data_9IN8
# 
_entry.id   9IN8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9IN8         pdb_00009in8 10.2210/pdb9in8/pdb 
WWPDB D_1300049192 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'Structure model' 1 1 2025-04-23 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_DOI'    
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IN8 
_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 
'Bourenkov, G.'  4 0000-0002-2617-5920 
'Gordeliy, V.'   5 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      10.1038/s41594-025-01488-7 
_citation.pdbx_database_id_PubMed   40205223 
_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  0000-0002-0157-532X 
primary 'Bukhalovich, S.' 3  0000-0002-0770-6597 
primary 'Tsybrov, F.'     4  0000-0001-7422-0899 
primary 'Lamm, G.H.U.'    5  0009-0006-6743-2344 
primary 'Astashkin, R.'   6  ?                   
primary 'Doroginin, D.'   7  ?                   
primary 'Matveev, G.'     8  ?                   
primary 'Sudarev, V.'     9  ?                   
primary 'Kuzmin, A.'      10 0000-0003-3945-3691 
primary 'Zinovev, E.'     11 ?                   
primary 'Vlasova, A.'     12 ?                   
primary 'Ryzhykau, Y.'    13 0000-0003-3719-1464 
primary 'Ilyinsky, N.'    14 0000-0002-8812-5849 
primary 'Gushchin, I.'    15 0000-0002-5348-6070 
primary 'Bourenkov, G.'   16 ?                   
primary 'Alekseev, A.'    17 ?                   
primary 'Round, A.'       18 0000-0002-0723-8228 
primary 'Wachtveitl, J.'  19 0000-0002-8496-8240 
primary 'Bamberg, E.'     20 0000-0002-5411-6207 
primary 'Gordeliy, V.'    21 0000-0001-5782-5896 
# 
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 RETINAL                                          284.436   1   ? ? ? ? 
3 non-polymer syn 'SODIUM ION'                                     22.990    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   9   ? ? ? ? 
7 non-polymer syn GLYCEROL                                         92.094    3   ? ? ? ? 
8 water       nat water                                            18.015    151 ? ? ? ? 
# 
_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 RETINAL                                          RET 
3 'SODIUM ION'                                     NA  
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 RET ? ? RET ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NA  ? ? NA  ? ? '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 RET 1   301 301 RET RET A . 
C 3 NA  1   302 302 NA  NA  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 7 GOL 1   314 411 GOL GOL A . 
P 7 GOL 1   315 412 GOL GOL A . 
Q 7 GOL 1   316 413 GOL GOL A . 
R 5 OLC 1   317 414 OLC OLC 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 8 HOH 1   401 560 HOH HOH A . 
W 8 HOH 2   402 604 HOH HOH A . 
W 8 HOH 3   403 534 HOH HOH A . 
W 8 HOH 4   404 516 HOH HOH A . 
W 8 HOH 5   405 577 HOH HOH A . 
W 8 HOH 6   406 523 HOH HOH A . 
W 8 HOH 7   407 513 HOH HOH A . 
W 8 HOH 8   408 507 HOH HOH A . 
W 8 HOH 9   409 581 HOH HOH A . 
W 8 HOH 10  410 640 HOH HOH A . 
W 8 HOH 11  411 624 HOH HOH A . 
W 8 HOH 12  412 524 HOH HOH A . 
W 8 HOH 13  413 589 HOH HOH A . 
W 8 HOH 14  414 583 HOH HOH A . 
W 8 HOH 15  415 567 HOH HOH A . 
W 8 HOH 16  416 530 HOH HOH A . 
W 8 HOH 17  417 634 HOH HOH A . 
W 8 HOH 18  418 650 HOH HOH A . 
W 8 HOH 19  419 561 HOH HOH A . 
W 8 HOH 20  420 515 HOH HOH A . 
W 8 HOH 21  421 619 HOH HOH A . 
W 8 HOH 22  422 547 HOH HOH A . 
W 8 HOH 23  423 552 HOH HOH A . 
W 8 HOH 24  424 526 HOH HOH A . 
W 8 HOH 25  425 649 HOH HOH A . 
W 8 HOH 26  426 505 HOH HOH A . 
W 8 HOH 27  427 584 HOH HOH A . 
W 8 HOH 28  428 504 HOH HOH A . 
W 8 HOH 29  429 514 HOH HOH A . 
W 8 HOH 30  430 517 HOH HOH A . 
W 8 HOH 31  431 537 HOH HOH A . 
W 8 HOH 32  432 625 HOH HOH A . 
W 8 HOH 33  433 628 HOH HOH A . 
W 8 HOH 34  434 564 HOH HOH A . 
W 8 HOH 35  435 503 HOH HOH A . 
W 8 HOH 36  436 585 HOH HOH A . 
W 8 HOH 37  437 556 HOH HOH A . 
W 8 HOH 38  438 636 HOH HOH A . 
W 8 HOH 39  439 512 HOH HOH A . 
W 8 HOH 40  440 596 HOH HOH A . 
W 8 HOH 41  441 506 HOH HOH A . 
W 8 HOH 42  442 545 HOH HOH A . 
W 8 HOH 43  443 542 HOH HOH A . 
W 8 HOH 44  444 519 HOH HOH A . 
W 8 HOH 45  445 520 HOH HOH A . 
W 8 HOH 46  446 549 HOH HOH A . 
W 8 HOH 47  447 533 HOH HOH A . 
W 8 HOH 48  448 502 HOH HOH A . 
W 8 HOH 49  449 522 HOH HOH A . 
W 8 HOH 50  450 509 HOH HOH A . 
W 8 HOH 51  451 541 HOH HOH A . 
W 8 HOH 52  452 626 HOH HOH A . 
W 8 HOH 53  453 629 HOH HOH A . 
W 8 HOH 54  454 510 HOH HOH A . 
W 8 HOH 55  455 566 HOH HOH A . 
W 8 HOH 56  456 586 HOH HOH A . 
W 8 HOH 57  457 525 HOH HOH A . 
W 8 HOH 58  458 538 HOH HOH A . 
W 8 HOH 59  459 642 HOH HOH A . 
W 8 HOH 60  460 579 HOH HOH A . 
W 8 HOH 61  461 508 HOH HOH A . 
W 8 HOH 62  462 521 HOH HOH A . 
W 8 HOH 63  463 644 HOH HOH A . 
W 8 HOH 64  464 591 HOH HOH A . 
W 8 HOH 65  465 532 HOH HOH A . 
W 8 HOH 66  466 576 HOH HOH A . 
W 8 HOH 67  467 643 HOH HOH A . 
W 8 HOH 68  468 588 HOH HOH A . 
W 8 HOH 69  469 641 HOH HOH A . 
W 8 HOH 70  470 607 HOH HOH A . 
W 8 HOH 71  471 630 HOH HOH A . 
W 8 HOH 72  472 558 HOH HOH A . 
W 8 HOH 73  473 580 HOH HOH A . 
W 8 HOH 74  474 609 HOH HOH A . 
W 8 HOH 75  475 563 HOH HOH A . 
W 8 HOH 76  476 574 HOH HOH A . 
W 8 HOH 77  477 639 HOH HOH A . 
W 8 HOH 78  478 606 HOH HOH A . 
W 8 HOH 79  479 555 HOH HOH A . 
W 8 HOH 80  480 571 HOH HOH A . 
W 8 HOH 81  481 529 HOH HOH A . 
W 8 HOH 82  482 550 HOH HOH A . 
W 8 HOH 83  483 616 HOH HOH A . 
W 8 HOH 84  484 605 HOH HOH A . 
W 8 HOH 85  485 511 HOH HOH A . 
W 8 HOH 86  486 531 HOH HOH A . 
W 8 HOH 87  487 610 HOH HOH A . 
W 8 HOH 88  488 593 HOH HOH A . 
W 8 HOH 89  489 539 HOH HOH A . 
W 8 HOH 90  490 573 HOH HOH A . 
W 8 HOH 91  491 648 HOH HOH A . 
W 8 HOH 92  492 518 HOH HOH A . 
W 8 HOH 93  493 557 HOH HOH A . 
W 8 HOH 94  494 528 HOH HOH A . 
W 8 HOH 95  495 603 HOH HOH A . 
W 8 HOH 96  496 575 HOH HOH A . 
W 8 HOH 97  497 565 HOH HOH A . 
W 8 HOH 98  498 613 HOH HOH A . 
W 8 HOH 99  499 608 HOH HOH A . 
W 8 HOH 100 500 633 HOH HOH A . 
W 8 HOH 101 501 551 HOH HOH A . 
W 8 HOH 102 502 527 HOH HOH A . 
W 8 HOH 103 503 623 HOH HOH A . 
W 8 HOH 104 504 618 HOH HOH A . 
W 8 HOH 105 505 592 HOH HOH A . 
W 8 HOH 106 506 594 HOH HOH A . 
W 8 HOH 107 507 572 HOH HOH A . 
W 8 HOH 108 508 535 HOH HOH A . 
W 8 HOH 109 509 632 HOH HOH A . 
W 8 HOH 110 510 546 HOH HOH A . 
W 8 HOH 111 511 595 HOH HOH A . 
W 8 HOH 112 512 553 HOH HOH A . 
W 8 HOH 113 513 590 HOH HOH A . 
W 8 HOH 114 514 536 HOH HOH A . 
W 8 HOH 115 515 543 HOH HOH A . 
W 8 HOH 116 516 646 HOH HOH A . 
W 8 HOH 117 517 501 HOH HOH A . 
W 8 HOH 118 518 598 HOH HOH A . 
W 8 HOH 119 519 617 HOH HOH A . 
W 8 HOH 120 520 600 HOH HOH A . 
W 8 HOH 121 521 578 HOH HOH A . 
W 8 HOH 122 522 559 HOH HOH A . 
W 8 HOH 123 523 651 HOH HOH A . 
W 8 HOH 124 524 554 HOH HOH A . 
W 8 HOH 125 525 638 HOH HOH A . 
W 8 HOH 126 526 544 HOH HOH A . 
W 8 HOH 127 527 612 HOH HOH A . 
W 8 HOH 128 528 635 HOH HOH A . 
W 8 HOH 129 529 582 HOH HOH A . 
W 8 HOH 130 530 587 HOH HOH A . 
W 8 HOH 131 531 615 HOH HOH A . 
W 8 HOH 132 532 627 HOH HOH A . 
W 8 HOH 133 533 647 HOH HOH A . 
W 8 HOH 134 534 645 HOH HOH A . 
W 8 HOH 135 535 614 HOH HOH A . 
W 8 HOH 136 536 621 HOH HOH A . 
W 8 HOH 137 537 562 HOH HOH A . 
W 8 HOH 138 538 569 HOH HOH A . 
W 8 HOH 139 539 548 HOH HOH A . 
W 8 HOH 140 540 568 HOH HOH A . 
W 8 HOH 141 541 599 HOH HOH A . 
W 8 HOH 142 542 631 HOH HOH A . 
W 8 HOH 143 543 597 HOH HOH A . 
W 8 HOH 144 544 620 HOH HOH A . 
W 8 HOH 145 545 570 HOH HOH A . 
W 8 HOH 146 546 540 HOH HOH A . 
W 8 HOH 147 547 601 HOH HOH A . 
W 8 HOH 148 548 637 HOH HOH A . 
W 8 HOH 149 549 611 HOH HOH A . 
W 8 HOH 150 550 602 HOH HOH A . 
W 8 HOH 151 551 622 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 ASN 66  ? CG  ? A ASN 66  CG  
5   1 Y 1 A ASN 66  ? OD1 ? A ASN 66  OD1 
6   1 Y 1 A ASN 66  ? ND2 ? A ASN 66  ND2 
7   1 Y 1 A ASP 98  ? OD1 ? A ASP 98  OD1 
8   1 Y 1 A ASP 98  ? OD2 ? A ASP 98  OD2 
9   1 Y 1 A ASP 99  ? CG  ? A ASP 99  CG  
10  1 Y 1 A ASP 99  ? OD1 ? A ASP 99  OD1 
11  1 Y 1 A ASP 99  ? OD2 ? A ASP 99  OD2 
12  1 Y 1 A LYS 221 ? CD  ? A LYS 221 CD  
13  1 Y 1 A LYS 221 ? CE  ? A LYS 221 CE  
14  1 Y 1 A LYS 221 ? NZ  ? A LYS 221 NZ  
15  1 Y 1 A LEU 224 ? CG  ? A LEU 224 CG  
16  1 Y 1 A LEU 224 ? CD1 ? A LEU 224 CD1 
17  1 Y 1 A LEU 224 ? CD2 ? A LEU 224 CD2 
18  1 N 1 A OLC 304 ? C18 ? E OLC 1   C18 
19  1 N 1 A OLC 304 ? C17 ? E OLC 1   C17 
20  1 N 1 A OLC 304 ? C24 ? E OLC 1   C24 
21  1 N 1 A OLC 304 ? C16 ? E OLC 1   C16 
22  1 N 1 A OLC 304 ? C15 ? E OLC 1   C15 
23  1 N 1 A OLC 304 ? C21 ? E OLC 1   C21 
24  1 N 1 A OLC 304 ? C22 ? E OLC 1   C22 
25  1 N 1 A OLC 304 ? O25 ? E OLC 1   O25 
26  1 N 1 A OLC 304 ? O23 ? E OLC 1   O23 
27  1 N 1 A LFA 305 ? C11 ? F LFA 1   C11 
28  1 N 1 A LFA 305 ? C12 ? F LFA 1   C12 
29  1 N 1 A LFA 305 ? C13 ? F LFA 1   C13 
30  1 N 1 A LFA 305 ? C14 ? F LFA 1   C14 
31  1 N 1 A LFA 305 ? C15 ? F LFA 1   C15 
32  1 N 1 A LFA 305 ? C16 ? F LFA 1   C16 
33  1 N 1 A LFA 305 ? C17 ? F LFA 1   C17 
34  1 N 1 A LFA 305 ? C18 ? F LFA 1   C18 
35  1 N 1 A LFA 305 ? C19 ? F LFA 1   C19 
36  1 N 1 A LFA 305 ? C20 ? F LFA 1   C20 
37  1 N 1 A LFA 306 ? C1  ? G LFA 1   C1  
38  1 N 1 A LFA 306 ? C2  ? G LFA 1   C2  
39  1 N 1 A LFA 306 ? C3  ? G LFA 1   C3  
40  1 N 1 A LFA 306 ? C4  ? G LFA 1   C4  
41  1 N 1 A LFA 306 ? C5  ? G LFA 1   C5  
42  1 N 1 A LFA 306 ? C6  ? G LFA 1   C6  
43  1 N 1 A LFA 306 ? C7  ? G LFA 1   C7  
44  1 N 1 A LFA 307 ? C13 ? H LFA 1   C13 
45  1 N 1 A LFA 307 ? C14 ? H LFA 1   C14 
46  1 N 1 A LFA 307 ? C15 ? H LFA 1   C15 
47  1 N 1 A LFA 307 ? C16 ? H LFA 1   C16 
48  1 N 1 A LFA 307 ? C17 ? H LFA 1   C17 
49  1 N 1 A LFA 307 ? C18 ? H LFA 1   C18 
50  1 N 1 A LFA 307 ? C19 ? H LFA 1   C19 
51  1 N 1 A LFA 307 ? C20 ? H LFA 1   C20 
52  1 N 1 A LFA 308 ? C1  ? I LFA 1   C1  
53  1 N 1 A LFA 308 ? C2  ? I LFA 1   C2  
54  1 N 1 A LFA 308 ? C3  ? I LFA 1   C3  
55  1 N 1 A LFA 308 ? C4  ? I LFA 1   C4  
56  1 N 1 A LFA 308 ? C5  ? I LFA 1   C5  
57  1 N 1 A LFA 309 ? C1  ? J LFA 1   C1  
58  1 N 1 A LFA 309 ? C2  ? J LFA 1   C2  
59  1 N 1 A LFA 309 ? C3  ? J LFA 1   C3  
60  1 N 1 A LFA 309 ? C4  ? J LFA 1   C4  
61  1 N 1 A LFA 310 ? C6  ? K LFA 1   C6  
62  1 N 1 A LFA 310 ? C7  ? K LFA 1   C7  
63  1 N 1 A LFA 310 ? C8  ? K LFA 1   C8  
64  1 N 1 A LFA 310 ? C9  ? K LFA 1   C9  
65  1 N 1 A LFA 310 ? C10 ? K LFA 1   C10 
66  1 N 1 A LFA 310 ? C11 ? K LFA 1   C11 
67  1 N 1 A LFA 310 ? C12 ? K LFA 1   C12 
68  1 N 1 A LFA 310 ? C13 ? K LFA 1   C13 
69  1 N 1 A LFA 310 ? C14 ? K LFA 1   C14 
70  1 N 1 A LFA 310 ? C15 ? K LFA 1   C15 
71  1 N 1 A LFA 310 ? C16 ? K LFA 1   C16 
72  1 N 1 A LFA 310 ? C17 ? K LFA 1   C17 
73  1 N 1 A LFA 310 ? C18 ? K LFA 1   C18 
74  1 N 1 A LFA 310 ? C19 ? K LFA 1   C19 
75  1 N 1 A LFA 310 ? C20 ? K LFA 1   C20 
76  1 N 1 A LFA 311 ? C1  ? L LFA 1   C1  
77  1 N 1 A LFA 311 ? C2  ? L LFA 1   C2  
78  1 N 1 A LFA 311 ? C3  ? L LFA 1   C3  
79  1 N 1 A LFA 311 ? C4  ? L LFA 1   C4  
80  1 N 1 A LFA 311 ? C5  ? L LFA 1   C5  
81  1 N 1 A LFA 311 ? C6  ? L LFA 1   C6  
82  1 N 1 A LFA 311 ? C7  ? L LFA 1   C7  
83  1 N 1 A LFA 311 ? C8  ? L LFA 1   C8  
84  1 N 1 A LFA 311 ? C9  ? L LFA 1   C9  
85  1 N 1 A LFA 311 ? C10 ? L LFA 1   C10 
86  1 N 1 A LFA 311 ? C11 ? L LFA 1   C11 
87  1 N 1 A LFA 311 ? C12 ? L LFA 1   C12 
88  1 N 1 A LFA 311 ? C13 ? L LFA 1   C13 
89  1 N 1 A LFA 311 ? C14 ? L LFA 1   C14 
90  1 N 1 A LFA 311 ? C15 ? L LFA 1   C15 
91  1 N 1 A LFA 311 ? C19 ? L LFA 1   C19 
92  1 N 1 A LFA 311 ? C20 ? L LFA 1   C20 
93  1 N 1 A LFA 312 ? C1  ? M LFA 1   C1  
94  1 N 1 A LFA 312 ? C2  ? M LFA 1   C2  
95  1 N 1 A LFA 312 ? C3  ? M LFA 1   C3  
96  1 N 1 A LFA 312 ? C4  ? M LFA 1   C4  
97  1 N 1 A LFA 312 ? C5  ? M LFA 1   C5  
98  1 N 1 A LFA 312 ? C6  ? M LFA 1   C6  
99  1 N 1 A LFA 312 ? C7  ? M LFA 1   C7  
100 1 N 1 A LFA 312 ? C8  ? M LFA 1   C8  
101 1 N 1 A LFA 312 ? C9  ? M LFA 1   C9  
102 1 N 1 A LFA 312 ? C10 ? M LFA 1   C10 
103 1 N 1 A LFA 312 ? C11 ? M LFA 1   C11 
104 1 N 1 A LFA 312 ? C12 ? M LFA 1   C12 
105 1 N 1 A LFA 312 ? C13 ? M LFA 1   C13 
106 1 N 1 A LFA 312 ? C14 ? M LFA 1   C14 
107 1 N 1 A OLC 317 ? C18 ? R OLC 1   C18 
108 1 N 1 A OLC 317 ? C10 ? R OLC 1   C10 
109 1 N 1 A OLC 317 ? C9  ? R OLC 1   C9  
110 1 N 1 A OLC 317 ? C17 ? R OLC 1   C17 
111 1 N 1 A OLC 317 ? C11 ? R OLC 1   C11 
112 1 N 1 A OLC 317 ? C8  ? R OLC 1   C8  
113 1 N 1 A OLC 317 ? C16 ? R OLC 1   C16 
114 1 N 1 A OLC 317 ? C12 ? R OLC 1   C12 
115 1 N 1 A OLC 317 ? C7  ? R OLC 1   C7  
116 1 N 1 A OLC 317 ? C15 ? R OLC 1   C15 
117 1 N 1 A OLC 317 ? C13 ? R OLC 1   C13 
118 1 N 1 A OLC 317 ? C6  ? R OLC 1   C6  
119 1 N 1 A OLC 317 ? C14 ? R OLC 1   C14 
120 1 N 1 A OLC 317 ? C5  ? R OLC 1   C5  
121 1 N 1 A OLC 318 ? C18 ? S OLC 1   C18 
122 1 N 1 A OLC 318 ? C17 ? S OLC 1   C17 
123 1 N 1 A OLC 318 ? C16 ? S OLC 1   C16 
124 1 N 1 A OLC 318 ? C12 ? S OLC 1   C12 
125 1 N 1 A OLC 318 ? C15 ? S OLC 1   C15 
126 1 N 1 A OLC 318 ? C13 ? S OLC 1   C13 
127 1 N 1 A OLC 318 ? C14 ? S OLC 1   C14 
128 1 N 1 A OLC 319 ? C18 ? T OLC 1   C18 
129 1 N 1 A OLC 319 ? C10 ? T OLC 1   C10 
130 1 N 1 A OLC 319 ? C9  ? T OLC 1   C9  
131 1 N 1 A OLC 319 ? C17 ? T OLC 1   C17 
132 1 N 1 A OLC 319 ? C11 ? T OLC 1   C11 
133 1 N 1 A OLC 319 ? C8  ? T OLC 1   C8  
134 1 N 1 A OLC 319 ? C24 ? T OLC 1   C24 
135 1 N 1 A OLC 319 ? C16 ? T OLC 1   C16 
136 1 N 1 A OLC 319 ? C12 ? T OLC 1   C12 
137 1 N 1 A OLC 319 ? C15 ? T OLC 1   C15 
138 1 N 1 A OLC 319 ? C13 ? T OLC 1   C13 
139 1 N 1 A OLC 319 ? C14 ? T OLC 1   C14 
140 1 N 1 A OLC 319 ? C21 ? T OLC 1   C21 
141 1 N 1 A OLC 319 ? C22 ? T OLC 1   C22 
142 1 N 1 A OLC 319 ? O25 ? T OLC 1   O25 
143 1 N 1 A OLC 319 ? O23 ? T OLC 1   O23 
144 1 N 1 A OLC 320 ? C18 ? U OLC 1   C18 
145 1 N 1 A OLC 320 ? C17 ? U OLC 1   C17 
146 1 N 1 A OLC 320 ? C24 ? U OLC 1   C24 
147 1 N 1 A OLC 320 ? C16 ? U OLC 1   C16 
148 1 N 1 A OLC 320 ? C15 ? U OLC 1   C15 
149 1 N 1 A OLC 320 ? C13 ? U OLC 1   C13 
150 1 N 1 A OLC 320 ? C14 ? U OLC 1   C14 
151 1 N 1 A OLC 320 ? O25 ? U OLC 1   O25 
152 1 N 1 A OLC 320 ? O23 ? U OLC 1   O23 
153 1 N 1 A OLC 321 ? C18 ? V OLC 1   C18 
154 1 N 1 A OLC 321 ? C17 ? V OLC 1   C17 
155 1 N 1 A OLC 321 ? C24 ? V OLC 1   C24 
156 1 N 1 A OLC 321 ? C16 ? V OLC 1   C16 
157 1 N 1 A OLC 321 ? C15 ? V OLC 1   C15 
158 1 N 1 A OLC 321 ? C21 ? V OLC 1   C21 
159 1 N 1 A OLC 321 ? C22 ? V OLC 1   C22 
160 1 N 1 A OLC 321 ? O25 ? V OLC 1   O25 
161 1 N 1 A OLC 321 ? O23 ? V 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 reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .           1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .           2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .           3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.20.1_4487 4 
# 
_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                     9IN8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.427 
_cell.length_a_esd                 ? 
_cell.length_b                     115.029 
_cell.length_b_esd                 ? 
_cell.length_c                     53.337 
_cell.length_c_esd                 ? 
_cell.volume                       284843.655 
_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                         9IN8 
_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                   9IN8 
_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             2.74 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.1 
_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         2023-03-21 
_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   0.9763 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9763 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          20.81 
_reflns.entry_id                                       9IN8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.34 
_reflns.d_resolution_low                               43.05 
_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                                     47593 
_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                           93.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.1 
_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                                0.024 
_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                                    1.34 
_reflns_shell.d_res_low                                     1.46 
_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                             2380 
_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                               12.6 
_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                               1.331 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.175 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          57.8 
_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                               29.24 
_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                                 9IN8 
_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                            1.34 
_refine.ls_d_res_low                             39.11 
_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                     47512 
_refine.ls_number_reflns_R_free                  2346 
_refine.ls_number_reflns_R_work                  45166 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    72.88 
_refine.ls_percent_reflns_R_free                 4.94 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1853 
_refine.ls_R_factor_R_free                       0.2120 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1838 
_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                 29.4736 
_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                            0.1612 
_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                       1.34 
_refine_hist.d_res_low                        39.11 
_refine_hist.number_atoms_solvent             151 
_refine_hist.number_atoms_total               2307 
_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        1908 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         248 
_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' ? 0.0079  ? 2958 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9019  ? 3980 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0757  ? 413  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0058  ? 475  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.8261 ? 1135 ? 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' 1.34 1.37  . . 3   105  2.89  . . . . 0.3510 . . . . . . . . . . . 0.4574 
'X-RAY DIFFRACTION' 1.37 1.40  . . 12  286  7.97  . . . . 0.3761 . . . . . . . . . . . 0.3430 
'X-RAY DIFFRACTION' 1.40 1.43  . . 30  692  19.18 . . . . 0.3655 . . . . . . . . . . . 0.3743 
'X-RAY DIFFRACTION' 1.43 1.46  . . 79  1169 32.91 . . . . 0.3125 . . . . . . . . . . . 0.3733 
'X-RAY DIFFRACTION' 1.46 1.50  . . 94  1831 50.64 . . . . 0.3154 . . . . . . . . . . . 0.3811 
'X-RAY DIFFRACTION' 1.50 1.55  . . 124 2330 64.66 . . . . 0.3012 . . . . . . . . . . . 0.3121 
'X-RAY DIFFRACTION' 1.55 1.60  . . 148 2743 76.26 . . . . 0.2885 . . . . . . . . . . . 0.3019 
'X-RAY DIFFRACTION' 1.60 1.65  . . 161 3103 85.47 . . . . 0.2695 . . . . . . . . . . . 0.3278 
'X-RAY DIFFRACTION' 1.65 1.72  . . 165 3419 93.90 . . . . 0.2598 . . . . . . . . . . . 0.2841 
'X-RAY DIFFRACTION' 1.72 1.80  . . 155 3627 99.76 . . . . 0.2319 . . . . . . . . . . . 0.2661 
'X-RAY DIFFRACTION' 1.80 1.89  . . 183 3629 99.82 . . . . 0.2004 . . . . . . . . . . . 0.2550 
'X-RAY DIFFRACTION' 1.89 2.01  . . 197 3637 99.84 . . . . 0.1731 . . . . . . . . . . . 0.2192 
'X-RAY DIFFRACTION' 2.01 2.17  . . 178 3652 99.95 . . . . 0.1496 . . . . . . . . . . . 0.1728 
'X-RAY DIFFRACTION' 2.17 2.39  . . 189 3669 99.87 . . . . 0.1501 . . . . . . . . . . . 0.1715 
'X-RAY DIFFRACTION' 2.39 2.73  . . 212 3680 99.97 . . . . 0.1518 . . . . . . . . . . . 0.1727 
'X-RAY DIFFRACTION' 2.73 3.44  . . 188 3718 99.87 . . . . 0.1622 . . . . . . . . . . . 0.1941 
'X-RAY DIFFRACTION' 3.44 39.11 . . 228 3876 99.64 . . . . 0.1881 . . . . . . . . . . . 0.2128 
# 
_struct.entry_id                     9IN8 
_struct.title                        
'True-atomic resolution crystal structure of the open 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        9IN8 
_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 7 ? 
P N N 7 ? 
Q N N 7 ? 
R N N 5 ? 
S N N 5 ? 
T N N 5 ? 
U N N 5 ? 
V N N 5 ? 
W 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              9IN8 
_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 9IN8 LEU A 224 ? UNP F2Y337 ? ? 'expression tag' 224 1 
1 9IN8 GLU A 225 ? UNP F2Y337 ? ? 'expression tag' 225 2 
1 9IN8 HIS A 226 ? UNP F2Y337 ? ? 'expression tag' 226 3 
1 9IN8 HIS A 227 ? UNP F2Y337 ? ? 'expression tag' 227 4 
1 9IN8 HIS A 228 ? UNP F2Y337 ? ? 'expression tag' 228 5 
1 9IN8 HIS A 229 ? UNP F2Y337 ? ? 'expression tag' 229 6 
1 9IN8 HIS A 230 ? UNP F2Y337 ? ? 'expression tag' 230 7 
1 9IN8 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 
# 
_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  ? GLN A 63  ? ASP A 34  GLN A 63  1 ? 30 
HELX_P HELX_P4  AA4 ASP A 68  ? TYR A 71  ? ASP A 68  TYR A 71  5 ? 4  
HELX_P HELX_P5  AA5 VAL A 72  ? SER A 97  ? VAL A 72  SER A 97  1 ? 26 
HELX_P HELX_P6  AA6 ARG A 102 ? THR A 133 ? ARG A 102 THR A 133 1 ? 32 
HELX_P HELX_P7  AA7 ASN A 137 ? THR A 161 ? ASN A 137 THR A 161 1 ? 25 
HELX_P HELX_P8  AA8 ASN A 164 ? MET A 186 ? ASN A 164 MET A 186 1 ? 23 
HELX_P HELX_P9  AA9 PRO A 188 ? LYS A 204 ? PRO A 188 LYS A 204 1 ? 17 
HELX_P HELX_P10 AB1 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 ? A FME 1   A ASP 2   1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale2 covale both ? A FME 1   C   ? ? ? 1_555 A ASP 2 N   B ? A FME 1   A ASP 2   1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale3 covale one  ? A LYS 204 NZ  A ? ? 1_555 B RET . C15 A ? A LYS 204 A RET 301 1_555 ? ? ? ? ? ? ? 1.400 ? ? 
covale4 covale one  ? A LYS 204 NZ  B ? ? 1_555 B RET . C15 B ? A LYS 204 A RET 301 1_555 ? ? ? ? ? ? ? 1.505 ? ? 
covale5 covale one  ? A LYS 204 NZ  C ? ? 1_555 B RET . C15 C ? A LYS 204 A RET 301 1_555 ? ? ? ? ? ? ? 1.501 ? ? 
metalc1 metalc ?    ? A ASP 68  OD1 A ? ? 1_555 C NA  . NA  A ? A ASP 68  A NA  302 1_555 ? ? ? ? ? ? ? 3.186 ? ? 
metalc2 metalc ?    ? A ASP 68  OD2 A ? ? 1_555 C NA  . NA  A ? A ASP 68  A NA  302 1_555 ? ? ? ? ? ? ? 2.766 ? ? 
metalc3 metalc ?    ? A GLU 132 O   A ? ? 1_555 C NA  . NA  A ? A GLU 132 A NA  302 1_555 ? ? ? ? ? ? ? 2.527 ? ? 
metalc4 metalc ?    ? A GLU 132 OE2 A ? ? 1_555 C NA  . NA  A ? A GLU 132 A NA  302 1_555 ? ? ? ? ? ? ? 2.390 ? ? 
# 
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 OD1 A A ASP 68  ? A ASP 68  ? 1_555 NA A C NA . ? A NA 302 ? 1_555 OD2 A A ASP 68  ? A ASP 68  ? 1_555 42.8  ? 
2 OD1 A A ASP 68  ? A ASP 68  ? 1_555 NA A C NA . ? A NA 302 ? 1_555 O   A A GLU 132 ? A GLU 132 ? 1_555 156.1 ? 
3 OD2 A A ASP 68  ? A ASP 68  ? 1_555 NA A C NA . ? A NA 302 ? 1_555 O   A A GLU 132 ? A GLU 132 ? 1_555 157.7 ? 
4 OD1 A A ASP 68  ? A ASP 68  ? 1_555 NA A C NA . ? A NA 302 ? 1_555 OE2 A A GLU 132 ? A GLU 132 ? 1_555 93.5  ? 
5 OD2 A A ASP 68  ? A ASP 68  ? 1_555 NA A C NA . ? A NA 302 ? 1_555 OE2 A A GLU 132 ? A GLU 132 ? 1_555 108.6 ? 
6 O   A A GLU 132 ? A GLU 132 ? 1_555 NA A C NA . ? A NA 302 ? 1_555 OE2 A A GLU 132 ? A GLU 132 ? 1_555 86.2  ? 
# 
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 B . A LYS A 204 A RET A 301 ? 1_555 LYS A 204 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like             
3 RET B . B LYS A 204 B RET A 301 ? 1_555 LYS A 204 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like             
4 RET B . C LYS A 204 C RET A 301 ? 1_555 LYS A 204 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like             
# 
_pdbx_entry_details.entry_id                   9IN8 
_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 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 64  ? B -158.16 57.50  
2 1 LYS A 134 ? A 72.32   30.75  
3 1 LYS A 204 ? A -99.31  -62.41 
# 
_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 GOL 314 ? O GOL . 
2 1 A HOH 449 ? W HOH . 
3 1 A HOH 545 ? W 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         
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 2.21786507612  24.791950603  -2.49818443832  0.150969197147 ? -0.0486407814408 ? -0.00706140989967 
? 0.196584940025 ? 0.00263409896001  ? 0.212610620933 ? 0.600499134498   ? -0.0666393484853 ? 0.014936974768   ? 1.16410049826   ? 
0.510568541073  ? 0.202807755649  ? 0.0517942547722 ? 0.0586582880188  ? 0.0526808967467  ? -0.0779546764366 ? 0.0186077396007  ? 
-0.104626214174 ? -0.266198922355 ? 0.159091256146  ? -0.000245312213189 ? 
2 'X-RAY DIFFRACTION' ? refined 2.54097927887  16.5486288429 -22.8071621235  0.54715339095  ? 0.00524623266001 ? -0.042360378119   
? 0.529869988302 ? 0.0958405201398   ? 0.275244848008 ? 0.00824067966579 ? -0.0163201565455 ? -0.0162551947656 ? 0.0652321980036 ? 
0.0182577069605 ? 0.0144535500604 ? 0.033649942188  ? 0.261347508233   ? -0.0850746315213 ? -0.181488941836  ? -0.0643361433796 ? 
0.15114132102   ? 0.0621611396443 ? 0.121075442141  ? 0.00337143728735   ? 
3 'X-RAY DIFFRACTION' ? refined -10.0670455066 10.3980029332 0.0542884960051 0.128078017431 ? 0.00893636591097 ? -0.0200348242229  
? 0.127026205694 ? -0.00995136573675 ? 0.153246019225 ? 0.759640430885   ? -0.202198898323  ? -0.250710899616  ? 0.996561096699  ? 
-0.020079899595 ? 1.07926701366   ? 0.0071918075929 ? 0.0157114855692  ? -0.0148547734674 ? -0.0357982113306 ? -0.0149095968914 ? 
0.100982762892  ? 0.116903450766  ? -0.108837528595 ? 7.37019274074e-05  ? 
4 'X-RAY DIFFRACTION' ? refined -5.83350151228 25.6335219376 2.77481975722   0.191793834184 ? -0.0103561908242 ? -0.0130226911412  
? 0.202530488759 ? -0.00643099891193 ? 0.214841209299 ? 0.150629167528   ? -0.265013255964  ? 0.155503891317   ? 0.481227590746  ? 
-0.220334363595 ? 0.116034903329  ? 0.0275605891341 ? -0.0267688590322 ? -0.0166779926525 ? -0.0635713611518 ? 0.0799879601929  ? 
-0.086637069196 ? -0.446079661272 ? 0.132185895344  ? 9.81760485163e-05  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 2   A 2   ? A 63  A 63  ? ? 
;chain 'A' and (resid 2 through 63 )
;
2 'X-RAY DIFFRACTION' 2 A 64  A 64  ? A 69  A 69  ? ? 
;chain 'A' and (resid 64 through 69 )
;
3 'X-RAY DIFFRACTION' 3 A 70  A 70  ? A 188 A 188 ? ? 
;chain 'A' and (resid 70 through 188 )
;
4 'X-RAY DIFFRACTION' 4 A 189 A 189 ? A 224 A 224 ? ? 
;chain 'A' and (resid 189 through 224 )
;
# 
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 
# 
_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                    9IN8 
_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]   0.021539 
_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]   0.008693 
_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]   0.018749 
_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 ? ? 9.38062 1.54875 ? ? 3.38349  72.32734 ? ? 0.0 
;2-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   ? -2.91369  26.32148 -23.45507 1.000 53.63769  ? 1   FME A N   1 
HETATM 2    C  CN  . FME A 1 1   ? -4.14164  26.26594 -22.84132 1.000 51.32943  ? 1   FME A CN  1 
HETATM 3    O  O1  . FME A 1 1   ? -4.26957  26.23895 -21.61131 1.000 43.07732  ? 1   FME A O1  1 
HETATM 4    C  CA  . FME A 1 1   ? -1.64694  26.34163 -22.77503 1.000 56.05106  ? 1   FME A CA  1 
HETATM 5    C  CB  . FME A 1 1   ? -0.45052  26.42362 -23.74132 1.000 63.12220  ? 1   FME A CB  1 
HETATM 6    C  CG  . FME A 1 1   ? -0.38155  25.21786 -24.64762 1.000 90.16471  ? 1   FME A CG  1 
HETATM 7    S  SD  . FME A 1 1   ? -1.35665  23.89424 -23.97166 1.000 134.56293 ? 1   FME A SD  1 
HETATM 8    C  CE  . FME A 1 1   ? -0.12327  22.74832 -23.48448 1.000 58.04528  ? 1   FME A CE  1 
HETATM 9    C  C   . FME A 1 1   ? -1.48750  27.50719 -21.80137 1.000 49.11910  ? 1   FME A C   1 
HETATM 10   O  O   . FME A 1 1   ? -1.04538  27.35215 -20.65329 1.000 36.50910  ? 1   FME A O   1 
ATOM   11   N  N   A ASP A 1 2   ? -1.86392  28.68980 -22.28342 0.700 46.52736  ? 2   ASP A N   1 
ATOM   12   N  N   B ASP A 1 2   ? -1.85489  28.69540 -22.27395 0.300 46.78245  ? 2   ASP A N   1 
ATOM   13   C  CA  A ASP A 1 2   ? -1.82371  29.91585 -21.49396 0.700 47.43335  ? 2   ASP A CA  1 
ATOM   14   C  CA  B ASP A 1 2   ? -1.73220  29.91782 -21.48337 0.300 47.32062  ? 2   ASP A CA  1 
ATOM   15   C  C   A ASP A 1 2   ? -2.70026  29.82468 -20.23998 0.700 38.90715  ? 2   ASP A C   1 
ATOM   16   C  C   B ASP A 1 2   ? -2.55272  29.87355 -20.19511 0.300 38.35943  ? 2   ASP A C   1 
ATOM   17   O  O   A ASP A 1 2   ? -2.30284  30.29830 -19.18186 0.700 30.92264  ? 2   ASP A O   1 
ATOM   18   O  O   B ASP A 1 2   ? -2.08864  30.32017 -19.15002 0.300 31.27838  ? 2   ASP A O   1 
ATOM   19   C  CB  A ASP A 1 2   ? -2.23131  31.13095 -22.34392 0.700 47.71190  ? 2   ASP A CB  1 
ATOM   20   C  CB  B ASP A 1 2   ? -2.11601  31.14959 -22.31230 0.300 48.27177  ? 2   ASP A CB  1 
ATOM   21   C  CG  A ASP A 1 2   ? -1.05604  31.74972 -23.09937 0.700 67.83425  ? 2   ASP A CG  1 
ATOM   22   C  CG  B ASP A 1 2   ? -1.01205  31.58541 -23.26053 0.300 66.61967  ? 2   ASP A CG  1 
ATOM   23   O  OD1 A ASP A 1 2   ? 0.10299   31.35029 -22.84871 0.700 70.41690  ? 2   ASP A OD1 1 
ATOM   24   O  OD1 B ASP A 1 2   ? 0.14077   31.13589 -23.08356 0.300 68.95705  ? 2   ASP A OD1 1 
ATOM   25   O  OD2 A ASP A 1 2   ? -1.29352  32.64175 -23.94593 0.700 70.95743  ? 2   ASP A OD2 1 
ATOM   26   O  OD2 B ASP A 1 2   ? -1.29506  32.38734 -24.17691 0.300 70.30100  ? 2   ASP A OD2 1 
ATOM   27   N  N   A ASN A 1 3   ? -3.88708  29.21265 -20.34966 0.700 31.73066  ? 3   ASN A N   1 
ATOM   28   N  N   B ASN A 1 3   ? -3.77300  29.33505 -20.26989 0.300 33.44196  ? 3   ASN A N   1 
ATOM   29   C  CA  A ASN A 1 3   ? -4.76838  29.12648 -19.18545 0.700 35.10189  ? 3   ASN A CA  1 
ATOM   30   C  CA  B ASN A 1 3   ? -4.60306  29.24413 -19.07299 0.300 33.19416  ? 3   ASN A CA  1 
ATOM   31   C  C   A ASN A 1 3   ? -4.30795  28.07587 -18.17840 0.700 28.53796  ? 3   ASN A C   1 
ATOM   32   C  C   B ASN A 1 3   ? -4.12314  28.15718 -18.11951 0.300 29.46366  ? 3   ASN A C   1 
ATOM   33   O  O   A ASN A 1 3   ? -4.47498  28.27420 -16.97147 0.700 25.94247  ? 3   ASN A O   1 
ATOM   34   O  O   B ASN A 1 3   ? -4.28692  28.29463 -16.90375 0.300 26.53320  ? 3   ASN A O   1 
ATOM   35   C  CB  A ASN A 1 3   ? -6.21381  28.85998 -19.60717 0.700 37.84679  ? 3   ASN A CB  1 
ATOM   36   C  CB  B ASN A 1 3   ? -6.07096  29.02771 -19.44679 0.300 38.54148  ? 3   ASN A CB  1 
ATOM   37   C  CG  A ASN A 1 3   ? -6.88680  30.08185 -20.19229 0.700 46.72747  ? 3   ASN A CG  1 
ATOM   38   C  CG  B ASN A 1 3   ? -6.68855  30.24535 -20.10358 0.300 45.92456  ? 3   ASN A CG  1 
ATOM   39   O  OD1 A ASN A 1 3   ? -6.55754  31.21492 -19.84186 0.700 44.29123  ? 3   ASN A OD1 1 
ATOM   40   O  OD1 B ASN A 1 3   ? -6.22466  31.36862 -19.91078 0.300 44.41211  ? 3   ASN A OD1 1 
ATOM   41   N  ND2 A ASN A 1 3   ? -7.83951  29.85560 -21.08867 0.700 49.60686  ? 3   ASN A ND2 1 
ATOM   42   N  ND2 B ASN A 1 3   ? -7.74252  30.02843 -20.88229 0.300 48.22516  ? 3   ASN A ND2 1 
ATOM   43   N  N   A ILE A 1 4   ? -3.75646  26.94392 -18.63654 0.700 29.60696  ? 4   ILE A N   1 
ATOM   44   N  N   B ILE A 1 4   ? -3.53684  27.07654 -18.63997 0.300 29.02749  ? 4   ILE A N   1 
ATOM   45   C  CA  A ILE A 1 4   ? -3.14180  26.02260 -17.68314 0.700 24.93349  ? 4   ILE A CA  1 
ATOM   46   C  CA  B ILE A 1 4   ? -2.95140  26.06565 -17.76260 0.300 26.11446  ? 4   ILE A CA  1 
ATOM   47   C  C   A ILE A 1 4   ? -2.02042  26.72696 -16.93903 0.700 21.67103  ? 4   ILE A C   1 
ATOM   48   C  C   B ILE A 1 4   ? -1.81753  26.67201 -16.94910 0.300 22.39612  ? 4   ILE A C   1 
ATOM   49   O  O   A ILE A 1 4   ? -1.87420  26.58525 -15.72012 0.700 24.01953  ? 4   ILE A O   1 
ATOM   50   O  O   B ILE A 1 4   ? -1.71170  26.46012 -15.73530 0.300 22.75826  ? 4   ILE A O   1 
ATOM   51   C  CB  A ILE A 1 4   ? -2.62185  24.74459 -18.36836 0.700 25.72572  ? 4   ILE A CB  1 
ATOM   52   C  CB  B ILE A 1 4   ? -2.46948  24.85087 -18.57483 0.300 23.98414  ? 4   ILE A CB  1 
ATOM   53   C  CG1 A ILE A 1 4   ? -3.69871  24.08761 -19.22321 0.700 35.03776  ? 4   ILE A CG1 1 
ATOM   54   C  CG1 B ILE A 1 4   ? -3.63273  24.20646 -19.32441 0.300 33.68759  ? 4   ILE A CG1 1 
ATOM   55   C  CG2 A ILE A 1 4   ? -2.14994  23.77659 -17.29871 0.700 23.83518  ? 4   ILE A CG2 1 
ATOM   56   C  CG2 B ILE A 1 4   ? -1.83448  23.83421 -17.65185 0.300 27.98299  ? 4   ILE A CG2 1 
ATOM   57   C  CD1 A ILE A 1 4   ? -3.15033  22.92138 -20.05179 0.700 34.35592  ? 4   ILE A CD1 1 
ATOM   58   C  CD1 B ILE A 1 4   ? -3.20224  23.05194 -20.21241 0.300 34.39798  ? 4   ILE A CD1 1 
ATOM   59   N  N   A ILE A 1 5   ? -1.19954  27.47829 -17.66678 0.700 22.63276  ? 5   ILE A N   1 
ATOM   60   N  N   B ILE A 1 5   ? -0.94507  27.42750 -17.61479 0.300 25.71632  ? 5   ILE A N   1 
ATOM   61   C  CA  A ILE A 1 5   ? -0.08117  28.17156 -17.03195 0.700 23.38359  ? 5   ILE A CA  1 
ATOM   62   C  CA  B ILE A 1 5   ? 0.17655   28.05425 -16.92512 0.300 21.77757  ? 5   ILE A CA  1 
ATOM   63   C  C   A ILE A 1 5   ? -0.58956  29.20038 -16.02971 0.700 23.14196  ? 5   ILE A C   1 
ATOM   64   C  C   B ILE A 1 5   ? -0.31031  29.15654 -15.99275 0.300 25.34933  ? 5   ILE A C   1 
ATOM   65   O  O   A ILE A 1 5   ? -0.17423  29.20794 -14.86339 0.700 22.13714  ? 5   ILE A O   1 
ATOM   66   O  O   B ILE A 1 5   ? 0.34852   29.46836 -14.99127 0.300 22.81862  ? 5   ILE A O   1 
ATOM   67   C  CB  A ILE A 1 5   ? 0.85937   28.76409 -18.09821 0.700 27.57106  ? 5   ILE A CB  1 
ATOM   68   C  CB  B ILE A 1 5   ? 1.20401   28.54631 -17.96279 0.300 29.77105  ? 5   ILE A CB  1 
ATOM   69   C  CG1 A ILE A 1 5   ? 1.66183   27.62347 -18.72118 0.700 33.19231  ? 5   ILE A CG1 1 
ATOM   70   C  CG1 B ILE A 1 5   ? 1.64597   27.38547 -18.85489 0.300 33.33478  ? 5   ILE A CG1 1 
ATOM   71   C  CG2 A ILE A 1 5   ? 1.80432   29.78750 -17.49854 0.700 31.07242  ? 5   ILE A CG2 1 
ATOM   72   C  CG2 B ILE A 1 5   ? 2.42428   29.12757 -17.29548 0.300 30.21824  ? 5   ILE A CG2 1 
ATOM   73   C  CD1 A ILE A 1 5   ? 2.48019   28.02948 -19.94146 0.700 46.44172  ? 5   ILE A CD1 1 
ATOM   74   C  CD1 B ILE A 1 5   ? 2.62989   27.79133 -19.95066 0.300 46.03815  ? 5   ILE A CD1 1 
ATOM   75   N  N   A MET A 1 6   ? -1.51370  30.07048 -16.45519 0.700 24.20941  ? 6   MET A N   1 
ATOM   76   N  N   B MET A 1 6   ? -1.47214  29.74996 -16.28369 0.300 24.48396  ? 6   MET A N   1 
ATOM   77   C  CA  A MET A 1 6   ? -1.98152  31.12381 -15.55220 0.700 22.64069  ? 6   MET A CA  1 
ATOM   78   C  CA  B MET A 1 6   ? -2.00469  30.79620 -15.41486 0.300 23.62670  ? 6   MET A CA  1 
ATOM   79   C  C   A MET A 1 6   ? -2.57786  30.54476 -14.27305 0.700 20.69116  ? 6   MET A C   1 
ATOM   80   C  C   B MET A 1 6   ? -2.53978  30.21364 -14.11014 0.300 22.75535  ? 6   MET A C   1 
ATOM   81   O  O   A MET A 1 6   ? -2.29756  31.03748 -13.16840 0.700 20.81076  ? 6   MET A O   1 
ATOM   82   O  O   B MET A 1 6   ? -2.18210  30.68072 -13.02076 0.300 19.19326  ? 6   MET A O   1 
ATOM   83   C  CB  A MET A 1 6   ? -2.99535  32.03598 -16.24992 0.700 24.64211  ? 6   MET A CB  1 
ATOM   84   C  CB  B MET A 1 6   ? -3.07154  31.61948 -16.14661 0.300 29.41682  ? 6   MET A CB  1 
ATOM   85   C  CG  A MET A 1 6   ? -3.71930  32.97054 -15.26683 0.700 33.31091  ? 6   MET A CG  1 
ATOM   86   C  CG  B MET A 1 6   ? -3.66416  32.75289 -15.30364 0.300 33.11947  ? 6   MET A CG  1 
ATOM   87   S  SD  A MET A 1 6   ? -5.04281  33.91961 -16.04040 0.700 46.29588  ? 6   MET A SD  1 
ATOM   88   S  SD  B MET A 1 6   ? -4.67157  33.93584 -16.23527 0.300 39.44925  ? 6   MET A SD  1 
ATOM   89   C  CE  A MET A 1 6   ? -4.17465  34.54378 -17.47363 0.700 37.27352  ? 6   MET A CE  1 
ATOM   90   C  CE  B MET A 1 6   ? -5.29217  34.96205 -14.89874 0.300 28.26904  ? 6   MET A CE  1 
ATOM   91   N  N   A THR A 1 7   ? -3.38687  29.48325 -14.39580 0.700 22.04094  ? 7   THR A N   1 
ATOM   92   N  N   B THR A 1 7   ? -3.39384  29.18556 -14.19417 0.300 22.79026  ? 7   THR A N   1 
ATOM   93   C  CA  A THR A 1 7   ? -3.94008  28.84926 -13.20022 0.700 18.36901  ? 7   THR A CA  1 
ATOM   94   C  CA  B THR A 1 7   ? -3.86555  28.53449 -12.97500 0.300 18.37561  ? 7   THR A CA  1 
ATOM   95   C  C   A THR A 1 7   ? -2.85645  28.21808 -12.34049 0.700 18.56827  ? 7   THR A C   1 
ATOM   96   C  C   B THR A 1 7   ? -2.73341  27.81734 -12.24417 0.300 18.07871  ? 7   THR A C   1 
ATOM   97   O  O   A THR A 1 7   ? -2.98421  28.19335 -11.11165 0.700 18.17578  ? 7   THR A O   1 
ATOM   98   O  O   B THR A 1 7   ? -2.84978  27.55683 -11.03997 0.300 19.07018  ? 7   THR A O   1 
ATOM   99   C  CB  A THR A 1 7   ? -5.01975  27.81797 -13.54933 0.700 18.73093  ? 7   THR A CB  1 
ATOM   100  C  CB  B THR A 1 7   ? -5.01714  27.56921 -13.28430 0.300 19.57916  ? 7   THR A CB  1 
ATOM   101  O  OG1 A THR A 1 7   ? -4.53156  26.87811 -14.51856 0.700 17.96976  ? 7   THR A OG1 1 
ATOM   102  O  OG1 B THR A 1 7   ? -4.50402  26.39516 -13.91132 0.300 18.40285  ? 7   THR A OG1 1 
ATOM   103  C  CG2 A THR A 1 7   ? -6.28976  28.51922 -14.06166 0.700 20.67058  ? 7   THR A CG2 1 
ATOM   104  C  CG2 B THR A 1 7   ? -6.02555  28.20379 -14.23271 0.300 23.51521  ? 7   THR A CG2 1 
ATOM   105  N  N   A ALA A 1 8   ? -1.81083  27.67092 -12.96690 0.700 18.95483  ? 8   ALA A N   1 
ATOM   106  N  N   B ALA A 1 8   ? -1.64632  27.49358 -12.95233 0.300 20.02165  ? 8   ALA A N   1 
ATOM   107  C  CA  A ALA A 1 8   ? -0.68924  27.15117 -12.18430 0.700 18.74897  ? 8   ALA A CA  1 
ATOM   108  C  CA  B ALA A 1 8   ? -0.46855  26.92803 -12.29864 0.300 20.00206  ? 8   ALA A CA  1 
ATOM   109  C  C   A ALA A 1 8   ? 0.00708   28.26912 -11.43470 0.700 18.78545  ? 8   ALA A C   1 
ATOM   110  C  C   B ALA A 1 8   ? 0.18535   27.94272 -11.37858 0.300 17.73095  ? 8   ALA A C   1 
ATOM   111  O  O   A ALA A 1 8   ? 0.35952   28.10414 -10.26616 0.700 17.52858  ? 8   ALA A O   1 
ATOM   112  O  O   B ALA A 1 8   ? 0.54373   27.61467 -10.24536 0.300 19.07763  ? 8   ALA A O   1 
ATOM   113  C  CB  A ALA A 1 8   ? 0.28636   26.36203 -13.06207 0.700 18.28063  ? 8   ALA A CB  1 
ATOM   114  C  CB  B ALA A 1 8   ? 0.53287   26.44143 -13.34587 0.300 21.18422  ? 8   ALA A CB  1 
ATOM   115  N  N   A TYR A 1 9   ? 0.18801   29.42837 -12.07813 0.700 20.58331  ? 9   TYR A N   1 
ATOM   116  N  N   B TYR A 1 9   ? 0.35235   29.18078 -11.85288 0.300 18.85000  ? 9   TYR A N   1 
ATOM   117  C  CA  A TYR A 1 9   ? 0.76981   30.57625 -11.38663 0.700 22.86189  ? 9   TYR A CA  1 
ATOM   118  C  CA  B TYR A 1 9   ? 0.91127   30.23612 -11.01700 0.300 18.69621  ? 9   TYR A CA  1 
ATOM   119  C  C   A TYR A 1 9   ? -0.08751  31.01752 -10.20909 0.700 20.38527  ? 9   TYR A C   1 
ATOM   120  C  C   B TYR A 1 9   ? -0.04686  30.62095 -9.89625  0.300 18.21473  ? 9   TYR A C   1 
ATOM   121  O  O   A TYR A 1 9   ? 0.44440   31.34056 -9.14266  0.700 18.34196  ? 9   TYR A O   1 
ATOM   122  O  O   B TYR A 1 9   ? 0.39136   30.92615 -8.78275  0.300 19.01030  ? 9   TYR A O   1 
ATOM   123  C  CB  A TYR A 1 9   ? 0.97282   31.73581 -12.35903 0.700 19.96474  ? 9   TYR A CB  1 
ATOM   124  C  CB  B TYR A 1 9   ? 1.26379   31.45318 -11.88046 0.300 19.68465  ? 9   TYR A CB  1 
ATOM   125  C  CG  A TYR A 1 9   ? 2.14384   31.58805 -13.29795 0.700 22.25221  ? 9   TYR A CG  1 
ATOM   126  C  CG  B TYR A 1 9   ? 2.46326   31.24944 -12.78757 0.300 20.29887  ? 9   TYR A CG  1 
ATOM   127  C  CD1 A TYR A 1 9   ? 3.22044   30.76202 -12.99195 0.700 22.89104  ? 9   TYR A CD1 1 
ATOM   128  C  CD1 B TYR A 1 9   ? 3.68874   30.85284 -12.26783 0.300 20.20942  ? 9   TYR A CD1 1 
ATOM   129  C  CD2 A TYR A 1 9   ? 2.18334   32.30717 -14.48091 0.700 24.04923  ? 9   TYR A CD2 1 
ATOM   130  C  CD2 B TYR A 1 9   ? 2.37344   31.45756 -14.16347 0.300 21.04717  ? 9   TYR A CD2 1 
ATOM   131  C  CE1 A TYR A 1 9   ? 4.31002   30.64687 -13.87043 0.700 26.21369  ? 9   TYR A CE1 1 
ATOM   132  C  CE1 B TYR A 1 9   ? 4.79005   30.65892 -13.08607 0.300 28.12732  ? 9   TYR A CE1 1 
ATOM   133  C  CE2 A TYR A 1 9   ? 3.26449   32.20876 -15.35857 0.700 26.64919  ? 9   TYR A CE2 1 
ATOM   134  C  CE2 B TYR A 1 9   ? 3.48001   31.27322 -14.98736 0.300 28.33643  ? 9   TYR A CE2 1 
ATOM   135  C  CZ  A TYR A 1 9   ? 4.31810   31.37889 -15.04770 0.700 25.89742  ? 9   TYR A CZ  1 
ATOM   136  C  CZ  B TYR A 1 9   ? 4.68494   30.87091 -14.44205 0.300 23.77910  ? 9   TYR A CZ  1 
ATOM   137  O  OH  A TYR A 1 9   ? 5.38385   31.26580 -15.91654 0.700 29.78535  ? 9   TYR A OH  1 
ATOM   138  O  OH  B TYR A 1 9   ? 5.78892   30.67657 -15.25231 0.300 31.85112  ? 9   TYR A OH  1 
ATOM   139  N  N   A ILE A 1 10  ? -1.41519  31.06611 -10.38820 0.700 18.82271  ? 10  ILE A N   1 
ATOM   140  N  N   B ILE A 1 10  ? -1.35869  30.59568 -10.16174 0.300 18.06192  ? 10  ILE A N   1 
ATOM   141  C  CA  A ILE A 1 10  ? -2.28943  31.37739 -9.26318  0.700 18.96436  ? 10  ILE A CA  1 
ATOM   142  C  CA  B ILE A 1 10  ? -2.32339  31.03824 -9.15342  0.300 19.74698  ? 10  ILE A CA  1 
ATOM   143  C  C   A ILE A 1 10  ? -2.08740  30.35471 -8.15056  0.700 19.88639  ? 10  ILE A C   1 
ATOM   144  C  C   B ILE A 1 10  ? -2.25287  30.14684 -7.91718  0.300 19.84558  ? 10  ILE A C   1 
ATOM   145  O  O   A ILE A 1 10  ? -1.93135  30.71755 -6.97214  0.700 19.34987  ? 10  ILE A O   1 
ATOM   146  O  O   B ILE A 1 10  ? -2.24314  30.63008 -6.77580  0.300 19.40777  ? 10  ILE A O   1 
ATOM   147  C  CB  A ILE A 1 10  ? -3.76386  31.45797 -9.71084  0.700 21.63515  ? 10  ILE A CB  1 
ATOM   148  C  CB  B ILE A 1 10  ? -3.74265  31.12177 -9.74766  0.300 21.71208  ? 10  ILE A CB  1 
ATOM   149  C  CG1 A ILE A 1 10  ? -3.99117  32.61630 -10.69308 0.700 20.32801  ? 10  ILE A CG1 1 
ATOM   150  C  CG1 B ILE A 1 10  ? -3.81078  32.22799 -10.80739 0.300 21.85206  ? 10  ILE A CG1 1 
ATOM   151  C  CG2 A ILE A 1 10  ? -4.67340  31.57629 -8.49389  0.700 21.15902  ? 10  ILE A CG2 1 
ATOM   152  C  CG2 B ILE A 1 10  ? -4.76233  31.39641 -8.65431  0.300 21.42630  ? 10  ILE A CG2 1 
ATOM   153  C  CD1 A ILE A 1 10  ? -5.39043  32.57258 -11.34549 0.700 26.57122  ? 10  ILE A CD1 1 
ATOM   154  C  CD1 B ILE A 1 10  ? -5.16570  32.33980 -11.49862 0.300 27.57619  ? 10  ILE A CD1 1 
ATOM   155  N  N   A SER A 1 11  ? -2.04924  29.06150 -8.51358  0.700 17.94461  ? 11  SER A N   1 
ATOM   156  N  N   B SER A 1 11  ? -2.17689  28.83249 -8.12596  0.300 19.54548  ? 11  SER A N   1 
ATOM   157  C  CA  A SER A 1 11  ? -1.91252  28.00618 -7.50782  0.700 17.52286  ? 11  SER A CA  1 
ATOM   158  C  CA  B SER A 1 11  ? -1.92627  27.92505 -7.01214  0.300 15.86049  ? 11  SER A CA  1 
ATOM   159  C  C   A SER A 1 11  ? -0.56929  28.10218 -6.79096  0.700 17.61256  ? 11  SER A C   1 
ATOM   160  C  C   B SER A 1 11  ? -0.59282  28.23754 -6.34893  0.300 20.93852  ? 11  SER A C   1 
ATOM   161  O  O   A SER A 1 11  ? -0.49029  27.89861 -5.57092  0.700 18.53322  ? 11  SER A O   1 
ATOM   162  O  O   B SER A 1 11  ? -0.52216  28.41390 -5.12868  0.300 17.70964  ? 11  SER A O   1 
ATOM   163  C  CB  A SER A 1 11  ? -2.13709  26.61853 -8.12714  0.700 15.67688  ? 11  SER A CB  1 
ATOM   164  C  CB  B SER A 1 11  ? -1.94005  26.48688 -7.51801  0.300 21.96722  ? 11  SER A CB  1 
ATOM   165  O  OG  A SER A 1 11  ? -2.08410  25.57596 -7.13700  0.700 16.65352  ? 11  SER A OG  1 
ATOM   166  O  OG  B SER A 1 11  ? -1.46305  26.43049 -8.85018  0.300 23.08792  ? 11  SER A OG  1 
ATOM   167  N  N   A ILE A 1 12  ? 0.49323   28.41897 -7.53219  0.700 17.84028  ? 12  ILE A N   1 
ATOM   168  N  N   B ILE A 1 12  ? 0.47838   28.29626 -7.14488  0.300 18.70750  ? 12  ILE A N   1 
ATOM   169  C  CA  A ILE A 1 12  ? 1.80605   28.60780 -6.91452  0.700 22.85885  ? 12  ILE A CA  1 
ATOM   170  C  CA  B ILE A 1 12  ? 1.82208   28.53410 -6.61691  0.300 21.40020  ? 12  ILE A CA  1 
ATOM   171  C  C   A ILE A 1 12  ? 1.76183   29.75566 -5.90812  0.700 20.36674  ? 12  ILE A C   1 
ATOM   172  C  C   B ILE A 1 12  ? 1.89990   29.86540 -5.87409  0.300 20.83361  ? 12  ILE A C   1 
ATOM   173  O  O   A ILE A 1 12  ? 2.27465   29.64335 -4.78624  0.700 21.30167  ? 12  ILE A O   1 
ATOM   174  O  O   B ILE A 1 12  ? 2.66221   30.00324 -4.90693  0.300 20.43077  ? 12  ILE A O   1 
ATOM   175  C  CB  A ILE A 1 12  ? 2.86734   28.82060 -8.01128  0.700 21.54813  ? 12  ILE A CB  1 
ATOM   176  C  CB  B ILE A 1 12  ? 2.87418   28.42130 -7.74169  0.300 18.67404  ? 12  ILE A CB  1 
ATOM   177  C  CG1 A ILE A 1 12  ? 3.15807   27.48830 -8.70996  0.700 19.01470  ? 12  ILE A CG1 1 
ATOM   178  C  CG1 B ILE A 1 12  ? 2.88299   27.01844 -8.34188  0.300 16.91877  ? 12  ILE A CG1 1 
ATOM   179  C  CG2 A ILE A 1 12  ? 4.12073   29.49019 -7.44504  0.700 26.74925  ? 12  ILE A CG2 1 
ATOM   180  C  CG2 B ILE A 1 12  ? 4.26490   28.76381 -7.22837  0.300 25.98494  ? 12  ILE A CG2 1 
ATOM   181  C  CD1 A ILE A 1 12  ? 3.91226   27.63080 -10.01875 0.700 23.47445  ? 12  ILE A CD1 1 
ATOM   182  C  CD1 B ILE A 1 12  ? 3.68313   26.93108 -9.62684  0.300 23.78525  ? 12  ILE A CD1 1 
ATOM   183  N  N   . PHE A 1 13  ? 1.12614   30.86921 -6.29555  1.000 20.29666  ? 13  PHE A N   1 
ATOM   184  C  CA  . PHE A 1 13  ? 1.05336   32.07463 -5.47389  1.000 21.14295  ? 13  PHE A CA  1 
ATOM   185  C  C   . PHE A 1 13  ? 0.45915   31.73197 -4.11452  1.000 20.61768  ? 13  PHE A C   1 
ATOM   186  O  O   . PHE A 1 13  ? 1.05098   32.02848 -3.05943  1.000 22.41718  ? 13  PHE A O   1 
ATOM   187  C  CB  . PHE A 1 13  ? 0.19325   33.09841 -6.21714  1.000 20.19387  ? 13  PHE A CB  1 
ATOM   188  C  CG  . PHE A 1 13  ? 0.05728   34.42317 -5.51539  1.000 24.49683  ? 13  PHE A CG  1 
ATOM   189  C  CD1 . PHE A 1 13  ? 0.88965   35.48161 -5.84214  1.000 29.60621  ? 13  PHE A CD1 1 
ATOM   190  C  CD2 . PHE A 1 13  ? -0.92389  34.62202 -4.55766  1.000 25.12132  ? 13  PHE A CD2 1 
ATOM   191  C  CE1 . PHE A 1 13  ? 0.76042   36.73581 -5.20975  1.000 28.96268  ? 13  PHE A CE1 1 
ATOM   192  C  CE2 . PHE A 1 13  ? -1.04769  35.86804 -3.91248  1.000 28.79155  ? 13  PHE A CE2 1 
ATOM   193  C  CZ  . PHE A 1 13  ? -0.19933  36.91550 -4.24266  1.000 31.47530  ? 13  PHE A CZ  1 
ATOM   194  N  N   A VAL A 1 14  ? -0.67261  31.02954 -4.11595  0.500 19.69908  ? 14  VAL A N   1 
ATOM   195  N  N   B VAL A 1 14  ? -0.71596  31.10932 -4.11362  0.500 19.67632  ? 14  VAL A N   1 
ATOM   196  C  CA  A VAL A 1 14  ? -1.33047  30.66049 -2.86585  0.500 22.18762  ? 14  VAL A CA  1 
ATOM   197  C  CA  B VAL A 1 14  ? -1.31382  30.67067 -2.85883  0.500 22.22770  ? 14  VAL A CA  1 
ATOM   198  C  C   A VAL A 1 14  ? -0.51545  29.62811 -2.08701  0.500 19.70214  ? 14  VAL A C   1 
ATOM   199  C  C   B VAL A 1 14  ? -0.35691  29.76813 -2.08979  0.500 19.58720  ? 14  VAL A C   1 
ATOM   200  O  O   A VAL A 1 14  ? -0.58651  29.57550 -0.85044  0.500 19.59925  ? 14  VAL A O   1 
ATOM   201  O  O   B VAL A 1 14  ? -0.16628  29.94429 -0.87985  0.500 17.54602  ? 14  VAL A O   1 
ATOM   202  C  CB  A VAL A 1 14  ? -2.77328  30.20938 -3.13325  0.500 23.14330  ? 14  VAL A CB  1 
ATOM   203  C  CB  B VAL A 1 14  ? -2.67492  30.00432 -3.09598  0.500 18.75896  ? 14  VAL A CB  1 
ATOM   204  C  CG1 A VAL A 1 14  ? -3.54520  30.06538 -1.81580  0.500 18.78697  ? 14  VAL A CG1 1 
ATOM   205  C  CG1 B VAL A 1 14  ? -3.19548  29.45661 -1.78898  0.500 18.92437  ? 14  VAL A CG1 1 
ATOM   206  C  CG2 A VAL A 1 14  ? -3.45794  31.21834 -4.06739  0.500 18.24874  ? 14  VAL A CG2 1 
ATOM   207  C  CG2 B VAL A 1 14  ? -3.65035  31.03563 -3.67040  0.500 17.43806  ? 14  VAL A CG2 1 
ATOM   208  N  N   . GLN A 1 15  ? 0.28015   28.81117 -2.77936  1.000 19.11561  ? 15  GLN A N   1 
ATOM   209  C  CA  . GLN A 1 15  ? 1.13622   27.84448 -2.08737  1.000 22.06254  ? 15  GLN A CA  1 
ATOM   210  C  C   . GLN A 1 15  ? 2.24147   28.54861 -1.30855  1.000 21.46972  ? 15  GLN A C   1 
ATOM   211  O  O   . GLN A 1 15  ? 2.52018   28.19555 -0.14983  1.000 21.67205  ? 15  GLN A O   1 
ATOM   212  C  CB  . GLN A 1 15  ? 1.75554   26.85973 -3.08309  1.000 21.01366  ? 15  GLN A CB  1 
ATOM   213  C  CG  . GLN A 1 15  ? 0.75953   25.83046 -3.64402  1.000 22.35732  ? 15  GLN A CG  1 
ATOM   214  C  CD  . GLN A 1 15  ? 1.38726   25.03671 -4.74519  1.000 24.72316  ? 15  GLN A CD  1 
ATOM   215  O  OE1 . GLN A 1 15  ? 2.47914   24.48540 -4.57692  1.000 24.00338  ? 15  GLN A OE1 1 
ATOM   216  N  NE2 . GLN A 1 15  ? 0.73666   25.00744 -5.90627  1.000 21.30714  ? 15  GLN A NE2 1 
ATOM   217  N  N   A ILE A 1 16  ? 2.90227   29.52131 -1.93995  0.700 21.15345  ? 16  ILE A N   1 
ATOM   218  N  N   B ILE A 1 16  ? 2.87143   29.55283 -1.91684  0.300 21.86988  ? 16  ILE A N   1 
ATOM   219  C  CA  A ILE A 1 16  ? 4.03301   30.20407 -1.31306  0.700 20.80225  ? 16  ILE A CA  1 
ATOM   220  C  CA  B ILE A 1 16  ? 3.90731   30.31868 -1.22693  0.300 21.52444  ? 16  ILE A CA  1 
ATOM   221  C  C   A ILE A 1 16  ? 3.57579   30.99126 -0.09419  0.700 18.72314  ? 16  ILE A C   1 
ATOM   222  C  C   B ILE A 1 16  ? 3.38161   30.86343 0.09390   0.300 22.83067  ? 16  ILE A C   1 
ATOM   223  O  O   A ILE A 1 16  ? 4.20068   30.93393 0.97320   0.700 25.79937  ? 16  ILE A O   1 
ATOM   224  O  O   B ILE A 1 16  ? 3.95801   30.62721 1.16278   0.300 23.37096  ? 16  ILE A O   1 
ATOM   225  C  CB  A ILE A 1 16  ? 4.73931   31.09983 -2.34380  0.700 24.40261  ? 16  ILE A CB  1 
ATOM   226  C  CB  B ILE A 1 16  ? 4.42116   31.44346 -2.14046  0.300 25.35571  ? 16  ILE A CB  1 
ATOM   227  C  CG1 A ILE A 1 16  ? 5.44114   30.24113 -3.38973  0.700 27.87019  ? 16  ILE A CG1 1 
ATOM   228  C  CG1 B ILE A 1 16  ? 5.39471   30.87673 -3.17313  0.300 25.32878  ? 16  ILE A CG1 1 
ATOM   229  C  CG2 A ILE A 1 16  ? 5.69594   32.04715 -1.63844  0.700 25.76256  ? 16  ILE A CG2 1 
ATOM   230  C  CG2 B ILE A 1 16  ? 5.04666   32.54464 -1.30889  0.300 18.98075  ? 16  ILE A CG2 1 
ATOM   231  C  CD1 A ILE A 1 16  ? 5.94246   31.06303 -4.57609  0.700 34.26424  ? 16  ILE A CD1 1 
ATOM   232  C  CD1 B ILE A 1 16  ? 5.61829   31.78880 -4.36379  0.300 26.15166  ? 16  ILE A CD1 1 
ATOM   233  N  N   A ILE A 1 17  ? 2.47542   31.74118 -0.22587  0.700 22.87181  ? 17  ILE A N   1 
ATOM   234  N  N   B ILE A 1 17  ? 2.25903   31.58250 0.04195   0.300 24.22896  ? 17  ILE A N   1 
ATOM   235  C  CA  A ILE A 1 17  ? 1.94468   32.47761 0.92268   0.700 27.73653  ? 17  ILE A CA  1 
ATOM   236  C  CA  B ILE A 1 17  ? 1.79775   32.29933 1.22580   0.300 24.73889  ? 17  ILE A CA  1 
ATOM   237  C  C   A ILE A 1 17  ? 1.56329   31.51625 2.05256   0.700 23.97063  ? 17  ILE A C   1 
ATOM   238  C  C   B ILE A 1 17  ? 1.23618   31.33888 2.26892   0.300 24.57865  ? 17  ILE A C   1 
ATOM   239  O  O   A ILE A 1 17  ? 1.96212   31.70267 3.21090   0.700 23.51221  ? 17  ILE A O   1 
ATOM   240  O  O   B ILE A 1 17  ? 1.29915   31.60894 3.47510   0.300 17.88394  ? 17  ILE A O   1 
ATOM   241  C  CB  A ILE A 1 17  ? 0.77414   33.38641 0.49317   0.700 24.93176  ? 17  ILE A CB  1 
ATOM   242  C  CB  B ILE A 1 17  ? 0.82024   33.41802 0.81839   0.300 29.86231  ? 17  ILE A CB  1 
ATOM   243  C  CG1 A ILE A 1 17  ? 1.20161   34.33870 -0.63520  0.700 33.37067  ? 17  ILE A CG1 1 
ATOM   244  C  CG1 B ILE A 1 17  ? -0.56013  32.85137 0.50189   0.300 23.34080  ? 17  ILE A CG1 1 
ATOM   245  C  CG2 A ILE A 1 17  ? 0.22638   34.16509 1.70370   0.700 28.49510  ? 17  ILE A CG2 1 
ATOM   246  C  CG2 B ILE A 1 17  ? 1.35263   34.16225 -0.39535  0.300 32.22758  ? 17  ILE A CG2 1 
ATOM   247  C  CD1 A ILE A 1 17  ? 2.54369   35.05263 -0.39289  0.700 36.09958  ? 17  ILE A CD1 1 
ATOM   248  C  CD1 B ILE A 1 17  ? -1.60021  33.22079 1.53833   0.300 31.13386  ? 17  ILE A CD1 1 
ATOM   249  N  N   A THR A 1 18  ? 0.81636   30.45482 1.72181   0.700 20.14263  ? 18  THR A N   1 
ATOM   250  N  N   B THR A 1 18  ? 0.70807   30.19596 1.83805   0.300 20.76915  ? 18  THR A N   1 
ATOM   251  C  CA  A THR A 1 18  ? 0.37425   29.45946 2.70443   0.700 20.38112  ? 18  THR A CA  1 
ATOM   252  C  CA  B THR A 1 18  ? 0.26234   29.19299 2.79448   0.300 20.49224  ? 18  THR A CA  1 
ATOM   253  C  C   A THR A 1 18  ? 1.55349   28.83674 3.44634   0.700 19.31332  ? 18  THR A C   1 
ATOM   254  C  C   B THR A 1 18  ? 1.44559   28.45304 3.39865   0.300 21.82583  ? 18  THR A C   1 
ATOM   255  O  O   A THR A 1 18  ? 1.51492   28.65893 4.67144   0.700 21.28539  ? 18  THR A O   1 
ATOM   256  O  O   B THR A 1 18  ? 1.33587   27.89405 4.50053   0.300 21.89028  ? 18  THR A O   1 
ATOM   257  C  CB  A THR A 1 18  ? -0.42302  28.35596 1.98523   0.700 24.81255  ? 18  THR A CB  1 
ATOM   258  C  CB  B THR A 1 18  ? -0.67734  28.21431 2.10021   0.300 24.55204  ? 18  THR A CB  1 
ATOM   259  O  OG1 A THR A 1 18  ? -1.61695  28.90725 1.41879   0.700 24.40846  ? 18  THR A OG1 1 
ATOM   260  O  OG1 B THR A 1 18  ? -0.00310  27.63707 0.98362   0.300 24.30954  ? 18  THR A OG1 1 
ATOM   261  C  CG2 A THR A 1 18  ? -0.81026  27.21242 2.94552   0.700 22.39481  ? 18  THR A CG2 1 
ATOM   262  C  CG2 B THR A 1 18  ? -1.90053  28.94449 1.59857   0.300 22.89021  ? 18  THR A CG2 1 
ATOM   263  N  N   . ALA A 1 19  ? 2.58899   28.44484 2.71145   1.000 22.13637  ? 19  ALA A N   1 
ATOM   264  C  CA  . ALA A 1 19  ? 3.75908   27.83064 3.32512   1.000 20.18967  ? 19  ALA A CA  1 
ATOM   265  C  C   . ALA A 1 19  ? 4.38583   28.76861 4.35681   1.000 24.19687  ? 19  ALA A C   1 
ATOM   266  O  O   . ALA A 1 19  ? 4.74324   28.33243 5.46002   1.000 23.31461  ? 19  ALA A O   1 
ATOM   267  C  CB  . ALA A 1 19  ? 4.77779   27.47041 2.26175   1.000 21.34691  ? 19  ALA A CB  1 
ATOM   268  N  N   . ILE A 1 20  ? 4.51937   30.05727 4.02169   1.000 21.85530  ? 20  ILE A N   1 
ATOM   269  C  CA  . ILE A 1 20  ? 5.08417   31.02899 4.97408   1.000 22.30761  ? 20  ILE A CA  1 
ATOM   270  C  C   . ILE A 1 20  ? 4.25071   31.05345 6.24940   1.000 25.55092  ? 20  ILE A C   1 
ATOM   271  O  O   . ILE A 1 20  ? 4.77802   30.97232 7.36817   1.000 24.13998  ? 20  ILE A O   1 
ATOM   272  C  CB  . ILE A 1 20  ? 5.16166   32.41911 4.32149   1.000 21.64037  ? 20  ILE A CB  1 
ATOM   273  C  CG1 . ILE A 1 20  ? 6.20602   32.39046 3.20838   1.000 24.20593  ? 20  ILE A CG1 1 
ATOM   274  C  CG2 . ILE A 1 20  ? 5.43455   33.54992 5.38659   1.000 23.70954  ? 20  ILE A CG2 1 
ATOM   275  C  CD1 . ILE A 1 20  ? 6.10825   33.56182 2.25591   1.000 31.68599  ? 20  ILE A CD1 1 
ATOM   276  N  N   . ILE A 1 21  ? 2.93561   31.16816 6.09270   1.000 23.03462  ? 21  ILE A N   1 
ATOM   277  C  CA  . ILE A 1 21  ? 2.01475   31.14891 7.22809   1.000 27.28625  ? 21  ILE A CA  1 
ATOM   278  C  C   . ILE A 1 21  ? 2.18168   29.87287 8.05015   1.000 25.90568  ? 21  ILE A C   1 
ATOM   279  O  O   . ILE A 1 21  ? 2.24068   29.90851 9.28834   1.000 24.55363  ? 21  ILE A O   1 
ATOM   280  C  CB  . ILE A 1 21  ? 0.57590   31.27474 6.70113   1.000 26.40601  ? 21  ILE A CB  1 
ATOM   281  C  CG1 . ILE A 1 21  ? 0.31410   32.69499 6.21563   1.000 28.82068  ? 21  ILE A CG1 1 
ATOM   282  C  CG2 . ILE A 1 21  ? -0.41795  30.89833 7.76126   1.000 36.55971  ? 21  ILE A CG2 1 
ATOM   283  C  CD1 . ILE A 1 21  ? -0.96227  32.79160 5.38968   1.000 34.85729  ? 21  ILE A CD1 1 
ATOM   284  N  N   . SER A 1 22  ? 2.25286   28.72808 7.37627   1.000 24.62765  ? 22  SER A N   1 
ATOM   285  C  CA  . SER A 1 22  ? 2.34742   27.46132 8.08549   1.000 22.07557  ? 22  SER A CA  1 
ATOM   286  C  C   . SER A 1 22  ? 3.62072   27.38724 8.91161   1.000 23.77800  ? 22  SER A C   1 
ATOM   287  O  O   . SER A 1 22  ? 3.60387   26.89049 10.03916  1.000 23.56362  ? 22  SER A O   1 
ATOM   288  C  CB  . SER A 1 22  ? 2.27744   26.31168 7.09782   1.000 27.63645  ? 22  SER A CB  1 
ATOM   289  O  OG  . SER A 1 22  ? 1.00638   26.31189 6.47491   1.000 27.85713  ? 22  SER A OG  1 
ATOM   290  N  N   . VAL A 1 23  ? 4.73261   27.88478 8.37410   1.000 21.16592  ? 23  VAL A N   1 
ATOM   291  C  CA  . VAL A 1 23  ? 5.98109   27.86771 9.13248   1.000 20.12122  ? 23  VAL A CA  1 
ATOM   292  C  C   . VAL A 1 23  ? 5.85517   28.65938 10.42967  1.000 21.20377  ? 23  VAL A C   1 
ATOM   293  O  O   . VAL A 1 23  ? 6.24022   28.17166 11.49537  1.000 22.96633  ? 23  VAL A O   1 
ATOM   294  C  CB  . VAL A 1 23  ? 7.16286   28.31648 8.25667   1.000 20.89112  ? 23  VAL A CB  1 
ATOM   295  C  CG1 . VAL A 1 23  ? 8.40465   28.51969 9.09827   1.000 30.69763  ? 23  VAL A CG1 1 
ATOM   296  C  CG2 . VAL A 1 23  ? 7.41627   27.25410 7.18289   1.000 24.83155  ? 23  VAL A CG2 1 
ATOM   297  N  N   . TYR A 1 24  ? 5.34051   29.89765 10.37059  1.000 20.62830  ? 24  TYR A N   1 
ATOM   298  C  CA  . TYR A 1 24  ? 5.15819   30.65731 11.60622  1.000 20.13120  ? 24  TYR A CA  1 
ATOM   299  C  C   . TYR A 1 24  ? 4.24614   29.90273 12.56256  1.000 19.62055  ? 24  TYR A C   1 
ATOM   300  O  O   . TYR A 1 24  ? 4.47502   29.90983 13.78772  1.000 22.56407  ? 24  TYR A O   1 
ATOM   301  C  CB  . TYR A 1 24  ? 4.58410   32.04407 11.30788  1.000 22.10804  ? 24  TYR A CB  1 
ATOM   302  C  CG  . TYR A 1 24  ? 5.64746   33.01015 10.85521  1.000 20.97447  ? 24  TYR A CG  1 
ATOM   303  C  CD1 . TYR A 1 24  ? 6.00337   33.08316 9.51681   1.000 22.17739  ? 24  TYR A CD1 1 
ATOM   304  C  CD2 . TYR A 1 24  ? 6.31930   33.83587 11.75802  1.000 21.30777  ? 24  TYR A CD2 1 
ATOM   305  C  CE1 . TYR A 1 24  ? 6.96245   33.92261 9.09510   1.000 20.85965  ? 24  TYR A CE1 1 
