0.40417 -0.02065 -0.07213 -0.09679 541 HOH A O   
2549 O  O   B HOH X .   ? 0.51552 0.28164 0.23865 0.09354  -0.06217 0.05317  541 HOH A O   
2550 O  O   . HOH X .   ? 0.87159 0.73332 0.62275 -0.31041 0.24385  0.12298  542 HOH A O   
2551 O  O   . HOH X .   ? 0.46358 0.96079 0.68177 0.09599  -0.10756 0.20892  543 HOH A O   
2552 O  O   . HOH X .   ? 0.85553 0.77594 0.59295 -0.03696 0.01145  0.28202  544 HOH A O   
2553 O  O   A HOH X .   ? 0.71196 0.31661 0.46066 -0.12385 0.27540  -0.12943 545 HOH A O   
2554 O  O   . HOH X .   ? 0.73876 0.71965 0.66978 0.03939  -0.22151 0.20286  546 HOH A O   
# 