ATOM   306  C  CE2 . TYR A 1 24  ? 7.31243   34.72037 11.32843  1.000 23.62001  ? 24  TYR A CE2 1 
ATOM   307  C  CZ  . TYR A 1 24  ? 7.63911   34.74766 9.98753   1.000 23.74141  ? 24  TYR A CZ  1 
ATOM   308  O  OH  . TYR A 1 24  ? 8.62083   35.61567 9.56149   1.000 21.96121  ? 24  TYR A OH  1 
ATOM   309  N  N   . GLY A 1 25  ? 3.21899   29.24692 12.01230  1.000 21.10158  ? 25  GLY A N   1 
ATOM   310  C  CA  . GLY A 1 25  ? 2.28143   28.47244 12.82028  1.000 21.91875  ? 25  GLY A CA  1 
ATOM   311  C  C   . GLY A 1 25  ? 2.95190   27.41531 13.67824  1.000 23.04590  ? 25  GLY A C   1 
ATOM   312  O  O   . GLY A 1 25  ? 2.48699   27.12897 14.78549  1.000 25.14857  ? 25  GLY A O   1 
ATOM   313  N  N   . LEU A 1 26  ? 4.03307   26.80569 13.17176  1.000 23.20938  ? 26  LEU A N   1 
ATOM   314  C  CA  . LEU A 1 26  ? 4.73896   25.75585 13.90073  1.000 25.25287  ? 26  LEU A CA  1 
ATOM   315  C  C   . LEU A 1 26  ? 5.33221   26.23550 15.21570  1.000 28.65598  ? 26  LEU A C   1 
ATOM   316  O  O   . LEU A 1 26  ? 5.62034   25.40653 16.09787  1.000 26.68397  ? 26  LEU A O   1 
ATOM   317  C  CB  . LEU A 1 26  ? 5.89446   25.22575 13.05274  1.000 23.28274  ? 26  LEU A CB  1 
ATOM   318  C  CG  . LEU A 1 26  ? 5.47233   24.57959 11.74971  1.000 23.38981  ? 26  LEU A CG  1 
ATOM   319  C  CD1 . LEU A 1 26  ? 6.68693   24.06840 11.00363  1.000 36.74241  ? 26  LEU A CD1 1 
ATOM   320  C  CD2 . LEU A 1 26  ? 4.50226   23.43838 12.07066  1.000 31.75336  ? 26  LEU A CD2 1 
ATOM   321  N  N   . PHE A 1 27  ? 5.54141   27.53803 15.37379  1.000 23.59654  ? 27  PHE A N   1 
ATOM   322  C  CA  . PHE A 1 27  ? 6.20604   28.09638 16.54041  1.000 23.19316  ? 27  PHE A CA  1 
ATOM   323  C  C   . PHE A 1 27  ? 5.24746   28.78768 17.49738  1.000 26.89661  ? 27  PHE A C   1 
ATOM   324  O  O   . PHE A 1 27  ? 5.68599   29.33990 18.51127  1.000 28.65503  ? 27  PHE A O   1 
ATOM   325  C  CB  . PHE A 1 27  ? 7.33691   29.04656 16.10334  1.000 25.93021  ? 27  PHE A CB  1 
ATOM   326  C  CG  . PHE A 1 27  ? 8.37628   28.35207 15.29547  1.000 31.55657  ? 27  PHE A CG  1 
ATOM   327  C  CD1 . PHE A 1 27  ? 9.37318   27.62144 15.92453  1.000 37.91080  ? 27  PHE A CD1 1 
ATOM   328  C  CD2 . PHE A 1 27  ? 8.31967   28.36155 13.91040  1.000 26.01071  ? 27  PHE A CD2 1 
ATOM   329  C  CE1 . PHE A 1 27  ? 10.32455  26.93396 15.18673  1.000 35.94169  ? 27  PHE A CE1 1 
ATOM   330  C  CE2 . PHE A 1 27  ? 9.26804   27.67506 13.15724  1.000 33.82310  ? 27  PHE A CE2 1 
ATOM   331  C  CZ  . PHE A 1 27  ? 10.26936  26.94856 13.80856  1.000 34.22027  ? 27  PHE A CZ  1 
ATOM   332  N  N   . ILE A 1 28  ? 3.95748   28.78190 17.19527  1.000 24.90096  ? 28  ILE A N   1 
ATOM   333  C  CA  . ILE A 1 28  ? 2.97630   29.35901 18.11973  1.000 23.06669  ? 28  ILE A CA  1 
ATOM   334  C  C   . ILE A 1 28  ? 2.83998   28.42933 19.32431  1.000 24.49755  ? 28  ILE A C   1 
ATOM   335  O  O   . ILE A 1 28  ? 2.64686   27.21417 19.14146  1.000 25.58211  ? 28  ILE A O   1 
ATOM   336  C  CB  . ILE A 1 28  ? 1.63684   29.52606 17.40003  1.000 24.13680  ? 28  ILE A CB  1 
ATOM   337  C  CG1 . ILE A 1 28  ? 1.76229   30.56576 16.28449  1.000 25.53566  ? 28  ILE A CG1 1 
ATOM   338  C  CG2 . ILE A 1 28  ? 0.54752   29.91978 18.39795  1.000 23.59429  ? 28  ILE A CG2 1 
ATOM   339  C  CD1 . ILE A 1 28  ? 0.52857   30.70458 15.47628  1.000 27.49895  ? 28  ILE A CD1 1 
ATOM   340  N  N   . PRO A 1 29  ? 3.00041   28.92706 20.55151  1.000 28.89846  ? 29  PRO A N   1 
ATOM   341  C  CA  . PRO A 1 29  ? 2.91080   28.05126 21.72913  1.000 24.86231  ? 29  PRO A CA  1 
ATOM   342  C  C   . PRO A 1 29  ? 1.49080   27.51864 21.89620  1.000 30.41321  ? 29  PRO A C   1 
ATOM   343  O  O   . PRO A 1 29  ? 0.51211   28.20124 21.58280  1.000 28.34989  ? 29  PRO A O   1 
ATOM   344  C  CB  . PRO A 1 29  ? 3.30699   28.97092 22.88913  1.000 30.18892  ? 29  PRO A CB  1 
ATOM   345  C  CG  . PRO A 1 29  ? 3.08752   30.35562 22.38019  1.000 43.23314  ? 29  PRO A CG  1 
ATOM   346  C  CD  . PRO A 1 29  ? 3.31157   30.32248 20.90014  1.000 31.92482  ? 29  PRO A CD  1 
ATOM   347  N  N   . LEU A 1 30  ? 1.38878   26.27689 22.37504  1.000 26.93082  ? 30  LEU A N   1 
ATOM   348  C  CA  . LEU A 1 30  ? 0.12114   25.54627 22.42845  1.000 23.36946  ? 30  LEU A CA  1 
ATOM   349  C  C   . LEU A 1 30  ? -0.15706  25.03520 23.83239  1.000 26.17345  ? 30  LEU A C   1 
ATOM   350  O  O   . LEU A 1 30  ? 0.74670   24.54065 24.50395  1.000 27.33310  ? 30  LEU A O   1 
ATOM   351  C  CB  . LEU A 1 30  ? 0.18350   24.31530 21.52550  1.000 28.62559  ? 30  LEU A CB  1 
ATOM   352  C  CG  . LEU A 1 30  ? 0.38216   24.60884 20.05323  1.000 40.61927  ? 30  LEU A CG  1 
ATOM   353  C  CD1 . LEU A 1 30  ? 0.52444   23.30321 19.28397  1.000 44.19250  ? 30  LEU A CD1 1 
ATOM   354  C  CD2 . LEU A 1 30  ? -0.81386  25.40360 19.57114  1.000 28.29235  ? 30  LEU A CD2 1 
ATOM   355  N  N   . ASN A 1 31  ? -1.41468  25.13208 24.26150  1.000 24.31736  ? 31  ASN A N   1 
ATOM   356  C  CA  . ASN A 1 31  ? -1.87611  24.44602 25.46054  1.000 25.42644  ? 31  ASN A CA  1 
ATOM   357  C  C   . ASN A 1 31  ? -1.88703  22.92968 25.21685  1.000 23.47802  ? 31  ASN A C   1 
ATOM   358  O  O   . ASN A 1 31  ? -1.98899  22.47364 24.08614  1.000 24.90888  ? 31  ASN A O   1 
ATOM   359  C  CB  . ASN A 1 31  ? -3.31816  24.87066 25.75495  1.000 27.76078  ? 31  ASN A CB  1 
ATOM   360  C  CG  . ASN A 1 31  ? -3.44063  26.36124 26.09072  1.000 46.10178  ? 31  ASN A CG  1 
ATOM   361  O  OD1 . ASN A 1 31  ? -4.12061  27.12861 25.40298  1.000 59.67578  ? 31  ASN A OD1 1 
ATOM   362  N  ND2 . ASN A 1 31  ? -2.78231  26.76649 27.14962  1.000 32.83291  ? 31  ASN A ND2 1 
ATOM   363  N  N   . PHE A 1 32  ? -1.82310  22.14610 26.31065  1.000 28.00334  ? 32  PHE A N   1 
ATOM   364  C  CA  . PHE A 1 32  ? -1.77225  20.67547 26.23328  1.000 23.91559  ? 32  PHE A CA  1 
ATOM   365  C  C   . PHE A 1 32  ? -2.80821  20.10793 25.27997  1.000 24.91810  ? 32  PHE A C   1 
ATOM   366  O  O   . PHE A 1 32  ? -2.50607  19.23337 24.45794  1.000 25.27841  ? 32  PHE A O   1 
ATOM   367  C  CB  . PHE A 1 32  ? -2.00462  20.08353 27.63313  1.000 25.46227  ? 32  PHE A CB  1 
ATOM   368  C  CG  . PHE A 1 32  ? -2.36530  18.60284 27.63841  1.000 27.32782  ? 32  PHE A CG  1 
ATOM   369  C  CD1 . PHE A 1 32  ? -1.37906  17.63810 27.50759  1.000 30.60948  ? 32  PHE A CD1 1 
ATOM   370  C  CD2 . PHE A 1 32  ? -3.69063  18.18034 27.78616  1.000 25.05414  ? 32  PHE A CD2 1 
ATOM   371  C  CE1 . PHE A 1 32  ? -1.69386  16.29328 27.51939  1.000 30.29314  ? 32  PHE A CE1 1 
ATOM   372  C  CE2 . PHE A 1 32  ? -4.02760  16.82349 27.82515  1.000 26.67571  ? 32  PHE A CE2 1 
ATOM   373  C  CZ  . PHE A 1 32  ? -3.02610  15.86946 27.67659  1.000 29.61203  ? 32  PHE A CZ  1 
ATOM   374  N  N   . LYS A 1 33  ? -4.04149  20.60712 25.35464  1.000 23.27281  ? 33  LYS A N   1 
ATOM   375  C  CA  . LYS A 1 33  ? -5.09691  19.98264 24.56820  1.000 24.19442  ? 33  LYS A CA  1 
ATOM   376  C  C   . LYS A 1 33  ? -4.92683  20.21296 23.06906  1.000 23.41098  ? 33  LYS A C   1 
ATOM   377  O  O   . LYS A 1 33  ? -5.51137  19.47948 22.26776  1.000 24.06938  ? 33  LYS A O   1 
ATOM   378  C  CB  . LYS A 1 33  ? -6.46734  20.49457 25.02732  1.000 28.19711  ? 33  LYS A CB  1 
ATOM   379  C  CG  . LYS A 1 33  ? -6.76274  21.94676 24.71931  1.000 37.28068  ? 33  LYS A CG  1 
ATOM   380  C  CD  . LYS A 1 33  ? -8.17544  22.24087 25.22485  1.000 43.19468  ? 33  LYS A CD  1 
ATOM   381  C  CE  . LYS A 1 33  ? -8.51686  23.71136 25.22313  1.000 57.31668  ? 33  LYS A CE  1 
ATOM   382  N  NZ  . LYS A 1 33  ? -8.29523  24.33541 23.88408  1.000 46.57480  ? 33  LYS A NZ  1 
ATOM   383  N  N   . ASP A 1 34  ? -4.11405  21.19242 22.67069  1.000 20.89775  ? 34  ASP A N   1 
ATOM   384  C  CA  . ASP A 1 34  ? -4.02629  21.62810 21.27813  1.000 19.30967  ? 34  ASP A CA  1 
ATOM   385  C  C   . ASP A 1 34  ? -2.77828  21.13842 20.54340  1.000 21.01656  ? 34  ASP A C   1 
ATOM   386  O  O   . ASP A 1 34  ? -2.59196  21.48921 19.36647  1.000 19.04987  ? 34  ASP A O   1 
ATOM   387  C  CB  . ASP A 1 34  ? -4.07684  23.15825 21.19901  1.000 19.30496  ? 34  ASP A CB  1 
ATOM   388  C  CG  . ASP A 1 34  ? -5.37214  23.73021 21.76376  1.000 25.60878  ? 34  ASP A CG  1 
ATOM   389  O  OD1 . ASP A 1 34  ? -6.45560  23.13937 21.48723  1.000 25.64536  ? 34  ASP A OD1 1 
ATOM   390  O  OD2 . ASP A 1 34  ? -5.30449  24.73242 22.49535  1.000 25.29756  ? 34  ASP A OD2 1 
ATOM   391  N  N   . ILE A 1 35  ? -1.93784  20.32515 21.18766  1.000 22.51465  ? 35  ILE A N   1 
ATOM   392  C  CA  . ILE A 1 35  ? -0.65872  19.94079 20.58879  1.000 23.60863  ? 35  ILE A CA  1 
ATOM   393  C  C   . ILE A 1 35  ? -0.84736  19.23923 19.24455  1.000 20.08097  ? 35  ILE A C   1 
ATOM   394  O  O   . ILE A 1 35  ? -0.04452  19.41795 18.30449  1.000 21.25522  ? 35  ILE A O   1 
ATOM   395  C  CB  . ILE A 1 35  ? 0.11518   19.05796 21.58174  1.000 23.64091  ? 35  ILE A CB  1 
ATOM   396  C  CG1 . ILE A 1 35  ? 0.46528   19.85545 22.84469  1.000 29.85034  ? 35  ILE A CG1 1 
ATOM   397  C  CG2 . ILE A 1 35  ? 1.36266   18.48473 20.92234  1.000 34.82391  ? 35  ILE A CG2 1 
ATOM   398  C  CD1 . ILE A 1 35  ? 1.15304   19.01443 23.93037  1.000 47.14136  ? 35  ILE A CD1 1 
ATOM   399  N  N   . ILE A 1 36  ? -1.90655  18.42843 19.11151  1.000 18.13042  ? 36  ILE A N   1 
ATOM   400  C  CA  . ILE A 1 36  ? -2.12243  17.72824 17.84636  1.000 16.68243  ? 36  ILE A CA  1 
ATOM   401  C  C   . ILE A 1 36  ? -2.23590  18.69858 16.65380  1.000 19.91709  ? 36  ILE A C   1 
ATOM   402  O  O   . ILE A 1 36  ? -1.98509  18.31156 15.50736  1.000 20.33094  ? 36  ILE A O   1 
ATOM   403  C  CB  . ILE A 1 36  ? -3.32024  16.76909 17.96250  1.000 20.22293  ? 36  ILE A CB  1 
ATOM   404  C  CG1 . ILE A 1 36  ? -3.32538  15.75093 16.80911  1.000 19.28485  ? 36  ILE A CG1 1 
ATOM   405  C  CG2 . ILE A 1 36  ? -4.62213  17.55179 18.06471  1.000 18.79475  ? 36  ILE A CG2 1 
ATOM   406  C  CD1 . ILE A 1 36  ? -4.42580  14.69595 17.00454  1.000 21.13603  ? 36  ILE A CD1 1 
ATOM   407  N  N   . LEU A 1 37  ? -2.65118  19.94289 16.88180  1.000 19.34752  ? 37  LEU A N   1 
ATOM   408  C  CA  . LEU A 1 37  ? -2.73679  20.88827 15.76674  1.000 20.15026  ? 37  LEU A CA  1 
ATOM   409  C  C   . LEU A 1 37  ? -1.37763  21.12431 15.10663  1.000 19.73502  ? 37  LEU A C   1 
ATOM   410  O  O   . LEU A 1 37  ? -1.29983  21.29136 13.87828  1.000 20.17761  ? 37  LEU A O   1 
ATOM   411  C  CB  . LEU A 1 37  ? -3.33470  22.21420 16.23208  1.000 18.46067  ? 37  LEU A CB  1 
ATOM   412  C  CG  . LEU A 1 37  ? -4.80608  22.08646 16.63948  1.000 20.56028  ? 37  LEU A CG  1 
ATOM   413  C  CD1 . LEU A 1 37  ? -5.30575  23.41186 17.21191  1.000 23.27738  ? 37  LEU A CD1 1 
ATOM   414  C  CD2 . LEU A 1 37  ? -5.67066  21.65767 15.46166  1.000 26.69369  ? 37  LEU A CD2 1 
ATOM   415  N  N   . ARG A 1 38  ? -0.29933  21.19791 15.89995  1.000 21.21310  ? 38  ARG A N   1 
ATOM   416  C  CA  . ARG A 1 38  ? 1.03323   21.35247 15.31587  1.000 20.53625  ? 38  ARG A CA  1 
ATOM   417  C  C   . ARG A 1 38  ? 1.45158   20.08848 14.58093  1.000 21.28990  ? 38  ARG A C   1 
ATOM   418  O  O   . ARG A 1 38  ? 2.12275   20.17487 13.54177  1.000 21.28298  ? 38  ARG A O   1 
ATOM   419  C  CB  . ARG A 1 38  ? 2.05909   21.70052 16.40132  1.000 23.34321  ? 38  ARG A CB  1 
ATOM   420  C  CG  . ARG A 1 38  ? 3.43877   22.09511 15.84037  1.000 22.47662  ? 38  ARG A CG  1 
ATOM   421  C  CD  . ARG A 1 38  ? 4.40262   22.35404 16.97298  1.000 23.91191  ? 38  ARG A CD  1 
ATOM   422  N  NE  . ARG A 1 38  ? 4.00708   23.48846 17.79350  1.000 28.18713  ? 38  ARG A NE  1 
ATOM   423  C  CZ  . ARG A 1 38  ? 4.29056   23.61881 19.08391  1.000 42.81481  ? 38  ARG A CZ  1 
ATOM   424  N  NH1 . ARG A 1 38  ? 4.89407   22.65608 19.76195  1.000 41.42420  ? 38  ARG A NH1 1 
ATOM   425  N  NH2 . ARG A 1 38  ? 3.94591   24.73749 19.71475  1.000 38.11999  ? 38  ARG A NH2 1 
ATOM   426  N  N   . GLU A 1 39  ? 1.05382   18.91080 15.09499  1.000 18.74865  ? 39  GLU A N   1 
ATOM   427  C  CA  . GLU A 1 39  ? 1.31019   17.64780 14.39965  1.000 22.03227  ? 39  GLU A CA  1 
ATOM   428  C  C   . GLU A 1 39  ? 0.65384   17.65330 13.02008  1.000 22.37220  ? 39  GLU A C   1 
ATOM   429  O  O   . GLU A 1 39  ? 1.26520   17.24484 12.01926  1.000 20.87101  ? 39  GLU A O   1 
ATOM   430  C  CB  . GLU A 1 39  ? 0.80026   16.48595 15.27820  1.000 20.02058  ? 39  GLU A CB  1 
ATOM   431  C  CG  . GLU A 1 39  ? 1.52785   16.43555 16.65792  1.000 22.62598  ? 39  GLU A CG  1 
ATOM   432  C  CD  . GLU A 1 39  ? 1.11253   15.27027 17.53880  1.000 27.17220  ? 39  GLU A CD  1 
ATOM   433  O  OE1 . GLU A 1 39  ? -0.06628  14.89569 17.51048  1.000 25.49664  ? 39  GLU A OE1 1 
ATOM   434  O  OE2 . GLU A 1 39  ? 1.96760   14.73940 18.27340  1.000 30.01780  ? 39  GLU A OE2 1 
ATOM   435  N  N   . ILE A 1 40  ? -0.59281  18.11909 12.95589  1.000 20.64818  ? 40  ILE A N   1 
ATOM   436  C  CA  . ILE A 1 40  ? -1.29586  18.27890 11.68767  1.000 18.15983  ? 40  ILE A CA  1 
ATOM   437  C  C   . ILE A 1 40  ? -0.55169  19.24598 10.77081  1.000 19.29852  ? 40  ILE A C   1 
ATOM   438  O  O   . ILE A 1 40  ? -0.34578  18.95980 9.58324   1.000 19.34131  ? 40  ILE A O   1 
ATOM   439  C  CB  . ILE A 1 40  ? -2.73943  18.74982 11.96059  1.000 15.91965  ? 40  ILE A CB  1 
ATOM   440  C  CG1 . ILE A 1 40  ? -3.50503  17.60111 12.63834  1.000 18.09563  ? 40  ILE A CG1 1 
ATOM   441  C  CG2 . ILE A 1 40  ? -3.42080  19.17933 10.66425  1.000 19.73563  ? 40  ILE A CG2 1 
ATOM   442  C  CD1 . ILE A 1 40  ? -4.87597  17.93943 13.19810  1.000 22.03381  ? 40  ILE A CD1 1 
ATOM   443  N  N   . LEU A 1 41  ? -0.14243  20.39857 11.29958  1.000 18.59549  ? 41  LEU A N   1 
ATOM   444  C  CA  . LEU A 1 41  ? 0.41607   21.43311 10.44026  1.000 20.25896  ? 41  LEU A CA  1 
ATOM   445  C  C   . LEU A 1 41  ? 1.73960   20.97795 9.82607   1.000 18.34034  ? 41  LEU A C   1 
ATOM   446  O  O   . LEU A 1 41  ? 2.02716   21.29555 8.66135   1.000 20.59638  ? 41  LEU A O   1 
ATOM   447  C  CB  . LEU A 1 41  ? 0.57209   22.73677 11.23364  1.000 27.67129  ? 41  LEU A CB  1 
ATOM   448  C  CG  . LEU A 1 41  ? 0.86851   24.02306 10.46101  1.000 26.01175  ? 41  LEU A CG  1 
ATOM   449  C  CD1 . LEU A 1 41  ? -0.13537  24.20030 9.33952   1.000 23.62070  ? 41  LEU A CD1 1 
ATOM   450  C  CD2 . LEU A 1 41  ? 0.83055   25.22209 11.38591  1.000 26.34606  ? 41  LEU A CD2 1 
ATOM   451  N  N   A ILE A 1 42  ? 2.53723   20.19231 10.55268  0.500 18.67742  ? 42  ILE A N   1 
ATOM   452  N  N   B ILE A 1 42  ? 2.55796   20.26021 10.60670  0.500 18.70778  ? 42  ILE A N   1 
ATOM   453  C  CA  A ILE A 1 42  ? 3.80498   19.74433 9.96238   0.500 20.24145  ? 42  ILE A CA  1 
ATOM   454  C  CA  B ILE A 1 42  ? 3.78619   19.65713 10.07591  0.500 20.45106  ? 42  ILE A CA  1 
ATOM   455  C  C   A ILE A 1 42  ? 3.56921   18.69916 8.86762   0.500 22.90557  ? 42  ILE A C   1 
ATOM   456  C  C   B ILE A 1 42  ? 3.46814   18.81487 8.84563   0.500 22.95720  ? 42  ILE A C   1 
ATOM   457  O  O   A ILE A 1 42  ? 4.34454   18.61310 7.90406   0.500 20.83468  ? 42  ILE A O   1 
ATOM   458  O  O   B ILE A 1 42  ? 4.05562   19.00144 7.77147   0.500 19.77106  ? 42  ILE A O   1 
ATOM   459  C  CB  A ILE A 1 42  ? 4.79410   19.25720 11.03003  0.500 26.61480  ? 42  ILE A CB  1 
ATOM   460  C  CB  B ILE A 1 42  ? 4.48934   18.82931 11.16756  0.500 21.94530  ? 42  ILE A CB  1 
ATOM   461  C  CG1 A ILE A 1 42  ? 6.13123   18.89266 10.36279  0.500 25.88237  ? 42  ILE A CG1 1 
ATOM   462  C  CG1 B ILE A 1 42  ? 5.16347   19.76341 12.17193  0.500 22.64800  ? 42  ILE A CG1 1 
ATOM   463  C  CG2 A ILE A 1 42  ? 4.20467   18.09111 11.78936  0.500 25.28897  ? 42  ILE A CG2 1 
ATOM   464  C  CG2 B ILE A 1 42  ? 5.51828   17.83735 10.56619  0.500 22.88661  ? 42  ILE A CG2 1 
ATOM   465  C  CD1 A ILE A 1 42  ? 6.99505   17.97408 11.19018  0.500 38.78922  ? 42  ILE A CD1 1 
ATOM   466  C  CD1 B ILE A 1 42  ? 5.76810   19.06158 13.37314  0.500 35.03864  ? 42  ILE A CD1 1 
ATOM   467  N  N   . LEU A 1 43  ? 2.50766   17.89560 8.97893   1.000 19.61417  ? 43  LEU A N   1 
ATOM   468  C  CA  . LEU A 1 43  ? 2.18820   16.99411 7.87244   1.000 20.54771  ? 43  LEU A CA  1 
ATOM   469  C  C   . LEU A 1 43  ? 1.66801   17.76592 6.66676   1.000 24.76755  ? 43  LEU A C   1 
ATOM   470  O  O   . LEU A 1 43  ? 1.95611   17.40111 5.51302   1.000 21.81322  ? 43  LEU A O   1 
ATOM   471  C  CB  . LEU A 1 43  ? 1.19001   15.93027 8.31729   1.000 22.34106  ? 43  LEU A CB  1 
ATOM   472  C  CG  . LEU A 1 43  ? 1.79869   14.94980 9.32437   1.000 21.69329  ? 43  LEU A CG  1 
ATOM   473  C  CD1 . LEU A 1 43  ? 0.69968   14.15509 9.99773   1.000 26.02438  ? 43  LEU A CD1 1 
ATOM   474  C  CD2 . LEU A 1 43  ? 2.78088   14.00705 8.61781   1.000 30.01418  ? 43  LEU A CD2 1 
ATOM   475  N  N   A GLU A 1 44  ? 0.90378   18.83907 6.89814   0.700 20.53508  ? 44  GLU A N   1 
ATOM   476  N  N   B GLU A 1 44  ? 0.91681   18.84024 6.90592   0.300 20.71425  ? 44  GLU A N   1 
ATOM   477  C  CA  A GLU A 1 44  ? 0.43580   19.66014 5.77714   0.700 19.58930  ? 44  GLU A CA  1 
ATOM   478  C  CA  B GLU A 1 44  ? 0.52430   19.71721 5.80860   0.300 20.22339  ? 44  GLU A CA  1 
ATOM   479  C  C   A GLU A 1 44  ? 1.58790   20.37049 5.07843   0.700 19.67528  ? 44  GLU A C   1 
ATOM   480  C  C   B GLU A 1 44  ? 1.74977   20.25670 5.08059   0.300 19.34799  ? 44  GLU A C   1 
ATOM   481  O  O   A GLU A 1 44  ? 1.51854   20.62732 3.86647   0.700 19.87330  ? 44  GLU A O   1 
ATOM   482  O  O   B GLU A 1 44  ? 1.84528   20.16122 3.85224   0.300 19.91689  ? 44  GLU A O   1 
ATOM   483  C  CB  A GLU A 1 44  ? -0.58210  20.68561 6.26838   0.700 27.38967  ? 44  GLU A CB  1 
ATOM   484  C  CB  B GLU A 1 44  ? -0.35413  20.84901 6.34004   0.300 25.77099  ? 44  GLU A CB  1 
ATOM   485  C  CG  A GLU A 1 44  ? -1.87739  20.07238 6.73425   0.700 27.06208  ? 44  GLU A CG  1 
ATOM   486  C  CG  B GLU A 1 44  ? -1.63230  20.34223 6.98836   0.300 23.76267  ? 44  GLU A CG  1 
ATOM   487  C  CD  A GLU A 1 44  ? -2.56156  19.26566 5.64424   0.700 33.38021  ? 44  GLU A CD  1 
ATOM   488  C  CD  B GLU A 1 44  ? -2.61592  21.44689 7.31689   0.300 25.73576  ? 44  GLU A CD  1 
ATOM   489  O  OE1 A GLU A 1 44  ? -2.59012  19.72666 4.47888   0.700 42.84663  ? 44  GLU A OE1 1 
ATOM   490  O  OE1 B GLU A 1 44  ? -2.21760  22.43785 7.96004   0.300 35.24398  ? 44  GLU A OE1 1 
ATOM   491  O  OE2 A GLU A 1 44  ? -3.06477  18.16404 5.95253   0.700 38.11515  ? 44  GLU A OE2 1 
ATOM   492  O  OE2 B GLU A 1 44  ? -3.79229  21.33004 6.92273   0.300 35.15935  ? 44  GLU A OE2 1 
ATOM   493  N  N   A LEU A 1 45  ? 2.63309   20.72617 5.82243   0.500 18.86442  ? 45  LEU A N   1 
ATOM   494  N  N   B LEU A 1 45  ? 2.71473   20.79895 5.82866   0.500 18.87980  ? 45  LEU A N   1 
ATOM   495  C  CA  A LEU A 1 45  ? 3.79737   21.34148 5.19977   0.500 19.89146  ? 45  LEU A CA  1 
ATOM   496  C  CA  B LEU A 1 45  ? 3.89790   21.38383 5.20359   0.500 19.60142  ? 45  LEU A CA  1 
ATOM   497  C  C   A LEU A 1 45  ? 4.52817   20.33537 4.32800   0.500 23.21340  ? 45  LEU A C   1 
ATOM   498  C  C   B LEU A 1 45  ? 4.64330   20.35426 4.36599   0.500 23.63910  ? 45  LEU A C   1 
ATOM   499  O  O   A LEU A 1 45  ? 4.98617   20.67708 3.23499   0.500 23.28981  ? 45  LEU A O   1 
ATOM   500  O  O   B LEU A 1 45  ? 5.23220   20.69615 3.33567   0.500 24.04408  ? 45  LEU A O   1 
ATOM   501  C  CB  A LEU A 1 45  ? 4.71803   21.91307 6.27634   0.500 20.20809  ? 45  LEU A CB  1 
ATOM   502  C  CB  B LEU A 1 45  ? 4.81321   21.97553 6.27315   0.500 20.31659  ? 45  LEU A CB  1 
ATOM   503  C  CG  A LEU A 1 45  ? 4.33694   23.33039 6.69893   0.500 23.41403  ? 45  LEU A CG  1 
ATOM   504  C  CG  B LEU A 1 45  ? 5.80398   22.99118 5.70571   0.500 19.76728  ? 45  LEU A CG  1 
ATOM   505  C  CD1 A LEU A 1 45  ? 4.99941   23.70150 8.00785   0.500 26.96203  ? 45  LEU A CD1 1 
ATOM   506  C  CD1 B LEU A 1 45  ? 5.05172   24.09834 4.97889   0.500 23.90323  ? 45  LEU A CD1 1 
ATOM   507  C  CD2 A LEU A 1 45  ? 4.74260   24.31951 5.61353   0.500 20.71809  ? 45  LEU A CD2 1 
ATOM   508  C  CD2 B LEU A 1 45  ? 6.70900   23.57479 6.79130   0.500 28.08242  ? 45  LEU A CD2 1 
ATOM   509  N  N   . ILE A 1 46  ? 4.64242   19.09270 4.80417   1.000 22.91266  ? 46  ILE A N   1 
ATOM   510  C  CA  . ILE A 1 46  ? 5.23200   18.01403 4.00503   1.000 25.20387  ? 46  ILE A CA  1 
ATOM   511  C  C   . ILE A 1 46  ? 4.46254   17.83283 2.70012   1.000 24.94574  ? 46  ILE A C   1 
ATOM   512  O  O   . ILE A 1 46  ? 5.05736   17.71308 1.61795   1.000 24.87608  ? 46  ILE A O   1 
ATOM   513  C  CB  . ILE A 1 46  ? 5.27545   16.71111 4.82366   1.000 25.89215  ? 46  ILE A CB  1 
ATOM   514  C  CG1 . ILE A 1 46  ? 6.33611   16.80567 5.92057   1.000 25.24410  ? 46  ILE A CG1 1 
ATOM   515  C  CG2 . ILE A 1 46  ? 5.58971   15.51931 3.92835   1.000 31.80283  ? 46  ILE A CG2 1 
ATOM   516  C  CD1 . ILE A 1 46  ? 6.22295   15.68476 6.96130   1.000 33.30711  ? 46  ILE A CD1 1 
ATOM   517  N  N   . VAL A 1 47  ? 3.12891   17.78528 2.78558   1.000 21.16035  ? 47  VAL A N   1 
ATOM   518  C  CA  . VAL A 1 47  ? 2.28605   17.78159 1.58463   1.000 21.36943  ? 47  VAL A CA  1 
ATOM   519  C  C   . VAL A 1 47  ? 2.66216   18.95635 0.68368   1.000 22.86808  ? 47  VAL A C   1 
ATOM   520  O  O   . VAL A 1 47  ? 2.76027   18.80692 -0.54585  1.000 23.13523  ? 47  VAL A O   1 
ATOM   521  C  CB  . VAL A 1 47  ? 0.79200   17.77312 1.95973   1.000 17.63233  ? 47  VAL A CB  1 
ATOM   522  C  CG1 . VAL A 1 47  ? -0.12469  18.11276 0.75346   1.000 20.81102  ? 47  VAL A CG1 1 
ATOM   523  C  CG2 . VAL A 1 47  ? 0.39606   16.41522 2.54359   1.000 19.81496  ? 47  VAL A CG2 1 
ATOM   524  N  N   A GLN A 1 48  ? 2.87661   20.14177 1.26976   0.700 20.54716  ? 48  GLN A N   1 
ATOM   525  N  N   B GLN A 1 48  ? 2.91957   20.12923 1.28485   0.300 20.84177  ? 48  GLN A N   1 
ATOM   526  C  CA  A GLN A 1 48  ? 3.22793   21.30876 0.45489   0.700 22.77385  ? 48  GLN A CA  1 
ATOM   527  C  CA  B GLN A 1 48  ? 3.23249   21.33615 0.51692   0.300 23.29859  ? 48  GLN A CA  1 
ATOM   528  C  C   A GLN A 1 48  ? 4.55811   21.12488 -0.26136  0.700 24.77149  ? 48  GLN A C   1 
ATOM   529  C  C   B GLN A 1 48  ? 4.59254   21.25054 -0.17093  0.300 24.42571  ? 48  GLN A C   1 
ATOM   530  O  O   A GLN A 1 48  ? 4.72356   21.57412 -1.40434  0.700 22.35407  ? 48  GLN A O   1 
ATOM   531  O  O   B GLN A 1 48  ? 4.80524   21.89763 -1.20586  0.300 24.11420  ? 48  GLN A O   1 
ATOM   532  C  CB  A GLN A 1 48  ? 3.23186   22.58894 1.29085   0.700 25.05852  ? 48  GLN A CB  1 
ATOM   533  C  CB  B GLN A 1 48  ? 3.15621   22.57059 1.42392   0.300 24.89894  ? 48  GLN A CB  1 
ATOM   534  C  CG  A GLN A 1 48  ? 1.84280   23.17278 1.47967   0.700 24.09160  ? 48  GLN A CG  1 
ATOM   535  C  CG  B GLN A 1 48  ? 1.78667   22.77515 2.07767   0.300 18.27276  ? 48  GLN A CG  1 
ATOM   536  C  CD  A GLN A 1 48  ? 1.84422   24.68796 1.58459   0.700 29.55505  ? 48  GLN A CD  1 
ATOM   537  C  CD  B GLN A 1 48  ? 1.77282   23.87692 3.13329   0.300 30.73764  ? 48  GLN A CD  1 
ATOM   538  O  OE1 A GLN A 1 48  ? 1.55266   25.24226 2.64963   0.700 26.18943  ? 48  GLN A OE1 1 
ATOM   539  O  OE1 B GLN A 1 48  ? 2.14574   25.01992 2.86888   0.300 26.18082  ? 48  GLN A OE1 1 
ATOM   540  N  NE2 A GLN A 1 48  ? 2.15809   25.37264 0.47472   0.700 19.95586  ? 48  GLN A NE2 1 
ATOM   541  N  NE2 B GLN A 1 48  ? 1.33683   23.53050 4.33746   0.300 24.03688  ? 48  GLN A NE2 1 
ATOM   542  N  N   . ILE A 1 49  ? 5.52684   20.47434 0.38017   1.000 22.46080  ? 49  ILE A N   1 
ATOM   543  C  CA  . ILE A 1 49  ? 6.81126   20.27462 -0.27735  1.000 24.11116  ? 49  ILE A CA  1 
ATOM   544  C  C   . ILE A 1 49  ? 6.60711   19.45038 -1.55056  1.000 23.08952  ? 49  ILE A C   1 
ATOM   545  O  O   . ILE A 1 49  ? 7.11932   19.79476 -2.62250  1.000 24.43070  ? 49  ILE A O   1 
ATOM   546  C  CB  . ILE A 1 49  ? 7.81101   19.61532 0.68125   1.000 23.67367  ? 49  ILE A CB  1 
ATOM   547  C  CG1 . ILE A 1 49  ? 8.11152   20.56209 1.85146   1.000 27.87090  ? 49  ILE A CG1 1 
ATOM   548  C  CG2 . ILE A 1 49  ? 9.09860   19.24169 -0.08908  1.000 29.76944  ? 49  ILE A CG2 1 
ATOM   549  C  CD1 . ILE A 1 49  ? 8.99289   19.94681 2.96493   1.000 32.05447  ? 49  ILE A CD1 1 
ATOM   550  N  N   A ILE A 1 50  ? 5.84673   18.36694 -1.43327  0.500 23.76128  ? 50  ILE A N   1 
ATOM   551  N  N   B ILE A 1 50  ? 5.82162   18.38226 -1.44296  0.500 23.77737  ? 50  ILE A N   1 
ATOM   552  C  CA  A ILE A 1 50  ? 5.56957   17.52369 -2.59875  0.500 23.21284  ? 50  ILE A CA  1 
ATOM   553  C  CA  B ILE A 1 50  ? 5.53404   17.54826 -2.61218  0.500 23.26635  ? 50  ILE A CA  1 
ATOM   554  C  C   A ILE A 1 50  ? 4.81090   18.31108 -3.65869  0.500 24.95228  ? 50  ILE A C   1 
ATOM   555  C  C   B ILE A 1 50  ? 4.77845   18.33342 -3.67902  0.500 24.94677  ? 50  ILE A C   1 
ATOM   556  O  O   A ILE A 1 50  ? 5.22822   18.37094 -4.82680  0.500 22.31174  ? 50  ILE A O   1 
ATOM   557  O  O   B ILE A 1 50  ? 4.93353   18.07438 -4.88320  0.500 22.28895  ? 50  ILE A O   1 
ATOM   558  C  CB  A ILE A 1 50  ? 4.80691   16.25851 -2.17331  0.500 26.18310  ? 50  ILE A CB  1 
ATOM   559  C  CB  B ILE A 1 50  ? 4.79144   16.27109 -2.17585  0.500 26.20401  ? 50  ILE A CB  1 
ATOM   560  C  CG1 A ILE A 1 50  ? 5.69189   15.37625 -1.28980  0.500 27.38897  ? 50  ILE A CG1 1 
ATOM   561  C  CG1 B ILE A 1 50  ? 5.65996   15.47248 -1.20211  0.500 27.40756  ? 50  ILE A CG1 1 
ATOM   562  C  CG2 A ILE A 1 50  ? 4.29661   15.50558 -3.40229  0.500 24.12736  ? 50  ILE A CG2 1 
ATOM   563  C  CG2 B ILE A 1 50  ? 4.39329   15.42696 -3.38541  0.500 24.30621  ? 50  ILE A CG2 1 
ATOM   564  C  CD1 A ILE A 1 50  ? 4.89328   14.49181 -0.33393  0.500 22.81266  ? 50  ILE A CD1 1 
ATOM   565  C  CD1 B ILE A 1 50  ? 6.98461   15.07688 -1.76275  0.500 34.18222  ? 50  ILE A CD1 1 
ATOM   566  N  N   A GLU A 1 51  ? 3.68716   18.93014 -3.26614  0.700 20.91994  ? 51  GLU A N   1 
ATOM   567  N  N   B GLU A 1 51  ? 3.97018   19.31565 -3.27357  0.300 20.37121  ? 51  GLU A N   1 
ATOM   568  C  CA  A GLU A 1 51  ? 2.88295   19.70465 -4.20656  0.700 21.09391  ? 51  GLU A CA  1 
ATOM   569  C  CA  B GLU A 1 51  ? 3.27781   20.12385 -4.27023  0.300 22.10431  ? 51  GLU A CA  1 
ATOM   570  C  C   A GLU A 1 51  ? 3.73627   20.71108 -4.97225  0.700 19.80589  ? 51  GLU A C   1 
ATOM   571  C  C   B GLU A 1 51  ? 4.22926   21.12641 -4.92246  0.300 17.28178  ? 51  GLU A C   1 
ATOM   572  O  O   A GLU A 1 51  ? 3.63162   20.82532 -6.19428  0.700 20.93044  ? 51  GLU A O   1 
ATOM   573  O  O   B GLU A 1 51  ? 4.14764   21.36740 -6.13071  0.300 17.95807  ? 51  GLU A O   1 
ATOM   574  C  CB  A GLU A 1 51  ? 1.73342   20.42418 -3.48045  0.700 21.03011  ? 51  GLU A CB  1 
ATOM   575  C  CB  B GLU A 1 51  ? 2.04396   20.79562 -3.65305  0.300 20.16166  ? 51  GLU A CB  1 
ATOM   576  C  CG  A GLU A 1 51  ? 0.97761   21.36510 -4.42718  0.700 25.92173  ? 51  GLU A CG  1 
ATOM   577  C  CG  B GLU A 1 51  ? 0.73177   20.62018 -4.46912  0.300 24.01286  ? 51  GLU A CG  1 
ATOM   578  C  CD  A GLU A 1 51  ? -0.03462  22.23423 -3.73694  0.700 25.52887  ? 51  GLU A CD  1 
ATOM   579  C  CD  B GLU A 1 51  ? 0.25790   19.17323 -4.59504  0.300 24.50785  ? 51  GLU A CD  1 
ATOM   580  O  OE1 A GLU A 1 51  ? 0.16916   22.59387 -2.55454  0.700 23.84297  ? 51  GLU A OE1 1 
ATOM   581  O  OE1 B GLU A 1 51  ? 0.63772   18.32807 -3.75572  0.300 32.35303  ? 51  GLU A OE1 1 
ATOM   582  O  OE2 A GLU A 1 51  ? -1.03082  22.58204 -4.40106  0.700 27.38856  ? 51  GLU A OE2 1 
ATOM   583  O  OE2 B GLU A 1 51  ? -0.51178  18.87524 -5.53377  0.300 27.20766  ? 51  GLU A OE2 1 
ATOM   584  N  N   A PHE A 1 52  ? 4.60201   21.43997 -4.26329  0.700 20.53882  ? 52  PHE A N   1 
ATOM   585  N  N   B PHE A 1 52  ? 5.16222   21.68792 -4.14571  0.300 20.26823  ? 52  PHE A N   1 
ATOM   586  C  CA  A PHE A 1 52  ? 5.40303   22.47399 -4.90854  0.700 19.94473  ? 52  PHE A CA  1 
ATOM   587  C  CA  B PHE A 1 52  ? 6.14022   22.62094 -4.70122  0.300 24.18839  ? 52  PHE A CA  1 
ATOM   588  C  C   A PHE A 1 52  ? 6.33488   21.87677 -5.95120  0.700 23.26804  ? 52  PHE A C   1 
ATOM   589  C  C   B PHE A 1 52  ? 6.98292   21.95123 -5.77790  0.300 22.46382  ? 52  PHE A C   1 
ATOM   590  O  O   A PHE A 1 52  ? 6.50220   22.43753 -7.03899  0.700 21.43576  ? 52  PHE A O   1 
ATOM   591  O  O   B PHE A 1 52  ? 7.21293   22.52211 -6.85033  0.300 21.67981  ? 52  PHE A O   1 
ATOM   592  C  CB  A PHE A 1 52  ? 6.17865   23.26750 -3.85437  0.700 24.72879  ? 52  PHE A CB  1 
ATOM   593  C  CB  B PHE A 1 52  ? 7.05135   23.15231 -3.59265  0.300 18.26932  ? 52  PHE A CB  1 
ATOM   594  C  CG  A PHE A 1 52  ? 6.89033   24.47449 -4.39478  0.700 24.28876  ? 52  PHE A CG  1 
ATOM   595  C  CG  B PHE A 1 52  ? 6.53217   24.38967 -2.89936  0.300 27.07488  ? 52  PHE A CG  1 
ATOM   596  C  CD1 A PHE A 1 52  ? 6.17946   25.59898 -4.77365  0.700 29.45408  ? 52  PHE A CD1 1 
ATOM   597  C  CD1 B PHE A 1 52  ? 5.88069   25.38836 -3.60608  0.300 26.21468  ? 52  PHE A CD1 1 
ATOM   598  C  CD2 A PHE A 1 52  ? 8.28293   24.49586 -4.50258  0.700 27.34843  ? 52  PHE A CD2 1 
ATOM   599  C  CD2 B PHE A 1 52  ? 6.71543   24.55481 -1.53076  0.300 25.37404  ? 52  PHE A CD2 1 
ATOM   600  C  CE1 A PHE A 1 52  ? 6.84043   26.71948 -5.26395  0.700 28.21040  ? 52  PHE A CE1 1 
ATOM   601  C  CE1 B PHE A 1 52  ? 5.41824   26.53028 -2.95449  0.300 20.10467  ? 52  PHE A CE1 1 
ATOM   602  C  CE2 A PHE A 1 52  ? 8.94966   25.62500 -4.98842  0.700 29.91031  ? 52  PHE A CE2 1 
ATOM   603  C  CE2 B PHE A 1 52  ? 6.25903   25.68860 -0.87883  0.300 25.84862  ? 52  PHE A CE2 1 
ATOM   604  C  CZ  A PHE A 1 52  ? 8.22612   26.73312 -5.36780  0.700 28.47414  ? 52  PHE A CZ  1 
ATOM   605  C  CZ  B PHE A 1 52  ? 5.61615   26.68039 -1.59659  0.300 18.95609  ? 52  PHE A CZ  1 
ATOM   606  N  N   A ILE A 1 53  ? 6.93903   20.72988 -5.64246  0.700 22.13219  ? 53  ILE A N   1 
ATOM   607  N  N   B ILE A 1 53  ? 7.46646   20.74075 -5.49999  0.300 20.09380  ? 53  ILE A N   1 
ATOM   608  C  CA  A ILE A 1 53  ? 7.78507   20.04859 -6.61891  0.700 24.64037  ? 53  ILE A CA  1 
ATOM   609  C  CA  B ILE A 1 53  ? 8.25113   20.00911 -6.49104  0.300 24.13449  ? 53  ILE A CA  1 
ATOM   610  C  C   A ILE A 1 53  ? 7.01020   19.75035 -7.89548  0.700 19.30459  ? 53  ILE A C   1 
ATOM   611  C  C   B ILE A 1 53  ? 7.41694   19.72851 -7.73427  0.300 22.20900  ? 53  ILE A C   1 
ATOM   612  O  O   A ILE A 1 53  ? 7.50841   19.97634 -9.00860  0.700 21.54662  ? 53  ILE A O   1 
ATOM   613  O  O   B ILE A 1 53  ? 7.85447   19.98655 -8.86312  0.300 22.75909  ? 53  ILE A O   1 
ATOM   614  C  CB  A ILE A 1 53  ? 8.40771   18.78357 -6.00556  0.700 22.59050  ? 53  ILE A CB  1 
ATOM   615  C  CB  B ILE A 1 53  ? 8.82350   18.71615 -5.88563  0.300 26.54926  ? 53  ILE A CB  1 
ATOM   616  C  CG1 A ILE A 1 53  ? 9.50309   19.20749 -5.03044  0.700 22.52270  ? 53  ILE A CG1 1 
ATOM   617  C  CG1 B ILE A 1 53  ? 9.66156   19.03661 -4.64875  0.300 27.03780  ? 53  ILE A CG1 1 
ATOM   618  C  CG2 A ILE A 1 53  ? 8.99858   17.89463 -7.10354  0.700 25.72409  ? 53  ILE A CG2 1 
ATOM   619  C  CG2 B ILE A 1 53  ? 9.66133   17.97729 -6.92581  0.300 21.97194  ? 53  ILE A CG2 1 
ATOM   620  C  CD1 A ILE A 1 53  ? 9.92000   18.10697 -4.07565  0.700 34.19306  ? 53  ILE A CD1 1 
ATOM   621  C  CD1 B ILE A 1 53  ? 10.09244  17.80920 -3.87398  0.300 31.36293  ? 53  ILE A CD1 1 
ATOM   622  N  N   A PHE A 1 54  ? 5.77790   19.25074 -7.76437  0.700 20.18342  ? 54  PHE A N   1 
ATOM   623  N  N   B PHE A 1 54  ? 6.20438   19.19391 -7.54784  0.300 23.85727  ? 54  PHE A N   1 
ATOM   624  C  CA  A PHE A 1 54  ? 5.00661   18.98114 -8.97366  0.700 20.57273  ? 54  PHE A CA  1 
ATOM   625  C  CA  B PHE A 1 54  ? 5.34730   18.90236 -8.69394  0.300 21.98048  ? 54  PHE A CA  1 
ATOM   626  C  C   A PHE A 1 54  ? 4.73130   20.26376 -9.75231  0.700 24.11379  ? 54  PHE A C   1 
ATOM   627  C  C   B PHE A 1 54  ? 5.07420   20.15785 -9.51365  0.300 23.88559  ? 54  PHE A C   1 
ATOM   628  O  O   A PHE A 1 54  ? 4.77811   20.26826 -10.98684 0.700 23.13983  ? 54  PHE A O   1 
ATOM   629  O  O   B PHE A 1 54  ? 5.21417   20.14667 -10.74174 0.300 17.25328  ? 54  PHE A O   1 
ATOM   630  C  CB  A PHE A 1 54  ? 3.67951   18.28704 -8.67448  0.700 22.65100  ? 54  PHE A CB  1 
ATOM   631  C  CB  B PHE A 1 54  ? 4.03487   18.25839 -8.24419  0.300 21.05911  ? 54  PHE A CB  1 
ATOM   632  C  CG  A PHE A 1 54  ? 2.74995   18.31343 -9.85014  0.700 23.60104  ? 54  PHE A CG  1 
ATOM   633  C  CG  B PHE A 1 54  ? 3.01361   18.15950 -9.34560  0.300 20.42659  ? 54  PHE A CG  1 
ATOM   634  C  CD1 A PHE A 1 54  ? 2.85099   17.36765 -10.86420 0.700 21.15832  ? 54  PHE A CD1 1 
ATOM   635  C  CD1 B PHE A 1 54  ? 3.12783   17.19180 -10.33379 0.300 21.30650  ? 54  PHE A CD1 1 
ATOM   636  C  CD2 A PHE A 1 54  ? 1.84368   19.34930 -9.99496  0.700 19.39797  ? 54  PHE A CD2 1 
ATOM   637  C  CD2 B PHE A 1 54  ? 1.95366   19.04898 -9.40444  0.300 22.02518  ? 54  PHE A CD2 1 
ATOM   638  C  CE1 A PHE A 1 54  ? 2.01381   17.44598 -11.96911 0.700 20.72790  ? 54  PHE A CE1 1 
ATOM   639  C  CE1 B PHE A 1 54  ? 2.19463   17.11135 -11.35512 0.300 23.23393  ? 54  PHE A CE1 1 
ATOM   640  C  CE2 A PHE A 1 54  ? 1.02003   19.43553 -11.08582 0.700 19.26635  ? 54  PHE A CE2 1 
ATOM   641  C  CE2 B PHE A 1 54  ? 1.01847   18.97581 -10.42131 0.300 23.43073  ? 54  PHE A CE2 1 
ATOM   642  C  CZ  A PHE A 1 54  ? 1.10984   18.47886 -12.07977 0.700 26.74504  ? 54  PHE A CZ  1 
ATOM   643  C  CZ  B PHE A 1 54  ? 1.13977   18.00428 -11.39723 0.300 27.48734  ? 54  PHE A CZ  1 
ATOM   644  N  N   A TYR A 1 55  ? 4.38819   21.34831 -9.05568  0.700 20.33295  ? 55  TYR A N   1 
ATOM   645  N  N   B TYR A 1 55  ? 4.70196   21.25549 -8.85191  0.300 21.86278  ? 55  TYR A N   1 
ATOM   646  C  CA  A TYR A 1 55  ? 4.02099   22.56152 -9.77827  0.700 20.19394  ? 55  TYR A CA  1 
ATOM   647  C  CA  B TYR A 1 55  ? 4.39056   22.47751 -9.58636  0.300 20.24390  ? 55  TYR A CA  1 
ATOM   648  C  C   A TYR A 1 55  ? 5.20416   23.20597 -10.47874 0.700 20.18275  ? 55  TYR A C   1 
ATOM   649  C  C   B TYR A 1 55  ? 5.61435   23.04550 -10.28336 0.300 24.00684  ? 55  TYR A C   1 
ATOM   650  O  O   A TYR A 1 55  ? 5.03457   23.78003 -11.56028 0.700 21.13431  ? 55  TYR A O   1 
ATOM   651  O  O   B TYR A 1 55  ? 5.50558   23.59836 -11.38400 0.300 21.47096  ? 55  TYR A O   1 
ATOM   652  C  CB  A TYR A 1 55  ? 3.24610   23.53528 -8.88476  0.700 22.47207  ? 55  TYR A CB  1 
ATOM   653  C  CB  B TYR A 1 55  ? 3.77372   23.51483 -8.65740  0.300 18.63191  ? 55  TYR A CB  1 
ATOM   654  C  CG  A TYR A 1 55  ? 1.79691   23.13602 -8.86636  0.700 16.46868  ? 55  TYR A CG  1 
ATOM   655  C  CG  B TYR A 1 55  ? 2.28280   23.38254 -8.59608  0.300 18.43472  ? 55  TYR A CG  1 
ATOM   656  C  CD1 A TYR A 1 55  ? 0.92900   23.60675 -9.83219  0.700 27.46740  ? 55  TYR A CD1 1 
ATOM   657  C  CD1 B TYR A 1 55  ? 1.47215   24.05840 -9.49279  0.300 15.88436  ? 55  TYR A CD1 1 
ATOM   658  C  CD2 A TYR A 1 55  ? 1.31396   22.20565 -7.95017  0.700 17.95549  ? 55  TYR A CD2 1 
ATOM   659  C  CD2 B TYR A 1 55  ? 1.68972   22.55689 -7.66487  0.300 19.05939  ? 55  TYR A CD2 1 
ATOM   660  C  CE1 A TYR A 1 55  ? -0.37944  23.21490 -9.85635  0.700 22.05925  ? 55  TYR A CE1 1 
ATOM   661  C  CE1 B TYR A 1 55  ? 0.09206   23.92617 -9.44436  0.300 15.79289  ? 55  TYR A CE1 1 
ATOM   662  C  CE2 A TYR A 1 55  ? -0.01224  21.80442 -7.96405  0.700 14.44266  ? 55  TYR A CE2 1 
ATOM   663  C  CE2 B TYR A 1 55  ? 0.32689   22.41533 -7.60683  0.300 14.57768  ? 55  TYR A CE2 1 
ATOM   664  C  CZ  A TYR A 1 55  ? -0.85533  22.31296 -8.93713  0.700 20.89118  ? 55  TYR A CZ  1 
ATOM   665  C  CZ  B TYR A 1 55  ? -0.47129  23.10134 -8.49651  0.300 18.53668  ? 55  TYR A CZ  1 
ATOM   666  O  OH  A TYR A 1 55  ? -2.18379  21.93748 -9.00461  0.700 21.19433  ? 55  TYR A OH  1 
ATOM   667  O  OH  B TYR A 1 55  ? -1.83834  22.94960 -8.41875  0.300 20.94779  ? 55  TYR A OH  1 
ATOM   668  N  N   A ILE A 1 56  ? 6.40196   23.14399 -9.88853  0.700 22.45536  ? 56  ILE A N   1 
ATOM   669  N  N   B ILE A 1 56  ? 6.78218   22.95489 -9.64758  0.300 21.94455  ? 56  ILE A N   1 
ATOM   670  C  CA  A ILE A 1 56  ? 7.59198   23.61907 -10.60017 0.700 24.59912  ? 56  ILE A CA  1 
ATOM   671  C  CA  B ILE A 1 56  ? 8.00856   23.39477 -10.31192 0.300 21.52170  ? 56  ILE A CA  1 
ATOM   672  C  C   A ILE A 1 56  ? 7.87760   22.73362 -11.81172 0.700 19.10588  ? 56  ILE A C   1 
ATOM   673  C  C   B ILE A 1 56  ? 8.23659   22.58853 -11.58424 0.300 19.76145  ? 56  ILE A C   1 
ATOM   674  O  O   A ILE A 1 56  ? 8.15828   23.22965 -12.90929 0.700 21.86703  ? 56  ILE A O   1 
ATOM   675  O  O   B ILE A 1 56  ? 8.51612   23.14365 -12.65236 0.300 25.42875  ? 56  ILE A O   1 
ATOM   676  C  CB  A ILE A 1 56  ? 8.79809   23.71832 -9.65192  0.700 23.87810  ? 56  ILE A CB  1 
ATOM   677  C  CB  B ILE A 1 56  ? 9.20602   23.31401 -9.35190  0.300 23.88053  ? 56  ILE A CB  1 
ATOM   678  C  CG1 A ILE A 1 56  ? 8.49390   24.69580 -8.51423  0.700 28.23125  ? 56  ILE A CG1 1 
ATOM   679  C  CG1 B ILE A 1 56  ? 9.13663   24.44845 -8.33042  0.300 23.03308  ? 56  ILE A CG1 1 
ATOM   680  C  CG2 A ILE A 1 56  ? 10.04644  24.16799 -10.42054 0.700 30.41756  ? 56  ILE A CG2 1 
ATOM   681  C  CG2 B ILE A 1 56  ? 10.51383  23.39455 -10.13033 0.300 28.60097  ? 56  ILE A CG2 1 
ATOM   682  C  CD1 A ILE A 1 56  ? 7.88104   26.01576 -8.97787  0.700 32.07266  ? 56  ILE A CD1 1 
ATOM   683  C  CD1 B ILE A 1 56  ? 9.95508   24.19914 -7.10123  0.300 24.51194  ? 56  ILE A CD1 1 
ATOM   684  N  N   A TRP A 1 57  ? 7.80592   21.41338 -11.62841 0.700 21.40673  ? 57  TRP A N   1 
ATOM   685  N  N   B TRP A 1 57  ? 8.10165   21.26586 -11.48973 0.300 22.68162  ? 57  TRP A N   1 
ATOM   686  C  CA  A TRP A 1 57  ? 7.88444   20.49655 -12.76494 0.700 20.20501  ? 57  TRP A CA  1 
ATOM   687  C  CA  B TRP A 1 57  ? 8.19376   20.42849 -12.68089 0.300 24.08265  ? 57  TRP A CA  1 
ATOM   688  C  C   A TRP A 1 57  ? 6.89796   20.89568 -13.85863 0.700 24.41471  ? 57  TRP A C   1 
ATOM   689  C  C   B TRP A 1 57  ? 7.09486   20.75954 -13.68447 0.300 24.23211  ? 57  TRP A C   1 
ATOM   690  O  O   A TRP A 1 57  ? 7.25661   20.98699 -15.04248 0.700 22.77466  ? 57  TRP A O   1 
ATOM   691  O  O   B TRP A 1 57  ? 7.31336   20.66602 -14.90002 0.300 24.33426  ? 57  TRP A O   1 
ATOM   692  C  CB  A TRP A 1 57  ? 7.63014   19.05986 -12.29778 0.700 20.35747  ? 57  TRP A CB  1 
ATOM   693  C  CB  B TRP A 1 57  ? 8.15184   18.95137 -12.28180 0.300 22.66676  ? 57  TRP A CB  1 
ATOM   694  C  CG  A TRP A 1 57  ? 7.61768   18.09053 -13.43837 0.700 20.84262  ? 57  TRP A CG  1 
ATOM   695  C  CG  B TRP A 1 57  ? 8.01129   18.03968 -13.44580 0.300 23.91955  ? 57  TRP A CG  1 
ATOM   696  C  CD1 A TRP A 1 57  ? 8.69305   17.45419 -13.98598 0.700 32.69338  ? 57  TRP A CD1 1 
ATOM   697  C  CD1 B TRP A 1 57  ? 9.01330   17.40277 -14.12041 0.300 27.58477  ? 57  TRP A CD1 1 
ATOM   698  C  CD2 A TRP A 1 57  ? 6.47722   17.67837 -14.19342 0.700 24.95125  ? 57  TRP A CD2 1 
ATOM   699  C  CD2 B TRP A 1 57  ? 6.79358   17.68260 -14.10120 0.300 20.53194  ? 57  TRP A CD2 1 
ATOM   700  N  NE1 A TRP A 1 57  ? 8.28363   16.65856 -15.02908 0.700 28.16045  ? 57  TRP A NE1 1 
ATOM   701  N  NE1 B TRP A 1 57  ? 8.48573   16.65917 -15.15069 0.300 29.61886  ? 57  TRP A NE1 1 
ATOM   702  C  CE2 A TRP A 1 57  ? 6.92861   16.78304 -15.17993 0.700 29.86494  ? 57  TRP A CE2 1 
ATOM   703  C  CE2 B TRP A 1 57  ? 7.12509   16.81839 -15.16077 0.300 28.71328  ? 57  TRP A CE2 1 
ATOM   704  C  CE3 A TRP A 1 57  ? 5.11158   17.96869 -14.12424 0.700 24.85941  ? 57  TRP A CE3 1 
ATOM   705  C  CE3 B TRP A 1 57  ? 5.44912   18.00353 -13.88790 0.300 22.21687  ? 57  TRP A CE3 1 
ATOM   706  C  CZ2 A TRP A 1 57  ? 6.06429   16.18149 -16.09630 0.700 29.56329  ? 57  TRP A CZ2 1 
ATOM   707  C  CZ2 B TRP A 1 57  ? 6.16186   16.27567 -16.00761 0.300 28.94787  ? 57  TRP A CZ2 1 
ATOM   708  C  CZ3 A TRP A 1 57  ? 4.24695   17.36320 -15.03975 0.700 28.11646  ? 57  TRP A CZ3 1 
ATOM   709  C  CZ3 B TRP A 1 57  ? 4.49612   17.46869 -14.73304 0.300 28.40424  ? 57  TRP A CZ3 1 
ATOM   710  C  CH2 A TRP A 1 57  ? 4.73058   16.48384 -16.00941 0.700 27.33751  ? 57  TRP A CH2 1 
ATOM   711  C  CH2 B TRP A 1 57  ? 4.85631   16.61321 -15.77644 0.300 27.67213  ? 57  TRP A CH2 1 
ATOM   712  N  N   A LEU A 1 58  ? 5.64669   21.14629 -13.47084 0.700 21.60171  ? 58  LEU A N   1 
ATOM   713  N  N   B LEU A 1 58  ? 5.91196   21.14666 -13.20028 0.300 21.58836  ? 58  LEU A N   1 
ATOM   714  C  CA  A LEU A 1 58  ? 4.60378   21.43203 -14.44872 0.700 20.23726  ? 58  LEU A CA  1 
ATOM   715  C  CA  B LEU A 1 58  ? 4.79980   21.42727 -14.10255 0.300 22.31406  ? 58  LEU A CA  1 
ATOM   716  C  C   A LEU A 1 58  ? 4.92169   22.68537 -15.26096 0.700 22.35256  ? 58  LEU A C   1 
ATOM   717  C  C   B LEU A 1 58  ? 5.04536   22.70567 -14.89577 0.300 23.89249  ? 58  LEU A C   1 
ATOM   718  O  O   A LEU A 1 58  ? 4.86721   22.66348 -16.49730 0.700 23.19721  ? 58  LEU A O   1 
ATOM   719  O  O   B LEU A 1 58  ? 4.80772   22.74753 -16.10752 0.300 24.20083  ? 58  LEU A O   1 
ATOM   720  C  CB  A LEU A 1 58  ? 3.26628   21.60105 -13.73702 0.700 22.32374  ? 58  LEU A CB  1 
ATOM   721  C  CB  B LEU A 1 58  ? 3.48614   21.50331 -13.32007 0.300 23.87186  ? 58  LEU A CB  1 
ATOM   722  C  CG  A LEU A 1 58  ? 2.12638   21.99252 -14.66995 0.700 19.54838  ? 58  LEU A CG  1 
ATOM   723  C  CG  B LEU A 1 58  ? 2.17559   21.55382 -14.11577 0.300 23.58157  ? 58  LEU A CG  1 
ATOM   724  C  CD1 A LEU A 1 58  ? 1.77239   20.85098 -15.62164 0.700 20.03656  ? 58  LEU A CD1 1 
ATOM   725  C  CD1 B LEU A 1 58  ? 1.97031   20.29525 -14.95805 0.300 19.62961  ? 58  LEU A CD1 1 
ATOM   726  C  CD2 A LEU A 1 58  ? 0.89958   22.46088 -13.88647 0.700 19.45797  ? 58  LEU A CD2 1 
ATOM   727  C  CD2 B LEU A 1 58  ? 0.98171   21.76892 -13.18584 0.300 17.12702  ? 58  LEU A CD2 1 
ATOM   728  N  N   A ILE A 1 59  ? 5.21325   23.80223 -14.58366 0.700 23.57804  ? 59  ILE A N   1 
ATOM   729  N  N   B ILE A 1 59  ? 5.51892   23.76406 -14.23150 0.300 21.30419  ? 59  ILE A N   1 
ATOM   730  C  CA  A ILE A 1 59  ? 5.40097   25.04793 -15.32640 0.700 27.46836  ? 59  ILE A CA  1 
ATOM   731  C  CA  B ILE A 1 59  ? 5.74545   25.01440 -14.95389 0.300 23.35773  ? 59  ILE A CA  1 
ATOM   732  C  C   A ILE A 1 59  ? 6.61381   24.95621 -16.23945 0.700 29.30415  ? 59  ILE A C   1 
ATOM   733  C  C   B ILE A 1 59  ? 6.86742   24.86385 -15.97202 0.300 29.01865  ? 59  ILE A C   1 
ATOM   734  O  O   A ILE A 1 59  ? 6.59485   25.47880 -17.35946 0.700 29.95593  ? 59  ILE A O   1 
ATOM   735  O  O   B ILE A 1 59  ? 6.83307   25.48491 -17.04135 0.300 31.01781  ? 59  ILE A O   1 
ATOM   736  C  CB  A ILE A 1 59  ? 5.39787   26.31255 -14.43934 0.700 29.38631  ? 59  ILE A CB  1 
ATOM   737  C  CB  B ILE A 1 59  ? 5.97133   26.20327 -14.00030 0.300 21.31051  ? 59  ILE A CB  1 
ATOM   738  C  CG1 A ILE A 1 59  ? 6.47759   26.26487 -13.36226 0.700 28.11489  ? 59  ILE A CG1 1 
ATOM   739  C  CG1 B ILE A 1 59  ? 7.29626   26.06722 -13.24693 0.300 23.79551  ? 59  ILE A CG1 1 
ATOM   740  C  CG2 A ILE A 1 59  ? 4.01753   26.55734 -13.81021 0.700 27.02755  ? 59  ILE A CG2 1 
ATOM   741  C  CG2 B ILE A 1 59  ? 4.80273   26.35104 -13.03964 0.300 23.58288  ? 59  ILE A CG2 1 
ATOM   742  C  CD1 A ILE A 1 59  ? 6.76358   27.63974 -12.76141 0.700 30.49190  ? 59  ILE A CD1 1 
ATOM   743  C  CD1 B ILE A 1 59  ? 7.50831   27.13432 -12.18440 0.300 31.68228  ? 59  ILE A CD1 1 
ATOM   744  N  N   A ILE A 1 60  ? 7.66903   24.26850 -15.80055 0.700 24.50953  ? 60  ILE A N   1 
ATOM   745  N  N   B ILE A 1 60  ? 7.86204   24.02609 -15.67551 0.300 23.63570  ? 60  ILE A N   1 
ATOM   746  C  CA  A ILE A 1 60  ? 8.79759   23.99652 -16.68971 0.700 25.82157  ? 60  ILE A CA  1 
ATOM   747  C  CA  B ILE A 1 60  ? 8.97493   23.83574 -16.60132 0.300 27.00058  ? 60  ILE A CA  1 
ATOM   748  C  C   A ILE A 1 60  ? 8.35790   23.12406 -17.86070 0.700 35.43629  ? 60  ILE A C   1 
ATOM   749  C  C   B ILE A 1 60  ? 8.53719   23.00742 -17.80112 0.300 35.06537  ? 60  ILE A C   1 
ATOM   750  O  O   A ILE A 1 60  ? 8.60684   23.45078 -19.02909 0.700 35.11119  ? 60  ILE A O   1 
ATOM   751  O  O   B ILE A 1 60  ? 8.94467   23.27227 -18.94013 0.300 36.60528  ? 60  ILE A O   1 
ATOM   752  C  CB  A ILE A 1 60  ? 9.96091   23.37571 -15.89156 0.700 27.85720  ? 60  ILE A CB  1 
ATOM   753  C  CB  B ILE A 1 60  ? 10.17142  23.20923 -15.86052 0.300 28.95470  ? 60  ILE A CB  1 
ATOM   754  C  CG1 A ILE A 1 60  ? 10.57821  24.42276 -14.96443 0.700 27.56862  ? 60  ILE A CG1 1 
ATOM   755  C  CG1 B ILE A 1 60  ? 10.67769  24.16017 -14.77442 0.300 26.95397  ? 60  ILE A CG1 1 
ATOM   756  C  CG2 A ILE A 1 60  ? 11.02512  22.77855 -16.82610 0.700 28.98147  ? 60  ILE A CG2 1 
ATOM   757  C  CG2 B ILE A 1 60  ? 11.29156  22.85270 -16.83269 0.300 28.67307  ? 60  ILE A CG2 1 
ATOM   758  C  CD1 A ILE A 1 60  ? 11.54357  23.85586 -13.96284 0.700 32.85705  ? 60  ILE A CD1 1 
ATOM   759  C  CD1 B ILE A 1 60  ? 11.75650  23.57327 -13.90466 0.300 33.56224  ? 60  ILE A CD1 1 
ATOM   760  N  N   . THR A 1 61  ? 7.67786   22.01149 -17.56828 1.000 27.71267  ? 61  THR A N   1 
ATOM   761  C  CA  . THR A 1 61  ? 7.29781   21.07405 -18.62348 1.000 27.17675  ? 61  THR A CA  1 
ATOM   762  C  C   . THR A 1 61  ? 6.31739   21.69853 -19.61324 1.000 32.87030  ? 61  THR A C   1 
ATOM   763  O  O   . THR A 1 61  ? 6.35647   21.38196 -20.80917 1.000 39.82389  ? 61  THR A O   1 
ATOM   764  C  CB  . THR A 1 61  ? 6.67651   19.83698 -17.97406 1.000 31.53455  ? 61  THR A CB  1 
ATOM   765  O  OG1 . THR A 1 61  ? 7.66682   19.17857 -17.16345 1.000 30.07423  ? 61  THR A OG1 1 
ATOM   766  C  CG2 . THR A 1 61  ? 6.13796   18.86241 -19.02120 1.000 34.98651  ? 61  THR A CG2 1 
ATOM   767  N  N   A LEU A 1 62  ? 5.43869   22.59120 -19.14715 0.700 34.80870  ? 62  LEU A N   1 
ATOM   768  N  N   B LEU A 1 62  ? 5.41419   22.55372 -19.11999 0.300 34.99096  ? 62  LEU A N   1 
ATOM   769  C  CA  A LEU A 1 62  ? 4.45252   23.20314 -20.03467 0.700 37.96200  ? 62  LEU A CA  1 
ATOM   770  C  CA  B LEU A 1 62  ? 4.40808   23.22137 -19.93859 0.300 38.17516  ? 62  LEU A CA  1 
ATOM   771  C  C   A LEU A 1 62  ? 5.08720   24.07864 -21.10994 0.700 49.56314  ? 62  LEU A C   1 
ATOM   772  C  C   B LEU A 1 62  ? 5.00676   24.24189 -20.89464 0.300 49.42117  ? 62  LEU A C   1 
ATOM   773  O  O   A LEU A 1 62  ? 4.42230   24.38985 -22.10425 0.700 62.49576  ? 62  LEU A O   1 
ATOM   774  O  O   B LEU A 1 62  ? 4.30144   24.70472 -21.79789 0.300 56.10670  ? 62  LEU A O   1 
ATOM   775  C  CB  A LEU A 1 62  ? 3.43887   24.02167 -19.23158 0.700 36.37291  ? 62  LEU A CB  1 
ATOM   776  C  CB  B LEU A 1 62  ? 3.37033   23.90800 -19.04668 0.300 36.78801  ? 62  LEU A CB  1 
ATOM   777  C  CG  A LEU A 1 62  ? 2.37648   23.20325 -18.49882 0.700 32.35662  ? 62  LEU A CG  1 
ATOM   778  C  CG  B LEU A 1 62  ? 2.41379   23.00815 -18.26350 0.300 32.29455  ? 62  LEU A CG  1 
ATOM   779  C  CD1 A LEU A 1 62  ? 1.44992   24.09550 -17.69250 0.700 30.81758  ? 62  LEU A CD1 1 
ATOM   780  C  CD1 B LEU A 1 62  ? 1.69918   23.80373 -17.18377 0.300 29.89513  ? 62  LEU A CD1 1 
ATOM   781  C  CD2 A LEU A 1 62  ? 1.58628   22.36674 -19.49391 0.700 36.38203  ? 62  LEU A CD2 1 
ATOM   782  C  CD2 B LEU A 1 62  ? 1.40772   22.35160 -19.19637 0.300 34.67682  ? 62  LEU A CD2 1 
ATOM   783  N  N   A GLN A 1 63  ? 6.34562   24.49064 -20.93055 0.700 43.37768  ? 63  GLN A N   1 
ATOM   784  N  N   B GLN A 1 63  ? 6.27347   24.61752 -20.70951 0.300 43.85259  ? 63  GLN A N   1 
ATOM   785  C  CA  A GLN A 1 63  ? 7.02140   25.29764 -21.94555 0.700 55.62301  ? 63  GLN A CA  1 
ATOM   786  C  CA  B GLN A 1 63  ? 6.96911   25.41147 -21.71295 0.300 55.21042  ? 63  GLN A CA  1 
ATOM   787  C  C   A GLN A 1 63  ? 7.06088   24.57717 -23.28808 0.700 62.96674  ? 63  GLN A C   1 
ATOM   788  C  C   B GLN A 1 63  ? 7.17970   24.64578 -23.01331 0.300 62.69041  ? 63  GLN A C   1 
ATOM   789  O  O   A GLN A 1 63  ? 6.76580   25.16779 -24.33354 0.700 67.31348  ? 63  GLN A O   1 
ATOM   790  O  O   B GLN A 1 63  ? 7.55824   25.25741 -24.01823 0.300 67.85138  ? 63  GLN A O   1 
ATOM   791  C  CB  A GLN A 1 63  ? 8.43932   25.62806 -21.48724 0.700 53.11887  ? 63  GLN A CB  1 
ATOM   792  C  CB  B GLN A 1 63  ? 8.30940   25.90830 -21.16224 0.300 52.35032  ? 63  GLN A CB  1 
ATOM   793  C  CG  A GLN A 1 63  ? 8.51179   26.43155 -20.21022 0.700 41.80325  ? 63  GLN A CG  1 
ATOM   794  C  CG  B GLN A 1 63  ? 8.30884   27.36303 -20.69779 0.300 52.58714  ? 63  GLN A CG  1 
ATOM   795  C  CD  A GLN A 1 63  ? 9.88571   26.35181 -19.57713 0.700 55.49044  ? 63  GLN A CD  1 
ATOM   796  C  CD  B GLN A 1 63  ? 7.54459   27.58529 -19.40257 0.300 51.26510  ? 63  GLN A CD  1 
ATOM   797  O  OE1 A GLN A 1 63  ? 10.59842  25.35487 -19.74014 0.700 44.80893  ? 63  GLN A OE1 1 
ATOM   798  O  OE1 B GLN A 1 63  ? 8.13984   27.70920 -18.33037 0.300 50.10585  ? 63  GLN A OE1 1 
ATOM   799  N  NE2 A GLN A 1 63  ? 10.27196  27.40301 -18.85759 0.700 55.36623  ? 63  GLN A NE2 1 
ATOM   800  N  NE2 B GLN A 1 63  ? 6.22139   27.65371 -19.49813 0.300 47.69236  ? 63  GLN A NE2 1 
ATOM   801  N  N   A SER A 1 64  ? 7.43727   23.30187 -23.28065 0.700 71.72021  ? 64  SER A N   1 
ATOM   802  N  N   B SER A 1 64  ? 6.94188   23.33248 -23.01607 0.300 68.95448  ? 64  SER A N   1 
ATOM   803  C  CA  A SER A 1 64  ? 7.44683   22.46626 -24.47954 0.700 75.05684  ? 64  SER A CA  1 
ATOM   804  C  CA  B SER A 1 64  ? 7.03261   22.51987 -24.22254 0.300 73.82439  ? 64  SER A CA  1 
ATOM   805  C  C   A SER A 1 64  ? 6.57925   21.24666 -24.18141 0.700 72.44288  ? 64  SER A C   1 
ATOM   806  C  C   B SER A 1 64  ? 6.21785   21.24220 -24.05970 0.300 72.78947  ? 64  SER A C   1 
ATOM   807  O  O   A SER A 1 64  ? 7.06492   20.22734 -23.68385 0.700 79.77029  ? 64  SER A O   1 
ATOM   808  O  O   B SER A 1 64  ? 6.75471   20.13723 -24.18486 0.300 75.79027  ? 64  SER A O   1 
ATOM   809  C  CB  A SER A 1 64  ? 8.87154   22.07438 -24.87761 0.700 73.86934  ? 64  SER A CB  1 
ATOM   810  C  CB  B SER A 1 64  ? 8.49082   22.17496 -24.52810 0.300 74.98108  ? 64  SER A CB  1 
ATOM   811  O  OG  A SER A 1 64  ? 9.54966   21.44765 -23.80486 0.700 74.95356  ? 64  SER A OG  1 
ATOM   812  O  OG  B SER A 1 64  ? 9.04493   21.36303 -23.50731 0.300 75.50493  ? 64  SER A OG  1 
ATOM   813  N  N   A ILE A 1 65  ? 5.28911   21.36101 -24.48521 0.700 73.87352  ? 65  ILE A N   1 
ATOM   814  N  N   B ILE A 1 65  ? 4.92370   21.38066 -23.78128 0.300 74.32884  ? 65  ILE A N   1 
ATOM   815  C  CA  A ILE A 1 65  ? 4.30963   20.31718 -24.21255 0.700 86.75092  ? 65  ILE A CA  1 
ATOM   816  C  CA  B ILE A 1 65  ? 4.06283   20.22418 -23.54582 0.300 83.31960  ? 65  ILE A CA  1 
ATOM   817  C  C   A ILE A 1 65  ? 3.89913   19.67470 -25.52924 0.700 79.18756  ? 65  ILE A C   1 
ATOM   818  C  C   B ILE A 1 65  ? 3.79526   19.53762 -24.88247 0.300 83.66026  ? 65  ILE A C   1 
ATOM   819  O  O   A ILE A 1 65  ? 3.46339   20.36474 -26.45917 0.700 79.52394  ? 65  ILE A O   1 
ATOM   820  O  O   B ILE A 1 65  ? 3.08414   20.07267 -25.73741 0.300 84.82163  ? 65  ILE A O   1 
ATOM   821  C  CB  A ILE A 1 65  ? 3.08638   20.87573 -23.46558 0.700 88.47969  ? 65  ILE A CB  1 
ATOM   822  C  CB  B ILE A 1 65  ? 2.75830   20.62313 -22.84782 0.300 81.59427  ? 65  ILE A CB  1 
ATOM   823  N  N   A ASN A 1 66  ? 4.03996   18.35462 -25.60428 0.700 81.33571  ? 66  ASN A N   1 
ATOM   824  N  N   B ASN A 1 66  ? 4.36464   18.34760 -25.06333 0.300 84.53891  ? 66  ASN A N   1 
ATOM   825  C  CA  A ASN A 1 66  ? 3.57829   17.58725 -26.75174 0.700 84.97779  ? 66  ASN A CA  1 
ATOM   826  C  CA  B ASN A 1 66  ? 4.17738   17.57236 -26.27986 0.300 84.95003  ? 66  ASN A CA  1 
ATOM   827  C  C   A ASN A 1 66  ? 2.69273   16.45186 -26.26386 0.700 84.98286  ? 66  ASN A C   1 
ATOM   828  C  C   B ASN A 1 66  ? 3.22410   16.39963 -26.10220 0.300 82.89171  ? 66  ASN A C   1 
ATOM   829  O  O   A ASN A 1 66  ? 1.79658   15.99683 -26.98270 0.700 90.13984  ? 66  ASN A O   1 
ATOM   830  O  O   B ASN A 1 66  ? 2.86085   15.76411 -27.09733 0.300 85.05011  ? 66  ASN A O   1 
ATOM   831  C  CB  A ASN A 1 66  ? 4.76535   17.02569 -27.53748 0.700 89.58481  ? 66  ASN A CB  1 
ATOM   832  C  CB  B ASN A 1 66  ? 5.52647   17.05588 -26.79617 0.300 89.87354  ? 66  ASN A CB  1 
ATOM   833  N  N   A GLU A 1 67  ? 2.93762   15.99624 -25.03925 0.700 65.34308  ? 67  GLU A N   1 
ATOM   834  N  N   B GLU A 1 67  ? 2.81487   16.09435 -24.87267 0.300 66.04747  ? 67  GLU A N   1 
ATOM   835  C  CA  A GLU A 1 67  ? 2.20687   14.88517 -24.45513 0.700 58.42746  ? 67  GLU A CA  1 
ATOM   836  C  CA  B GLU A 1 67  ? 1.91788   14.97867 -24.61724 0.300 59.65329  ? 67  GLU A CA  1 
ATOM   837  C  C   A GLU A 1 67  ? 1.17442   15.39429 -23.45374 0.700 48.92067  ? 67  GLU A C   1 
ATOM   838  C  C   B GLU A 1 67  ? 0.95324   15.33840 -23.49669 0.300 49.02878  ? 67  GLU A C   1 
ATOM   839  O  O   A GLU A 1 67  ? 1.32164   16.45922 -22.84656 0.700 41.40564  ? 67  GLU A O   1 
ATOM   840  O  O   B GLU A 1 67  ? 1.05180   16.39297 -22.86321 0.300 40.57324  ? 67  GLU A O   1 
ATOM   841  C  CB  A GLU A 1 67  ? 3.16219   13.90208 -23.76222 0.700 68.29717  ? 67  GLU A CB  1 
ATOM   842  C  CB  B GLU A 1 67  ? 2.68229   13.69295 -24.26782 0.300 62.76063  ? 67  GLU A CB  1 
ATOM   843  C  CG  A GLU A 1 67  ? 2.57076   12.50917 -23.49637 0.700 67.68563  ? 67  GLU A CG  1 
ATOM   844  C  CG  B GLU A 1 67  ? 3.23303   12.93697 -25.46620 0.300 64.00234  ? 67  GLU A CG  1 
ATOM   845  C  CD  A GLU A 1 67  ? 3.38550   11.68779 -22.50030 0.700 66.04398  ? 67  GLU A CD  1 
ATOM   846  C  CD  B GLU A 1 67  ? 4.01656   11.70100 -25.06638 0.300 64.95216  ? 67  GLU A CD  1 
ATOM   847  O  OE1 A GLU A 1 67  ? 4.30984   12.24705 -21.86956 0.700 60.32688  ? 67  GLU A OE1 1 
ATOM   848  O  OE1 B GLU A 1 67  ? 3.72687   11.12639 -23.99523 0.300 66.69562  ? 67  GLU A OE1 1 
ATOM   849  O  OE2 A GLU A 1 67  ? 3.09475   10.48027 -22.34394 0.700 63.01969  ? 67  GLU A OE2 1 
ATOM   850  O  OE2 B GLU A 1 67  ? 4.92892   11.30764 -25.82184 0.300 61.67284  ? 67  GLU A OE2 1 
ATOM   851  N  N   A ASP A 1 68  ? 0.11435   14.62119 -23.30100 0.700 42.58049  ? 68  ASP A N   1 
ATOM   852  N  N   B ASP A 1 68  ? 0.01130   14.43402 -23.26167 0.300 43.85961  ? 68  ASP A N   1 
ATOM   853  C  CA  A ASP A 1 68  ? -0.86643  14.86561 -22.25554 0.700 35.69710  ? 68  ASP A CA  1 
ATOM   854  C  CA  B ASP A 1 68  ? -0.95496  14.58318 -22.18575 0.300 35.71029  ? 68  ASP A CA  1 
ATOM   855  C  C   A ASP A 1 68  ? -0.21758  14.46220 -20.93404 0.700 35.19574  ? 68  ASP A C   1 
ATOM   856  C  C   B ASP A 1 68  ? -0.30405  14.13551 -20.88083 0.300 35.22180  ? 68  ASP A C   1 
ATOM   857  O  O   A ASP A 1 68  ? -0.12697  13.27545 -20.61140 0.700 35.22568  ? 68  ASP A O   1 
ATOM   858  O  O   B ASP A 1 68  ? 0.06710   12.96655 -20.73673 0.300 37.50712  ? 68  ASP A O   1 
ATOM   859  C  CB  A ASP A 1 68  ? -2.09868  14.02665 -22.56565 0.700 35.97928  ? 68  ASP A CB  1 
ATOM   860  C  CB  B ASP A 1 68  ? -2.17489  13.72733 -22.50679 0.300 35.99911  ? 68  ASP A CB  1 
ATOM   861  C  CG  A ASP A 1 68  ? -3.17512  14.14578 -21.51722 0.700 35.57395  ? 68  ASP A CG  1 
ATOM   862  C  CG  B ASP A 1 68  ? -3.25664  13.86147 -21.47862 0.300 35.60042  ? 68  ASP A CG  1 
ATOM   863  O  OD1 A ASP A 1 68  ? -2.87556  14.49025 -20.34942 0.700 35.04250  ? 68  ASP A OD1 1 
ATOM   864  O  OD1 B ASP A 1 68  ? -3.06671  14.65039 -20.53508 0.300 35.10216  ? 68  ASP A OD1 1 
ATOM   865  O  OD2 A ASP A 1 68  ? -4.33268  13.86573 -21.88443 0.700 35.80361  ? 68  ASP A OD2 1 
ATOM   866  O  OD2 B ASP A 1 68  ? -4.28899  13.17701 -21.61387 0.300 35.78739  ? 68  ASP A OD2 1 
ATOM   867  N  N   A ILE A 1 69  ? 0.21721   15.45180 -20.14487 0.700 34.72754  ? 69  ILE A N   1 
ATOM   868  N  N   B ILE A 1 69  ? -0.19895  15.05160 -19.91756 0.300 34.70334  ? 69  ILE A N   1 
ATOM   869  C  CA  A ILE A 1 69  ? 0.98762   15.19356 -18.92957 0.700 34.25026  ? 69  ILE A CA  1 
ATOM   870  C  CA  B ILE A 1 69  ? 0.68569   14.88122 -18.77329 0.300 34.23914  ? 69  ILE A CA  1 
ATOM   871  C  C   A ILE A 1 69  ? 0.11501   14.99409 -17.69756 0.700 33.80853  ? 69  ILE A C   1 
ATOM   872  C  C   B ILE A 1 69  ? -0.03985  14.87281 -17.43185 0.300 33.72339  ? 69  ILE A C   1 
ATOM   873  O  O   A ILE A 1 69  ? 0.62993   14.94889 -16.57451 0.700 33.35016  ? 69  ILE A O   1 
ATOM   874  O  O   B ILE A 1 69  ? 0.61985   14.80242 -16.38629 0.300 33.29552  ? 69  ILE A O   1 
ATOM   875  C  CB  A ILE A 1 69  ? 2.04670   16.28871 -18.68753 0.700 33.97313  ? 69  ILE A CB  1 
ATOM   876  C  CB  B ILE A 1 69  ? 1.84116   15.90737 -18.79381 0.300 34.07366  ? 69  ILE A CB  1 
ATOM   877  C  CG1 A ILE A 1 69  ? 1.44477   17.70286 -18.81135 0.700 33.84646  ? 69  ILE A CG1 1 
ATOM   878  C  CG1 B ILE A 1 69  ? 3.15533   15.25536 -18.35728 0.300 33.98306  ? 69  ILE A CG1 1 
ATOM   879  C  CG2 A ILE A 1 69  ? 3.21081   16.12061 -19.67797 0.700 34.36363  ? 69  ILE A CG2 1 
ATOM   880  C  CG2 B ILE A 1 69  ? 1.49564   17.18066 -18.01049 0.300 33.59423  ? 69  ILE A CG2 1 
ATOM   881  C  CD1 A ILE A 1 69  ? 0.36730   18.08851 -17.79784 0.700 33.41639  ? 69  ILE A CD1 1 
ATOM   882  C  CD1 B ILE A 1 69  ? 3.71105   14.26994 -19.36827 0.300 35.38471  ? 69  ILE A CD1 1 
ATOM   883  N  N   A THR A 1 70  ? -1.20412  14.89298 -17.88999 0.700 23.36382  ? 70  THR A N   1 
ATOM   884  N  N   B THR A 1 70  ? -1.37929  14.89008 -17.41948 0.300 19.82159  ? 70  THR A N   1 
ATOM   885  C  CA  A THR A 1 70  ? -2.10633  14.88120 -16.74050 0.700 19.76693  ? 70  THR A CA  1 
ATOM   886  C  CA  B THR A 1 70  ? -2.08758  14.87670 -16.14039 0.300 20.82727  ? 70  THR A CA  1 
ATOM   887  C  C   A THR A 1 70  ? -1.75526  13.76452 -15.76442 0.700 19.03926  ? 70  THR A C   1 
ATOM   888  C  C   B THR A 1 70  ? -1.90398  13.56862 -15.37934 0.300 24.59665  ? 70  THR A C   1 
ATOM   889  O  O   A THR A 1 70  ? -1.79187  13.96629 -14.54281 0.700 17.94915  ? 70  THR A O   1 
ATOM   890  O  O   B THR A 1 70  ? -2.18395  13.52150 -14.17531 0.300 24.33264  ? 70  THR A O   1 
ATOM   891  C  CB  A THR A 1 70  ? -3.57003  14.78535 -17.18800 0.700 23.18302  ? 70  THR A CB  1 
ATOM   892  C  CB  B THR A 1 70  ? -3.57499  15.24990 -16.28902 0.300 27.81760  ? 70  THR A CB  1 
ATOM   893  O  OG1 A THR A 1 70  ? -3.82988  15.75788 -18.21684 0.700 19.95900  ? 70  THR A OG1 1 
ATOM   894  O  OG1 B THR A 1 70  ? -4.39485  14.31603 -15.57335 0.300 28.45759  ? 70  THR A OG1 1 
ATOM   895  C  CG2 A THR A 1 70  ? -4.51759  15.03870 -16.00947 0.700 23.01455  ? 70  THR A CG2 1 
ATOM   896  C  CG2 B THR A 1 70  ? -3.99983  15.27960 -17.72775 0.300 25.82291  ? 70  THR A CG2 1 
ATOM   897  N  N   A TYR A 1 71  ? -1.33146  12.60186 -16.28665 0.700 18.78091  ? 71  TYR A N   1 
ATOM   898  N  N   B TYR A 1 71  ? -1.42695  12.50993 -16.04110 0.300 21.42236  ? 71  TYR A N   1 
ATOM   899  C  CA  A TYR A 1 71  ? -1.08210  11.42232 -15.45217 0.700 22.38388  ? 71  TYR A CA  1 
ATOM   900  C  CA  B TYR A 1 71  ? -1.06653  11.30016 -15.31095 0.300 21.81525  ? 71  TYR A CA  1 
ATOM   901  C  C   A TYR A 1 71  ? -0.02623  11.67515 -14.37231 0.700 19.06035  ? 71  TYR A C   1 
ATOM   902  C  C   B TYR A 1 71  ? 0.13535   11.52555 -14.40273 0.300 19.53421  ? 71  TYR A C   1 
ATOM   903  O  O   A TYR A 1 71  ? -0.04304  11.02800 -13.31704 0.700 16.91303  ? 71  TYR A O   1 
ATOM   904  O  O   B TYR A 1 71  ? 0.36970   10.72026 -13.48919 0.300 21.11608  ? 71  TYR A O   1 
ATOM   905  C  CB  A TYR A 1 71  ? -0.66298  10.25336 -16.35138 0.700 23.71333  ? 71  TYR A CB  1 
ATOM   906  C  CB  B TYR A 1 71  ? -0.82657  10.12367 -16.26975 0.300 24.07906  ? 71  TYR A CB  1 
ATOM   907  C  CG  A TYR A 1 71  ? 0.74417   10.38656 -16.90429 0.700 24.17115  ? 71  TYR A CG  1 
ATOM   908  C  CG  B TYR A 1 71  ? 0.49598   10.16644 -17.00621 0.300 25.56725  ? 71  TYR A CG  1 
ATOM   909  C  CD1 A TYR A 1 71  ? 1.00324   11.13201 -18.05155 0.700 25.37719  ? 71  TYR A CD1 1 
ATOM   910  C  CD1 B TYR A 1 71  ? 0.62778   10.86679 -18.19864 0.300 24.89018  ? 71  TYR A CD1 1 
ATOM   911  C  CD2 A TYR A 1 71  ? 1.81184   9.76938  -16.26705 0.700 23.37023  ? 71  TYR A CD2 1 
ATOM   912  C  CD2 B TYR A 1 71  ? 1.60988   9.49831  -16.51147 0.300 24.18797  ? 71  TYR A CD2 1 
ATOM   913  C  CE1 A TYR A 1 71  ? 2.30200   11.25047 -18.54532 0.700 28.00350  ? 71  TYR A CE1 1 
ATOM   914  C  CE1 B TYR A 1 71  ? 1.83293   10.90657 -18.87356 0.300 29.37074  ? 71  TYR A CE1 1 
ATOM   915  C  CE2 A TYR A 1 71  ? 3.09920   9.87549  -16.75051 0.700 24.60317  ? 71  TYR A CE2 1 
ATOM   916  C  CE2 B TYR A 1 71  ? 2.82003   9.53526  -17.17942 0.300 25.68648  ? 71  TYR A CE2 1 
ATOM   917  C  CZ  A TYR A 1 71  ? 3.34065   10.61808 -17.88469 0.700 34.18865  ? 71  TYR A CZ  1 
ATOM   918  C  CZ  B TYR A 1 71  ? 2.92449   10.24003 -18.35913 0.300 35.25480  ? 71  TYR A CZ  1 
ATOM   919  O  OH  A TYR A 1 71  ? 4.62529   10.73045 -18.36454 0.700 34.24388  ? 71  TYR A OH  1 
ATOM   920  O  OH  B TYR A 1 71  ? 4.12663   10.28024 -19.03016 0.300 29.76366  ? 71  TYR A OH  1 
ATOM   921  N  N   . VAL A 1 72  ? 0.90763   12.59604 -14.63040 1.000 20.15281  ? 72  VAL A N   1 
ATOM   922  C  CA  . VAL A 1 72  ? 2.00752   12.85951 -13.69438 1.000 18.89165  ? 72  VAL A CA  1 
ATOM   923  C  C   . VAL A 1 72  ? 1.48433   13.34191 -12.35204 1.000 20.40288  ? 72  VAL A C   1 
ATOM   924  O  O   . VAL A 1 72  ? 2.13197   13.13257 -11.30697 1.000 21.95754  ? 72  VAL A O   1 
ATOM   925  C  CB  . VAL A 1 72  ? 3.01794   13.83479 -14.33101 1.000 21.04381  ? 72  VAL A CB  1 
ATOM   926  C  CG1 . VAL A 1 72  ? 4.11428   14.21172 -13.31951 1.000 23.51991  ? 72  VAL A CG1 1 
ATOM   927  C  CG2 . VAL A 1 72  ? 3.63531   13.17782 -15.56572 1.000 22.23427  ? 72  VAL A CG2 1 
ATOM   928  N  N   A ARG A 1 73  ? 0.30698   13.99229 -12.34587 0.700 16.99051  ? 73  ARG A N   1 
ATOM   929  N  N   B ARG A 1 73  ? 0.30309   13.96657 -12.34211 0.300 17.22672  ? 73  ARG A N   1 
ATOM   930  C  CA  A ARG A 1 73  ? -0.29748  14.41075 -11.08207 0.700 19.52587  ? 73  ARG A CA  1 
ATOM   931  C  CA  B ARG A 1 73  ? -0.28657  14.42159 -11.09017 0.300 20.06875  ? 73  ARG A CA  1 
ATOM   932  C  C   A ARG A 1 73  ? -0.45039  13.24453 -10.12022 0.700 19.23552  ? 73  ARG A C   1 
ATOM   933  C  C   B ARG A 1 73  ? -0.56168  13.27100 -10.13036 0.300 19.52732  ? 73  ARG A C   1 
ATOM   934  O  O   A ARG A 1 73  ? -0.35825  13.42733 -8.89941  0.700 17.67996  ? 73  ARG A O   1 
ATOM   935  O  O   B ARG A 1 73  ? -0.66094  13.50287 -8.91753  0.300 18.77221  ? 73  ARG A O   1 
ATOM   936  C  CB  A ARG A 1 73  ? -1.67095  15.05038 -11.32314 0.700 19.31131  ? 73  ARG A CB  1 
ATOM   937  C  CB  B ARG A 1 73  ? -1.57602  15.18346 -11.38664 0.300 20.17870  ? 73  ARG A CB  1 
ATOM   938  C  CG  A ARG A 1 73  ? -1.62740  16.41464 -12.02494 0.700 18.05907  ? 73  ARG A CG  1 
ATOM   939  C  CG  B ARG A 1 73  ? -2.00746  16.13909 -10.29979 0.300 26.40283  ? 73  ARG A CG  1 
ATOM   940  C  CD  A ARG A 1 73  ? -3.01260  16.99048 -12.31935 0.700 20.50942  ? 73  ARG A CD  1 
ATOM   941  C  CD  B ARG A 1 73  ? -3.15504  17.01839 -10.78917 0.300 27.28085  ? 73  ARG A CD  1 
ATOM   942  N  NE  A ARG A 1 73  ? -2.94214  18.15721 -13.18923 0.700 19.51294  ? 73  ARG A NE  1 
ATOM   943  N  NE  B ARG A 1 73  ? -2.74309  17.88567 -11.89009 0.300 25.90168  ? 73  ARG A NE  1 
ATOM   944  C  CZ  A ARG A 1 73  ? -2.71844  19.39380 -12.76597 0.700 21.46126  ? 73  ARG A CZ  1 
ATOM   945  C  CZ  B ARG A 1 73  ? -2.60720  19.20300 -11.80011 0.300 20.64778  ? 73  ARG A CZ  1 
ATOM   946  N  NH1 A ARG A 1 73  ? -2.55926  19.66398 -11.47511 0.700 18.38094  ? 73  ARG A NH1 1 
ATOM   947  N  NH1 B ARG A 1 73  ? -2.85000  19.85165 -10.67143 0.300 24.83413  ? 73  ARG A NH1 1 
ATOM   948  N  NH2 A ARG A 1 73  ? -2.59952  20.36981 -13.66011 0.700 18.17267  ? 73  ARG A NH2 1 
ATOM   949  N  NH2 B ARG A 1 73  ? -2.23939  19.89237 -12.87668 0.300 19.52543  ? 73  ARG A NH2 1 
ATOM   950  N  N   . TYR A 1 74  ? -0.68585  12.03941 -10.64423 1.000 17.59195  ? 74  TYR A N   1 
ATOM   951  C  CA  . TYR A 1 74  ? -0.88219  10.87823 -9.77497  1.000 17.08334  ? 74  TYR A CA  1 
ATOM   952  C  C   . TYR A 1 74  ? 0.34948   10.54942 -8.93492  1.000 17.89059  ? 74  TYR A C   1 
ATOM   953  O  O   . TYR A 1 74  ? 0.22356   9.98068  -7.84724  1.000 19.26855  ? 74  TYR A O   1 
ATOM   954  C  CB  . TYR A 1 74  ? -1.32227  9.67303  -10.61278 1.000 18.37522  ? 74  TYR A CB  1 
ATOM   955  C  CG  . TYR A 1 74  ? -2.75489  9.80526  -11.06544 1.000 18.29511  ? 74  TYR A CG  1 
ATOM   956  C  CD1 . TYR A 1 74  ? -3.09830  10.63144 -12.13324 1.000 21.51068  ? 74  TYR A CD1 1 
ATOM   957  C  CD2 . TYR A 1 74  ? -3.78859  9.12648  -10.38903 1.000 18.34247  ? 74  TYR A CD2 1 
ATOM   958  C  CE1 . TYR A 1 74  ? -4.43697  10.76834 -12.53343 1.000 21.06582  ? 74  TYR A CE1 1 
ATOM   959  C  CE2 . TYR A 1 74  ? -5.09819  9.24678  -10.78134 1.000 21.76562  ? 74  TYR A CE2 1 
ATOM   960  C  CZ  . TYR A 1 74  ? -5.41948  10.05572 -11.85305 1.000 22.65217  ? 74  TYR A CZ  1 
ATOM   961  O  OH  . TYR A 1 74  ? -6.71765  10.17527 -12.22393 1.000 23.29243  ? 74  TYR A OH  1 
ATOM   962  N  N   . PHE A 1 75  ? 1.54323   10.87454 -9.42207  1.000 21.83347  ? 75  PHE A N   1 
ATOM   963  C  CA  . PHE A 1 75  ? 2.74778   10.65123 -8.62068  1.000 20.99486  ? 75  PHE A CA  1 
ATOM   964  C  C   . PHE A 1 75  ? 2.77752   11.57139 -7.41133  1.000 22.60471  ? 75  PHE A C   1 
ATOM   965  O  O   . PHE A 1 75  ? 3.36902   11.22398 -6.37712  1.000 25.00391  ? 75  PHE A O   1 
ATOM   966  C  CB  . PHE A 1 75  ? 3.98246   10.78001 -9.52194  1.000 24.39087  ? 75  PHE A CB  1 
ATOM   967  C  CG  . PHE A 1 75  ? 3.94703   9.85109  -10.70525 1.000 25.63170  ? 75  PHE A CG  1 
ATOM   968  C  CD1 . PHE A 1 75  ? 3.47854   8.54963  -10.56981 1.000 35.44764  ? 75  PHE A CD1 1 
ATOM   969  C  CD2 . PHE A 1 75  ? 4.32244   10.28353 -11.95221 1.000 26.31272  ? 75  PHE A CD2 1 
ATOM   970  C  CE1 . PHE A 1 75  ? 3.42929   7.68784  -11.67934 1.000 37.76402  ? 75  PHE A CE1 1 
ATOM   971  C  CE2 . PHE A 1 75  ? 4.28944   9.42351  -13.05760 1.000 30.70903  ? 75  PHE A CE2 1 
ATOM   972  C  CZ  . PHE A 1 75  ? 3.83852   8.14080  -12.92302 1.000 33.34279  ? 75  PHE A CZ  1 
ATOM   973  N  N   A ASP A 1 76  ? 2.16092   12.74589 -7.52783  0.700 19.59647  ? 76  ASP A N   1 
ATOM   974  N  N   B ASP A 1 76  ? 2.12628   12.72605 -7.50468  0.300 19.70456  ? 76  ASP A N   1 
ATOM   975  C  CA  A ASP A 1 76  ? 1.91577   13.60194 -6.37166  0.700 20.17182  ? 76  ASP A CA  1 
ATOM   976  C  CA  B ASP A 1 76  ? 1.99646   13.63032 -6.36776  0.300 20.36355  ? 76  ASP A CA  1 
ATOM   977  C  C   A ASP A 1 76  ? 0.83861   12.97870 -5.49433  0.700 18.24270  ? 76  ASP A C   1 
ATOM   978  C  C   B ASP A 1 76  ? 0.78171   13.26987 -5.51969  0.300 20.49191  ? 76  ASP A C   1 
ATOM   979  O  O   A ASP A 1 76  ? 1.06679   12.67536 -4.31750  0.700 14.84341  ? 76  ASP A O   1 
ATOM   980  O  O   B ASP A 1 76  ? 0.79861   13.44345 -4.29499  0.300 24.69691  ? 76  ASP A O   1 
ATOM   981  C  CB  A ASP A 1 76  ? 1.47400   14.97438 -6.91755  0.700 21.98219  ? 76  ASP A CB  1 
ATOM   982  C  CB  B ASP A 1 76  ? 1.90945   15.07045 -6.88678  0.300 23.84628  ? 76  ASP A CB  1 
ATOM   983  C  CG  A ASP A 1 76  ? 0.85363   15.92679 -5.86996  0.700 31.22968  ? 76  ASP A CG  1 
ATOM   984  C  CG  B ASP A 1 76  ? 1.45915   16.06016 -5.83331  0.300 22.89845  ? 76  ASP A CG  1 
ATOM   985  O  OD1 A ASP A 1 76  ? 0.36712   15.52465 -4.78149  0.700 22.35576  ? 76  ASP A OD1 1 
ATOM   986  O  OD1 B ASP A 1 76  ? 0.28390   16.00755 -5.40124  0.300 31.99199  ? 76  ASP A OD1 1 
ATOM   987  O  OD2 A ASP A 1 76  ? 0.80976   17.14316 -6.18472  0.700 26.01521  ? 76  ASP A OD2 1 
ATOM   988  O  OD2 B ASP A 1 76  ? 2.27674   16.91714 -5.44681  0.300 31.62075  ? 76  ASP A OD2 1 
ATOM   989  N  N   A TRP A 1 77  ? -0.35057  12.77161 -6.06072  0.700 18.42495  ? 77  TRP A N   1 
ATOM   990  N  N   B TRP A 1 77  ? -0.28431  12.78018 -6.15534  0.300 18.11200  ? 77  TRP A N   1 
ATOM   991  C  CA  A TRP A 1 77  ? -1.50620  12.39880 -5.24018  0.700 15.10024  ? 77  TRP A CA  1 
ATOM   992  C  CA  B TRP A 1 77  ? -1.45894  12.34645 -5.40016  0.300 16.73529  ? 77  TRP A CA  1 
ATOM   993  C  C   A TRP A 1 77  ? -1.32357  11.07504 -4.48684  0.700 15.59088  ? 77  TRP A C   1 
ATOM   994  C  C   B TRP A 1 77  ? -1.12125  11.19402 -4.46904  0.300 17.03609  ? 77  TRP A C   1 
ATOM   995  O  O   A TRP A 1 77  ? -1.91000  10.89838 -3.40479  0.700 15.44915  ? 77  TRP A O   1 
ATOM   996  O  O   B TRP A 1 77  ? -1.35817  11.26523 -3.25492  0.300 17.19936  ? 77  TRP A O   1 
ATOM   997  C  CB  A TRP A 1 77  ? -2.75341  12.29836 -6.11589  0.700 15.56559  ? 77  TRP A CB  1 
ATOM   998  C  CB  B TRP A 1 77  ? -2.56158  11.90922 -6.36160  0.300 14.88703  ? 77  TRP A CB  1 
ATOM   999  C  CG  A TRP A 1 77  ? -3.14499  13.53515 -6.84967  0.700 17.05037  ? 77  TRP A CG  1 
ATOM   1000 C  CG  B TRP A 1 77  ? -3.18276  13.04520 -7.08013  0.300 14.25644  ? 77  TRP A CG  1 
ATOM   1001 C  CD1 A TRP A 1 77  ? -2.71365  14.82285 -6.62526  0.700 16.61967  ? 77  TRP A CD1 1 
ATOM   1002 C  CD1 B TRP A 1 77  ? -2.88434  14.37106 -6.92899  0.300 21.05310  ? 77  TRP A CD1 1 
ATOM   1003 C  CD2 A TRP A 1 77  ? -4.05378  13.60016 -7.94560  0.700 14.68406  ? 77  TRP A CD2 1 
ATOM   1004 C  CD2 B TRP A 1 77  ? -4.20649  12.97562 -8.07736  0.300 13.87517  ? 77  TRP A CD2 1 
ATOM   1005 N  NE1 A TRP A 1 77  ? -3.31559  15.67975 -7.52055  0.700 16.71385  ? 77  TRP A NE1 1 
ATOM   1006 N  NE1 B TRP A 1 77  ? -3.65541  15.12714 -7.76756  0.300 17.91404  ? 77  TRP A NE1 1 
ATOM   1007 C  CE2 A TRP A 1 77  ? -4.14542  14.95945 -8.34449  0.700 16.89920  ? 77  TRP A CE2 1 
ATOM   1008 C  CE2 B TRP A 1 77  ? -4.47832  14.29817 -8.48564  0.300 13.78178  ? 77  TRP A CE2 1 
ATOM   1009 C  CE3 A TRP A 1 77  ? -4.79878  12.63724 -8.63811  0.700 16.76037  ? 77  TRP A CE3 1 
ATOM   1010 C  CE3 B TRP A 1 77  ? -4.91209  11.92966 -8.67184  0.300 11.92064  ? 77  TRP A CE3 1 
ATOM   1011 C  CZ2 A TRP A 1 77  ? -4.96489  15.37451 -9.39824  0.700 19.01953  ? 77  TRP A CZ2 1 
ATOM   1012 C  CZ2 B TRP A 1 77  ? -5.42986  14.60500 -9.45116  0.300 16.38501  ? 77  TRP A CZ2 1 
ATOM   1013 C  CZ3 A TRP A 1 77  ? -5.62832  13.05780 -9.68877  0.700 19.40738  ? 77  TRP A CZ3 1 
ATOM   1014 C  CZ3 B TRP A 1 77  ? -5.88606  12.24739 -9.63967  0.300 15.05241  ? 77  TRP A CZ3 1 
ATOM   1015 C  CH2 A TRP A 1 77  ? -5.68403  14.41755 -10.06700 0.700 21.62776  ? 77  TRP A CH2 1 
ATOM   1016 C  CH2 B TRP A 1 77  ? -6.12105  13.56664 -10.01916 0.300 19.01225  ? 77  TRP A CH2 1 
ATOM   1017 N  N   . VAL A 1 78  ? -0.54141  10.12501 -5.02905  1.000 16.23593  ? 78  VAL A N   1 
ATOM   1018 C  CA  . VAL A 1 78  ? -0.35331  8.86490  -4.32344  1.000 17.06107  ? 78  VAL A CA  1 
ATOM   1019 C  C   . VAL A 1 78  ? 0.43314   9.06001  -3.02601  1.000 19.93742  ? 78  VAL A C   1 
ATOM   1020 O  O   . VAL A 1 78  ? 0.27932   8.27023  -2.08421  1.000 20.63786  ? 78  VAL A O   1 
ATOM   1021 C  CB  . VAL A 1 78  ? 0.27404   7.82627  -5.27772  1.000 21.86093  ? 78  VAL A CB  1 
ATOM   1022 C  CG1 . VAL A 1 78  ? 1.73849   8.11827  -5.47393  1.000 21.83766  ? 78  VAL A CG1 1 
ATOM   1023 C  CG2 . VAL A 1 78  ? 0.00722   6.39376  -4.79921  1.000 33.48062  ? 78  VAL A CG2 1 
ATOM   1024 N  N   . LEU A 1 79  ? 1.24425   10.12143 -2.93776  1.000 19.20475  ? 79  LEU A N   1 
ATOM   1025 C  CA  . LEU A 1 79  ? 1.96715   10.46722 -1.71279  1.000 21.48639  ? 79  LEU A CA  1 
ATOM   1026 C  C   . LEU A 1 79  ? 1.15755   11.41946 -0.83564  1.000 21.53354  ? 79  LEU A C   1 
ATOM   1027 O  O   . LEU A 1 79  ? 1.11757   11.26156 0.39924   1.000 20.85178  ? 79  LEU A O   1 
ATOM   1028 C  CB  . LEU A 1 79  ? 3.28655   11.15342 -2.08483  1.000 20.35648  ? 79  LEU A CB  1 
ATOM   1029 C  CG  . LEU A 1 79  ? 4.17608   10.34008 -3.00871  1.000 22.11846  ? 79  LEU A CG  1 
ATOM   1030 C  CD1 . LEU A 1 79  ? 5.46374   11.12030 -3.29162  1.000 24.60986  ? 79  LEU A CD1 1 
ATOM   1031 C  CD2 . LEU A 1 79  ? 4.45252   8.93866  -2.43785  1.000 31.47633  ? 79  LEU A CD2 1 
ATOM   1032 N  N   . THR A 1 80  ? 0.52067   12.42606 -1.43337  1.000 18.06868  ? 80  THR A N   1 
ATOM   1033 C  CA  . THR A 1 80  ? -0.09275  13.48129 -0.61875  1.000 17.44359  ? 80  THR A CA  1 
ATOM   1034 C  C   . THR A 1 80  ? -1.44347  13.07217 -0.06219  1.000 20.09473  ? 80  THR A C   1 
ATOM   1035 O  O   . THR A 1 80  ? -1.76911  13.41428 1.08942   1.000 18.23194  ? 80  THR A O   1 
ATOM   1036 C  CB  . THR A 1 80  ? -0.18909  14.80364 -1.37801  1.000 16.20640  ? 80  THR A CB  1 
ATOM   1037 O  OG1 . THR A 1 80  ? -0.91402  14.59630 -2.58736  1.000 18.08449  ? 80  THR A OG1 1 
ATOM   1038 C  CG2 . THR A 1 80  ? 1.19858   15.36925 -1.70137  1.000 20.95592  ? 80  THR A CG2 1 
ATOM   1039 N  N   . THR A 1 81  ? -2.28149  12.39961 -0.86588  1.000 17.18224  ? 81  THR A N   1 
ATOM   1040 C  CA  . THR A 1 81  ? -3.64149  12.13028 -0.39382  1.000 17.66244  ? 81  THR A CA  1 
ATOM   1041 C  C   . THR A 1 81  ? -3.70122  11.21940 0.83623   1.000 16.45904  ? 81  THR A C   1 
ATOM   1042 O  O   . THR A 1 81  ? -4.53223  11.49409 1.72100   1.000 17.26130  ? 81  THR A O   1 
ATOM   1043 C  CB  . THR A 1 81  ? -4.56948  11.67662 -1.53823  1.000 16.06811  ? 81  THR A CB  1 
ATOM   1044 O  OG1 . THR A 1 81  ? -4.07677  10.44979 -2.08654  1.000 16.08667  ? 81  THR A OG1 1 
ATOM   1045 C  CG2 . THR A 1 81  ? -4.63949  12.76012 -2.66167  1.000 18.52346  ? 81  THR A CG2 1 
ATOM   1046 N  N   . PRO A 1 82  ? -2.86680  10.18601 1.00410   1.000 16.48988  ? 82  PRO A N   1 
ATOM   1047 C  CA  . PRO A 1 82  ? -2.94092  9.45559  2.28435   1.000 18.42847  ? 82  PRO A CA  1 
ATOM   1048 C  C   . PRO A 1 82  ? -2.57716  10.32754 3.46593   1.000 20.04502  ? 82  PRO A C   1 
ATOM   1049 O  O   . PRO A 1 82  ? -3.22263  10.23436 4.52516   1.000 18.35896  ? 82  PRO A O   1 
ATOM   1050 C  CB  . PRO A 1 82  ? -1.98974  8.26467  2.11393   1.000 18.38718  ? 82  PRO A CB  1 
ATOM   1051 C  CG  . PRO A 1 82  ? -1.05119  8.65907  0.98800   1.000 17.94771  ? 82  PRO A CG  1 
ATOM   1052 C  CD  . PRO A 1 82  ? -1.92877  9.52693  0.06844   1.000 16.00341  ? 82  PRO A CD  1 
ATOM   1053 N  N   . VAL A 1 83  ? -1.56872  11.19333 3.30961   1.000 17.06604  ? 83  VAL A N   1 
ATOM   1054 C  CA  . VAL A 1 83  ? -1.22977  12.11826 4.39705   1.000 16.51336  ? 83  VAL A CA  1 
ATOM   1055 C  C   . VAL A 1 83  ? -2.42845  12.99894 4.73752   1.000 17.81778  ? 83  VAL A C   1 
ATOM   1056 O  O   . VAL A 1 83  ? -2.76497  13.20773 5.92128   1.000 18.15157  ? 83  VAL A O   1 
ATOM   1057 C  CB  . VAL A 1 83  ? 0.03290   12.92631 4.04456   1.000 18.42913  ? 83  VAL A CB  1 
ATOM   1058 C  CG1 . VAL A 1 83  ? 0.32680   13.94376 5.16041   1.000 18.81577  ? 83  VAL A CG1 1 
ATOM   1059 C  CG2 . VAL A 1 83  ? 1.24072   11.97014 3.79506   1.000 19.94989  ? 83  VAL A CG2 1 
ATOM   1060 N  N   . MET A 1 84  ? -3.09151  13.53860 3.71464   1.000 16.53357  ? 84  MET A N   1 
ATOM   1061 C  CA  . MET A 1 84  ? -4.23364  14.41284 3.94820   1.000 15.83330  ? 84  MET A CA  1 
ATOM   1062 C  C   . MET A 1 84  ? -5.35096  13.66105 4.66210   1.000 19.60378  ? 84  MET A C   1 
ATOM   1063 O  O   . MET A 1 84  ? -6.07747  14.23364 5.49292   1.000 18.88492  ? 84  MET A O   1 
ATOM   1064 C  CB  . MET A 1 84  ? -4.71749  14.95117 2.60519   1.000 17.46375  ? 84  MET A CB  1 
ATOM   1065 C  CG  . MET A 1 84  ? -3.66540  15.85464 1.96016   1.000 17.74638  ? 84  MET A CG  1 
ATOM   1066 S  SD  . MET A 1 84  ? -4.08319  16.26315 0.26707   1.000 21.25486  ? 84  MET A SD  1 
ATOM   1067 C  CE  . MET A 1 84  ? -5.40571  17.40014 0.48508   1.000 24.11592  ? 84  MET A CE  1 
ATOM   1068 N  N   . LEU A 1 85  ? -5.52608  12.37893 4.32594   1.000 17.65274  ? 85  LEU A N   1 
ATOM   1069 C  CA  . LEU A 1 85  ? -6.55685  11.60529 5.00792   1.000 17.11281  ? 85  LEU A CA  1 
ATOM   1070 C  C   . LEU A 1 85  ? -6.19105  11.40548 6.47744   1.000 17.09664  ? 85  LEU A C   1 
ATOM   1071 O  O   . LEU A 1 85  ? -7.05016  11.55308 7.36093   1.000 18.04437  ? 85  LEU A O   1 
ATOM   1072 C  CB  . LEU A 1 85  ? -6.79207  10.28286 4.27789   1.000 17.37461  ? 85  LEU A CB  1 
ATOM   1073 C  CG  . LEU A 1 85  ? -7.56019  10.41139 2.94003   1.000 15.41902  ? 85  LEU A CG  1 
ATOM   1074 C  CD1 . LEU A 1 85  ? -7.38693  9.10799  2.13858   1.000 18.79742  ? 85  LEU A CD1 1 
ATOM   1075 C  CD2 . LEU A 1 85  ? -9.05669  10.68571 3.17329   1.000 17.41433  ? 85  LEU A CD2 1 
ATOM   1076 N  N   . LEU A 1 86  ? -4.92046  11.08891 6.75931   1.000 18.08631  ? 86  LEU A N   1 
ATOM   1077 C  CA  . LEU A 1 86  ? -4.47105  10.99263 8.14930   1.000 18.34419  ? 86  LEU A CA  1 
ATOM   1078 C  C   . LEU A 1 86  ? -4.70018  12.30049 8.90564   1.000 18.30391  ? 86  LEU A C   1 
ATOM   1079 O  O   . LEU A 1 86  ? -5.19529  12.29418 10.04361  1.000 17.01769  ? 86  LEU A O   1 
ATOM   1080 C  CB  . LEU A 1 86  ? -3.00074  10.56986 8.16897   1.000 19.34188  ? 86  LEU A CB  1 
ATOM   1081 C  CG  . LEU A 1 86  ? -2.74851  9.12884  7.68865   1.000 23.50191  ? 86  LEU A CG  1 
ATOM   1082 C  CD1 . LEU A 1 86  ? -1.23976  8.86485  7.68718   1.000 32.07143  ? 86  LEU A CD1 1 
ATOM   1083 C  CD2 . LEU A 1 86  ? -3.47077  8.07495  8.54985   1.000 30.01765  ? 86  LEU A CD2 1 
ATOM   1084 N  N   . THR A 1 87  ? -4.35622  13.44613 8.29227   1.000 18.82428  ? 87  THR A N   1 
ATOM   1085 C  CA  . THR A 1 87  ? -4.52000  14.71155 9.01284   1.000 18.22691  ? 87  THR A CA  1 
ATOM   1086 C  C   . THR A 1 87  ? -5.98236  15.03557 9.23986   1.000 18.00046  ? 87  THR A C   1 
ATOM   1087 O  O   . THR A 1 87  ? -6.32948  15.61693 10.27239  1.000 20.97262  ? 87  THR A O   1 
ATOM   1088 C  CB  . THR A 1 87  ? -3.80471  15.87961 8.33127   1.000 23.88617  ? 87  THR A CB  1 
ATOM   1089 O  OG1 . THR A 1 87  ? -4.31325  16.06105 7.01422   1.000 22.02657  ? 87  THR A OG1 1 
ATOM   1090 C  CG2 . THR A 1 87  ? -2.31879  15.62854 8.24503   1.000 25.98682  ? 87  THR A CG2 1 
ATOM   1091 N  N   . THR A 1 88  ? -6.84962  14.62499 8.31823   1.000 17.49361  ? 88  THR A N   1 
ATOM   1092 C  CA  . THR A 1 88  ? -8.29017  14.76939 8.51754   1.000 17.14205  ? 88  THR A CA  1 
ATOM   1093 C  C   . THR A 1 88  ? -8.76897  13.94374 9.71620   1.000 16.54941  ? 88  THR A C   1 
ATOM   1094 O  O   . THR A 1 88  ? -9.51778  14.44428 10.57315  1.000 16.82380  ? 88  THR A O   1 
ATOM   1095 C  CB  . THR A 1 88  ? -9.00870  14.36296 7.22832   1.000 20.98354  ? 88  THR A CB  1 
ATOM   1096 O  OG1 . THR A 1 88  ? -8.61898  15.28721 6.19027   1.000 26.41862  ? 88  THR A OG1 1 
ATOM   1097 C  CG2 . THR A 1 88  ? -10.51102 14.46222 7.43752   1.000 29.04284  ? 88  THR A CG2 1 
ATOM   1098 N  N   . VAL A 1 89  ? -8.34580  12.68341 9.79456   1.000 16.44402  ? 89  VAL A N   1 
ATOM   1099 C  CA  . VAL A 1 89  ? -8.63527  11.86252 10.98087  1.000 14.36916  ? 89  VAL A CA  1 
ATOM   1100 C  C   . VAL A 1 89  ? -8.19032  12.57486 12.24998  1.000 18.13138  ? 89  VAL A C   1 
ATOM   1101 O  O   . VAL A 1 89  ? -8.93484  12.66290 13.23793  1.000 17.19538  ? 89  VAL A O   1 
ATOM   1102 C  CB  . VAL A 1 89  ? -7.95072  10.49382 10.85075  1.000 17.16284  ? 89  VAL A CB  1 
ATOM   1103 C  CG1 . VAL A 1 89  ? -8.02487  9.75767  12.18774  1.000 17.89358  ? 89  VAL A CG1 1 
ATOM   1104 C  CG2 . VAL A 1 89  ? -8.65054  9.67653  9.72767   1.000 18.25362  ? 89  VAL A CG2 1 
ATOM   1105 N  N   . TYR A 1 90  ? -6.96251  13.09443 12.24172  1.000 16.33169  ? 90  TYR A N   1 
ATOM   1106 C  CA  . TYR A 1 90  ? -6.44675  13.74907 13.44414  1.000 16.24129  ? 90  TYR A CA  1 
ATOM   1107 C  C   . TYR A 1 90  ? -7.28537  14.96209 13.80969  1.000 17.76935  ? 90  TYR A C   1 
ATOM   1108 O  O   . TYR A 1 90  ? -7.55943  15.20018 14.98792  1.000 19.10614  ? 90  TYR A O   1 
ATOM   1109 C  CB  . TYR A 1 90  ? -4.97848  14.16698 13.27758  1.000 17.24755  ? 90  TYR A CB  1 
ATOM   1110 C  CG  . TYR A 1 90  ? -4.01558  13.02638 12.92860  1.000 17.43390  ? 90  TYR A CG  1 
ATOM   1111 C  CD1 . TYR A 1 90  ? -4.31322  11.68171 13.23585  1.000 18.62694  ? 90  TYR A CD1 1 
ATOM   1112 C  CD2 . TYR A 1 90  ? -2.85626  13.29521 12.21839  1.000 19.41728  ? 90  TYR A CD2 1 
ATOM   1113 C  CE1 . TYR A 1 90  ? -3.43189  10.64021 12.88784  1.000 17.82265  ? 90  TYR A CE1 1 
ATOM   1114 C  CE2 . TYR A 1 90  ? -1.97497  12.25967 11.83330  1.000 20.93724  ? 90  TYR A CE2 1 
ATOM   1115 C  CZ  . TYR A 1 90  ? -2.27585  10.93865 12.16917  1.000 21.32458  ? 90  TYR A CZ  1 
ATOM   1116 O  OH  . TYR A 1 90  ? -1.42299  9.90983  11.77431  1.000 22.48165  ? 90  TYR A OH  1 
ATOM   1117 N  N   . PHE A 1 91  ? -7.71117  15.74332 12.81462  1.000 17.26893  ? 91  PHE A N   1 
ATOM   1118 C  CA  . PHE A 1 91  ? -8.54602  16.90677 13.14166  1.000 14.90781  ? 91  PHE A CA  1 
ATOM   1119 C  C   . PHE A 1 91  ? -9.91155  16.49691 13.69668  1.000 17.21534  ? 91  PHE A C   1 
ATOM   1120 O  O   . PHE A 1 91  ? -10.41834 17.10414 14.64961  1.000 16.84589  ? 91  PHE A O   1 
ATOM   1121 C  CB  . PHE A 1 91  ? -8.67343  17.84164 11.94871  1.000 18.26187  ? 91  PHE A CB  1 
ATOM   1122 C  CG  . PHE A 1 91  ? -9.29579  19.13418 12.34597  1.000 19.39237  ? 91  PHE A CG  1 
ATOM   1123 C  CD1 . PHE A 1 91  ? -8.56512  20.05706 13.10184  1.000 18.12579  ? 91  PHE A CD1 1 
ATOM   1124 C  CD2 . PHE A 1 91  ? -10.62156 19.39532 12.07588  1.000 22.95994  ? 91  PHE A CD2 1 
ATOM   1125 C  CE1 . PHE A 1 91  ? -9.15572  21.24277 13.53639  1.000 21.23993  ? 91  PHE A CE1 1 
ATOM   1126 C  CE2 . PHE A 1 91  ? -11.22399 20.59278 12.49472  1.000 19.90146  ? 91  PHE A CE2 1 
ATOM   1127 C  CZ  . PHE A 1 91  ? -10.48057 21.51922 13.24170  1.000 22.37380  ? 91  PHE A CZ  1 
ATOM   1128 N  N   . PHE A 1 92  ? -10.53107 15.46663 13.11641  1.000 17.34276  ? 92  PHE A N   1 
ATOM   1129 C  CA  . PHE A 1 92  ? -11.79520 14.99262 13.65715  1.000 16.82216  ? 92  PHE A CA  1 
ATOM   1130 C  C   . PHE A 1 92  ? -11.62154 14.52871 15.09633  1.000 17.06154  ? 92  PHE A C   1 
ATOM   1131 O  O   . PHE A 1 92  ? -12.43592 14.85684 15.96736  1.000 17.67983  ? 92  PHE A O   1 
ATOM   1132 C  CB  . PHE A 1 92  ? -12.35861 13.88240 12.77411  1.000 17.11957  ? 92  PHE A CB  1 
ATOM   1133 C  CG  . PHE A 1 92  ? -13.10792 14.38939 11.57250  1.000 16.37428  ? 92  PHE A CG  1 
ATOM   1134 C  CD1 . PHE A 1 92  ? -14.27589 15.12465 11.73575  1.000 20.51631  ? 92  PHE A CD1 1 
ATOM   1135 C  CD2 . PHE A 1 92  ? -12.68595 14.09438 10.29862  1.000 27.74522  ? 92  PHE A CD2 1 
ATOM   1136 C  CE1 . PHE A 1 92  ? -14.97296 15.57816 10.61720  1.000 21.69812  ? 92  PHE A CE1 1 
ATOM   1137 C  CE2 . PHE A 1 92  ? -13.39501 14.54214 9.18934   1.000 30.33888  ? 92  PHE A CE2 1 
ATOM   1138 C  CZ  . PHE A 1 92  ? -14.51502 15.31207 9.35794   1.000 24.91526  ? 92  PHE A CZ  1 
ATOM   1139 N  N   A GLU A 1 93  ? -10.54108 13.80104 15.36936  0.700 17.75226  ? 93  GLU A N   1 
ATOM   1140 N  N   B GLU A 1 93  ? -10.54522 13.78110 15.37106  0.300 17.80845  ? 93  GLU A N   1 
ATOM   1141 C  CA  A GLU A 1 93  ? -10.27744 13.35027 16.73220  0.700 20.85654  ? 93  GLU A CA  1 
ATOM   1142 C  CA  B GLU A 1 93  ? -10.27470 13.34290 16.73897  0.300 21.20337  ? 93  GLU A CA  1 
ATOM   1143 C  C   A GLU A 1 93  ? -10.05558 14.53209 17.65992  0.700 19.08836  ? 93  GLU A C   1 
ATOM   1144 C  C   B GLU A 1 93  ? -10.05649 14.53150 17.66013  0.300 19.47064  ? 93  GLU A C   1 
ATOM   1145 O  O   A GLU A 1 93  ? -10.54938 14.55346 18.79464  0.700 21.15766  ? 93  GLU A O   1 
ATOM   1146 O  O   B GLU A 1 93  ? -10.52982 14.54058 18.80264  0.300 21.35623  ? 93  GLU A O   1 
ATOM   1147 C  CB  A GLU A 1 93  ? -9.05260  12.43561 16.73210  0.700 18.80438  ? 93  GLU A CB  1 
ATOM   1148 C  CB  B GLU A 1 93  ? -9.04350  12.43508 16.77625  0.300 19.22561  ? 93  GLU A CB  1 
ATOM   1149 C  CG  A GLU A 1 93  ? -9.34353  11.07281 16.13824  0.700 17.87880  ? 93  GLU A CG  1 
ATOM   1150 C  CG  B GLU A 1 93  ? -9.27689  11.01102 16.29019  0.300 18.83475  ? 93  GLU A CG  1 
ATOM   1151 C  CD  A GLU A 1 93  ? -10.12754 10.17990 17.09590  0.700 23.86822  ? 93  GLU A CD  1 
ATOM   1152 C  CD  B GLU A 1 93  ? -10.09994 10.15940 17.25588  0.300 23.22916  ? 93  GLU A CD  1 
ATOM   1153 O  OE1 A GLU A 1 93  ? -9.50072  9.57404  17.97940  0.700 31.70173  ? 93  GLU A OE1 1 
ATOM   1154 O  OE1 B GLU A 1 93  ? -10.43686 10.64377 18.35928  0.300 18.40474  ? 93  GLU A OE1 1 
ATOM   1155 O  OE2 A GLU A 1 93  ? -11.36827 10.10434 16.97749  0.700 26.63919  ? 93  GLU A OE2 1 
ATOM   1156 O  OE2 B GLU A 1 93  ? -10.41601 9.00411  16.89332  0.300 14.31635  ? 93  GLU A OE2 1 
ATOM   1157 N  N   . TYR A 1 94  ? -9.33124  15.54519 17.18377  1.000 20.59589  ? 94  TYR A N   1 
ATOM   1158 C  CA  . TYR A 1 94  ? -9.15767  16.75519 17.98137  1.000 19.14631  ? 94  TYR A CA  1 
ATOM   1159 C  C   . TYR A 1 94  ? -10.50109 17.41543 18.29539  1.000 17.37730  ? 94  TYR A C   1 
ATOM   1160 O  O   . TYR A 1 94  ? -10.78235 17.77104 19.44910  1.000 23.38107  ? 94  TYR A O   1 
ATOM   1161 C  CB  . TYR A 1 94  ? -8.26438  17.72407 17.21507  1.000 19.55481  ? 94  TYR A CB  1 
ATOM   1162 C  CG  . TYR A 1 94  ? -8.23942  19.11050 17.82211  1.000 21.12423  ? 94  TYR A CG  1 
ATOM   1163 C  CD1 . TYR A 1 94  ? -7.55634  19.35191 19.03707  1.000 21.77861  ? 94  TYR A CD1 1 
ATOM   1164 C  CD2 . TYR A 1 94  ? -8.86831  20.18768 17.19005  1.000 20.48301  ? 94  TYR A CD2 1 
ATOM   1165 C  CE1 . TYR A 1 94  ? -7.50180  20.63482 19.59502  1.000 21.38515  ? 94  TYR A CE1 1 
ATOM   1166 C  CE2 . TYR A 1 94  ? -8.82673  21.47764 17.74264  1.000 24.35677  ? 94  TYR A CE2 1 
ATOM   1167 C  CZ  . TYR A 1 94  ? -8.14985  21.68640 18.94838  1.000 22.55929  ? 94  TYR A CZ  1 
ATOM   1168 O  OH  . TYR A 1 94  ? -8.11681  22.94877 19.48850  1.000 26.36319  ? 94  TYR A OH  1 
ATOM   1169 N  N   . MET A 1 95  ? -11.36087 17.57110 17.27441  1.000 18.98919  ? 95  MET A N   1 
ATOM   1170 C  CA  . MET A 1 95  ? -12.65581 18.22957 17.48272  1.000 21.63633  ? 95  MET A CA  1 
ATOM   1171 C  C   . MET A 1 95  ? -13.56246 17.43598 18.41523  1.000 20.22582  ? 95  MET A C   1 
ATOM   1172 O  O   . MET A 1 95  ? -14.34352 18.01266 19.18035  1.000 24.35141  ? 95  MET A O   1 
ATOM   1173 C  CB  . MET A 1 95  ? -13.39241 18.32404 16.14007  1.000 25.86967  ? 95  MET A CB  1 
ATOM   1174 C  CG  . MET A 1 95  ? -13.09755 19.53125 15.31741  1.000 31.39821  ? 95  MET A CG  1 
ATOM   1175 S  SD  . MET A 1 95  ? -14.49339 19.89075 14.18315  1.000 27.73595  ? 95  MET A SD  1 
ATOM   1176 C  CE  . MET A 1 95  ? -14.47169 18.43242 13.18867  1.000 23.80890  ? 95  MET A CE  1 
ATOM   1177 N  N   . ASN A 1 96  ? -13.47508 16.10913 18.37703  1.000 21.58069  ? 96  ASN A N   1 
ATOM   1178 C  CA  . ASN A 1 96  ? -14.50596 15.25588 18.94546  1.000 20.56249  ? 96  ASN A CA  1 
ATOM   1179 C  C   . ASN A 1 96  ? -14.11910 14.57398 20.24871  1.000 29.54036  ? 96  ASN A C   1 
ATOM   1180 O  O   . ASN A 1 96  ? -15.00417 14.04202 20.93254  1.000 28.67127  ? 96  ASN A O   1 
ATOM   1181 C  CB  . ASN A 1 96  ? -14.96300 14.21675 17.90694  1.000 22.27719  ? 96  ASN A CB  1 
ATOM   1182 C  CG  . ASN A 1 96  ? -15.63263 14.87366 16.71650  1.000 21.00630  ? 96  ASN A CG  1 
ATOM   1183 O  OD1 . ASN A 1 96  ? -16.22672 15.96037 16.84820  1.000 21.92407  ? 96  ASN A OD1 1 
ATOM   1184 N  ND2 . ASN A 1 96  ? -15.57402 14.21984 15.56464  1.000 23.76255  ? 96  ASN A ND2 1 
ATOM   1185 N  N   A SER A 1 97  ? -12.83989 14.56494 20.61270  0.500 27.25767  ? 97  SER A N   1 
ATOM   1186 N  N   B SER A 1 97  ? -12.84639 14.59330 20.62925  0.500 27.25904  ? 97  SER A N   1 
ATOM   1187 C  CA  A SER A 1 97  ? -12.40094 13.91978 21.84432  0.500 25.84726  ? 97  SER A CA  1 
ATOM   1188 C  CA  B SER A 1 97  ? -12.41715 13.97214 21.87584  0.500 25.96597  ? 97  SER A CA  1 
ATOM   1189 C  C   A SER A 1 97  ? -12.52213 14.88968 23.01564  0.500 36.21563  ? 97  SER A C   1 
ATOM   1190 C  C   B SER A 1 97  ? -12.58069 14.95606 23.02993  0.500 36.16279  ? 97  SER A C   1 
ATOM   1191 O  O   A SER A 1 97  ? -12.09861 16.04653 22.92445  0.500 35.83208  ? 97  SER A O   1 
ATOM   1192 O  O   B SER A 1 97  ? -12.17620 16.11814 22.92912  0.500 35.67081  ? 97  SER A O   1 
ATOM   1193 C  CB  A SER A 1 97  ? -10.95442 13.43976 21.71920  0.500 34.56360  ? 97  SER A CB  1 
ATOM   1194 C  CB  B SER A 1 97  ? -10.95748 13.52992 21.77983  0.500 34.64351  ? 97  SER A CB  1 
ATOM   1195 O  OG  A SER A 1 97  ? -10.80832 12.53579 20.63749  0.500 35.18664  ? 97  SER A OG  1 
ATOM   1196 O  OG  B SER A 1 97  ? -10.10254 14.65289 21.66546  0.500 35.51779  ? 97  SER A OG  1 
ATOM   1197 N  N   A ASP A 1 98  ? -13.10259 14.40986 24.11772  0.700 44.10303  ? 98  ASP A N   1 
ATOM   1198 N  N   B ASP A 1 98  ? -13.17165 14.48371 24.13009  0.300 43.90387  ? 98  ASP A N   1 
ATOM   1199 C  CA  A ASP A 1 98  ? -13.26341 15.24880 25.30287  0.700 51.04883  ? 98  ASP A CA  1 
ATOM   1200 C  CA  B ASP A 1 98  ? -13.34856 15.33281 25.30333  0.300 50.49254  ? 98  ASP A CA  1 
ATOM   1201 C  C   A ASP A 1 98  ? -11.91472 15.55258 25.94423  0.700 45.12853  ? 98  ASP A C   1 
ATOM   1202 C  C   B ASP A 1 98  ? -12.04172 15.57397 26.04695  0.300 45.21750  ? 98  ASP A C   1 
ATOM   1203 O  O   A ASP A 1 98  ? -11.63811 16.69703 26.32493  0.700 54.12344  ? 98  ASP A O   1 
ATOM   1204 O  O   B ASP A 1 98  ? -11.95547 16.52506 26.83049  0.300 48.14773  ? 98  ASP A O   1 
ATOM   1205 C  CB  A ASP A 1 98  ? -14.19300 14.55995 26.30216  0.700 50.52966  ? 98  ASP A CB  1 
ATOM   1206 C  CB  B ASP A 1 98  ? -14.38220 14.72248 26.25172  0.300 51.70406  ? 98  ASP A CB  1 
ATOM   1207 C  CG  A ASP A 1 98  ? -13.77261 13.13415 26.59379  0.700 57.38596  ? 98  ASP A CG  1 
ATOM   1208 C  CG  B ASP A 1 98  ? -13.99718 13.33147 26.71477  0.300 56.94896  ? 98  ASP A CG  1 
ATOM   1209 N  N   A ASP A 1 99  ? -11.06406 14.54211 26.07339  0.700 40.42263  ? 99  ASP A N   1 
ATOM   1210 N  N   B ASP A 1 99  ? -11.03113 14.73982 25.82518  0.300 40.06186  ? 99  ASP A N   1 
ATOM   1211 C  CA  A ASP A 1 99  ? -9.72990  14.75114 26.60808  0.700 46.91989  ? 99  ASP A CA  1 
ATOM   1212 C  CA  B ASP A 1 99  ? -9.72811  14.90129 26.44776  0.300 45.60732  ? 99  ASP A CA  1 
ATOM   1213 C  C   A ASP A 1 99  ? -8.74534  15.00791 25.46934  0.700 35.69538  ? 99  ASP A C   1 
ATOM   1214 C  C   B ASP A 1 99  ? -8.66268  15.06823 25.37243  0.300 35.37782  ? 99  ASP A C   1 
ATOM   1215 O  O   A ASP A 1 99  ? -8.99643  14.66931 24.30681  0.700 33.72949  ? 99  ASP A O   1 
ATOM   1216 O  O   B ASP A 1 99  ? -8.83363  14.63867 24.22660  0.300 33.97920  ? 99  ASP A O   1 
ATOM   1217 C  CB  A ASP A 1 99  ? -9.28779  13.53579 27.42438  0.700 46.48685  ? 99  ASP A CB  1 
ATOM   1218 C  CB  B ASP A 1 99  ? -9.38549  13.69592 27.33481  0.300 45.68549  ? 99  ASP A CB  1 
ATOM   1219 N  N   A GLY A 1 100 ? -7.61906  15.62598 25.81797  0.700 35.55707  ? 100 GLY A N   1 
ATOM   1220 N  N   B GLY A 1 100 ? -7.55781  15.70412 25.76103  0.300 35.20031  ? 100 GLY A N   1 
ATOM   1221 C  CA  A GLY A 1 100 ? -6.58498  15.85530 24.82500  0.700 22.49417  ? 100 GLY A CA  1 
ATOM   1222 C  CA  B GLY A 1 100 ? -6.44759  15.94145 24.85983  0.300 21.99128  ? 100 GLY A CA  1 
ATOM   1223 C  C   A GLY A 1 100 ? -6.12651  14.54087 24.21507  0.700 29.56654  ? 100 GLY A C   1 
ATOM   1224 C  C   B GLY A 1 100 ? -5.91288  14.66575 24.24128  0.300 30.05731  ? 100 GLY A C   1 
ATOM   1225 O  O   A GLY A 1 100 ? -6.05380  13.51022 24.88864  0.700 27.22164  ? 100 GLY A O   1 
ATOM   1226 O  O   B GLY A 1 100 ? -5.56072  13.72065 24.95282  0.300 31.45728  ? 100 GLY A O   1 
ATOM   1227 N  N   A ILE A 1 101 ? -5.83618  14.57431 22.92464  0.700 23.10975  ? 101 ILE A N   1 
ATOM   1228 N  N   B ILE A 1 101 ? -5.86036  14.62716 22.91440  0.300 23.84912  ? 101 ILE A N   1 
ATOM   1229 C  CA  A ILE A 1 101 ? -5.38797  13.39052 22.20040  0.700 19.71530  ? 101 ILE A CA  1 
ATOM   1230 C  CA  B ILE A 1 101 ? -5.41150  13.45938 22.16973  0.300 20.72558  ? 101 ILE A CA  1 
ATOM   1231 C  C   A ILE A 1 101 ? -4.36544  13.81148 21.15314  0.700 21.42787  ? 101 ILE A C   1 
ATOM   1232 C  C   B ILE A 1 101 ? -4.20929  13.86135 21.32340  0.300 21.38834  ? 101 ILE A C   1 
ATOM   1233 O  O   A ILE A 1 101 ? -4.50234  14.86908 20.51935  0.700 18.95508  ? 101 ILE A O   1 
ATOM   1234 O  O   B ILE A 1 101 ? -4.00418  15.04253 21.01870  0.300 18.73499  ? 101 ILE A O   1 
ATOM   1235 C  CB  A ILE A 1 101 ? -6.57036  12.62430 21.57514  0.700 18.99003  ? 101 ILE A CB  1 
ATOM   1236 C  CB  B ILE A 1 101 ? -6.56352  12.87026 21.31364  0.300 19.13853  ? 101 ILE A CB  1 
ATOM   1237 C  CG1 A ILE A 1 101 ? -6.08647  11.26048 21.05174  0.700 25.69122  ? 101 ILE A CG1 1 
ATOM   1238 C  CG1 B ILE A 1 101 ? -6.19543  11.48871 20.76109  0.300 26.37251  ? 101 ILE A CG1 1 
ATOM   1239 C  CG2 A ILE A 1 101 ? -7.24013  13.46168 20.48783  0.700 25.86923  ? 101 ILE A CG2 1 
ATOM   1240 C  CG2 B ILE A 1 101 ? -6.96834  13.84277 20.20361  0.300 20.70083  ? 101 ILE A CG2 1 
ATOM   1241 C  CD1 A ILE A 1 101 ? -7.20862  10.27924 20.76883  0.700 35.39376  ? 101 ILE A CD1 1 
ATOM   1242 C  CD1 B ILE A 1 101 ? -7.39438  10.59037 20.51215  0.300 31.00209  ? 101 ILE A CD1 1 
ATOM   1243 N  N   A ARG A 1 102 ? -3.32684  12.98402 20.99377  0.700 20.78627  ? 102 ARG A N   1 
ATOM   1244 N  N   B ARG A 1 102 ? -3.39201  12.87142 20.97013  0.300 21.88779  ? 102 ARG A N   1 
ATOM   1245 C  CA  A ARG A 1 102 ? -2.24848  13.20227 20.03772  0.700 22.92381  ? 102 ARG A CA  1 
ATOM   1246 C  CA  B ARG A 1 102 ? -2.23321  13.07183 20.11374  0.300 23.04610  ? 102 ARG A CA  1 
ATOM   1247 C  C   A ARG A 1 102 ? -2.14183  12.05532 19.03436  0.700 17.88161  ? 102 ARG A C   1 
ATOM   1248 C  C   B ARG A 1 102 ? -2.30151  12.11678 18.92506  0.300 22.17693  ? 102 ARG A C   1 
ATOM   1249 O  O   A ARG A 1 102 ? -2.68427  10.95661 19.22568  0.700 18.95641  ? 102 ARG A O   1 
ATOM   1250 O  O   B ARG A 1 102 ? -3.13526  11.20599 18.87415  0.300 19.13930  ? 102 ARG A O   1 
ATOM   1251 C  CB  A ARG A 1 102 ? -0.90640  13.39559 20.75449  0.700 23.01681  ? 102 ARG A CB  1 
ATOM   1252 C  CB  B ARG A 1 102 ? -0.92635  12.87326 20.90299  0.300 27.84757  ? 102 ARG A CB  1 
ATOM   1253 C  CG  A ARG A 1 102 ? -1.01432  14.20337 22.03252  0.700 38.42718  ? 102 ARG A CG  1 
ATOM   1254 C  CG  B ARG A 1 102 ? -0.70385  13.89005 22.02643  0.300 40.21399  ? 102 ARG A CG  1 
ATOM   1255 C  CD  A ARG A 1 102 ? -0.19137  15.45931 21.94741  0.700 43.53550  ? 102 ARG A CD  1 
ATOM   1256 C  CD  B ARG A 1 102 ? 0.05192   15.12380 21.53763  0.300 39.96383  ? 102 ARG A CD  1 
ATOM   1257 N  NE  A ARG A 1 102 ? 1.16551   15.21075 21.46829  0.700 46.59700  ? 102 ARG A NE  1 
ATOM   1258 N  NE  B ARG A 1 102 ? 1.45545   14.83865 21.25090  0.300 43.75540  ? 102 ARG A NE  1 
ATOM   1259 C  CZ  A ARG A 1 102 ? 2.26048   15.33804 22.20778  0.700 57.77801  ? 102 ARG A CZ  1 
ATOM   1260 C  CZ  B ARG A 1 102 ? 2.46098   15.07853 22.08436  0.300 55.77449  ? 102 ARG A CZ  1 
ATOM   1261 N  NH1 A ARG A 1 102 ? 2.19832   15.69647 23.48065  0.700 56.21995  ? 102 ARG A NH1 1 
ATOM   1262 N  NH1 B ARG A 1 102 ? 2.26186   15.63420 23.26919  0.300 56.22394  ? 102 ARG A NH1 1 
ATOM   1263 N  NH2 A ARG A 1 102 ? 3.44893   15.10912 21.65350  0.700 57.56695  ? 102 ARG A NH2 1 
ATOM   1264 N  NH2 B ARG A 1 102 ? 3.69841   14.75232 21.71985  0.300 54.52812  ? 102 ARG A NH2 1 
ATOM   1265 N  N   . LYS A 1 103 ? -1.43353  12.33726 17.93565  1.000 20.39040  ? 103 LYS A N   1 
ATOM   1266 C  CA  . LYS A 1 103 ? -1.43593  11.41662 16.80375  1.000 19.82593  ? 103 LYS A CA  1 
ATOM   1267 C  C   . LYS A 1 103 ? -0.86379  10.04853 17.16834  1.000 20.50767  ? 103 LYS A C   1 
ATOM   1268 O  O   . LYS A 1 103 ? -1.31408  9.04116  16.62368  1.000 22.76480  ? 103 LYS A O   1 
ATOM   1269 C  CB  . LYS A 1 103 ? -0.74743  12.01113 15.57187  1.000 24.75257  ? 103 LYS A CB  1 
ATOM   1270 C  CG  . LYS A 1 103 ? 0.73178   11.83340 15.52419  1.000 26.88751  ? 103 LYS A CG  1 
ATOM   1271 C  CD  . LYS A 1 103 ? 1.30665   12.40624 14.22125  1.000 28.57217  ? 103 LYS A CD  1 
ATOM   1272 C  CE  . LYS A 1 103 ? 2.81300   12.22564 14.22942  1.000 28.30339  ? 103 LYS A CE  1 
ATOM   1273 N  NZ  . LYS A 1 103 ? 3.37703   12.45187 12.86359  1.000 34.90468  ? 103 LYS A NZ  1 
ATOM   1274 N  N   . LYS A 1 104 ? 0.07919   9.98031  18.10123  1.000 21.97453  ? 104 LYS A N   1 
ATOM   1275 C  CA  . LYS A 1 104 ? 0.64606   8.67363  18.45026  1.000 24.03321  ? 104 LYS A CA  1 
ATOM   1276 C  C   . LYS A 1 104 ? -0.41858  7.74706  19.02967  1.000 21.67987  ? 104 LYS A C   1 
ATOM   1277 O  O   . LYS A 1 104 ? -0.46833  6.55615  18.68772  1.000 23.77679  ? 104 LYS A O   1 
ATOM   1278 C  CB  . LYS A 1 104 ? 1.79642   8.83057  19.43724  1.000 24.31439  ? 104 LYS A CB  1 
ATOM   1279 C  CG  . LYS A 1 104 ? 2.35905   7.46344  19.90172  1.000 32.46144  ? 104 LYS A CG  1 
ATOM   1280 C  CD  . LYS A 1 104 ? 3.60990   7.59224  20.77595  1.000 35.80318  ? 104 LYS A CD  1 
ATOM   1281 C  CE  . LYS A 1 104 ? 3.93492   6.25485  21.45557  1.000 43.31684  ? 104 LYS A CE  1 
ATOM   1282 N  NZ  . LYS A 1 104 ? 3.93556   5.12776  20.47337  1.000 43.03995  ? 104 LYS A NZ  1 
ATOM   1283 N  N   . GLU A 1 105 ? -1.27909  8.27550  19.90816  1.000 21.61652  ? 105 GLU A N   1 
ATOM   1284 C  CA  . GLU A 1 105 ? -2.36454  7.48178  20.47991  1.000 22.16324  ? 105 GLU A CA  1 
ATOM   1285 C  C   . GLU A 1 105 ? -3.31416  6.98933  19.40315  1.000 19.88168  ? 105 GLU A C   1 
ATOM   1286 O  O   . GLU A 1 105 ? -3.73427  5.81735  19.40869  1.000 22.41777  ? 105 GLU A O   1 
ATOM   1287 C  CB  . GLU A 1 105 ? -3.13217  8.31123  21.52172  1.000 23.06275  ? 105 GLU A CB  1 
ATOM   1288 C  CG  . GLU A 1 105 ? -4.35234  7.59907  22.06941  1.000 24.77360  ? 105 GLU A CG  1 
ATOM   1289 C  CD  . GLU A 1 105 ? -5.00534  8.34533  23.22136  1.000 45.21592  ? 105 GLU A CD  1 
ATOM   1290 O  OE1 . GLU A 1 105 ? -4.41170  9.33152  23.70110  1.000 35.90016  ? 105 GLU A OE1 1 
ATOM   1291 O  OE2 . GLU A 1 105 ? -6.11903  7.95186  23.63180  1.000 42.24291  ? 105 GLU A OE2 1 
ATOM   1292 N  N   . ILE A 1 106 ? -3.65622  7.86428  18.45674  1.000 19.29309  ? 106 ILE A N   1 
ATOM   1293 C  CA  . ILE A 1 106 ? -4.55051  7.49865  17.36288  1.000 17.62052  ? 106 ILE A CA  1 
ATOM   1294 C  C   . ILE A 1 106 ? -3.90399  6.44397  16.47827  1.000 18.41724  ? 106 ILE A C   1 
ATOM   1295 O  O   . ILE A 1 106 ? -4.54210  5.45328  16.11134  1.000 20.60300  ? 106 ILE A O   1 
ATOM   1296 C  CB  . ILE A 1 106 ? -4.91466  8.75069  16.54479  1.000 16.99560  ? 106 ILE A CB  1 
ATOM   1297 C  CG1 . ILE A 1 106 ? -5.70952  9.72663  17.41400  1.000 17.60870  ? 106 ILE A CG1 1 
ATOM   1298 C  CG2 . ILE A 1 106 ? -5.75813  8.37643  15.31919  1.000 19.16318  ? 106 ILE A CG2 1 
ATOM   1299 C  CD1 . ILE A 1 106 ? -5.70904  11.18337 16.87608  1.000 19.07934  ? 106 ILE A CD1 1 
ATOM   1300 N  N   . ASN A 1 107 ? -2.66869  6.69942  16.04492  1.000 19.36983  ? 107 ASN A N   1 
ATOM   1301 C  CA  . ASN A 1 107 ? -1.97046  5.76907  15.15511  1.000 17.90040  ? 107 ASN A CA  1 
ATOM   1302 C  C   . ASN A 1 107 ? -1.82023  4.39755  15.81068  1.000 19.03425  ? 107 ASN A C   1 
ATOM   1303 O  O   . ASN A 1 107 ? -2.05996  3.35981  15.17380  1.000 21.04933  ? 107 ASN A O   1 
ATOM   1304 C  CB  . ASN A 1 107 ? -0.59522  6.33269  14.80809  1.000 19.56398  ? 107 ASN A CB  1 
ATOM   1305 C  CG  . ASN A 1 107 ? -0.66992  7.51093  13.84539  1.000 18.18763  ? 107 ASN A CG  1 
ATOM   1306 O  OD1 . ASN A 1 107 ? -1.64756  7.67449  13.12287  1.000 21.64303  ? 107 ASN A OD1 1 
ATOM   1307 N  ND2 . ASN A 1 107 ? 0.40112   8.31200  13.81772  1.000 24.00320  ? 107 ASN A ND2 1 
ATOM   1308 N  N   . ASP A 1 108 ? -1.40756  4.37233  17.08342  1.000 19.41733  ? 108 ASP A N   1 
ATOM   1309 C  CA  . ASP A 1 108 ? -1.15020  3.09579  17.73306  1.000 20.76358  ? 108 ASP A CA  1 
ATOM   1310 C  C   . ASP A 1 108 ? -2.43948  2.29816  17.89977  1.000 23.86854  ? 108 ASP A C   1 
ATOM   1311 O  O   . ASP A 1 108 ? -2.41017  1.05830  17.93530  1.000 24.16207  ? 108 ASP A O   1 
ATOM   1312 C  CB  . ASP A 1 108 ? -0.54835  3.31021  19.11193  1.000 20.44224  ? 108 ASP A CB  1 
ATOM   1313 C  CG  . ASP A 1 108 ? 0.90252   3.73662  19.09555  1.000 21.76780  ? 108 ASP A CG  1 
ATOM   1314 O  OD1 . ASP A 1 108 ? 1.57113   3.72539  18.04243  1.000 24.57166  ? 108 ASP A OD1 1 
ATOM   1315 O  OD2 . ASP A 1 108 ? 1.38274   4.10409  20.20042  1.000 25.24463  ? 108 ASP A OD2 1 
ATOM   1316 N  N   . ARG A 1 109 ? -3.56341  2.99566  18.07846  1.000 21.63480  ? 109 ARG A N   1 
ATOM   1317 C  CA  . ARG A 1 109 ? -4.83805  2.32661  18.30076  1.000 22.46097  ? 109 ARG A CA  1 
ATOM   1318 C  C   . ARG A 1 109 ? -5.47609  1.90859  16.98293  1.000 23.41366  ? 109 ARG A C   1 
ATOM   1319 O  O   . ARG A 1 109 ? -6.06812  0.81908  16.90201  1.000 24.35105  ? 109 ARG A O   1 
ATOM   1320 C  CB  . ARG A 1 109 ? -5.76874  3.29030  19.04463  1.000 22.50347  ? 109 ARG A CB  1 
ATOM   1321 C  CG  . ARG A 1 109 ? -7.15965  2.75031  19.43154  1.000 24.82744  ? 109 ARG A CG  1 
ATOM   1322 C  CD  . ARG A 1 109 ? -8.04954  3.87821  19.95269  1.000 24.66178  ? 109 ARG A CD  1 
ATOM   1323 N  NE  . ARG A 1 109 ? -8.38889  4.78984  18.86245  1.000 22.90478  ? 109 ARG A NE  1 
ATOM   1324 C  CZ  . ARG A 1 109 ? -8.73943  6.06009  19.01468  1.000 25.18535  ? 109 ARG A CZ  1 
ATOM   1325 N  NH1 . ARG A 1 109 ? -8.78340  6.62814  20.21313  1.000 30.42906  ? 109 ARG A NH1 1 
ATOM   1326 N  NH2 . ARG A 1 109 ? -9.03554  6.78141  17.93934  1.000 26.73264  ? 109 ARG A NH2 1 
ATOM   1327 N  N   . ASP A 1 110 ? -5.37805  2.75458  15.94866  1.000 19.96422  ? 110 ASP A N   1 
ATOM   1328 C  CA  . ASP A 1 110 ? -6.19792  2.61995  14.74715  1.000 22.20416  ? 110 ASP A CA  1 
ATOM   1329 C  C   . ASP A 1 110 ? -5.43709  2.24209  13.48130  1.000 20.69992  ? 110 ASP A C   1 
ATOM   1330 O  O   . ASP A 1 110 ? -6.02217  2.33413  12.39736  1.000 18.19055  ? 110 ASP A O   1 
ATOM   1331 C  CB  . ASP A 1 110 ? -6.98942  3.90142  14.46914  1.000 19.12317  ? 110 ASP A CB  1 
ATOM   1332 C  CG  . ASP A 1 110 ? -8.02816  4.20797  15.52337  1.000 21.42609  ? 110 ASP A CG  1 
ATOM   1333 O  OD1 . ASP A 1 110 ? -8.32864  3.36275  16.40959  1.000 25.71121  ? 110 ASP A OD1 1 
ATOM   1334 O  OD2 . ASP A 1 110 ? -8.57032  5.32582  15.46879  1.000 23.31837  ? 110 ASP A OD2 1 
ATOM   1335 N  N   . TYR A 1 111 ? -4.16587  1.82211  13.56463  1.000 18.75989  ? 111 TYR A N   1 
ATOM   1336 C  CA  . TYR A 1 111 ? -3.37462  1.65266  12.34513  1.000 18.98153  ? 111 TYR A CA  1 
ATOM   1337 C  C   . TYR A 1 111 ? -4.03824  0.71735  11.32854  1.000 18.93207  ? 111 TYR A C   1 
ATOM   1338 O  O   . TYR A 1 111 ? -3.94649  0.95799  10.11424  1.000 20.32462  ? 111 TYR A O   1 
ATOM   1339 C  CB  . TYR A 1 111 ? -1.93099  1.23585  12.66312  1.000 18.23391  ? 111 TYR A CB  1 
ATOM   1340 C  CG  . TYR A 1 111 ? -1.80134  -0.07644 13.39749  1.000 18.86615  ? 111 TYR A CG  1 
ATOM   1341 C  CD1 . TYR A 1 111 ? -1.80128  -0.11935 14.79087  1.000 20.91864  ? 111 TYR A CD1 1 
ATOM   1342 C  CD2 . TYR A 1 111 ? -1.66083  -1.29051 12.69362  1.000 21.14510  ? 111 TYR A CD2 1 
ATOM   1343 C  CE1 . TYR A 1 111 ? -1.66291  -1.33327 15.47845  1.000 24.66095  ? 111 TYR A CE1 1 
ATOM   1344 C  CE2 . TYR A 1 111 ? -1.51333  -2.48929 13.36861  1.000 20.89649  ? 111 TYR A CE2 1 
ATOM   1345 C  CZ  . TYR A 1 111 ? -1.53751  -2.52411 14.74561  1.000 22.35926  ? 111 TYR A CZ  1 
ATOM   1346 O  OH  . TYR A 1 111 ? -1.39401  -3.71868 15.41675  1.000 22.21699  ? 111 TYR A OH  1 
ATOM   1347 N  N   . VAL A 1 112 ? -4.70850  -0.35035 11.78743  1.000 19.53880  ? 112 VAL A N   1 
ATOM   1348 C  CA  . VAL A 1 112 ? -5.37356  -1.22232 10.81091  1.000 20.18909  ? 112 VAL A CA  1 
ATOM   1349 C  C   . VAL A 1 112 ? -6.46599  -0.47234 10.06051  1.000 20.14321  ? 112 VAL A C   1 
ATOM   1350 O  O   . VAL A 1 112 ? -6.54357  -0.51634 8.82683   1.000 19.93497  ? 112 VAL A O   1 
ATOM   1351 C  CB  . VAL A 1 112 ? -5.95434  -2.46984 11.48510  1.000 21.65112  ? 112 VAL A CB  1 
ATOM   1352 C  CG1 . VAL A 1 112 ? -6.70171  -3.31271 10.42202  1.000 22.96806  ? 112 VAL A CG1 1 
ATOM   1353 C  CG2 . VAL A 1 112 ? -4.82994  -3.27534 12.11652  1.000 25.07767  ? 112 VAL A CG2 1 
ATOM   1354 N  N   . TYR A 1 113 ? -7.33382  0.22232  10.79402  1.000 18.96660  ? 113 TYR A N   1 
ATOM   1355 C  CA  . TYR A 1 113 ? -8.42891  0.94427  10.13843  1.000 19.49095  ? 113 TYR A CA  1 
ATOM   1356 C  C   . TYR A 1 113 ? -7.89262  2.05032  9.23934   1.000 20.40566  ? 113 TYR A C   1 
ATOM   1357 O  O   . TYR A 1 113 ? -8.41080  2.27311  8.14139   1.000 18.86795  ? 113 TYR A O   1 
ATOM   1358 C  CB  . TYR A 1 113 ? -9.34442  1.53268  11.19991  1.000 20.76926  ? 113 TYR A CB  1 
ATOM   1359 C  CG  . TYR A 1 113 ? -10.69756 1.96733  10.66978  1.000 22.23114  ? 113 TYR A CG  1 
ATOM   1360 C  CD1 . TYR A 1 113 ? -11.74734 1.05758  10.60625  1.000 22.89540  ? 113 TYR A CD1 1 
ATOM   1361 C  CD2 . TYR A 1 113 ? -10.93052 3.27645  10.24119  1.000 23.39395  ? 113 TYR A CD2 1 
ATOM   1362 C  CE1 . TYR A 1 113 ? -12.98295 1.42360  10.13885  1.000 24.28105  ? 113 TYR A CE1 1 
ATOM   1363 C  CE2 . TYR A 1 113 ? -12.20662 3.66636  9.77413   1.000 22.87295  ? 113 TYR A CE2 1 
ATOM   1364 C  CZ  . TYR A 1 113 ? -13.22126 2.72439  9.73212   1.000 21.49632  ? 113 TYR A CZ  1 
ATOM   1365 O  OH  . TYR A 1 113 ? -14.49512 3.02639  9.29403   1.000 22.98996  ? 113 TYR A OH  1 
ATOM   1366 N  N   . LEU A 1 114 ? -6.82585  2.72192  9.67190   1.000 17.66316  ? 114 LEU A N   1 
ATOM   1367 C  CA  . LEU A 1 114 ? -6.23115  3.76746  8.85773   1.000 19.30755  ? 114 LEU A CA  1 
ATOM   1368 C  C   . LEU A 1 114 ? -5.65872  3.18914  7.57631   1.000 19.64825  ? 114 LEU A C   1 
ATOM   1369 O  O   . LEU A 1 114 ? -5.77514  3.79729  6.49745   1.000 19.60348  ? 114 LEU A O   1 
ATOM   1370 C  CB  . LEU A 1 114 ? -5.16075  4.48107  9.67696   1.000 19.13419  ? 114 LEU A CB  1 
ATOM   1371 C  CG  . LEU A 1 114 ? -5.70207  5.21260  10.92103  1.000 19.50042  ? 114 LEU A CG  1 
ATOM   1372 C  CD1 . LEU A 1 114 ? -4.54677  5.79988  11.72273  1.000 21.37061  ? 114 LEU A CD1 1 
ATOM   1373 C  CD2 . LEU A 1 114 ? -6.69216  6.29577  10.52335  1.000 24.51292  ? 114 LEU A CD2 1 
ATOM   1374 N  N   . PHE A 1 115 ? -5.05368  1.99611  7.67272   1.000 18.98151  ? 115 PHE A N   1 
ATOM   1375 C  CA  . PHE A 1 115 ? -4.60576  1.32131  6.46112   1.000 20.34556  ? 115 PHE A CA  1 
ATOM   1376 C  C   . PHE A 1 115 ? -5.76943  1.03845  5.51786   1.000 19.48219  ? 115 PHE A C   1 
ATOM   1377 O  O   . PHE A 1 115 ? -5.65233  1.28637  4.31114   1.000 22.49619  ? 115 PHE A O   1 
ATOM   1378 C  CB  . PHE A 1 115 ? -3.82618  0.05416  6.79279   1.000 22.71281  ? 115 PHE A CB  1 
ATOM   1379 C  CG  . PHE A 1 115 ? -3.48528  -0.75463 5.59200   1.000 27.60891  ? 115 PHE A CG  1 
ATOM   1380 C  CD1 . PHE A 1 115 ? -2.42708  -0.40370 4.78135   1.000 28.87731  ? 115 PHE A CD1 1 
ATOM   1381 C  CD2 . PHE A 1 115 ? -4.25916  -1.83136 5.25222   1.000 23.21017  ? 115 PHE A CD2 1 
ATOM   1382 C  CE1 . PHE A 1 115 ? -2.12243  -1.16594 3.65692   1.000 28.87456  ? 115 PHE A CE1 1 
ATOM   1383 C  CE2 . PHE A 1 115 ? -3.95349  -2.60915 4.13008   1.000 34.60207  ? 115 PHE A CE2 1 
ATOM   1384 C  CZ  . PHE A 1 115 ? -2.88855  -2.27270 3.34373   1.000 31.00689  ? 115 PHE A CZ  1 
ATOM   1385 N  N   . TYR A 1 116 ? -6.91118  0.55665  6.03849   1.000 20.92762  ? 116 TYR A N   1 
ATOM   1386 C  CA  . TYR A 1 116 ? -8.07679  0.34868  5.16141   1.000 20.27632  ? 116 TYR A CA  1 
ATOM   1387 C  C   . TYR A 1 116 ? -8.48300  1.64007  4.44536   1.000 18.40022  ? 116 TYR A C   1 
ATOM   1388 O  O   . TYR A 1 116 ? -8.80400  1.61725  3.25218   1.000 19.12375  ? 116 TYR A O   1 
ATOM   1389 C  CB  . TYR A 1 116 ? -9.28847  -0.11526 5.95553   1.000 23.19675  ? 116 TYR A CB  1 
ATOM   1390 C  CG  . TYR A 1 116 ? -9.20011  -1.44711 6.61358   1.000 33.39906  ? 116 TYR A CG  1 
ATOM   1391 C  CD1 . TYR A 1 116 ? -8.34077  -2.42421 6.14698   1.000 29.85827  ? 116 TYR A CD1 1 
ATOM   1392 C  CD2 . TYR A 1 116 ? -9.99706  -1.72742 7.71530   1.000 39.50837  ? 116 TYR A CD2 1 
ATOM   1393 C  CE1 . TYR A 1 116 ? -8.28701  -3.67733 6.77519   1.000 33.36954  ? 116 TYR A CE1 1 
ATOM   1394 C  CE2 . TYR A 1 116 ? -9.94586  -2.94495 8.33778   1.000 37.35952  ? 116 TYR A CE2 1 
ATOM   1395 C  CZ  . TYR A 1 116 ? -9.08870  -3.91585 7.86776   1.000 39.30687  ? 116 TYR A CZ  1 
ATOM   1396 O  OH  . TYR A 1 116 ? -9.04069  -5.13966 8.50210   1.000 53.17647  ? 116 TYR A OH  1 
ATOM   1397 N  N   . ILE A 1 117 ? -8.51821  2.77363  5.16615   1.000 18.09097  ? 117 ILE A N   1 
ATOM   1398 C  CA  . ILE A 1 117 ? -8.87269  4.04096  4.53451   1.000 18.43452  ? 117 ILE A CA  1 
ATOM   1399 C  C   . ILE A 1 117 ? -7.89739  4.34649  3.40083   1.000 20.71302  ? 117 ILE A C   1 
ATOM   1400 O  O   . ILE A 1 117 ? -8.29545  4.71559  2.29179   1.000 19.64072  ? 117 ILE A O   1 
ATOM   1401 C  CB  . ILE A 1 117 ? -8.88128  5.17289  5.57696   1.000 19.24816  ? 117 ILE A CB  1 
ATOM   1402 C  CG1 . ILE A 1 117 ? -10.04616 4.96947  6.55288   1.000 18.75699  ? 117 ILE A CG1 1 
ATOM   1403 C  CG2 . ILE A 1 117 ? -8.88326  6.58550  4.89270   1.000 18.66507  ? 117 ILE A CG2 1 
ATOM   1404 C  CD1 . ILE A 1 117 ? -10.02728 5.94815  7.69484   1.000 19.17218  ? 117 ILE A CD1 1 
ATOM   1405 N  N   . CYS A 1 118 ? -6.60534  4.23466  3.67511   1.000 19.53002  ? 118 CYS A N   1 
ATOM   1406 C  CA  . CYS A 1 118 ? -5.58790  4.56938  2.67483   1.000 19.10919  ? 118 CYS A CA  1 
ATOM   1407 C  C   . CYS A 1 118 ? -5.56200  3.55617  1.54446   1.000 22.28301  ? 118 CYS A C   1 
ATOM   1408 O  O   . CYS A 1 118 ? -5.24355  3.91427  0.41141   1.000 19.43357  ? 118 CYS A O   1 
ATOM   1409 C  CB  . CYS A 1 118 ? -4.21755  4.65413  3.33376   1.000 19.84231  ? 118 CYS A CB  1 
ATOM   1410 S  SG  . CYS A 1 118 ? -4.08952  6.11355  4.41516   1.000 23.92325  ? 118 CYS A SG  1 
ATOM   1411 N  N   . LEU A 1 119 ? -5.91841  2.30433  1.82755   1.000 18.76713  ? 119 LEU A N   1 
ATOM   1412 C  CA  . LEU A 1 119 ? -5.99238  1.27913  0.78220   1.000 19.55784  ? 119 LEU A CA  1 
ATOM   1413 C  C   . LEU A 1 119 ? -7.13265  1.56595  -0.18367  1.000 20.14396  ? 119 LEU A C   1 
ATOM   1414 O  O   . LEU A 1 119 ? -6.94416  1.53957  -1.40167  1.000 19.52615  ? 119 LEU A O   1 
ATOM   1415 C  CB  . LEU A 1 119 ? -6.12654  -0.11406 1.40550   1.000 19.99662  ? 119 LEU A CB  1 
ATOM   1416 C  CG  . LEU A 1 119 ? -6.12838  -1.22377 0.34422   1.000 24.36022  ? 119 LEU A CG  1 
ATOM   1417 C  CD1 . LEU A 1 119 ? -4.78809  -1.21952 -0.43178  1.000 23.70927  ? 119 LEU A CD1 1 
ATOM   1418 C  CD2 . LEU A 1 119 ? -6.36261  -2.58479 1.01321   1.000 24.15203  ? 119 LEU A CD2 1 
ATOM   1419 N  N   . SER A 1 120 ? -8.31824  1.88289  0.34237   1.000 19.75834  ? 120 SER A N   1 
ATOM   1420 C  CA  . SER A 1 120 ? -9.42866  2.30704  -0.50253  1.000 18.50439  ? 120 SER A CA  1 
ATOM   1421 C  C   . SER A 1 120 ? -9.02506  3.49188  -1.37255  1.000 17.25415  ? 120 SER A C   1 
ATOM   1422 O  O   . SER A 1 120 ? -9.26906  3.49791  -2.58052  1.000 18.90276  ? 120 SER A O   1 
ATOM   1423 C  CB  . SER A 1 120 ? -10.59373 2.69589  0.41404   1.000 18.94470  ? 120 SER A CB  1 
ATOM   1424 O  OG  . SER A 1 120 ? -11.71667 3.12739  -0.32827  1.000 21.67461  ? 120 SER A OG  1 
ATOM   1425 N  N   . ASN A 1 121 ? -8.39756  4.50134  -0.76634  1.000 17.50274  ? 121 ASN A N   1 
ATOM   1426 C  CA  . ASN A 1 121 ? -7.93234  5.67500  -1.50442  1.000 16.94356  ? 121 ASN A CA  1 
ATOM   1427 C  C   . ASN A 1 121 ? -6.90057  5.29725  -2.57197  1.000 17.69860  ? 121 ASN A C   1 
ATOM   1428 O  O   . ASN A 1 121 ? -6.93473  5.82732  -3.69508  1.000 18.73238  ? 121 ASN A O   1 
ATOM   1429 C  CB  . ASN A 1 121 ? -7.33592  6.67347  -0.50879  1.000 17.57400  ? 121 ASN A CB  1 
ATOM   1430 C  CG  . ASN A 1 121 ? -6.95587  7.98359  -1.17497  1.000 17.22972  ? 121 ASN A CG  1 
ATOM   1431 O  OD1 . ASN A 1 121 ? -7.81354  8.75578  -1.60639  1.000 19.57107  ? 121 ASN A OD1 1 
ATOM   1432 N  ND2 . ASN A 1 121 ? -5.65322  8.20574  -1.31584  1.000 18.30970  ? 121 ASN A ND2 1 
ATOM   1433 N  N   . PHE A 1 122 ? -6.00718  4.35204  -2.25890  1.000 18.58848  ? 122 PHE A N   1 
ATOM   1434 C  CA  . PHE A 1 122 ? -5.04911  3.89198  -3.26216  1.000 18.12301  ? 122 PHE A CA  1 
ATOM   1435 C  C   . PHE A 1 122 ? -5.74546  3.25264  -4.45682  1.000 18.36754  ? 122 PHE A C   1 
ATOM   1436 O  O   . PHE A 1 122 ? -5.38984  3.52669  -5.60837  1.000 19.87194  ? 122 PHE A O   1 
ATOM   1437 C  CB  . PHE A 1 122 ? -4.01893  2.94100  -2.65769  1.000 18.37769  ? 122 PHE A CB  1 
ATOM   1438 C  CG  . PHE A 1 122 ? -3.06595  2.42160  -3.68869  1.000 23.97248  ? 122 PHE A CG  1 
ATOM   1439 C  CD1 . PHE A 1 122 ? -2.06913  3.25118  -4.18208  1.000 24.77863  ? 122 PHE A CD1 1 
ATOM   1440 C  CD2 . PHE A 1 122 ? -3.20717  1.15190  -4.22260  1.000 34.11972  ? 122 PHE A CD2 1 
ATOM   1441 C  CE1 . PHE A 1 122 ? -1.20321  2.80211  -5.18620  1.000 30.47598  ? 122 PHE A CE1 1 
ATOM   1442 C  CE2 . PHE A 1 122 ? -2.34092  0.69470  -5.21977  1.000 25.78387  ? 122 PHE A CE2 1 
ATOM   1443 C  CZ  . PHE A 1 122 ? -1.34348  1.52719  -5.69719  1.000 29.85891  ? 122 PHE A CZ  1 
ATOM   1444 N  N   . PHE A 1 123 ? -6.78345  2.44364  -4.21686  1.000 19.48942  ? 123 PHE A N   1 
ATOM   1445 C  CA  . PHE A 1 123 ? -7.51575  1.85817  -5.33391  1.000 18.17212  ? 123 PHE A CA  1 
ATOM   1446 C  C   . PHE A 1 123 ? -8.20854  2.92053  -6.17136  1.000 19.27170  ? 123 PHE A C   1 
ATOM   1447 O  O   . PHE A 1 123 ? -8.24072  2.81861  -7.40786  1.000 20.49168  ? 123 PHE A O   1 
ATOM   1448 C  CB  . PHE A 1 123 ? -8.51244  0.81794  -4.81669  1.000 21.22990  ? 123 PHE A CB  1 
ATOM   1449 C  CG  . PHE A 1 123 ? -7.85205  -0.46908 -4.36982  1.000 24.55680  ? 123 PHE A CG  1 
ATOM   1450 C  CD1 . PHE A 1 123 ? -6.67729  -0.88999 -4.95716  1.000 35.70188  ? 123 PHE A CD1 1 
ATOM   1451 C  CD2 . PHE A 1 123 ? -8.38073  -1.21429 -3.33387  1.000 26.31009  ? 123 PHE A CD2 1 
ATOM   1452 C  CE1 . PHE A 1 123 ? -6.06566  -2.06575 -4.53964  1.000 49.87927  ? 123 PHE A CE1 1 
ATOM   1453 C  CE2 . PHE A 1 123 ? -7.76940  -2.37887 -2.91391  1.000 28.63809  ? 123 PHE A CE2 1 
ATOM   1454 C  CZ  . PHE A 1 123 ? -6.62296  -2.80655 -3.52525  1.000 28.50761  ? 123 PHE A CZ  1 
ATOM   1455 N  N   . MET A 1 124 ? -8.79277  3.92950  -5.52672  1.000 16.83683  ? 124 MET A N   1 
ATOM   1456 C  CA  . MET A 1 124 ? -9.34931  5.04583  -6.28396  1.000 20.22770  ? 124 MET A CA  1 
ATOM   1457 C  C   . MET A 1 124 ? -8.30651  5.63209  -7.24047  1.000 17.43305  ? 124 MET A C   1 
ATOM   1458 O  O   . MET A 1 124 ? -8.57022  5.83541  -8.43154  1.000 19.80236  ? 124 MET A O   1 
ATOM   1459 C  CB  . MET A 1 124 ? -9.81439  6.12668  -5.30141  1.000 17.54803  ? 124 MET A CB  1 
ATOM   1460 C  CG  . MET A 1 124 ? -10.38123 7.34851  -6.02741  1.000 18.99243  ? 124 MET A CG  1 
ATOM   1461 S  SD  . MET A 1 124 ? -10.64407 8.71217  -4.88675  1.000 19.76367  ? 124 MET A SD  1 
ATOM   1462 C  CE  . MET A 1 124 ? -8.95951  9.28530  -4.65024  1.000 17.01976  ? 124 MET A CE  1 
ATOM   1463 N  N   . LEU A 1 125 ? -7.11133  5.92090  -6.72981  1.000 17.61142  ? 125 LEU A N   1 
ATOM   1464 C  CA  . LEU A 1 125 ? -6.08531  6.55741  -7.55187  1.000 18.12371  ? 125 LEU A CA  1 
ATOM   1465 C  C   . LEU A 1 125 ? -5.57751  5.62352  -8.64106  1.000 18.42267  ? 125 LEU A C   1 
ATOM   1466 O  O   . LEU A 1 125 ? -5.29585  6.06271  -9.76407  1.000 19.70910  ? 125 LEU A O   1 
ATOM   1467 C  CB  . LEU A 1 125 ? -4.92061  6.95114  -6.65123  1.000 17.88858  ? 125 LEU A CB  1 
ATOM   1468 C  CG  . LEU A 1 125 ? -5.20676  8.04875  -5.62852  1.000 20.85120  ? 125 LEU A CG  1 
ATOM   1469 C  CD1 . LEU A 1 125 ? -3.97307  8.31842  -4.76199  1.000 19.70400  ? 125 LEU A CD1 1 
ATOM   1470 C  CD2 . LEU A 1 125 ? -5.70859  9.32239  -6.30195  1.000 18.79083  ? 125 LEU A CD2 1 
ATOM   1471 N  N   . LEU A 1 126 ? -5.41508  4.34303  -8.31561  1.000 20.31293  ? 126 LEU A N   1 
ATOM   1472 C  CA  . LEU A 1 126 ? -4.95315  3.39245  -9.33490  1.000 19.86677  ? 126 LEU A CA  1 
ATOM   1473 C  C   . LEU A 1 126 ? -5.94032  3.33233  -10.49568 1.000 21.88860  ? 126 LEU A C   1 
ATOM   1474 O  O   . LEU A 1 126 ? -5.54848  3.34178  -11.67704 1.000 20.76410  ? 126 LEU A O   1 
ATOM   1475 C  CB  . LEU A 1 126 ? -4.80043  1.99884  -8.71570  1.000 20.92902  ? 126 LEU A CB  1 
ATOM   1476 C  CG  . LEU A 1 126 ? -4.44720  0.86897  -9.67959  1.000 26.73000  ? 126 LEU A CG  1 
ATOM   1477 C  CD1 . LEU A 1 126 ? -3.12297  1.18917  -10.38291 1.000 31.22899  ? 126 LEU A CD1 1 
ATOM   1478 C  CD2 . LEU A 1 126 ? -4.38594  -0.45157 -8.88759  1.000 31.17207  ? 126 LEU A CD2 1 
ATOM   1479 N  N   . ILE A 1 127 ? -7.23541  3.28741  -10.17932 1.000 20.20739  ? 127 ILE A N   1 
ATOM   1480 C  CA  . ILE A 1 127 ? -8.25778  3.25108  -11.22500 1.000 20.73196  ? 127 ILE A CA  1 
ATOM   1481 C  C   . ILE A 1 127 ? -8.21082  4.53162  -12.05517 1.000 21.65942  ? 127 ILE A C   1 
ATOM   1482 O  O   . ILE A 1 127 ? -8.26016  4.49060  -13.29209 1.000 20.94804  ? 127 ILE A O   1 
ATOM   1483 C  CB  . ILE A 1 127 ? -9.65216  3.00758  -10.60246 1.000 19.58519  ? 127 ILE A CB  1 
ATOM   1484 C  CG1 . ILE A 1 127 ? -9.71467  1.57988  -10.04776 1.000 22.22796  ? 127 ILE A CG1 1 
ATOM   1485 C  CG2 . ILE A 1 127 ? -10.75651 3.24901  -11.63176 1.000 22.52575  ? 127 ILE A CG2 1 
ATOM   1486 C  CD1 . ILE A 1 127 ? -10.86658 1.29658  -9.07575  1.000 22.79108  ? 127 ILE A CD1 1 
ATOM   1487 N  N   . GLY A 1 128 ? -8.10686  5.68210  -11.38901 1.000 18.87378  ? 128 GLY A N   1 
ATOM   1488 C  CA  . GLY A 1 128 ? -7.96038  6.93296  -12.10812 1.000 20.00590  ? 128 GLY A CA  1 
ATOM   1489 C  C   . GLY A 1 128 ? -6.73499  6.95161  -13.00395 1.000 19.76729  ? 128 GLY A C   1 
ATOM   1490 O  O   . GLY A 1 128 ? -6.79769  7.42611  -14.13566 1.000 20.22244  ? 128 GLY A O   1 
ATOM   1491 N  N   . TYR A 1 129 ? -5.60825  6.42407  -12.51479 1.000 18.23385  ? 129 TYR A N   1 
ATOM   1492 C  CA  . TYR A 1 129 ? -4.39333  6.42313  -13.32393 1.000 19.09463  ? 129 TYR A CA  1 
ATOM   1493 C  C   . TYR A 1 129 ? -4.58947  5.57843  -14.57416 1.000 20.77649  ? 129 TYR A C   1 
ATOM   1494 O  O   . TYR A 1 129 ? -4.22862  5.99045  -15.68808 1.000 22.26619  ? 129 TYR A O   1 
ATOM   1495 C  CB  . TYR A 1 129 ? -3.22178  5.87799  -12.49171 1.000 19.20119  ? 129 TYR A CB  1 
ATOM   1496 C  CG  . TYR A 1 129 ? -1.91840  5.85806  -13.26298 1.000 23.27044  ? 129 TYR A CG  1 
ATOM   1497 C  CD1 . TYR A 1 129 ? -1.14576  7.00761  -13.36382 1.000 24.21073  ? 129 TYR A CD1 1 
ATOM   1498 C  CD2 . TYR A 1 129 ? -1.47252  4.70216  -13.89301 1.000 28.40713  ? 129 TYR A CD2 1 
ATOM   1499 C  CE1 . TYR A 1 129 ? 0.03690   7.01647  -14.06632 1.000 25.27139  ? 129 TYR A CE1 1 
ATOM   1500 C  CE2 . TYR A 1 129 ? -0.27524  4.70468  -14.61356 1.000 28.10372  ? 129 TYR A CE2 1 
ATOM   1501 C  CZ  . TYR A 1 129 ? 0.46641   5.88084  -14.67847 1.000 27.45071  ? 129 TYR A CZ  1 
ATOM   1502 O  OH  . TYR A 1 129 ? 1.65140   5.90622  -15.37727 1.000 44.78814  ? 129 TYR A OH  1 
ATOM   1503 N  N   . LEU A 1 130 ? -5.18254  4.40011  -14.41021 1.000 18.67254  ? 130 LEU A N   1 
ATOM   1504 C  CA  . LEU A 1 130 ? -5.52963  3.55996  -15.55348 1.000 22.97126  ? 130 LEU A CA  1 
ATOM   1505 C  C   . LEU A 1 130 ? -6.43289  4.29592  -16.54003 1.000 22.78179  ? 130 LEU A C   1 
ATOM   1506 O  O   . LEU A 1 130 ? -6.25660  4.17660  -17.75466 1.000 24.09865  ? 130 LEU A O   1 
ATOM   1507 C  CB  . LEU A 1 130 ? -6.17547  2.26513  -15.05091 1.000 22.68519  ? 130 LEU A CB  1 
ATOM   1508 C  CG  . LEU A 1 130 ? -5.26420  1.33014  -14.23214 1.000 24.31307  ? 130 LEU A CG  1 
ATOM   1509 C  CD1 . LEU A 1 130 ? -6.07764  0.18939  -13.67281 1.000 27.57108  ? 130 LEU A CD1 1 
ATOM   1510 C  CD2 . LEU A 1 130 ? -4.10156  0.76701  -15.06846 1.000 26.76134  ? 130 LEU A CD2 1 
ATOM   1511 N  N   . GLY A 1 131 ? -7.39826  5.06921  -16.04094 1.000 21.22183  ? 131 GLY A N   1 
ATOM   1512 C  CA  . GLY A 1 131 ? -8.25759  5.83198  -16.94135 1.000 21.43857  ? 131 GLY A CA  1 
ATOM   1513 C  C   . GLY A 1 131 ? -7.54064  7.00927  -17.59463 1.000 21.21074  ? 131 GLY A C   1 
ATOM   1514 O  O   . GLY A 1 131 ? -7.76100  7.30077  -18.77490 1.000 23.75691  ? 131 GLY A O   1 
ATOM   1515 N  N   A GLU A 1 132 ? -6.71810  7.71230  -16.82062 0.700 21.73503  ? 132 GLU A N   1 
ATOM   1516 N  N   B GLU A 1 132 ? -6.66826  7.67606  -16.84255 0.300 21.97711  ? 132 GLU A N   1 
ATOM   1517 C  CA  A GLU A 1 132 ? -6.06280  8.91840  -17.32446 0.700 22.37554  ? 132 GLU A CA  1 
ATOM   1518 C  CA  B GLU A 1 132 ? -5.88020  8.76239  -17.42075 0.300 23.60665  ? 132 GLU A CA  1 
ATOM   1519 C  C   A GLU A 1 132 ? -5.07538  8.57125  -18.42285 0.700 23.74308  ? 132 GLU A C   1 
ATOM   1520 C  C   B GLU A 1 132 ? -4.96360  8.23859  -18.51442 0.300 26.50993  ? 132 GLU A C   1 
ATOM   1521 O  O   A GLU A 1 132 ? -4.87742  9.36800  -19.34453 0.700 25.82589  ? 132 GLU A O   1 
ATOM   1522 O  O   B GLU A 1 132 ? -4.84846  8.84485  -19.58735 0.300 28.44194  ? 132 GLU A O   1 
ATOM   1523 C  CB  A GLU A 1 132 ? -5.35809  9.63406  -16.16232 0.700 25.50002  ? 132 GLU A CB  1 
ATOM   1524 C  CB  B GLU A 1 132 ? -5.06301  9.44585  -16.32406 0.300 20.79649  ? 132 GLU A CB  1 
ATOM   1525 C  CG  A GLU A 1 132 ? -4.84243  11.03351 -16.46095 0.700 25.36753  ? 132 GLU A CG  1 
ATOM   1526 C  CG  B GLU A 1 132 ? -4.55189  10.81346 -16.71791 0.300 24.63544  ? 132 GLU A CG  1 
ATOM   1527 C  CD  A GLU A 1 132 ? -5.89513  11.94870 -17.05639 0.700 25.40708  ? 132 GLU A CD  1 
ATOM   1528 C  CD  B GLU A 1 132 ? -5.64747  11.69719 -17.27968 0.300 22.05784  ? 132 GLU A CD  1 
ATOM   1529 O  OE1 A GLU A 1 132 ? -6.93061  12.20672 -16.39804 0.700 18.44425  ? 132 GLU A OE1 1 
ATOM   1530 O  OE1 B GLU A 1 132 ? -6.74815  11.75413 -16.68445 0.300 23.02147  ? 132 GLU A OE1 1 
ATOM   1531 O  OE2 A GLU A 1 132 ? -5.66874  12.42135 -18.18276 0.700 27.10250  ? 132 GLU A OE2 1 
ATOM   1532 O  OE2 B GLU A 1 132 ? -5.41118  12.33136 -18.32532 0.300 25.92319  ? 132 GLU A OE2 1 
ATOM   1533 N  N   A THR A 1 133 ? -4.46458  7.38145  -18.35024 0.700 23.71334  ? 133 THR A N   1 
ATOM   1534 N  N   B THR A 1 133 ? -4.31319  7.10355  -18.26522 0.300 23.76656  ? 133 THR A N   1 
ATOM   1535 C  CA  A THR A 1 133 ? -3.52932  6.88648  -19.35550 0.700 20.91975  ? 133 THR A CA  1 
ATOM   1536 C  CA  B THR A 1 133 ? -3.50302  6.42853  -19.26824 0.300 25.58299  ? 133 THR A CA  1 
ATOM   1537 C  C   A THR A 1 133 ? -4.19902  5.99301  -20.39924 0.700 26.69148  ? 133 THR A C   1 
ATOM   1538 C  C   B THR A 1 133 ? -4.34124  5.63635  -20.26035 0.300 26.51406  ? 133 THR A C   1 
ATOM   1539 O  O   A THR A 1 133 ? -3.50924  5.43350  -21.25742 0.700 28.12340  ? 133 THR A O   1 
ATOM   1540 O  O   B THR A 1 133 ? -3.78724  4.80828  -20.99027 0.300 27.63175  ? 133 THR A O   1 
ATOM   1541 C  CB  A THR A 1 133 ? -2.34800  6.15361  -18.69280 0.700 23.62179  ? 133 THR A CB  1 
ATOM   1542 C  CB  B THR A 1 133 ? -2.47484  5.50723  -18.60055 0.300 26.18561  ? 133 THR A CB  1 
ATOM   1543 O  OG1 A THR A 1 133 ? -2.82298  5.01400  -17.95927 0.700 24.96556  ? 133 THR A OG1 1 
ATOM   1544 O  OG1 B THR A 1 133 ? -3.14528  4.55850  -17.75961 0.300 22.78519  ? 133 THR A OG1 1 
ATOM   1545 C  CG2 A THR A 1 133 ? -1.59572  7.07490  -17.73496 0.700 28.48900  ? 133 THR A CG2 1 
ATOM   1546 C  CG2 B THR A 1 133 ? -1.49746  6.31449  -17.75766 0.300 25.42538  ? 133 THR A CG2 1 
ATOM   1547 N  N   A LYS A 1 134 ? -5.52319  5.84625  -20.33427 0.700 25.85702  ? 134 LYS A N   1 
ATOM   1548 N  N   B LYS A 1 134 ? -5.65746  5.85693  -20.27566 0.300 26.61767  ? 134 LYS A N   1 
ATOM   1549 C  CA  A LYS A 1 134 ? -6.33347  5.22348  -21.38258 0.700 28.07741  ? 134 LYS A CA  1 
ATOM   1550 C  CA  B LYS A 1 134 ? -6.58728  5.24235  -21.22211 0.300 27.43023  ? 134 LYS A CA  1 
ATOM   1551 C  C   A LYS A 1 134 ? -6.15679  3.70657  -21.46493 0.700 27.47537  ? 134 LYS A C   1 
ATOM   1552 C  C   B LYS A 1 134 ? -6.49357  3.71875  -21.25467 0.300 30.43878  ? 134 LYS A C   1 
ATOM   1553 O  O   A LYS A 1 134 ? -6.30332  3.11748  -22.53632 0.700 31.85936  ? 134 LYS A O   1 
ATOM   1554 O  O   B LYS A 1 134 ? -6.88873  3.09159  -22.24330 0.300 32.76907  ? 134 LYS A O   1 
ATOM   1555 C  CB  A LYS A 1 134 ? -6.16949  5.91425  -22.75030 0.700 33.11873  ? 134 LYS A CB  1 
ATOM   1556 C  CB  B LYS A 1 134 ? -6.46200  5.85244  -22.62543 0.300 34.24199  ? 134 LYS A CB  1 
ATOM   1557 C  CG  A LYS A 1 134 ? -6.42114  7.43182  -22.71149 0.700 36.60046  ? 134 LYS A CG  1 
ATOM   1558 C  CG  B LYS A 1 134 ? -6.82780  7.33346  -22.68074 0.300 36.65113  ? 134 LYS A CG  1 
ATOM   1559 C  CD  A LYS A 1 134 ? -6.46037  8.02678  -24.11138 0.700 44.77328  ? 134 LYS A CD  1 
ATOM   1560 C  CD  B LYS A 1 134 ? -6.44439  7.95179  -24.01216 0.300 45.09811  ? 134 LYS A CD  1 
ATOM   1561 C  CE  A LYS A 1 134 ? -6.46921  9.54959  -24.10167 0.700 47.74525  ? 134 LYS A CE  1 
ATOM   1562 C  CE  B LYS A 1 134 ? -6.93405  9.38511  -24.12210 0.300 46.00255  ? 134 LYS A CE  1 
ATOM   1563 N  NZ  A LYS A 1 134 ? -6.61622  10.10386 -25.49142 0.700 47.75874  ? 134 LYS A NZ  1 
ATOM   1564 N  NZ  B LYS A 1 134 ? -6.55563  10.00034 -25.42986 0.300 48.15262  ? 134 LYS A NZ  1 
ATOM   1565 N  N   A GLN A 1 135 ? -5.87421  3.06228  -20.32791 0.700 28.06580  ? 135 GLN A N   1 
ATOM   1566 N  N   B GLN A 1 135 ? -5.98241  3.11004  -20.18015 0.300 29.56871  ? 135 GLN A N   1 
ATOM   1567 C  CA  A GLN A 1 135 ? -5.83749  1.60864  -20.22127 0.700 31.62088  ? 135 GLN A CA  1 
ATOM   1568 C  CA  B GLN A 1 135 ? -5.89549  1.65571  -20.12021 0.300 31.61626  ? 135 GLN A CA  1 
ATOM   1569 C  C   A GLN A 1 135 ? -7.21057  1.00974  -19.94768 0.700 39.30161  ? 135 GLN A C   1 
ATOM   1570 C  C   B GLN A 1 135 ? -7.26974  1.02678  -19.92780 0.300 38.62129  ? 135 GLN A C   1 
ATOM   1571 O  O   A GLN A 1 135 ? -7.43278  -0.17075 -20.25471 0.700 38.63822  ? 135 GLN A O   1 
ATOM   1572 O  O   B GLN A 1 135 ? -7.50228  -0.10435 -20.37269 0.300 37.52952  ? 135 GLN A O   1 
ATOM   1573 C  CB  A GLN A 1 135 ? -4.82085  1.18964  -19.14778 0.700 30.74250  ? 135 GLN A CB  1 
ATOM   1574 C  CB  B GLN A 1 135 ? -4.91891  1.23200  -19.01867 0.300 31.08899  ? 135 GLN A CB  1 
ATOM   1575 C  CG  A GLN A 1 135 ? -3.44902  1.75933  -19.43975 0.700 26.87893  ? 135 GLN A CG  1 
ATOM   1576 C  CG  B GLN A 1 135 ? -4.30890  -0.14202 -19.23408 0.300 41.76968  ? 135 GLN A CG  1 
ATOM   1577 C  CD  A GLN A 1 135 ? -2.39317  1.41447  -18.41390 0.700 47.94249  ? 135 GLN A CD  1 
ATOM   1578 C  CD  B GLN A 1 135 ? -3.06433  -0.37146 -18.39977 0.300 39.74074  ? 135 GLN A CD  1 
ATOM   1579 O  OE1 A GLN A 1 135 ? -1.78873  2.30820  -17.81877 0.700 39.77208  ? 135 GLN A OE1 1 
ATOM   1580 O  OE1 B GLN A 1 135 ? -2.21485  0.51017  -18.27628 0.300 47.71138  ? 135 GLN A OE1 1 
ATOM   1581 N  NE2 A GLN A 1 135 ? -2.12836  0.11980  -18.23571 0.700 43.00448  ? 135 GLN A NE2 1 
ATOM   1582 N  NE2 B GLN A 1 135 ? -2.94777  -1.56279 -17.82587 0.300 50.36837  ? 135 GLN A NE2 1 
ATOM   1583 N  N   A ILE A 1 136 ? -8.12859  1.80590  -19.39405 0.700 32.38973  ? 136 ILE A N   1 
ATOM   1584 N  N   B ILE A 1 136 ? -8.18618  1.74357  -19.27342 0.300 31.99195  ? 136 ILE A N   1 
ATOM   1585 C  CA  A ILE A 1 136 ? -9.53999  1.47759  -19.24049 0.700 27.72600  ? 136 ILE A CA  1 
ATOM   1586 C  CA  B ILE A 1 136 ? -9.59250  1.37600  -19.18291 0.300 28.81885  ? 136 ILE A CA  1 
ATOM   1587 C  C   A ILE A 1 136 ? -10.34499 2.67782  -19.72974 0.700 31.82716  ? 136 ILE A C   1 
ATOM   1588 C  C   B ILE A 1 136 ? -10.41605 2.58646  -19.59726 0.300 30.81545  ? 136 ILE A C   1 
ATOM   1589 O  O   A ILE A 1 136 ? -9.82683  3.78777  -19.85977 0.700 30.55955  ? 136 ILE A O   1 
ATOM   1590 O  O   B ILE A 1 136 ? -9.92312  3.71512  -19.65073 0.300 30.19113  ? 136 ILE A O   1 
ATOM   1591 C  CB  A ILE A 1 136 ? -9.92784  1.14188  -17.78025 0.700 27.33347  ? 136 ILE A CB  1 
ATOM   1592 C  CB  B ILE A 1 136 ? -10.02682 0.90357  -17.77435 0.300 29.24595  ? 136 ILE A CB  1 
ATOM   1593 C  CG1 A ILE A 1 136 ? -9.51728  2.27628  -16.83890 0.700 22.16853  ? 136 ILE A CG1 1 
ATOM   1594 C  CG1 B ILE A 1 136 ? -8.86404  0.97277  -16.78741 0.300 33.91521  ? 136 ILE A CG1 1 
ATOM   1595 C  CG2 A ILE A 1 136 ? -9.31176  -0.18750 -17.31273 0.700 25.71627  ? 136 ILE A CG2 1 
ATOM   1596 C  CG2 B ILE A 1 136 ? -10.58967 -0.51153 -17.82352 0.300 37.64162  ? 136 ILE A CG2 1 
ATOM   1597 C  CD1 A ILE A 1 136 ? -10.04893 2.10363  -15.42890 0.700 24.80865  ? 136 ILE A CD1 1 
ATOM   1598 C  CD1 B ILE A 1 136 ? -7.94170  -0.22706 -16.83869 0.300 32.21369  ? 136 ILE A CD1 1 
ATOM   1599 N  N   A ASN A 1 137 ? -11.63125 2.45345  -19.99334 0.700 30.87920  ? 137 ASN A N   1 
ATOM   1600 N  N   B ASN A 1 137 ? -11.69169 2.34000  -19.87871 0.300 30.43080  ? 137 ASN A N   1 
ATOM   1601 C  CA  A ASN A 1 137 ? -12.44036 3.53687  -20.53941 0.700 28.84821  ? 137 ASN A CA  1 
ATOM   1602 C  CA  B ASN A 1 137 ? -12.56692 3.40127  -20.35205 0.300 28.53979  ? 137 ASN A CA  1 
ATOM   1603 C  C   A ASN A 1 137 ? -12.90376 4.50407  -19.45052 0.700 33.17651  ? 137 ASN A C   1 
ATOM   1604 C  C   B ASN A 1 137 ? -12.89106 4.38731  -19.23279 0.300 34.11695  ? 137 ASN A C   1 
ATOM   1605 O  O   A ASN A 1 137 ? -12.86312 4.20570  -18.25097 0.700 30.94216  ? 137 ASN A O   1 
ATOM   1606 O  O   B ASN A 1 137 ? -12.71739 4.10425  -18.04335 0.300 28.59081  ? 137 ASN A O   1 
ATOM   1607 C  CB  A ASN A 1 137 ? -13.65042 2.99443  -21.31356 0.700 32.34076  ? 137 ASN A CB  1 
ATOM   1608 C  CB  B ASN A 1 137 ? -13.86519 2.80993  -20.89953 0.300 34.69643  ? 137 ASN A CB  1 
ATOM   1609 C  CG  A ASN A 1 137 ? -14.65261 2.29563  -20.41474 0.700 39.85709  ? 137 ASN A CG  1 
ATOM   1610 C  CG  B ASN A 1 137 ? -14.64215 2.05310  -19.84552 0.300 37.62748  ? 137 ASN A CG  1 
ATOM   1611 O  OD1 A ASN A 1 137 ? -15.38636 2.94066  -19.66597 0.700 35.35048  ? 137 ASN A OD1 1 
ATOM   1612 O  OD1 B ASN A 1 137 ? -15.48891 2.61868  -19.15896 0.300 37.04276  ? 137 ASN A OD1 1 
ATOM   1613 N  ND2 A ASN A 1 137 ? -14.69744 0.96928  -20.49488 0.700 51.33275  ? 137 ASN A ND2 1 
ATOM   1614 N  ND2 B ASN A 1 137 ? -14.34857 0.76669  -19.70376 0.300 45.28568  ? 137 ASN A ND2 1 
ATOM   1615 N  N   A LYS A 1 138 ? -13.35452 5.68518  -19.89333 0.700 35.72669  ? 138 LYS A N   1 
ATOM   1616 N  N   B LYS A 1 138 ? -13.38006 5.56459  -19.63588 0.300 34.06736  ? 138 LYS A N   1 
ATOM   1617 C  CA  A LYS A 1 138 ? -13.72760 6.74734  -18.95979 0.700 29.43305  ? 138 LYS A CA  1 
ATOM   1618 C  CA  B LYS A 1 138 ? -13.67051 6.62461  -18.67432 0.300 28.24325  ? 138 LYS A CA  1 
ATOM   1619 C  C   A LYS A 1 138 ? -14.86891 6.31870  -18.05211 0.700 33.28142  ? 138 LYS A C   1 
ATOM   1620 C  C   B LYS A 1 138 ? -14.88942 6.30040  -17.82048 0.300 33.34068  ? 138 LYS A C   1 
ATOM   1621 O  O   A LYS A 1 138 ? -14.88670 6.65878  -16.86246 0.700 29.17654  ? 138 LYS A O   1 
ATOM   1622 O  O   B LYS A 1 138 ? -14.94263 6.69507  -16.64972 0.300 29.11629  ? 138 LYS A O   1 
ATOM   1623 C  CB  A LYS A 1 138 ? -14.11524 8.01921  -19.71945 0.700 35.42096  ? 138 LYS A CB  1 
ATOM   1624 C  CB  B LYS A 1 138 ? -13.84940 7.96086  -19.39871 0.300 36.36484  ? 138 LYS A CB  1 
ATOM   1625 C  CG  A LYS A 1 138 ? -12.93735 8.83078  -20.22085 0.700 33.93359  ? 138 LYS A CG  1 
ATOM   1626 C  CG  B LYS A 1 138 ? -14.91777 7.92616  -20.47188 0.300 34.32093  ? 138 LYS A CG  1 
ATOM   1627 C  CD  A LYS A 1 138 ? -13.32875 10.27744 -20.49173 0.700 42.63044  ? 138 LYS A CD  1 
ATOM   1628 C  CD  B LYS A 1 138 ? -14.80474 9.08223  -21.44954 0.300 37.24698  ? 138 LYS A CD  1 
ATOM   1629 C  CE  A LYS A 1 138 ? -12.07895 11.10935 -20.73011 0.700 52.36305  ? 138 LYS A CE  1 
ATOM   1630 C  CE  B LYS A 1 138 ? -15.78691 8.89057  -22.60081 0.300 42.72478  ? 138 LYS A CE  1 
ATOM   1631 N  NZ  A LYS A 1 138 ? -12.16851 12.47513 -20.15266 0.700 41.11861  ? 138 LYS A NZ  1 
ATOM   1632 N  NZ  B LYS A 1 138 ? -15.61645 9.89437  -23.68388 0.300 40.12176  ? 138 LYS A NZ  1 
ATOM   1633 N  N   A MET A 1 139 ? -15.83891 5.57625  -18.59555 0.700 31.68036  ? 139 MET A N   1 
ATOM   1634 N  N   B MET A 1 139 ? -15.87673 5.59307  -18.37865 0.300 32.63668  ? 139 MET A N   1 
ATOM   1635 C  CA  A MET A 1 139 ? -17.00346 5.21146  -17.79583 0.700 33.64972  ? 139 MET A CA  1 
ATOM   1636 C  CA  B MET A 1 139 ? -17.02758 5.18954  -17.57620 0.300 31.75780  ? 139 MET A CA  1 
ATOM   1637 C  C   A MET A 1 139 ? -16.61520 4.27920  -16.65950 0.700 30.45060  ? 139 MET A C   1 
ATOM   1638 C  C   B MET A 1 139 ? -16.59972 4.25418  -16.45688 0.300 31.48500  ? 139 MET A C   1 
ATOM   1639 O  O   A MET A 1 139 ? -17.05098 4.47053  -15.51844 0.700 32.89399  ? 139 MET A O   1 
ATOM   1640 O  O   B MET A 1 139 ? -16.95434 4.45846  -15.28972 0.300 32.59711  ? 139 MET A O   1 
ATOM   1641 C  CB  A MET A 1 139 ? -18.09468 4.59884  -18.68167 0.700 38.04427  ? 139 MET A CB  1 
ATOM   1642 C  CB  B MET A 1 139 ? -18.09313 4.53081  -18.45456 0.300 40.39552  ? 139 MET A CB  1 
ATOM   1643 C  CG  A MET A 1 139 ? -19.49398 4.71210  -18.09062 0.700 50.44806  ? 139 MET A CG  1 
ATOM   1644 C  CG  B MET A 1 139 ? -19.14285 3.76463  -17.65938 0.300 40.02516  ? 139 MET A CG  1 
ATOM   1645 S  SD  A MET A 1 139 ? -20.81762 4.16425  -19.19799 0.700 72.06311  ? 139 MET A SD  1 
ATOM   1646 S  SD  B MET A 1 139 ? -20.58695 3.32985  -18.64445 0.300 65.79615  ? 139 MET A SD  1 
ATOM   1647 C  CE  A MET A 1 139 ? -19.98970 4.17625  -20.78916 0.700 50.33046  ? 139 MET A CE  1 
ATOM   1648 C  CE  B MET A 1 139 ? -21.17051 4.96168  -19.10223 0.300 57.98281  ? 139 MET A CE  1 
ATOM   1649 N  N   A LEU A 1 140 ? -15.76281 3.28992  -16.94335 0.700 32.21807  ? 140 LEU A N   1 
ATOM   1650 N  N   B LEU A 1 140 ? -15.81754 3.22652  -16.79613 0.300 32.25139  ? 140 LEU A N   1 
ATOM   1651 C  CA  A LEU A 1 140 ? -15.28786 2.39080  -15.89751 0.700 29.22665  ? 140 LEU A CA  1 
ATOM   1652 C  CA  B LEU A 1 140 ? -15.28174 2.33776  -15.77369 0.300 29.72927  ? 140 LEU A CA  1 
ATOM   1653 C  C   A LEU A 1 140 ? -14.47591 3.14874  -14.85101 0.700 29.82944  ? 140 LEU A C   1 
ATOM   1654 C  C   B LEU A 1 140 ? -14.38906 3.09987  -14.80358 0.300 30.28598  ? 140 LEU A C   1 
ATOM   1655 O  O   A LEU A 1 140 ? -14.57716 2.86947  -13.65058 0.700 30.28809  ? 140 LEU A O   1 
ATOM   1656 O  O   B LEU A 1 140 ? -14.34757 2.78178  -13.60874 0.300 28.51996  ? 140 LEU A O   1 
ATOM   1657 C  CB  A LEU A 1 140 ? -14.45151 1.27169  -16.52224 0.700 34.44179  ? 140 LEU A CB  1 
ATOM   1658 C  CB  B LEU A 1 140 ? -14.52024 1.18219  -16.42604 0.300 33.49245  ? 140 LEU A CB  1 
ATOM   1659 C  CG  A LEU A 1 140 ? -13.89851 0.23847  -15.54368 0.700 35.30740  ? 140 LEU A CG  1 
ATOM   1660 C  CG  B LEU A 1 140 ? -14.10543 0.00855  -15.53316 0.300 36.88058  ? 140 LEU A CG  1 
ATOM   1661 C  CD1 A LEU A 1 140 ? -15.02849 -0.30033 -14.68316 0.700 42.82623  ? 140 LEU A CD1 1 
ATOM   1662 C  CD1 B LEU A 1 140 ? -12.73162 0.22225  -14.91284 0.300 37.57203  ? 140 LEU A CD1 1 
ATOM   1663 C  CD2 A LEU A 1 140 ? -13.19542 -0.89729 -16.28663 0.700 38.72132  ? 140 LEU A CD2 1 
ATOM   1664 C  CD2 B LEU A 1 140 ? -15.15051 -0.24144 -14.45208 0.300 41.35507  ? 140 LEU A CD2 1 
ATOM   1665 N  N   . THR A 1 141 ? -13.65865 4.10721  -15.29220 1.000 27.95112  ? 141 THR A N   1 
ATOM   1666 C  CA  . THR A 1 141 ? -12.84448 4.89371  -14.36993 1.000 25.33402  ? 141 THR A CA  1 
ATOM   1667 C  C   . THR A 1 141 ? -13.72959 5.68307  -13.41977 1.000 22.19526  ? 141 THR A C   1 
ATOM   1668 O  O   . THR A 1 141 ? -13.48642 5.72587  -12.20710 1.000 23.61783  ? 141 THR A O   1 
ATOM   1669 C  CB  . THR A 1 141 ? -11.95220 5.85929  -15.15784 1.000 26.46166  ? 141 THR A CB  1 
ATOM   1670 O  OG1 . THR A 1 141 ? -11.17848 5.14274  -16.12283 1.000 26.22991  ? 141 THR A OG1 1 
ATOM   1671 C  CG2 . THR A 1 141 ? -10.99541 6.59594  -14.20173 1.000 21.87193  ? 141 THR A CG2 1 
ATOM   1672 N  N   A LEU A 1 142 ? -14.78911 6.28893  -13.94048 0.700 24.67948  ? 142 LEU A N   1 
ATOM   1673 N  N   B LEU A 1 142 ? -14.74888 6.35241  -13.96269 0.300 25.24865  ? 142 LEU A N   1 
ATOM   1674 C  CA  A LEU A 1 142 ? -15.62671 7.12363  -13.09338 0.700 27.65274  ? 142 LEU A CA  1 
ATOM   1675 C  CA  B LEU A 1 142 ? -15.59526 7.20361  -13.13506 0.300 27.87068  ? 142 LEU A CA  1 
ATOM   1676 C  C   A LEU A 1 142 ? -16.43760 6.29167  -12.10713 0.700 26.41128  ? 142 LEU A C   1 
ATOM   1677 C  C   B LEU A 1 142 ? -16.41424 6.37791  -12.15282 0.300 26.40284  ? 142 LEU A C   1 
ATOM   1678 O  O   A LEU A 1 142 ? -16.61659 6.69779  -10.95323 0.700 27.37997  ? 142 LEU A O   1 
ATOM   1679 O  O   B LEU A 1 142 ? -16.58588 6.77717  -10.99575 0.300 27.99283  ? 142 LEU A O   1 
ATOM   1680 C  CB  A LEU A 1 142 ? -16.52619 7.99624  -13.95627 0.700 27.84395  ? 142 LEU A CB  1 
ATOM   1681 C  CB  B LEU A 1 142 ? -16.49710 8.07740  -14.00989 0.300 28.06717  ? 142 LEU A CB  1 
ATOM   1682 C  CG  A LEU A 1 142 ? -15.80818 9.12556  -14.68757 0.700 25.56564  ? 142 LEU A CG  1 
ATOM   1683 C  CG  B LEU A 1 142 ? -17.32831 9.15070  -13.29246 0.300 26.03062  ? 142 LEU A CG  1 
ATOM   1684 C  CD1 A LEU A 1 142 ? -16.78309 9.71192  -15.68452 0.700 28.83945  ? 142 LEU A CD1 1 
ATOM   1685 C  CD1 B LEU A 1 142 ? -16.42926 10.14186 -12.56951 0.300 23.66059  ? 142 LEU A CD1 1 
ATOM   1686 C  CD2 A LEU A 1 142 ? -15.30563 10.21320 -13.71298 0.700 26.50410  ? 142 LEU A CD2 1 
ATOM   1687 C  CD2 B LEU A 1 142 ? -18.24574 9.87729  -14.26134 0.300 24.11889  ? 142 LEU A CD2 1 
ATOM   1688 N  N   A PHE A 1 143 ? -16.92230 5.12334  -12.52320 0.500 27.96791  ? 143 PHE A N   1 
ATOM   1689 N  N   B PHE A 1 143 ? -16.91765 5.22143  -12.58584 0.500 27.45076  ? 143 PHE A N   1 
ATOM   1690 C  CA  A PHE A 1 143 ? -17.70101 4.30541  -11.59392 0.500 31.11841  ? 143 PHE A CA  1 
ATOM   1691 C  CA  B PHE A 1 143 ? -17.64239 4.34624  -11.66631 0.500 31.19416  ? 143 PHE A CA  1 
ATOM   1692 C  C   A PHE A 1 143 ? -16.81625 3.60190  -10.57165 0.500 27.19671  ? 143 PHE A C   1 
ATOM   1693 C  C   B PHE A 1 143 ? -16.71669 3.80462  -10.58497 0.500 27.27522  ? 143 PHE A C   1 
ATOM   1694 O  O   A PHE A 1 143 ? -17.16291 3.53465  -9.38569  0.500 28.45971  ? 143 PHE A O   1 
ATOM   1695 O  O   B PHE A 1 143 ? -16.94012 4.02877  -9.38599  0.500 25.20056  ? 143 PHE A O   1 
ATOM   1696 C  CB  A PHE A 1 143 ? -18.58663 3.31285  -12.34835 0.500 37.36119  ? 143 PHE A CB  1 
ATOM   1697 C  CB  B PHE A 1 143 ? -18.28769 3.17752  -12.41385 0.500 34.46231  ? 143 PHE A CB  1 
ATOM   1698 C  CG  A PHE A 1 143 ? -19.84840 3.92650  -12.87370 0.500 35.54430  ? 143 PHE A CG  1 
ATOM   1699 C  CG  B PHE A 1 143 ? -18.81303 2.11563  -11.49475 0.500 35.19887  ? 143 PHE A CG  1 
ATOM   1700 C  CD1 A PHE A 1 143 ? -20.81109 4.40515  -11.99986 0.500 38.88152  ? 143 PHE A CD1 1 
ATOM   1701 C  CD1 B PHE A 1 143 ? -19.93981 2.35559  -10.72266 0.500 43.79271  ? 143 PHE A CD1 1 
ATOM   1702 C  CD2 A PHE A 1 143 ? -20.06387 4.05103  -14.23428 0.500 43.47501  ? 143 PHE A CD2 1 
ATOM   1703 C  CD2 B PHE A 1 143 ? -18.16439 0.89788  -11.36376 0.500 40.18418  ? 143 PHE A CD2 1 
ATOM   1704 C  CE1 A PHE A 1 143 ? -21.96984 4.98310  -12.47625 0.500 44.67713  ? 143 PHE A CE1 1 
ATOM   1705 C  CE1 B PHE A 1 143 ? -20.42166 1.39203  -9.84988  0.500 45.49290  ? 143 PHE A CE1 1 
ATOM   1706 C  CE2 A PHE A 1 143 ? -21.21919 4.63185  -14.71366 0.500 44.60538  ? 143 PHE A CE2 1 
ATOM   1707 C  CE2 B PHE A 1 143 ? -18.64136 -0.06909 -10.48961 0.500 40.55732  ? 143 PHE A CE2 1 
ATOM   1708 C  CZ  A PHE A 1 143 ? -22.17276 5.09703  -13.83309 0.500 51.51019  ? 143 PHE A CZ  1 
ATOM   1709 C  CZ  B PHE A 1 143 ? -19.77047 0.18100  -9.73423  0.500 42.96943  ? 143 PHE A CZ  1 
ATOM   1710 N  N   . GLY A 1 144 ? -15.67144 3.07817  -11.00580 1.000 27.48424  ? 144 GLY A N   1 
ATOM   1711 C  CA  . GLY A 1 144 ? -14.76758 2.44372  -10.06341 1.000 29.48268  ? 144 GLY A CA  1 
ATOM   1712 C  C   . GLY A 1 144 ? -14.10434 3.43869  -9.13430  1.000 27.16048  ? 144 GLY A C   1 
ATOM   1713 O  O   . GLY A 1 144 ? -14.00525 3.20050  -7.92894  1.000 24.63683  ? 144 GLY A O   1 
ATOM   1714 N  N   . GLY A 1 145 ? -13.63451 4.56288  -9.67872  1.000 21.44149  ? 145 GLY A N   1 
ATOM   1715 C  CA  . GLY A 1 145 ? -13.01846 5.57283  -8.82992  1.000 20.88250  ? 145 GLY A CA  1 
ATOM   1716 C  C   . GLY A 1 145 ? -13.99423 6.17976  -7.83919  1.000 21.88458  ? 145 GLY A C   1 
ATOM   1717 O  O   . GLY A 1 145 ? -13.65332 6.38952  -6.67662  1.000 22.87612  ? 145 GLY A O   1 
ATOM   1718 N  N   . SER A 1 146 ? -15.23135 6.44687  -8.28161  1.000 21.96470  ? 146 SER A N   1 
ATOM   1719 C  CA  . SER A 1 146 ? -16.24089 6.99572  -7.37634  1.000 19.76605  ? 146 SER A CA  1 
ATOM   1720 C  C   . SER A 1 146 ? -16.61970 5.98581  -6.30237  1.000 22.56559  ? 146 SER A C   1 
ATOM   1721 O  O   . SER A 1 146 ? -16.81684 6.36175  -5.14322  1.000 21.85355  ? 146 SER A O   1 
ATOM   1722 C  CB  . SER A 1 146 ? -17.48226 7.44505  -8.14966  1.000 31.32567  ? 146 SER A CB  1 
ATOM   1723 O  OG  . SER A 1 146 ? -17.18110 8.52344  -9.02261  1.000 32.75516  ? 146 SER A OG  1 
ATOM   1724 N  N   . PHE A 1 147 ? -16.68538 4.69412  -6.64920  1.000 23.79510  ? 147 PHE A N   1 
ATOM   1725 C  CA  . PHE A 1 147 ? -16.94063 3.68113  -5.62382  1.000 24.00404  ? 147 PHE A CA  1 
ATOM   1726 C  C   . PHE A 1 147 ? -15.91777 3.76975  -4.49448  1.000 24.38534  ? 147 PHE A C   1 
ATOM   1727 O  O   . PHE A 1 147 ? -16.28065 3.84312  -3.31610  1.000 22.57612  ? 147 PHE A O   1 
ATOM   1728 C  CB  . PHE A 1 147 ? -16.94108 2.27550  -6.21305  1.000 24.48453  ? 147 PHE A CB  1 
ATOM   1729 C  CG  . PHE A 1 147 ? -17.02865 1.19666  -5.15312  1.000 26.91641  ? 147 PHE A CG  1 
ATOM   1730 C  CD1 . PHE A 1 147 ? -18.26124 0.82536  -4.64635  1.000 33.58586  ? 147 PHE A CD1 1 
ATOM   1731 C  CD2 . PHE A 1 147 ? -15.88800 0.60310  -4.63618  1.000 26.95779  ? 147 PHE A CD2 1 
ATOM   1732 C  CE1 . PHE A 1 147 ? -18.35506 -0.14653 -3.66299  1.000 41.55378  ? 147 PHE A CE1 1 
ATOM   1733 C  CE2 . PHE A 1 147 ? -15.97189 -0.37316 -3.64323  1.000 29.13610  ? 147 PHE A CE2 1 
ATOM   1734 C  CZ  . PHE A 1 147 ? -17.20511 -0.74565 -3.15912  1.000 37.20389  ? 147 PHE A CZ  1 
ATOM   1735 N  N   . PHE A 1 148 ? -14.62587 3.78344  -4.84229  1.000 20.71264  ? 148 PHE A N   1 
ATOM   1736 C  CA  . PHE A 1 148 ? -13.59210 3.87977  -3.81169  1.000 18.66992  ? 148 PHE A CA  1 
ATOM   1737 C  C   . PHE A 1 148 ? -13.57000 5.22706  -3.10078  1.000 19.48991  ? 148 PHE A C   1 
ATOM   1738 O  O   . PHE A 1 148 ? -13.28064 5.27247  -1.89458  1.000 19.97614  ? 148 PHE A O   1 
ATOM   1739 C  CB  . PHE A 1 148 ? -12.23875 3.44238  -4.36229  1.000 21.11150  ? 148 PHE A CB  1 
ATOM   1740 C  CG  . PHE A 1 148 ? -12.15685 1.95897  -4.52739  1.000 19.90106  ? 148 PHE A CG  1 
ATOM   1741 C  CD1 . PHE A 1 148 ? -12.03392 1.14344  -3.40792  1.000 23.67595  ? 148 PHE A CD1 1 
ATOM   1742 C  CD2 . PHE A 1 148 ? -12.27880 1.36814  -5.77543  1.000 23.05628  ? 148 PHE A CD2 1 
ATOM   1743 C  CE1 . PHE A 1 148 ? -11.99922 -0.23458 -3.54822  1.000 25.42599  ? 148 PHE A CE1 1 
ATOM   1744 C  CE2 . PHE A 1 148 ? -12.23499 -0.01808 -5.91925  1.000 24.69823  ? 148 PHE A CE2 1 
ATOM   1745 C  CZ  . PHE A 1 148 ? -12.09782 -0.81676 -4.80898  1.000 22.96765  ? 148 PHE A CZ  1 
ATOM   1746 N  N   . LEU A 1 149 ? -13.86138 6.32665  -3.79607  1.000 18.30661  ? 149 LEU A N   1 
ATOM   1747 C  CA  . LEU A 1 149 ? -13.96163 7.60244  -3.08234  1.000 18.47112  ? 149 LEU A CA  1 
ATOM   1748 C  C   . LEU A 1 149 ? -15.05726 7.51989  -2.01736  1.000 18.23958  ? 149 LEU A C   1 
ATOM   1749 O  O   . LEU A 1 149 ? -14.87250 7.95162  -0.86860  1.000 20.25206  ? 149 LEU A O   1 
ATOM   1750 C  CB  . LEU A 1 149 ? -14.29746 8.72614  -4.06718  1.000 18.25653  ? 149 LEU A CB  1 
ATOM   1751 C  CG  . LEU A 1 149 ? -14.51169 10.08589 -3.39325  1.000 17.47307  ? 149 LEU A CG  1 
ATOM   1752 C  CD1 . LEU A 1 149 ? -13.18690 10.71502 -2.95929  1.000 21.59925  ? 149 LEU A CD1 1 
ATOM   1753 C  CD2 . LEU A 1 149 ? -15.34852 11.01327 -4.32847  1.000 23.66432  ? 149 LEU A CD2 1 
ATOM   1754 N  N   A PHE A 1 150 ? -16.21162 6.97475  -2.39698  0.500 19.88384  ? 150 PHE A N   1 
ATOM   1755 N  N   B PHE A 1 150 ? -16.19620 6.91950  -2.37283  0.500 19.84789  ? 150 PHE A N   1 
ATOM   1756 C  CA  A PHE A 1 150 ? -17.30142 6.80893  -1.44494  0.500 21.08562  ? 150 PHE A CA  1 
ATOM   1757 C  CA  B PHE A 1 150 ? -17.30993 6.81794  -1.43322  0.500 21.06468  ? 150 PHE A CA  1 
ATOM   1758 C  C   A PHE A 1 150 ? -16.85772 5.95800  -0.26553  0.500 20.65292  ? 150 PHE A C   1 
ATOM   1759 C  C   B PHE A 1 150 ? -17.00409 5.85882  -0.29057  0.500 21.90759  ? 150 PHE A C   1 
ATOM   1760 O  O   A PHE A 1 150 ? -17.06202 6.33594  0.90005   0.500 18.25286  ? 150 PHE A O   1 
ATOM   1761 O  O   B PHE A 1 150 ? -17.50349 6.04561  0.82841   0.500 19.67225  ? 150 PHE A O   1 
ATOM   1762 C  CB  A PHE A 1 150 ? -18.49906 6.18583  -2.15857  0.500 21.60775  ? 150 PHE A CB  1 
ATOM   1763 C  CB  B PHE A 1 150 ? -18.56582 6.37928  -2.17968  0.500 22.55907  ? 150 PHE A CB  1 
ATOM   1764 C  CG  A PHE A 1 150 ? -19.12336 7.09124  -3.18394  0.500 23.86112  ? 150 PHE A CG  1 
ATOM   1765 C  CG  B PHE A 1 150 ? -19.31189 7.51300  -2.82426  0.500 24.35559  ? 150 PHE A CG  1 
ATOM   1766 C  CD1 A PHE A 1 150 ? -18.82282 8.45277  -3.20458  0.500 24.20587  ? 150 PHE A CD1 1 
ATOM   1767 C  CD1 B PHE A 1 150 ? -18.77092 8.20117  -3.90108  0.500 30.19466  ? 150 PHE A CD1 1 
ATOM   1768 C  CD2 A PHE A 1 150 ? -20.01119 6.59065  -4.11055  0.500 24.25723  ? 150 PHE A CD2 1 
ATOM   1769 C  CD2 B PHE A 1 150 ? -20.54721 7.89744  -2.34538  0.500 26.75797  ? 150 PHE A CD2 1 
ATOM   1770 C  CE1 A PHE A 1 150 ? -19.38612 9.28927  -4.13481  0.500 27.72487  ? 150 PHE A CE1 1 
ATOM   1771 C  CE1 B PHE A 1 150 ? -19.45134 9.24436  -4.49643  0.500 28.97108  ? 150 PHE A CE1 1 
ATOM   1772 C  CE2 A PHE A 1 150 ? -20.58297 7.42536  -5.04793  0.500 23.79465  ? 150 PHE A CE2 1 
ATOM   1773 C  CE2 B PHE A 1 150 ? -21.24163 8.93677  -2.94187  0.500 29.87988  ? 150 PHE A CE2 1 
ATOM   1774 C  CZ  A PHE A 1 150 ? -20.27555 8.77374  -5.05853  0.500 28.41762  ? 150 PHE A CZ  1 
ATOM   1775 C  CZ  B PHE A 1 150 ? -20.69229 9.61350  -4.01171  0.500 28.52823  ? 150 PHE A CZ  1 
ATOM   1776 N  N   . LEU A 1 151 ? -16.21086 4.81964  -0.55486  1.000 20.52806  ? 151 LEU A N   1 
ATOM   1777 C  CA  . LEU A 1 151 ? -15.81377 3.89752  0.50001   1.000 19.57414  ? 151 LEU A CA  1 
ATOM   1778 C  C   . LEU A 1 151 ? -14.85193 4.57656  1.46169   1.000 20.20601  ? 151 LEU A C   1 
ATOM   1779 O  O   . LEU A 1 151 ? -14.99895 4.46720  2.68650   1.000 20.96213  ? 151 LEU A O   1 
ATOM   1780 C  CB  . LEU A 1 151 ? -15.22829 2.60689  -0.09640  1.000 23.12346  ? 151 LEU A CB  1 
ATOM   1781 C  CG  . LEU A 1 151 ? -14.65601 1.61911  0.92885   1.000 21.29476  ? 151 LEU A CG  1 
ATOM   1782 C  CD1 . LEU A 1 151 ? -15.75454 1.17039  1.86603   1.000 25.03127  ? 151 LEU A CD1 1 
ATOM   1783 C  CD2 . LEU A 1 151 ? -14.01899 0.43595  0.24232   1.000 23.47847  ? 151 LEU A CD2 1 
ATOM   1784 N  N   . THR A 1 152 ? -13.90662 5.34470  0.92209   1.000 18.16159  ? 152 THR A N   1 
ATOM   1785 C  CA  . THR A 1 152 ? -12.94665 6.04970  1.77094   1.000 17.08351  ? 152 THR A CA  1 
ATOM   1786 C  C   . THR A 1 152 ? -13.66970 7.00415  2.70885   1.000 18.37122  ? 152 THR A C   1 
ATOM   1787 O  O   . THR A 1 152 ? -13.43673 6.99931  3.92410   1.000 19.08803  ? 152 THR A O   1 
ATOM   1788 C  CB  . THR A 1 152 ? -11.98168 6.84141  0.88671   1.000 18.48971  ? 152 THR A CB  1 
ATOM   1789 O  OG1 . THR A 1 152 ? -11.21746 5.93505  0.07812   1.000 18.97201  ? 152 THR A OG1 1 
ATOM   1790 C  CG2 . THR A 1 152 ? -11.04672 7.74173  1.74341   1.000 18.09650  ? 152 THR A CG2 1 
ATOM   1791 N  N   . PHE A 1 153 ? -14.58864 7.79760  2.15652   1.000 17.23408  ? 153 PHE A N   1 
ATOM   1792 C  CA  . PHE A 1 153 ? -15.28120 8.79130  2.96433   1.000 17.13835  ? 153 PHE A CA  1 
ATOM   1793 C  C   . PHE A 1 153 ? -16.27286 8.15272  3.91858   1.000 19.15499  ? 153 PHE A C   1 
ATOM   1794 O  O   . PHE A 1 153 ? -16.47593 8.67390  5.02115   1.000 19.61382  ? 153 PHE A O   1 
ATOM   1795 C  CB  . PHE A 1 153 ? -15.87084 9.87759  2.05496   1.000 19.26230  ? 153 PHE A CB  1 
ATOM   1796 C  CG  . PHE A 1 153 ? -14.86211 10.92904 1.73434   1.000 18.20768  ? 153 PHE A CG  1 
ATOM   1797 C  CD1 . PHE A 1 153 ? -13.89111 10.70310 0.75626   1.000 19.16872  ? 153 PHE A CD1 1 
ATOM   1798 C  CD2 . PHE A 1 153 ? -14.81606 12.10779 2.47396   1.000 20.89083  ? 153 PHE A CD2 1 
ATOM   1799 C  CE1 . PHE A 1 153 ? -12.91843 11.67122 0.47995   1.000 22.34099  ? 153 PHE A CE1 1 
ATOM   1800 C  CE2 . PHE A 1 153 ? -13.84676 13.07949 2.20563   1.000 22.45313  ? 153 PHE A CE2 1 
ATOM   1801 C  CZ  . PHE A 1 153 ? -12.88201 12.83845 1.20481   1.000 22.16391  ? 153 PHE A CZ  1 
ATOM   1802 N  N   . TYR A 1 154 ? -16.87808 7.02732  3.52463   1.000 19.56315  ? 154 TYR A N   1 
ATOM   1803 C  CA  . TYR A 1 154 ? -17.76761 6.31376  4.43830   1.000 23.00172  ? 154 TYR A CA  1 
ATOM   1804 C  C   . TYR A 1 154 ? -16.99293 5.78346  5.64082   1.000 19.73532  ? 154 TYR A C   1 
ATOM   1805 O  O   . TYR A 1 154 ? -17.43108 5.93526  6.78779   1.000 20.64778  ? 154 TYR A O   1 
ATOM   1806 C  CB  . TYR A 1 154 ? -18.42697 5.14987  3.70203   1.000 22.53999  ? 154 TYR A CB  1 
ATOM   1807 C  CG  . TYR A 1 154 ? -19.24306 4.29406  4.64377   1.000 26.70758  ? 154 TYR A CG  1 
ATOM   1808 C  CD1 . TYR A 1 154 ? -20.46425 4.74342  5.11509   1.000 35.40746  ? 154 TYR A CD1 1 
ATOM   1809 C  CD2 . TYR A 1 154 ? -18.76910 3.06984  5.08739   1.000 28.68212  ? 154 TYR A CD2 1 
ATOM   1810 C  CE1 . TYR A 1 154 ? -21.21062 3.98386  5.98500   1.000 31.46511  ? 154 TYR A CE1 1 
ATOM   1811 C  CE2 . TYR A 1 154 ? -19.51636 2.29320  5.97318   1.000 34.97570  ? 154 TYR A CE2 1 
ATOM   1812 C  CZ  . TYR A 1 154 ? -20.73104 2.77337  6.41810   1.000 34.46401  ? 154 TYR A CZ  1 
ATOM   1813 O  OH  . TYR A 1 154 ? -21.50336 2.02845  7.29633   1.000 46.07248  ? 154 TYR A OH  1 
ATOM   1814 N  N   . LEU A 1 155 ? -15.83847 5.14505  5.39172   1.000 21.60345  ? 155 LEU A N   1 
ATOM   1815 C  CA  . LEU A 1 155 ? -14.97798 4.67613  6.48531   1.000 20.37611  ? 155 LEU A CA  1 
ATOM   1816 C  C   . LEU A 1 155 ? -14.57821 5.82310  7.40900   1.000 20.12070  ? 155 LEU A C   1 
ATOM   1817 O  O   . LEU A 1 155 ? -14.58713 5.67972  8.63780   1.000 19.45198  ? 155 LEU A O   1 
ATOM   1818 C  CB  . LEU A 1 155 ? -13.71709 3.99802  5.93389   1.000 20.21059  ? 155 LEU A CB  1 
ATOM   1819 C  CG  . LEU A 1 155 ? -13.97506 2.67717  5.19996   1.000 22.45506  ? 155 LEU A CG  1 
ATOM   1820 C  CD1 . LEU A 1 155 ? -12.69092 2.20879  4.51680   1.000 26.09613  ? 155 LEU A CD1 1 
ATOM   1821 C  CD2 . LEU A 1 155 ? -14.45265 1.63265  6.18921   1.000 25.92267  ? 155 LEU A CD2 1 
ATOM   1822 N  N   A LEU A 1 156 ? -14.18206 6.95323  6.83104   0.700 19.54010  ? 156 LEU A N   1 
ATOM   1823 N  N   B LEU A 1 156 ? -14.25273 6.99240  6.84668   0.300 19.87330  ? 156 LEU A N   1 
ATOM   1824 C  CA  A LEU A 1 156 ? -13.89870 8.13290  7.63016   0.700 19.44056  ? 156 LEU A CA  1 
ATOM   1825 C  CA  B LEU A 1 156 ? -13.86467 8.11507  7.69988   0.300 19.83504  ? 156 LEU A CA  1 
ATOM   1826 C  C   A LEU A 1 156 ? -15.09967 8.50183  8.50210   0.700 17.19370  ? 156 LEU A C   1 
ATOM   1827 C  C   B LEU A 1 156 ? -15.06351 8.72092  8.43670   0.300 20.13687  ? 156 LEU A C   1 
ATOM   1828 O  O   A LEU A 1 156 ? -14.97690 8.68716  9.72726   0.700 17.40333  ? 156 LEU A O   1 
ATOM   1829 O  O   B LEU A 1 156 ? -14.89431 9.30334  9.52078   0.300 20.84996  ? 156 LEU A O   1 
ATOM   1830 C  CB  A LEU A 1 156 ? -13.55832 9.27039  6.65924   0.700 18.63966  ? 156 LEU A CB  1 
ATOM   1831 C  CB  B LEU A 1 156 ? -13.11016 9.18016  6.88651   0.300 21.05570  ? 156 LEU A CB  1 
ATOM   1832 C  CG  A LEU A 1 156 ? -13.28875 10.63085 7.26424   0.700 17.07351  ? 156 LEU A CG  1 
ATOM   1833 C  CG  B LEU A 1 156 ? -11.77514 9.69254  7.45286   0.300 14.12475  ? 156 LEU A CG  1 
ATOM   1834 C  CD1 A LEU A 1 156 ? -12.20679 10.50922 8.32792   0.700 19.29433  ? 156 LEU A CD1 1 
ATOM   1835 C  CD1 B LEU A 1 156 ? -10.66520 9.46866  6.43062   0.300 30.87363  ? 156 LEU A CD1 1 
ATOM   1836 C  CD2 A LEU A 1 156 ? -12.89708 11.59815 6.13420   0.700 21.42408  ? 156 LEU A CD2 1 
ATOM   1837 C  CD2 B LEU A 1 156 ? -11.86922 11.15169 7.85296   0.300 28.83357  ? 156 LEU A CD2 1 
ATOM   1838 N  N   . TYR A 1 157 ? -16.27296 8.60319  7.87315   1.000 19.59115  ? 157 TYR A N   1 
ATOM   1839 C  CA  . TYR A 1 157 ? -17.45055 9.15980  8.52920   1.000 19.95727  ? 157 TYR A CA  1 
ATOM   1840 C  C   . TYR A 1 157 ? -17.84185 8.31340  9.72450   1.000 20.18061  ? 157 TYR A C   1 
ATOM   1841 O  O   . TYR A 1 157 ? -18.05200 8.83445  10.83187  1.000 22.22934  ? 157 TYR A O   1 
ATOM   1842 C  CB  . TYR A 1 157 ? -18.61618 9.23448  7.53998   1.000 19.60320  ? 157 TYR A CB  1 
ATOM   1843 C  CG  . TYR A 1 157 ? -19.77255 10.03099 8.11702   1.000 22.26394  ? 157 TYR A CG  1 
ATOM   1844 C  CD1 . TYR A 1 157 ? -20.71823 9.42683  8.92421   1.000 25.85018  ? 157 TYR A CD1 1 
ATOM   1845 C  CD2 . TYR A 1 157 ? -19.88698 11.39221 7.87602   1.000 23.01723  ? 157 TYR A CD2 1 
ATOM   1846 C  CE1 . TYR A 1 157 ? -21.77620 10.16095 9.45530   1.000 22.38699  ? 157 TYR A CE1 1 
ATOM   1847 C  CE2 . TYR A 1 157 ? -20.93869 12.14127 8.40824   1.000 23.75656  ? 157 TYR A CE2 1 
ATOM   1848 C  CZ  . TYR A 1 157 ? -21.87787 11.51810 9.19751   1.000 23.05516  ? 157 TYR A CZ  1 
ATOM   1849 O  OH  . TYR A 1 157 ? -22.92040 12.26084 9.72323   1.000 29.75524  ? 157 TYR A OH  1 
ATOM   1850 N  N   . VAL A 1 158 ? -17.90168 6.99733  9.52791   1.000 19.70637  ? 158 VAL A N   1 
ATOM   1851 C  CA  . VAL A 1 158 ? -18.49436 6.13132  10.54662  1.000 23.87287  ? 158 VAL A CA  1 
ATOM   1852 C  C   . VAL A 1 158 ? -17.59514 5.92805  11.75000  1.000 28.64749  ? 158 VAL A C   1 
ATOM   1853 O  O   . VAL A 1 158 ? -18.08852 5.55278  12.82164  1.000 30.74344  ? 158 VAL A O   1 
ATOM   1854 C  CB  . VAL A 1 158 ? -18.96524 4.77962  9.98318   1.000 23.84997  ? 158 VAL A CB  1 
ATOM   1855 C  CG1 . VAL A 1 158 ? -20.00166 5.01441  8.91636   1.000 27.65641  ? 158 VAL A CG1 1 
ATOM   1856 C  CG2 . VAL A 1 158 ? -17.78604 3.96509  9.45884   1.000 22.46730  ? 158 VAL A CG2 1 
ATOM   1857 N  N   . LYS A 1 159 ? -16.28561 6.12554  11.61132  1.000 20.39859  ? 159 LYS A N   1 
ATOM   1858 C  CA  . LYS A 1 159 ? -15.39698 5.96171  12.75008  1.000 18.76926  ? 159 LYS A CA  1 
ATOM   1859 C  C   . LYS A 1 159 ? -15.08581 7.27613  13.44988  1.000 22.98032  ? 159 LYS A C   1 
ATOM   1860 O  O   . LYS A 1 159 ? -14.97182 7.29075  14.67992  1.000 23.61907  ? 159 LYS A O   1 
ATOM   1861 C  CB  . LYS A 1 159 ? -14.09283 5.27935  12.31466  1.000 23.71886  ? 159 LYS A CB  1 
ATOM   1862 C  CG  . LYS A 1 159 ? -13.27020 4.87617  13.53767  1.000 34.65887  ? 159 LYS A CG  1 
ATOM   1863 C  CD  . LYS A 1 159 ? -12.18415 3.89605  13.20778  1.000 38.38356  ? 159 LYS A CD  1 
ATOM   1864 C  CE  . LYS A 1 159 ? -11.46614 3.42214  14.44112  1.000 30.42032  ? 159 LYS A CE  1 
ATOM   1865 N  NZ  . LYS A 1 159 ? -12.29623 2.44820  15.21153  1.000 38.07133  ? 159 LYS A NZ  1 
ATOM   1866 N  N   . TYR A 1 160 ? -14.99410 8.39551  12.71644  1.000 21.46950  ? 160 TYR A N   1 
ATOM   1867 C  CA  . TYR A 1 160 ? -14.34872 9.57775  13.25870  1.000 19.64677  ? 160 TYR A CA  1 
ATOM   1868 C  C   . TYR A 1 160 ? -15.24643 10.80084 13.44456  1.000 21.45894  ? 160 TYR A C   1 
ATOM   1869 O  O   . TYR A 1 160 ? -14.83139 11.73733 14.13996  1.000 23.24211  ? 160 TYR A O   1 
ATOM   1870 C  CB  . TYR A 1 160 ? -13.10087 9.94580  12.44269  1.000 19.00879  ? 160 TYR A CB  1 
ATOM   1871 C  CG  . TYR A 1 160 ? -12.03521 8.88568  12.57848  1.000 17.37350  ? 160 TYR A CG  1 
ATOM   1872 C  CD1 . TYR A 1 160 ? -11.38729 8.68324  13.80452  1.000 18.20906  ? 160 TYR A CD1 1 
ATOM   1873 C  CD2 . TYR A 1 160 ? -11.68379 8.06681  11.49840  1.000 21.93691  ? 160 TYR A CD2 1 
ATOM   1874 C  CE1 . TYR A 1 160 ? -10.39413 7.67955  13.94258  1.000 20.37673  ? 160 TYR A CE1 1 
ATOM   1875 C  CE2 . TYR A 1 160 ? -10.70724 7.08876  11.62486  1.000 20.91300  ? 160 TYR A CE2 1 
ATOM   1876 C  CZ  . TYR A 1 160 ? -10.06537 6.90529  12.84113  1.000 21.50814  ? 160 TYR A CZ  1 
ATOM   1877 O  OH  . TYR A 1 160 ? -9.10213  5.93437  12.94034  1.000 21.31576  ? 160 TYR A OH  1 
ATOM   1878 N  N   . THR A 1 161 ? -16.42363 10.85029 12.83335  1.000 22.63227  ? 161 THR A N   1 
ATOM   1879 C  CA  . THR A 1 161 ? -17.23209 12.05509 12.98664  1.000 20.91566  ? 161 THR A CA  1 
ATOM   1880 C  C   . THR A 1 161 ? -18.18794 11.95863 14.17193  1.000 23.23058  ? 161 THR A C   1 
ATOM   1881 O  O   . THR A 1 161 ? -18.41759 10.88594 14.74820  1.000 25.01191  ? 161 THR A O   1 
ATOM   1882 C  CB  . THR A 1 161 ? -18.05357 12.33704 11.71627  1.000 21.63613  ? 161 THR A CB  1 
ATOM   1883 O  OG1 . THR A 1 161 ? -19.02628 11.29292 11.50327  1.000 22.91170  ? 161 THR A OG1 1 
ATOM   1884 C  CG2 . THR A 1 161 ? -17.15999 12.43428 10.51565  1.000 20.82090  ? 161 THR A CG2 1 
ATOM   1885 N  N   A LYS A 1 162 ? -18.74304 13.10980 14.54494  0.700 21.34597  ? 162 LYS A N   1 
ATOM   1886 N  N   B LYS A 1 162 ? -18.76190 13.10998 14.52521  0.300 22.12663  ? 162 LYS A N   1 
ATOM   1887 C  CA  A LYS A 1 162 ? -19.89714 13.19078 15.42553  0.700 21.43504  ? 162 LYS A CA  1 
ATOM   1888 C  CA  B LYS A 1 162 ? -19.89432 13.20623 15.43541  0.300 21.90861  ? 162 LYS A CA  1 
ATOM   1889 C  C   A LYS A 1 162 ? -20.99795 13.91416 14.65752  0.700 23.86859  ? 162 LYS A C   1 
ATOM   1890 C  C   B LYS A 1 162 ? -20.97811 14.03620 14.75775  0.300 23.08780  ? 162 LYS A C   1 
ATOM   1891 O  O   A LYS A 1 162 ? -20.75004 14.53583 13.61476  0.700 21.27277  ? 162 LYS A O   1 
ATOM   1892 O  O   B LYS A 1 162 ? -20.69859 14.86931 13.89343  0.300 20.53116  ? 162 LYS A O   1 
ATOM   1893 C  CB  A LYS A 1 162 ? -19.57579 13.94103 16.73230  0.700 26.16837  ? 162 LYS A CB  1 
ATOM   1894 C  CB  B LYS A 1 162 ? -19.51079 13.85661 16.77154  0.300 26.61878  ? 162 LYS A CB  1 
ATOM   1895 C  CG  A LYS A 1 162 ? -18.67560 13.15204 17.68354  0.700 28.63244  ? 162 LYS A CG  1 
ATOM   1896 C  CG  B LYS A 1 162 ? -18.63000 12.98767 17.65374  0.300 28.25511  ? 162 LYS A CG  1 
ATOM   1897 C  CD  A LYS A 1 162 ? -18.29810 13.94157 18.93438  0.700 30.99786  ? 162 LYS A CD  1 
ATOM   1898 C  CD  B LYS A 1 162 ? -18.54759 13.54476 19.06625  0.300 32.19724  ? 162 LYS A CD  1 
ATOM   1899 C  CE  A LYS A 1 162 ? -19.49128 14.33125 19.78107  0.700 45.66746  ? 162 LYS A CE  1 
ATOM   1900 C  CE  B LYS A 1 162 ? -17.76025 12.61615 19.97045  0.300 28.36268  ? 162 LYS A CE  1 
ATOM   1901 N  NZ  A LYS A 1 162 ? -19.02550 14.98544 21.02945  0.700 40.34379  ? 162 LYS A NZ  1 
ATOM   1902 N  NZ  B LYS A 1 162 ? -17.54061 13.20998 21.31509  0.300 28.98044  ? 162 LYS A NZ  1 
ATOM   1903 N  N   . GLU A 1 163 ? -22.22771 13.80663 15.16045  1.000 21.76565  ? 163 GLU A N   1 
ATOM   1904 C  CA  . GLU A 1 163 ? -23.38181 14.39505 14.47651  1.000 22.20099  ? 163 GLU A CA  1 
ATOM   1905 C  C   . GLU A 1 163 ? -23.57791 15.83256 14.95185  1.000 23.47000  ? 163 GLU A C   1 
ATOM   1906 O  O   . GLU A 1 163 ? -24.37855 16.12180 15.85154  1.000 25.20061  ? 163 GLU A O   1 
ATOM   1907 C  CB  . GLU A 1 163 ? -24.62799 13.54063 14.70952  1.000 25.76238  ? 163 GLU A CB  1 
ATOM   1908 C  CG  . GLU A 1 163 ? -24.54310 12.16632 14.09889  1.000 26.80675  ? 163 GLU A CG  1 
ATOM   1909 C  CD  . GLU A 1 163 ? -24.54239 12.19530 12.58515  1.000 26.05453  ? 163 GLU A CD  1 
ATOM   1910 O  OE1 . GLU A 1 163 ? -25.26966 13.04677 11.99140  1.000 28.70147  ? 163 GLU A OE1 1 
ATOM   1911 O  OE2 . GLU A 1 163 ? -23.82255 11.35245 12.00538  1.000 27.24403  ? 163 GLU A OE2 1 
ATOM   1912 N  N   . ASN A 1 164 ? -22.81735 16.75486 14.34603  1.000 21.08209  ? 164 ASN A N   1 
ATOM   1913 C  CA  . ASN A 1 164 ? -23.01621 18.17213 14.64221  1.000 25.17607  ? 164 ASN A CA  1 
ATOM   1914 C  C   . ASN A 1 164 ? -22.50385 18.98969 13.46066  1.000 22.11446  ? 164 ASN A C   1 
ATOM   1915 O  O   . ASN A 1 164 ? -21.79508 18.47776 12.59243  1.000 20.24792  ? 164 ASN A O   1 
ATOM   1916 C  CB  . ASN A 1 164 ? -22.41298 18.59221 16.00304  1.000 26.04067  ? 164 ASN A CB  1 
ATOM   1917 C  CG  . ASN A 1 164 ? -20.92373 18.38490 16.07011  1.000 25.83449  ? 164 ASN A CG  1 
ATOM   1918 O  OD1 . ASN A 1 164 ? -20.20095 18.73070 15.13977  1.000 23.23334  ? 164 ASN A OD1 1 
ATOM   1919 N  ND2 . ASN A 1 164 ? -20.44771 17.79102 17.17525  1.000 26.63230  ? 164 ASN A ND2 1 
ATOM   1920 N  N   . TRP A 1 165 ? -22.88125 20.27525 13.43372  1.000 22.41830  ? 165 TRP A N   1 
ATOM   1921 C  CA  . TRP A 1 165 ? -22.60631 21.07706 12.23569  1.000 23.17407  ? 165 TRP A CA  1 
ATOM   1922 C  C   . TRP A 1 165 ? -21.12486 21.34956 12.00775  1.000 26.26999  ? 165 TRP A C   1 
ATOM   1923 O  O   . TRP A 1 165 ? -20.70220 21.45192 10.85362  1.000 21.58151  ? 165 TRP A O   1 
ATOM   1924 C  CB  . TRP A 1 165 ? -23.47555 22.34843 12.15622  1.000 21.57822  ? 165 TRP A CB  1 
ATOM   1925 C  CG  . TRP A 1 165 ? -24.89378 22.00842 11.73712  1.000 25.60578  ? 165 TRP A CG  1 
ATOM   1926 C  CD1 . TRP A 1 165 ? -25.94284 21.73131 12.55742  1.000 32.23258  ? 165 TRP A CD1 1 
ATOM   1927 C  CD2 . TRP A 1 165 ? -25.38176 21.85030 10.39495  1.000 25.66521  ? 165 TRP A CD2 1 
ATOM   1928 N  NE1 . TRP A 1 165 ? -27.06309 21.41866 11.81023  1.000 28.85206  ? 165 TRP A NE1 1 
ATOM   1929 C  CE2 . TRP A 1 165 ? -26.73788 21.48712 10.48224  1.000 29.48408  ? 165 TRP A CE2 1 
ATOM   1930 C  CE3 . TRP A 1 165 ? -24.79779 21.98360 9.12518   1.000 26.88662  ? 165 TRP A CE3 1 
ATOM   1931 C  CZ2 . TRP A 1 165 ? -27.52457 21.27495 9.35994   1.000 30.85721  ? 165 TRP A CZ2 1 
ATOM   1932 C  CZ3 . TRP A 1 165 ? -25.58771 21.76002 8.00476   1.000 26.27717  ? 165 TRP A CZ3 1 
ATOM   1933 C  CH2 . TRP A 1 165 ? -26.92883 21.40055 8.13546   1.000 28.60953  ? 165 TRP A CH2 1 
ATOM   1934 N  N   A MET A 1 166 ? -20.29914 21.44398 13.05949  0.500 22.29775  ? 166 MET A N   1 
ATOM   1935 N  N   B MET A 1 166 ? -20.34164 21.52487 13.07379  0.500 22.33762  ? 166 MET A N   1 
ATOM   1936 C  CA  A MET A 1 166 ? -18.87069 21.64249 12.80206  0.500 20.52063  ? 166 MET A CA  1 
ATOM   1937 C  CA  B MET A 1 166 ? -18.90120 21.61987 12.88836  0.500 20.69031  ? 166 MET A CA  1 
ATOM   1938 C  C   A MET A 1 166 ? -18.22377 20.39209 12.21277  0.500 20.00406  ? 166 MET A C   1 
ATOM   1939 C  C   B MET A 1 166 ? -18.40280 20.43087 12.07670  0.500 18.85423  ? 166 MET A C   1 
ATOM   1940 O  O   A MET A 1 166 ? -17.19525 20.48377 11.53214  0.500 24.76714  ? 166 MET A O   1 
ATOM   1941 O  O   B MET A 1 166 ? -17.72224 20.60041 11.05880  0.500 16.07813  ? 166 MET A O   1 
ATOM   1942 C  CB  A MET A 1 166 ? -18.13459 22.09538 14.06280  0.500 24.01319  ? 166 MET A CB  1 
ATOM   1943 C  CB  B MET A 1 166 ? -18.20710 21.70405 14.24909  0.500 24.76861  ? 166 MET A CB  1 
ATOM   1944 C  CG  A MET A 1 166 ? -18.13258 21.08373 15.18925  0.500 26.08663  ? 166 MET A CG  1 
ATOM   1945 C  CG  B MET A 1 166 ? -18.50381 22.98949 15.01198  0.500 33.69668  ? 166 MET A CG  1 
ATOM   1946 S  SD  A MET A 1 166 ? -16.96781 21.56230 16.48808  0.500 29.65206  ? 166 MET A SD  1 
ATOM   1947 S  SD  B MET A 1 166 ? -18.11343 22.86167 16.77157  0.500 47.31223  ? 166 MET A SD  1 
ATOM   1948 C  CE  A MET A 1 166 ? -17.20326 23.32788 16.54609  0.500 42.10204  ? 166 MET A CE  1 
ATOM   1949 C  CE  B MET A 1 166 ? -16.38487 23.33877 16.75351  0.500 39.21912  ? 166 MET A CE  1 
ATOM   1950 N  N   . ASN A 1 167 ? -18.79001 19.21461 12.48615  1.000 18.54371  ? 167 ASN A N   1 
ATOM   1951 C  CA  . ASN A 1 167 ? -18.39607 18.02103 11.74728  1.000 19.69087  ? 167 ASN A CA  1 
ATOM   1952 C  C   . ASN A 1 167 ? -18.90746 18.03945 10.30610  1.000 18.48694  ? 167 ASN A C   1 
ATOM   1953 O  O   . ASN A 1 167 ? -18.17348 17.65448 9.38013   1.000 20.78738  ? 167 ASN A O   1 
ATOM   1954 C  CB  . ASN A 1 167 ? -18.89057 16.76640 12.47420  1.000 19.27688  ? 167 ASN A CB  1 
ATOM   1955 C  CG  . ASN A 1 167 ? -17.95331 16.34051 13.60191  1.000 20.85799  ? 167 ASN A CG  1 
ATOM   1956 O  OD1 . ASN A 1 167 ? -17.17974 15.37790 13.44470  1.000 21.09113  ? 167 ASN A OD1 1 
ATOM   1957 N  ND2 . ASN A 1 167 ? -17.99679 17.05947 14.72240  1.000 21.30209  ? 167 ASN A ND2 1 
ATOM   1958 N  N   . TYR A 1 168 ? -20.17815 18.39810 10.10390  1.000 20.72423  ? 168 TYR A N   1 
ATOM   1959 C  CA  . TYR A 1 168 ? -20.72579 18.37723 8.74899   1.000 21.15710  ? 168 TYR A CA  1 
ATOM   1960 C  C   . TYR A 1 168 ? -19.94168 19.30897 7.83969   1.000 19.67789  ? 168 TYR A C   1 
ATOM   1961 O  O   . TYR A 1 168 ? -19.67303 18.97903 6.67404   1.000 20.30862  ? 168 TYR A O   1 
ATOM   1962 C  CB  . TYR A 1 168 ? -22.21099 18.74699 8.73690   1.000 20.02840  ? 168 TYR A CB  1 
ATOM   1963 C  CG  . TYR A 1 168 ? -23.09787 17.87362 9.62805   1.000 19.15570  ? 168 TYR A CG  1 
ATOM   1964 C  CD1 . TYR A 1 168 ? -22.77228 16.53528 9.90113   1.000 22.27664  ? 168 TYR A CD1 1 
ATOM   1965 C  CD2 . TYR A 1 168 ? -24.23274 18.40301 10.20601  1.000 23.36060  ? 168 TYR A CD2 1 
ATOM   1966 C  CE1 . TYR A 1 168 ? -23.59213 15.74623 10.73668  1.000 22.75127  ? 168 TYR A CE1 1 
ATOM   1967 C  CE2 . TYR A 1 168 ? -25.02331 17.65120 11.04788  1.000 25.51382  ? 168 TYR A CE2 1 
ATOM   1968 C  CZ  . TYR A 1 168 ? -24.71527 16.33239 11.30511  1.000 24.00823  ? 168 TYR A CZ  1 
ATOM   1969 O  OH  . TYR A 1 168 ? -25.56417 15.63680 12.14034  1.000 24.82961  ? 168 TYR A OH  1 
ATOM   1970 N  N   . ILE A 1 169 ? -19.57949 20.48585 8.34795   1.000 19.31190  ? 169 ILE A N   1 
ATOM   1971 C  CA  . ILE A 1 169 ? -18.80430 21.42631 7.53526   1.000 20.20001  ? 169 ILE A CA  1 
ATOM   1972 C  C   . ILE A 1 169 ? -17.49355 20.79998 7.07757   1.000 17.96833  ? 169 ILE A C   1 
ATOM   1973 O  O   . ILE A 1 169 ? -17.17989 20.78052 5.87943   1.000 21.18124  ? 169 ILE A O   1 
ATOM   1974 C  CB  . ILE A 1 169 ? -18.57414 22.74769 8.28843   1.000 20.69185  ? 169 ILE A CB  1 
ATOM   1975 C  CG1 . ILE A 1 169 ? -19.88480 23.51093 8.45668   1.000 21.85279  ? 169 ILE A CG1 1 
ATOM   1976 C  CG2 . ILE A 1 169 ? -17.56452 23.63338 7.49717   1.000 23.56405  ? 169 ILE A CG2 1 
ATOM   1977 C  CD1 . ILE A 1 169 ? -19.76833 24.69283 9.41559   1.000 24.26361  ? 169 ILE A CD1 1 
ATOM   1978 N  N   . VAL A 1 170 ? -16.68760 20.30556 8.01789   1.000 17.92139  ? 170 VAL A N   1 
ATOM   1979 C  CA  . VAL A 1 170 ? -15.38360 19.74354 7.66281   1.000 20.91596  ? 170 VAL A CA  1 
ATOM   1980 C  C   . VAL A 1 170 ? -15.54834 18.53791 6.74941   1.000 19.55927  ? 170 VAL A C   1 
ATOM   1981 O  O   . VAL A 1 170 ? -14.86828 18.41068 5.71533   1.000 20.39986  ? 170 VAL A O   1 
ATOM   1982 C  CB  . VAL A 1 170 ? -14.61269 19.41480 8.95426   1.000 23.58008  ? 170 VAL A CB  1 
ATOM   1983 C  CG1 . VAL A 1 170 ? -13.29743 18.72271 8.63399   1.000 25.91748  ? 170 VAL A CG1 1 
ATOM   1984 C  CG2 . VAL A 1 170 ? -14.40012 20.68228 9.75937   1.000 23.34405  ? 170 VAL A CG2 1 
ATOM   1985 N  N   . PHE A 1 171 ? -16.49588 17.65796 7.07693   1.000 17.55349  ? 171 PHE A N   1 
ATOM   1986 C  CA  . PHE A 1 171 ? -16.62372 16.41675 6.32905   1.000 18.99322  ? 171 PHE A CA  1 
ATOM   1987 C  C   . PHE A 1 171 ? -17.11611 16.66825 4.91133   1.000 19.28578  ? 171 PHE A C   1 
ATOM   1988 O  O   . PHE A 1 171 ? -16.50803 16.20144 3.94004   1.000 18.61749  ? 171 PHE A O   1 
ATOM   1989 C  CB  . PHE A 1 171 ? -17.54089 15.42550 7.04503   1.000 18.18574  ? 171 PHE A CB  1 
ATOM   1990 C  CG  . PHE A 1 171 ? -17.67453 14.13127 6.29764   1.000 17.31001  ? 171 PHE A CG  1 
ATOM   1991 C  CD1 . PHE A 1 171 ? -16.71269 13.12513 6.42369   1.000 17.79758  ? 171 PHE A CD1 1 
ATOM   1992 C  CD2 . PHE A 1 171 ? -18.72348 13.94141 5.40351   1.000 19.98015  ? 171 PHE A CD2 1 
ATOM   1993 C  CE1 . PHE A 1 171 ? -16.80459 11.93818 5.70188   1.000 19.75484  ? 171 PHE A CE1 1 
ATOM   1994 C  CE2 . PHE A 1 171 ? -18.82809 12.74838 4.67603   1.000 30.04091  ? 171 PHE A CE2 1 
ATOM   1995 C  CZ  . PHE A 1 171 ? -17.88349 11.74201 4.83479   1.000 20.56873  ? 171 PHE A CZ  1 
ATOM   1996 N  N   . TYR A 1 172 ? -18.24001 17.36923 4.76802   1.000 19.34507  ? 172 TYR A N   1 
ATOM   1997 C  CA  . TYR A 1 172 ? -18.83166 17.52136 3.44250   1.000 17.69898  ? 172 TYR A CA  1 
ATOM   1998 C  C   . TYR A 1 172 ? -18.05702 18.48133 2.55699   1.000 20.25115  ? 172 TYR A C   1 
ATOM   1999 O  O   . TYR A 1 172 ? -18.06027 18.30913 1.34116   1.000 20.45790  ? 172 TYR A O   1 
ATOM   2000 C  CB  . TYR A 1 172 ? -20.30495 17.86121 3.53471   1.000 21.14378  ? 172 TYR A CB  1 
ATOM   2001 C  CG  . TYR A 1 172 ? -21.09221 16.67728 4.00619   1.000 19.95475  ? 172 TYR A CG  1 
ATOM   2002 C  CD1 . TYR A 1 172 ? -21.33736 15.58878 3.16060   1.000 21.45078  ? 172 TYR A CD1 1 
ATOM   2003 C  CD2 . TYR A 1 172 ? -21.58319 16.63966 5.30299   1.000 19.36892  ? 172 TYR A CD2 1 
ATOM   2004 C  CE1 . TYR A 1 172 ? -22.04711 14.50634 3.59583   1.000 26.17162  ? 172 TYR A CE1 1 
ATOM   2005 C  CE2 . TYR A 1 172 ? -22.33612 15.54475 5.75751   1.000 27.40322  ? 172 TYR A CE2 1 
ATOM   2006 C  CZ  . TYR A 1 172 ? -22.54968 14.47497 4.89614   1.000 26.44035  ? 172 TYR A CZ  1 
ATOM   2007 O  OH  . TYR A 1 172 ? -23.29213 13.37928 5.31400   1.000 27.74687  ? 172 TYR A OH  1 
ATOM   2008 N  N   A PHE A 1 173 ? -17.49221 19.55192 3.11086   0.700 18.75708  ? 173 PHE A N   1 
ATOM   2009 N  N   B PHE A 1 173 ? -17.28088 19.39433 3.14371   0.300 15.62072  ? 173 PHE A N   1 
ATOM   2010 C  CA  A PHE A 1 173 ? -16.67430 20.42666 2.27576   0.700 19.01894  ? 173 PHE A CA  1 
ATOM   2011 C  CA  B PHE A 1 173 ? -16.37196 20.19770 2.33273   0.300 16.19064  ? 173 PHE A CA  1 
ATOM   2012 C  C   A PHE A 1 173 ? -15.58299 19.60011 1.60961   0.700 19.19789  ? 173 PHE A C   1 
ATOM   2013 C  C   B PHE A 1 173 ? -15.26800 19.33209 1.74927   0.300 20.42678  ? 173 PHE A C   1 
ATOM   2014 O  O   A PHE A 1 173 ? -15.42460 19.62102 0.38523   0.700 18.16747  ? 173 PHE A O   1 
ATOM   2015 O  O   B PHE A 1 173 ? -14.91893 19.45009 0.56741   0.300 14.42548  ? 173 PHE A O   1 
ATOM   2016 C  CB  A PHE A 1 173 ? -16.11480 21.55666 3.14317   0.700 20.94010  ? 173 PHE A CB  1 
ATOM   2017 C  CB  B PHE A 1 173 ? -15.75935 21.31225 3.17201   0.300 22.13238  ? 173 PHE A CB  1 
ATOM   2018 C  CG  A PHE A 1 173 ? -15.31517 22.60882 2.40740   0.700 21.71035  ? 173 PHE A CG  1 
ATOM   2019 C  CG  B PHE A 1 173 ? -14.86218 22.21844 2.39391   0.300 22.87743  ? 173 PHE A CG  1 
ATOM   2020 C  CD1 A PHE A 1 173 ? -15.34039 22.72603 1.03992   0.700 25.39161  ? 173 PHE A CD1 1 
ATOM   2021 C  CD1 B PHE A 1 173 ? -13.50084 21.99371 2.33097   0.300 32.19794  ? 173 PHE A CD1 1 
ATOM   2022 C  CD2 A PHE A 1 173 ? -14.53514 23.50472 3.13463   0.700 33.20969  ? 173 PHE A CD2 1 
ATOM   2023 C  CD2 B PHE A 1 173 ? -15.38797 23.29351 1.71727   0.300 28.15418  ? 173 PHE A CD2 1 
ATOM   2024 C  CE1 A PHE A 1 173 ? -14.59182 23.71227 0.39547   0.700 35.12398  ? 173 PHE A CE1 1 
ATOM   2025 C  CE1 B PHE A 1 173 ? -12.68478 22.84012 1.60266   0.300 31.84792  ? 173 PHE A CE1 1 
ATOM   2026 C  CE2 A PHE A 1 173 ? -13.78878 24.48953 2.50301   0.700 34.02264  ? 173 PHE A CE2 1 
ATOM   2027 C  CE2 B PHE A 1 173 ? -14.57999 24.14153 0.99683   0.300 32.19246  ? 173 PHE A CE2 1 
ATOM   2028 C  CZ  A PHE A 1 173 ? -13.82103 24.59090 1.12372   0.700 31.34661  ? 173 PHE A CZ  1 
ATOM   2029 C  CZ  B PHE A 1 173 ? -13.22950 23.91111 0.94390   0.300 27.36403  ? 173 PHE A CZ  1 
ATOM   2030 N  N   A MET A 1 174 ? -14.87094 18.80082 2.39970   0.600 14.95657  ? 174 MET A N   1 
ATOM   2031 N  N   B MET A 1 174 ? -14.67315 18.48127 2.58105   0.400 18.29458  ? 174 MET A N   1 
ATOM   2032 C  CA  A MET A 1 174 ? -13.80875 17.96522 1.85026   0.600 13.44019  ? 174 MET A CA  1 
ATOM   2033 C  CA  B MET A 1 174 ? -13.62732 17.60315 2.08342   0.400 18.53549  ? 174 MET A CA  1 
ATOM   2034 C  C   A MET A 1 174 ? -14.35935 16.94008 0.85496   0.600 14.29525  ? 174 MET A C   1 
ATOM   2035 C  C   B MET A 1 174 ? -14.18839 16.64844 1.03855   0.400 20.76027  ? 174 MET A C   1 
ATOM   2036 O  O   A MET A 1 174 ? -13.83660 16.80036 -0.26273  0.600 14.77917  ? 174 MET A O   1 
ATOM   2037 O  O   B MET A 1 174 ? -13.54585 16.34460 0.02731   0.400 15.39557  ? 174 MET A O   1 
ATOM   2038 C  CB  A MET A 1 174 ? -13.05957 17.28780 3.00345   0.600 16.87123  ? 174 MET A CB  1 
ATOM   2039 C  CB  B MET A 1 174 ? -13.03088 16.84462 3.26543   0.400 16.84877  ? 174 MET A CB  1 
ATOM   2040 C  CG  A MET A 1 174 ? -11.92870 16.35823 2.53554   0.600 11.62718  ? 174 MET A CG  1 
ATOM   2041 C  CG  B MET A 1 174 ? -11.87653 17.56794 3.93575   0.400 34.55239  ? 174 MET A CG  1 
ATOM   2042 S  SD  A MET A 1 174 ? -11.19751 15.52508 3.93858   0.600 17.42573  ? 174 MET A SD  1 
ATOM   2043 S  SD  B MET A 1 174 ? -10.65408 16.40069 4.56961   0.400 30.79132  ? 174 MET A SD  1 
ATOM   2044 C  CE  A MET A 1 174 ? -9.76392  14.75904 3.17043   0.600 17.69802  ? 174 MET A CE  1 
ATOM   2045 C  CE  B MET A 1 174 ? -11.33402 14.84723 3.94662   0.400 12.09658  ? 174 MET A CE  1 
ATOM   2046 N  N   . PHE A 1 175 ? -15.41217 16.20065 1.24376   1.000 19.06721  ? 175 PHE A N   1 
ATOM   2047 C  CA  . PHE A 1 175 ? -15.99140 15.19950 0.35116   1.000 18.07031  ? 175 PHE A CA  1 
ATOM   2048 C  C   . PHE A 1 175 ? -16.35740 15.81471 -1.00058  1.000 17.92673  ? 175 PHE A C   1 
ATOM   2049 O  O   . PHE A 1 175 ? -15.99919 15.26662 -2.04747  1.000 19.37337  ? 175 PHE A O   1 
ATOM   2050 C  CB  . PHE A 1 175 ? -17.22977 14.60042 1.04138   1.000 15.88102  ? 175 PHE A CB  1 
ATOM   2051 C  CG  . PHE A 1 175 ? -17.86434 13.38853 0.33168   1.000 17.56208  ? 175 PHE A CG  1 
ATOM   2052 C  CD1 . PHE A 1 175 ? -17.14732 12.54183 -0.50952  1.000 19.01237  ? 175 PHE A CD1 1 
ATOM   2053 C  CD2 . PHE A 1 175 ? -19.19232 13.08767 0.58170   1.000 29.97048  ? 175 PHE A CD2 1 
ATOM   2054 C  CE1 . PHE A 1 175 ? -17.74512 11.46435 -1.11670  1.000 26.36520  ? 175 PHE A CE1 1 
ATOM   2055 C  CE2 . PHE A 1 175 ? -19.80263 12.00017 -0.02150  1.000 35.32295  ? 175 PHE A CE2 1 
ATOM   2056 C  CZ  . PHE A 1 175 ? -19.07847 11.18647 -0.86956  1.000 34.61980  ? 175 PHE A CZ  1 
ATOM   2057 N  N   . LEU A 1 176 ? -17.03441 16.97016 -0.99309  1.000 17.51614  ? 176 LEU A N   1 
ATOM   2058 C  CA  . LEU A 1 176 ? -17.37552 17.63303 -2.25609  1.000 17.74130  ? 176 LEU A CA  1 
ATOM   2059 C  C   . LEU A 1 176 ? -16.12409 17.97988 -3.06487  1.000 17.98904  ? 176 LEU A C   1 
ATOM   2060 O  O   . LEU A 1 176 ? -16.05594 17.69794 -4.27799  1.000 19.08106  ? 176 LEU A O   1 
ATOM   2061 C  CB  . LEU A 1 176 ? -18.21714 18.88202 -2.01332  1.000 17.17082  ? 176 LEU A CB  1 
ATOM   2062 C  CG  . LEU A 1 176 ? -18.49798 19.75181 -3.25944  1.000 21.06791  ? 176 LEU A CG  1 
ATOM   2063 C  CD1 . LEU A 1 176 ? -19.21131 18.95954 -4.36811  1.000 24.15433  ? 176 LEU A CD1 1 
ATOM   2064 C  CD2 . LEU A 1 176 ? -19.31887 20.97585 -2.84386  1.000 31.01257  ? 176 LEU A CD2 1 
ATOM   2065 N  N   . VAL A 1 177 ? -15.13006 18.59245 -2.41431  1.000 16.96025  ? 177 VAL A N   1 
ATOM   2066 C  CA  . VAL A 1 177 ? -13.90788 18.99986 -3.12180  1.000 16.40341  ? 177 VAL A CA  1 
ATOM   2067 C  C   . VAL A 1 177 ? -13.21448 17.79396 -3.75625  1.000 16.28393  ? 177 VAL A C   1 
ATOM   2068 O  O   . VAL A 1 177 ? -12.80024 17.83880 -4.93122  1.000 17.31342  ? 177 VAL A O   1 
ATOM   2069 C  CB  . VAL A 1 177 ? -12.97814 19.77039 -2.17678  1.000 16.80353  ? 177 VAL A CB  1 
ATOM   2070 C  CG1 . VAL A 1 177 ? -11.62756 19.94814 -2.82223  1.000 18.88557  ? 177 VAL A CG1 1 
ATOM   2071 C  CG2 . VAL A 1 177 ? -13.62246 21.12611 -1.82804  1.000 19.71072  ? 177 VAL A CG2 1 
ATOM   2072 N  N   A TRP A 1 178 ? -13.07212 16.70117 -3.00503  0.700 15.95402  ? 178 TRP A N   1 
ATOM   2073 N  N   B TRP A 1 178 ? -13.07961 16.69987 -2.99595  0.300 15.96679  ? 178 TRP A N   1 
ATOM   2074 C  CA  A TRP A 1 178 ? -12.43714 15.52911 -3.59815  0.700 16.35008  ? 178 TRP A CA  1 
ATOM   2075 C  CA  B TRP A 1 178 ? -12.46870 15.49054 -3.54513  0.300 16.81861  ? 178 TRP A CA  1 
ATOM   2076 C  C   A TRP A 1 178 ? -13.27533 14.94998 -4.73590  0.700 17.45137  ? 178 TRP A C   1 
ATOM   2077 C  C   B TRP A 1 178 ? -13.27638 14.94343 -4.71310  0.300 17.79640  ? 178 TRP A C   1 
ATOM   2078 O  O   A TRP A 1 178 ? -12.74118 14.61390 -5.80256  0.700 16.49926  ? 178 TRP A O   1 
ATOM   2079 O  O   B TRP A 1 178 ? -12.71295 14.57520 -5.75096  0.300 16.72185  ? 178 TRP A O   1 
ATOM   2080 C  CB  A TRP A 1 178 ? -12.12543 14.50316 -2.51211  0.700 15.84795  ? 178 TRP A CB  1 
ATOM   2081 C  CB  B TRP A 1 178 ? -12.31790 14.43046 -2.45303  0.300 15.30726  ? 178 TRP A CB  1 
ATOM   2082 C  CG  A TRP A 1 178 ? -10.95049 14.91150 -1.61672  0.700 14.12320  ? 178 TRP A CG  1 
ATOM   2083 C  CG  B TRP A 1 178 ? -11.18184 14.70375 -1.49895  0.300 18.47644  ? 178 TRP A CG  1 
ATOM   2084 C  CD1 A TRP A 1 178 ? -10.68605 16.14736 -1.08774  0.700 14.49963  ? 178 TRP A CD1 1 
ATOM   2085 C  CD1 B TRP A 1 178 ? -10.91848 15.87465 -0.85869  0.300 13.70854  ? 178 TRP A CD1 1 
ATOM   2086 C  CD2 A TRP A 1 178 ? -9.88477  14.05541 -1.18708  0.700 14.46029  ? 178 TRP A CD2 1 
ATOM   2087 C  CD2 B TRP A 1 178 ? -10.16732 13.77745 -1.07326  0.300 19.49861  ? 178 TRP A CD2 1 
ATOM   2088 N  NE1 A TRP A 1 178 ? -9.51723  16.10429 -0.33899  0.700 15.02681  ? 178 TRP A NE1 1 
ATOM   2089 N  NE1 B TRP A 1 178 ? -9.80547  15.74244 -0.05672  0.300 16.57229  ? 178 TRP A NE1 1 
ATOM   2090 C  CE2 A TRP A 1 178 ? -9.02036  14.82938 -0.38177  0.700 15.58949  ? 178 TRP A CE2 1 
ATOM   2091 C  CE2 B TRP A 1 178 ? -9.32877  14.46430 -0.17089  0.300 18.53226  ? 178 TRP A CE2 1 
ATOM   2092 C  CE3 A TRP A 1 178 ? -9.59331  12.68880 -1.38329  0.700 16.91736  ? 178 TRP A CE3 1 
ATOM   2093 C  CE3 B TRP A 1 178 ? -9.88910  12.43222 -1.36524  0.300 16.31348  ? 178 TRP A CE3 1 
ATOM   2094 C  CZ2 A TRP A 1 178 ? -7.87733  14.29372 0.20793   0.700 16.35534  ? 178 TRP A CZ2 1 
ATOM   2095 C  CZ2 B TRP A 1 178 ? -8.22572  13.86047 0.43622   0.300 19.69945  ? 178 TRP A CZ2 1 
ATOM   2096 C  CZ3 A TRP A 1 178 ? -8.45001  12.14984 -0.79910  0.700 15.84851  ? 178 TRP A CZ3 1 
ATOM   2097 C  CZ3 B TRP A 1 178 ? -8.78611  11.82917 -0.75944  0.300 13.28598  ? 178 TRP A CZ3 1 
ATOM   2098 C  CH2 A TRP A 1 178 ? -7.60432  12.96072 -0.00349  0.700 17.85727  ? 178 TRP A CH2 1 
ATOM   2099 C  CH2 B TRP A 1 178 ? -7.97379  12.54574 0.13702   0.300 15.53856  ? 178 TRP A CH2 1 
ATOM   2100 N  N   . PHE A 1 179 ? -14.60457 14.90493 -4.57367  1.000 17.41595  ? 179 PHE A N   1 
ATOM   2101 C  CA  . PHE A 1 179 ? -15.45822 14.45959 -5.67824  1.000 18.13685  ? 179 PHE A CA  1 
ATOM   2102 C  C   . PHE A 1 179 ? -15.24608 15.29697 -6.94092  1.000 19.78627  ? 179 PHE A C   1 
ATOM   2103 O  O   . PHE A 1 179 ? -15.24176 14.75971 -8.05821  1.000 18.32312  ? 179 PHE A O   1 
ATOM   2104 C  CB  . PHE A 1 179 ? -16.90397 14.61693 -5.24323  1.000 21.77966  ? 179 PHE A CB  1 
ATOM   2105 C  CG  . PHE A 1 179 ? -17.87253 14.13292 -6.26979  1.000 29.82594  ? 179 PHE A CG  1 
ATOM   2106 C  CD1 . PHE A 1 179 ? -18.10627 12.76956 -6.42112  1.000 32.28838  ? 179 PHE A CD1 1 
ATOM   2107 C  CD2 . PHE A 1 179 ? -18.51719 15.02716 -7.11462  1.000 35.33012  ? 179 PHE A CD2 1 
ATOM   2108 C  CE1 . PHE A 1 179 ? -19.00177 12.30083 -7.37891  1.000 46.23177  ? 179 PHE A CE1 1 
ATOM   2109 C  CE2 . PHE A 1 179 ? -19.41230 14.56900 -8.07617  1.000 38.51342  ? 179 PHE A CE2 1 
ATOM   2110 C  CZ  . PHE A 1 179 ? -19.65283 13.20493 -8.20729  1.000 41.01798  ? 179 PHE A CZ  1 
ATOM   2111 N  N   . LEU A 1 180 ? -14.95254 16.59313 -6.78036  1.000 18.98996  ? 180 LEU A N   1 
ATOM   2112 C  CA  . LEU A 1 180 ? -14.74984 17.44584 -7.94474  1.000 18.87741  ? 180 LEU A CA  1 
ATOM   2113 C  C   . LEU A 1 180 ? -13.47700 17.09502 -8.72658  1.000 16.67049  ? 180 LEU A C   1 
ATOM   2114 O  O   . LEU A 1 180 ? -13.37616 17.47353 -9.89930  1.000 18.68217  ? 180 LEU A O   1 
ATOM   2115 C  CB  . LEU A 1 180 ? -14.79471 18.91930 -7.54691  1.000 18.64391  ? 180 LEU A CB  1 
ATOM   2116 C  CG  . LEU A 1 180 ? -16.20668 19.38692 -7.13893  1.000 20.44213  ? 180 LEU A CG  1 
ATOM   2117 C  CD1 . LEU A 1 180 ? -16.08065 20.76646 -6.46936  1.000 19.13566  ? 180 LEU A CD1 1 
ATOM   2118 C  CD2 . LEU A 1 180 ? -17.18023 19.39788 -8.36078  1.000 20.26708  ? 180 LEU A CD2 1 
ATOM   2119 N  N   A TYR A 1 181 ? -12.53125 16.36344 -8.13944  0.700 15.31082  ? 181 TYR A N   1 
ATOM   2120 N  N   B TYR A 1 181 ? -12.48216 16.45802 -8.09485  0.300 15.58226  ? 181 TYR A N   1 
ATOM   2121 C  CA  A TYR A 1 181 ? -11.40403 15.87336 -8.94168  0.700 16.18315  ? 181 TYR A CA  1 
ATOM   2122 C  CA  B TYR A 1 181 ? -11.40005 15.86310 -8.88291  0.300 16.66946  ? 181 TYR A CA  1 
ATOM   2123 C  C   A TYR A 1 181 ? -11.85912 14.79040 -9.90654  0.700 19.67332  ? 181 TYR A C   1 
ATOM   2124 C  C   B TYR A 1 181 ? -11.97787 14.91800 -9.92920  0.300 18.42029  ? 181 TYR A C   1 
ATOM   2125 O  O   A TYR A 1 181 ? -11.31194 14.64839 -11.00528 0.700 18.17866  ? 181 TYR A O   1 
ATOM   2126 O  O   B TYR A 1 181 ? -11.69652 15.05159 -11.12677 0.300 18.90147  ? 181 TYR A O   1 
ATOM   2127 C  CB  A TYR A 1 181 ? -10.31771 15.32326 -8.02457  0.700 15.09247  ? 181 TYR A CB  1 
ATOM   2128 C  CB  B TYR A 1 181 ? -10.37317 15.14058 -7.98925  0.300 16.39654  ? 181 TYR A CB  1 
ATOM   2129 C  CG  A TYR A 1 181 ? -9.48695  16.35492 -7.33007  0.700 17.72978  ? 181 TYR A CG  1 
ATOM   2130 C  CG  B TYR A 1 181 ? -9.35955  16.03919 -7.29135  0.300 13.32083  ? 181 TYR A CG  1 
ATOM   2131 C  CD1 A TYR A 1 181 ? -9.98470  17.06036 -6.22339  0.700 12.80952  ? 181 TYR A CD1 1 
ATOM   2132 C  CD1 B TYR A 1 181 ? -9.71808  16.75174 -6.15678  0.300 15.61767  ? 181 TYR A CD1 1 
ATOM   2133 C  CD2 A TYR A 1 181 ? -8.18366  16.61623 -7.75736  0.700 17.07109  ? 181 TYR A CD2 1 
ATOM   2134 C  CD2 B TYR A 1 181 ? -8.03932  16.16978 -7.75669  0.300 14.99157  ? 181 TYR A CD2 1 
ATOM   2135 C  CE1 A TYR A 1 181 ? -9.19274  17.99597 -5.57307  0.700 19.63733  ? 181 TYR A CE1 1 
ATOM   2136 C  CE1 B TYR A 1 181 ? -8.81127  17.58088 -5.50615  0.300 12.21565  ? 181 TYR A CE1 1 
ATOM   2137 C  CE2 A TYR A 1 181 ? -7.39345  17.55173 -7.11757  0.700 14.70593  ? 181 TYR A CE2 1 
ATOM   2138 C  CE2 B TYR A 1 181 ? -7.11467  17.01336 -7.09835  0.300 15.62841  ? 181 TYR A CE2 1 
ATOM   2139 C  CZ  A TYR A 1 181 ? -7.90444  18.24275 -6.02911  0.700 13.70703  ? 181 TYR A CZ  1 
ATOM   2140 C  CZ  B TYR A 1 181 ? -7.51481  17.71013 -5.97128  0.300 16.76721  ? 181 TYR A CZ  1 
ATOM   2141 O  OH  A TYR A 1 181 ? -7.09745  19.16002 -5.40320  0.700 16.29445  ? 181 TYR A OH  1 
ATOM   2142 O  OH  B TYR A 1 181 ? -6.64267  18.54462 -5.28783  0.300 12.21070  ? 181 TYR A OH  1 
ATOM   2143 N  N   . GLY A 1 182 ? -12.82693 13.97735 -9.49560  1.000 19.35258  ? 182 GLY A N   1 
ATOM   2144 C  CA  . GLY A 1 182 ? -13.43988 13.05793 -10.43876 1.000 19.01752  ? 182 GLY A CA  1 
ATOM   2145 C  C   . GLY A 1 182 ? -14.23647 13.76331 -11.51394 1.000 19.94498  ? 182 GLY A C   1 
ATOM   2146 O  O   . GLY A 1 182 ? -14.23838 13.34578 -12.67613 1.000 22.63545  ? 182 GLY A O   1 
ATOM   2147 N  N   . PHE A 1 183 ? -14.95812 14.82967 -11.14483 1.000 19.87076  ? 183 PHE A N   1 
ATOM   2148 C  CA  . PHE A 1 183 ? -15.67230 15.60482 -12.14831 1.000 19.11737  ? 183 PHE A CA  1 
ATOM   2149 C  C   . PHE A 1 183 ? -14.70805 16.17302 -13.19149 1.000 19.88804  ? 183 PHE A C   1 
ATOM   2150 O  O   . PHE A 1 183 ? -14.97892 16.11967 -14.39381 1.000 21.14082  ? 183 PHE A O   1 
ATOM   2151 C  CB  . PHE A 1 183 ? -16.44002 16.72235 -11.43926 1.000 22.56602  ? 183 PHE A CB  1 
ATOM   2152 C  CG  . PHE A 1 183 ? -17.29342 17.57054 -12.34889 1.000 26.24970  ? 183 PHE A CG  1 
ATOM   2153 C  CD1 . PHE A 1 183 ? -18.33947 17.01284 -13.05639 1.000 27.05721  ? 183 PHE A CD1 1 
ATOM   2154 C  CD2 . PHE A 1 183 ? -17.07776 18.93118 -12.44979 1.000 22.85746  ? 183 PHE A CD2 1 
ATOM   2155 C  CE1 . PHE A 1 183 ? -19.12998 17.80264 -13.85967 1.000 30.53136  ? 183 PHE A CE1 1 
ATOM   2156 C  CE2 . PHE A 1 183 ? -17.85744 19.72958 -13.25443 1.000 24.87364  ? 183 PHE A CE2 1 
ATOM   2157 C  CZ  . PHE A 1 183 ? -18.89028 19.16639 -13.96617 1.000 29.43221  ? 183 PHE A CZ  1 
ATOM   2158 N  N   . ALA A 1 184 ? -13.55603 16.68169 -12.74752 1.000 20.07461  ? 184 ALA A N   1 
ATOM   2159 C  CA  . ALA A 1 184 ? -12.56773 17.22407 -13.68136 1.000 18.53858  ? 184 ALA A CA  1 
ATOM   2160 C  C   . ALA A 1 184 ? -12.04198 16.17776 -14.65790 1.000 18.85002  ? 184 ALA A C   1 
ATOM   2161 O  O   . ALA A 1 184 ? -11.69281 16.51643 -15.79317 1.000 19.05017  ? 184 ALA A O   1 
ATOM   2162 C  CB  . ALA A 1 184 ? -11.39023 17.83175 -12.91240 1.000 18.21034  ? 184 ALA A CB  1 
ATOM   2163 N  N   . PHE A 1 185 ? -11.94236 14.92044 -14.22887 1.000 19.92848  ? 185 PHE A N   1 
ATOM   2164 C  CA  . PHE A 1 185 ? -11.45388 13.84786 -15.09720 1.000 19.38155  ? 185 PHE A CA  1 
ATOM   2165 C  C   . PHE A 1 185 ? -12.21132 13.76868 -16.40802 1.000 22.84066  ? 185 PHE A C   1 
ATOM   2166 O  O   . PHE A 1 185 ? -11.66874 13.29307 -17.41315 1.000 25.38639  ? 185 PHE A O   1 
ATOM   2167 C  CB  . PHE A 1 185 ? -11.58147 12.53317 -14.32689 1.000 24.10429  ? 185 PHE A CB  1 
ATOM   2168 C  CG  . PHE A 1 185 ? -11.25568 11.31644 -15.13686 1.000 20.10498  ? 185 PHE A CG  1 
ATOM   2169 C  CD1 . PHE A 1 185 ? -12.26570 10.62616 -15.81468 1.000 25.49116  ? 185 PHE A CD1 1 
ATOM   2170 C  CD2 . PHE A 1 185 ? -9.96191  10.84862 -15.20553 1.000 27.24000  ? 185 PHE A CD2 1 
ATOM   2171 C  CE1 . PHE A 1 185 ? -11.97513 9.50845  -16.57822 1.000 25.47599  ? 185 PHE A CE1 1 
ATOM   2172 C  CE2 . PHE A 1 185 ? -9.66440  9.70520  -15.95957 1.000 26.03107  ? 185 PHE A CE2 1 
ATOM   2173 C  CZ  . PHE A 1 185 ? -10.66996 9.05076  -16.65238 1.000 25.33080  ? 185 PHE A CZ  1 
ATOM   2174 N  N   A MET A 1 186 ? -13.46895 14.21312 -16.42567 0.500 24.23034  ? 186 MET A N   1 
ATOM   2175 N  N   B MET A 1 186 ? -13.45595 14.24707 -16.43262 0.500 24.23203  ? 186 MET A N   1 
ATOM   2176 C  CA  A MET A 1 186 ? -14.28753 14.10624 -17.62722 0.500 28.30535  ? 186 MET A CA  1 
ATOM   2177 C  CA  B MET A 1 186 ? -14.34680 14.14231 -17.58131 0.500 28.45027  ? 186 MET A CA  1 
ATOM   2178 C  C   A MET A 1 186 ? -13.79292 15.00362 -18.75685 0.500 26.58956  ? 186 MET A C   1 
ATOM   2179 C  C   B MET A 1 186 ? -14.09217 15.19172 -18.66153 0.500 28.81632  ? 186 MET A C   1 
ATOM   2180 O  O   A MET A 1 186 ? -13.96837 14.66688 -19.93329 0.500 29.62157  ? 186 MET A O   1 
ATOM   2181 O  O   B MET A 1 186 ? -14.75147 15.14887 -19.71575 0.500 23.47962  ? 186 MET A O   1 
ATOM   2182 C  CB  A MET A 1 186 ? -15.72950 14.48299 -17.28633 0.500 27.85778  ? 186 MET A CB  1 
ATOM   2183 C  CB  B MET A 1 186 ? -15.78886 14.29772 -17.10099 0.500 26.37684  ? 186 MET A CB  1 
ATOM   2184 C  CG  A MET A 1 186 ? -16.42111 13.48768 -16.38829 0.500 37.29114  ? 186 MET A CG  1 
ATOM   2185 C  CG  B MET A 1 186 ? -16.22976 13.27643 -16.07947 0.500 31.57041  ? 186 MET A CG  1 
ATOM   2186 S  SD  A MET A 1 186 ? -18.21207 13.60510 -16.58891 0.500 49.99293  ? 186 MET A SD  1 
ATOM   2187 S  SD  B MET A 1 186 ? -18.00081 13.51325 -15.79056 0.500 31.17243  ? 186 MET A SD  1 
ATOM   2188 C  CE  A MET A 1 186 ? -18.51713 15.29274 -16.08747 0.500 27.72982  ? 186 MET A CE  1 
ATOM   2189 C  CE  B MET A 1 186 ? -18.66627 13.13494 -17.41960 0.500 34.76317  ? 186 MET A CE  1 
ATOM   2190 N  N   . PHE A 1 187 ? -13.17993 16.14023 -18.42167 1.000 22.43079  ? 187 PHE A N   1 
ATOM   2191 C  CA  . PHE A 1 187 ? -12.98533 17.25681 -19.32333 1.000 22.97229  ? 187 PHE A CA  1 
ATOM   2192 C  C   . PHE A 1 187 ? -11.71153 17.12184 -20.15639 1.000 20.70895  ? 187 PHE A C   1 
ATOM   2193 O  O   . PHE A 1 187 ? -10.79309 16.37178 -19.81273 1.000 22.83773  ? 187 PHE A O   1 
ATOM   2194 C  CB  . PHE A 1 187 ? -12.96472 18.56785 -18.51724 1.000 24.02873  ? 187 PHE A CB  1 
ATOM   2195 C  CG  . PHE A 1 187 ? -14.32238 18.97805 -17.99227 1.000 22.29310  ? 187 PHE A CG  1 
ATOM   2196 C  CD1 . PHE A 1 187 ? -14.81019 18.45896 -16.79874 1.000 20.87860  ? 187 PHE A CD1 1 
ATOM   2197 C  CD2 . PHE A 1 187 ? -15.12300 19.86315 -18.71348 1.000 22.79423  ? 187 PHE A CD2 1 
ATOM   2198 C  CE1 . PHE A 1 187 ? -16.07256 18.81685 -16.31521 1.000 23.20399  ? 187 PHE A CE1 1 
ATOM   2199 C  CE2 . PHE A 1 187 ? -16.36398 20.23848 -18.22645 1.000 28.65188  ? 187 PHE A CE2 1 
ATOM   2200 C  CZ  . PHE A 1 187 ? -16.83973 19.71778 -17.04205 1.000 23.33850  ? 187 PHE A CZ  1 
ATOM   2201 N  N   . PRO A 1 188 ? -11.64717 17.81498 -21.29193 1.000 24.66423  ? 188 PRO A N   1 
ATOM   2202 C  CA  . PRO A 1 188 ? -10.44108 17.74677 -22.11991 1.000 28.67612  ? 188 PRO A CA  1 
ATOM   2203 C  C   . PRO A 1 188 ? -9.24816  18.33660 -21.38392 1.000 26.46521  ? 188 PRO A C   1 
ATOM   2204 O  O   . PRO A 1 188 ? -9.39754  19.09002 -20.41434 1.000 24.00475  ? 188 PRO A O   1 
ATOM   2205 C  CB  . PRO A 1 188 ? -10.79291 18.59328 -23.34771 1.000 28.57058  ? 188 PRO A CB  1 
ATOM   2206 C  CG  . PRO A 1 188 ? -12.28537 18.79858 -23.31716 1.000 34.93358  ? 188 PRO A CG  1 
ATOM   2207 C  CD  . PRO A 1 188 ? -12.69309 18.67218 -21.87696 1.000 25.01100  ? 188 PRO A CD  1 
ATOM   2208 N  N   . PHE A 1 189 ? -8.06190  18.02951 -21.92016 1.000 23.49248  ? 189 PHE A N   1 
ATOM   2209 C  CA  . PHE A 1 189 ? -6.76056  18.35788 -21.33380 1.000 19.95632  ? 189 PHE A CA  1 
ATOM   2210 C  C   . PHE A 1 189 ? -6.70218  19.71943 -20.64457 1.000 20.54964  ? 189 PHE A C   1 
ATOM   2211 O  O   . PHE A 1 189 ? -6.36660  19.81300 -19.45347 1.000 20.10487  ? 189 PHE A O   1 
ATOM   2212 C  CB  . PHE A 1 189 ? -5.69143  18.30083 -22.44005 1.000 21.11819  ? 189 PHE A CB  1 
ATOM   2213 C  CG  . PHE A 1 189 ? -4.30303  18.61231 -21.94440 1.000 20.54771  ? 189 PHE A CG  1 
ATOM   2214 C  CD1 . PHE A 1 189 ? -3.65114  17.71820 -21.09380 1.000 23.21109  ? 189 PHE A CD1 1 
ATOM   2215 C  CD2 . PHE A 1 189 ? -3.65161  19.78155 -22.30848 1.000 23.02361  ? 189 PHE A CD2 1 
ATOM   2216 C  CE1 . PHE A 1 189 ? -2.38424  17.98925 -20.60491 1.000 25.75029  ? 189 PHE A CE1 1 
ATOM   2217 C  CE2 . PHE A 1 189 ? -2.36289  20.06479 -21.84135 1.000 22.91246  ? 189 PHE A CE2 1 
ATOM   2218 C  CZ  . PHE A 1 189 ? -1.72698  19.16731 -20.98354 1.000 25.69569  ? 189 PHE A CZ  1 
ATOM   2219 N  N   . SER A 1 190 ? -6.96750  20.79907 -21.37404 1.000 20.86410  ? 190 SER A N   1 
ATOM   2220 C  CA  . SER A 1 190 ? -6.70512  22.12092 -20.81523 1.000 20.15204  ? 190 SER A CA  1 
ATOM   2221 C  C   . SER A 1 190 ? -7.65237  22.42655 -19.66868 1.000 20.10110  ? 190 SER A C   1 
ATOM   2222 O  O   . SER A 1 190 ? -7.21647  22.84405 -18.59543 1.000 21.60608  ? 190 SER A O   1 
ATOM   2223 C  CB  . SER A 1 190 ? -6.79375  23.19236 -21.90964 1.000 23.89314  ? 190 SER A CB  1 
ATOM   2224 O  OG  . SER A 1 190 ? -6.57266  24.49729 -21.35477 1.000 28.17137  ? 190 SER A OG  1 
ATOM   2225 N  N   . ILE A 1 191 ? -8.95841  22.21498 -19.87406 1.000 21.37208  ? 191 ILE A N   1 
ATOM   2226 C  CA  . ILE A 1 191 ? -9.95106  22.50724 -18.83390 1.000 20.38733  ? 191 ILE A CA  1 
ATOM   2227 C  C   . ILE A 1 191 ? -9.71097  21.62331 -17.61227 1.000 19.13444  ? 191 ILE A C   1 
ATOM   2228 O  O   . ILE A 1 191 ? -9.77016  22.08981 -16.45841 1.000 19.72926  ? 191 ILE A O   1 
ATOM   2229 C  CB  . ILE A 1 191 ? -11.36207 22.27537 -19.40072 1.000 22.00422  ? 191 ILE A CB  1 
ATOM   2230 C  CG1 . ILE A 1 191 ? -11.64557 23.26738 -20.53678 1.000 28.72189  ? 191 ILE A CG1 1 
ATOM   2231 C  CG2 . ILE A 1 191 ? -12.44072 22.42809 -18.30277 1.000 25.37162  ? 191 ILE A CG2 1 
ATOM   2232 C  CD1 . ILE A 1 191 ? -12.95942 22.99217 -21.24759 1.000 38.57221  ? 191 ILE A CD1 1 
ATOM   2233 N  N   . LYS A 1 192 ? -9.48515  20.32616 -17.84928 1.000 17.97829  ? 192 LYS A N   1 
ATOM   2234 C  CA  . LYS A 1 192 ? -9.20124  19.37347 -16.77958 1.000 17.76096  ? 192 LYS A CA  1 
ATOM   2235 C  C   . LYS A 1 192 ? -8.03734  19.84360 -15.90567 1.000 18.61137  ? 192 LYS A C   1 
ATOM   2236 O  O   . LYS A 1 192 ? -8.12568  19.83816 -14.66972 1.000 19.03830  ? 192 LYS A O   1 
ATOM   2237 C  CB  . LYS A 1 192 ? -8.94823  17.99610 -17.40084 1.000 18.73169  ? 192 LYS A CB  1 
ATOM   2238 C  CG  . LYS A 1 192 ? -8.46689  16.92078 -16.44019 1.000 17.89731  ? 192 LYS A CG  1 
ATOM   2239 C  CD  . LYS A 1 192 ? -8.48163  15.55397 -17.12238 1.000 18.30883  ? 192 LYS A CD  1 
ATOM   2240 C  CE  . LYS A 1 192 ? -7.56540  15.57773 -18.35753 1.000 23.09894  ? 192 LYS A CE  1 
ATOM   2241 N  NZ  . LYS A 1 192 ? -7.48884  14.22891 -19.02022 1.000 29.15143  ? 192 LYS A NZ  1 
ATOM   2242 N  N   A ASN A 1 193 ? -6.93517  20.26085 -16.53573 0.700 16.71827  ? 193 ASN A N   1 
ATOM   2243 N  N   B ASN A 1 193 ? -6.93565  20.27829 -16.52980 0.300 16.70243  ? 193 ASN A N   1 
ATOM   2244 C  CA  A ASN A 1 193 ? -5.75577  20.66454 -15.77658 0.700 17.26483  ? 193 ASN A CA  1 
ATOM   2245 C  CA  B ASN A 1 193 ? -5.74851  20.64100 -15.75651 0.300 17.43374  ? 193 ASN A CA  1 
ATOM   2246 C  C   A ASN A 1 193 ? -5.95925  21.98835 -15.06677 0.700 17.74296  ? 193 ASN A C   1 
ATOM   2247 C  C   B ASN A 1 193 ? -5.84409  22.03153 -15.13010 0.300 17.55871  ? 193 ASN A C   1 
ATOM   2248 O  O   A ASN A 1 193 ? -5.48827  22.17145 -13.93704 0.700 18.81445  ? 193 ASN A O   1 
ATOM   2249 O  O   B ASN A 1 193 ? -5.18354  22.29688 -14.11876 0.300 19.19203  ? 193 ASN A O   1 
ATOM   2250 C  CB  A ASN A 1 193 ? -4.54440  20.68926 -16.68580 0.700 19.08888  ? 193 ASN A CB  1 
ATOM   2251 C  CB  B ASN A 1 193 ? -4.48505  20.46569 -16.59994 0.300 21.99760  ? 193 ASN A CB  1 
ATOM   2252 C  CG  A ASN A 1 193 ? -4.00897  19.31018 -16.88364 0.700 21.60991  ? 193 ASN A CG  1 
ATOM   2253 C  CG  B ASN A 1 193 ? -4.06271  19.00778 -16.70913 0.300 21.53143  ? 193 ASN A CG  1 
ATOM   2254 O  OD1 A ASN A 1 193 ? -3.21244  18.82965 -16.06362 0.700 19.89691  ? 193 ASN A OD1 1 
ATOM   2255 O  OD1 B ASN A 1 193 ? -4.12748  18.40695 -17.78150 0.300 23.31214  ? 193 ASN A OD1 1 
ATOM   2256 N  ND2 A ASN A 1 193 ? -4.51354  18.61269 -17.90128 0.700 19.79854  ? 193 ASN A ND2 1 
ATOM   2257 N  ND2 B ASN A 1 193 ? -3.63169  18.43051 -15.58927 0.300 18.44468  ? 193 ASN A ND2 1 
ATOM   2258 N  N   . GLN A 1 194 ? -6.63622  22.93212 -15.71364 1.000 18.99959  ? 194 GLN A N   1 
ATOM   2259 C  CA  . GLN A 1 194 ? -7.00923  24.15992 -15.01128 1.000 17.94127  ? 194 GLN A CA  1 
ATOM   2260 C  C   . GLN A 1 194 ? -7.80535  23.83838 -13.75903 1.000 18.30267  ? 194 GLN A C   1 
ATOM   2261 O  O   . GLN A 1 194 ? -7.56436  24.41327 -12.68506 1.000 18.76315  ? 194 GLN A O   1 
ATOM   2262 C  CB  . GLN A 1 194 ? -7.82554  25.05862 -15.93224 1.000 19.83173  ? 194 GLN A CB  1 
ATOM   2263 C  CG  . GLN A 1 194 ? -7.02090  25.68985 -17.04779 1.000 18.89667  ? 194 GLN A CG  1 
ATOM   2264 C  CD  . GLN A 1 194 ? -7.91782  26.49611 -17.94015 1.000 28.66953  ? 194 GLN A CD  1 
ATOM   2265 O  OE1 . GLN A 1 194 ? -8.49861  27.48842 -17.49482 1.000 27.81658  ? 194 GLN A OE1 1 
ATOM   2266 N  NE2 . GLN A 1 194 ? -8.06445  26.06766 -19.18751 1.000 28.34407  ? 194 GLN A NE2 1 
ATOM   2267 N  N   A MET A 1 195 ? -8.70923  22.86342 -13.85187 0.500 19.04049  ? 195 MET A N   1 
ATOM   2268 N  N   B MET A 1 195 ? -8.78425  22.93904 -13.87633 0.500 19.09515  ? 195 MET A N   1 
ATOM   2269 C  CA  A MET A 1 195 ? -9.54030  22.53022 -12.70162 0.500 17.38974  ? 195 MET A CA  1 
ATOM   2270 C  CA  B MET A 1 195 ? -9.52979  22.49834 -12.70247 0.500 17.44462  ? 195 MET A CA  1 
ATOM   2271 C  C   A MET A 1 195 ? -8.73135  21.86423 -11.58948 0.500 15.90122  ? 195 MET A C   1 
ATOM   2272 C  C   B MET A 1 195 ? -8.58605  22.01455 -11.61408 0.500 15.77879  ? 195 MET A C   1 
ATOM   2273 O  O   A MET A 1 195 ? -8.97881  22.12324 -10.40584 0.500 16.59493  ? 195 MET A O   1 
ATOM   2274 O  O   B MET A 1 195 ? -8.58353  22.54745 -10.49352 0.500 15.74914  ? 195 MET A O   1 
ATOM   2275 C  CB  A MET A 1 195 ? -10.71752 21.65955 -13.13663 0.500 16.36103  ? 195 MET A CB  1 
ATOM   2276 C  CB  B MET A 1 195 ? -10.50202 21.37443 -13.07692 0.500 17.04639  ? 195 MET A CB  1 
ATOM   2277 C  CG  A MET A 1 195 ? -11.77369 22.39861 -13.92833 0.500 16.48645  ? 195 MET A CG  1 
ATOM   2278 C  CG  B MET A 1 195 ? -11.75357 21.86842 -13.74907 0.500 19.26022  ? 195 MET A CG  1 
ATOM   2279 S  SD  A MET A 1 195 ? -12.96547 21.17709 -14.50945 0.500 16.75923  ? 195 MET A SD  1 
ATOM   2280 S  SD  B MET A 1 195 ? -12.87305 20.54735 -14.19198 0.500 17.28492  ? 195 MET A SD  1 
ATOM   2281 C  CE  A MET A 1 195 ? -14.32239 22.22229 -15.08672 0.500 16.99494  ? 195 MET A CE  1 
ATOM   2282 C  CE  B MET A 1 195 ? -14.24100 21.49418 -14.83576 0.500 19.93621  ? 195 MET A CE  1 
ATOM   2283 N  N   . TYR A 1 196 ? -7.76439  21.00998 -11.93906 1.000 17.11574  ? 196 TYR A N   1 
ATOM   2284 C  CA  . TYR A 1 196 ? -6.88669  20.43153 -10.91191 1.000 16.11849  ? 196 TYR A CA  1 
ATOM   2285 C  C   . TYR A 1 196 ? -6.02063  21.50324 -10.25922 1.000 19.19251  ? 196 TYR A C   1 
ATOM   2286 O  O   . TYR A 1 196 ? -5.79813  21.47367 -9.04250  1.000 18.69420  ? 196 TYR A O   1 
ATOM   2287 C  CB  . TYR A 1 196 ? -5.99932  19.33880 -11.51781 1.000 15.97547  ? 196 TYR A CB  1 
ATOM   2288 C  CG  . TYR A 1 196 ? -6.77281  18.06476 -11.87139 1.000 17.33523  ? 196 TYR A CG  1 
ATOM   2289 C  CD1 . TYR A 1 196 ? -7.79730  17.59291 -11.03209 1.000 18.27131  ? 196 TYR A CD1 1 
ATOM   2290 C  CD2 . TYR A 1 196 ? -6.44757  17.31029 -13.00546 1.000 18.14295  ? 196 TYR A CD2 1 
ATOM   2291 C  CE1 . TYR A 1 196 ? -8.50810  16.41676 -11.32985 1.000 18.47917  ? 196 TYR A CE1 1 
ATOM   2292 C  CE2 . TYR A 1 196 ? -7.16025  16.13475 -13.32004 1.000 19.18268  ? 196 TYR A CE2 1 
ATOM   2293 C  CZ  . TYR A 1 196 ? -8.18073  15.69707 -12.46492 1.000 21.39344  ? 196 TYR A CZ  1 
ATOM   2294 O  OH  . TYR A 1 196 ? -8.87724  14.54426 -12.73954 1.000 23.80858  ? 196 TYR A OH  1 
ATOM   2295 N  N   . ASN A 1 197 ? -5.51377  22.45369 -11.05117 1.000 17.06774  ? 197 ASN A N   1 
ATOM   2296 C  CA  . ASN A 1 197 ? -4.63887  23.49296 -10.48960 1.000 18.52420  ? 197 ASN A CA  1 
ATOM   2297 C  C   . ASN A 1 197 ? -5.34945  24.29604 -9.40374  1.000 20.16419  ? 197 ASN A C   1 
ATOM   2298 O  O   . ASN A 1 197 ? -4.74743  24.64868 -8.37894  1.000 20.50845  ? 197 ASN A O   1 
ATOM   2299 C  CB  . ASN A 1 197 ? -4.16142  24.43435 -11.60090 1.000 19.17868  ? 197 ASN A CB  1 
ATOM   2300 C  CG  . ASN A 1 197 ? -3.13432  23.80351 -12.52710 1.000 20.34074  ? 197 ASN A CG  1 
ATOM   2301 O  OD1 . ASN A 1 197 ? -2.60873  22.73367 -12.24967 1.000 19.39584  ? 197 ASN A OD1 1 
ATOM   2302 N  ND2 . ASN A 1 197 ? -2.84641  24.47993 -13.64432 1.000 22.68211  ? 197 ASN A ND2 1 
ATOM   2303 N  N   . ILE A 1 198 ? -6.62394  24.63293 -9.63182  1.000 17.28165  ? 198 ILE A N   1 
ATOM   2304 C  CA  . ILE A 1 198 ? -7.40548  25.42477 -8.68125  1.000 19.77414  ? 198 ILE A CA  1 
ATOM   2305 C  C   . ILE A 1 198 ? -7.94106  24.55037 -7.54389  1.000 19.16595  ? 198 ILE A C   1 
ATOM   2306 O  O   . ILE A 1 198 ? -7.91778  24.95891 -6.37527  1.000 18.23955  ? 198 ILE A O   1 
ATOM   2307 C  CB  . ILE A 1 198 ? -8.53483  26.16426 -9.41482  1.000 19.98368  ? 198 ILE A CB  1 
ATOM   2308 C  CG1 . ILE A 1 198 ? -7.98641  27.08220 -10.51972 1.000 20.86701  ? 198 ILE A CG1 1 
ATOM   2309 C  CG2 . ILE A 1 198 ? -9.35194  26.97499 -8.40191  1.000 21.16424  ? 198 ILE A CG2 1 
ATOM   2310 C  CD1 . ILE A 1 198 ? -6.96842  28.10616 -10.01465 1.000 27.27308  ? 198 ILE A CD1 1 
ATOM   2311 N  N   . LEU A 1 199 ? -8.41152  23.33320 -7.85867  1.000 18.42707  ? 199 LEU A N   1 
ATOM   2312 C  CA  . LEU A 1 199 ? -8.84127  22.40609 -6.80611  1.000 17.41719  ? 199 LEU A CA  1 
ATOM   2313 C  C   . LEU A 1 199 ? -7.73942  22.18842 -5.76590  1.000 18.12860  ? 199 LEU A C   1 
ATOM   2314 O  O   . LEU A 1 199 ? -8.02660  22.08445 -4.56864  1.000 19.05678  ? 199 LEU A O   1 
ATOM   2315 C  CB  . LEU A 1 199 ? -9.23903  21.04563 -7.39097  1.000 18.35140  ? 199 LEU A CB  1 
ATOM   2316 C  CG  . LEU A 1 199 ? -10.62336 21.04766 -8.06349  1.000 19.03784  ? 199 LEU A CG  1 
ATOM   2317 C  CD1 . LEU A 1 199 ? -10.76806 19.78588 -8.96087  1.000 19.47958  ? 199 LEU A CD1 1 
ATOM   2318 C  CD2 . LEU A 1 199 ? -11.72083 21.10387 -7.00099  1.000 19.79608  ? 199 LEU A CD2 1 
ATOM   2319 N  N   A ASP A 1 200 ? -6.46593  22.11956 -6.18877  0.700 17.48079  ? 200 ASP A N   1 
ATOM   2320 N  N   B ASP A 1 200 ? -6.49276  22.05093 -6.23146  0.300 17.72840  ? 200 ASP A N   1 
ATOM   2321 C  CA  A ASP A 1 200 ? -5.37402  21.92900 -5.22411  0.700 19.08517  ? 200 ASP A CA  1 
ATOM   2322 C  CA  B ASP A 1 200 ? -5.32662  21.99271 -5.35453  0.300 19.28176  ? 200 ASP A CA  1 
ATOM   2323 C  C   A ASP A 1 200 ? -5.26251  23.09823 -4.23628  0.700 18.78754  ? 200 ASP A C   1 
ATOM   2324 C  C   B ASP A 1 200 ? -5.40616  23.05508 -4.26387  0.300 18.13675  ? 200 ASP A C   1 
ATOM   2325 O  O   A ASP A 1 200 ? -4.83977  22.90975 -3.07973  0.700 18.65125  ? 200 ASP A O   1 
ATOM   2326 O  O   B ASP A 1 200 ? -5.31850  22.74792 -3.06585  0.300 23.04700  ? 200 ASP A O   1 
ATOM   2327 C  CB  A ASP A 1 200 ? -4.02410  21.74631 -5.94072  0.700 20.58095  ? 200 ASP A CB  1 
ATOM   2328 C  CB  B ASP A 1 200 ? -4.06985  22.21211 -6.20643  0.300 22.13686  ? 200 ASP A CB  1 
ATOM   2329 C  CG  A ASP A 1 200 ? -3.87187  20.39154 -6.64770  0.700 15.63561  ? 200 ASP A CG  1 
ATOM   2330 C  CG  B ASP A 1 200 ? -3.01461  21.14798 -5.99291  0.300 26.68066  ? 200 ASP A CG  1 
ATOM   2331 O  OD1 A ASP A 1 200 ? -4.58706  19.41111 -6.34327  0.700 17.19955  ? 200 ASP A OD1 1 
ATOM   2332 O  OD1 B ASP A 1 200 ? -2.50901  21.04972 -4.85897  0.300 30.66784  ? 200 ASP A OD1 1 
ATOM   2333 O  OD2 A ASP A 1 200 ? -2.96497  20.29876 -7.51956  0.700 22.01269  ? 200 ASP A OD2 1 
ATOM   2334 O  OD2 B ASP A 1 200 ? -2.67490  20.42413 -6.96415  0.300 23.30825  ? 200 ASP A OD2 1 
ATOM   2335 N  N   . ILE A 1 201 ? -5.58191  24.31687 -4.67092  1.000 19.73054  ? 201 ILE A N   1 
ATOM   2336 C  CA  . ILE A 1 201 ? -5.63370  25.44062 -3.72737  1.000 18.49042  ? 201 ILE A CA  1 
ATOM   2337 C  C   . ILE A 1 201 ? -6.63067  25.14326 -2.62994  1.000 20.01306  ? 201 ILE A C   1 
ATOM   2338 O  O   . ILE A 1 201 ? -6.36573  25.37710 -1.44542  1.000 23.24384  ? 201 ILE A O   1 
ATOM   2339 C  CB  . ILE A 1 201 ? -6.03155  26.73790 -4.44782  1.000 22.01150  ? 201 ILE A CB  1 
ATOM   2340 C  CG1 . ILE A 1 201 ? -5.01974  27.07321 -5.52432  1.000 20.99074  ? 201 ILE A CG1 1 
ATOM   2341 C  CG2 . ILE A 1 201 ? -6.17055  27.88186 -3.41866  1.000 21.88196  ? 201 ILE A CG2 1 
ATOM   2342 C  CD1 . ILE A 1 201 ? -5.46434  28.24630 -6.41637  1.000 23.79045  ? 201 ILE A CD1 1 
ATOM   2343 N  N   . VAL A 1 202 ? -7.78333  24.59752 -3.00729  1.000 18.58801  ? 202 VAL A N   1 
ATOM   2344 C  CA  . VAL A 1 202 ? -8.86255  24.38618 -2.05070  1.000 17.40387  ? 202 VAL A CA  1 
ATOM   2345 C  C   . VAL A 1 202 ? -8.57362  23.17690 -1.18075  1.000 21.33585  ? 202 VAL A C   1 
ATOM   2346 O  O   . VAL A 1 202 ? -8.71801  23.21881 0.04990   1.000 23.58986  ? 202 VAL A O   1 
ATOM   2347 C  CB  . VAL A 1 202 ? -10.19514 24.23844 -2.80198  1.000 19.57283  ? 202 VAL A CB  1 
ATOM   2348 C  CG1 . VAL A 1 202 ? -11.34915 24.07493 -1.78835  1.000 22.81775  ? 202 VAL A CG1 1 
ATOM   2349 C  CG2 . VAL A 1 202 ? -10.45459 25.44272 -3.71033  1.000 20.79449  ? 202 VAL A CG2 1 
ATOM   2350 N  N   . SER A 1 203 ? -8.13881  22.07095 -1.78872  1.000 19.01110  ? 203 SER A N   1 
ATOM   2351 C  CA  . SER A 1 203 ? -8.00743  20.84333 -1.01626  1.000 18.80761  ? 203 SER A CA  1 
ATOM   2352 C  C   . SER A 1 203 ? -6.77230  20.83490 -0.10408  1.000 20.80939  ? 203 SER A C   1 
ATOM   2353 O  O   . SER A 1 203 ? -6.80679  20.21092 0.96449   1.000 23.44456  ? 203 SER A O   1 
ATOM   2354 C  CB  . SER A 1 203 ? -7.96349  19.62778 -1.95823  1.000 19.58451  ? 203 SER A CB  1 
ATOM   2355 O  OG  . SER A 1 203 ? -6.73411  19.63031 -2.67763  1.000 17.99968  ? 203 SER A OG  1 
ATOM   2356 N  N   A LYS A 1 204 ? -5.67036  21.46212 -0.51377  0.500 18.43713  ? 204 LYS A N   1 
ATOM   2357 N  N   B LYS A 1 204 ? -5.70880  21.57024 -0.47387  0.300 18.75907  ? 204 LYS A N   1 
ATOM   2358 N  N   C LYS A 1 204 ? -5.69175  21.51052 -0.50625  0.200 18.57667  ? 204 LYS A N   1 
ATOM   2359 C  CA  A LYS A 1 204 ? -4.48393  21.54298 0.33699   0.500 19.20937  ? 204 LYS A CA  1 
ATOM   2360 C  CA  B LYS A 1 204 ? -4.41036  21.51063 0.20341   0.300 19.48712  ? 204 LYS A CA  1 
ATOM   2361 C  CA  C LYS A 1 204 ? -4.44120  21.54287 0.25318   0.200 19.51901  ? 204 LYS A CA  1 
ATOM   2362 C  C   A LYS A 1 204 ? -4.38100  22.88451 1.05860   0.500 20.18559  ? 204 LYS A C   1 
ATOM   2363 C  C   B LYS A 1 204 ? -3.98829  22.80433 0.89484   0.300 19.51651  ? 204 LYS A C   1 
ATOM   2364 C  C   C LYS A 1 204 ? -4.25504  22.85004 1.01841   0.200 20.80507  ? 204 LYS A C   1 
ATOM   2365 O  O   A LYS A 1 204 ? -4.43910  22.94099 2.29232   0.500 17.38448  ? 204 LYS A O   1 
ATOM   2366 O  O   B LYS A 1 204 ? -3.39979  22.74593 1.98432   0.300 23.08109  ? 204 LYS A O   1 
ATOM   2367 O  O   C LYS A 1 204 ? -4.10011  22.84551 2.24453   0.200 19.67059  ? 204 LYS A O   1 
ATOM   2368 C  CB  A LYS A 1 204 ? -3.22101  21.24395 -0.48645  0.500 18.85882  ? 204 LYS A CB  1 
ATOM   2369 C  CB  B LYS A 1 204 ? -3.32059  21.03726 -0.77972  0.300 19.58711  ? 204 LYS A CB  1 
ATOM   2370 C  CB  C LYS A 1 204 ? -3.24570  21.33177 -0.68956  0.200 19.33331  ? 204 LYS A CB  1 
ATOM   2371 C  CG  A LYS A 1 204 ? -3.12324  19.78743 -0.97653  0.500 18.67256  ? 204 LYS A CG  1 
ATOM   2372 C  CG  B LYS A 1 204 ? -3.80994  19.90147 -1.69026  0.300 19.82456  ? 204 LYS A CG  1 
ATOM   2373 C  CG  C LYS A 1 204 ? -3.15971  19.94973 -1.32231  0.200 21.60916  ? 204 LYS A CG  1 
ATOM   2374 C  CD  A LYS A 1 204 ? -2.03603  19.66864 -2.03355  0.500 14.91841  ? 204 LYS A CD  1 
ATOM   2375 C  CD  B LYS A 1 204 ? -2.70668  19.03762 -2.27652  0.300 21.35695  ? 204 LYS A CD  1 
ATOM   2376 C  CD  C LYS A 1 204 ? -1.91666  19.83734 -2.19775  0.200 15.42193  ? 204 LYS A CD  1 
ATOM   2377 C  CE  A LYS A 1 204 ? -1.77494  18.20842 -2.43485  0.500 19.60957  ? 204 LYS A CE  1 
ATOM   2378 C  CE  B LYS A 1 204 ? -3.18501  18.34982 -3.56949  0.300 18.99376  ? 204 LYS A CE  1 
ATOM   2379 C  CE  C LYS A 1 204 ? -1.97717  18.58241 -3.06227  0.200 25.17295  ? 204 LYS A CE  1 
ATOM   2380 N  NZ  A LYS A 1 204 ? -2.63346  17.70681 -3.57379  0.500 15.79525  ? 204 LYS A NZ  1 
ATOM   2381 N  NZ  B LYS A 1 204 ? -3.18737  16.85643 -3.58639  0.300 21.64440  ? 204 LYS A NZ  1 
ATOM   2382 N  NZ  C LYS A 1 204 ? -2.81653  17.55571 -2.39365  0.200 19.98471  ? 204 LYS A NZ  1 
ATOM   2383 N  N   . ASN A 1 205 ? -4.25508  23.97989 0.30570   1.000 17.97564  ? 205 ASN A N   1 
ATOM   2384 C  CA  . ASN A 1 205 ? -3.84799  25.24870 0.91879   1.000 20.45738  ? 205 ASN A CA  1 
ATOM   2385 C  C   . ASN A 1 205 ? -4.90752  25.81443 1.85732   1.000 25.25303  ? 205 ASN A C   1 
ATOM   2386 O  O   . ASN A 1 205 ? -4.57785  26.31634 2.94037   1.000 22.78242  ? 205 ASN A O   1 
ATOM   2387 C  CB  . ASN A 1 205 ? -3.50960  26.27463 -0.16121  1.000 21.24393  ? 205 ASN A CB  1 
ATOM   2388 C  CG  . ASN A 1 205 ? -2.41366  25.82010 -1.09142  1.000 24.92759  ? 205 ASN A CG  1 
ATOM   2389 O  OD1 . ASN A 1 205 ? -2.40432  26.21809 -2.25395  1.000 29.10413  ? 205 ASN A OD1 1 
ATOM   2390 N  ND2 . ASN A 1 205 ? -1.48679  24.98927 -0.60929  1.000 26.05222  ? 205 ASN A ND2 1 
ATOM   2391 N  N   . ILE A 1 206 ? -6.18087  25.78730 1.45998   1.000 18.95365  ? 206 ILE A N   1 
ATOM   2392 C  CA  . ILE A 1 206 ? -7.22289  26.27502 2.37035   1.000 21.06988  ? 206 ILE A CA  1 
ATOM   2393 C  C   . ILE A 1 206 ? -7.20582  25.48374 3.66625   1.000 25.57470  ? 206 ILE A C   1 
ATOM   2394 O  O   . ILE A 1 206 ? -7.38695  26.04456 4.75824   1.000 23.32486  ? 206 ILE A O   1 
ATOM   2395 C  CB  . ILE A 1 206 ? -8.60203  26.27767 1.68823   1.000 27.97769  ? 206 ILE A CB  1 
ATOM   2396 C  CG1 . ILE A 1 206 ? -8.67999  27.43042 0.69100   1.000 28.79620  ? 206 ILE A CG1 1 
ATOM   2397 C  CG2 . ILE A 1 206 ? -9.73018  26.36269 2.72047   1.000 30.40222  ? 206 ILE A CG2 1 
ATOM   2398 C  CD1 . ILE A 1 206 ? -10.02078 27.50657 -0.05695  1.000 30.46759  ? 206 ILE A CD1 1 
ATOM   2399 N  N   A TYR A 1 207 ? -6.95846  24.17522 3.57777   0.700 21.30517  ? 207 TYR A N   1 
ATOM   2400 N  N   B TYR A 1 207 ? -6.94502  24.17490 3.58318   0.300 21.67452  ? 207 TYR A N   1 
ATOM   2401 C  CA  A TYR A 1 207 ? -6.90289  23.36500 4.78748   0.700 21.02548  ? 207 TYR A CA  1 
ATOM   2402 C  CA  B TYR A 1 207 ? -6.91199  23.35560 4.79169   0.300 21.04860  ? 207 TYR A CA  1 
ATOM   2403 C  C   A TYR A 1 207 ? -5.78701  23.83716 5.70807   0.700 23.29380  ? 207 TYR A C   1 
ATOM   2404 C  C   B TYR A 1 207 ? -5.77157  23.77716 5.71462   0.300 23.91845  ? 207 TYR A C   1 
ATOM   2405 O  O   A TYR A 1 207 ? -5.99042  23.98888 6.91693   0.700 23.91076  ? 207 TYR A O   1 
ATOM   2406 O  O   B TYR A 1 207 ? -5.93748  23.81266 6.93786   0.300 24.90774  ? 207 TYR A O   1 
ATOM   2407 C  CB  A TYR A 1 207 ? -6.75618  21.88138 4.44184   0.700 24.48729  ? 207 TYR A CB  1 
ATOM   2408 C  CB  B TYR A 1 207 ? -6.83396  21.86516 4.43516   0.300 24.51258  ? 207 TYR A CB  1 
ATOM   2409 C  CG  A TYR A 1 207 ? -6.95833  20.98806 5.64666   0.700 25.18646  ? 207 TYR A CG  1 
ATOM   2410 C  CG  B TYR A 1 207 ? -7.41121  20.93923 5.49866   0.300 28.89975  ? 207 TYR A CG  1 
ATOM   2411 C  CD1 A TYR A 1 207 ? -8.23893  20.76208 6.14929   0.700 31.78478  ? 207 TYR A CD1 1 
ATOM   2412 C  CD1 B TYR A 1 207 ? -6.77667  20.77075 6.72485   0.300 31.21464  ? 207 TYR A CD1 1 
ATOM   2413 C  CD2 A TYR A 1 207 ? -5.88043  20.38847 6.29301   0.700 27.57982  ? 207 TYR A CD2 1 
ATOM   2414 C  CD2 B TYR A 1 207 ? -8.58884  20.23038 5.27178   0.300 32.60839  ? 207 TYR A CD2 1 
ATOM   2415 C  CE1 A TYR A 1 207 ? -8.44577  19.94880 7.25518   0.700 43.80586  ? 207 TYR A CE1 1 
ATOM   2416 C  CE1 B TYR A 1 207 ? -7.30127  19.92753 7.69870   0.300 29.38213  ? 207 TYR A CE1 1 
ATOM   2417 C  CE2 A TYR A 1 207 ? -6.07725  19.56110 7.39748   0.700 25.93633  ? 207 TYR A CE2 1 
ATOM   2418 C  CE2 B TYR A 1 207 ? -9.11854  19.38444 6.23836   0.300 35.70739  ? 207 TYR A CE2 1 
ATOM   2419 C  CZ  A TYR A 1 207 ? -7.36693  19.35280 7.87565   0.700 33.07993  ? 207 TYR A CZ  1 
ATOM   2420 C  CZ  B TYR A 1 207 ? -8.47009  19.23619 7.44975   0.300 32.53354  ? 207 TYR A CZ  1 
ATOM   2421 O  OH  A TYR A 1 207 ? -7.58142  18.54314 8.97716   0.700 33.62537  ? 207 TYR A OH  1 
ATOM   2422 O  OH  B TYR A 1 207 ? -8.98950  18.39750 8.41519   0.300 34.16592  ? 207 TYR A OH  1 
ATOM   2423 N  N   . SER A 1 208 ? -4.61037  24.12183 5.14986   1.000 20.51268  ? 208 SER A N   1 
ATOM   2424 C  CA  . SER A 1 208 ? -3.51264  24.61944 5.97210   1.000 20.56512  ? 208 SER A CA  1 
ATOM   2425 C  C   . SER A 1 208 ? -3.86315  25.95517 6.62399   1.000 24.19539  ? 208 SER A C   1 
ATOM   2426 O  O   . SER A 1 208 ? -3.57423  26.17662 7.80591   1.000 21.80884  ? 208 SER A O   1 
ATOM   2427 C  CB  . SER A 1 208 ? -2.25876  24.78458 5.12024   1.000 32.20828  ? 208 SER A CB  1 
ATOM   2428 O  OG  . SER A 1 208 ? -1.69302  23.52936 4.79176   1.000 30.30301  ? 208 SER A OG  1 
ATOM   2429 N  N   . ILE A 1 209 ? -4.46618  26.87109 5.86277   1.000 22.05849  ? 209 ILE A N   1 
ATOM   2430 C  CA  . ILE A 1 209 ? -4.85387  28.16793 6.42591   1.000 24.30994  ? 209 ILE A CA  1 
ATOM   2431 C  C   . ILE A 1 209 ? -5.86836  27.98045 7.54817   1.000 21.17642  ? 209 ILE A C   1 
ATOM   2432 O  O   . ILE A 1 209 ? -5.79823  28.65393 8.58821   1.000 19.66639  ? 209 ILE A O   1 
ATOM   2433 C  CB  . ILE A 1 209 ? -5.40581  29.08144 5.31767   1.000 25.58352  ? 209 ILE A CB  1 
ATOM   2434 C  CG1 . ILE A 1 209 ? -4.31747  29.34850 4.28713   1.000 22.89504  ? 209 ILE A CG1 1 
ATOM   2435 C  CG2 . ILE A 1 209 ? -5.92265  30.41146 5.91669   1.000 24.24033  ? 209 ILE A CG2 1 
ATOM   2436 C  CD1 . ILE A 1 209 ? -4.83421  29.99584 2.99393   1.000 29.62397  ? 209 ILE A CD1 1 
ATOM   2437 N  N   . PHE A 1 210 ? -6.84518  27.09270 7.33842   1.000 22.00568  ? 210 PHE A N   1 
ATOM   2438 C  CA  . PHE A 1 210 ? -7.81966  26.75717 8.37623   1.000 18.98807  ? 210 PHE A CA  1 
ATOM   2439 C  C   . PHE A 1 210 ? -7.12827  26.31346 9.66188   1.000 21.47474  ? 210 PHE A C   1 
ATOM   2440 O  O   . PHE A 1 210 ? -7.41024  26.82952 10.75651  1.000 20.45926  ? 210 PHE A O   1 
ATOM   2441 C  CB  . PHE A 1 210 ? -8.72858  25.64658 7.83633   1.000 16.86999  ? 210 PHE A CB  1 
ATOM   2442 C  CG  . PHE A 1 210 ? -9.60566  25.01420 8.87190   1.000 20.88489  ? 210 PHE A CG  1 
ATOM   2443 C  CD1 . PHE A 1 210 ? -10.62012 25.75050 9.48575   1.000 22.26122  ? 210 PHE A CD1 1 
ATOM   2444 C  CD2 . PHE A 1 210 ? -9.44339  23.68692 9.21236   1.000 25.03067  ? 210 PHE A CD2 1 
ATOM   2445 C  CE1 . PHE A 1 210 ? -11.45312 25.16389 10.44024  1.000 23.97860  ? 210 PHE A CE1 1 
ATOM   2446 C  CE2 . PHE A 1 210 ? -10.26210 23.09374 10.18218  1.000 23.83740  ? 210 PHE A CE2 1 
ATOM   2447 C  CZ  . PHE A 1 210 ? -11.28075 23.84269 10.78904  1.000 20.57814  ? 210 PHE A CZ  1 
ATOM   2448 N  N   . ILE A 1 211 ? -6.21300  25.35346 9.54819   1.000 20.59930  ? 211 ILE A N   1 
ATOM   2449 C  CA  . ILE A 1 211 ? -5.49619  24.87411 10.72655  1.000 19.01684  ? 211 ILE A CA  1 
ATOM   2450 C  C   . ILE A 1 211 ? -4.73062  26.01080 11.38838  1.000 20.46503  ? 211 ILE A C   1 
ATOM   2451 O  O   . ILE A 1 211 ? -4.70349  26.12644 12.61558  1.000 19.61013  ? 211 ILE A O   1 
ATOM   2452 C  CB  . ILE A 1 211 ? -4.57556  23.70248 10.34599  1.000 17.47761  ? 211 ILE A CB  1 
ATOM   2453 C  CG1 . ILE A 1 211 ? -5.41766  22.49690 9.83667   1.000 19.92305  ? 211 ILE A CG1 1 
ATOM   2454 C  CG2 . ILE A 1 211 ? -3.65111  23.33868 11.52390  1.000 19.13363  ? 211 ILE A CG2 1 
ATOM   2455 C  CD1 . ILE A 1 211 ? -6.32284  21.88364 10.88529  1.000 19.39721  ? 211 ILE A CD1 1 
ATOM   2456 N  N   . PHE A 1 212 ? -4.05111  26.84165 10.59028  1.000 19.22317  ? 212 PHE A N   1 
ATOM   2457 C  CA  . PHE A 1 212 ? -3.33086  27.98520 11.15006  1.000 18.45918  ? 212 PHE A CA  1 
ATOM   2458 C  C   . PHE A 1 212 ? -4.25634  28.88033 11.97114  1.000 22.55380  ? 212 PHE A C   1 
ATOM   2459 O  O   . PHE A 1 212 ? -3.91750  29.31085 13.08295  1.000 21.51218  ? 212 PHE A O   1 
ATOM   2460 C  CB  . PHE A 1 212 ? -2.68377  28.78048 10.01569  1.000 21.81759  ? 212 PHE A CB  1 
ATOM   2461 C  CG  . PHE A 1 212 ? -2.05305  30.04791 10.48815  1.000 24.42559  ? 212 PHE A CG  1 
ATOM   2462 C  CD1 . PHE A 1 212 ? -0.79173  30.03724 11.05828  1.000 22.44547  ? 212 PHE A CD1 1 
ATOM   2463 C  CD2 . PHE A 1 212 ? -2.75274  31.23440 10.43797  1.000 25.72578  ? 212 PHE A CD2 1 
ATOM   2464 C  CE1 . PHE A 1 212 ? -0.19977  31.20028 11.52906  1.000 25.50895  ? 212 PHE A CE1 1 
ATOM   2465 C  CE2 . PHE A 1 212 ? -2.17579  32.41368 10.89339  1.000 30.07227  ? 212 PHE A CE2 1 
ATOM   2466 C  CZ  . PHE A 1 212 ? -0.88426  32.39627 11.44925  1.000 26.22372  ? 212 PHE A CZ  1 
ATOM   2467 N  N   . ILE A 1 213 ? -5.43253  29.17946 11.42976  1.000 18.68638  ? 213 ILE A N   1 
ATOM   2468 C  CA  . ILE A 1 213 ? -6.37230  30.05252 12.14103  1.000 20.56174  ? 213 ILE A CA  1 
ATOM   2469 C  C   . ILE A 1 213 ? -6.88085  29.39243 13.42607  1.000 21.45436  ? 213 ILE A C   1 
ATOM   2470 O  O   . ILE A 1 213 ? -7.01955  30.05150 14.46850  1.000 21.87973  ? 213 ILE A O   1 
ATOM   2471 C  CB  . ILE A 1 213 ? -7.51724  30.46665 11.19586  1.000 20.64265  ? 213 ILE A CB  1 
ATOM   2472 C  CG1 . ILE A 1 213 ? -6.97658  31.32047 10.04298  1.000 23.64470  ? 213 ILE A CG1 1 
ATOM   2473 C  CG2 . ILE A 1 213 ? -8.58616  31.20444 11.97639  1.000 25.30808  ? 213 ILE A CG2 1 
ATOM   2474 C  CD1 . ILE A 1 213 ? -8.01013  31.61667 8.93450   1.000 23.29350  ? 213 ILE A CD1 1 
ATOM   2475 N  N   . VAL A 1 214 ? -7.17206  28.08853 13.37779  1.000 21.03626  ? 214 VAL A N   1 
ATOM   2476 C  CA  . VAL A 1 214 ? -7.52397  27.36568 14.60774  1.000 19.51265  ? 214 VAL A CA  1 
ATOM   2477 C  C   . VAL A 1 214 ? -6.40989  27.49589 15.63903  1.000 23.29889  ? 214 VAL A C   1 
ATOM   2478 O  O   . VAL A 1 214 ? -6.65887  27.81325 16.80070  1.000 20.59809  ? 214 VAL A O   1 
ATOM   2479 C  CB  . VAL A 1 214 ? -7.88854  25.90061 14.30199  1.000 19.50882  ? 214 VAL A CB  1 
ATOM   2480 C  CG1 . VAL A 1 214 ? -8.12582  25.13704 15.61020  1.000 22.01388  ? 214 VAL A CG1 1 
ATOM   2481 C  CG2 . VAL A 1 214 ? -9.15953  25.85440 13.41874  1.000 21.68338  ? 214 VAL A CG2 1 
ATOM   2482 N  N   . ILE A 1 215 ? -5.15609  27.29169 15.21981  1.000 18.16743  ? 215 ILE A N   1 
ATOM   2483 C  CA  . ILE A 1 215 ? -4.03714  27.41099 16.14939  1.000 18.52645  ? 215 ILE A CA  1 
ATOM   2484 C  C   . ILE A 1 215 ? -3.96917  28.80953 16.73375  1.000 18.33059  ? 215 ILE A C   1 
ATOM   2485 O  O   . ILE A 1 215 ? -3.80096  28.98527 17.94389  1.000 21.45888  ? 215 ILE A O   1 
ATOM   2486 C  CB  . ILE A 1 215 ? -2.72256  27.05138 15.43866  1.000 21.70287  ? 215 ILE A CB  1 
ATOM   2487 C  CG1 . ILE A 1 215 ? -2.68385  25.55023 15.19014  1.000 18.98420  ? 215 ILE A CG1 1 
ATOM   2488 C  CG2 . ILE A 1 215 ? -1.50940  27.55725 16.25134  1.000 22.30060  ? 215 ILE A CG2 1 
ATOM   2489 C  CD1 . ILE A 1 215 ? -1.51391  25.13872 14.29080  1.000 20.16041  ? 215 ILE A CD1 1 
ATOM   2490 N  N   A LEU A 1 216 ? -4.04256  29.82707 15.87771  0.700 20.76212  ? 216 LEU A N   1 
ATOM   2491 N  N   B LEU A 1 216 ? -4.06893  29.83701 15.88450  0.300 20.94115  ? 216 LEU A N   1 
ATOM   2492 C  CA  A LEU A 1 216 ? -3.88340  31.19053 16.35276  0.700 19.61213  ? 216 LEU A CA  1 
ATOM   2493 C  CA  B LEU A 1 216 ? -4.06131  31.20740 16.38716  0.300 20.90232  ? 216 LEU A CA  1 
ATOM   2494 C  C   A LEU A 1 216 ? -5.00169  31.55243 17.31892  0.700 22.06909  ? 216 LEU A C   1 
ATOM   2495 C  C   B LEU A 1 216 ? -5.18495  31.41740 17.38989  0.300 23.68388  ? 216 LEU A C   1 
ATOM   2496 O  O   A LEU A 1 216 ? -4.75555  32.19777 18.34389  0.700 24.61680  ? 216 LEU A O   1 
ATOM   2497 O  O   B LEU A 1 216 ? -4.95830  31.90904 18.50118  0.300 26.08832  ? 216 LEU A O   1 
ATOM   2498 C  CB  A LEU A 1 216 ? -3.86481  32.13214 15.15091  0.700 26.47336  ? 216 LEU A CB  1 
ATOM   2499 C  CB  B LEU A 1 216 ? -4.20803  32.19770 15.23144  0.300 25.79414  ? 216 LEU A CB  1 
ATOM   2500 C  CG  A LEU A 1 216 ? -3.72258  33.61618 15.44282  0.700 29.12740  ? 216 LEU A CG  1 
ATOM   2501 C  CG  B LEU A 1 216 ? -2.95886  32.78675 14.57976  0.300 28.22421  ? 216 LEU A CG  1 
ATOM   2502 C  CD1 A LEU A 1 216 ? -2.36463  33.91320 16.05099  0.700 41.80187  ? 216 LEU A CD1 1 
ATOM   2503 C  CD1 B LEU A 1 216 ? -3.36983  33.94290 13.68586  0.300 33.20231  ? 216 LEU A CD1 1 
ATOM   2504 C  CD2 A LEU A 1 216 ? -3.94085  34.39601 14.15378  0.700 34.20058  ? 216 LEU A CD2 1 
ATOM   2505 C  CD2 B LEU A 1 216 ? -1.95925  33.25312 15.62427  0.300 29.42092  ? 216 LEU A CD2 1 
ATOM   2506 N  N   A ASN A 1 217 ? -6.22959  31.09706 17.02824  0.700 24.34148  ? 217 ASN A N   1 
ATOM   2507 N  N   B ASN A 1 217 ? -6.40569  31.02416 17.01521  0.300 24.67585  ? 217 ASN A N   1 
ATOM   2508 C  CA  A ASN A 1 217 ? -7.37970  31.34719 17.90365  0.700 27.94297  ? 217 ASN A CA  1 
ATOM   2509 C  CA  B ASN A 1 217 ? -7.56720  31.24902 17.87202  0.300 28.46876  ? 217 ASN A CA  1 
ATOM   2510 C  C   A ASN A 1 217 ? -7.24710  30.62042 19.24305  0.700 28.76026  ? 217 ASN A C   1 
ATOM   2511 C  C   B ASN A 1 217 ? -7.42336  30.54273 19.21523  0.300 28.46758  ? 217 ASN A C   1 
ATOM   2512 O  O   A ASN A 1 217 ? -7.53043  31.19517 20.30142  0.700 29.79356  ? 217 ASN A O   1 
ATOM   2513 O  O   B ASN A 1 217 ? -7.86685  31.05877 20.24690  0.300 29.81876  ? 217 ASN A O   1 
ATOM   2514 C  CB  A ASN A 1 217 ? -8.66782  30.94401 17.16869  0.700 30.59226  ? 217 ASN A CB  1 
ATOM   2515 C  CB  B ASN A 1 217 ? -8.83181  30.78303 17.14949  0.300 31.09636  ? 217 ASN A CB  1 
ATOM   2516 C  CG  A ASN A 1 217 ? -9.89275  30.92570 18.07298  0.700 42.86151  ? 217 ASN A CG  1 
ATOM   2517 C  CG  B ASN A 1 217 ? -10.05039 30.77732 18.04951  0.300 41.60207  ? 217 ASN A CG  1 
ATOM   2518 O  OD1 A ASN A 1 217 ? -10.45057 29.86517 18.37851  0.700 46.43789  ? 217 ASN A OD1 1 
ATOM   2519 O  OD1 B ASN A 1 217 ? -10.51991 29.72152 18.47958  0.300 44.73630  ? 217 ASN A OD1 1 
ATOM   2520 N  ND2 A ASN A 1 217 ? -10.31734 32.10107 18.50088  0.700 38.40145  ? 217 ASN A ND2 1 
ATOM   2521 N  ND2 B ASN A 1 217 ? -10.56555 31.96013 18.34541  0.300 37.98217  ? 217 ASN A ND2 1 
ATOM   2522 N  N   . GLN A 1 218 ? -6.80834  29.36103 19.22715  1.000 22.49576  ? 218 GLN A N   1 
ATOM   2523 C  CA  . GLN A 1 218 ? -6.65701  28.62983 20.48251  1.000 24.71528  ? 218 GLN A CA  1 
ATOM   2524 C  C   . GLN A 1 218 ? -5.56538  29.21344 21.36882  1.000 31.30468  ? 218 GLN A C   1 
ATOM   2525 O  O   . GLN A 1 218 ? -5.65185  29.12181 22.59851  1.000 29.95855  ? 218 GLN A O   1 
ATOM   2526 C  CB  . GLN A 1 218 ? -6.31534  27.16360 20.20023  1.000 22.47767  ? 218 GLN A CB  1 
ATOM   2527 C  CG  . GLN A 1 218 ? -7.46690  26.35205 19.60176  1.000 25.13827  ? 218 GLN A CG  1 
ATOM   2528 C  CD  . GLN A 1 218 ? -8.67320  26.34710 20.50254  1.000 34.57269  ? 218 GLN A CD  1 
ATOM   2529 O  OE1 . GLN A 1 218 ? -8.67634  25.69267 21.54293  1.000 44.44996  ? 218 GLN A OE1 1 
ATOM   2530 N  NE2 . GLN A 1 218 ? -9.68911  27.10977 20.13314  1.000 38.50964  ? 218 GLN A NE2 1 
ATOM   2531 N  N   . SER A 1 219 ? -4.53705  29.81601 20.78056  1.000 24.49524  ? 219 SER A N   1 
ATOM   2532 C  CA  . SER A 1 219 ? -3.32936  30.12975 21.52778  1.000 32.51439  ? 219 SER A CA  1 
ATOM   2533 C  C   . SER A 1 219 ? -3.07647  31.61631 21.69118  1.000 40.92301  ? 219 SER A C   1 
ATOM   2534 O  O   . SER A 1 219 ? -2.03305  31.98391 22.23858  1.000 44.12979  ? 219 SER A O   1 
ATOM   2535 C  CB  . SER A 1 219 ? -2.11992  29.50929 20.83079  1.000 33.04902  ? 219 SER A CB  1 
ATOM   2536 O  OG  . SER A 1 219 ? -2.37274  28.15410 20.49675  1.000 39.56417  ? 219 SER A OG  1 
ATOM   2537 N  N   A TYR A 1 220 ? -3.99227  32.48134 21.23996  0.500 34.23143  ? 220 TYR A N   1 
ATOM   2538 N  N   B TYR A 1 220 ? -3.99509  32.47994 21.24570  0.500 34.22559  ? 220 TYR A N   1 
ATOM   2539 C  CA  A TYR A 1 220 ? -3.65212  33.89864 21.12458  0.500 48.31064  ? 220 TYR A CA  1 
ATOM   2540 C  CA  B TYR A 1 220 ? -3.66466  33.89901 21.11997  0.500 48.30509  ? 220 TYR A CA  1 
ATOM   2541 C  C   A TYR A 1 220 ? -3.29109  34.52049 22.46833  0.500 61.57604  ? 220 TYR A C   1 
ATOM   2542 C  C   B TYR A 1 220 ? -3.32136  34.53953 22.46147  0.500 61.57728  ? 220 TYR A C   1 
ATOM   2543 O  O   A TYR A 1 220 ? -2.50907  35.47785 22.51501  0.500 68.51223  ? 220 TYR A O   1 
ATOM   2544 O  O   B TYR A 1 220 ? -2.58406  35.53186 22.49948  0.500 68.60432  ? 220 TYR A O   1 
ATOM   2545 C  CB  A TYR A 1 220 ? -4.76997  34.68571 20.44300  0.500 48.08065  ? 220 TYR A CB  1 
ATOM   2546 C  CB  B TYR A 1 220 ? -4.79446  34.65512 20.42409  0.500 48.10545  ? 220 TYR A CB  1 
ATOM   2547 C  CG  A TYR A 1 220 ? -4.38621  36.12095 20.16300  0.500 56.72476  ? 220 TYR A CG  1 
ATOM   2548 C  CG  B TYR A 1 220 ? -6.02932  34.82012 21.26977  0.500 46.47344  ? 220 TYR A CG  1 
ATOM   2549 C  CD1 A TYR A 1 220 ? -3.58041  36.44785 19.07699  0.500 56.07628  ? 220 TYR A CD1 1 
ATOM   2550 C  CD1 B TYR A 1 220 ? -6.91424  33.76825 21.45362  0.500 49.38641  ? 220 TYR A CD1 1 
ATOM   2551 C  CD2 A TYR A 1 220 ? -4.82202  37.14805 20.98854  0.500 56.87754  ? 220 TYR A CD2 1 
ATOM   2552 C  CD2 B TYR A 1 220 ? -6.31576  36.03530 21.88006  0.500 55.23617  ? 220 TYR A CD2 1 
ATOM   2553 C  CE1 A TYR A 1 220 ? -3.22430  37.76109 18.82125  0.500 61.80121  ? 220 TYR A CE1 1 
ATOM   2554 C  CE1 B TYR A 1 220 ? -8.04764  33.91914 22.22723  0.500 64.10903  ? 220 TYR A CE1 1 
ATOM   2555 C  CE2 A TYR A 1 220 ? -4.47220  38.46115 20.74113  0.500 68.24532  ? 220 TYR A CE2 1 
ATOM   2556 C  CE2 B TYR A 1 220 ? -7.44507  36.19685 22.65189  0.500 61.48480  ? 220 TYR A CE2 1 
ATOM   2557 C  CZ  A TYR A 1 220 ? -3.67337  38.76260 19.65773  0.500 69.41319  ? 220 TYR A CZ  1 
ATOM   2558 C  CZ  B TYR A 1 220 ? -8.30743  35.13706 22.82277  0.500 64.43556  ? 220 TYR A CZ  1 
ATOM   2559 O  OH  A TYR A 1 220 ? -3.32643  40.07213 19.41388  0.500 82.60344  ? 220 TYR A OH  1 
ATOM   2560 O  OH  B TYR A 1 220 ? -9.43407  35.29570 23.59427  0.500 74.78430  ? 220 TYR A OH  1 
ATOM   2561 N  N   . LYS A 1 221 ? -3.83659  33.99415 23.56792  1.000 68.45855  ? 221 LYS A N   1 
ATOM   2562 C  CA  . LYS A 1 221 ? -3.46693  34.51516 24.88240  1.000 63.32321  ? 221 LYS A CA  1 
ATOM   2563 C  C   . LYS A 1 221 ? -2.02843  34.15010 25.23998  1.000 71.38789  ? 221 LYS A C   1 
ATOM   2564 O  O   . LYS A 1 221 ? -1.31656  34.94665 25.86296  1.000 77.17461  ? 221 LYS A O   1 
ATOM   2565 C  CB  . LYS A 1 221 ? -4.44870  34.03475 25.94988  1.000 59.41426  ? 221 LYS A CB  1 
ATOM   2566 C  CG  . LYS A 1 221 ? -5.84266  34.62183 25.81197  1.000 60.13034  ? 221 LYS A CG  1 
ATOM   2567 N  N   . LEU A 1 222 ? -1.57794  32.95492 24.84893  1.000 65.25216  ? 222 LEU A N   1 
ATOM   2568 C  CA  . LEU A 1 222 ? -0.17645  32.59672 25.03448  1.000 72.93230  ? 222 LEU A CA  1 
ATOM   2569 C  C   . LEU A 1 222 ? 0.75207   33.43464 24.16343  1.000 81.76091  ? 222 LEU A C   1 
ATOM   2570 O  O   . LEU A 1 222 ? 1.94084   33.55238 24.47988  1.000 84.97562  ? 222 LEU A O   1 
ATOM   2571 C  CB  . LEU A 1 222 ? 0.03985   31.12005 24.71251  1.000 66.32246  ? 222 LEU A CB  1 
ATOM   2572 C  CG  . LEU A 1 222 ? -0.83144  30.09272 25.42845  1.000 57.15887  ? 222 LEU A CG  1 
ATOM   2573 C  CD1 . LEU A 1 222 ? -0.53890  28.71523 24.85852  1.000 46.34297  ? 222 LEU A CD1 1 
ATOM   2574 C  CD2 . LEU A 1 222 ? -0.57653  30.12543 26.92410  1.000 61.49364  ? 222 LEU A CD2 1 
ATOM   2575 N  N   . LEU A 1 223 ? 0.24097   34.00682 23.07090  1.000 77.92322  ? 223 LEU A N   1 
ATOM   2576 C  CA  . LEU A 1 223 ? 1.05980   34.84641 22.20234  1.000 87.71333  ? 223 LEU A CA  1 
ATOM   2577 C  C   . LEU A 1 223 ? 1.10571   36.28729 22.69877  1.000 104.12977 ? 223 LEU A C   1 
ATOM   2578 O  O   . LEU A 1 223 ? 2.18049   36.89307 22.77450  1.000 116.94369 ? 223 LEU A O   1 
ATOM   2579 C  CB  . LEU A 1 223 ? 0.51824   34.80347 20.77318  1.000 71.68561  ? 223 LEU A CB  1 
ATOM   2580 C  CG  . LEU A 1 223 ? 1.00792   33.69545 19.84779  1.000 64.37597  ? 223 LEU A CG  1 
ATOM   2581 C  CD1 . LEU A 1 223 ? 0.28418   33.80589 18.52792  1.000 59.51390  ? 223 LEU A CD1 1 
ATOM   2582 C  CD2 . LEU A 1 223 ? 2.51367   33.78361 19.64058  1.000 56.36255  ? 223 LEU A CD2 1 
ATOM   2583 N  N   . LEU A 1 224 ? -0.05026  36.85460 23.02508  1.000 93.85098  ? 224 LEU A N   1 
ATOM   2584 C  CA  . LEU A 1 224 ? -0.12270  38.24069 23.46201  1.000 95.03344  ? 224 LEU A CA  1 
ATOM   2585 C  C   . LEU A 1 224 ? 0.13767   38.34504 24.96048  1.000 105.33288 ? 224 LEU A C   1 
ATOM   2586 O  O   . LEU A 1 224 ? 0.09321   37.34613 25.67995  1.000 86.58955  ? 224 LEU A O   1 
ATOM   2587 C  CB  . LEU A 1 224 ? -1.48769  38.84026 23.11358  1.000 89.87510  ? 224 LEU A CB  1 
HETATM 2588 C  C1  A RET B 2 .   ? -10.06588 10.45422 -9.91758  0.500 15.60577  ? 301 RET A C1  1 
HETATM 2589 C  C1  B RET B 2 .   ? -10.22284 10.02949 -10.05530 0.300 18.86400  ? 301 RET A C1  1 
HETATM 2590 C  C1  C RET B 2 .   ? -9.96028  10.24012 -10.07377 0.200 18.93510  ? 301 RET A C1  1 
HETATM 2591 C  C2  A RET B 2 .   ? -10.74137 9.68059  -11.06214 0.500 20.08855  ? 301 RET A C2  1 
HETATM 2592 C  C2  B RET B 2 .   ? -10.84352 9.18032  -11.17105 0.300 20.97317  ? 301 RET A C2  1 
HETATM 2593 C  C2  C RET B 2 .   ? -10.57222 9.19719  -11.01690 0.200 20.07520  ? 301 RET A C2  1 
HETATM 2594 C  C3  A RET B 2 .   ? -11.75597 8.63824  -10.61105 0.500 21.15146  ? 301 RET A C3  1 
HETATM 2595 C  C3  B RET B 2 .   ? -12.27706 9.58412  -11.47257 0.300 21.14148  ? 301 RET A C3  1 
HETATM 2596 C  C3  C RET B 2 .   ? -12.02346 9.50078  -11.36103 0.200 21.76319  ? 301 RET A C3  1 
HETATM 2597 C  C4  A RET B 2 .   ? -12.81848 9.20593  -9.68462  0.500 19.93853  ? 301 RET A C4  1 
HETATM 2598 C  C4  B RET B 2 .   ? -13.14884 9.40630  -10.24499 0.300 18.31945  ? 301 RET A C4  1 
HETATM 2599 C  C4  C RET B 2 .   ? -12.87905 9.56707  -10.10892 0.200 19.18472  ? 301 RET A C4  1 
HETATM 2600 C  C5  A RET B 2 .   ? -12.33108 10.32439 -8.79735  0.500 17.53399  ? 301 RET A C5  1 
HETATM 2601 C  C5  B RET B 2 .   ? -12.49241 9.83912  -8.95582  0.300 18.85517  ? 301 RET A C5  1 
HETATM 2602 C  C5  C RET B 2 .   ? -12.23081 10.30369 -8.96463  0.200 18.02777  ? 301 RET A C5  1 
HETATM 2603 C  C6  A RET B 2 .   ? -11.04231 10.71073 -8.75798  0.500 16.04141  ? 301 RET A C6  1 
HETATM 2604 C  C6  B RET B 2 .   ? -11.19030 10.17802 -8.87057  0.300 16.36872  ? 301 RET A C6  1 
HETATM 2605 C  C6  C RET B 2 .   ? -10.90417 10.51441 -8.89721  0.200 15.85790  ? 301 RET A C6  1 
HETATM 2606 C  C7  A RET B 2 .   ? -10.54103 11.45976 -7.61670  0.500 15.51121  ? 301 RET A C7  1 
HETATM 2607 C  C7  B RET B 2 .   ? -10.72980 10.97479 -7.74327  0.300 16.94436  ? 301 RET A C7  1 
HETATM 2608 C  C7  C RET B 2 .   ? -10.31217 11.11610 -7.71980  0.200 16.42197  ? 301 RET A C7  1 
HETATM 2609 C  C8  A RET B 2 .   ? -9.32838  11.93535 -7.32563  0.500 11.65903  ? 301 RET A C8  1 
HETATM 2610 C  C8  B RET B 2 .   ? -9.53451  11.49002 -7.29903  0.300 18.51530  ? 301 RET A C8  1 
HETATM 2611 C  C8  C RET B 2 .   ? -9.67058  12.27557 -7.62964  0.200 17.63037  ? 301 RET A C8  1 
HETATM 2612 C  C9  A RET B 2 .   ? -8.98490  12.68168 -6.15693  0.500 14.71142  ? 301 RET A C9  1 
HETATM 2613 C  C9  B RET B 2 .   ? -9.38655  12.29296 -6.09796  0.300 15.43457  ? 301 RET A C9  1 
HETATM 2614 C  C9  C RET B 2 .   ? -9.14528  12.83898 -6.41303  0.200 15.84492  ? 301 RET A C9  1 
HETATM 2615 C  C10 A RET B 2 .   ? -7.82670  13.37424 -6.13627  0.500 15.93523  ? 301 RET A C10 1 
HETATM 2616 C  C10 B RET B 2 .   ? -8.23000  12.96383 -5.85727  0.300 15.60444  ? 301 RET A C10 1 
HETATM 2617 C  C10 C RET B 2 .   ? -7.96750  13.50777 -6.42028  0.200 16.81508  ? 301 RET A C10 1 
HETATM 2618 C  C11 A RET B 2 .   ? -7.34003  14.20589 -5.08104  0.500 12.71672  ? 301 RET A C11 1 
HETATM 2619 C  C11 B RET B 2 .   ? -7.95185  13.82923 -4.74504  0.300 13.99776  ? 301 RET A C11 1 
HETATM 2620 C  C11 C RET B 2 .   ? -7.33195  14.11799 -5.28853  0.200 12.14812  ? 301 RET A C11 1 
HETATM 2621 C  C12 A RET B 2 .   ? -6.24629  14.95988 -5.14526  0.500 14.52560  ? 301 RET A C12 1 
HETATM 2622 C  C12 B RET B 2 .   ? -6.94535  14.72351 -4.67020  0.300 19.70890  ? 301 RET A C12 1 
HETATM 2623 C  C12 C RET B 2 .   ? -6.48340  15.15575 -5.27701  0.200 16.60824  ? 301 RET A C12 1 
HETATM 2624 C  C13 A RET B 2 .   ? -5.75809  15.83479 -4.09957  0.500 14.92386  ? 301 RET A C13 1 
HETATM 2625 C  C13 B RET B 2 .   ? -6.69707  15.64074 -3.56838  0.300 22.62851  ? 301 RET A C13 1 
HETATM 2626 C  C13 C RET B 2 .   ? -5.91299  15.72873 -4.07127  0.200 15.64851  ? 301 RET A C13 1 
HETATM 2627 C  C14 A RET B 2 .   ? -4.62841  16.54565 -4.30032  0.500 17.65164  ? 301 RET A C14 1 
HETATM 2628 C  C14 B RET B 2 .   ? -5.49169  16.24661 -3.42916  0.300 24.10523  ? 301 RET A C14 1 
HETATM 2629 C  C14 C RET B 2 .   ? -4.61350  16.11358 -4.03852  0.200 20.43288  ? 301 RET A C14 1 
HETATM 2630 C  C15 A RET B 2 .   ? -3.99678  17.45193 -3.38157  0.500 14.86208  ? 301 RET A C15 1 
HETATM 2631 C  C15 B RET B 2 .   ? -4.31217  16.09776 -4.23794  0.300 22.02441  ? 301 RET A C15 1 
HETATM 2632 C  C15 C RET B 2 .   ? -3.90142  16.65518 -2.90869  0.200 13.55277  ? 301 RET A C15 1 
HETATM 2633 C  C16 A RET B 2 .   ? -8.86830  9.61007  -9.44410  0.500 19.93989  ? 301 RET A C16 1 
HETATM 2634 C  C16 B RET B 2 .   ? -8.92321  9.33648  -9.62014  0.300 19.64229  ? 301 RET A C16 1 
HETATM 2635 C  C16 C RET B 2 .   ? -8.60697  9.71850  -9.56657  0.200 19.51305  ? 301 RET A C16 1 
HETATM 2636 C  C17 A RET B 2 .   ? -9.54753  11.76939 -10.53198 0.500 17.91966  ? 301 RET A C17 1 
HETATM 2637 C  C17 B RET B 2 .   ? -9.88370  11.39949 -10.66213 0.300 19.11816  ? 301 RET A C17 1 
HETATM 2638 C  C17 C RET B 2 .   ? -9.72273  11.51959 -10.89021 0.200 17.25781  ? 301 RET A C17 1 
HETATM 2639 C  C18 A RET B 2 .   ? -13.36901 10.75299 -7.79459  0.500 21.88613  ? 301 RET A C18 1 
HETATM 2640 C  C18 B RET B 2 .   ? -13.44167 9.82513  -7.78864  0.300 18.59345  ? 301 RET A C18 1 
HETATM 2641 C  C18 C RET B 2 .   ? -13.18707 10.59294 -7.83901  0.200 21.82921  ? 301 RET A C18 1 
HETATM 2642 C  C19 A RET B 2 .   ? -9.97169  12.70980 -5.02152  0.500 16.68617  ? 301 RET A C19 1 
HETATM 2643 C  C19 B RET B 2 .   ? -10.56164 12.36113 -5.16386  0.300 19.36731  ? 301 RET A C19 1 
HETATM 2644 C  C19 C RET B 2 .   ? -9.96980  12.68200 -5.16581  0.200 17.29579  ? 301 RET A C19 1 
HETATM 2645 C  C20 A RET B 2 .   ? -6.58421  15.97316 -2.84692  0.500 18.28290  ? 301 RET A C20 1 
HETATM 2646 C  C20 B RET B 2 .   ? -7.83449  15.92480 -2.63304  0.300 20.64856  ? 301 RET A C20 1 
HETATM 2647 C  C20 C RET B 2 .   ? -6.81986  15.86893 -2.87890  0.200 18.13992  ? 301 RET A C20 1 
HETATM 2648 NA NA  A NA  C 3 .   ? -4.45805  11.73454 -20.12501 0.700 28.26298  ? 302 NA  A NA  1 
HETATM 2649 C  C   . 97N D 4 .   ? -12.53084 23.59282 16.28882  1.000 37.24664  ? 303 97N A C   1 
HETATM 2650 O  O   A 97N D 4 .   ? -13.04452 21.03932 5.61241   0.700 48.13544  ? 303 97N A O   1 
HETATM 2651 C  C1  . 97N D 4 .   ? -13.02187 24.45053 15.12409  1.000 48.50260  ? 303 97N A C1  1 
HETATM 2652 O  O1  A 97N D 4 .   ? -11.29983 21.87725 4.49738   0.700 40.99468  ? 303 97N A O1  1 
HETATM 2653 C  C2  . 97N D 4 .   ? -13.90898 23.71097 14.12948  1.000 42.47434  ? 303 97N A C2  1 
HETATM 2654 O  O2  A 97N D 4 .   ? -9.49977  21.63821 2.22826   0.700 40.08717  ? 303 97N A O2  1 
HETATM 2655 C  C3  . 97N D 4 .   ? -14.79254 24.61079 13.26784  1.000 42.17681  ? 303 97N A C3  1 
HETATM 2656 O  O3  A 97N D 4 .   ? -11.04728 19.51715 0.98222   0.700 33.24138  ? 303 97N A O3  1 
HETATM 2657 C  C4  . 97N D 4 .   ? -15.22212 23.94717 11.96612  1.000 33.82865  ? 303 97N A C4  1 
HETATM 2658 C  C5  . 97N D 4 .   ? -16.17587 24.77577 11.08877  1.000 43.10874  ? 303 97N A C5  1 
HETATM 2659 C  C6  . 97N D 4 .   ? -15.87787 26.24306 11.06835  1.000 50.34446  ? 303 97N A C6  1 
HETATM 2660 C  C7  . 97N D 4 .   ? -15.57917 27.06009 10.05151  1.000 40.82406  ? 303 97N A C7  1 
HETATM 2661 C  C8  . 97N D 4 .   ? -15.41794 26.76718 8.59316   1.000 50.92548  ? 303 97N A C8  1 
HETATM 2662 C  C9  . 97N D 4 .   ? -13.93381 26.72798 8.22344   1.000 58.33039  ? 303 97N A C9  1 
HETATM 2663 C  C10 . 97N D 4 .   ? -13.65463 26.91687 6.73778   1.000 55.51329  ? 303 97N A C10 1 
HETATM 2664 C  C11 . 97N D 4 .   ? -13.97519 25.67393 5.92557   1.000 46.19461  ? 303 97N A C11 1 
HETATM 2665 C  C12 . 97N D 4 .   ? -13.49322 24.40378 6.60957   1.000 50.69265  ? 303 97N A C12 1 
HETATM 2666 C  C13 . 97N D 4 .   ? -12.03207 24.16123 6.30407   1.000 51.70499  ? 303 97N A C13 1 
HETATM 2667 C  C14 . 97N D 4 .   ? -11.65981 22.73252 6.62466   1.000 41.03507  ? 303 97N A C14 1 
HETATM 2668 C  C15 A 97N D 4 .   ? -12.09867 21.78672 5.55174   0.700 45.42599  ? 303 97N A C15 1 
HETATM 2669 C  C16 A 97N D 4 .   ? -11.42844 20.88869 3.47352   0.700 38.78517  ? 303 97N A C16 1 
HETATM 2670 C  C17 A 97N D 4 .   ? -10.90939 21.55400 2.21304   0.700 34.36816  ? 303 97N A C17 1 
HETATM 2671 C  C18 A 97N D 4 .   ? -11.47641 20.85324 0.99011   0.700 30.77786  ? 303 97N A C18 1 
HETATM 2672 C  C10 . OLC E 5 .   ? 2.42390   35.06770 12.18249  1.000 39.15423  ? 304 OLC A C10 1 
HETATM 2673 C  C9  . OLC E 5 .   ? 1.64810   34.82047 13.20854  1.000 44.21767  ? 304 OLC A C9  1 
HETATM 2674 C  C11 . OLC E 5 .   ? 1.93944   35.23138 10.77658  1.000 41.22862  ? 304 OLC A C11 1 
HETATM 2675 C  C8  . OLC E 5 .   ? 2.11237   34.58830 14.61028  1.000 45.99121  ? 304 OLC A C8  1 
HETATM 2676 C  C12 . OLC E 5 .   ? 3.00762   35.64501 9.81014   1.000 32.99696  ? 304 OLC A C12 1 
HETATM 2677 C  C7  . OLC E 5 .   ? 3.59506   34.45793 14.71127  1.000 45.56303  ? 304 OLC A C7  1 
HETATM 2678 C  C13 . OLC E 5 .   ? 2.72202   35.23082 8.37391   1.000 44.12359  ? 304 OLC A C13 1 
HETATM 2679 C  C6  . OLC E 5 .   ? 4.04512   33.75374 15.97788  1.000 46.99777  ? 304 OLC A C6  1 
HETATM 2680 C  C14 . OLC E 5 .   ? 2.35143   36.35488 7.43746   1.000 39.04025  ? 304 OLC A C14 1 
HETATM 2681 C  C5  . OLC E 5 .   ? 5.53007   33.60413 16.12735  1.000 38.87398  ? 304 OLC A C5  1 
HETATM 2682 C  C4  . OLC E 5 .   ? 5.89572   32.76237 17.31468  1.000 54.11516  ? 304 OLC A C4  1 
HETATM 2683 C  C3  . OLC E 5 .   ? 7.33789   32.86697 17.76645  1.000 54.27154  ? 304 OLC A C3  1 
HETATM 2684 C  C2  . OLC E 5 .   ? 7.54740   32.24074 19.11366  1.000 56.92444  ? 304 OLC A C2  1 
HETATM 2685 C  C1  . OLC E 5 .   ? 6.79600   32.93004 20.22400  1.000 55.86648  ? 304 OLC A C1  1 
HETATM 2686 O  O19 . OLC E 5 .   ? 6.13759   33.93340 20.11009  1.000 60.24713  ? 304 OLC A O19 1 
HETATM 2687 O  O20 . OLC E 5 .   ? 6.94573   32.29098 21.38019  1.000 73.63652  ? 304 OLC A O20 1 
HETATM 2688 C  C1  . LFA F 6 .   ? -9.81949  30.14656 4.67103   1.000 46.85901  ? 305 LFA A C1  1 
HETATM 2689 C  C2  . LFA F 6 .   ? -10.52801 29.35976 5.75303   1.000 37.01535  ? 305 LFA A C2  1 
HETATM 2690 C  C3  . LFA F 6 .   ? -10.65615 30.07165 7.07936   1.000 42.01638  ? 305 LFA A C3  1 
HETATM 2691 C  C4  . LFA F 6 .   ? -11.47296 29.34772 8.12981   1.000 32.94747  ? 305 LFA A C4  1 
HETATM 2692 C  C5  . LFA F 6 .   ? -11.34279 29.88988 9.53623   1.000 40.33149  ? 305 LFA A C5  1 
HETATM 2693 C  C6  . LFA F 6 .   ? -12.10395 29.10541 10.58700  1.000 39.40012  ? 305 LFA A C6  1 
HETATM 2694 C  C7  . LFA F 6 .   ? -11.64441 29.36023 12.00189  1.000 32.72099  ? 305 LFA A C7  1 
HETATM 2695 C  C8  . LFA F 6 .   ? -12.45420 28.68465 13.07885  1.000 44.08622  ? 305 LFA A C8  1 
HETATM 2696 C  C9  . LFA F 6 .   ? -12.04689 29.05113 14.48657  1.000 47.36569  ? 305 LFA A C9  1 
HETATM 2697 C  C10 . LFA F 6 .   ? -13.00566 28.58092 15.55700  1.000 46.30212  ? 305 LFA A C10 1 
HETATM 2698 C  C8  . LFA G 6 .   ? 12.23155  11.07559 -10.11796 1.000 54.36402  ? 306 LFA A C8  1 
HETATM 2699 C  C9  . LFA G 6 .   ? 11.43128  10.64966 -8.90728  1.000 75.28896  ? 306 LFA A C9  1 
HETATM 2700 C  C10 . LFA G 6 .   ? 9.93225   10.78293 -9.06858  1.000 68.05174  ? 306 LFA A C10 1 
HETATM 2701 C  C11 . LFA G 6 .   ? 9.12883   10.30622 -7.87871  1.000 50.80768  ? 306 LFA A C11 1 
HETATM 2702 C  C12 . LFA G 6 .   ? 7.63978   10.30742 -8.10605  1.000 46.33791  ? 306 LFA A C12 1 
HETATM 2703 C  C13 . LFA G 6 .   ? 6.82864   9.66787  -7.00048  1.000 48.20735  ? 306 LFA A C13 1 
HETATM 2704 C  C14 . LFA G 6 .   ? 7.33434   8.31313  -6.57004  1.000 59.21204  ? 306 LFA A C14 1 
HETATM 2705 C  C15 . LFA G 6 .   ? 6.28149   7.38614  -6.00852  1.000 49.26904  ? 306 LFA A C15 1 
HETATM 2706 C  C16 . LFA G 6 .   ? 5.36098   6.80181  -7.05150  1.000 58.49439  ? 306 LFA A C16 1 
HETATM 2707 C  C17 . LFA G 6 .   ? 4.61523   5.56946  -6.60319  1.000 50.90965  ? 306 LFA A C17 1 
HETATM 2708 C  C18 . LFA G 6 .   ? 3.82044   4.90190  -7.69818  1.000 56.22074  ? 306 LFA A C18 1 
HETATM 2709 C  C19 . LFA G 6 .   ? 3.22496   3.56458  -7.33989  1.000 42.66369  ? 306 LFA A C19 1 
HETATM 2710 C  C20 . LFA G 6 .   ? 2.22077   3.59279  -6.21389  1.000 56.01334  ? 306 LFA A C20 1 
HETATM 2711 C  C1  . LFA H 6 .   ? -13.55973 24.35775 -5.80883  1.000 49.28698  ? 307 LFA A C1  1 
HETATM 2712 C  C2  . LFA H 6 .   ? -12.84790 25.16407 -6.86640  1.000 33.82001  ? 307 LFA A C2  1 
HETATM 2713 C  C3  . LFA H 6 .   ? -12.90871 24.57416 -8.25291  1.000 46.05775  ? 307 LFA A C3  1 
HETATM 2714 C  C4  . LFA H 6 .   ? -12.53322 25.54179 -9.34456  1.000 34.96120  ? 307 LFA A C4  1 
HETATM 2715 C  C5  . LFA H 6 .   ? -12.89808 25.09868 -10.74821 1.000 38.56252  ? 307 LFA A C5  1 
HETATM 2716 C  C6  . LFA H 6 .   ? -12.38744 26.01124 -11.84122 1.000 48.93622  ? 307 LFA A C6  1 
HETATM 2717 C  C7  . LFA H 6 .   ? -12.93844 25.70365 -13.22007 1.000 46.40911  ? 307 LFA A C7  1 
HETATM 2718 C  C8  . LFA H 6 .   ? -12.19352 26.37433 -14.34857 1.000 43.25947  ? 307 LFA A C8  1 
HETATM 2719 C  C9  . LFA H 6 .   ? -12.38899 25.71784 -15.69687 1.000 39.28829  ? 307 LFA A C9  1 
HETATM 2720 C  C10 . LFA H 6 .   ? -11.39442 26.14875 -16.75050 1.000 48.54097  ? 307 LFA A C10 1 
HETATM 2721 C  C11 . LFA H 6 .   ? -11.78474 27.36148 -17.55742 1.000 46.91986  ? 307 LFA A C11 1 
HETATM 2722 C  C12 . LFA H 6 .   ? -12.65412 27.05841 -18.74631 1.000 43.04324  ? 307 LFA A C12 1 
HETATM 2723 C  C6  . LFA I 6 .   ? 9.49650   14.08273 -4.00065  1.000 51.75698  ? 308 LFA A C6  1 
HETATM 2724 C  C7  . LFA I 6 .   ? 8.74036   14.26194 -5.29783  1.000 54.67087  ? 308 LFA A C7  1 
HETATM 2725 C  C8  . LFA I 6 .   ? 7.43794   13.50732 -5.36101  1.000 50.31675  ? 308 LFA A C8  1 
HETATM 2726 C  C9  . LFA I 6 .   ? 6.75027   13.54721 -6.70305  1.000 37.03963  ? 308 LFA A C9  1 
HETATM 2727 C  C10 . LFA I 6 .   ? 6.38686   14.93161 -7.17787  1.000 35.17511  ? 308 LFA A C10 1 
HETATM 2728 C  C11 . LFA I 6 .   ? 5.38749   14.94559 -8.31289  1.000 33.38611  ? 308 LFA A C11 1 
HETATM 2729 C  C12 . LFA I 6 .   ? 5.90810   14.51669 -9.65649  1.000 38.81553  ? 308 LFA A C12 1 
HETATM 2730 C  C13 . LFA I 6 .   ? 6.96327   15.41733 -10.24465 1.000 40.76013  ? 308 LFA A C13 1 
HETATM 2731 C  C14 . LFA I 6 .   ? 7.55273   14.90044 -11.53737 1.000 55.48820  ? 308 LFA A C14 1 
HETATM 2732 C  C15 . LFA I 6 .   ? 8.16884   13.52117 -11.44262 1.000 59.12668  ? 308 LFA A C15 1 
HETATM 2733 C  C16 . LFA I 6 .   ? 8.71667   12.99745 -12.75257 1.000 54.09087  ? 308 LFA A C16 1 
HETATM 2734 C  C17 . LFA I 6 .   ? 7.66357   12.60099 -13.76326 1.000 48.02133  ? 308 LFA A C17 1 
HETATM 2735 C  C18 . LFA I 6 .   ? 8.13295   12.62847 -15.20282 1.000 47.06454  ? 308 LFA A C18 1 
HETATM 2736 C  C19 . LFA I 6 .   ? 7.12348   12.15139 -16.21655 1.000 40.55427  ? 308 LFA A C19 1 
HETATM 2737 C  C20 . LFA I 6 .   ? 7.37530   12.65019 -17.62460 1.000 36.87293  ? 308 LFA A C20 1 
HETATM 2738 C  C5  . LFA J 6 .   ? -8.09049  -2.01585 -9.28327  1.000 48.30461  ? 309 LFA A C5  1 
HETATM 2739 C  C6  . LFA J 6 .   ? -8.07371  -2.74482 -7.95733  1.000 58.90992  ? 309 LFA A C6  1 
HETATM 2740 C  C7  . LFA J 6 .   ? -9.31335  -2.54827 -7.11542  1.000 46.40051  ? 309 LFA A C7  1 
HETATM 2741 C  C8  . LFA J 6 .   ? -10.23992 -3.74168 -7.05219  1.000 61.87885  ? 309 LFA A C8  1 
HETATM 2742 C  C9  . LFA J 6 .   ? -9.77045  -4.87238 -6.16051  1.000 61.30735  ? 309 LFA A C9  1 
HETATM 2743 C  C10 . LFA J 6 .   ? -9.75495  -4.54764 -4.68327  1.000 63.64140  ? 309 LFA A C10 1 
HETATM 2744 C  C11 . LFA J 6 .   ? -11.10586 -4.19143 -4.09747  1.000 82.30095  ? 309 LFA A C11 1 
HETATM 2745 C  C12 . LFA J 6 .   ? -11.03932 -3.39491 -2.80862  1.000 75.71699  ? 309 LFA A C12 1 
HETATM 2746 C  C13 . LFA J 6 .   ? -11.08345 -4.19226 -1.52845  1.000 64.96863  ? 309 LFA A C13 1 
HETATM 2747 C  C14 . LFA J 6 .   ? -10.53818 -3.44831 -0.32680  1.000 55.55400  ? 309 LFA A C14 1 
HETATM 2748 C  C15 . LFA J 6 .   ? -10.91347 -1.98880 -0.26685  1.000 47.58101  ? 309 LFA A C15 1 
HETATM 2749 C  C16 . LFA J 6 .   ? -10.30090 -1.24388 0.89597   1.000 36.80237  ? 309 LFA A C16 1 
HETATM 2750 C  C17 . LFA J 6 .   ? -10.66332 -1.82493 2.24224   1.000 42.96533  ? 309 LFA A C17 1 
HETATM 2751 C  C18 . LFA J 6 .   ? -12.14615 -1.81051 2.54636   1.000 53.43991  ? 309 LFA A C18 1 
HETATM 2752 C  C19 . LFA J 6 .   ? -12.63489 -2.64845 3.70692   1.000 54.40756  ? 309 LFA A C19 1 
HETATM 2753 C  C20 . LFA J 6 .   ? -12.33292 -2.16186 5.10072   1.000 42.86140  ? 309 LFA A C20 1 
HETATM 2754 C  C1  . LFA K 6 .   ? -20.22989 8.81874  2.50569   1.000 36.63382  ? 310 LFA A C1  1 
HETATM 2755 C  C2  . LFA K 6 .   ? -20.92107 9.62719  3.58477   1.000 39.74203  ? 310 LFA A C2  1 
HETATM 2756 C  C3  . LFA K 6 .   ? -21.64356 8.76519  4.59469   1.000 49.64293  ? 310 LFA A C3  1 
HETATM 2757 C  C4  . LFA K 6 .   ? -22.55452 9.47705  5.56276   1.000 45.48850  ? 310 LFA A C4  1 
HETATM 2758 C  C5  . LFA K 6 .   ? -23.24122 8.56218  6.55250   1.000 45.78013  ? 310 LFA A C5  1 
HETATM 2759 C  C16 . LFA L 6 .   ? 9.45064   24.87525 3.99016   1.000 57.96621  ? 311 LFA A C16 1 
HETATM 2760 C  C17 . LFA L 6 .   ? 8.14495   24.52240 3.32390   1.000 52.35768  ? 311 LFA A C17 1 
HETATM 2761 C  C18 . LFA L 6 .   ? 8.21208   24.43953 1.81647   1.000 50.83995  ? 311 LFA A C18 1 
HETATM 2762 C  C15 . LFA M 6 .   ? 12.04627  19.09471 -16.44118 1.000 40.31956  ? 312 LFA A C15 1 
HETATM 2763 C  C16 . LFA M 6 .   ? 12.63644  18.90994 -15.06425 1.000 42.26089  ? 312 LFA A C16 1 
HETATM 2764 C  C17 . LFA M 6 .   ? 11.94369  19.72004 -13.99236 1.000 36.89980  ? 312 LFA A C17 1 
HETATM 2765 C  C18 . LFA M 6 .   ? 12.41037  19.44805 -12.58059 1.000 49.44499  ? 312 LFA A C18 1 
HETATM 2766 C  C19 . LFA M 6 .   ? 11.66111  20.27006 -11.56201 1.000 40.79427  ? 312 LFA A C19 1 
HETATM 2767 C  C20 . LFA M 6 .   ? 12.01142  20.02467 -10.11639 1.000 37.05970  ? 312 LFA A C20 1 
HETATM 2768 C  C1  . LFA N 6 .   ? -14.58563 27.90455 0.36410   1.000 51.36195  ? 313 LFA A C1  1 
HETATM 2769 C  C2  . LFA N 6 .   ? -15.07464 28.19195 -1.03425  1.000 53.31566  ? 313 LFA A C2  1 
HETATM 2770 C  C3  . LFA N 6 .   ? -14.01294 28.00487 -2.08673  1.000 45.67627  ? 313 LFA A C3  1 
HETATM 2771 C  C4  . LFA N 6 .   ? -14.35763 28.52978 -3.46292  1.000 45.30730  ? 313 LFA A C4  1 
HETATM 2772 C  C5  . LFA N 6 .   ? -13.23025 28.38458 -4.45477  1.000 51.50731  ? 313 LFA A C5  1 
HETATM 2773 C  C6  . LFA N 6 .   ? -11.87028 28.55728 -3.82175  1.000 66.21885  ? 313 LFA A C6  1 
HETATM 2774 C  C7  . LFA N 6 .   ? -11.03134 29.67581 -4.37574  1.000 61.16385  ? 313 LFA A C7  1 
HETATM 2775 C  C8  . LFA N 6 .   ? -10.68673 29.53100 -5.82989  1.000 51.33710  ? 313 LFA A C8  1 
HETATM 2776 C  C9  . LFA N 6 .   ? -9.72768  30.58149 -6.31930  1.000 66.98871  ? 313 LFA A C9  1 
HETATM 2777 C  C10 . LFA N 6 .   ? -9.63616  30.68938 -7.81788  1.000 61.66652  ? 313 LFA A C10 1 
HETATM 2778 C  C11 . LFA N 6 .   ? -10.94456 31.01488 -8.49591  1.000 55.67978  ? 313 LFA A C11 1 
HETATM 2779 C  C12 . LFA N 6 .   ? -10.80388 31.29449 -9.96920  1.000 49.63080  ? 313 LFA A C12 1 
HETATM 2780 C  C13 . LFA N 6 .   ? -10.03118 30.23485 -10.69975 1.000 43.41148  ? 313 LFA A C13 1 
HETATM 2781 C  C14 . LFA N 6 .   ? -9.81672  30.48334 -12.16940 1.000 48.55653  ? 313 LFA A C14 1 
HETATM 2782 C  C15 . LFA N 6 .   ? -8.91334  31.63779 -12.50030 1.000 45.80854  ? 313 LFA A C15 1 
HETATM 2783 C  C16 . LFA N 6 .   ? -8.23943  31.50130 -13.83900 1.000 49.21911  ? 313 LFA A C16 1 
HETATM 2784 C  C17 . LFA N 6 .   ? -9.17650  31.15575 -14.96515 1.000 54.08217  ? 313 LFA A C17 1 
HETATM 2785 C  C18 . LFA N 6 .   ? -8.48588  30.81813 -16.26385 1.000 49.26590  ? 313 LFA A C18 1 
HETATM 2786 C  C19 . LFA N 6 .   ? -9.44510  30.60171 -17.40404 1.000 56.42588  ? 313 LFA A C19 1 
HETATM 2787 C  C20 . LFA N 6 .   ? -10.34978 31.79485 -17.61289 1.000 62.55291  ? 313 LFA A C20 1 
HETATM 2788 C  C1  A GOL O 7 .   ? -0.14583  1.25965  -15.47462 0.500 52.54118  ? 314 GOL A C1  1 
HETATM 2789 O  O1  A GOL O 7 .   ? 1.18962   1.15706  -15.86702 0.500 56.32863  ? 314 GOL A O1  1 
HETATM 2790 C  C2  A GOL O 7 .   ? -0.54356  -0.07005 -14.80174 0.500 49.99842  ? 314 GOL A C2  1 
HETATM 2791 O  O2  A GOL O 7 .   ? -0.00101  -0.19300 -13.53099 0.500 51.95788  ? 314 GOL A O2  1 
HETATM 2792 C  C3  A GOL O 7 .   ? -0.03649  -1.16497 -15.75578 0.500 52.17086  ? 314 GOL A C3  1 
HETATM 2793 O  O3  A GOL O 7 .   ? -1.14293  -1.70289 -16.43237 0.500 48.51769  ? 314 GOL A O3  1 
HETATM 2794 C  C1  . GOL P 7 .   ? -11.22274 21.76845 20.87350  1.000 58.48350  ? 315 GOL A C1  1 
HETATM 2795 O  O1  . GOL P 7 .   ? -11.59918 20.45011 20.58272  1.000 37.17224  ? 315 GOL A O1  1 
HETATM 2796 C  C2  . GOL P 7 .   ? -10.10558 21.68210 21.95954  1.000 60.23586  ? 315 GOL A C2  1 
HETATM 2797 O  O2  . GOL P 7 .   ? -9.76927  22.94008 22.43929  1.000 72.86962  ? 315 GOL A O2  1 
HETATM 2798 C  C3  . GOL P 7 .   ? -10.68173 20.77121 23.07476  1.000 62.45129  ? 315 GOL A C3  1 
HETATM 2799 O  O3  . GOL P 7 .   ? -9.71838  19.80072 23.39224  1.000 53.92028  ? 315 GOL A O3  1 
HETATM 2800 C  C1  . GOL Q 7 .   ? 1.80059   7.29262  -19.92798 1.000 48.12285  ? 316 GOL A C1  1 
HETATM 2801 O  O1  . GOL Q 7 .   ? 2.83268   7.81567  -20.71668 1.000 64.54856  ? 316 GOL A O1  1 
HETATM 2802 C  C2  . GOL Q 7 .   ? 2.46611   6.46713  -18.79102 1.000 60.98199  ? 316 GOL A C2  1 
HETATM 2803 O  O2  . GOL Q 7 .   ? 3.83874   6.69852  -18.71139 1.000 64.75217  ? 316 GOL A O2  1 
HETATM 2804 C  C3  . GOL Q 7 .   ? 2.12452   4.97884  -19.10752 1.000 75.46890  ? 316 GOL A C3  1 
HETATM 2805 O  O3  . GOL Q 7 .   ? 2.06654   4.29048  -17.88009 1.000 69.21572  ? 316 GOL A O3  1 
HETATM 2806 C  C24 . OLC R 5 .   ? 2.15574   9.89561  10.19274  0.700 44.75213  ? 317 OLC A C24 1 
HETATM 2807 C  C4  . OLC R 5 .   ? -1.26434  3.68479  9.42547   0.700 38.33065  ? 317 OLC A C4  1 
HETATM 2808 C  C3  . OLC R 5 .   ? -0.91235  4.48222  10.67089  0.700 41.83151  ? 317 OLC A C3  1 
HETATM 2809 C  C2  . OLC R 5 .   ? -0.33827  5.82015  10.34237  0.700 37.34966  ? 317 OLC A C2  1 
HETATM 2810 C  C21 . OLC R 5 .   ? 2.76159   7.63976  11.16492  0.700 51.35333  ? 317 OLC A C21 1 
HETATM 2811 C  C1  . OLC R 5 .   ? 0.98614   6.09473  10.99741  0.700 42.87841  ? 317 OLC A C1  1 
HETATM 2812 C  C22 . OLC R 5 .   ? 3.25184   8.89049  10.47121  0.700 46.32768  ? 317 OLC A C22 1 
HETATM 2813 O  O19 . OLC R 5 .   ? 1.51868   5.39215  11.81526  0.700 62.11821  ? 317 OLC A O19 1 
HETATM 2814 O  O25 . OLC R 5 .   ? 1.55668   10.36457 11.39675  0.700 33.26765  ? 317 OLC A O25 1 
HETATM 2815 O  O23 . OLC R 5 .   ? 4.27249   9.49214  11.26627  0.700 62.15903  ? 317 OLC A O23 1 
HETATM 2816 O  O20 . OLC R 5 .   ? 1.53097   7.21806  10.53666  0.700 57.22557  ? 317 OLC A O20 1 
HETATM 2817 C  C10 . OLC S 5 .   ? 2.20915   40.80331 1.64033   1.000 53.96114  ? 318 OLC A C10 1 
HETATM 2818 C  C9  . OLC S 5 .   ? 1.34669   40.33090 0.76635   1.000 40.08967  ? 318 OLC A C9  1 
HETATM 2819 C  C11 . OLC S 5 .   ? 2.43018   42.23768 2.01649   1.000 41.08462  ? 318 OLC A C11 1 
HETATM 2820 C  C8  . OLC S 5 .   ? 1.16117   38.88119 0.43486   1.000 47.49506  ? 318 OLC A C8  1 
HETATM 2821 C  C24 . OLC S 5 .   ? -5.44296  39.44154 -9.95184  1.000 50.63862  ? 318 OLC A C24 1 
HETATM 2822 C  C7  . OLC S 5 .   ? 0.19828   38.61328 -0.68322  1.000 52.18522  ? 318 OLC A C7  1 
HETATM 2823 C  C6  . OLC S 5 .   ? -1.22864  39.09113 -0.44345  1.000 65.02297  ? 318 OLC A C6  1 
HETATM 2824 C  C5  . OLC S 5 .   ? -1.67309  40.20949 -1.36158  1.000 60.06976  ? 318 OLC A C5  1 
HETATM 2825 C  C4  . OLC S 5 .   ? -1.83005  39.81768 -2.81495  1.000 48.84337  ? 318 OLC A C4  1 
HETATM 2826 C  C3  . OLC S 5 .   ? -1.93664  41.00687 -3.75550  1.000 52.85059  ? 318 OLC A C3  1 
HETATM 2827 C  C2  . OLC S 5 .   ? -3.13991  40.96260 -4.64801  1.000 58.39750  ? 318 OLC A C2  1 
HETATM 2828 C  C21 . OLC S 5 .   ? -3.86046  39.55266 -7.97583  1.000 59.02503  ? 318 OLC A C21 1 
HETATM 2829 C  C1  . OLC S 5 .   ? -3.01362  40.03021 -5.82297  1.000 64.20729  ? 318 OLC A C1  1 
HETATM 2830 C  C22 . OLC S 5 .   ? -4.48732  40.29136 -9.13955  1.000 61.76161  ? 318 OLC A C22 1 
HETATM 2831 O  O19 . OLC S 5 .   ? -2.28896  39.07071 -5.88682  1.000 68.27159  ? 318 OLC A O19 1 
HETATM 2832 O  O25 . OLC S 5 .   ? -5.71799  40.01871 -11.22601 1.000 60.26094  ? 318 OLC A O25 1 
HETATM 2833 O  O23 . OLC S 5 .   ? -5.11968  41.49022 -8.69134  1.000 77.08163  ? 318 OLC A O23 1 
HETATM 2834 O  O20 . OLC S 5 .   ? -3.78661  40.42880 -6.83053  1.000 77.08439  ? 318 OLC A O20 1 
HETATM 2835 C  C7  . OLC T 5 .   ? 16.32041  21.16314 -10.44251 1.000 46.94341  ? 319 OLC A C7  1 
HETATM 2836 C  C6  . OLC T 5 .   ? 16.44953  21.60813 -11.89235 1.000 43.82027  ? 319 OLC A C6  1 
HETATM 2837 C  C5  . OLC T 5 .   ? 15.24754  22.34482 -12.40463 1.000 46.24990  ? 319 OLC A C5  1 
HETATM 2838 C  C4  . OLC T 5 .   ? 15.42194  22.99066 -13.75340 1.000 42.98662  ? 319 OLC A C4  1 
HETATM 2839 C  C3  . OLC T 5 .   ? 15.57049  22.02982 -14.91960 1.000 49.69481  ? 319 OLC A C3  1 
HETATM 2840 C  C2  . OLC T 5 .   ? 15.18052  22.67013 -16.21972 1.000 50.10807  ? 319 OLC A C2  1 
HETATM 2841 C  C1  . OLC T 5 .   ? 15.27544  21.74568 -17.39944 1.000 66.70769  ? 319 OLC A C1  1 
HETATM 2842 O  O19 . OLC T 5 .   ? 15.81556  20.66963 -17.39371 1.000 93.26650  ? 319 OLC A O19 1 
HETATM 2843 O  O20 . OLC T 5 .   ? 14.66226  22.25105 -18.46664 1.000 75.02140  ? 319 OLC A O20 1 
HETATM 2844 C  C10 . OLC U 5 .   ? -16.06549 -3.43050 1.10798   1.000 48.86237  ? 320 OLC A C10 1 
HETATM 2845 C  C9  . OLC U 5 .   ? -17.02978 -2.59589 1.41167   1.000 63.09787  ? 320 OLC A C9  1 
HETATM 2846 C  C11 . OLC U 5 .   ? -15.12229 -3.30857 -0.04704  1.000 49.93509  ? 320 OLC A C11 1 
HETATM 2847 C  C8  . OLC U 5 .   ? -18.03812 -2.79657 2.50189   1.000 68.46707  ? 320 OLC A C8  1 
HETATM 2848 C  C12 . OLC U 5 .   ? -15.80712 -3.46785 -1.36911  1.000 53.86535  ? 320 OLC A C12 1 
HETATM 2849 C  C7  . OLC U 5 .   ? -18.13989 -1.67945 3.49758   1.000 56.34679  ? 320 OLC A C7  1 
HETATM 2850 C  C6  . OLC U 5 .   ? -17.25077 -1.82260 4.72669   1.000 54.01031  ? 320 OLC A C6  1 
HETATM 2851 C  C5  . OLC U 5 .   ? -17.66043 -0.91866 5.86801   1.000 52.72191  ? 320 OLC A C5  1 
HETATM 2852 C  C4  . OLC U 5 .   ? -16.86683 -1.08679 7.14391   1.000 51.23530  ? 320 OLC A C4  1 
HETATM 2853 C  C3  . OLC U 5 .   ? -17.36147 -0.21048 8.28683   1.000 68.04318  ? 320 OLC A C3  1 
HETATM 2854 C  C2  . OLC U 5 .   ? -16.52948 -0.33774 9.53253   1.000 61.77582  ? 320 OLC A C2  1 
HETATM 2855 C  C21 . OLC U 5 .   ? -16.27255 1.97071  12.41531  1.000 50.06309  ? 320 OLC A C21 1 
HETATM 2856 C  C1  . OLC U 5 .   ? -16.98564 0.56825  10.64544  1.000 66.62471  ? 320 OLC A C1  1 
HETATM 2857 C  C22 . OLC U 5 .   ? -16.68874 1.15312  13.61795  1.000 63.18485  ? 320 OLC A C22 1 
HETATM 2858 O  O19 . OLC U 5 .   ? -18.13629 0.81401  10.89821  1.000 86.75566  ? 320 OLC A O19 1 
HETATM 2859 O  O20 . OLC U 5 .   ? -15.95842 1.08066  11.32011  1.000 80.19336  ? 320 OLC A O20 1 
HETATM 2860 C  C10 . OLC V 5 .   ? -0.69103  -2.83551 -11.45656 1.000 60.96691  ? 321 OLC A C10 1 
HETATM 2861 C  C9  . OLC V 5 .   ? -1.74748  -2.21795 -11.89663 1.000 60.97801  ? 321 OLC A C9  1 
HETATM 2862 C  C11 . OLC V 5 .   ? -0.69761  -4.25663 -10.98775 1.000 49.86907  ? 321 OLC A C11 1 
HETATM 2863 C  C8  . OLC V 5 .   ? -3.08594  -2.87727 -11.99145 1.000 54.21376  ? 321 OLC A C8  1 
HETATM 2864 C  C12 . OLC V 5 .   ? 0.12833   -4.44986 -9.76227  1.000 54.02377  ? 321 OLC A C12 1 
HETATM 2865 C  C7  . OLC V 5 .   ? -3.41186  -3.29381 -13.38607 1.000 58.84954  ? 321 OLC A C7  1 
HETATM 2866 C  C13 . OLC V 5 .   ? 0.32915   -5.89580 -9.35627  1.000 33.31241  ? 321 OLC A C13 1 
HETATM 2867 C  C6  . OLC V 5 .   ? -4.77128  -3.95928 -13.53860 1.000 54.08403  ? 321 OLC A C6  1 
HETATM 2868 C  C14 . OLC V 5 .   ? 1.47291   -6.06631 -8.39491  1.000 34.42769  ? 321 OLC A C14 1 
HETATM 2869 C  C5  . OLC V 5 .   ? -5.04952  -4.45304 -14.93223 1.000 56.21963  ? 321 OLC A C5  1 
HETATM 2870 C  C4  . OLC V 5 .   ? -5.28959  -3.36599 -15.94973 1.000 57.87549  ? 321 OLC A C4  1 
HETATM 2871 C  C3  . OLC V 5 .   ? -5.27882  -3.86735 -17.38498 1.000 66.44129  ? 321 OLC A C3  1 
HETATM 2872 C  C2  . OLC V 5 .   ? -6.09181  -3.01329 -18.30480 1.000 73.45774  ? 321 OLC A C2  1 
HETATM 2873 C  C1  . OLC V 5 .   ? -7.57092  -3.27143 -18.20643 1.000 79.43070  ? 321 OLC A C1  1 
HETATM 2874 O  O19 . OLC V 5 .   ? -8.20039  -3.34184 -17.18150 1.000 83.50187  ? 321 OLC A O19 1 
HETATM 2875 O  O20 . OLC V 5 .   ? -8.12277  -3.39781 -19.41001 1.000 84.88004  ? 321 OLC A O20 1 
HETATM 2876 O  O   . HOH W 8 .   ? -10.45530 13.89938 -20.32208 1.000 37.19667  ? 401 HOH A O   1 
HETATM 2877 O  O   . HOH W 8 .   ? -6.61244  25.82410 24.52958  1.000 46.26088  ? 402 HOH A O   1 
HETATM 2878 O  O   . HOH W 8 .   ? -6.33522  15.06764 -21.59798 1.000 30.45196  ? 403 HOH A O   1 
HETATM 2879 O  O   . HOH W 8 .   ? -1.18526  23.62959 1.92429   1.000 32.37546  ? 404 HOH A O   1 
HETATM 2880 O  O   . HOH W 8 .   ? -12.25776 -0.34517 -20.41164 1.000 46.27250  ? 405 HOH A O   1 
HETATM 2881 O  O   . HOH W 8 .   ? -2.82351  11.16664 23.19410  1.000 25.73836  ? 406 HOH A O   1 
HETATM 2882 O  O   . HOH W 8 .   ? -2.26277  24.74594 -4.35379  1.000 26.97804  ? 407 HOH A O   1 
HETATM 2883 O  O   . HOH W 8 .   ? -3.58321  17.50487 21.39282  1.000 22.02258  ? 408 HOH A O   1 
HETATM 2884 O  O   . HOH W 8 .   ? 10.01661  22.37607 -21.39473 1.000 48.34592  ? 409 HOH A O   1 
HETATM 2885 O  O   A HOH W 8 .   ? 0.13188   16.76272 -14.87047 0.300 29.71615  ? 410 HOH A O   1 
HETATM 2886 O  O   B HOH W 8 .   ? -3.22630  21.09337 3.91285   0.300 25.63654  ? 411 HOH A O   1 
HETATM 2887 O  O   A HOH W 8 .   ? -1.67003  18.04233 -5.90833  0.700 28.04720  ? 412 HOH A O   1 
HETATM 2888 O  O   . HOH W 8 .   ? 0.12452   10.73843 -21.98099 1.000 52.86438  ? 413 HOH A O   1 
HETATM 2889 O  O   . HOH W 8 .   ? 9.46587   17.70229 -18.22900 1.000 47.29239  ? 414 HOH A O   1 
HETATM 2890 O  O   . HOH W 8 .   ? -6.56980  10.99321 24.90240  1.000 41.73817  ? 415 HOH A O   1 
HETATM 2891 O  O   . HOH W 8 .   ? -9.75543  17.20751 21.73654  1.000 28.12505  ? 416 HOH A O   1 
HETATM 2892 O  O   . HOH W 8 .   ? -3.55807  31.89256 -25.29428 1.000 60.39081  ? 417 HOH A O   1 
HETATM 2893 O  O   . HOH W 8 .   ? -18.01801 9.51046  16.90593  1.000 55.34381  ? 418 HOH A O   1 
HETATM 2894 O  O   . HOH W 8 .   ? -6.92331  -0.86443 18.68186  1.000 35.88176  ? 419 HOH A O   1 
HETATM 2895 O  O   A HOH W 8 .   ? 0.86238   23.98800 4.93537   0.700 21.67437  ? 420 HOH A O   1 
HETATM 2896 O  O   . HOH W 8 .   ? -15.72529 12.94196 -20.79089 1.000 46.44511  ? 421 HOH A O   1 
HETATM 2897 O  O   . HOH W 8 .   ? 0.06041   5.11355  22.21415  1.000 31.81865  ? 422 HOH A O   1 
HETATM 2898 O  O   . HOH W 8 .   ? -10.39519 9.08503  20.46455  1.000 32.59111  ? 423 HOH A O   1 
HETATM 2899 O  O   . HOH W 8 .   ? -3.32015  26.44016 22.63673  1.000 27.68514  ? 424 HOH A O   1 
HETATM 2900 O  O   . HOH W 8 .   ? -9.24091  30.81385 22.47429  1.000 64.72489  ? 425 HOH A O   1 
HETATM 2901 O  O   . HOH W 8 .   ? 9.41956   37.49406 11.23066  1.000 22.11311  ? 426 HOH A O   1 
HETATM 2902 O  O   . HOH W 8 .   ? -14.23588 2.98180  16.92544  1.000 54.64089  ? 427 HOH A O   1 
HETATM 2903 O  O   . HOH W 8 .   ? -7.04713  12.33308 -13.75002 1.000 23.07999  ? 428 HOH A O   1 
HETATM 2904 O  O   . HOH W 8 .   ? 2.11305   25.61050 16.95410  1.000 24.19281  ? 429 HOH A O   1 
HETATM 2905 O  O   . HOH W 8 .   ? -0.66982  20.99663 2.36970   1.000 32.67556  ? 430 HOH A O   1 
HETATM 2906 O  O   A HOH W 8 .   ? -13.67760 11.39937 16.57762  0.700 26.16979  ? 431 HOH A O   1 
HETATM 2907 O  O   B HOH W 8 .   ? -12.67738 11.24613 16.26501  0.300 28.41184  ? 431 HOH A O   1 
HETATM 2908 O  O   . HOH W 8 .   ? -24.41653 13.53116 7.74356   1.000 31.77632  ? 432 HOH A O   1 
HETATM 2909 O  O   A HOH W 8 .   ? 6.88372   17.78613 -22.57438 0.700 56.67496  ? 433 HOH A O   1 
HETATM 2910 O  O   . HOH W 8 .   ? -7.49406  27.93643 24.16236  1.000 40.40653  ? 434 HOH A O   1 
HETATM 2911 O  O   . HOH W 8 .   ? -10.35521 7.86711  -1.69513  1.000 19.44127  ? 435 HOH A O   1 
HETATM 2912 O  O   . HOH W 8 .   ? -4.231    9.625    -26.741   1.000 53.93061  ? 436 HOH A O   1 
HETATM 2913 O  O   A HOH W 8 .   ? -3.27522  -5.49506 14.64374  0.500 29.00471  ? 437 HOH A O   1 
HETATM 2914 O  O   . HOH W 8 .   ? -6.749    7.483    26.221    1.000 54.97889  ? 438 HOH A O   1 
HETATM 2915 O  O   . HOH W 8 .   ? 1.96254   12.12235 18.96839  1.000 22.85836  ? 439 HOH A O   1 
HETATM 2916 O  O   . HOH W 8 .   ? -9.78054  18.84842 25.92636  1.000 36.79553  ? 440 HOH A O   1 
HETATM 2917 O  O   . HOH W 8 .   ? 3.07731   23.87966 -1.90516  1.000 24.59696  ? 441 HOH A O   1 
HETATM 2918 O  O   . HOH W 8 .   ? -10.03066 6.48691  -20.16611 1.000 29.81704  ? 442 HOH A O   1 
HETATM 2919 O  O   . HOH W 8 .   ? -17.67174 17.95227 18.01942  1.000 30.09016  ? 443 HOH A O   1 
HETATM 2920 O  O   . HOH W 8 .   ? -3.29768  4.18838  21.56534  1.000 24.83774  ? 444 HOH A O   1 
HETATM 2921 O  O   . HOH W 8 .   ? -1.32432  6.08727  -1.65484  1.000 24.74267  ? 445 HOH A O   1 
HETATM 2922 O  O   . HOH W 8 .   ? -18.77326 8.34388  13.77811  1.000 34.31286  ? 446 HOH A O   1 
HETATM 2923 O  O   . HOH W 8 .   ? -6.72981  17.07451 21.74875  1.000 26.17767  ? 447 HOH A O   1 
HETATM 2924 O  O   . HOH W 8 .   ? -8.65037  18.24239 1.50252   1.000 22.58724  ? 448 HOH A O   1 
HETATM 2925 O  O   . HOH W 8 .   ? -0.00000  0.00000  18.74267  0.500 26.19492  ? 449 HOH A O   1 
HETATM 2926 O  O   A HOH W 8 .   ? -2.79223  18.03433 -9.07793  0.700 21.05914  ? 450 HOH A O   1 
HETATM 2927 O  O   . HOH W 8 .   ? -21.34982 10.74579 13.06685  1.000 32.14901  ? 451 HOH A O   1 
HETATM 2928 O  O   . HOH W 8 .   ? -26.17120 12.31613 9.48747   1.000 41.45548  ? 452 HOH A O   1 
HETATM 2929 O  O   . HOH W 8 .   ? -14.35983 11.97908 23.67780  1.000 54.56009  ? 453 HOH A O   1 
HETATM 2930 O  O   A HOH W 8 .   ? -0.29189  17.10216 -8.73045  0.700 25.28131  ? 454 HOH A O   1 
HETATM 2931 O  O   . HOH W 8 .   ? 4.34815   3.69733  17.96323  1.000 44.17941  ? 455 HOH A O   1 
HETATM 2932 O  O   . HOH W 8 .   ? -8.97603  11.89795 24.67992  1.000 51.48423  ? 456 HOH A O   1 
HETATM 2933 O  O   . HOH W 8 .   ? 3.12754   15.21679 12.64967  1.000 27.22746  ? 457 HOH A O   1 
HETATM 2934 O  O   . HOH W 8 .   ? -9.55260  0.96218  15.68342  1.000 30.80458  ? 458 HOH A O   1 
HETATM 2935 O  O   B HOH W 8 .   ? -1.34724  23.05912 -3.30227  0.300 25.63654  ? 459 HOH A O   1 
HETATM 2936 O  O   . HOH W 8 .   ? -12.87671 7.67006  16.82216  1.000 46.32814  ? 460 HOH A O   1 
HETATM 2937 O  O   . HOH W 8 .   ? -3.72788  6.21892  -0.12441  1.000 19.67127  ? 461 HOH A O   1 
HETATM 2938 O  O   . HOH W 8 .   ? -9.20445  12.14842 -18.16227 1.000 28.23445  ? 462 HOH A O   1 
HETATM 2939 O  O   . HOH W 8 .   ? 5.44270   6.30219  18.39431  1.000 58.98649  ? 463 HOH A O   1 
HETATM 2940 O  O   . HOH W 8 .   ? 7.61113   28.78842 20.50245  1.000 46.11755  ? 464 HOH A O   1 
HETATM 2941 O  O   . HOH W 8 .   ? -2.69377  16.45678 23.92521  1.000 29.73081  ? 465 HOH A O   1 
HETATM 2942 O  O   . HOH W 8 .   ? -5.62250  31.78789 23.70877  1.000 64.76223  ? 466 HOH A O   1 
HETATM 2943 O  O   B HOH W 8 .   ? 1.96798   25.40130 -0.20829  0.300 25.63654  ? 467 HOH A O   1 
HETATM 2944 O  O   . HOH W 8 .   ? -3.65408  9.87987  -21.97058 1.000 50.13862  ? 468 HOH A O   1 
HETATM 2945 O  O   B HOH W 8 .   ? 0.31309   22.85003 -1.21535  0.300 25.63654  ? 469 HOH A O   1 
HETATM 2946 O  O   . HOH W 8 .   ? 3.90190   27.09380 -23.32142 1.000 66.47672  ? 470 HOH A O   1 
HETATM 2947 O  O   . HOH W 8 .   ? -3.80905  29.03841 28.55811  1.000 57.90271  ? 471 HOH A O   1 
HETATM 2948 O  O   . HOH W 8 .   ? -7.89037  5.82534  22.82024  1.000 41.93681  ? 472 HOH A O   1 
HETATM 2949 O  O   A HOH W 8 .   ? -4.208    12.303   -24.296   0.700 38.27836  ? 473 HOH A O   1 
HETATM 2950 O  O   B HOH W 8 .   ? -5.844    13.030   -25.574   0.300 31.75170  ? 473 HOH A O   1 
HETATM 2951 O  O   . HOH W 8 .   ? -27.55674 16.63126 13.96469  1.000 59.49874  ? 474 HOH A O   1 
HETATM 2952 O  O   . HOH W 8 .   ? -13.38125 6.24677  -22.72589 1.000 40.94851  ? 475 HOH A O   1 
HETATM 2953 O  O   . HOH W 8 .   ? -3.90366  -1.30709 18.65723  1.000 43.43846  ? 476 HOH A O   1 
HETATM 2954 O  O   B HOH W 8 .   ? -2.36864  17.29338 5.24613   0.300 27.99238  ? 477 HOH A O   1 
HETATM 2955 O  O   . HOH W 8 .   ? -2.64620  13.64302 24.73419  1.000 44.84275  ? 478 HOH A O   1 
HETATM 2956 O  O   . HOH W 8 .   ? -5.40160  29.00179 -22.84287 1.000 45.95640  ? 479 HOH A O   1 
HETATM 2957 O  O   . HOH W 8 .   ? -20.91134 5.58870  13.64077  1.000 47.15328  ? 480 HOH A O   1 
HETATM 2958 O  O   . HOH W 8 .   ? -5.26670  19.14605 3.23207   1.000 36.78710  ? 481 HOH A O   1 
HETATM 2959 O  O   A HOH W 8 .   ? -6.07928  17.19588 4.95403   0.700 33.83448  ? 482 HOH A O   1 
HETATM 2960 O  O   B HOH W 8 .   ? -6.78370  17.22445 5.94674   0.300 29.95477  ? 482 HOH A O   1 
HETATM 2961 O  O   . HOH W 8 .   ? -15.21627 17.84451 22.00846  1.000 56.94934  ? 483 HOH A O   1 
HETATM 2962 O  O   . HOH W 8 .   ? 6.17727   11.91465 13.72146  1.000 60.54592  ? 484 HOH A O   1 
HETATM 2963 O  O   . HOH W 8 .   ? -7.61897  20.79270 -24.28628 1.000 21.65532  ? 485 HOH A O   1 
HETATM 2964 O  O   . HOH W 8 .   ? -8.67737  9.94062  -19.82457 1.000 28.64296  ? 486 HOH A O   1 
HETATM 2965 O  O   . HOH W 8 .   ? -24.22212 8.42419  12.48735  1.000 58.70922  ? 487 HOH A O   1 
HETATM 2966 O  O   . HOH W 8 .   ? -21.15960 21.90872 15.93641  1.000 28.85174  ? 488 HOH A O   1 
HETATM 2967 O  O   . HOH W 8 .   ? -22.66382 11.86512 17.41431  1.000 29.46169  ? 489 HOH A O   1 
HETATM 2968 O  O   . HOH W 8 .   ? -9.66231  27.08842 -21.52726 1.000 58.41174  ? 490 HOH A O   1 
HETATM 2969 O  O   . HOH W 8 .   ? 2.70593   1.69820  21.44716  1.000 63.16687  ? 491 HOH A O   1 
HETATM 2970 O  O   . HOH W 8 .   ? -5.38057  -1.10536 14.62895  1.000 24.20236  ? 492 HOH A O   1 
HETATM 2971 O  O   . HOH W 8 .   ? -16.42102 5.38614  -21.55550 1.000 38.67798  ? 493 HOH A O   1 
HETATM 2972 O  O   . HOH W 8 .   ? -2.42009  11.76176 -19.11869 1.000 26.42958  ? 494 HOH A O   1 
HETATM 2973 O  O   . HOH W 8 .   ? -4.27121  30.06846 26.14654  1.000 50.58709  ? 495 HOH A O   1 
HETATM 2974 O  O   . HOH W 8 .   ? -14.44840 21.05137 19.19656  1.000 41.47284  ? 496 HOH A O   1 
HETATM 2975 O  O   . HOH W 8 .   ? -22.35365 16.78512 19.32234  1.000 39.30086  ? 497 HOH A O   1 
HETATM 2976 O  O   . HOH W 8 .   ? -17.80941 6.36525  15.77098  1.000 68.74475  ? 498 HOH A O   1 
HETATM 2977 O  O   . HOH W 8 .   ? -13.25022 19.13452 22.84747  1.000 55.64905  ? 499 HOH A O   1 
HETATM 2978 O  O   A HOH W 8 .   ? 6.37502   28.46188 -18.18764 0.700 47.81864  ? 500 HOH A O   1 
HETATM 2979 O  O   . HOH W 8 .   ? 4.17534   24.75293 22.81630  1.000 38.55871  ? 501 HOH A O   1 
HETATM 2980 O  O   . HOH W 8 .   ? -8.10628  -0.37051 13.75088  1.000 25.17847  ? 502 HOH A O   1 
HETATM 2981 O  O   . HOH W 8 .   ? 5.00483   2.88253  22.38060  1.000 44.79839  ? 503 HOH A O   1 
HETATM 2982 O  O   . HOH W 8 .   ? -27.37937 15.22528 16.11286  1.000 57.57377  ? 504 HOH A O   1 
HETATM 2983 O  O   . HOH W 8 .   ? -7.874    15.808   -24.152   1.000 25.63654  ? 505 HOH A O   1 
HETATM 2984 O  O   . HOH W 8 .   ? -24.75659 21.20241 15.82456  1.000 28.79297  ? 506 HOH A O   1 
HETATM 2985 O  O   . HOH W 8 .   ? 4.83922   14.44880 16.90003  1.000 48.02765  ? 507 HOH A O   1 
HETATM 2986 O  O   . HOH W 8 .   ? 3.00550   8.38166  15.69742  1.000 25.43860  ? 508 HOH A O   1 
HETATM 2987 O  O   . HOH W 8 .   ? 4.649     32.058   -18.948   1.000 47.21142  ? 509 HOH A O   1 
HETATM 2988 O  O   . HOH W 8 .   ? -0.20964  10.09411 22.38785  1.000 31.29607  ? 510 HOH A O   1 
HETATM 2989 O  O   . HOH W 8 .   ? -7.79428  18.41906 27.58408  1.000 29.20558  ? 511 HOH A O   1 
HETATM 2990 O  O   A HOH W 8 .   ? -6.76773  11.40365 -21.09972 0.700 32.08489  ? 512 HOH A O   1 
HETATM 2991 O  O   B HOH W 8 .   ? -5.72403  11.43447 -21.65150 0.300 33.81759  ? 512 HOH A O   1 
HETATM 2992 O  O   . HOH W 8 .   ? -10.25700 28.54510 23.04785  1.000 56.79047  ? 513 HOH A O   1 
HETATM 2993 O  O   . HOH W 8 .   ? 2.22519   11.67246 21.79045  1.000 32.63910  ? 514 HOH A O   1 
HETATM 2994 O  O   . HOH W 8 .   ? -9.83194  22.13039 -23.07145 1.000 33.85878  ? 515 HOH A O   1 
HETATM 2995 O  O   . HOH W 8 .   ? -7.763    12.340   -23.318   1.000 54.56125  ? 516 HOH A O   1 
HETATM 2996 O  O   . HOH W 8 .   ? -5.10699  22.32626 28.00135  1.000 16.83456  ? 517 HOH A O   1 
HETATM 2997 O  O   A HOH W 8 .   ? -8.91175  17.85337 4.05995   0.700 41.71979  ? 518 HOH A O   1 
HETATM 2998 O  O   B HOH W 8 .   ? -7.63777  16.57405 3.71879   0.300 25.63654  ? 518 HOH A O   1 
HETATM 2999 O  O   B HOH W 8 .   ? -17.31984 17.50671 20.74880  0.300 35.88753  ? 519 HOH A O   1 
HETATM 3000 O  O   . HOH W 8 .   ? -12.80876 15.01922 -23.11605 1.000 45.31836  ? 520 HOH A O   1 
HETATM 3001 O  O   . HOH W 8 .   ? -9.77664  10.35100 23.04659  1.000 47.97268  ? 521 HOH A O   1 
HETATM 3002 O  O   . HOH W 8 .   ? -21.57377 9.62087  15.54502  1.000 38.25126  ? 522 HOH A O   1 
HETATM 3003 O  O   . HOH W 8 .   ? -10.59574 2.34224  -23.40132 1.000 62.08270  ? 523 HOH A O   1 
HETATM 3004 O  O   . HOH W 8 .   ? -2.94158  1.40013  21.51908  1.000 36.82949  ? 524 HOH A O   1 
HETATM 3005 O  O   . HOH W 8 .   ? 0.202     12.832   -27.904   1.000 52.14802  ? 525 HOH A O   1 
HETATM 3006 O  O   . HOH W 8 .   ? 0.16854   7.48587  23.21512  1.000 31.70141  ? 526 HOH A O   1 
HETATM 3007 O  O   . HOH W 8 .   ? -21.19397 21.14083 18.59869  1.000 54.96514  ? 527 HOH A O   1 
HETATM 3008 O  O   A HOH W 8 .   ? -1.65959  12.22073 -25.51448 0.700 38.44891  ? 528 HOH A O   1 
HETATM 3009 O  O   . HOH W 8 .   ? -1.25926  9.30661  -20.64445 1.000 48.91635  ? 529 HOH A O   1 
HETATM 3010 O  O   . HOH W 8 .   ? 4.62049   18.74535 16.34720  1.000 54.03429  ? 530 HOH A O   1 
HETATM 3011 O  O   . HOH W 8 .   ? -15.13091 10.08173 17.82389  1.000 52.32029  ? 531 HOH A O   1 
HETATM 3012 O  O   B HOH W 8 .   ? -17.09552 20.31919 17.67298  0.500 31.30875  ? 532 HOH A O   1 
HETATM 3013 O  O   . HOH W 8 .   ? -9.49411  -0.68880 18.10567  1.000 61.14314  ? 533 HOH A O   1 
HETATM 3014 O  O   B HOH W 8 .   ? -19.71629 16.49872 20.92608  0.300 43.08231  ? 534 HOH A O   1 
HETATM 3015 O  O   . HOH W 8 .   ? -20.35326 7.60413  15.95360  1.000 66.99335  ? 535 HOH A O   1 
HETATM 3016 O  O   . HOH W 8 .   ? -5.52906  3.96163  23.41690  1.000 49.10343  ? 536 HOH A O   1 
HETATM 3017 O  O   . HOH W 8 .   ? 3.97562   10.85605 17.37805  1.000 37.81937  ? 537 HOH A O   1 
HETATM 3018 O  O   . HOH W 8 .   ? -9.85161  -2.42211 12.62219  1.000 41.35394  ? 538 HOH A O   1 
HETATM 3019 O  O   . HOH W 8 .   ? -5.51850  -3.75015 15.45052  1.000 35.31874  ? 539 HOH A O   1 
HETATM 3020 O  O   . HOH W 8 .   ? -6.652    24.986   -25.453   1.000 40.58189  ? 540 HOH A O   1 
HETATM 3021 O  O   . HOH W 8 .   ? -21.74504 7.55348  12.16412  1.000 45.01577  ? 541 HOH A O   1 
HETATM 3022 O  O   . HOH W 8 .   ? 1.14786   35.72126 -22.60092 1.000 63.31416  ? 542 HOH A O   1 
HETATM 3023 O  O   . HOH W 8 .   ? -0.39661  34.07865 -16.20229 1.000 42.11506  ? 543 HOH A O   1 
HETATM 3024 O  O   . HOH W 8 .   ? -10.64639 7.34071  -22.65354 1.000 49.08645  ? 544 HOH A O   1 
HETATM 3025 O  O   . HOH W 8 .   ? 0.00000   -0.00000 21.27695  0.500 42.36726  ? 545 HOH A O   1 
HETATM 3026 O  O   . HOH W 8 .   ? 4.89401   16.04114 14.81141  1.000 33.92589  ? 546 HOH A O   1 
HETATM 3027 O  O   . HOH W 8 .   ? -10.59744 1.06395  19.61052  1.000 47.15835  ? 547 HOH A O   1 
HETATM 3028 O  O   . HOH W 8 .   ? -7.62814  5.22619  -26.29463 1.000 58.44861  ? 548 HOH A O   1 
HETATM 3029 O  O   . HOH W 8 .   ? -25.31759 11.09250 17.47180  1.000 50.87801  ? 549 HOH A O   1 
HETATM 3030 O  O   . HOH W 8 .   ? 7.39498   15.54263 13.71148  1.000 55.50917  ? 550 HOH A O   1 
HETATM 3031 O  O   . HOH W 8 .   ? -7.17062  1.25267  22.87038  1.000 55.66720  ? 551 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 
11   N N   A ASP A 2   ? 0.69271 0.57427 0.50085 -0.00790 0.00221  0.04096  2   ASP A N   
12   N N   B ASP A 2   ? 0.69589 0.57749 0.50414 -0.00801 0.00230  0.04097  2   ASP A N   
13   C CA  A ASP A 2   ? 0.70871 0.57793 0.51561 -0.01299 0.00447  0.04524  2   ASP A CA  
14   C CA  B ASP A 2   ? 0.70701 0.57678 0.51417 -0.01374 0.00528  0.04523  2   ASP A CA  
15   C C   A ASP A 2   ? 0.59075 0.46766 0.41989 -0.00841 -0.00372 0.04243  2   ASP A C   
16   C C   B ASP A 2   ? 0.58361 0.46089 0.41298 -0.00976 -0.00240 0.04261  2   ASP A C   
17   O O   A ASP A 2   ? 0.48438 0.36483 0.32571 -0.01476 0.00011  0.04262  2   ASP A O   
18   O O   B ASP A 2   ? 0.48840 0.36988 0.33015 -0.01650 0.00187  0.04269  2   ASP A O   
19   C CB  A ASP A 2   ? 0.73231 0.57213 0.50840 -0.01118 0.00332  0.05230  2   ASP A CB  
20   C CB  B ASP A 2   ? 0.73905 0.57947 0.51559 -0.01223 0.00442  0.05235  2   ASP A CB  
21   C CG  A ASP A 2   ? 0.99782 0.82633 0.75324 -0.02096 0.01617  0.05687  2   ASP A CG  
22   C CG  B ASP A 2   ? 0.98233 0.81220 0.73671 -0.02058 0.01641  0.05641  2   ASP A CG  
23   O OD1 A ASP A 2   ? 1.02139 0.86522 0.78891 -0.02989 0.02630  0.05413  2   ASP A OD1 
24   O OD1 B ASP A 2   ? 1.00301 0.84829 0.76875 -0.02921 0.02649  0.05357  2   ASP A OD1 
25   O OD2 A ASP A 2   ? 1.05508 0.85873 0.78225 -0.01971 0.01621  0.06307  2   ASP A OD2 
26   O OD2 B ASP A 2   ? 1.04666 0.85219 0.77228 -0.01857 0.01587  0.06233  2   ASP A OD2 
27   N N   A ASN A 3   ? 0.49714 0.37659 0.33189 0.00252  -0.01467 0.03936  3   ASN A N   
28   N N   B ASN A 3   ? 0.51910 0.39789 0.35365 0.00116  -0.01351 0.03983  3   ASN A N   
29   C CA  A ASN A 3   ? 0.53080 0.41659 0.38632 0.00677  -0.02152 0.03640  3   ASN A CA  
30   C CA  B ASN A 3   ? 0.50659 0.39230 0.36233 0.00499  -0.01999 0.03686  3   ASN A CA  
31   C C   A ASN A 3   ? 0.43007 0.34117 0.31307 0.00364  -0.01893 0.03117  3   ASN A C   
32   C C   B ASN A 3   ? 0.44182 0.35307 0.32459 0.00196  -0.01741 0.03155  3   ASN A C   
33   O O   A ASN A 3   ? 0.39052 0.30635 0.28883 0.00170  -0.01932 0.03008  3   ASN A O   
34   O O   B ASN A 3   ? 0.39745 0.31437 0.29631 0.00016  -0.01794 0.03021  3   ASN A O   
35   C CB  A ASN A 3   ? 0.56801 0.44763 0.42236 0.01933  -0.03377 0.03422  3   ASN A CB  
36   C CB  B ASN A 3   ? 0.57693 0.45595 0.43153 0.01745  -0.03226 0.03487  3   ASN A CB  
37   C CG  A ASN A 3   ? 0.69696 0.55000 0.52847 0.02318  -0.03870 0.03920  3   ASN A CG  
38   C CG  B ASN A 3   ? 0.68740 0.53958 0.51795 0.02104  -0.03674 0.04006  3   ASN A CG  
39   O OD1 A ASN A 3   ? 0.67320 0.51325 0.49642 0.01709  -0.03429 0.04384  3   ASN A OD1 
40   O OD1 B ASN A 3   ? 0.67644 0.51505 0.49597 0.01434  -0.03136 0.04512  3   ASN A OD1 
41   N ND2 A ASN A 3   ? 0.73955 0.58408 0.56120 0.03361  -0.04843 0.03800  3   ASN A ND2 
42   N ND2 B ASN A 3   ? 0.72182 0.56589 0.54463 0.03187  -0.04709 0.03860  3   ASN A ND2 
43   N N   A ILE A 4   ? 0.43614 0.36324 0.32555 0.00341  -0.01664 0.02774  4   ILE A N   
44   N N   B ILE A 4   ? 0.42968 0.35591 0.31733 0.00148  -0.01480 0.02840  4   ILE A N   
45   C CA  A ILE A 4   ? 0.36118 0.31091 0.27528 -0.00070 -0.01351 0.02345  4   ILE A CA  
46   C CA  B ILE A 4   ? 0.37673 0.32630 0.28920 -0.00200 -0.01212 0.02377  4   ILE A CA  
47   C C   A ILE A 4   ? 0.31897 0.26917 0.23526 -0.01183 -0.00476 0.02552  4   ILE A C   
48   C C   B ILE A 4   ? 0.32734 0.27930 0.24431 -0.01309 -0.00348 0.02533  4   ILE A C   
49   O O   A ILE A 4   ? 0.33945 0.29972 0.27346 -0.01464 -0.00452 0.02359  4   ILE A O   
50   O O   B ILE A 4   ? 0.32220 0.28493 0.25758 -0.01540 -0.00371 0.02317  4   ILE A O   
51   C CB  A ILE A 4   ? 0.36362 0.32985 0.28399 0.00022  -0.01198 0.01936  4   ILE A CB  
52   C CB  B ILE A 4   ? 0.34363 0.30785 0.25981 -0.00074 -0.01070 0.01998  4   ILE A CB  
53   C CG1 A ILE A 4   ? 0.48316 0.44807 0.40005 0.01136  -0.02076 0.01689  4   ILE A CG1 
54   C CG1 B ILE A 4   ? 0.46775 0.43064 0.38159 0.01080  -0.02012 0.01749  4   ILE A CG1 
55   C CG2 A ILE A 4   ? 0.32339 0.31181 0.27044 -0.00266 -0.01069 0.01498  4   ILE A CG2 
56   C CG2 B ILE A 4   ? 0.37800 0.36530 0.31993 -0.00434 -0.00842 0.01544  4   ILE A CG2 
57   C CD1 A ILE A 4   ? 0.46859 0.44797 0.38880 0.01210  -0.01884 0.01284  4   ILE A CD1 
58   C CD1 B ILE A 4   ? 0.47155 0.44777 0.38764 0.01249  -0.01902 0.01345  4   ILE A CD1 
59   N N   A ILE A 5   ? 0.34087 0.27996 0.23911 -0.01832 0.00270  0.02918  5   ILE A N   
60   N N   B ILE A 5   ? 0.37855 0.32006 0.27849 -0.02010 0.00439  0.02887  5   ILE A N   
61   C CA  A ILE A 5   ? 0.34926 0.28869 0.25053 -0.02918 0.01145  0.03048  5   ILE A CA  
62   C CA  B ILE A 5   ? 0.32653 0.26973 0.23119 -0.03086 0.01289  0.02974  5   ILE A CA  
63   C C   A ILE A 5   ? 0.34917 0.27807 0.25205 -0.02988 0.00896  0.03281  5   ILE A C   
64   C C   B ILE A 5   ? 0.37584 0.30709 0.28023 -0.03178 0.01074  0.03247  5   ILE A C   
65   O O   A ILE A 5   ? 0.32780 0.26641 0.24690 -0.03452 0.01057  0.03069  5   ILE A O   
66   O O   B ILE A 5   ? 0.33799 0.27504 0.25397 -0.03863 0.01463  0.03144  5   ILE A O   
67   C CB  A ILE A 5   ? 0.41254 0.34109 0.29394 -0.03604 0.02088  0.03375  5   ILE A CB  
68   C CB  B ILE A 5   ? 0.43654 0.37116 0.32347 -0.03813 0.02277  0.03240  5   ILE A CB  
69   C CG1 A ILE A 5   ? 0.47604 0.42130 0.36381 -0.03789 0.02530  0.02948  5   ILE A CG1 
70   C CG1 B ILE A 5   ? 0.47678 0.42449 0.36530 -0.03693 0.02484  0.02873  5   ILE A CG1 
71   C CG2 A ILE A 5   ? 0.45845 0.38172 0.34043 -0.04658 0.02931  0.03573  5   ILE A CG2 
72   C CG2 B ILE A 5   ? 0.43859 0.37642 0.33314 -0.04945 0.03193  0.03215  5   ILE A CG2 
73   C CD1 A ILE A 5   ? 0.65429 0.58912 0.52116 -0.04359 0.03491  0.03200  5   ILE A CD1 
74   C CD1 B ILE A 5   ? 0.64660 0.58583 0.51681 -0.04402 0.03553  0.03081  5   ILE A CD1 
75   N N   A MET A 6   ? 0.37496 0.28371 0.26118 -0.02494 0.00444  0.03683  6   MET A N   
76   N N   B MET A 6   ? 0.37447 0.28922 0.26659 -0.02469 0.00406  0.03539  6   MET A N   
77   C CA  A MET A 6   ? 0.35832 0.25613 0.24580 -0.02590 0.00249  0.03879  6   MET A CA  
78   C CA  B MET A 6   ? 0.36724 0.27053 0.25994 -0.02513 0.00171  0.03741  6   MET A CA  
79   C C   A MET A 6   ? 0.32152 0.23311 0.23154 -0.02252 -0.00291 0.03434  6   MET A C   
80   C C   B MET A 6   ? 0.34395 0.26129 0.25935 -0.02223 -0.00323 0.03301  6   MET A C   
81   O O   A MET A 6   ? 0.31933 0.23278 0.23860 -0.02758 -0.00070 0.03377  6   MET A O   
82   O O   B MET A 6   ? 0.29500 0.21473 0.21953 -0.02769 -0.00062 0.03244  6   MET A O   
83   C CB  A MET A 6   ? 0.39809 0.27251 0.26569 -0.01970 -0.00311 0.04316  6   MET A CB  
84   C CB  B MET A 6   ? 0.45451 0.33534 0.32786 -0.01830 -0.00431 0.04145  6   MET A CB  
85   C CG  A MET A 6   ? 0.50938 0.37431 0.38197 -0.01875 -0.00700 0.04383  6   MET A CG  
86   C CG  B MET A 6   ? 0.50540 0.37342 0.37957 -0.01853 -0.00691 0.04322  6   MET A CG  
87   S SD  A MET A 6   ? 0.68918 0.52782 0.54204 -0.00986 -0.01579 0.04782  6   MET A SD  
88   S SD  B MET A 6   ? 0.60365 0.44223 0.45301 -0.01219 -0.01304 0.04872  6   MET A SD  
89   C CE  A MET A 6   ? 0.59052 0.41179 0.41391 -0.01472 -0.00872 0.05445  6   MET A CE  
90   C CE  B MET A 6   ? 0.46069 0.29237 0.32103 -0.01305 -0.01576 0.04817  6   MET A CE  
91   N N   A THR A 7   ? 0.33242 0.25361 0.25143 -0.01412 -0.00966 0.03093  7   THR A N   
92   N N   B THR A 7   ? 0.33830 0.26474 0.26289 -0.01372 -0.01012 0.02966  7   THR A N   
93   C CA  A THR A 7   ? 0.27459 0.20866 0.21469 -0.01118 -0.01369 0.02679  7   THR A CA  
94   C CA  B THR A 7   ? 0.27086 0.21066 0.21666 -0.01133 -0.01363 0.02557  7   THR A CA  
95   C C   A THR A 7   ? 0.26582 0.21808 0.22161 -0.01822 -0.00847 0.02415  7   THR A C   
96   C C   B THR A 7   ? 0.25587 0.21434 0.21670 -0.01817 -0.00843 0.02292  7   THR A C   
97   O O   A THR A 7   ? 0.25462 0.21264 0.22333 -0.01949 -0.00926 0.02228  7   THR A O   
98   O O   B THR A 7   ? 0.26073 0.22760 0.23625 -0.01885 -0.00955 0.02057  7   THR A O   
99   C CB  A THR A 7   ? 0.27453 0.21496 0.22220 -0.00090 -0.02141 0.02338  7   THR A CB  
100  C CB  B THR A 7   ? 0.28184 0.22696 0.23512 -0.00089 -0.02151 0.02230  7   THR A CB  
101  O OG1 A THR A 7   ? 0.26237 0.21222 0.20818 0.00019  -0.02032 0.02210  7   THR A OG1 
102  O OG1 B THR A 7   ? 0.26051 0.22010 0.21861 -0.00009 -0.02047 0.01993  7   THR A OG1 
103  C CG2 A THR A 7   ? 0.30884 0.23114 0.24540 0.00701  -0.02858 0.02478  7   THR A CG2 
104  C CG2 B THR A 7   ? 0.34316 0.26989 0.28042 0.00638  -0.02749 0.02439  7   THR A CG2 
105  N N   A ALA A 8   ? 0.26794 0.22929 0.22297 -0.02249 -0.00347 0.02355  8   ALA A N   
106  N N   B ALA A 8   ? 0.27967 0.24423 0.23683 -0.02312 -0.00288 0.02299  8   ALA A N   
107  C CA  A ALA A 8   ? 0.25485 0.23258 0.22495 -0.02947 0.00109  0.02073  8   ALA A CA  
108  C CA  B ALA A 8   ? 0.26909 0.25026 0.24064 -0.03011 0.00191  0.02015  8   ALA A CA  
109  C C   A ALA A 8   ? 0.25817 0.22918 0.22641 -0.03782 0.00604  0.02233  8   ALA A C   
110  C C   B ALA A 8   ? 0.24169 0.21800 0.21400 -0.03813 0.00624  0.02126  8   ALA A C   
111  O O   A ALA A 8   ? 0.23458 0.21491 0.21652 -0.04097 0.00606  0.01990  8   ALA A O   
112  O O   B ALA A 8   ? 0.25015 0.23748 0.23724 -0.04079 0.00590  0.01853  8   ALA A O   
113  C CB  A ALA A 8   ? 0.24497 0.23373 0.21588 -0.03236 0.00557  0.01898  8   ALA A CB  
114  C CB  B ALA A 8   ? 0.28320 0.27090 0.25081 -0.03379 0.00741  0.01936  8   ALA A CB  
115  N N   A TYR A 9   ? 0.29239 0.24637 0.24331 -0.04127 0.01000  0.02639  9   TYR A N   
116  N N   B TYR A 9   ? 0.26696 0.22620 0.22305 -0.04193 0.01013  0.02520  9   TYR A N   
117  C CA  A TYR A 9   ? 0.32431 0.27053 0.27381 -0.04894 0.01456  0.02776  9   TYR A CA  
118  C CA  B TYR A 9   ? 0.26673 0.22005 0.22359 -0.04932 0.01408  0.02603  9   TYR A CA  
119  C C   A TYR A 9   ? 0.29211 0.23451 0.24793 -0.04611 0.00942  0.02721  9   TYR A C   
120  C C   B TYR A 9   ? 0.26019 0.20933 0.22256 -0.04568 0.00852  0.02561  9   TYR A C   
121  O O   A TYR A 9   ? 0.26174 0.20851 0.22667 -0.05149 0.01133  0.02538  9   TYR A O   
122  O O   B TYR A 9   ? 0.26587 0.21912 0.23731 -0.05044 0.00981  0.02378  9   TYR A O   
123  C CB  A TYR A 9   ? 0.30108 0.22763 0.22985 -0.05232 0.01953  0.03274  9   TYR A CB  
124  C CB  B TYR A 9   ? 0.29179 0.22658 0.22956 -0.05398 0.01988  0.03064  9   TYR A CB  
125  C CG  A TYR A 9   ? 0.33123 0.26030 0.25395 -0.05872 0.02797  0.03304  9   TYR A CG  
126  C CG  B TYR A 9   ? 0.29976 0.23841 0.23310 -0.06040 0.02813  0.03053  9   TYR A CG  
127  C CD1 A TYR A 9   ? 0.32764 0.27584 0.26627 -0.06385 0.03197  0.02838  9   TYR A CD1 
128  C CD1 B TYR A 9   ? 0.28841 0.24248 0.23698 -0.06776 0.03322  0.02636  9   TYR A CD1 
129  C CD2 A TYR A 9   ? 0.36720 0.27856 0.26800 -0.05982 0.03218  0.03786  9   TYR A CD2 
130  C CD2 B TYR A 9   ? 0.31984 0.24625 0.23362 -0.05905 0.03085  0.03420  9   TYR A CD2 
131  C CE1 A TYR A 9   ? 0.37035 0.32097 0.30468 -0.07017 0.04058  0.02787  9   TYR A CE1 
132  C CE1 B TYR A 9   ? 0.38798 0.34620 0.33453 -0.07392 0.04139  0.02534  9   TYR A CE1 
133  C CE2 A TYR A 9   ? 0.40191 0.31449 0.29615 -0.06630 0.04133  0.03801  9   TYR A CE2 
134  C CE2 B TYR A 9   ? 0.41251 0.34218 0.32196 -0.06543 0.03960  0.03371  9   TYR A CE2 
135  C CZ  A TYR A 9   ? 0.37980 0.31250 0.29169 -0.07155 0.04574  0.03269  9   TYR A CZ  
136  C CZ  B TYR A 9   ? 0.34350 0.28957 0.27042 -0.07301 0.04516  0.02901  9   TYR A CZ  
137  O OH  A TYR A 9   ? 0.43006 0.36455 0.33710 -0.07817 0.05538  0.03197  9   TYR A OH  
138  O OH  B TYR A 9   ? 0.44519 0.39516 0.36985 -0.07961 0.05442  0.02760  9   TYR A OH  
139  N N   A ILE A 10  ? 0.27671 0.21057 0.22790 -0.03771 0.00290  0.02827  10  ILE A N   
140  N N   B ILE A 10  ? 0.26249 0.20370 0.22008 -0.03717 0.00225  0.02667  10  ILE A N   
141  C CA  A ILE A 10  ? 0.27676 0.20818 0.23562 -0.03476 -0.00152 0.02683  10  ILE A CA  
142  C CA  B ILE A 10  ? 0.28391 0.21984 0.24655 -0.03387 -0.00223 0.02586  10  ILE A CA  
143  C C   A ILE A 10  ? 0.27611 0.22606 0.25342 -0.03504 -0.00259 0.02248  10  ILE A C   
144  C C   B ILE A 10  ? 0.27356 0.22611 0.25437 -0.03389 -0.00368 0.02164  10  ILE A C   
145  O O   A ILE A 10  ? 0.26650 0.21804 0.25067 -0.03853 -0.00193 0.02094  10  ILE A O   
146  O O   B ILE A 10  ? 0.26653 0.21828 0.25260 -0.03681 -0.00333 0.02044  10  ILE A O   
147  C CB  A ILE A 10  ? 0.31591 0.23669 0.26944 -0.02517 -0.00854 0.02756  10  ILE A CB  
148  C CB  B ILE A 10  ? 0.31471 0.23956 0.27069 -0.02442 -0.00887 0.02686  10  ILE A CB  
149  C CG1 A ILE A 10  ? 0.31303 0.21260 0.24674 -0.02479 -0.00843 0.03230  10  ILE A CG1 
150  C CG1 B ILE A 10  ? 0.32996 0.23470 0.26562 -0.02479 -0.00796 0.03168  10  ILE A CG1 
151  C CG2 A ILE A 10  ? 0.30603 0.22718 0.27074 -0.02213 -0.01233 0.02480  10  ILE A CG2 
152  C CG2 B ILE A 10  ? 0.30907 0.23118 0.27385 -0.02087 -0.01301 0.02468  10  ILE A CG2 
153  C CD1 A ILE A 10  ? 0.39734 0.28682 0.32542 -0.01437 -0.01662 0.03251  10  ILE A CD1 
154  C CD1 B ILE A 10  ? 0.40904 0.30166 0.33708 -0.01497 -0.01569 0.03245  10  ILE A CD1 
155  N N   A SER A 11  ? 0.24436 0.20812 0.22933 -0.03145 -0.00427 0.02043  11  SER A N   
156  N N   B SER A 11  ? 0.26178 0.22911 0.25175 -0.03070 -0.00529 0.01935  11  SER A N   
157  C CA  A SER A 11  ? 0.22787 0.20822 0.22970 -0.03100 -0.00580 0.01676  11  SER A CA  
158  C CA  B SER A 11  ? 0.20460 0.18743 0.21060 -0.03141 -0.00619 0.01591  11  SER A CA  
159  C C   A SER A 11  ? 0.22425 0.21284 0.23211 -0.03966 -0.00139 0.01541  11  SER A C   
160  C C   B SER A 11  ? 0.26584 0.25422 0.27552 -0.04040 -0.00163 0.01500  11  SER A C   
161  O O   A SER A 11  ? 0.23067 0.22550 0.24801 -0.04094 -0.00262 0.01325  11  SER A O   
162  O O   B SER A 11  ? 0.22219 0.21260 0.23810 -0.04261 -0.00223 0.01340  11  SER A O   
163  C CB  A SER A 11  ? 0.19790 0.19067 0.20708 -0.02532 -0.00855 0.01484  11  SER A CB  
164  C CB  B SER A 11  ? 0.27425 0.27138 0.28903 -0.02697 -0.00827 0.01386  11  SER A CB  
165  O OG  A SER A 11  ? 0.20005 0.20746 0.22525 -0.02441 -0.01030 0.01175  11  SER A OG  
166  O OG  B SER A 11  ? 0.29174 0.28771 0.29778 -0.02763 -0.00601 0.01516  11  SER A OG  
167  N N   A ILE A 12  ? 0.22910 0.21731 0.23144 -0.04562 0.00378  0.01633  12  ILE A N   
168  N N   B ILE A 12  ? 0.23795 0.22879 0.24406 -0.04560 0.00299  0.01551  12  ILE A N   
169  C CA  A ILE A 12  ? 0.28795 0.28335 0.29723 -0.05407 0.00797  0.01425  12  ILE A CA  
170  C CA  B ILE A 12  ? 0.26795 0.26524 0.27992 -0.05419 0.00734  0.01362  12  ILE A CA  
171  C C   A ILE A 12  ? 0.26023 0.24611 0.26751 -0.05779 0.00846  0.01458  12  ILE A C   
172  C C   B ILE A 12  ? 0.26628 0.25183 0.27348 -0.05888 0.00909  0.01451  12  ILE A C   
173  O O   A ILE A 12  ? 0.26628 0.25979 0.28330 -0.06103 0.00775  0.01165  12  ILE A O   
174  O O   B ILE A 12  ? 0.25648 0.24796 0.27184 -0.06403 0.00993  0.01179  12  ILE A O   
175  C CB  A ILE A 12  ? 0.27340 0.26841 0.27692 -0.05985 0.01454  0.01490  12  ILE A CB  
176  C CB  B ILE A 12  ? 0.23334 0.23395 0.24224 -0.05894 0.01306  0.01365  12  ILE A CB  
177  C CG1 A ILE A 12  ? 0.23419 0.24361 0.24467 -0.05726 0.01408  0.01270  12  ILE A CG1 
178  C CG1 B ILE A 12  ? 0.20402 0.21855 0.22026 -0.05459 0.01111  0.01165  12  ILE A CG1 
179  C CG2 A ILE A 12  ? 0.33704 0.33375 0.34556 -0.06929 0.01968  0.01296  12  ILE A CG2 
180  C CG2 B ILE A 12  ? 0.32138 0.32796 0.33797 -0.06808 0.01784  0.01089  12  ILE A CG2 
181  C CD1 A ILE A 12  ? 0.29440 0.30142 0.29610 -0.06127 0.02070  0.01356  12  ILE A CD1 
182  C CD1 B ILE A 12  ? 0.29262 0.30817 0.30295 -0.05812 0.01699  0.01178  12  ILE A CD1 
183  N N   . PHE A 13  ? 0.26940 0.23802 0.26376 -0.05700 0.00915  0.01797  13  PHE A N   
184  C CA  . PHE A 13  ? 0.28455 0.24254 0.27624 -0.06058 0.00997  0.01828  13  PHE A CA  
185  C C   . PHE A 13  ? 0.27291 0.23644 0.27403 -0.05761 0.00540  0.01542  13  PHE A C   
186  O O   . PHE A 13  ? 0.29256 0.25960 0.29959 -0.06238 0.00611  0.01285  13  PHE A O   
187  C CB  . PHE A 13  ? 0.28394 0.22256 0.26077 -0.05779 0.00972  0.02249  13  PHE A CB  
188  C CG  . PHE A 13  ? 0.34375 0.26973 0.31729 -0.06125 0.01067  0.02299  13  PHE A CG  
189  C CD1 . PHE A 13  ? 0.41382 0.33044 0.38064 -0.06858 0.01646  0.02483  13  PHE A CD1 
190  C CD2 . PHE A 13  ? 0.35135 0.27435 0.32880 -0.05724 0.00626  0.02137  13  PHE A CD2 
191  C CE1 . PHE A 13  ? 0.41041 0.31507 0.37498 -0.07177 0.01728  0.02505  13  PHE A CE1 
192  C CE2 . PHE A 13  ? 0.40254 0.31397 0.37744 -0.06048 0.00720  0.02130  13  PHE A CE2 
193  C CZ  . PHE A 13  ? 0.44156 0.34406 0.41030 -0.06763 0.01240  0.02315  13  PHE A CZ  
194  N N   A VAL A 14  ? 0.26014 0.22513 0.26321 -0.04975 0.00083  0.01537  14  VAL A N   
195  N N   B VAL A 14  ? 0.26040 0.22433 0.26288 -0.04973 0.00083  0.01549  14  VAL A N   
196  C CA  A VAL A 14  ? 0.28765 0.25672 0.29866 -0.04675 -0.00252 0.01281  14  VAL A CA  
197  C CA  B VAL A 14  ? 0.28816 0.25723 0.29916 -0.04687 -0.00247 0.01280  14  VAL A CA  
198  C C   A VAL A 14  ? 0.24699 0.23238 0.26922 -0.04895 -0.00302 0.00989  14  VAL A C   
199  C C   B VAL A 14  ? 0.24590 0.23075 0.26757 -0.05009 -0.00247 0.00991  14  VAL A C   
200  O O   A VAL A 14  ? 0.24338 0.23118 0.27012 -0.04965 -0.00440 0.00774  14  VAL A O   
201  O O   B VAL A 14  ? 0.21828 0.20476 0.24362 -0.05256 -0.00310 0.00774  14  VAL A O   
202  C CB  A VAL A 14  ? 0.30076 0.26644 0.31214 -0.03797 -0.00653 0.01309  14  VAL A CB  
203  C CB  B VAL A 14  ? 0.24382 0.21217 0.25677 -0.03801 -0.00657 0.01279  14  VAL A CB  
204  C CG1 A VAL A 14  ? 0.24311 0.20959 0.26112 -0.03561 -0.00843 0.01048  14  VAL A CG1 
205  C CG1 B VAL A 14  ? 0.24101 0.21514 0.26289 -0.03586 -0.00851 0.00997  14  VAL A CG1 
206  C CG2 A VAL A 14  ? 0.24819 0.19731 0.24787 -0.03556 -0.00703 0.01596  14  VAL A CG2 
207  C CG2 B VAL A 14  ? 0.23601 0.18738 0.23918 -0.03471 -0.00776 0.01490  14  VAL A CG2 
208  N N   . GLN A 15  ? 0.23456 0.23074 0.26100 -0.05007 -0.00207 0.00959  15  GLN A N   
209  C CA  . GLN A 15  ? 0.26303 0.27441 0.30083 -0.05219 -0.00320 0.00664  15  GLN A CA  
210  C C   . GLN A 15  ? 0.25476 0.26667 0.29432 -0.05982 -0.00134 0.00453  15  GLN A C   
211  O O   . GLN A 15  ? 0.25320 0.27127 0.29897 -0.06066 -0.00399 0.00200  15  GLN A O   
212  C CB  . GLN A 15  ? 0.24422 0.26697 0.28723 -0.05179 -0.00245 0.00619  15  GLN A CB  
213  C CG  . GLN A 15  ? 0.25916 0.28571 0.30461 -0.04371 -0.00555 0.00686  15  GLN A CG  
214  C CD  . GLN A 15  ? 0.28474 0.32094 0.33369 -0.04376 -0.00425 0.00620  15  GLN A CD  
215  O OE1 . GLN A 15  ? 0.26871 0.31668 0.32663 -0.04779 -0.00340 0.00371  15  GLN A OE1 
216  N NE2 . GLN A 15  ? 0.24561 0.27657 0.28739 -0.03935 -0.00422 0.00798  15  GLN A NE2 
217  N N   A ILE A 16  ? 0.25478 0.26004 0.28891 -0.06540 0.00315  0.00535  16  ILE A N   
218  N N   B ILE A 16  ? 0.26408 0.26890 0.29797 -0.06535 0.00311  0.00539  16  ILE A N   
219  C CA  A ILE A 16  ? 0.24876 0.25510 0.28653 -0.07300 0.00529  0.00258  16  ILE A CA  
220  C CA  B ILE A 16  ? 0.25879 0.26347 0.29557 -0.07275 0.00511  0.00277  16  ILE A CA  
221  C C   A ILE A 16  ? 0.22590 0.22442 0.26107 -0.07338 0.00329  0.00162  16  ILE A C   
222  C C   B ILE A 16  ? 0.27770 0.27663 0.31314 -0.07217 0.00228  0.00154  16  ILE A C   
223  O O   A ILE A 16  ? 0.31153 0.31583 0.35290 -0.07626 0.00125  -0.00195 16  ILE A O   
224  O O   B ILE A 16  ? 0.28004 0.28594 0.32201 -0.07432 -0.00020 -0.00192 16  ILE A O   
225  C CB  A ILE A 16  ? 0.29853 0.29786 0.33080 -0.07888 0.01168  0.00393  16  ILE A CB  
226  C CB  B ILE A 16  ? 0.31313 0.30769 0.34258 -0.07832 0.01122  0.00455  16  ILE A CB  
227  C CG1 A ILE A 16  ? 0.33763 0.34710 0.37421 -0.07977 0.01429  0.00344  16  ILE A CG1 
228  C CG1 B ILE A 16  ? 0.30855 0.31181 0.34202 -0.08144 0.01515  0.00386  16  ILE A CG1 
229  C CG2 A ILE A 16  ? 0.31517 0.31254 0.35115 -0.08649 0.01407  0.00090  16  ILE A CG2 
230  C CG2 B ILE A 16  ? 0.23364 0.22310 0.26444 -0.08476 0.01291  0.00218  16  ILE A CG2 
231  C CD1 A ILE A 16  ? 0.42455 0.42488 0.45245 -0.08477 0.02164  0.00567  16  ILE A CD1 
232  C CD1 B ILE A 16  ? 0.32660 0.31791 0.34913 -0.08523 0.02189  0.00706  16  ILE A CD1 
233  N N   A ILE A 17  ? 0.28599 0.27104 0.31199 -0.07029 0.00349  0.00436  17  ILE A N   
234  N N   B ILE A 17  ? 0.30265 0.28852 0.32942 -0.06895 0.00228  0.00403  17  ILE A N   
235  C CA  A ILE A 17  ? 0.35085 0.32837 0.37464 -0.07035 0.00191  0.00297  17  ILE A CA  
236  C CA  B ILE A 17  ? 0.31208 0.29097 0.33691 -0.06933 0.00082  0.00242  17  ILE A CA  
237  C C   A ILE A 17  ? 0.29862 0.28440 0.32776 -0.06654 -0.00238 0.00073  17  ILE A C   
238  C C   B ILE A 17  ? 0.30631 0.29211 0.33546 -0.06475 -0.00331 0.00069  17  ILE A C   
239  O O   A ILE A 17  ? 0.29153 0.27910 0.32272 -0.06922 -0.00387 -0.00235 17  ILE A O   
240  O O   B ILE A 17  ? 0.22171 0.20667 0.25113 -0.06632 -0.00475 -0.00195 17  ILE A O   
241  C CB  A ILE A 17  ? 0.32367 0.28549 0.33813 -0.06714 0.00259  0.00593  17  ILE A CB  
242  C CB  B ILE A 17  ? 0.38555 0.34806 0.40103 -0.06764 0.00223  0.00509  17  ILE A CB  
243  C CG1 A ILE A 17  ? 0.43629 0.38819 0.44345 -0.07105 0.00690  0.00885  17  ILE A CG1 
244  C CG1 B ILE A 17  ? 0.30446 0.26430 0.31808 -0.05947 -0.00044 0.00689  17  ILE A CG1 
245  C CG2 A ILE A 17  ? 0.37169 0.32609 0.38491 -0.06746 0.00141  0.00372  17  ILE A CG2 
246  C CG2 B ILE A 17  ? 0.41995 0.37511 0.42944 -0.07146 0.00649  0.00792  17  ILE A CG2 
247  C CD1 A ILE A 17  ? 0.46950 0.42246 0.47966 -0.07978 0.01078  0.00673  17  ILE A CD1 
248  C CD1 B ILE A 17  ? 0.40552 0.35877 0.41866 -0.05657 -0.00220 0.00516  17  ILE A CD1 
249  N N   A THR A 18  ? 0.24784 0.23847 0.27902 -0.06026 -0.00437 0.00214  18  THR A N   
250  N N   B THR A 18  ? 0.25482 0.24721 0.28710 -0.05917 -0.00506 0.00198  18  THR A N   
251  C CA  A THR A 18  ? 0.24710 0.24447 0.28283 -0.05635 -0.00764 0.00068  18  THR A CA  
252  C CA  B THR A 18  ? 0.24762 0.24661 0.28438 -0.05524 -0.00823 0.00063  18  THR A CA  
253  C C   A THR A 18  ? 0.22760 0.23641 0.26982 -0.05985 -0.00977 -0.00206 18  THR A C   
254  C C   B THR A 18  ? 0.25811 0.26938 0.30179 -0.05836 -0.01040 -0.00180 18  THR A C   
255  O O   A THR A 18  ? 0.25238 0.26194 0.29442 -0.05971 -0.01213 -0.00397 18  THR A O   
256  O O   B THR A 18  ? 0.25740 0.27186 0.30246 -0.05691 -0.01315 -0.00323 18  THR A O   
257  C CB  A THR A 18  ? 0.30051 0.30264 0.33962 -0.04964 -0.00889 0.00245  18  THR A CB  
258  C CB  B THR A 18  ? 0.29713 0.29915 0.33659 -0.04831 -0.00929 0.00245  18  THR A CB  
259  O OG1 A THR A 18  ? 0.30083 0.29193 0.33465 -0.04550 -0.00819 0.00420  18  THR A OG1 
260  O OG1 B THR A 18  ? 0.29018 0.30024 0.33323 -0.04876 -0.00885 0.00334  18  THR A OG1 
261  C CG2 A THR A 18  ? 0.26565 0.27499 0.31026 -0.04590 -0.01155 0.00128  18  THR A CG2 
262  C CG2 B THR A 18  ? 0.28224 0.27170 0.31578 -0.04456 -0.00839 0.00403  18  THR A CG2 
263  N N   . ALA A 19  ? 0.25848 0.27615 0.30645 -0.06267 -0.00920 -0.00253 19  ALA A N   
264  C CA  . ALA A 19  ? 0.22733 0.25636 0.28342 -0.06574 -0.01197 -0.00577 19  ALA A CA  
265  C C   . ALA A 19  ? 0.28005 0.30496 0.33437 -0.07087 -0.01270 -0.00895 19  ALA A C   
266  O O   . ALA A 19  ? 0.26661 0.29604 0.32319 -0.07083 -0.01697 -0.01149 19  ALA A O   
267  C CB  . ALA A 19  ? 0.23654 0.27462 0.29992 -0.06874 -0.01010 -0.00654 19  ALA A CB  
268  N N   . ILE A 20  ? 0.25493 0.27066 0.30481 -0.07513 -0.00887 -0.00890 20  ILE A N   
269  C CA  . ILE A 20  ? 0.26238 0.27381 0.31139 -0.08003 -0.00944 -0.01246 20  ILE A CA  
270  C C   . ILE A 20  ? 0.30727 0.31345 0.35010 -0.07676 -0.01253 -0.01312 20  ILE A C   
271  O O   . ILE A 20  ? 0.28809 0.29721 0.33191 -0.07821 -0.01632 -0.01670 20  ILE A O   
272  C CB  . ILE A 20  ? 0.25892 0.25956 0.30375 -0.08453 -0.00419 -0.01157 20  ILE A CB  
273  C CG1 . ILE A 20  ? 0.28757 0.29367 0.33847 -0.08905 -0.00035 -0.01176 20  ILE A CG1 
274  C CG2 . ILE A 20  ? 0.28795 0.28184 0.33106 -0.08869 -0.00477 -0.01527 20  ILE A CG2 
275  C CD1 . ILE A 20  ? 0.38848 0.38252 0.43293 -0.09240 0.00581  -0.00900 20  ILE A CD1 
276  N N   . ILE A 21  ? 0.28032 0.27829 0.31660 -0.07223 -0.01095 -0.01006 21  ILE A N   
277  C CA  . ILE A 21  ? 0.33791 0.33040 0.36844 -0.06901 -0.01248 -0.01077 21  ILE A CA  
278  C C   . ILE A 21  ? 0.31678 0.31806 0.34946 -0.06624 -0.01664 -0.01160 21  ILE A C   
279  O O   . ILE A 21  ? 0.30172 0.30115 0.33006 -0.06665 -0.01906 -0.01404 21  ILE A O   
280  C CB  . ILE A 21  ? 0.33087 0.31505 0.35739 -0.06404 -0.00997 -0.00771 21  ILE A CB  
281  C CG1 . ILE A 21  ? 0.36681 0.33919 0.38905 -0.06658 -0.00685 -0.00722 21  ILE A CG1 
282  C CG2 . ILE A 21  ? 0.46175 0.44269 0.48466 -0.06008 -0.01071 -0.00852 21  ILE A CG2 
283  C CD1 . ILE A 21  ? 0.44663 0.41141 0.46637 -0.06143 -0.00536 -0.00421 21  ILE A CD1 
284  N N   . SER A 22  ? 0.29559 0.30586 0.33429 -0.06325 -0.01761 -0.00959 22  SER A N   
285  C CA  . SER A 22  ? 0.26001 0.27778 0.30098 -0.06019 -0.02156 -0.00976 22  SER A CA  
286  C C   . SER A 22  ? 0.27896 0.30236 0.32214 -0.06393 -0.02619 -0.01341 22  SER A C   
287  O O   . SER A 22  ? 0.27774 0.30088 0.31669 -0.06234 -0.02986 -0.01435 22  SER A O   
288  C CB  . SER A 22  ? 0.32479 0.35166 0.37360 -0.05668 -0.02176 -0.00741 22  SER A CB  
289  O OG  . SER A 22  ? 0.33015 0.35142 0.37687 -0.05231 -0.01857 -0.00469 22  SER A OG  
290  N N   . VAL A 23  ? 0.24224 0.27012 0.29185 -0.06889 -0.02611 -0.01576 23  VAL A N   
291  C CA  . VAL A 23  ? 0.22568 0.25925 0.27959 -0.07240 -0.03111 -0.02034 23  VAL A CA  
292  C C   . VAL A 23  ? 0.24537 0.27028 0.29001 -0.07370 -0.03304 -0.02304 23  VAL A C   
293  O O   . VAL A 23  ? 0.26787 0.29472 0.31003 -0.07271 -0.03879 -0.02527 23  VAL A O   
294  C CB  . VAL A 23  ? 0.22988 0.26965 0.29424 -0.07792 -0.02943 -0.02307 23  VAL A CB  
295  C CG1 . VAL A 23  ? 0.35068 0.39504 0.42064 -0.08179 -0.03466 -0.02904 23  VAL A CG1 
296  C CG2 . VAL A 23  ? 0.27319 0.32347 0.34682 -0.07619 -0.02878 -0.02135 23  VAL A CG2 
297  N N   . TYR A 24  ? 0.24333 0.25814 0.28231 -0.07585 -0.02865 -0.02310 24  TYR A N   
298  C CA  . TYR A 24  ? 0.24272 0.24928 0.27289 -0.07696 -0.03017 -0.02614 24  TYR A CA  
299  C C   . TYR A 24  ? 0.24070 0.24360 0.26119 -0.07191 -0.03181 -0.02442 24  TYR A C   
300  O O   . TYR A 24  ? 0.28121 0.28153 0.29459 -0.07200 -0.03586 -0.02734 24  TYR A O   
301  C CB  . TYR A 24  ? 0.27257 0.26846 0.29898 -0.07942 -0.02477 -0.02608 24  TYR A CB  
302  C CG  . TYR A 24  ? 0.25544 0.25239 0.28910 -0.08563 -0.02364 -0.02926 24  TYR A CG  
303  C CD1 . TYR A 24  ? 0.26723 0.26734 0.30807 -0.08769 -0.01975 -0.02704 24  TYR A CD1 
304  C CD2 . TYR A 24  ? 0.26052 0.25514 0.29394 -0.08955 -0.02618 -0.03481 24  TYR A CD2 
305  C CE1 . TYR A 24  ? 0.24816 0.24868 0.29573 -0.09366 -0.01760 -0.02983 24  TYR A CE1 
306  C CE2 . TYR A 24  ? 0.28658 0.28230 0.32857 -0.09555 -0.02455 -0.03818 24  TYR A CE2 
307  C CZ  . TYR A 24  ? 0.28475 0.28335 0.33397 -0.09778 -0.01984 -0.03551 24  TYR A CZ  
308  O OH  . TYR A 24  ? 0.25924 0.25819 0.31699 -0.10415 -0.01707 -0.03883 24  TYR A OH  
309  N N   . GLY A 25  ? 0.25986 0.26208 0.27983 -0.06751 -0.02856 -0.01996 25  GLY A N   
310  C CA  . GLY A 25  ? 0.27407 0.27256 0.28618 -0.06287 -0.02861 -0.01811 25  GLY A CA  
311  C C   . GLY A 25  ? 0.28712 0.29110 0.29742 -0.06147 -0.03481 -0.01877 25  GLY A C   
312  O O   . GLY A 25  ? 0.31934 0.31727 0.31892 -0.05946 -0.03567 -0.01877 25  GLY A O   
313  N N   . LEU A 26  ? 0.28217 0.29706 0.30262 -0.06242 -0.03909 -0.01938 26  LEU A N   
314  C CA  . LEU A 26  ? 0.30626 0.32667 0.32657 -0.06072 -0.04613 -0.02008 26  LEU A CA  
315  C C   . LEU A 26  ? 0.35410 0.36958 0.36512 -0.06259 -0.05148 -0.02430 26  LEU A C   
316  O O   . LEU A 26  ? 0.33100 0.34662 0.33625 -0.06014 -0.05742 -0.02429 26  LEU A O   
317  C CB  . LEU A 26  ? 0.27197 0.30533 0.30734 -0.06220 -0.04970 -0.02142 26  LEU A CB  
318  C CG  . LEU A 26  ? 0.26811 0.30780 0.31279 -0.06006 -0.04559 -0.01778 26  LEU A CG  
319  C CD1 . LEU A 26  ? 0.42802 0.48058 0.48744 -0.06198 -0.04888 -0.02002 26  LEU A CD1 
320  C CD2 . LEU A 26  ? 0.37606 0.41409 0.41633 -0.05435 -0.04533 -0.01359 26  LEU A CD2 
321  N N   . PHE A 27  ? 0.29224 0.30294 0.30139 -0.06668 -0.04999 -0.02801 27  PHE A N   
322  C CA  . PHE A 27  ? 0.29083 0.29766 0.29274 -0.06873 -0.05556 -0.03315 27  PHE A CA  
323  C C   . PHE A 27  ? 0.34728 0.34130 0.33337 -0.06824 -0.05222 -0.03358 27  PHE A C   
324  O O   . PHE A 27  ? 0.37369 0.36320 0.35188 -0.06980 -0.05643 -0.03817 27  PHE A O   
325  C CB  . PHE A 27  ? 0.31994 0.33182 0.33347 -0.07416 -0.05706 -0.03845 27  PHE A CB  
326  C CG  . PHE A 27  ? 0.38168 0.40631 0.41101 -0.07504 -0.06037 -0.03926 27  PHE A CG  
327  C CD1 . PHE A 27  ? 0.45898 0.48986 0.49160 -0.07403 -0.06962 -0.04261 27  PHE A CD1 
328  C CD2 . PHE A 27  ? 0.30599 0.33597 0.34633 -0.07645 -0.05447 -0.03672 27  PHE A CD2 
329  C CE1 . PHE A 27  ? 0.42452 0.46773 0.47337 -0.07475 -0.07268 -0.04401 27  PHE A CE1 
330  C CE2 . PHE A 27  ? 0.39600 0.43804 0.45109 -0.07738 -0.05684 -0.03790 27  PHE A CE2 
331  C CZ  . PHE A 27  ? 0.39696 0.44604 0.45721 -0.07658 -0.06588 -0.04176 27  PHE A CZ  
332  N N   . ILE A 28  ? 0.32529 0.31350 0.30733 -0.06608 -0.04488 -0.02960 28  ILE A N   
333  C CA  . ILE A 28  ? 0.31078 0.28697 0.27868 -0.06551 -0.04095 -0.03044 28  ILE A CA  
334  C C   . ILE A 28  ? 0.33499 0.30698 0.28883 -0.06227 -0.04444 -0.02952 28  ILE A C   
335  O O   . ILE A 28  ? 0.34712 0.32266 0.30223 -0.05877 -0.04505 -0.02525 28  ILE A O   
336  C CB  . ILE A 28  ? 0.32507 0.29694 0.29508 -0.06377 -0.03243 -0.02697 28  ILE A CB  
337  C CG1 . ILE A 28  ? 0.33875 0.31204 0.31945 -0.06695 -0.02939 -0.02772 28  ILE A CG1 
338  C CG2 . ILE A 28  ? 0.32666 0.28666 0.28316 -0.06277 -0.02781 -0.02810 28  ILE A CG2 
339  C CD1 . ILE A 28  ? 0.36397 0.33325 0.34762 -0.06468 -0.02268 -0.02453 28  ILE A CD1 
340  N N   . PRO A 29  ? 0.39787 0.36219 0.33795 -0.06329 -0.04717 -0.03342 29  PRO A N   
341  C CA  . PRO A 29  ? 0.35412 0.31263 0.27790 -0.06020 -0.05066 -0.03223 29  PRO A CA  
342  C C   . PRO A 29  ? 0.42964 0.38057 0.34536 -0.05722 -0.04218 -0.02777 29  PRO A C   
343  O O   . PRO A 29  ? 0.40434 0.35084 0.32198 -0.05801 -0.03414 -0.02803 29  PRO A O   
344  C CB  . PRO A 29  ? 0.42843 0.37945 0.33916 -0.06242 -0.05436 -0.03825 29  PRO A CB  
345  C CG  . PRO A 29  ? 0.59120 0.54143 0.51004 -0.06628 -0.04931 -0.04175 29  PRO A CG  
346  C CD  . PRO A 29  ? 0.43805 0.39832 0.37662 -0.06732 -0.04741 -0.03927 29  PRO A CD  
347  N N   . LEU A 30  ? 0.38871 0.33804 0.29650 -0.05372 -0.04408 -0.02388 30  LEU A N   
348  C CA  . LEU A 30  ? 0.34701 0.29065 0.25028 -0.05076 -0.03592 -0.01932 30  LEU A CA  
349  C C   . LEU A 30  ? 0.39392 0.32570 0.27485 -0.04912 -0.03590 -0.01842 30  LEU A C   
350  O O   . LEU A 30  ? 0.41187 0.34304 0.28362 -0.04818 -0.04463 -0.01845 30  LEU A O   
351  C CB  . LEU A 30  ? 0.40607 0.35904 0.32253 -0.04778 -0.03700 -0.01433 30  LEU A CB  
352  C CG  . LEU A 30  ? 0.54726 0.51156 0.48452 -0.04882 -0.03631 -0.01436 30  LEU A CG  
353  C CD1 . LEU A 30  ? 0.58556 0.55911 0.53444 -0.04566 -0.03820 -0.01004 30  LEU A CD1 
354  C CD2 . LEU A 30  ? 0.39150 0.35120 0.33228 -0.04938 -0.02702 -0.01487 30  LEU A CD2 
355  N N   . ASN A 31  ? 0.37662 0.29851 0.24882 -0.04867 -0.02605 -0.01773 31  ASN A N   
356  C CA  . ASN A 31  ? 0.40171 0.31150 0.25288 -0.04692 -0.02342 -0.01557 31  ASN A CA  
357  C C   . ASN A 31  ? 0.37504 0.28776 0.22925 -0.04326 -0.02466 -0.00921 31  ASN A C   
358  O O   . ASN A 31  ? 0.38334 0.30631 0.25677 -0.04199 -0.02387 -0.00681 31  ASN A O   
359  C CB  . ASN A 31  ? 0.43615 0.33628 0.28235 -0.04759 -0.01067 -0.01666 31  ASN A CB  
360  C CG  . ASN A 31  ? 0.67112 0.56692 0.51361 -0.05108 -0.00856 -0.02320 31  ASN A CG  
361  O OD1 . ASN A 31  ? 0.83800 0.73588 0.69353 -0.05233 -0.00259 -0.02543 31  ASN A OD1 
362  N ND2 . ASN A 31  ? 0.51110 0.40052 0.33589 -0.05240 -0.01397 -0.02647 31  ASN A ND2 
363  N N   . PHE A 32  ? 0.44245 0.34505 0.27650 -0.04147 -0.02635 -0.00647 32  PHE A N   
364  C CA  . PHE A 32  ? 0.39012 0.29365 0.22491 -0.03794 -0.02820 -0.00024 32  PHE A CA  
365  C C   . PHE A 32  ? 0.39535 0.30382 0.24761 -0.03647 -0.01890 0.00292  32  PHE A C   
366  O O   . PHE A 32  ? 0.39146 0.30992 0.25908 -0.03423 -0.02243 0.00614  32  PHE A O   
367  C CB  . PHE A 32  ? 0.42443 0.31154 0.23148 -0.03663 -0.02688 0.00252  32  PHE A CB  
368  C CG  . PHE A 32  ? 0.44930 0.33352 0.25551 -0.03326 -0.02453 0.00949  32  PHE A CG  
369  C CD1 . PHE A 32  ? 0.48805 0.37765 0.29732 -0.03052 -0.03561 0.01287  32  PHE A CD1 
370  C CD2 . PHE A 32  ? 0.42415 0.30014 0.22766 -0.03291 -0.01111 0.01221  32  PHE A CD2 
371  C CE1 . PHE A 32  ? 0.48513 0.37171 0.29416 -0.02744 -0.03366 0.01923  32  PHE A CE1 
372  C CE2 . PHE A 32  ? 0.44597 0.31856 0.24903 -0.03002 -0.00841 0.01850  32  PHE A CE2 
373  C CZ  . PHE A 32  ? 0.48049 0.35837 0.28626 -0.02722 -0.01984 0.02230  32  PHE A CZ  
374  N N   . LYS A 33  ? 0.37693 0.27891 0.22842 -0.03759 -0.00718 0.00135  33  LYS A N   
375  C CA  . LYS A 33  ? 0.38220 0.28753 0.24955 -0.03567 0.00152  0.00386  33  LYS A CA  
376  C C   . LYS A 33  ? 0.35864 0.27923 0.25164 -0.03524 -0.00109 0.00287  33  LYS A C   
377  O O   . LYS A 33  ? 0.36003 0.28623 0.26827 -0.03278 0.00268  0.00528  33  LYS A O   
378  C CB  . LYS A 33  ? 0.43826 0.33294 0.30015 -0.03694 0.01459  0.00135  33  LYS A CB  
379  C CG  . LYS A 33  ? 0.55086 0.44682 0.41882 -0.03969 0.01714  -0.00465 33  LYS A CG  
380  C CD  . LYS A 33  ? 0.63074 0.51596 0.49451 -0.04050 0.03044  -0.00722 33  LYS A CD  
381  C CE  . LYS A 33  ? 0.80966 0.69288 0.67524 -0.04336 0.03334  -0.01363 33  LYS A CE  
382  N NZ  . LYS A 33  ? 0.66233 0.55768 0.54962 -0.04317 0.02883  -0.01509 33  LYS A NZ  
383  N N   . ASP A 34  ? 0.32308 0.25012 0.22081 -0.03755 -0.00748 -0.00068 34  ASP A N   
384  C CA  . ASP A 34  ? 0.29185 0.23089 0.21094 -0.03779 -0.00852 -0.00197 34  ASP A CA  
385  C C   . ASP A 34  ? 0.30556 0.25733 0.23564 -0.03727 -0.01842 -0.00059 34  ASP A C   
386  O O   . ASP A 34  ? 0.27198 0.23348 0.21835 -0.03775 -0.01940 -0.00156 34  ASP A O   
387  C CB  . ASP A 34  ? 0.29253 0.22952 0.21146 -0.04120 -0.00711 -0.00705 34  ASP A CB  
388  C CG  . ASP A 34  ? 0.37842 0.30418 0.29042 -0.04179 0.00311  -0.00944 34  ASP A CG  
389  O OD1 . ASP A 34  ? 0.37712 0.30136 0.29593 -0.03939 0.01061  -0.00780 34  ASP A OD1 
390  O OD2 . ASP A 34  ? 0.38058 0.29931 0.28131 -0.04460 0.00371  -0.01343 34  ASP A OD2 
391  N N   . ILE A 35  ? 0.32743 0.27893 0.24909 -0.03620 -0.02565 0.00149  35  ILE A N   
392  C CA  . ILE A 35  ? 0.33360 0.29719 0.26623 -0.03606 -0.03559 0.00152  35  ILE A CA  
393  C C   . ILE A 35  ? 0.27801 0.25341 0.23157 -0.03394 -0.03419 0.00377  35  ILE A C   
394  O O   . ILE A 35  ? 0.28437 0.27126 0.25198 -0.03505 -0.03887 0.00218  35  ILE A O   
395  C CB  . ILE A 35  ? 0.33963 0.29928 0.25933 -0.03438 -0.04364 0.00354  35  ILE A CB  
396  C CG1 . ILE A 35  ? 0.42891 0.37764 0.32763 -0.03644 -0.04673 0.00035  35  ILE A CG1 
397  C CG2 . ILE A 35  ? 0.47205 0.44495 0.40615 -0.03371 -0.05369 0.00331  35  ILE A CG2 
398  C CD1 . ILE A 35  ? 0.65562 0.59766 0.53787 -0.03423 -0.05521 0.00243  35  ILE A CD1 
399  N N   . ILE A 36  ? 0.25321 0.22602 0.20965 -0.03096 -0.02741 0.00709  36  ILE A N   
400  C CA  . ILE A 36  ? 0.22453 0.20851 0.20082 -0.02853 -0.02641 0.00873  36  ILE A CA  
401  C C   . ILE A 36  ? 0.25892 0.24975 0.24809 -0.03015 -0.02442 0.00582  36  ILE A C   
402  O O   . ILE A 36  ? 0.25528 0.25713 0.26007 -0.02895 -0.02623 0.00623  36  ILE A O   
403  C CB  . ILE A 36  ? 0.27044 0.24965 0.24829 -0.02510 -0.01894 0.01197  36  ILE A CB  
404  C CG1 . ILE A 36  ? 0.24790 0.23927 0.24557 -0.02193 -0.02022 0.01379  36  ILE A CG1 
405  C CG2 . ILE A 36  ? 0.25602 0.22680 0.23130 -0.02570 -0.00900 0.00998  36  ILE A CG2 
406  C CD1 . ILE A 36  ? 0.27202 0.25875 0.27231 -0.01851 -0.01333 0.01678  36  ILE A CD1 
407  N N   . LEU A 37  ? 0.25625 0.24009 0.23878 -0.03272 -0.02048 0.00294  37  LEU A N   
408  C CA  . LEU A 37  ? 0.26126 0.24989 0.25447 -0.03418 -0.01900 0.00069  37  LEU A CA  
409  C C   . LEU A 37  ? 0.25016 0.24900 0.25068 -0.03661 -0.02618 -0.00058 37  LEU A C   
410  O O   . LEU A 37  ? 0.24916 0.25545 0.26204 -0.03660 -0.02577 -0.00076 37  LEU A O   
411  C CB  . LEU A 37  ? 0.24615 0.22469 0.23059 -0.03669 -0.01426 -0.00239 37  LEU A CB  
412  C CG  . LEU A 37  ? 0.27677 0.24625 0.25818 -0.03446 -0.00569 -0.00221 37  LEU A CG  
413  C CD1 . LEU A 37  ? 0.31745 0.27695 0.29003 -0.03721 -0.00149 -0.00598 37  LEU A CD1 
414  C CD2 . LEU A 37  ? 0.34738 0.32205 0.34481 -0.03096 -0.00209 -0.00123 37  LEU A CD2 
415  N N   . ARG A 38  ? 0.27145 0.27021 0.26433 -0.03881 -0.03263 -0.00196 38  ARG A N   
416  C CA  . ARG A 38  ? 0.25645 0.26545 0.25838 -0.04128 -0.03923 -0.00399 38  ARG A CA  
417  C C   . ARG A 38  ? 0.25788 0.27817 0.27286 -0.03862 -0.04259 -0.00181 38  ARG A C   
418  O O   . ARG A 38  ? 0.25023 0.28051 0.27792 -0.04005 -0.04431 -0.00311 38  ARG A O   
419  C CB  . ARG A 38  ? 0.29631 0.30244 0.28819 -0.04378 -0.04610 -0.00691 38  ARG A CB  
420  C CG  . ARG A 38  ? 0.27838 0.29451 0.28112 -0.04716 -0.05212 -0.01054 38  ARG A CG  
421  C CD  . ARG A 38  ? 0.30053 0.31373 0.29429 -0.04887 -0.05982 -0.01411 38  ARG A CD  
422  N NE  . ARG A 38  ? 0.36290 0.36507 0.34301 -0.05106 -0.05717 -0.01654 38  ARG A NE  
423  C CZ  . ARG A 38  ? 0.55568 0.55018 0.52091 -0.05107 -0.06189 -0.01859 38  ARG A CZ  
424  N NH1 . ARG A 38  ? 0.53953 0.53461 0.49980 -0.04858 -0.06969 -0.01783 38  ARG A NH1 
425  N NH2 . ARG A 38  ? 0.50281 0.48824 0.45733 -0.05340 -0.05899 -0.02155 38  ARG A NH2 
426  N N   . GLU A 39  ? 0.22727 0.24573 0.23937 -0.03489 -0.04304 0.00141  39  GLU A N   
427  C CA  . GLU A 39  ? 0.26094 0.28975 0.28643 -0.03191 -0.04572 0.00349  39  GLU A CA  
428  C C   . GLU A 39  ? 0.25863 0.29377 0.29764 -0.03062 -0.04039 0.00391  39  GLU A C   
429  O O   . GLU A 39  ? 0.23125 0.27788 0.28387 -0.03048 -0.04298 0.00325  39  GLU A O   
430  C CB  . GLU A 39  ? 0.23986 0.26267 0.25817 -0.02819 -0.04571 0.00725  39  GLU A CB  
431  C CG  . GLU A 39  ? 0.28061 0.29599 0.28309 -0.02902 -0.05229 0.00704  39  GLU A CG  
432  C CD  . GLU A 39  ? 0.34378 0.35163 0.33701 -0.02549 -0.05251 0.01139  39  GLU A CD  
433  O OE1 . GLU A 39  ? 0.32448 0.32721 0.31706 -0.02342 -0.04452 0.01409  39  GLU A OE1 
434  O OE2 . GLU A 39  ? 0.38251 0.38892 0.36910 -0.02475 -0.06076 0.01194  39  GLU A OE2 
435  N N   . ILE A 40  ? 0.24057 0.26804 0.27592 -0.02954 -0.03313 0.00456  40  ILE A N   
436  C CA  . ILE A 40  ? 0.20407 0.23555 0.25037 -0.02795 -0.02872 0.00448  40  ILE A CA  
437  C C   . ILE A 40  ? 0.21535 0.25185 0.26606 -0.03148 -0.03011 0.00214  40  ILE A C   
438  O O   . ILE A 40  ? 0.20919 0.25451 0.27119 -0.03063 -0.03047 0.00210  40  ILE A O   
439  C CB  . ILE A 40  ? 0.18103 0.20185 0.22199 -0.02636 -0.02141 0.00460  40  ILE A CB  
440  C CG1 . ILE A 40  ? 0.21010 0.22738 0.25007 -0.02271 -0.01873 0.00701  40  ILE A CG1 
441  C CG2 . ILE A 40  ? 0.22531 0.24860 0.27596 -0.02480 -0.01814 0.00376  40  ILE A CG2 
442  C CD1 . ILE A 40  ? 0.26568 0.27162 0.29989 -0.02156 -0.01098 0.00654  40  ILE A CD1 
443  N N   . LEU A 41  ? 0.21144 0.24198 0.25312 -0.03558 -0.03053 0.00005  41  LEU A N   
444  C CA  . LEU A 41  ? 0.23052 0.26352 0.27571 -0.03924 -0.03026 -0.00196 41  LEU A CA  
445  C C   . LEU A 41  ? 0.19879 0.24397 0.25409 -0.04113 -0.03509 -0.00317 41  LEU A C   
446  O O   . LEU A 41  ? 0.22322 0.27353 0.28582 -0.04253 -0.03356 -0.00373 41  LEU A O   
447  C CB  . LEU A 41  ? 0.33111 0.35489 0.36539 -0.04327 -0.02967 -0.00432 41  LEU A CB  
448  C CG  . LEU A 41  ? 0.31007 0.33237 0.34589 -0.04716 -0.02764 -0.00607 41  LEU A CG  
449  C CD1 . LEU A 41  ? 0.27909 0.29944 0.31895 -0.04453 -0.02291 -0.00421 41  LEU A CD1 
450  C CD2 . LEU A 41  ? 0.32113 0.33344 0.34646 -0.05045 -0.02677 -0.00854 41  LEU A CD2 
451  N N   A ILE A 42  ? 0.20131 0.25097 0.25738 -0.04099 -0.04085 -0.00370 42  ILE A N   
452  N N   B ILE A 42  ? 0.20207 0.25125 0.25749 -0.04122 -0.04090 -0.00384 42  ILE A N   
453  C CA  A ILE A 42  ? 0.21306 0.27497 0.28106 -0.04278 -0.04552 -0.00578 42  ILE A CA  
454  C CA  B ILE A 42  ? 0.21599 0.27762 0.28344 -0.04247 -0.04589 -0.00563 42  ILE A CA  
455  C C   A ILE A 42  ? 0.23953 0.31088 0.31990 -0.03938 -0.04446 -0.00412 42  ILE A C   
456  C C   B ILE A 42  ? 0.24082 0.31114 0.32030 -0.03945 -0.04380 -0.00402 42  ILE A C   
457  O O   A ILE A 42  ? 0.20651 0.28751 0.29761 -0.04123 -0.04510 -0.00602 42  ILE A O   
458  O O   B ILE A 42  ? 0.19497 0.27288 0.28336 -0.04159 -0.04296 -0.00567 42  ILE A O   
459  C CB  A ILE A 42  ? 0.29363 0.35758 0.36004 -0.04340 -0.05326 -0.00758 42  ILE A CB  
460  C CB  B ILE A 42  ? 0.23499 0.29826 0.30057 -0.04147 -0.05326 -0.00615 42  ILE A CB  
461  C CG1 A ILE A 42  ? 0.27496 0.35213 0.35632 -0.04563 -0.05786 -0.01094 42  ILE A CG1 
462  C CG1 B ILE A 42  ? 0.24906 0.30633 0.30513 -0.04519 -0.05681 -0.00938 42  ILE A CG1 
463  C CG2 A ILE A 42  ? 0.27936 0.34029 0.34121 -0.03860 -0.05514 -0.00419 42  ILE A CG2 
464  C CG2 B ILE A 42  ? 0.23714 0.31423 0.31822 -0.04106 -0.05850 -0.00768 42  ILE A CG2 
465  C CD1 A ILE A 42  ? 0.43609 0.51755 0.52017 -0.04427 -0.06667 -0.01231 42  ILE A CD1 
466  C CD1 B ILE A 42  ? 0.40828 0.46425 0.45879 -0.04370 -0.06488 -0.00990 42  ILE A CD1 
467  N N   . LEU A 43  ? 0.19890 0.26774 0.27861 -0.03453 -0.04243 -0.00104 43  LEU A N   
468  C CA  . LEU A 43  ? 0.20375 0.28127 0.29570 -0.03110 -0.04116 -0.00004 43  LEU A CA  
469  C C   . LEU A 43  ? 0.25703 0.33362 0.35040 -0.03150 -0.03606 -0.00028 43  LEU A C   
470  O O   . LEU A 43  ? 0.21341 0.29886 0.31653 -0.03096 -0.03581 -0.00102 43  LEU A O   
471  C CB  . LEU A 43  ? 0.22719 0.30215 0.31952 -0.02588 -0.04016 0.00285  43  LEU A CB  
472  C CG  . LEU A 43  ? 0.21861 0.29519 0.31045 -0.02493 -0.04589 0.00372  43  LEU A CG  
473  C CD1 . LEU A 43  ? 0.27712 0.34673 0.36496 -0.02067 -0.04321 0.00703  43  LEU A CD1 
474  C CD2 . LEU A 43  ? 0.31417 0.40489 0.42135 -0.02444 -0.05085 0.00222  43  LEU A CD2 
475  N N   A GLU A 44  ? 0.21050 0.27594 0.29380 -0.03231 -0.03213 0.00019  44  GLU A N   
476  N N   B GLU A 44  ? 0.21277 0.27823 0.29604 -0.03236 -0.03218 0.00017  44  GLU A N   
477  C CA  A GLU A 44  ? 0.19950 0.26221 0.28259 -0.03257 -0.02815 0.00016  44  GLU A CA  
478  C CA  B GLU A 44  ? 0.20763 0.27035 0.29042 -0.03300 -0.02829 0.00002  44  GLU A CA  
479  C C   A GLU A 44  ? 0.19864 0.26553 0.28340 -0.03773 -0.02847 -0.00170 44  GLU A C   
480  C C   B GLU A 44  ? 0.19357 0.26205 0.27952 -0.03794 -0.02902 -0.00192 44  GLU A C   
481  O O   A GLU A 44  ? 0.19978 0.26830 0.28701 -0.03768 -0.02603 -0.00152 44  GLU A O   
482  O O   B GLU A 44  ? 0.19731 0.27079 0.28865 -0.03752 -0.02743 -0.00195 44  GLU A O   
483  C CB  A GLU A 44  ? 0.30619 0.35559 0.37890 -0.03244 -0.02449 0.00064  44  GLU A CB  
484  C CB  B GLU A 44  ? 0.28602 0.33535 0.35781 -0.03360 -0.02483 0.00032  44  GLU A CB  
485  C CG  A GLU A 44  ? 0.30361 0.34838 0.37625 -0.02740 -0.02236 0.00189  44  GLU A CG  
486  C CG  B GLU A 44  ? 0.26320 0.30661 0.33306 -0.02900 -0.02273 0.00157  44  GLU A CG  
487  C CD  A GLU A 44  ? 0.37833 0.42874 0.46123 -0.02235 -0.02154 0.00250  44  GLU A CD  
488  C CD  B GLU A 44  ? 0.29513 0.32603 0.35668 -0.02915 -0.01874 0.00110  44  GLU A CD  
489  O OE1 A GLU A 44  ? 0.49721 0.54869 0.58207 -0.02217 -0.02086 0.00216  44  GLU A OE1 
490  O OE1 B GLU A 44  ? 0.42042 0.44519 0.47350 -0.03331 -0.01867 -0.00007 44  GLU A OE1 
491  O OE2 A GLU A 44  ? 0.43542 0.48872 0.52406 -0.01850 -0.02160 0.00326  44  GLU A OE2 
492  O OE2 B GLU A 44  ? 0.41463 0.44201 0.47925 -0.02500 -0.01590 0.00136  44  GLU A OE2 
493  N N   A LEU A 45  ? 0.18863 0.25648 0.27165 -0.04221 -0.03124 -0.00374 45  LEU A N   
494  N N   B LEU A 45  ? 0.18888 0.25671 0.27176 -0.04266 -0.03128 -0.00393 45  LEU A N   
495  C CA  A LEU A 45  ? 0.19879 0.27130 0.28570 -0.04755 -0.03100 -0.00623 45  LEU A CA  
496  C CA  B LEU A 45  ? 0.19495 0.26775 0.28207 -0.04799 -0.03111 -0.00647 45  LEU A CA  
497  C C   A LEU A 45  ? 0.23210 0.31805 0.33186 -0.04706 -0.03255 -0.00743 45  LEU A C   
498  C C   B LEU A 45  ? 0.23723 0.32361 0.33734 -0.04749 -0.03281 -0.00772 45  LEU A C   
499  O O   A LEU A 45  ? 0.23073 0.32012 0.33406 -0.04967 -0.02954 -0.00840 45  LEU A O   
500  O O   B LEU A 45  ? 0.23961 0.33004 0.34391 -0.05057 -0.03010 -0.00906 45  LEU A O   
501  C CB  A LEU A 45  ? 0.20439 0.27515 0.28827 -0.05204 -0.03425 -0.00909 45  LEU A CB  
502  C CB  B LEU A 45  ? 0.20565 0.27658 0.28971 -0.05252 -0.03430 -0.00937 45  LEU A CB  
503  C CG  A LEU A 45  ? 0.25278 0.31121 0.32563 -0.05488 -0.03122 -0.00926 45  LEU A CG  
504  C CG  B LEU A 45  ? 0.19746 0.26943 0.28418 -0.05878 -0.03216 -0.01225 45  LEU A CG  
505  C CD1 A LEU A 45  ? 0.29999 0.35588 0.36856 -0.05770 -0.03539 -0.01218 45  LEU A CD1 
506  C CD1 B LEU A 45  ? 0.25581 0.31770 0.33470 -0.05968 -0.02606 -0.01009 45  LEU A CD1 
507  C CD2 A LEU A 45  ? 0.21861 0.27580 0.29278 -0.05918 -0.02682 -0.00994 45  LEU A CD2 
508  C CD2 B LEU A 45  ? 0.30368 0.37425 0.38907 -0.06298 -0.03593 -0.01607 45  LEU A CD2 
509  N N   . ILE A 46  ? 0.22369 0.31674 0.33014 -0.04381 -0.03698 -0.00741 46  ILE A N   
510  C CA  . ILE A 46  ? 0.24374 0.35003 0.36386 -0.04262 -0.03873 -0.00881 46  ILE A CA  
511  C C   . ILE A 46  ? 0.23941 0.34698 0.36144 -0.03959 -0.03439 -0.00723 46  ILE A C   
512  O O   . ILE A 46  ? 0.23363 0.34889 0.36265 -0.04129 -0.03272 -0.00906 46  ILE A O   
513  C CB  . ILE A 46  ? 0.24889 0.36024 0.37466 -0.03882 -0.04438 -0.00832 46  ILE A CB  
514  C CG1 . ILE A 46  ? 0.24054 0.35261 0.36601 -0.04192 -0.05020 -0.01087 46  ILE A CG1 
515  C CG2 . ILE A 46  ? 0.31447 0.43887 0.45502 -0.03641 -0.04571 -0.00946 46  ILE A CG2 
516  C CD1 . ILE A 46  ? 0.34256 0.45478 0.46818 -0.03787 -0.05605 -0.00928 46  ILE A CD1 
517  N N   . VAL A 47  ? 0.19595 0.29596 0.31209 -0.03494 -0.03259 -0.00430 47  VAL A N   
518  C CA  . VAL A 47  ? 0.19883 0.29791 0.31520 -0.03158 -0.02919 -0.00318 47  VAL A CA  
519  C C   . VAL A 47  ? 0.22130 0.31614 0.33144 -0.03584 -0.02540 -0.00363 47  VAL A C   
520  O O   . VAL A 47  ? 0.22237 0.32143 0.33524 -0.03528 -0.02346 -0.00408 47  VAL A O   
521  C CB  . VAL A 47  ? 0.15628 0.24620 0.26747 -0.02646 -0.02789 -0.00085 47  VAL A CB  
522  C CG1 . VAL A 47  ? 0.19853 0.28447 0.30772 -0.02313 -0.02506 -0.00021 47  VAL A CG1 
523  C CG2 . VAL A 47  ? 0.17947 0.27465 0.29876 -0.02188 -0.03044 -0.00028 47  VAL A CG2 
524  N N   A GLN A 48  ? 0.19792 0.28373 0.29905 -0.04019 -0.02406 -0.00354 48  GLN A N   
525  N N   B GLN A 48  ? 0.20147 0.28758 0.30284 -0.04032 -0.02415 -0.00363 48  GLN A N   
526  C CA  A GLN A 48  ? 0.23014 0.31031 0.32486 -0.04456 -0.01996 -0.00357 48  GLN A CA  
527  C CA  B GLN A 48  ? 0.23695 0.31684 0.33146 -0.04468 -0.02003 -0.00358 48  GLN A CA  
528  C C   A GLN A 48  ? 0.24949 0.33973 0.35199 -0.04922 -0.01887 -0.00631 48  GLN A C   
529  C C   B GLN A 48  ? 0.24567 0.33498 0.34741 -0.04974 -0.01879 -0.00634 48  GLN A C   
530  O O   A GLN A 48  ? 0.22046 0.30905 0.31984 -0.05105 -0.01471 -0.00598 48  GLN A O   
531  O O   B GLN A 48  ? 0.24419 0.33035 0.34169 -0.05237 -0.01439 -0.00600 48  GLN A O   
532  C CB  A GLN A 48  ? 0.26597 0.33491 0.35122 -0.04844 -0.01886 -0.00340 48  GLN A CB  
533  C CB  B GLN A 48  ? 0.26420 0.33268 0.34916 -0.04813 -0.01916 -0.00333 48  GLN A CB  
534  C CG  A GLN A 48  ? 0.26101 0.31741 0.33695 -0.04468 -0.01755 -0.00091 48  GLN A CG  
535  C CG  B GLN A 48  ? 0.18603 0.24438 0.26387 -0.04367 -0.01930 -0.00126 48  GLN A CG  
536  C CD  A GLN A 48  ? 0.33750 0.38179 0.40367 -0.04888 -0.01469 -0.00056 48  GLN A CD  
537  C CD  B GLN A 48  ? 0.35000 0.39838 0.41950 -0.04709 -0.01885 -0.00182 48  GLN A CD  
538  O OE1 A GLN A 48  ? 0.29877 0.33619 0.36012 -0.04975 -0.01529 -0.00103 48  GLN A OE1 
539  O OE1 B GLN A 48  ? 0.29605 0.33820 0.36051 -0.05152 -0.01636 -0.00217 48  GLN A OE1 
540  N NE2 A GLN A 48  ? 0.21824 0.25913 0.28087 -0.05154 -0.01131 0.00028  48  GLN A NE2 
541  N NE2 B GLN A 48  ? 0.26642 0.31277 0.33411 -0.04510 -0.02096 -0.00199 48  GLN A NE2 
542  N N   . ILE A 49  ? 0.21357 0.31377 0.32607 -0.05122 -0.02246 -0.00926 49  ILE A N   
543  C CA  . ILE A 49  ? 0.22772 0.33830 0.35009 -0.05580 -0.02124 -0.01292 49  ILE A CA  
544  C C   . ILE A 49  ? 0.21062 0.32855 0.33813 -0.05266 -0.01936 -0.01279 49  ILE A C   
545  O O   . ILE A 49  ? 0.22725 0.34657 0.35444 -0.05604 -0.01454 -0.01393 49  ILE A O   
546  C CB  . ILE A 49  ? 0.21518 0.33536 0.34895 -0.05741 -0.02689 -0.01663 49  ILE A CB  
547  C CG1 . ILE A 49  ? 0.27299 0.38541 0.40056 -0.06097 -0.02868 -0.01752 49  ILE A CG1 
548  C CG2 . ILE A 49  ? 0.28364 0.41638 0.43109 -0.06160 -0.02562 -0.02138 49  ILE A CG2 
549  C CD1 . ILE A 49  ? 0.32065 0.44028 0.45699 -0.06156 -0.03595 -0.02107 49  ILE A CD1 
550  N N   A ILE A 50  ? 0.21629 0.33838 0.34816 -0.04624 -0.02282 -0.01154 50  ILE A N   
551  N N   B ILE A 50  ? 0.21667 0.33850 0.34826 -0.04619 -0.02275 -0.01146 50  ILE A N   
552  C CA  A ILE A 50  ? 0.20508 0.33443 0.34247 -0.04252 -0.02174 -0.01191 50  ILE A CA  
553  C CA  B ILE A 50  ? 0.20603 0.33499 0.34299 -0.04244 -0.02165 -0.01179 50  ILE A CA  
554  C C   A ILE A 50  ? 0.23458 0.35400 0.35949 -0.04139 -0.01713 -0.00940 50  ILE A C   
555  C C   B ILE A 50  ? 0.23477 0.35382 0.35927 -0.04131 -0.01704 -0.00930 50  ILE A C   
556  O O   A ILE A 50  ? 0.20040 0.32263 0.32471 -0.04317 -0.01342 -0.01057 50  ILE A O   
557  O O   B ILE A 50  ? 0.19940 0.32264 0.32484 -0.04092 -0.01441 -0.01030 50  ILE A O   
558  C CB  A ILE A 50  ? 0.23844 0.37297 0.38342 -0.03568 -0.02634 -0.01108 50  ILE A CB  
559  C CB  B ILE A 50  ? 0.23883 0.37318 0.38362 -0.03565 -0.02630 -0.01103 50  ILE A CB  
560  C CG1 A ILE A 50  ? 0.24957 0.39035 0.40073 -0.03597 -0.03044 -0.01192 50  ILE A CG1 
561  C CG1 B ILE A 50  ? 0.24999 0.39031 0.40107 -0.03626 -0.03056 -0.01199 50  ILE A CG1 
562  C CG2 A ILE A 50  ? 0.20899 0.34925 0.35849 -0.03103 -0.02529 -0.01153 50  ILE A CG2 
563  C CG2 B ILE A 50  ? 0.21044 0.35190 0.36119 -0.03122 -0.02551 -0.01183 50  ILE A CG2 
564  C CD1 A ILE A 50  ? 0.19357 0.33140 0.34180 -0.03011 -0.03341 -0.00956 50  ILE A CD1 
565  C CD1 B ILE A 50  ? 0.33317 0.47839 0.48721 -0.03876 -0.02958 -0.01314 50  ILE A CD1 
566  N N   A GLU A 51  ? 0.19115 0.29819 0.30552 -0.03836 -0.01735 -0.00612 51  GLU A N   
567  N N   B GLU A 51  ? 0.18552 0.29079 0.29770 -0.04071 -0.01617 -0.00625 51  GLU A N   
568  C CA  A GLU A 51  ? 0.20108 0.29715 0.30324 -0.03648 -0.01430 -0.00369 51  GLU A CA  
569  C CA  B GLU A 51  ? 0.21521 0.30967 0.31499 -0.03946 -0.01271 -0.00383 51  GLU A CA  
570  C C   A GLU A 51  ? 0.18886 0.28040 0.28328 -0.04296 -0.00909 -0.00379 51  GLU A C   
571  C C   B GLU A 51  ? 0.15768 0.24811 0.25083 -0.04655 -0.00737 -0.00420 51  GLU A C   
572  O O   A GLU A 51  ? 0.20587 0.29512 0.29428 -0.04218 -0.00624 -0.00314 51  GLU A O   
573  O O   B GLU A 51  ? 0.16982 0.25670 0.25581 -0.04635 -0.00395 -0.00327 51  GLU A O   
574  C CB  A GLU A 51  ? 0.20766 0.29051 0.30088 -0.03371 -0.01526 -0.00100 51  GLU A CB  
575  C CB  B GLU A 51  ? 0.19808 0.27931 0.28867 -0.03603 -0.01384 -0.00098 51  GLU A CB  
576  C CG  A GLU A 51  ? 0.27820 0.34823 0.35848 -0.03203 -0.01291 0.00135  51  GLU A CG  
577  C CG  B GLU A 51  ? 0.25013 0.32585 0.33640 -0.02882 -0.01470 0.00061  51  GLU A CG  
578  C CD  A GLU A 51  ? 0.28032 0.33697 0.35269 -0.03023 -0.01351 0.00325  51  GLU A CD  
579  C CD  B GLU A 51  ? 0.24870 0.33539 0.34710 -0.02262 -0.01801 -0.00093 51  GLU A CD  
580  O OE1 A GLU A 51  ? 0.25954 0.31416 0.33222 -0.03325 -0.01380 0.00296  51  GLU A OE1 
581  O OE1 B GLU A 51  ? 0.34148 0.43735 0.45044 -0.02288 -0.02017 -0.00224 51  GLU A OE1 
582  O OE2 A GLU A 51  ? 0.30904 0.35685 0.37476 -0.02570 -0.01390 0.00466  51  GLU A OE2 
583  O OE2 B GLU A 51  ? 0.28359 0.36921 0.38096 -0.01721 -0.01880 -0.00093 51  GLU A OE2 
584  N N   A PHE A 52  ? 0.19875 0.28856 0.29307 -0.04946 -0.00767 -0.00480 52  PHE A N   
585  N N   B PHE A 52  ? 0.19458 0.28539 0.29013 -0.05286 -0.00652 -0.00583 52  PHE A N   
586  C CA  A PHE A 52  ? 0.19529 0.27961 0.28291 -0.05620 -0.00183 -0.00495 52  PHE A CA  
587  C CA  B PHE A 52  ? 0.24666 0.33414 0.33826 -0.06026 -0.00071 -0.00679 52  PHE A CA  
588  C C   A PHE A 52  ? 0.23155 0.32652 0.32601 -0.05886 0.00156  -0.00781 52  PHE A C   
589  C C   B PHE A 52  ? 0.21877 0.31713 0.31762 -0.06233 0.00256  -0.00964 52  PHE A C   
590  O O   A PHE A 52  ? 0.21340 0.30239 0.29867 -0.06131 0.00713  -0.00672 52  PHE A O   
591  O O   B PHE A 52  ? 0.21355 0.30631 0.30388 -0.06528 0.00856  -0.00875 52  PHE A O   
592  C CB  A PHE A 52  ? 0.25605 0.33811 0.34542 -0.06244 -0.00153 -0.00657 52  PHE A CB  
593  C CB  B PHE A 52  ? 0.16952 0.25815 0.26648 -0.06621 -0.00139 -0.00944 52  PHE A CB  
594  C CG  A PHE A 52  ? 0.25537 0.32960 0.33789 -0.06958 0.00498  -0.00654 52  PHE A CG  
595  C CG  B PHE A 52  ? 0.28955 0.36377 0.37540 -0.06749 -0.00098 -0.00701 52  PHE A CG  
596  C CD1 A PHE A 52  ? 0.33124 0.38937 0.39851 -0.06947 0.00793  -0.00251 52  PHE A CD1 
597  C CD1 B PHE A 52  ? 0.28805 0.34814 0.35985 -0.06742 0.00301  -0.00330 52  PHE A CD1 
598  C CD2 A PHE A 52  ? 0.28809 0.37066 0.38037 -0.07653 0.00824  -0.01084 52  PHE A CD2 
599  C CD2 B PHE A 52  ? 0.26683 0.34125 0.35603 -0.06868 -0.00492 -0.00868 52  PHE A CD2 
600  C CE1 A PHE A 52  ? 0.32049 0.37024 0.38114 -0.07628 0.01440  -0.00208 52  PHE A CE1 
601  C CE1 B PHE A 52  ? 0.21792 0.26502 0.28095 -0.06864 0.00322  -0.00153 52  PHE A CE1 
602  C CE2 A PHE A 52  ? 0.32497 0.39975 0.41174 -0.08363 0.01528  -0.01098 52  PHE A CE2 
603  C CE2 B PHE A 52  ? 0.28024 0.34196 0.35992 -0.06999 -0.00440 -0.00714 52  PHE A CE2 
604  C CZ  A PHE A 52  ? 0.31783 0.37585 0.38821 -0.08354 0.01852  -0.00627 52  PHE A CZ  
605  C CZ  B PHE A 52  ? 0.20146 0.24986 0.26892 -0.07009 -0.00020 -0.00368 52  PHE A CZ  
606  N N   A ILE A 53  ? 0.20683 0.31706 0.31703 -0.05834 -0.00161 -0.01156 53  ILE A N   
607  N N   B ILE A 53  ? 0.17857 0.29202 0.29288 -0.06094 -0.00112 -0.01319 53  ILE A N   
608  C CA  A ILE A 53  ? 0.23189 0.35362 0.35071 -0.06045 0.00145  -0.01513 53  ILE A CA  
609  C CA  B ILE A 53  ? 0.22287 0.34800 0.34612 -0.06263 0.00180  -0.01676 53  ILE A CA  
610  C C   A ILE A 53  ? 0.16803 0.28702 0.27844 -0.05560 0.00331  -0.01314 53  ILE A C   
611  C C   B ILE A 53  ? 0.20256 0.32445 0.31683 -0.05763 0.00368  -0.01443 53  ILE A C   
612  O O   A ILE A 53  ? 0.19822 0.31667 0.30378 -0.05886 0.00926  -0.01403 53  ILE A O   
613  O O   B ILE A 53  ? 0.21173 0.33244 0.32057 -0.06074 0.00977  -0.01512 53  ILE A O   
614  C CB  A ILE A 53  ? 0.19399 0.33223 0.33212 -0.05942 -0.00373 -0.01945 53  ILE A CB  
615  C CB  B ILE A 53  ? 0.24158 0.38311 0.38406 -0.06117 -0.00374 -0.02101 53  ILE A CB  
616  C CG1 A ILE A 53  ? 0.18954 0.33062 0.33560 -0.06568 -0.00465 -0.02272 53  ILE A CG1 
617  C CG1 B ILE A 53  ? 0.24458 0.38815 0.39459 -0.06569 -0.00667 -0.02360 53  ILE A CG1 
618  C CG2 A ILE A 53  ? 0.22630 0.37699 0.37411 -0.05972 -0.00120 -0.02327 53  ILE A CG2 
619  C CG2 B ILE A 53  ? 0.17582 0.32998 0.32903 -0.06319 -0.00041 -0.02553 53  ILE A CG2 
620  C CD1 A ILE A 53  ? 0.32977 0.48018 0.48923 -0.06246 -0.01214 -0.02476 53  ILE A CD1 
621  C CD1 B ILE A 53  ? 0.29324 0.44407 0.45433 -0.06103 -0.01393 -0.02454 53  ILE A CD1 
622  N N   A PHE A 54  ? 0.18064 0.29734 0.28891 -0.04775 -0.00157 -0.01075 54  PHE A N   
623  N N   B PHE A 54  ? 0.22466 0.34468 0.33712 -0.04980 -0.00140 -0.01198 54  PHE A N   
624  C CA  A PHE A 54  ? 0.18911 0.30291 0.28965 -0.04250 -0.00087 -0.00949 54  PHE A CA  
625  C CA  B PHE A 54  ? 0.20448 0.32143 0.30925 -0.04417 -0.00094 -0.01045 54  PHE A CA  
626  C C   A PHE A 54  ? 0.24611 0.34335 0.32676 -0.04446 0.00388  -0.00591 54  PHE A C   
627  C C   B PHE A 54  ? 0.24052 0.34136 0.32566 -0.04613 0.00404  -0.00697 54  PHE A C   
628  O O   A PHE A 54  ? 0.23727 0.33233 0.30961 -0.04409 0.00731  -0.00582 54  PHE A O   
629  O O   B PHE A 54  ? 0.15939 0.25895 0.23721 -0.04632 0.00788  -0.00716 54  PHE A O   
630  C CB  A PHE A 54  ? 0.21465 0.32821 0.31777 -0.03365 -0.00695 -0.00816 54  PHE A CB  
631  C CB  B PHE A 54  ? 0.19226 0.30847 0.29942 -0.03566 -0.00713 -0.00882 54  PHE A CB  
632  C CG  A PHE A 54  ? 0.23245 0.33927 0.32501 -0.02795 -0.00704 -0.00676 54  PHE A CG  
633  C CG  B PHE A 54  ? 0.18914 0.29964 0.28733 -0.02932 -0.00763 -0.00742 54  PHE A CG  
634  C CD1 A PHE A 54  ? 0.19660 0.31306 0.29426 -0.02495 -0.00712 -0.00960 54  PHE A CD1 
635  C CD1 B PHE A 54  ? 0.19499 0.31553 0.29904 -0.02639 -0.00774 -0.01026 54  PHE A CD1 
636  C CD2 A PHE A 54  ? 0.18995 0.28021 0.26687 -0.02581 -0.00713 -0.00300 54  PHE A CD2 
637  C CD2 B PHE A 54  ? 0.21923 0.31419 0.30343 -0.02613 -0.00842 -0.00378 54  PHE A CD2 
638  C CE1 A PHE A 54  ? 0.19733 0.30658 0.28365 -0.01946 -0.00782 -0.00863 54  PHE A CE1 
639  C CE1 B PHE A 54  ? 0.22422 0.33915 0.31941 -0.02015 -0.00899 -0.00950 54  PHE A CE1 
640  C CE2 A PHE A 54  ? 0.19433 0.27715 0.26055 -0.02032 -0.00815 -0.00191 54  PHE A CE2 
641  C CE2 B PHE A 54  ? 0.24170 0.33084 0.31772 -0.01980 -0.01000 -0.00299 54  PHE A CE2 
642  C CZ  A PHE A 54  ? 0.28452 0.37676 0.35490 -0.01706 -0.00862 -0.00474 54  PHE A CZ  
643  C CZ  B PHE A 54  ? 0.28809 0.38713 0.36917 -0.01671 -0.01045 -0.00585 54  PHE A CZ  
644  N N   A TYR A 55  ? 0.20534 0.28992 0.27731 -0.04614 0.00389  -0.00284 55  TYR A N   
645  N N   B TYR A 55  ? 0.22236 0.31016 0.29816 -0.04767 0.00410  -0.00379 55  TYR A N   
646  C CA  A TYR A 55  ? 0.21566 0.28307 0.26855 -0.04725 0.00761  0.00102  55  TYR A CA  
647  C CA  B TYR A 55  ? 0.21375 0.28474 0.27069 -0.04919 0.00822  -0.00004 55  TYR A CA  
648  C C   A TYR A 55  ? 0.21813 0.28331 0.26541 -0.05555 0.01564  0.00047  55  TYR A C   
649  C C   B TYR A 55  ? 0.26309 0.33314 0.31592 -0.05752 0.01622  -0.00104 55  TYR A C   
650  O O   A TYR A 55  ? 0.23922 0.29319 0.27059 -0.05575 0.01958  0.00315  55  TYR A O   
651  O O   B TYR A 55  ? 0.23957 0.29914 0.27708 -0.05810 0.02062  0.00143  55  TYR A O   
652  C CB  A TYR A 55  ? 0.25123 0.30545 0.29716 -0.04631 0.00528  0.00412  55  TYR A CB  
653  C CB  B TYR A 55  ? 0.19994 0.25799 0.25000 -0.04932 0.00650  0.00294  55  TYR A CB  
654  C CG  A TYR A 55  ? 0.17693 0.22744 0.22137 -0.03715 -0.00061 0.00544  55  TYR A CG  
655  C CG  B TYR A 55  ? 0.20126 0.25240 0.24678 -0.04076 0.00110  0.00513  55  TYR A CG  
656  C CD1 A TYR A 55  ? 0.32515 0.36308 0.35541 -0.03261 -0.00125 0.00813  55  TYR A CD1 
657  C CD1 B TYR A 55  ? 0.17897 0.21570 0.20886 -0.03729 0.00126  0.00834  55  TYR A CD1 
658  C CD2 A TYR A 55  ? 0.18819 0.24802 0.24601 -0.03281 -0.00555 0.00361  55  TYR A CD2 
659  C CD2 B TYR A 55  ? 0.20277 0.26144 0.25996 -0.03604 -0.00415 0.00371  55  TYR A CD2 
660  C CE1 A TYR A 55  ? 0.25723 0.29253 0.28839 -0.02406 -0.00691 0.00828  55  TYR A CE1 
661  C CE1 B TYR A 55  ? 0.18041 0.21127 0.20837 -0.02915 -0.00419 0.00934  55  TYR A CE1 
662  C CE2 A TYR A 55  ? 0.14445 0.20136 0.20294 -0.02465 -0.01014 0.00409  55  TYR A CE2 
663  C CE2 B TYR A 55  ? 0.14861 0.20145 0.20382 -0.02849 -0.00837 0.00488  55  TYR A CE2 
664  C CZ  A TYR A 55  ? 0.23420 0.27932 0.28024 -0.02023 -0.01096 0.00603  55  TYR A CZ  
665  C CZ  B TYR A 55  ? 0.20776 0.24721 0.24935 -0.02497 -0.00860 0.00731  55  TYR A CZ  
666  O OH  A TYR A 55  ? 0.23825 0.28051 0.28652 -0.01187 -0.01587 0.00560  55  TYR A OH  
667  O OH  B TYR A 55  ? 0.23993 0.27411 0.28189 -0.01722 -0.01329 0.00749  55  TYR A OH  
668  N N   A ILE A 56  ? 0.23955 0.31434 0.29932 -0.06244 0.01825  -0.00311 56  ILE A N   
669  N N   B ILE A 56  ? 0.22931 0.30921 0.29527 -0.06406 0.01827  -0.00478 56  ILE A N   
670  C CA  A ILE A 56  ? 0.26739 0.34208 0.32519 -0.07067 0.02680  -0.00484 56  ILE A CA  
671  C CA  B ILE A 56  ? 0.22382 0.30459 0.28931 -0.07239 0.02666  -0.00694 56  ILE A CA  
672  C C   A ILE A 56  ? 0.19462 0.27779 0.25353 -0.06946 0.02973  -0.00717 56  ILE A C   
673  C C   B ILE A 56  ? 0.19926 0.28715 0.26443 -0.07114 0.02992  -0.00886 56  ILE A C   
674  O O   A ILE A 56  ? 0.23666 0.31181 0.28237 -0.07264 0.03685  -0.00587 56  ILE A O   
675  O O   B ILE A 56  ? 0.27827 0.35771 0.33019 -0.07458 0.03725  -0.00748 56  ILE A O   
676  C CB  A ILE A 56  ? 0.24988 0.33383 0.32354 -0.07790 0.02810  -0.00933 56  ILE A CB  
677  C CB  B ILE A 56  ? 0.24407 0.33602 0.32726 -0.07885 0.02697  -0.01196 56  ILE A CB  
678  C CG1 A ILE A 56  ? 0.30947 0.38352 0.37967 -0.07915 0.02554  -0.00715 56  ILE A CG1 
679  C CG1 B ILE A 56  ? 0.23823 0.31963 0.31729 -0.08188 0.02617  -0.01011 56  ILE A CG1 
680  C CG2 A ILE A 56  ? 0.33230 0.41694 0.40649 -0.08674 0.03786  -0.01208 56  ILE A CG2 
681  C CG2 B ILE A 56  ? 0.30024 0.39780 0.38866 -0.08678 0.03561  -0.01609 56  ILE A CG2 
682  C CD1 A ILE A 56  ? 0.37156 0.42544 0.42161 -0.07992 0.02933  -0.00171 56  ILE A CD1 
683  C CD1 B ILE A 56  ? 0.24764 0.33985 0.34385 -0.08509 0.02247  -0.01487 56  ILE A CD1 
684  N N   A TRP A 57  ? 0.21346 0.31233 0.28757 -0.06487 0.02449  -0.01066 57  TRP A N   
685  N N   B TRP A 57  ? 0.22663 0.32946 0.30571 -0.06614 0.02468  -0.01205 57  TRP A N   
686  C CA  A TRP A 57  ? 0.19508 0.30215 0.27047 -0.06230 0.02610  -0.01312 57  TRP A CA  
687  C CA  B TRP A 57  ? 0.24190 0.35199 0.32114 -0.06394 0.02689  -0.01432 57  TRP A CA  
688  C C   A TRP A 57  ? 0.26042 0.35309 0.31415 -0.05731 0.02679  -0.00869 57  TRP A C   
689  C C   B TRP A 57  ? 0.25541 0.35155 0.31374 -0.05815 0.02670  -0.00972 57  TRP A C   
690  O O   A TRP A 57  ? 0.24415 0.33374 0.28745 -0.05945 0.03298  -0.00904 57  TRP A O   
691  O O   B TRP A 57  ? 0.26034 0.35487 0.30938 -0.05885 0.03174  -0.01031 57  TRP A O   
692  C CB  A TRP A 57  ? 0.18531 0.30889 0.27930 -0.05632 0.01866  -0.01653 57  TRP A CB  
693  C CB  B TRP A 57  ? 0.21126 0.33945 0.31053 -0.05901 0.02030  -0.01848 57  TRP A CB  
694  C CG  A TRP A 57  ? 0.18780 0.32012 0.28401 -0.05297 0.01960  -0.01947 57  TRP A CG  
695  C CG  B TRP A 57  ? 0.22459 0.35999 0.32425 -0.05515 0.02111  -0.02085 57  TRP A CG  
696  C CD1 A TRP A 57  ? 0.32969 0.47521 0.43729 -0.05727 0.02411  -0.02502 57  TRP A CD1 
697  C CD1 B TRP A 57  ? 0.26351 0.41141 0.37318 -0.05901 0.02585  -0.02632 57  TRP A CD1 
698  C CD2 A TRP A 57  ? 0.24420 0.37253 0.33130 -0.04462 0.01595  -0.01768 57  TRP A CD2 
699  C CD2 B TRP A 57  ? 0.18658 0.31705 0.27649 -0.04658 0.01705  -0.01850 57  TRP A CD2 
700  N NE1 A TRP A 57  ? 0.27150 0.42156 0.37690 -0.05210 0.02364  -0.02664 57  TRP A NE1 
701  N NE1 B TRP A 57  ? 0.28950 0.44055 0.39533 -0.05332 0.02503  -0.02735 57  TRP A NE1 
702  C CE2 A TRP A 57  ? 0.30081 0.44040 0.39351 -0.04418 0.01839  -0.02221 57  TRP A CE2 
703  C CE2 B TRP A 57  ? 0.28560 0.42603 0.37934 -0.04550 0.01934  -0.02264 57  TRP A CE2 
704  C CE3 A TRP A 57  ? 0.25063 0.36730 0.32661 -0.03731 0.01059  -0.01338 57  TRP A CE3 
705  C CE3 B TRP A 57  ? 0.21526 0.33414 0.29475 -0.03959 0.01152  -0.01398 57  TRP A CE3 
706  C CZ2 A TRP A 57  ? 0.29912 0.43843 0.38572 -0.03653 0.01532  -0.02246 57  TRP A CZ2 
707  C CZ2 B TRP A 57  ? 0.29138 0.43035 0.37815 -0.03748 0.01582  -0.02233 57  TRP A CZ2 
708  C CZ3 A TRP A 57  ? 0.29358 0.41010 0.36461 -0.02959 0.00729  -0.01383 57  TRP A CZ3 
709  C CZ3 B TRP A 57  ? 0.29601 0.41352 0.36971 -0.03166 0.00799  -0.01386 57  TRP A CZ3 
710  C CH2 A TRP A 57  ? 0.27837 0.40605 0.35428 -0.02919 0.00951  -0.01827 57  TRP A CH2 
711  C CH2 B TRP A 57  ? 0.28230 0.40975 0.35936 -0.03054 0.00989  -0.01796 57  TRP A CH2 
712  N N   A LEU A 58  ? 0.23037 0.31353 0.27687 -0.05055 0.02039  -0.00478 58  LEU A N   
713  N N   B LEU A 58  ? 0.22800 0.31365 0.27861 -0.05230 0.02081  -0.00551 58  LEU A N   
714  C CA  A LEU A 58  ? 0.22374 0.29366 0.25152 -0.04433 0.01884  -0.00121 58  LEU A CA  
715  C CA  B LEU A 58  ? 0.24769 0.32010 0.28004 -0.04578 0.01890  -0.00176 58  LEU A CA  
716  C C   A LEU A 58  ? 0.26360 0.31610 0.26959 -0.04955 0.02622  0.00263  58  LEU A C   
717  C C   B LEU A 58  ? 0.28093 0.33549 0.29138 -0.05065 0.02594  0.00221  58  LEU A C   
718  O O   A LEU A 58  ? 0.28098 0.32777 0.27265 -0.04824 0.02922  0.00340  58  LEU A O   
719  O O   B LEU A 58  ? 0.29247 0.33963 0.28742 -0.04838 0.02804  0.00359  58  LEU A O   
720  C CB  A LEU A 58  ? 0.25305 0.31558 0.27957 -0.03704 0.01097  0.00157  58  LEU A CB  
721  C CB  B LEU A 58  ? 0.26933 0.33578 0.30192 -0.03847 0.01086  0.00075  58  LEU A CB  
722  C CG  A LEU A 58  ? 0.22903 0.27662 0.23710 -0.03007 0.00799  0.00485  58  LEU A CG  
723  C CG  B LEU A 58  ? 0.27378 0.32930 0.29291 -0.02975 0.00623  0.00318  58  LEU A CG  
724  C CD1 A LEU A 58  ? 0.23138 0.28782 0.24210 -0.02349 0.00497  0.00176  58  LEU A CD1 
725  C CD1 B LEU A 58  ? 0.21782 0.28495 0.24306 -0.02397 0.00361  -0.00044 58  LEU A CD1 
726  C CD2 A LEU A 58  ? 0.23151 0.26942 0.23839 -0.02455 0.00156  0.00735  58  LEU A CD2 
727  C CD2 B LEU A 58  ? 0.19311 0.24260 0.21503 -0.02402 -0.00048 0.00489  58  LEU A CD2 
728  N N   A ILE A 59  ? 0.28363 0.32641 0.28581 -0.05524 0.02910  0.00522  59  ILE A N   
729  N N   B ILE A 59  ? 0.25152 0.29820 0.25974 -0.05729 0.02962  0.00411  59  ILE A N   
730  C CA  A ILE A 59  ? 0.34632 0.37032 0.32703 -0.05979 0.03591  0.00960  59  ILE A CA  
731  C CA  B ILE A 59  ? 0.29051 0.31892 0.27805 -0.06218 0.03672  0.00830  59  ILE A CA  
732  C C   A ILE A 59  ? 0.36908 0.39695 0.34739 -0.06718 0.04594  0.00724  59  ILE A C   
733  C C   B ILE A 59  ? 0.36201 0.39414 0.34643 -0.06872 0.04631  0.00596  59  ILE A C   
734  O O   A ILE A 59  ? 0.38882 0.40300 0.34637 -0.06814 0.05124  0.01042  59  ILE A O   
735  O O   B ILE A 59  ? 0.39924 0.41670 0.36260 -0.06997 0.05175  0.00945  59  ILE A O   
736  C CB  A ILE A 59  ? 0.37582 0.38762 0.35310 -0.06411 0.03689  0.01277  59  ILE A CB  
737  C CB  B ILE A 59  ? 0.26790 0.28688 0.25492 -0.06777 0.03851  0.01050  59  ILE A CB  
738  C CG1 A ILE A 59  ? 0.34901 0.37344 0.34579 -0.07149 0.03942  0.00859  59  ILE A CG1 
739  C CG1 B ILE A 59  ? 0.28857 0.32118 0.29437 -0.07616 0.04283  0.00557  59  ILE A CG1 
740  C CG2 A ILE A 59  ? 0.34966 0.35326 0.32400 -0.05621 0.02791  0.01562  59  ILE A CG2 
741  C CG2 B ILE A 59  ? 0.29742 0.31212 0.28650 -0.06118 0.02964  0.01245  59  ILE A CG2 
742  C CD1 A ILE A 59  ? 0.38519 0.39670 0.37667 -0.07777 0.04305  0.01106  59  ILE A CD1 
743  C CD1 B ILE A 59  ? 0.39016 0.41555 0.39807 -0.08105 0.04335  0.00661  59  ILE A CD1 
744  N N   A ILE A 60  ? 0.29536 0.34141 0.29448 -0.07229 0.04866  0.00142  60  ILE A N   
745  N N   B ILE A 60  ? 0.28068 0.33182 0.28555 -0.07283 0.04854  -0.00011 60  ILE A N   
746  C CA  A ILE A 60  ? 0.30947 0.36187 0.30976 -0.07884 0.05817  -0.00228 60  ILE A CA  
747  C CA  B ILE A 60  ? 0.32164 0.37785 0.32641 -0.07953 0.05836  -0.00354 60  ILE A CA  
748  C C   A ILE A 60  ? 0.43294 0.48827 0.42520 -0.07277 0.05711  -0.00317 60  ILE A C   
749  C C   B ILE A 60  ? 0.42599 0.48442 0.42191 -0.07365 0.05764  -0.00423 60  ILE A C   
750  O O   A ILE A 60  ? 0.43799 0.48376 0.41231 -0.07527 0.06462  -0.00176 60  ILE A O   
751  O O   B ILE A 60  ? 0.45306 0.50410 0.43367 -0.07712 0.06599  -0.00366 60  ILE A O   
752  C CB  A ILE A 60  ? 0.31956 0.39194 0.34694 -0.08465 0.05959  -0.00927 60  ILE A CB  
753  C CB  B ILE A 60  ? 0.33080 0.40694 0.36241 -0.08549 0.06007  -0.01066 60  ILE A CB  
754  C CG1 A ILE A 60  ? 0.31613 0.38322 0.34813 -0.09208 0.06267  -0.00888 60  ILE A CG1 
755  C CG1 B ILE A 60  ? 0.30468 0.37675 0.34270 -0.09181 0.06136  -0.01033 60  ILE A CG1 
756  C CG2 A ILE A 60  ? 0.32829 0.41130 0.36157 -0.08990 0.06818  -0.01480 60  ILE A CG2 
757  C CG2 B ILE A 60  ? 0.32357 0.40735 0.35852 -0.09195 0.07013  -0.01560 60  ILE A CG2 
758  C CD1 A ILE A 60  ? 0.36806 0.45350 0.42686 -0.09610 0.06090  -0.01563 60  ILE A CD1 
759  C CD1 B ILE A 60  ? 0.37327 0.46400 0.43795 -0.09647 0.06063  -0.01748 60  ILE A CD1 
760  N N   . THR A 61  ? 0.32683 0.39461 0.33152 -0.06462 0.04789  -0.00554 61  THR A N   
761  C CA  . THR A 61  ? 0.31969 0.39269 0.32021 -0.05860 0.04620  -0.00764 61  THR A CA  
762  C C   . THR A 61  ? 0.40792 0.46078 0.38022 -0.05313 0.04496  -0.00210 61  THR A C   
763  O O   . THR A 61  ? 0.50084 0.55167 0.46062 -0.05162 0.04809  -0.00306 61  THR A O   
764  C CB  . THR A 61  ? 0.36277 0.45184 0.38356 -0.05079 0.03606  -0.01095 61  THR A CB  
765  O OG1 . THR A 61  ? 0.32977 0.43723 0.37569 -0.05567 0.03693  -0.01629 61  THR A OG1 
766  C CG2 . THR A 61  ? 0.40579 0.50012 0.42341 -0.04347 0.03300  -0.01344 61  THR A CG2 
767  N N   A LEU A 62  ? 0.44120 0.47858 0.40279 -0.04996 0.04018  0.00343  62  LEU A N   
768  N N   B LEU A 62  ? 0.44309 0.48100 0.40540 -0.04969 0.03982  0.00331  62  LEU A N   
769  C CA  A LEU A 62  ? 0.49652 0.51387 0.43199 -0.04396 0.03738  0.00857  62  LEU A CA  
770  C CA  B LEU A 62  ? 0.49889 0.51630 0.43529 -0.04378 0.03686  0.00866  62  LEU A CA  
771  C C   A LEU A 62  ? 0.65697 0.65824 0.56796 -0.05030 0.04765  0.01192  62  LEU A C   
772  C C   B LEU A 62  ? 0.65541 0.65521 0.56715 -0.05038 0.04690  0.01263  62  LEU A C   
773  O O   A LEU A 62  ? 0.83395 0.81947 0.72113 -0.04524 0.04591  0.01550  62  LEU A O   
774  O O   B LEU A 62  ? 0.75408 0.73628 0.64144 -0.04557 0.04503  0.01689  62  LEU A O   
775  C CB  A LEU A 62  ? 0.48199 0.48645 0.41357 -0.03986 0.03035  0.01316  62  LEU A CB  
776  C CB  B LEU A 62  ? 0.48519 0.49202 0.42057 -0.03923 0.02914  0.01265  62  LEU A CB  
777  C CG  A LEU A 62  ? 0.42238 0.43669 0.37033 -0.03077 0.01932  0.01087  62  LEU A CG  
778  C CG  B LEU A 62  ? 0.41824 0.43681 0.37199 -0.03075 0.01864  0.00991  62  LEU A CG  
779  C CD1 A LEU A 62  ? 0.40846 0.40961 0.35286 -0.02782 0.01388  0.01482  62  LEU A CD1 
780  C CD1 B LEU A 62  ? 0.39035 0.39975 0.34577 -0.02938 0.01402  0.01308  62  LEU A CD1 
781  C CD2 A LEU A 62  ? 0.47463 0.49062 0.41710 -0.02150 0.01351  0.00895  62  LEU A CD2 
782  C CD2 B LEU A 62  ? 0.45146 0.46836 0.39773 -0.02060 0.01178  0.00893  62  LEU A CD2 
783  N N   A GLN A 63  ? 0.57601 0.58007 0.49207 -0.06114 0.05824  0.01073  63  GLN A N   
784  N N   B GLN A 63  ? 0.58186 0.58509 0.49925 -0.06115 0.05736  0.01126  63  GLN A N   
785  C CA  A GLN A 63  ? 0.74367 0.73244 0.63731 -0.06814 0.06977  0.01369  63  GLN A CA  
786  C CA  B GLN A 63  ? 0.73790 0.72631 0.63353 -0.06825 0.06888  0.01409  63  GLN A CA  
787  C C   A GLN A 63  ? 0.84055 0.83060 0.72131 -0.06530 0.07248  0.01158  63  GLN A C   
788  C C   B GLN A 63  ? 0.83490 0.82673 0.72032 -0.06663 0.07276  0.01132  63  GLN A C   
789  O O   A GLN A 63  ? 0.91178 0.88222 0.76361 -0.06408 0.07545  0.01634  63  GLN A O   
790  O O   B GLN A 63  ? 0.91313 0.88976 0.77515 -0.07095 0.08184  0.01434  63  GLN A O   
791  C CB  A GLN A 63  ? 0.70480 0.70099 0.61248 -0.08032 0.08088  0.01059  63  GLN A CB  
792  C CB  B GLN A 63  ? 0.69575 0.68921 0.60411 -0.08036 0.07948  0.01185  63  GLN A CB  
793  C CG  A GLN A 63  ? 0.55860 0.55241 0.47733 -0.08392 0.07906  0.01228  63  GLN A CG  
794  C CG  B GLN A 63  ? 0.70851 0.68327 0.60629 -0.08523 0.08261  0.01765  63  GLN A CG  
795  C CD  A GLN A 63  ? 0.71947 0.72798 0.66093 -0.09401 0.08671  0.00646  63  GLN A CD  
796  C CD  B GLN A 63  ? 0.68726 0.66346 0.59713 -0.08069 0.07218  0.01888  63  GLN A CD  
797  O OE1 A GLN A 63  ? 0.57260 0.59949 0.53044 -0.09593 0.08920  -0.00015 63  GLN A OE1 
798  O OE1 B GLN A 63  ? 0.66287 0.64869 0.59223 -0.08586 0.07296  0.01595  63  GLN A OE1 
799  N NE2 A GLN A 63  ? 0.71983 0.72044 0.66340 -0.10039 0.09017  0.00833  63  GLN A NE2 
800  N NE2 B GLN A 63  ? 0.64924 0.61540 0.54745 -0.07099 0.06240  0.02282  63  GLN A NE2 
801  N N   A SER A 64  ? 1.00376 1.02299 0.69830 -0.00304 -0.02728 0.13378  64  SER A N   
802  N N   B SER A 64  ? 0.96826 0.98474 0.66696 -0.00409 -0.02820 0.13353  64  SER A N   
803  C CA  A SER A 64  ? 1.04791 1.06858 0.73533 0.00081  -0.03038 0.12827  64  SER A CA  
804  C CA  B SER A 64  ? 1.03184 1.05019 0.72296 -0.00018 -0.03106 0.12823  64  SER A CA  
805  C C   A SER A 64  ? 1.01473 1.02835 0.70941 0.00198  -0.03259 0.12179  64  SER A C   
806  C C   B SER A 64  ? 1.01887 1.03063 0.71617 0.00139  -0.03345 0.12136  64  SER A C   
807  O O   A SER A 64  ? 1.10749 1.11970 0.80372 0.00380  -0.02990 0.11865  64  SER A O   
808  O O   B SER A 64  ? 1.05767 1.06970 0.75232 0.00453  -0.03217 0.11702  64  SER A O   
809  C CB  A SER A 64  ? 1.03391 1.06085 0.71194 0.00383  -0.02682 0.12817  64  SER A CB  
810  C CB  B SER A 64  ? 1.04740 1.07203 0.72951 0.00261  -0.02717 0.12853  64  SER A CB  
811  O OG  A SER A 64  ? 1.04670 1.07242 0.72877 0.00404  -0.02207 0.12793  64  SER A OG  
812  O OG  B SER A 64  ? 1.05323 1.07583 0.73978 0.00318  -0.02296 0.12719  64  SER A OG  
813  N N   A ILE A 65  ? 1.03282 1.04202 0.73202 0.00090  -0.03751 0.11979  65  ILE A N   
814  N N   B ILE A 65  ? 1.03758 1.04340 0.74318 -0.00075 -0.03688 0.12032  65  ILE A N   
815  C CA  A ILE A 65  ? 1.19572 1.19784 0.90257 0.00160  -0.04009 0.11385  65  ILE A CA  
816  C CA  B ILE A 65  ? 1.15140 1.15048 0.86388 0.00038  -0.03916 0.11401  65  ILE A CA  
817  C C   A ILE A 65  ? 1.10174 1.10428 0.80274 0.00481  -0.04489 0.10832  65  ILE A C   
818  C C   B ILE A 65  ? 1.15760 1.15768 0.86343 0.00386  -0.04356 0.10847  65  ILE A C   
819  O O   A ILE A 65  ? 1.10677 1.11137 0.80341 0.00453  -0.04865 0.10938  65  ILE A O   
820  O O   B ILE A 65  ? 1.17293 1.17342 0.87649 0.00348  -0.04803 0.10849  65  ILE A O   
821  C CB  A ILE A 65  ? 1.21606 1.21218 0.93359 -0.00218 -0.04202 0.11550  65  ILE A CB  
822  C CB  B ILE A 65  ? 1.12810 1.12061 0.85150 -0.00306 -0.04148 0.11472  65  ILE A CB  
823  N N   A ASN A 66  ? 1.12966 1.13019 0.83053 0.00787  -0.04476 0.10242  66  ASN A N   
824  N N   B ASN A 66  ? 1.16966 1.17010 0.87234 0.00729  -0.04231 0.10372  66  ASN A N   
825  C CA  A ASN A 66  ? 1.17743 1.17743 0.87391 0.01099  -0.04931 0.09646  66  ASN A CA  
826  C CA  B ASN A 66  ? 1.17668 1.17792 0.87311 0.01084  -0.04614 0.09808  66  ASN A CA  
827  C C   A ASN A 66  ? 1.17705 1.16963 0.88229 0.01158  -0.05099 0.09052  66  ASN A C   
828  C C   B ASN A 66  ? 1.15057 1.14483 0.85410 0.01198  -0.04885 0.09141  66  ASN A C   
829  O O   A ASN A 66  ? 1.24314 1.23291 0.94885 0.01284  -0.05583 0.08586  66  ASN A O   
830  O O   B ASN A 66  ? 1.17932 1.17335 0.87884 0.01466  -0.05269 0.08642  66  ASN A O   
831  C CB  A ASN A 66  ? 1.23744 1.24328 0.92309 0.01480  -0.04754 0.09471  66  ASN A CB  
832  C CB  B ASN A 66  ? 1.24036 1.24754 0.92688 0.01425  -0.04314 0.09719  66  ASN A CB  
833  N N   A GLU A 67  ? 0.92706 0.91640 0.63928 0.01068  -0.04701 0.09067  67  GLU A N   
834  N N   B GLU A 67  ? 0.93569 0.92427 0.64954 0.01005  -0.04696 0.09116  67  GLU A N   
835  C CA  A GLU A 67  ? 0.83900 0.82126 0.55972 0.01122  -0.04786 0.08524  67  GLU A CA  
836  C CA  B GLU A 67  ? 0.85457 0.83627 0.57572 0.01099  -0.04921 0.08494  67  GLU A CA  
837  C C   A GLU A 67  ? 0.71678 0.69303 0.44896 0.00731  -0.04846 0.08732  67  GLU A C   
838  C C   B GLU A 67  ? 0.71814 0.69346 0.45127 0.00726  -0.04928 0.08663  67  GLU A C   
839  O O   A GLU A 67  ? 0.62045 0.59794 0.35483 0.00418  -0.04633 0.09334  67  GLU A O   
840  O O   B GLU A 67  ? 0.60986 0.58611 0.34562 0.00405  -0.04723 0.09256  67  GLU A O   
841  C CB  A GLU A 67  ? 0.96396 0.94620 0.68483 0.01314  -0.04302 0.08338  67  GLU A CB  
842  C CB  B GLU A 67  ? 0.89437 0.87553 0.61473 0.01392  -0.04589 0.08087  67  GLU A CB  
843  C CG  A GLU A 67  ? 0.95634 0.93229 0.68312 0.01498  -0.04423 0.07643  67  GLU A CG  
844  C CG  B GLU A 67  ? 0.91209 0.89721 0.62250 0.01816  -0.04733 0.07656  67  GLU A CG  
845  C CD  A GLU A 67  ? 0.93508 0.90984 0.66445 0.01594  -0.03903 0.07554  67  GLU A CD  
846  C CD  B GLU A 67  ? 0.92448 0.90911 0.63430 0.02094  -0.04381 0.07283  67  GLU A CD  
847  O OE1 A GLU A 67  ? 0.86199 0.84013 0.59002 0.01472  -0.03447 0.08057  67  GLU A OE1 
848  O OE1 B GLU A 67  ? 0.94545 0.92463 0.66405 0.02002  -0.04191 0.07133  67  GLU A OE1 
849  O OE2 A GLU A 67  ? 0.89708 0.86748 0.62990 0.01791  -0.03953 0.06979  67  GLU A OE2 
850  O OE2 B GLU A 67  ? 0.88436 0.87405 0.58488 0.02405  -0.04289 0.07144  67  GLU A OE2 
851  N N   A ASP A 68  ? 0.63624 0.60592 0.37571 0.00751  -0.05143 0.08223  68  ASP A N   
852  N N   B ASP A 68  ? 0.65244 0.62117 0.39286 0.00773  -0.05166 0.08125  68  ASP A N   
853  C CA  A ASP A 68  ? 0.54734 0.51047 0.29852 0.00413  -0.05170 0.08325  68  ASP A CA  
854  C CA  B ASP A 68  ? 0.54752 0.50946 0.29985 0.00451  -0.05179 0.08191  68  ASP A CA  
855  C C   A ASP A 68  ? 0.53995 0.50112 0.29621 0.00344  -0.04609 0.08449  68  ASP A C   
856  C C   B ASP A 68  ? 0.54034 0.50026 0.29767 0.00395  -0.04622 0.08294  68  ASP A C   
857  O O   A ASP A 68  ? 0.54057 0.49855 0.29930 0.00550  -0.04493 0.07971  68  ASP A O   
858  O O   B ASP A 68  ? 0.56983 0.52831 0.32697 0.00658  -0.04467 0.07844  68  ASP A O   
859  C CB  A ASP A 68  ? 0.55113 0.50814 0.30777 0.00507  -0.05643 0.07683  68  ASP A CB  
860  C CB  B ASP A 68  ? 0.55142 0.50728 0.30910 0.00552  -0.05651 0.07542  68  ASP A CB  
861  C CG  A ASP A 68  ? 0.54429 0.49402 0.31334 0.00184  -0.05692 0.07711  68  ASP A CG  
862  C CG  B ASP A 68  ? 0.54468 0.49332 0.31465 0.00228  -0.05707 0.07572  68  ASP A CG  
863  O OD1 A ASP A 68  ? 0.53625 0.48457 0.31064 -0.00055 -0.05277 0.08098  68  ASP A OD1 
864  O OD1 B ASP A 68  ? 0.53705 0.48547 0.31121 -0.00078 -0.05388 0.08110  68  ASP A OD1 
865  O OD2 A ASP A 68  ? 0.54721 0.49255 0.32062 0.00178  -0.06156 0.07326  68  ASP A OD2 
866  O OD2 B ASP A 68  ? 0.54703 0.49025 0.32248 0.00280  -0.06066 0.07058  68  ASP A OD2 
867  N N   A ILE A 69  ? 0.53285 0.49574 0.29090 0.00049  -0.04260 0.09093  69  ILE A N   
868  N N   B ILE A 69  ? 0.53232 0.49191 0.29434 0.00050  -0.04328 0.08875  69  ILE A N   
869  C CA  A ILE A 69  ? 0.52589 0.48792 0.28754 -0.00015 -0.03696 0.09286  69  ILE A CA  
870  C CA  B ILE A 69  ? 0.52563 0.48521 0.29009 -0.00008 -0.03747 0.09117  69  ILE A CA  
871  C C   A ILE A 69  ? 0.51878 0.47297 0.29282 -0.00276 -0.03633 0.09234  69  ILE A C   
872  C C   B ILE A 69  ? 0.51742 0.46989 0.29402 -0.00311 -0.03608 0.09193  69  ILE A C   
873  O O   A ILE A 69  ? 0.51203 0.46493 0.29019 -0.00394 -0.03174 0.09468  69  ILE A O   
874  O O   B ILE A 69  ? 0.51122 0.46317 0.29068 -0.00395 -0.03126 0.09428  69  ILE A O   
875  C CB  A ILE A 69  ? 0.52197 0.49022 0.27863 -0.00171 -0.03303 0.09996  69  ILE A CB  
876  C CB  B ILE A 69  ? 0.52347 0.49032 0.28086 -0.00095 -0.03395 0.09773  69  ILE A CB  
877  C CG1 A ILE A 69  ? 0.51961 0.48879 0.27762 -0.00518 -0.03517 0.10523  69  ILE A CG1 
878  C CG1 B ILE A 69  ? 0.52262 0.49234 0.27624 0.00118  -0.02876 0.09757  69  ILE A CG1 
879  C CG2 A ILE A 69  ? 0.52847 0.50420 0.27299 0.00159  -0.03204 0.09964  69  ILE A CG2 
880  C CG2 B ILE A 69  ? 0.51582 0.48171 0.27890 -0.00535 -0.03290 0.10413  69  ILE A CG2 
881  C CD1 A ILE A 69  ? 0.51250 0.47496 0.28221 -0.00889 -0.03578 0.10672  69  ILE A CD1 
882  C CD1 B ILE A 69  ? 0.54213 0.51500 0.28733 0.00558  -0.02973 0.09250  69  ILE A CD1 
883  N N   A THR A 70  ? 0.34217 0.28584 0.25971 0.05635  0.00838  0.01603  70  THR A N   
884  N N   B THR A 70  ? 0.29482 0.24076 0.21755 0.05484  0.00678  0.01518  70  THR A N   
885  C CA  A THR A 70  ? 0.29080 0.24039 0.21986 0.05238  0.00184  0.01339  70  THR A CA  
886  C CA  B THR A 70  ? 0.30114 0.25325 0.23695 0.05071  0.00138  0.01263  70  THR A CA  
887  C C   A THR A 70  ? 0.27860 0.23011 0.21470 0.04948  0.00114  0.00886  70  THR A C   
888  C C   B THR A 70  ? 0.34754 0.30036 0.28667 0.04824  -0.00030 0.00765  70  THR A C   
889  O O   A THR A 70  ? 0.25847 0.21544 0.20808 0.04636  0.00004  0.00817  70  THR A O   
890  O O   B THR A 70  ? 0.33866 0.29645 0.28941 0.04490  -0.00283 0.00602  70  THR A O   
891  C CB  A THR A 70  ? 0.33646 0.28645 0.25794 0.05258  -0.00644 0.01183  70  THR A CB  
892  C CB  B THR A 70  ? 0.38977 0.34399 0.32318 0.05050  -0.00613 0.01244  70  THR A CB  
893  O OG1 A THR A 70  ? 0.29952 0.24688 0.21195 0.05664  -0.00577 0.01661  70  THR A OG1 
894  O OG1 B THR A 70  ? 0.39550 0.35304 0.33272 0.04693  -0.01235 0.00744  70  THR A OG1 
895  C CG2 A THR A 70  ? 0.32738 0.28463 0.26244 0.04894  -0.01178 0.01031  70  THR A CG2 
896  C CG2 B THR A 70  ? 0.37175 0.32113 0.28827 0.05448  -0.00789 0.01387  70  THR A CG2 
897  N N   A TYR A 71  ? 0.28040 0.22655 0.20665 0.05099  0.00241  0.00599  71  TYR A N   
898  N N   B TYR A 71  ? 0.31286 0.25987 0.24123 0.05019  0.00152  0.00536  71  TYR A N   
899  C CA  A TYR A 71  ? 0.32470 0.27058 0.25521 0.04905  0.00154  0.00191  71  TYR A CA  
900  C CA  B TYR A 71  ? 0.31713 0.26316 0.24859 0.04872  0.00135  0.00147  71  TYR A CA  
901  C C   A TYR A 71  ? 0.27575 0.22734 0.22112 0.04831  0.00595  0.00345  71  TYR A C   
902  C C   B TYR A 71  ? 0.28212 0.23316 0.22692 0.04871  0.00666  0.00325  71  TYR A C   
903  O O   A TYR A 71  ? 0.24550 0.19919 0.19793 0.04614  0.00385  0.00105  71  TYR A O   
904  O O   B TYR A 71  ? 0.29992 0.25204 0.25036 0.04746  0.00578  0.00087  71  TYR A O   
905  C CB  A TYR A 71  ? 0.34929 0.28647 0.26524 0.05196  0.00363  -0.00093 71  TYR A CB  
906  C CB  B TYR A 71  ? 0.35401 0.29101 0.26988 0.05139  0.00251  -0.00164 71  TYR A CB  
907  C CG  A TYR A 71  ? 0.35627 0.29187 0.27025 0.05638  0.01248  0.00189  71  TYR A CG  
908  C CG  B TYR A 71  ? 0.37550 0.30949 0.28645 0.05616  0.01098  0.00079  71  TYR A CG  
909  C CD1 A TYR A 71  ? 0.37536 0.30856 0.28030 0.05966  0.01662  0.00548  71  TYR A CD1 
910  C CD1 B TYR A 71  ? 0.37130 0.30250 0.27191 0.05941  0.01425  0.00399  71  TYR A CD1 
911  C CD2 A TYR A 71  ? 0.34310 0.28021 0.26465 0.05754  0.01693  0.00134  71  TYR A CD2 
912  C CD2 B TYR A 71  ? 0.35602 0.29035 0.27266 0.05784  0.01600  0.00022  71  TYR A CD2 
913  C CE1 A TYR A 71  ? 0.40908 0.34163 0.31329 0.06343  0.02571  0.00831  71  TYR A CE1 
914  C CE1 B TYR A 71  ? 0.43021 0.35908 0.32666 0.06367  0.02299  0.00649  71  TYR A CE1 
915  C CE2 A TYR A 71  ? 0.35846 0.29609 0.28027 0.06163  0.02527  0.00393  71  TYR A CE2 
916  C CE2 B TYR A 71  ? 0.37633 0.30953 0.29010 0.06241  0.02428  0.00254  71  TYR A CE2 
917  C CZ  A TYR A 71  ? 0.48332 0.41882 0.39688 0.06425  0.02997  0.00736  71  TYR A CZ  
918  C CZ  B TYR A 71  ? 0.50174 0.43222 0.40556 0.06505  0.02809  0.00561  71  TYR A CZ  
919  O OH  A TYR A 71  ? 0.48320 0.41996 0.39795 0.06806  0.03919  0.01020  71  TYR A OH  
920  O OH  B TYR A 71  ? 0.43332 0.36302 0.33454 0.06950  0.03730  0.00820  71  TYR A OH  
921  N N   . VAL A 72  ? 0.28720 0.24135 0.23716 0.04997  0.01205  0.00747  72  VAL A N   
922  C CA  . VAL A 72  ? 0.26414 0.22497 0.22869 0.04902  0.01602  0.00861  72  VAL A CA  
923  C C   . VAL A 72  ? 0.27712 0.24397 0.25413 0.04485  0.01150  0.00770  72  VAL A C   
924  O O   . VAL A 72  ? 0.29156 0.26371 0.27902 0.04361  0.01189  0.00676  72  VAL A O   
925  C CB  . VAL A 72  ? 0.28987 0.25237 0.25733 0.05060  0.02357  0.01308  72  VAL A CB  
926  C CG1 . VAL A 72  ? 0.31254 0.28388 0.29722 0.04857  0.02672  0.01381  72  VAL A CG1 
927  C CG2 . VAL A 72  ? 0.31115 0.26785 0.26580 0.05533  0.02898  0.01364  72  VAL A CG2 
928  N N   A ARG A 73  ? 0.23445 0.20089 0.21023 0.04312  0.00711  0.00796  73  ARG A N   
929  N N   B ARG A 73  ? 0.23748 0.20389 0.21317 0.04312  0.00706  0.00789  73  ARG A N   
930  C CA  A ARG A 73  ? 0.26140 0.23286 0.24764 0.03962  0.00317  0.00675  73  ARG A CA  
931  C CA  B ARG A 73  ? 0.26827 0.23973 0.25452 0.03964  0.00324  0.00679  73  ARG A CA  
932  C C   A ARG A 73  ? 0.25667 0.22924 0.24495 0.03808  -0.00005 0.00319  73  ARG A C   
933  C C   B ARG A 73  ? 0.26048 0.23297 0.24850 0.03795  -0.00042 0.00315  73  ARG A C   
934  O O   A ARG A 73  ? 0.23216 0.20955 0.23005 0.03583  -0.00120 0.00235  73  ARG A O   
935  O O   B ARG A 73  ? 0.24627 0.22343 0.24356 0.03549  -0.00211 0.00224  73  ARG A O   
936  C CB  A ARG A 73  ? 0.25984 0.23067 0.24323 0.03905  -0.00121 0.00727  73  ARG A CB  
937  C CB  B ARG A 73  ? 0.27079 0.24154 0.25437 0.03924  -0.00058 0.00774  73  ARG A CB  
938  C CG  A ARG A 73  ? 0.24473 0.21400 0.22743 0.04071  0.00177  0.01155  73  ARG A CG  
939  C CG  B ARG A 73  ? 0.34442 0.31968 0.33908 0.03672  -0.00207 0.00788  73  ARG A CG  
940  C CD  A ARG A 73  ? 0.27692 0.24598 0.25637 0.04153  -0.00294 0.01244  73  ARG A CD  
941  C CD  B ARG A 73  ? 0.35677 0.33111 0.34866 0.03794  -0.00465 0.00981  73  ARG A CD  
942  N NE  A ARG A 73  ? 0.26685 0.23219 0.24237 0.04437  0.00024  0.01724  73  ARG A NE  
943  N NE  B ARG A 73  ? 0.34258 0.31252 0.32904 0.04083  -0.00057 0.01412  73  ARG A NE  
944  C CZ  A ARG A 73  ? 0.28897 0.25403 0.27243 0.04374  0.00336  0.01987  73  ARG A CZ  
945  C CZ  B ARG A 73  ? 0.27479 0.24346 0.26627 0.04103  0.00245  0.01726  73  ARG A CZ  
946  N NH1 A ARG A 73  ? 0.24462 0.21357 0.24020 0.04031  0.00324  0.01765  73  ARG A NH1 
947  N NH1 B ARG A 73  ? 0.32344 0.29488 0.32527 0.03863  0.00164  0.01605  73  ARG A NH1 
948  N NH2 A ARG A 73  ? 0.25083 0.21059 0.22906 0.04658  0.00702  0.02478  73  ARG A NH2 
949  N NH2 B ARG A 73  ? 0.26452 0.22789 0.24948 0.04379  0.00670  0.02173  73  ARG A NH2 
950  N N   . TYR A 74  ? 0.24095 0.20812 0.21934 0.03926  -0.00138 0.00104  74  TYR A N   
951  C CA  . TYR A 74  ? 0.23464 0.20072 0.21372 0.03779  -0.00394 -0.00191 74  TYR A CA  
952  C C   . TYR A 74  ? 0.24138 0.21062 0.22776 0.03908  -0.00087 -0.00150 74  TYR A C   
953  O O   . TYR A 74  ? 0.25719 0.22759 0.24733 0.03769  -0.00301 -0.00283 74  TYR A O   
954  C CB  . TYR A 74  ? 0.25810 0.21580 0.22428 0.03859  -0.00545 -0.00455 74  TYR A CB  
955  C CG  . TYR A 74  ? 0.25890 0.21589 0.22033 0.03605  -0.01073 -0.00597 74  TYR A CG  
956  C CD1 . TYR A 74  ? 0.30135 0.25852 0.25744 0.03765  -0.01121 -0.00423 74  TYR A CD1 
957  C CD2 . TYR A 74  ? 0.25898 0.21595 0.22200 0.03209  -0.01525 -0.00871 74  TYR A CD2 
958  C CE1 . TYR A 74  ? 0.29642 0.25483 0.24915 0.03585  -0.01691 -0.00541 74  TYR A CE1 
959  C CE2 . TYR A 74  ? 0.30250 0.26111 0.26338 0.02956  -0.02031 -0.01010 74  TYR A CE2 
960  C CZ  . TYR A 74  ? 0.31495 0.27483 0.27090 0.03165  -0.02155 -0.00858 74  TYR A CZ  
961  O OH  . TYR A 74  ? 0.32236 0.28555 0.27710 0.02966  -0.02726 -0.00985 74  TYR A OH  
962  N N   . PHE A 75  ? 0.28998 0.26113 0.27846 0.04192  0.00417  0.00053  75  PHE A N   
963  C CA  . PHE A 75  ? 0.27448 0.25127 0.27196 0.04333  0.00655  0.00104  75  PHE A CA  
964  C C   . PHE A 75  ? 0.28807 0.27300 0.29781 0.03999  0.00448  0.00130  75  PHE A C   
965  O O   . PHE A 75  ? 0.31465 0.30442 0.33097 0.04023  0.00356  0.00072  75  PHE A O   
966  C CB  . PHE A 75  ? 0.31693 0.29507 0.31474 0.04701  0.01291  0.00315  75  PHE A CB  
967  C CG  . PHE A 75  ? 0.34038 0.30932 0.32419 0.05076  0.01524  0.00236  75  PHE A CG  
968  C CD1 . PHE A 75  ? 0.47006 0.43139 0.44540 0.05173  0.01261  -0.00051 75  PHE A CD1 
969  C CD2 . PHE A 75  ? 0.35173 0.31839 0.32964 0.05308  0.02017  0.00430  75  PHE A CD2 
970  C CE1 . PHE A 75  ? 0.50745 0.45879 0.46862 0.05490  0.01464  -0.00210 75  PHE A CE1 
971  C CE2 . PHE A 75  ? 0.41544 0.37281 0.37855 0.05680  0.02235  0.00302  75  PHE A CE2 
972  C CZ  . PHE A 75  ? 0.45417 0.40379 0.40891 0.05759  0.01936  -0.00053 75  PHE A CZ  
973  N N   A ASP A 76  ? 0.24882 0.23483 0.26093 0.03730  0.00371  0.00211  76  ASP A N   
974  N N   B ASP A 76  ? 0.25025 0.23618 0.26225 0.03725  0.00354  0.00203  76  ASP A N   
975  C CA  A ASP A 76  ? 0.25125 0.24259 0.27260 0.03392  0.00129  0.00145  76  ASP A CA  
976  C CA  B ASP A 76  ? 0.25341 0.24507 0.27524 0.03395  0.00151  0.00152  76  ASP A CA  
977  C C   A ASP A 76  ? 0.22821 0.21799 0.24695 0.03234  -0.00344 -0.00076 76  ASP A C   
978  C C   B ASP A 76  ? 0.25621 0.24646 0.27593 0.03194  -0.00332 -0.00056 76  ASP A C   
979  O O   A ASP A 76  ? 0.18254 0.17577 0.20568 0.03156  -0.00517 -0.00194 76  ASP A O   
980  O O   B ASP A 76  ? 0.30609 0.30048 0.33180 0.03016  -0.00527 -0.00178 76  ASP A O   
981  C CB  A ASP A 76  ? 0.27408 0.26446 0.29669 0.03243  0.00251  0.00317  76  ASP A CB  
982  C CB  B ASP A 76  ? 0.29640 0.28825 0.32140 0.03248  0.00373  0.00349  76  ASP A CB  
983  C CG  A ASP A 76  ? 0.38807 0.38108 0.41744 0.02921  -0.00008 0.00202  76  ASP A CG  
984  C CG  B ASP A 76  ? 0.28091 0.27573 0.31340 0.02912  0.00144  0.00235  76  ASP A CG  
985  O OD1 A ASP A 76  ? 0.27454 0.26944 0.30543 0.02789  -0.00356 -0.00025 76  ASP A OD1 
986  O OD1 B ASP A 76  ? 0.39753 0.39070 0.42733 0.02824  -0.00216 0.00104  76  ASP A OD1 
987  O OD2 A ASP A 76  ? 0.32138 0.31343 0.35365 0.02825  0.00192  0.00361  76  ASP A OD2 
988  O OD2 B ASP A 76  ? 0.38712 0.38592 0.42841 0.02719  0.00350  0.00255  76  ASP A OD2 
989  N N   A TRP A 77  ? 0.23451 0.21953 0.24602 0.03182  -0.00554 -0.00121 77  TRP A N   
990  N N   B TRP A 77  ? 0.23068 0.21555 0.24194 0.03203  -0.00525 -0.00107 77  TRP A N   
991  C CA  A TRP A 77  ? 0.19260 0.17744 0.20369 0.02943  -0.00942 -0.00301 77  TRP A CA  
992  C CA  B TRP A 77  ? 0.21378 0.19807 0.22402 0.02972  -0.00919 -0.00291 77  TRP A CA  
993  C C   A TRP A 77  ? 0.20028 0.18306 0.20904 0.02962  -0.01034 -0.00432 77  TRP A C   
994  C C   B TRP A 77  ? 0.21800 0.20153 0.22776 0.02989  -0.00991 -0.00410 77  TRP A C   
995  O O   A TRP A 77  ? 0.19728 0.18150 0.20822 0.02756  -0.01237 -0.00526 77  TRP A O   
996  O O   B TRP A 77  ? 0.21762 0.20423 0.23164 0.02822  -0.01150 -0.00481 77  TRP A O   
997  C CB  A TRP A 77  ? 0.20177 0.18326 0.20640 0.02880  -0.01175 -0.00338 77  TRP A CB  
998  C CB  B TRP A 77  ? 0.19467 0.17433 0.19664 0.02944  -0.01135 -0.00355 77  TRP A CB  
999  C CG  A TRP A 77  ? 0.21994 0.20259 0.22531 0.02943  -0.01145 -0.00156 77  TRP A CG  
1000 C CG  B TRP A 77  ? 0.18620 0.16713 0.18835 0.02965  -0.01184 -0.00206 77  TRP A CG  
1001 C CD1 A TRP A 77  ? 0.21137 0.19673 0.22337 0.02953  -0.00923 0.00014  77  TRP A CD1 
1002 C CD1 B TRP A 77  ? 0.26919 0.25309 0.27764 0.02988  -0.00992 -0.00019 77  TRP A CD1 
1003 C CD2 A TRP A 77  ? 0.19296 0.17339 0.19158 0.03024  -0.01356 -0.00113 77  TRP A CD2 
1004 C CD2 B TRP A 77  ? 0.18434 0.16315 0.17970 0.02993  -0.01456 -0.00220 77  TRP A CD2 
1005 N NE1 A TRP A 77  ? 0.21395 0.19784 0.22326 0.03085  -0.00931 0.00216  77  TRP A NE1 
1006 N NE1 B TRP A 77  ? 0.23072 0.21366 0.23627 0.03095  -0.01083 0.00143  77  TRP A NE1 
1007 C CE2 A TRP A 77  ? 0.21980 0.20144 0.22085 0.03162  -0.01230 0.00154  77  TRP A CE2 
1008 C CE2 B TRP A 77  ? 0.18175 0.16251 0.17939 0.03120  -0.01406 0.00028  77  TRP A CE2 
1009 C CE3 A TRP A 77  ? 0.22306 0.20030 0.21346 0.02983  -0.01667 -0.00292 77  TRP A CE3 
1010 C CE3 B TRP A 77  ? 0.16342 0.13868 0.15083 0.02912  -0.01760 -0.00433 77  TRP A CE3 
1011 C CZ2 A TRP A 77  ? 0.24902 0.22944 0.24419 0.03349  -0.01428 0.00305  77  TRP A CZ2 
1012 C CZ2 B TRP A 77  ? 0.21668 0.19700 0.20888 0.03253  -0.01685 0.00118  77  TRP A CZ2 
1013 C CZ3 A TRP A 77  ? 0.25840 0.23552 0.24347 0.03101  -0.01927 -0.00212 77  TRP A CZ3 
1014 C CZ3 B TRP A 77  ? 0.20457 0.18026 0.18710 0.02958  -0.02090 -0.00415 77  TRP A CZ3 
1015 C CH2 A TRP A 77  ? 0.28520 0.26414 0.27242 0.03331  -0.01807 0.00118  77  TRP A CH2 
1016 C CH2 B TRP A 77  ? 0.25297 0.23161 0.23780 0.03171  -0.02063 -0.00116 77  TRP A CH2 
1017 N N   . VAL A 78  ? 0.21155 0.19016 0.21518 0.03245  -0.00840 -0.00417 78  VAL A N   
1018 C CA  . VAL A 78  ? 0.22419 0.19919 0.22486 0.03336  -0.00890 -0.00489 78  VAL A CA  
1019 C C   . VAL A 78  ? 0.25598 0.23740 0.26415 0.03409  -0.00910 -0.00418 78  VAL A C   
1020 O O   . VAL A 78  ? 0.26613 0.24553 0.27248 0.03414  -0.01040 -0.00436 78  VAL A O   
1021 C CB  . VAL A 78  ? 0.29007 0.25784 0.28271 0.03699  -0.00639 -0.00505 78  VAL A CB  
1022 C CG1 . VAL A 78  ? 0.28648 0.25918 0.28406 0.04099  -0.00278 -0.00334 78  VAL A CG1 
1023 C CG2 . VAL A 78  ? 0.44209 0.40171 0.42831 0.03729  -0.00714 -0.00611 78  VAL A CG2 
1024 N N   . LEU A 79  ? 0.24148 0.23044 0.25777 0.03437  -0.00799 -0.00342 79  LEU A N   
1025 C CA  . LEU A 79  ? 0.26536 0.26177 0.28926 0.03436  -0.00917 -0.00348 79  LEU A CA  
1026 C C   . LEU A 79  ? 0.26379 0.26314 0.29125 0.03053  -0.01150 -0.00475 79  LEU A C   
1027 O O   . LEU A 79  ? 0.25410 0.25578 0.28240 0.03005  -0.01364 -0.00549 79  LEU A O   
1028 C CB  . LEU A 79  ? 0.24594 0.24950 0.27801 0.03571  -0.00672 -0.00257 79  LEU A CB  
1029 C CG  . LEU A 79  ? 0.26968 0.27148 0.29924 0.04017  -0.00330 -0.00119 79  LEU A CG  
1030 C CD1 . LEU A 79  ? 0.29470 0.30566 0.33470 0.04079  -0.00034 -0.00011 79  LEU A CD1 
1031 C CD2 . LEU A 79  ? 0.39079 0.38946 0.41571 0.04404  -0.00429 -0.00097 79  LEU A CD2 
1032 N N   . THR A 80  ? 0.21958 0.21851 0.24843 0.02837  -0.01091 -0.00489 80  THR A N   
1033 C CA  . THR A 80  ? 0.20932 0.21103 0.24242 0.02552  -0.01231 -0.00619 80  THR A CA  
1034 C C   . THR A 80  ? 0.24522 0.24419 0.27409 0.02411  -0.01415 -0.00701 80  THR A C   
1035 O O   . THR A 80  ? 0.22025 0.22155 0.25094 0.02274  -0.01531 -0.00832 80  THR A O   
1036 C CB  . THR A 80  ? 0.19237 0.19423 0.22917 0.02440  -0.01053 -0.00561 80  THR A CB  
1037 O OG1 . THR A 80  ? 0.21965 0.21680 0.25068 0.02540  -0.00988 -0.00424 80  THR A OG1 
1038 C CG2 . THR A 80  ? 0.24913 0.25480 0.29230 0.02461  -0.00805 -0.00486 80  THR A CG2 
1039 N N   . THR A 81  ? 0.21169 0.20606 0.23509 0.02409  -0.01431 -0.00652 81  THR A N   
1040 C CA  . THR A 81  ? 0.21866 0.21209 0.24035 0.02194  -0.01574 -0.00730 81  THR A CA  
1041 C C   . THR A 81  ? 0.20453 0.19700 0.22384 0.02142  -0.01622 -0.00762 81  THR A C   
1042 O O   . THR A 81  ? 0.21357 0.20800 0.23428 0.01965  -0.01651 -0.00830 81  THR A O   
1043 C CB  . THR A 81  ? 0.20099 0.19105 0.21848 0.02125  -0.01655 -0.00718 81  THR A CB  
1044 O OG1 . THR A 81  ? 0.20524 0.18964 0.21634 0.02235  -0.01617 -0.00712 81  THR A OG1 
1045 C CG2 . THR A 81  ? 0.23124 0.22245 0.25012 0.02236  -0.01623 -0.00627 81  THR A CG2 
1046 N N   . PRO A 82  ? 0.20721 0.19662 0.22271 0.02339  -0.01591 -0.00686 82  PRO A N   
1047 C CA  . PRO A 82  ? 0.23320 0.22129 0.24570 0.02340  -0.01623 -0.00649 82  PRO A CA  
1048 C C   . PRO A 82  ? 0.25043 0.24454 0.26665 0.02352  -0.01708 -0.00726 82  PRO A C   
1049 O O   . PRO A 82  ? 0.22981 0.22386 0.24388 0.02233  -0.01711 -0.00748 82  PRO A O   
1050 C CB  . PRO A 82  ? 0.23590 0.21915 0.24358 0.02673  -0.01567 -0.00511 82  PRO A CB  
1051 C CG  . PRO A 82  ? 0.22871 0.21394 0.23928 0.02895  -0.01487 -0.00507 82  PRO A CG  
1052 C CD  . PRO A 82  ? 0.20316 0.18919 0.21571 0.02621  -0.01485 -0.00603 82  PRO A CD  
1053 N N   . VAL A 83  ? 0.20924 0.20839 0.23080 0.02459  -0.01755 -0.00791 83  VAL A N   
1054 C CA  . VAL A 83  ? 0.19928 0.20383 0.22433 0.02392  -0.01885 -0.00964 83  VAL A CA  
1055 C C   . VAL A 83  ? 0.21547 0.21999 0.24153 0.02133  -0.01825 -0.01119 83  VAL A C   
1056 O O   . VAL A 83  ? 0.22001 0.22559 0.24407 0.02076  -0.01870 -0.01247 83  VAL A O   
1057 C CB  . VAL A 83  ? 0.21937 0.22938 0.25147 0.02438  -0.01924 -0.01038 83  VAL A CB  
1058 C CG1 . VAL A 83  ? 0.22150 0.23640 0.25702 0.02269  -0.02107 -0.01316 83  VAL A CG1 
1059 C CG2 . VAL A 83  ? 0.23812 0.24975 0.27014 0.02786  -0.01951 -0.00863 83  VAL A CG2 
1060 N N   . MET A 84  ? 0.19873 0.20210 0.22737 0.02031  -0.01709 -0.01099 84  MET A N   
1061 C CA  . MET A 84  ? 0.18900 0.19297 0.21962 0.01886  -0.01633 -0.01213 84  MET A CA  
1062 C C   . MET A 84  ? 0.23832 0.24131 0.26523 0.01795  -0.01580 -0.01186 84  MET A C   
1063 O O   . MET A 84  ? 0.22845 0.23303 0.25606 0.01733  -0.01483 -0.01315 84  MET A O   
1064 C CB  . MET A 84  ? 0.20907 0.21213 0.24234 0.01894  -0.01566 -0.01114 84  MET A CB  
1065 C CG  . MET A 84  ? 0.21129 0.21467 0.24832 0.01950  -0.01501 -0.01101 84  MET A CG  
1066 S SD  . MET A 84  ? 0.25653 0.25747 0.29358 0.02057  -0.01403 -0.00875 84  MET A SD  
1067 C CE  . MET A 84  ? 0.29164 0.29304 0.33161 0.02062  -0.01368 -0.00926 84  MET A CE  
1068 N N   . LEU A 85  ? 0.21601 0.21581 0.23890 0.01772  -0.01585 -0.01022 85  LEU A N   
1069 C CA  . LEU A 85  ? 0.21064 0.20904 0.23053 0.01604  -0.01468 -0.00965 85  LEU A CA  
1070 C C   . LEU A 85  ? 0.21198 0.21017 0.22744 0.01689  -0.01420 -0.00972 85  LEU A C   
1071 O O   . LEU A 85  ? 0.22393 0.22322 0.23846 0.01583  -0.01241 -0.01007 85  LEU A O   
1072 C CB  . LEU A 85  ? 0.21684 0.21019 0.23313 0.01495  -0.01471 -0.00824 85  LEU A CB  
1073 C CG  . LEU A 85  ? 0.19080 0.18488 0.21017 0.01342  -0.01558 -0.00863 85  LEU A CG  
1074 C CD1 . LEU A 85  ? 0.23761 0.22496 0.25165 0.01273  -0.01606 -0.00812 85  LEU A CD1 
1075 C CD2 . LEU A 85  ? 0.21307 0.21162 0.23697 0.01076  -0.01492 -0.00908 85  LEU A CD2 
1076 N N   . LEU A 86  ? 0.22572 0.22316 0.23832 0.01920  -0.01575 -0.00930 86  LEU A N   
1077 C CA  . LEU A 86  ? 0.23043 0.22853 0.23804 0.02066  -0.01632 -0.00945 86  LEU A CA  
1078 C C   . LEU A 86  ? 0.22784 0.23004 0.23759 0.01998  -0.01634 -0.01244 86  LEU A C   
1079 O O   . LEU A 86  ? 0.21336 0.21517 0.21807 0.01999  -0.01512 -0.01286 86  LEU A O   
1080 C CB  . LEU A 86  ? 0.24323 0.24212 0.24954 0.02375  -0.01882 -0.00865 86  LEU A CB  
1081 C CG  . LEU A 86  ? 0.29945 0.29229 0.30122 0.02555  -0.01818 -0.00559 86  LEU A CG  
1082 C CD1 . LEU A 86  ? 0.40688 0.40246 0.40922 0.02961  -0.02052 -0.00484 86  LEU A CD1 
1083 C CD2 . LEU A 86  ? 0.38689 0.37338 0.38027 0.02535  -0.01621 -0.00323 86  LEU A CD2 
1084 N N   . THR A 87  ? 0.23123 0.23635 0.24765 0.01945  -0.01720 -0.01456 87  THR A N   
1085 C CA  . THR A 87  ? 0.22255 0.22963 0.24036 0.01881  -0.01701 -0.01790 87  THR A CA  
1086 C C   . THR A 87  ? 0.21989 0.22622 0.23783 0.01802  -0.01382 -0.01820 87  THR A C   
1087 O O   . THR A 87  ? 0.25846 0.26495 0.27345 0.01825  -0.01266 -0.02049 87  THR A O   
1088 C CB  . THR A 87  ? 0.29133 0.30009 0.31615 0.01809  -0.01803 -0.01990 87  THR A CB  
1089 O OG1 . THR A 87  ? 0.26661 0.27417 0.29612 0.01776  -0.01656 -0.01819 87  THR A OG1 
1090 C CG2 . THR A 87  ? 0.31644 0.32811 0.34283 0.01867  -0.02087 -0.01988 87  THR A CG2 
1091 N N   . THR A 88  ? 0.21252 0.21852 0.23364 0.01725  -0.01244 -0.01608 88  THR A N   
1092 C CA  . THR A 88  ? 0.20700 0.21440 0.22991 0.01654  -0.00948 -0.01592 88  THR A CA  
1093 C C   . THR A 88  ? 0.20199 0.20843 0.21838 0.01614  -0.00721 -0.01500 88  THR A C   
1094 O O   . THR A 88  ? 0.20531 0.21315 0.22076 0.01648  -0.00433 -0.01627 88  THR A O   
1095 C CB  . THR A 88  ? 0.25365 0.26209 0.28154 0.01543  -0.00965 -0.01395 88  THR A CB  
1096 O OG1 . THR A 88  ? 0.32082 0.32962 0.35335 0.01646  -0.01112 -0.01447 88  THR A OG1 
1097 C CG2 . THR A 88  ? 0.35317 0.36540 0.38492 0.01458  -0.00692 -0.01370 88  THR A CG2 
1098 N N   . VAL A 89  ? 0.20344 0.20670 0.21466 0.01578  -0.00790 -0.01259 89  VAL A N   
1099 C CA  . VAL A 89  ? 0.18068 0.18137 0.18391 0.01577  -0.00548 -0.01097 89  VAL A CA  
1100 C C   . VAL A 89  ? 0.23015 0.23144 0.22733 0.01785  -0.00563 -0.01329 89  VAL A C   
1101 O O   . VAL A 89  ? 0.21977 0.22101 0.21257 0.01795  -0.00211 -0.01348 89  VAL A O   
1102 C CB  . VAL A 89  ? 0.21973 0.21513 0.21725 0.01617  -0.00669 -0.00792 89  VAL A CB  
1103 C CG1 . VAL A 89  ? 0.23366 0.22524 0.22098 0.01715  -0.00437 -0.00578 89  VAL A CG1 
1104 C CG2 . VAL A 89  ? 0.23281 0.22613 0.23461 0.01327  -0.00578 -0.00622 89  VAL A CG2 
1105 N N   . TYR A 90  ? 0.20719 0.20933 0.20401 0.01935  -0.00965 -0.01534 90  TYR A N   
1106 C CA  . TYR A 90  ? 0.20794 0.21073 0.19842 0.02085  -0.01090 -0.01835 90  TYR A CA  
1107 C C   . TYR A 90  ? 0.22630 0.23007 0.21879 0.02043  -0.00806 -0.02184 90  TYR A C   
1108 O O   . TYR A 90  ? 0.24619 0.24891 0.23085 0.02149  -0.00629 -0.02355 90  TYR A O   
1109 C CB  . TYR A 90  ? 0.21928 0.22444 0.21161 0.02162  -0.01611 -0.02046 90  TYR A CB  
1110 C CG  . TYR A 90  ? 0.22215 0.22715 0.21311 0.02323  -0.01889 -0.01712 90  TYR A CG  
1111 C CD1 . TYR A 90  ? 0.24107 0.24182 0.22485 0.02455  -0.01721 -0.01286 90  TYR A CD1 
1112 C CD2 . TYR A 90  ? 0.24393 0.25245 0.24139 0.02348  -0.02240 -0.01799 90  TYR A CD2 
1113 C CE1 . TYR A 90  ? 0.23191 0.23117 0.21411 0.02684  -0.01932 -0.00975 90  TYR A CE1 
1114 C CE2 . TYR A 90  ? 0.26326 0.27199 0.26027 0.02578  -0.02435 -0.01489 90  TYR A CE2 
1115 C CZ  . TYR A 90  ? 0.27251 0.27616 0.26156 0.02776  -0.02288 -0.01087 90  TYR A CZ  
1116 O OH  . TYR A 90  ? 0.28788 0.29033 0.27599 0.03079  -0.02433 -0.00777 90  TYR A OH  
1117 N N   . PHE A 91  ? 0.21630 0.22150 0.21834 0.01947  -0.00734 -0.02281 91  PHE A N   
1118 C CA  . PHE A 91  ? 0.18565 0.19103 0.18975 0.02002  -0.00419 -0.02585 91  PHE A CA  
1119 C C   . PHE A 91  ? 0.21509 0.22155 0.21747 0.02036  0.00112  -0.02414 91  PHE A C   
1120 O O   . PHE A 91  ? 0.21208 0.21787 0.21012 0.02178  0.00438  -0.02662 91  PHE A O   
1121 C CB  . PHE A 91  ? 0.22459 0.23062 0.23866 0.01977  -0.00459 -0.02656 91  PHE A CB  
1122 C CG  . PHE A 91  ? 0.23896 0.24358 0.25429 0.02120  -0.00167 -0.03001 91  PHE A CG  
1123 C CD1 . PHE A 91  ? 0.22563 0.22668 0.23639 0.02129  -0.00286 -0.03479 91  PHE A CD1 
1124 C CD2 . PHE A 91  ? 0.28162 0.28854 0.30222 0.02258  0.00230  -0.02882 91  PHE A CD2 
1125 C CE1 . PHE A 91  ? 0.26626 0.26403 0.27674 0.02290  0.00038  -0.03846 91  PHE A CE1 
1126 C CE2 . PHE A 91  ? 0.24325 0.24827 0.26465 0.02495  0.00564  -0.03194 91  PHE A CE2 
1127 C CZ  . PHE A 91  ? 0.27839 0.27775 0.29396 0.02519  0.00494  -0.03689 91  PHE A CZ  
1128 N N   . PHE A 92  ? 0.21499 0.22312 0.22084 0.01884  0.00239  -0.02012 92  PHE A N   
1129 C CA  . PHE A 92  ? 0.20782 0.21796 0.21338 0.01827  0.00777  -0.01824 92  PHE A CA  
1130 C C   . PHE A 92  ? 0.21616 0.22294 0.20916 0.01925  0.01008  -0.01797 92  PHE A C   
1131 O O   . PHE A 92  ? 0.22468 0.23239 0.21469 0.02032  0.01515  -0.01879 92  PHE A O   
1132 C CB  . PHE A 92  ? 0.20910 0.22095 0.22042 0.01536  0.00801  -0.01442 92  PHE A CB  
1133 C CG  . PHE A 92  ? 0.19385 0.21103 0.21727 0.01474  0.00742  -0.01457 92  PHE A CG  
1134 C CD1 . PHE A 92  ? 0.24219 0.26505 0.27228 0.01585  0.01123  -0.01541 92  PHE A CD1 
1135 C CD2 . PHE A 92  ? 0.33660 0.35339 0.36420 0.01358  0.00327  -0.01364 92  PHE A CD2 
1136 C CE1 . PHE A 92  ? 0.25157 0.28015 0.29271 0.01606  0.01004  -0.01511 92  PHE A CE1 
1137 C CE2 . PHE A 92  ? 0.36456 0.38634 0.40184 0.01346  0.00224  -0.01353 92  PHE A CE2 
1138 C CZ  . PHE A 92  ? 0.29157 0.31943 0.33567 0.01489  0.00526  -0.01419 92  PHE A CZ  
1139 N N   A GLU A 93  ? 0.22885 0.23181 0.21385 0.01957  0.00652  -0.01672 93  GLU A N   
1140 N N   B GLU A 93  ? 0.22958 0.23252 0.21453 0.01955  0.00655  -0.01666 93  GLU A N   
1141 C CA  A GLU A 93  ? 0.27390 0.27333 0.24522 0.02128  0.00790  -0.01603 93  GLU A CA  
1142 C CA  B GLU A 93  ? 0.27834 0.27773 0.24956 0.02129  0.00791  -0.01601 93  GLU A CA  
1143 C C   A GLU A 93  ? 0.25360 0.25287 0.21881 0.02354  0.00772  -0.02111 93  GLU A C   
1144 C C   B GLU A 93  ? 0.25844 0.25771 0.22365 0.02354  0.00773  -0.02110 93  GLU A C   
1145 O O   A GLU A 93  ? 0.28354 0.28114 0.23921 0.02502  0.01193  -0.02145 93  GLU A O   
1146 O O   B GLU A 93  ? 0.28614 0.28368 0.24162 0.02503  0.01185  -0.02143 93  GLU A O   
1147 C CB  A GLU A 93  ? 0.25110 0.24727 0.21610 0.02220  0.00305  -0.01373 93  GLU A CB  
1148 C CB  B GLU A 93  ? 0.25660 0.25270 0.22118 0.02228  0.00307  -0.01374 93  GLU A CB  
1149 C CG  A GLU A 93  ? 0.23982 0.23305 0.20645 0.02036  0.00459  -0.00857 93  GLU A CG  
1150 C CG  B GLU A 93  ? 0.25266 0.24539 0.21758 0.02069  0.00459  -0.00839 93  GLU A CG  
1151 C CD  A GLU A 93  ? 0.31998 0.30913 0.27777 0.02000  0.01051  -0.00469 93  GLU A CD  
1152 C CD  B GLU A 93  ? 0.31257 0.30132 0.26872 0.02032  0.01069  -0.00459 93  GLU A CD  
1153 O OE1 A GLU A 93  ? 0.42495 0.40938 0.37020 0.02262  0.00980  -0.00248 93  GLU A OE1 
1154 O OE1 B GLU A 93  ? 0.25396 0.24290 0.20243 0.02195  0.01378  -0.00590 93  GLU A OE1 
1155 O OE2 A GLU A 93  ? 0.35251 0.34362 0.31604 0.01722  0.01598  -0.00367 93  GLU A OE2 
1156 O OE2 B GLU A 93  ? 0.20088 0.18560 0.15747 0.01821  0.01281  -0.00035 93  GLU A OE2 
1157 N N   . TYR A 94  ? 0.27068 0.27098 0.24089 0.02362  0.00331  -0.02527 94  TYR A N   
1158 C CA  . TYR A 94  ? 0.25450 0.25339 0.21958 0.02504  0.00315  -0.03101 94  TYR A CA  
1159 C C   . TYR A 94  ? 0.23145 0.23056 0.19825 0.02611  0.01008  -0.03237 94  TYR A C   
1160 O O   . TYR A 94  ? 0.31176 0.30839 0.26822 0.02807  0.01322  -0.03501 94  TYR A O   
1161 C CB  . TYR A 94  ? 0.25693 0.25632 0.22974 0.02392  -0.00185 -0.03477 94  TYR A CB  
1162 C CG  . TYR A 94  ? 0.27879 0.27523 0.24861 0.02455  -0.00135 -0.04125 94  TYR A CG  
1163 C CD1 . TYR A 94  ? 0.29199 0.28616 0.24933 0.02528  -0.00404 -0.04553 94  TYR A CD1 
1164 C CD2 . TYR A 94  ? 0.26815 0.26337 0.24674 0.02466  0.00150  -0.04332 94  TYR A CD2 
1165 C CE1 . TYR A 94  ? 0.28961 0.27965 0.24328 0.02538  -0.00378 -0.05241 94  TYR A CE1 
1166 C CE2 . TYR A 94  ? 0.31996 0.31033 0.29516 0.02534  0.00237  -0.04958 94  TYR A CE2 
1167 C CZ  . TYR A 94  ? 0.30236 0.28981 0.26498 0.02537  -0.00017 -0.05442 94  TYR A CZ  
1168 O OH  . TYR A 94  ? 0.35394 0.33533 0.31242 0.02562  0.00067  -0.06132 94  TYR A OH  
1169 N N   . MET A 95  ? 0.24645 0.24898 0.22607 0.02530  0.01258  -0.03052 95  MET A N   
1170 C CA  . MET A 95  ? 0.27797 0.28249 0.26162 0.02703  0.01909  -0.03152 95  MET A CA  
1171 C C   . MET A 95  ? 0.26174 0.26758 0.23917 0.02747  0.02553  -0.02864 95  MET A C   
1172 O O   . MET A 95  ? 0.31499 0.32094 0.28932 0.02991  0.03142  -0.03066 95  MET A O   
1173 C CB  . MET A 95  ? 0.32468 0.33446 0.32379 0.02620  0.01951  -0.02905 95  MET A CB  
1174 C CG  . MET A 95  ? 0.39275 0.40120 0.39904 0.02730  0.01688  -0.03193 95  MET A CG  
1175 S SD  . MET A 95  ? 0.33874 0.35436 0.36074 0.02874  0.01988  -0.02929 95  MET A SD  
1176 C CE  . MET A 95  ? 0.28569 0.30594 0.31300 0.02470  0.01650  -0.02412 95  MET A CE  
1177 N N   . ASN A 96  ? 0.27956 0.28566 0.25474 0.02523  0.02520  -0.02379 96  ASN A N   
1178 C CA  . ASN A 96  ? 0.26669 0.27461 0.23998 0.02440  0.03218  -0.01978 96  ASN A CA  
1179 C C   . ASN A 96  ? 0.38807 0.39032 0.34401 0.02555  0.03407  -0.01825 96  ASN A C   
1180 O O   . ASN A 96  ? 0.37813 0.38085 0.33040 0.02531  0.04137  -0.01522 96  ASN A O   
1181 C CB  . ASN A 96  ? 0.28353 0.29508 0.26783 0.02042  0.03190  -0.01503 96  ASN A CB  
1182 C CG  . ASN A 96  ? 0.25963 0.27815 0.26037 0.01982  0.03105  -0.01605 96  ASN A CG  
1183 O OD1 . ASN A 96  ? 0.26866 0.29049 0.27387 0.02259  0.03389  -0.01890 96  ASN A OD1 
1184 N ND2 . ASN A 96  ? 0.29116 0.31154 0.30017 0.01671  0.02735  -0.01372 96  ASN A ND2 
1185 N N   A SER A 97  ? 0.36429 0.36175 0.30963 0.02690  0.02785  -0.01996 97  SER A N   
1186 N N   B SER A 97  ? 0.36434 0.36180 0.30958 0.02696  0.02791  -0.02008 97  SER A N   
1187 C CA  A SER A 97  ? 0.35412 0.34632 0.28164 0.02886  0.02859  -0.01822 97  SER A CA  
1188 C CA  B SER A 97  ? 0.35567 0.34790 0.28302 0.02896  0.02872  -0.01846 97  SER A CA  
1189 C C   A SER A 97  ? 0.49006 0.48019 0.40577 0.03217  0.03123  -0.02325 97  SER A C   
1190 C C   B SER A 97  ? 0.48928 0.47953 0.40521 0.03224  0.03159  -0.02350 97  SER A C   
1191 O O   A SER A 97  ? 0.48462 0.47481 0.40202 0.03311  0.02761  -0.02940 97  SER A O   
1192 O O   B SER A 97  ? 0.48241 0.47272 0.40020 0.03317  0.02807  -0.02964 97  SER A O   
1193 C CB  A SER A 97  ? 0.46727 0.45680 0.38919 0.02943  0.02007  -0.01770 97  SER A CB  
1194 C CB  B SER A 97  ? 0.46844 0.45797 0.38988 0.02960  0.02012  -0.01815 97  SER A CB  
1195 O OG  A SER A 97  ? 0.47176 0.46192 0.40325 0.02689  0.01804  -0.01344 97  SER A OG  
1196 O OG  B SER A 97  ? 0.47868 0.46938 0.40145 0.03041  0.01395  -0.02441 97  SER A OG  
1197 N N   A ASP A 98  ? 0.59513 0.58246 0.49812 0.03382  0.03798  -0.02066 98  ASP A N   
1198 N N   B ASP A 98  ? 0.59243 0.57996 0.49576 0.03389  0.03841  -0.02095 98  ASP A N   
1199 C CA  A ASP A 98  ? 0.68870 0.67308 0.57784 0.03739  0.04127  -0.02546 98  ASP A CA  
1200 C CA  B ASP A 98  ? 0.68139 0.66599 0.57110 0.03746  0.04181  -0.02577 98  ASP A CA  
1201 C C   A ASP A 98  ? 0.61996 0.60019 0.49452 0.03949  0.03278  -0.02974 98  ASP A C   
1202 C C   B ASP A 98  ? 0.62147 0.60150 0.49509 0.03973  0.03390  -0.02974 98  ASP A C   
1203 O O   A ASP A 98  ? 0.73589 0.71456 0.60600 0.04094  0.03065  -0.03701 98  ASP A O   
1204 O O   B ASP A 98  ? 0.66289 0.64015 0.52635 0.04214  0.03410  -0.03602 98  ASP A O   
1205 C CB  A ASP A 98  ? 0.68645 0.66877 0.56468 0.03870  0.05119  -0.02083 98  ASP A CB  
1206 C CB  B ASP A 98  ? 0.70035 0.68350 0.58067 0.03869  0.05228  -0.02139 98  ASP A CB  
1207 C CG  A ASP A 98  ? 0.77789 0.75600 0.64651 0.03811  0.05042  -0.01367 98  ASP A CG  
1208 C CG  B ASP A 98  ? 0.77226 0.75079 0.64075 0.03844  0.05219  -0.01446 98  ASP A CG  
1209 N N   A ASP A 99  ? 0.56340 0.54183 0.43064 0.03972  0.02773  -0.02549 99  ASP A N   
1210 N N   B ASP A 99  ? 0.55719 0.53660 0.42838 0.03917  0.02686  -0.02650 99  ASP A N   
1211 C CA  A ASP A 99  ? 0.65008 0.62700 0.50566 0.04171  0.01854  -0.02915 99  ASP A CA  
1212 C CA  B ASP A 99  ? 0.63233 0.60988 0.49065 0.04127  0.01816  -0.02991 99  ASP A CA  
1213 C C   A ASP A 99  ? 0.50155 0.48278 0.37193 0.03921  0.00971  -0.03121 99  ASP A C   
1214 C C   B ASP A 99  ? 0.49695 0.47857 0.36868 0.03898  0.00897  -0.03159 99  ASP A C   
1215 O O   A ASP A 99  ? 0.47047 0.45441 0.35669 0.03653  0.01044  -0.02798 99  ASP A O   
1216 O O   B ASP A 99  ? 0.47332 0.45756 0.36018 0.03644  0.00928  -0.02798 99  ASP A O   
1217 C CB  A ASP A 99  ? 0.65144 0.62453 0.49031 0.04458  0.01764  -0.02306 99  ASP A CB  
1218 C CB  B ASP A 99  ? 0.64045 0.61400 0.48139 0.04418  0.01807  -0.02384 99  ASP A CB  
1219 N N   A GLY A 100 ? 0.50132 0.48343 0.36626 0.03993  0.00142  -0.03686 100 GLY A N   
1220 N N   B GLY A 100 ? 0.49639 0.47879 0.36227 0.03973  0.00088  -0.03736 100 GLY A N   
1221 C CA  A GLY A 100 ? 0.32980 0.31659 0.20829 0.03755  -0.00660 -0.03863 100 GLY A CA  
1222 C CA  B GLY A 100 ? 0.32346 0.31050 0.20160 0.03754  -0.00761 -0.03937 100 GLY A CA  
1223 C C   A GLY A 100 ? 0.41736 0.40583 0.30021 0.03789  -0.00888 -0.03117 100 GLY A C   
1224 C C   B GLY A 100 ? 0.42340 0.41249 0.30615 0.03790  -0.01043 -0.03219 100 GLY A C   
1225 O O   A GLY A 100 ? 0.39272 0.37841 0.26317 0.04083  -0.00814 -0.02595 100 GLY A O   
1226 O O   B GLY A 100 ? 0.44600 0.43327 0.31596 0.04110  -0.01177 -0.02788 100 GLY A O   
1227 N N   A ILE A 101 ? 0.32881 0.32078 0.22848 0.03520  -0.01115 -0.03051 101 ILE A N   
1228 N N   B ILE A 101 ? 0.33807 0.33005 0.23804 0.03510  -0.01105 -0.03075 101 ILE A N   
1229 C CA  A ILE A 101 ? 0.28383 0.27662 0.18864 0.03554  -0.01305 -0.02419 101 ILE A CA  
1230 C CA  B ILE A 101 ? 0.29638 0.28929 0.20180 0.03536  -0.01297 -0.02450 101 ILE A CA  
1231 C C   A ILE A 101 ? 0.29907 0.29731 0.21778 0.03370  -0.01950 -0.02666 101 ILE A C   
1232 C C   B ILE A 101 ? 0.29905 0.29761 0.21600 0.03407  -0.02049 -0.02723 101 ILE A C   
1233 O O   A ILE A 101 ? 0.26361 0.26367 0.19292 0.03082  -0.01936 -0.03112 101 ILE A O   
1234 O O   B ILE A 101 ? 0.26211 0.26317 0.18656 0.03164  -0.02245 -0.03313 101 ILE A O   
1235 C CB  A ILE A 101 ? 0.27372 0.26343 0.18439 0.03385  -0.00540 -0.01862 101 ILE A CB  
1236 C CB  B ILE A 101 ? 0.27395 0.26473 0.18850 0.03310  -0.00583 -0.01971 101 ILE A CB  
1237 C CG1 A ILE A 101 ? 0.35895 0.34671 0.27049 0.03473  -0.00700 -0.01220 101 ILE A CG1 
1238 C CG1 B ILE A 101 ? 0.36582 0.35459 0.28162 0.03373  -0.00679 -0.01315 101 ILE A CG1 
1239 C CG2 A ILE A 101 ? 0.35457 0.34707 0.28128 0.03038  -0.00301 -0.02135 101 ILE A CG2 
1240 C CG2 B ILE A 101 ? 0.28729 0.28129 0.21796 0.02984  -0.00501 -0.02322 101 ILE A CG2 
1241 C CD1 A ILE A 101 ? 0.48304 0.46596 0.39580 0.03292  0.00044  -0.00649 101 ILE A CD1 
1242 C CD1 B ILE A 101 ? 0.42549 0.40984 0.34261 0.03184  0.00085  -0.00781 101 ILE A CD1 
1243 N N   A ARG A 102 ? 0.29030 0.29087 0.20861 0.03580  -0.02472 -0.02343 102 ARG A N   
1244 N N   B ARG A 102 ? 0.30447 0.30458 0.22259 0.03590  -0.02423 -0.02277 102 ARG A N   
1245 C CA  A ARG A 102 ? 0.31109 0.31766 0.24224 0.03466  -0.03037 -0.02481 102 ARG A CA  
1246 C CA  B ARG A 102 ? 0.31317 0.31946 0.24302 0.03510  -0.03040 -0.02424 102 ARG A CA  
1247 C C   A ARG A 102 ? 0.24555 0.25080 0.18307 0.03548  -0.02912 -0.01861 102 ARG A C   
1248 C C   B ARG A 102 ? 0.29971 0.30454 0.23837 0.03494  -0.02828 -0.01870 102 ARG A C   
1249 O O   A ARG A 102 ? 0.26348 0.26288 0.19389 0.03726  -0.02527 -0.01309 102 ARG A O   
1250 O O   B ARG A 102 ? 0.26457 0.26343 0.19920 0.03537  -0.02306 -0.01380 102 ARG A O   
1251 C CB  A ARG A 102 ? 0.31172 0.32453 0.23829 0.03680  -0.03872 -0.02777 102 ARG A CB  
1252 C CB  B ARG A 102 ? 0.37460 0.38610 0.29739 0.03847  -0.03830 -0.02515 102 ARG A CB  
1253 C CG  A ARG A 102 ? 0.51118 0.52336 0.42551 0.03698  -0.04033 -0.03337 102 ARG A CG  
1254 C CG  B ARG A 102 ? 0.53348 0.54697 0.44750 0.03807  -0.04194 -0.03199 102 ARG A CG  
1255 C CD  A ARG A 102 ? 0.57128 0.58943 0.49344 0.03356  -0.04613 -0.04117 102 ARG A CD  
1256 C CD  B ARG A 102 ? 0.52400 0.54382 0.45062 0.03390  -0.04672 -0.03900 102 ARG A CD  
1257 N NE  A ARG A 102 ? 0.60386 0.63104 0.53558 0.03387  -0.05325 -0.04066 102 ARG A NE  
1258 N NE  B ARG A 102 ? 0.56649 0.59554 0.50049 0.03487  -0.05427 -0.03861 102 ARG A NE  
1259 C CZ  A ARG A 102 ? 0.74422 0.77892 0.67215 0.03511  -0.06149 -0.04385 102 ARG A CZ  
1260 C CZ  B ARG A 102 ? 0.71789 0.75405 0.64724 0.03594  -0.06224 -0.04239 102 ARG A CZ  
1261 N NH1 A ARG A 102 ? 0.72994 0.76332 0.64284 0.03619  -0.06426 -0.04804 102 ARG A NH1 
1262 N NH1 B ARG A 102 ? 0.72883 0.76288 0.64454 0.03602  -0.06414 -0.04739 102 ARG A NH1 
1263 N NH2 A ARG A 102 ? 0.73444 0.77884 0.67400 0.03537  -0.06715 -0.04300 102 ARG A NH2 
1264 N NH2 B ARG A 102 ? 0.69566 0.74186 0.63430 0.03711  -0.06855 -0.04132 102 ARG A NH2 
1265 N N   . LYS A 103 ? 0.27132 0.28127 0.22215 0.03394  -0.03196 -0.01973 103 LYS A N   
1266 C CA  . LYS A 103 ? 0.26265 0.27048 0.22017 0.03422  -0.03004 -0.01499 103 LYS A CA  
1267 C C   . LYS A 103 ? 0.27484 0.28019 0.22417 0.03904  -0.03153 -0.00953 103 LYS A C   
1268 O O   . LYS A 103 ? 0.30575 0.30472 0.25448 0.03947  -0.02778 -0.00493 103 LYS A O   
1269 C CB  . LYS A 103 ? 0.31845 0.33156 0.29047 0.03212  -0.03221 -0.01712 103 LYS A CB  
1270 C CG  . LYS A 103 ? 0.34187 0.36213 0.31760 0.03466  -0.03805 -0.01718 103 LYS A CG  
1271 C CD  . LYS A 103 ? 0.35681 0.38165 0.34715 0.03219  -0.03848 -0.01870 103 LYS A CD  
1272 C CE  . LYS A 103 ? 0.34862 0.38255 0.34423 0.03476  -0.04393 -0.01871 103 LYS A CE  
1273 N NZ  . LYS A 103 ? 0.42666 0.46407 0.43549 0.03329  -0.04282 -0.01846 103 LYS A NZ  
1274 N N   . LYS A 104 ? 0.29428 0.30397 0.23668 0.04279  -0.03697 -0.00996 104 LYS A N   
1275 C CA  . LYS A 104 ? 0.32401 0.33094 0.25819 0.04856  -0.03844 -0.00411 104 LYS A CA  
1276 C C   . LYS A 104 ? 0.30230 0.29797 0.22346 0.04958  -0.03233 0.00094  104 LYS A C   
1277 O O   . LYS A 104 ? 0.33219 0.32063 0.25059 0.05192  -0.02969 0.00655  104 LYS A O   
1278 C CB  . LYS A 104 ? 0.32681 0.34172 0.25531 0.05286  -0.04608 -0.00552 104 LYS A CB  
1279 C CG  . LYS A 104 ? 0.43448 0.44604 0.35287 0.06025  -0.04766 0.00131  104 LYS A CG  
1280 C CD  . LYS A 104 ? 0.47462 0.49661 0.38913 0.06529  -0.05656 0.00013  104 LYS A CD  
1281 C CE  . LYS A 104 ? 0.57628 0.59274 0.47682 0.07360  -0.05737 0.00768  104 LYS A CE  
1282 N NZ  . LYS A 104 ? 0.57384 0.58263 0.47886 0.07603  -0.05285 0.01355  104 LYS A NZ  
1283 N N   . GLU A 105 ? 0.30496 0.29841 0.21796 0.04774  -0.02944 -0.00101 105 GLU A N   
1284 C CA  . GLU A 105 ? 0.31900 0.30246 0.22064 0.04790  -0.02250 0.00376  105 GLU A CA  
1285 C C   . GLU A 105 ? 0.28904 0.26690 0.19947 0.04364  -0.01626 0.00605  105 GLU A C   
1286 O O   . GLU A 105 ? 0.32610 0.29493 0.23074 0.04432  -0.01189 0.01174  105 GLU A O   
1287 C CB  . GLU A 105 ? 0.33319 0.31674 0.22635 0.04649  -0.01986 0.00038  105 GLU A CB  
1288 C CG  . GLU A 105 ? 0.36117 0.33558 0.24454 0.04583  -0.01134 0.00518  105 GLU A CG  
1289 C CD  . GLU A 105 ? 0.62364 0.59802 0.49634 0.04582  -0.00831 0.00222  105 GLU A CD  
1290 O OE1 . GLU A 105 ? 0.50448 0.48469 0.37488 0.04686  -0.01373 -0.00362 105 GLU A OE1 
1291 O OE2 . GLU A 105 ? 0.58989 0.55835 0.45680 0.04450  -0.00018 0.00550  105 GLU A OE2 
1292 N N   . ILE A 106 ? 0.27540 0.25810 0.19955 0.03914  -0.01592 0.00167  106 ILE A N   
1293 C CA  . ILE A 106 ? 0.25242 0.23153 0.18556 0.03497  -0.01121 0.00306  106 ILE A CA  
1294 C C   . ILE A 106 ? 0.26298 0.23802 0.19877 0.03663  -0.01259 0.00654  106 ILE A C   
1295 O O   . ILE A 106 ? 0.29383 0.26078 0.22820 0.03501  -0.00824 0.01022  106 ILE A O   
1296 C CB  . ILE A 106 ? 0.23792 0.22365 0.18419 0.03105  -0.01160 -0.00223 106 ILE A CB  
1297 C CG1 . ILE A 106 ? 0.24602 0.23389 0.18915 0.02981  -0.00890 -0.00554 106 ILE A CG1 
1298 C CG2 . ILE A 106 ? 0.26302 0.24642 0.21868 0.02717  -0.00812 -0.00098 106 ILE A CG2 
1299 C CD1 . ILE A 106 ? 0.25906 0.25311 0.21275 0.02768  -0.01071 -0.01137 106 ILE A CD1 
1300 N N   . ASN A 107 ? 0.27142 0.25222 0.21233 0.03938  -0.01825 0.00493  107 ASN A N   
1301 C CA  . ASN A 107 ? 0.25294 0.23041 0.19678 0.04180  -0.01926 0.00780  107 ASN A CA  
1302 C C   . ASN A 107 ? 0.27473 0.24251 0.20597 0.04627  -0.01763 0.01381  107 ASN A C   
1303 O O   . ASN A 107 ? 0.30364 0.26213 0.23401 0.04607  -0.01439 0.01706  107 ASN A O   
1304 C CB  . ASN A 107 ? 0.26831 0.25546 0.21958 0.04464  -0.02531 0.00526  107 ASN A CB  
1305 C CG  . ASN A 107 ? 0.24422 0.23821 0.20862 0.04019  -0.02592 0.00039  107 ASN A CG  
1306 O OD1 . ASN A 107 ? 0.28762 0.27841 0.25630 0.03600  -0.02222 -0.00034 107 ASN A OD1 
1307 N ND2 . ASN A 107 ? 0.31246 0.31606 0.28349 0.04118  -0.03072 -0.00271 107 ASN A ND2 
1308 N N   . ASP A 108 ? 0.28277 0.25174 0.20326 0.05054  -0.01991 0.01534  108 ASP A N   
1309 C CA  . ASP A 108 ? 0.30737 0.26675 0.21481 0.05599  -0.01867 0.02177  108 ASP A CA  
1310 C C   . ASP A 108 ? 0.35328 0.29985 0.25377 0.05236  -0.01077 0.02560  108 ASP A C   
1311 O O   . ASP A 108 ? 0.36352 0.29828 0.25625 0.05504  -0.00783 0.03118  108 ASP A O   
1312 C CB  . ASP A 108 ? 0.30573 0.26937 0.20161 0.06130  -0.02293 0.02260  108 ASP A CB  
1313 C CG  . ASP A 108 ? 0.31671 0.29241 0.21796 0.06608  -0.03132 0.02029  108 ASP A CG  
1314 O OD1 . ASP A 108 ? 0.34673 0.32683 0.26004 0.06642  -0.03328 0.01912  108 ASP A OD1 
1315 O OD2 . ASP A 108 ? 0.36158 0.34304 0.25455 0.06953  -0.03606 0.01951  108 ASP A OD2 
1316 N N   . ARG A 109 ? 0.32346 0.27212 0.22645 0.04650  -0.00702 0.02285  109 ARG A N   
1317 C CA  . ARG A 109 ? 0.33876 0.27762 0.23704 0.04228  0.00081  0.02622  109 ARG A CA  
1318 C C   . ARG A 109 ? 0.34849 0.28340 0.25773 0.03661  0.00375  0.02550  109 ARG A C   
1319 O O   . ARG A 109 ? 0.36562 0.28897 0.27063 0.03439  0.00897  0.02959  109 ARG A O   
1320 C CB  . ARG A 109 ? 0.33767 0.28216 0.23520 0.03895  0.00377  0.02337  109 ARG A CB  
1321 C CG  . ARG A 109 ? 0.37078 0.30793 0.26463 0.03428  0.01263  0.02669  109 ARG A CG  
1322 C CD  . ARG A 109 ? 0.36511 0.31025 0.26167 0.03137  0.01549  0.02279  109 ARG A CD  
1323 N NE  . ARG A 109 ? 0.33431 0.28835 0.24762 0.02720  0.01359  0.01725  109 ARG A NE  
1324 C CZ  . ARG A 109 ? 0.35851 0.32131 0.27711 0.02625  0.01315  0.01223  109 ARG A CZ  
1325 N NH1 . ARG A 109 ? 0.42781 0.39206 0.33630 0.02888  0.01427  0.01112  109 ARG A NH1 
1326 N NH2 . ARG A 109 ? 0.37102 0.34040 0.30429 0.02303  0.01157  0.00822  109 ARG A NH2 
1327 N N   . ASP A 110 ? 0.29739 0.24113 0.22003 0.03402  0.00052  0.02032  110 ASP A N   
1328 C CA  . ASP A 110 ? 0.32277 0.26512 0.25577 0.02796  0.00294  0.01859  110 ASP A CA  
1329 C C   . ASP A 110 ? 0.30248 0.24298 0.24105 0.02921  -0.00022 0.01765  110 ASP A C   
1330 O O   . ASP A 110 ? 0.26760 0.20877 0.21479 0.02451  0.00046  0.01518  110 ASP A O   
1331 C CB  . ASP A 110 ? 0.27667 0.22969 0.22023 0.02357  0.00300  0.01374  110 ASP A CB  
1332 C CG  . ASP A 110 ? 0.30668 0.26096 0.24645 0.02138  0.00789  0.01437  110 ASP A CG  
1333 O OD1 . ASP A 110 ? 0.36714 0.31341 0.29635 0.02192  0.01225  0.01887  110 ASP A OD1 
1334 O OD2 . ASP A 110 ? 0.32529 0.28827 0.27244 0.01937  0.00794  0.01051  110 ASP A OD2 
1335 N N   . TYR A 111 ? 0.28007 0.21877 0.21395 0.03572  -0.00360 0.01951  111 TYR A N   
1336 C CA  . TYR A 111 ? 0.28067 0.21968 0.22085 0.03749  -0.00626 0.01803  111 TYR A CA  
1337 C C   . TYR A 111 ? 0.28341 0.21153 0.22439 0.03344  -0.00271 0.01845  111 TYR A C   
1338 O O   . TYR A 111 ? 0.29773 0.22823 0.24628 0.03172  -0.00408 0.01531  111 TYR A O   
1339 C CB  . TYR A 111 ? 0.27268 0.21195 0.20818 0.04576  -0.00980 0.02053  111 TYR A CB  
1340 C CG  . TYR A 111 ? 0.28937 0.21563 0.21182 0.05019  -0.00722 0.02648  111 TYR A CG  
1341 C CD1 . TYR A 111 ? 0.31890 0.24479 0.23112 0.05319  -0.00725 0.02967  111 TYR A CD1 
1342 C CD2 . TYR A 111 ? 0.32379 0.23679 0.24284 0.05178  -0.00452 0.02902  111 TYR A CD2 
1343 C CE1 . TYR A 111 ? 0.37510 0.28788 0.27402 0.05794  -0.00458 0.03600  111 TYR A CE1 
1344 C CE2 . TYR A 111 ? 0.32938 0.22873 0.23587 0.05634  -0.00175 0.03490  111 TYR A CE2 
1345 C CZ  . TYR A 111 ? 0.35135 0.25037 0.24783 0.05939  -0.00161 0.03876  111 TYR A CZ  
1346 O OH  . TYR A 111 ? 0.35898 0.24333 0.24184 0.06443  0.00147  0.04537  111 TYR A OH  
1347 N N   . VAL A 112 ? 0.29799 0.21362 0.23077 0.03159  0.00195  0.02214  112 VAL A N   
1348 C CA  . VAL A 112 ? 0.30941 0.21438 0.24330 0.02658  0.00498  0.02162  112 VAL A CA  
1349 C C   . VAL A 112 ? 0.30253 0.21548 0.24734 0.01890  0.00498  0.01710  112 VAL A C   
1350 O O   . VAL A 112 ? 0.29831 0.21074 0.24838 0.01652  0.00358  0.01399  112 VAL A O   
1351 C CB  . VAL A 112 ? 0.33647 0.22597 0.26021 0.02487  0.01056  0.02639  112 VAL A CB  
1352 C CG1 . VAL A 112 ? 0.35600 0.23471 0.28198 0.01819  0.01327  0.02464  112 VAL A CG1 
1353 C CG2 . VAL A 112 ? 0.38673 0.26716 0.29895 0.03371  0.01032  0.03141  112 VAL A CG2 
1354 N N   . TYR A 113 ? 0.28412 0.20461 0.23191 0.01546  0.00659  0.01677  113 TYR A N   
1355 C CA  . TYR A 113 ? 0.28423 0.21329 0.24305 0.00897  0.00663  0.01296  113 TYR A CA  
1356 C C   . TYR A 113 ? 0.28958 0.22918 0.25656 0.01087  0.00168  0.00893  113 TYR A C   
1357 O O   . TYR A 113 ? 0.26674 0.20923 0.24093 0.00715  0.00043  0.00600  113 TYR A O   
1358 C CB  . TYR A 113 ? 0.29777 0.23342 0.25795 0.00653  0.00982  0.01365  113 TYR A CB  
1359 C CG  . TYR A 113 ? 0.31008 0.25316 0.28144 -0.00039 0.01130  0.01096  113 TYR A CG  
1360 C CD1 . TYR A 113 ? 0.31996 0.25729 0.29267 -0.00697 0.01562  0.01228  113 TYR A CD1 
1361 C CD2 . TYR A 113 ? 0.31731 0.27324 0.29831 -0.00032 0.00842  0.00726  113 TYR A CD2 
1362 C CE1 . TYR A 113 ? 0.33074 0.27681 0.31502 -0.01320 0.01649  0.00986  113 TYR A CE1 
1363 C CE2 . TYR A 113 ? 0.30449 0.26833 0.29624 -0.00576 0.00954  0.00523  113 TYR A CE2 
1364 C CZ  . TYR A 113 ? 0.28772 0.24753 0.28151 -0.01214 0.01331  0.00649  113 TYR A CZ  
1365 O OH  . TYR A 113 ? 0.29956 0.26873 0.30522 -0.01769 0.01412  0.00458  113 TYR A OH  
1366 N N   . LEU A 114 ? 0.25346 0.19858 0.21908 0.01658  -0.00125 0.00884  114 LEU A N   
1367 C CA  . LEU A 114 ? 0.26873 0.22288 0.24199 0.01816  -0.00520 0.00549  114 LEU A CA  
1368 C C   . LEU A 114 ? 0.27459 0.22360 0.24835 0.01921  -0.00652 0.00481  114 LEU A C   
1369 O O   . LEU A 114 ? 0.27026 0.22397 0.25062 0.01762  -0.00821 0.00202  114 LEU A O   
1370 C CB  . LEU A 114 ? 0.26491 0.22545 0.23664 0.02330  -0.00793 0.00549  114 LEU A CB  
1371 C CG  . LEU A 114 ? 0.26839 0.23405 0.23849 0.02253  -0.00684 0.00513  114 LEU A CG  
1372 C CD1 . LEU A 114 ? 0.29118 0.26232 0.25849 0.02740  -0.01046 0.00457  114 LEU A CD1 
1373 C CD2 . LEU A 114 ? 0.32644 0.29939 0.30555 0.01836  -0.00615 0.00186  114 LEU A CD2 
1374 N N   . PHE A 115 ? 0.27232 0.21076 0.23814 0.02234  -0.00540 0.00753  115 PHE A N   
1375 C CA  . PHE A 115 ? 0.29227 0.22373 0.25704 0.02342  -0.00569 0.00665  115 PHE A CA  
1376 C C   . PHE A 115 ? 0.28182 0.20941 0.24901 0.01664  -0.00468 0.00417  115 PHE A C   
1377 O O   . PHE A 115 ? 0.31843 0.24756 0.28875 0.01618  -0.00642 0.00141  115 PHE A O   
1378 C CB  . PHE A 115 ? 0.32945 0.24883 0.28471 0.02851  -0.00407 0.01013  115 PHE A CB  
1379 C CG  . PHE A 115 ? 0.39554 0.30532 0.34815 0.02956  -0.00337 0.00894  115 PHE A CG  
1380 C CD1 . PHE A 115 ? 0.40900 0.32351 0.36470 0.03437  -0.00523 0.00758  115 PHE A CD1 
1381 C CD2 . PHE A 115 ? 0.34626 0.24224 0.29339 0.02524  -0.00053 0.00882  115 PHE A CD2 
1382 C CE1 . PHE A 115 ? 0.41347 0.31830 0.36533 0.03580  -0.00396 0.00623  115 PHE A CE1 
1383 C CE2 . PHE A 115 ? 0.49541 0.38084 0.43847 0.02619  0.00020  0.00699  115 PHE A CE2 
1384 C CZ  . PHE A 115 ? 0.44783 0.33760 0.39270 0.03185  -0.00142 0.00571  115 PHE A CZ  
1385 N N   . TYR A 116 ? 0.30187 0.22532 0.26796 0.01117  -0.00194 0.00505  116 TYR A N   
1386 C CA  . TYR A 116 ? 0.29257 0.21492 0.26292 0.00398  -0.00179 0.00220  116 TYR A CA  
1387 C C   . TYR A 116 ? 0.26101 0.19703 0.24109 0.00248  -0.00503 -0.00104 116 TYR A C   
1388 O O   . TYR A 116 ? 0.26946 0.20542 0.25174 -0.00000 -0.00707 -0.00393 116 TYR A O   
1389 C CB  . TYR A 116 ? 0.33013 0.25016 0.30108 -0.00218 0.00187  0.00371  116 TYR A CB  
1390 C CG  . TYR A 116 ? 0.46765 0.37240 0.42896 -0.00240 0.00601  0.00726  116 TYR A CG  
1391 C CD1 . TYR A 116 ? 0.43015 0.32130 0.38303 0.00122  0.00621  0.00793  116 TYR A CD1 
1392 C CD2 . TYR A 116 ? 0.54590 0.44913 0.50611 -0.00592 0.01042  0.01026  116 TYR A CD2 
1393 C CE1 . TYR A 116 ? 0.48320 0.35830 0.42639 0.00141  0.01053  0.01172  116 TYR A CE1 
1394 C CE2 . TYR A 116 ? 0.52702 0.41489 0.47758 -0.00616 0.01487  0.01422  116 TYR A CE2 
1395 C CZ  . TYR A 116 ? 0.55938 0.43277 0.50133 -0.00241 0.01478  0.01502  116 TYR A CZ  
1396 O OH  . TYR A 116 ? 0.74420 0.60052 0.67575 -0.00213 0.01963  0.01945  116 TYR A OH  
1397 N N   . ILE A 117 ? 0.25176 0.19877 0.23685 0.00406  -0.00548 -0.00066 117 ILE A N   
1398 C CA  . ILE A 117 ? 0.24940 0.20791 0.24313 0.00344  -0.00807 -0.00321 117 ILE A CA  
1399 C C   . ILE A 117 ? 0.27845 0.23686 0.27169 0.00709  -0.01081 -0.00462 117 ILE A C   
1400 O O   . ILE A 117 ? 0.26272 0.22413 0.25940 0.00546  -0.01282 -0.00674 117 ILE A O   
1401 C CB  . ILE A 117 ? 0.25544 0.22308 0.25282 0.00538  -0.00760 -0.00273 117 ILE A CB  
1402 C CG1 . ILE A 117 ? 0.24836 0.21735 0.24697 0.00149  -0.00414 -0.00158 117 ILE A CG1 
1403 C CG2 . ILE A 117 ? 0.24226 0.21964 0.24729 0.00654  -0.01020 -0.00501 117 ILE A CG2 
1404 C CD1 . ILE A 117 ? 0.25108 0.22682 0.25055 0.00387  -0.00299 -0.00131 117 ILE A CD1 
1405 N N   . CYS A 118 ? 0.26568 0.22156 0.25482 0.01234  -0.01083 -0.00324 118 CYS A N   
1406 C CA  . CYS A 118 ? 0.25987 0.21676 0.24943 0.01609  -0.01243 -0.00417 118 CYS A CA  
1407 C C   . CYS A 118 ? 0.30513 0.25236 0.28916 0.01556  -0.01218 -0.00524 118 CYS A C   
1408 O O   . CYS A 118 ? 0.26841 0.21694 0.25304 0.01678  -0.01331 -0.00677 118 CYS A O   
1409 C CB  . CYS A 118 ? 0.26912 0.22749 0.25731 0.02173  -0.01249 -0.00241 118 CYS A CB  
1410 S SG  . CYS A 118 ? 0.31466 0.28502 0.30930 0.02217  -0.01378 -0.00274 118 CYS A SG  
1411 N N   . LEU A 119 ? 0.26620 0.20280 0.24406 0.01363  -0.01038 -0.00454 119 LEU A N   
1412 C CA  . LEU A 119 ? 0.28207 0.20745 0.25359 0.01238  -0.01004 -0.00636 119 LEU A CA  
1413 C C   . LEU A 119 ? 0.28730 0.21594 0.26215 0.00661  -0.01234 -0.00969 119 LEU A C   
1414 O O   . LEU A 119 ? 0.28123 0.20755 0.25313 0.00731  -0.01382 -0.01206 119 LEU A O   
1415 C CB  . LEU A 119 ? 0.29471 0.20637 0.25870 0.01127  -0.00714 -0.00471 119 LEU A CB  
1416 C CG  . LEU A 119 ? 0.35724 0.25491 0.31343 0.01009  -0.00650 -0.00721 119 LEU A CG  
1417 C CD1 . LEU A 119 ? 0.35107 0.24652 0.30326 0.01759  -0.00637 -0.00747 119 LEU A CD1 
1418 C CD2 . LEU A 119 ? 0.36220 0.24450 0.31097 0.00826  -0.00306 -0.00538 119 LEU A CD2 
1419 N N   . SER A 120 ? 0.27821 0.21324 0.25928 0.00130  -0.01273 -0.00983 120 SER A N   
1420 C CA  . SER A 120 ? 0.25837 0.19997 0.24474 -0.00354 -0.01568 -0.01269 120 SER A CA  
1421 C C   . SER A 120 ? 0.23881 0.18880 0.22798 0.00024  -0.01830 -0.01344 120 SER A C   
1422 O O   . SER A 120 ? 0.26059 0.21001 0.24762 -0.00066 -0.02093 -0.01586 120 SER A O   
1423 C CB  . SER A 120 ? 0.25821 0.20856 0.25305 -0.00802 -0.01493 -0.01183 120 SER A CB  
1424 O OG  . SER A 120 ? 0.28767 0.24651 0.28935 -0.01224 -0.01807 -0.01428 120 SER A OG  
1425 N N   . ASN A 121 ? 0.23822 0.19535 0.23145 0.00437  -0.01755 -0.01139 121 ASN A N   
1426 C CA  . ASN A 121 ? 0.22797 0.19183 0.22398 0.00784  -0.01908 -0.01151 121 ASN A CA  
1427 C C   . ASN A 121 ? 0.24219 0.19926 0.23101 0.01148  -0.01885 -0.01207 121 ASN A C   
1428 O O   . ASN A 121 ? 0.25492 0.21403 0.24279 0.01243  -0.02045 -0.01303 121 ASN A O   
1429 C CB  . ASN A 121 ? 0.23201 0.20260 0.23312 0.01086  -0.01783 -0.00961 121 ASN A CB  
1430 C CG  . ASN A 121 ? 0.22423 0.20118 0.22924 0.01353  -0.01877 -0.00952 121 ASN A CG  
1431 O OD1 . ASN A 121 ? 0.25062 0.23312 0.25987 0.01226  -0.02034 -0.01003 121 ASN A OD1 
1432 N ND2 . ASN A 121 ? 0.23865 0.21465 0.24238 0.01741  -0.01759 -0.00863 121 ASN A ND2 
1433 N N   . PHE A 122 ? 0.25819 0.20683 0.24125 0.01402  -0.01659 -0.01129 122 PHE A N   
1434 C CA  . PHE A 122 ? 0.25692 0.19869 0.23298 0.01796  -0.01553 -0.01193 122 PHE A CA  
1435 C C   . PHE A 122 ? 0.26466 0.19939 0.23383 0.01498  -0.01720 -0.01516 122 PHE A C   
1436 O O   . PHE A 122 ? 0.28535 0.21935 0.25035 0.01734  -0.01758 -0.01624 122 PHE A O   
1437 C CB  . PHE A 122 ? 0.26421 0.19831 0.23576 0.02199  -0.01271 -0.01031 122 PHE A CB  
1438 C CG  . PHE A 122 ? 0.33975 0.26675 0.30434 0.02662  -0.01087 -0.01107 122 PHE A CG  
1439 C CD1 . PHE A 122 ? 0.34661 0.28044 0.31442 0.03111  -0.00977 -0.01001 122 PHE A CD1 
1440 C CD2 . PHE A 122 ? 0.47611 0.38935 0.43093 0.02616  -0.00981 -0.01310 122 PHE A CD2 
1441 C CE1 . PHE A 122 ? 0.42287 0.35077 0.38430 0.03569  -0.00720 -0.01062 122 PHE A CE1 
1442 C CE2 . PHE A 122 ? 0.37538 0.28149 0.32280 0.03100  -0.00755 -0.01417 122 PHE A CE2 
1443 C CZ  . PHE A 122 ? 0.42319 0.33724 0.37407 0.03599  -0.00607 -0.01277 122 PHE A CZ  
1444 N N   . PHE A 123 ? 0.28092 0.21081 0.24878 0.00938  -0.01828 -0.01688 123 PHE A N   
1445 C CA  . PHE A 123 ? 0.26820 0.19223 0.23003 0.00552  -0.02082 -0.02078 123 PHE A CA  
1446 C C   . PHE A 123 ? 0.27728 0.21191 0.24304 0.00440  -0.02478 -0.02186 123 PHE A C   
1447 O O   . PHE A 123 ? 0.29627 0.22753 0.25479 0.00489  -0.02685 -0.02441 123 PHE A O   
1448 C CB  . PHE A 123 ? 0.30909 0.22680 0.27075 -0.00137 -0.02104 -0.02241 123 PHE A CB  
1449 C CG  . PHE A 123 ? 0.35902 0.26139 0.31264 0.00003  -0.01717 -0.02186 123 PHE A CG  
1450 C CD1 . PHE A 123 ? 0.50614 0.39942 0.45094 0.00625  -0.01501 -0.02206 123 PHE A CD1 
1451 C CD2 . PHE A 123 ? 0.38249 0.27969 0.33748 -0.00420 -0.01512 -0.02059 123 PHE A CD2 
1452 C CE1 . PHE A 123 ? 0.69298 0.57181 0.63039 0.00863  -0.01129 -0.02119 123 PHE A CE1 
1453 C CE2 . PHE A 123 ? 0.41980 0.30172 0.36660 -0.00216 -0.01133 -0.01940 123 PHE A CE2 
1454 C CZ  . PHE A 123 ? 0.42414 0.29680 0.36221 0.00447  -0.00965 -0.01977 123 PHE A CZ  
1455 N N   . MET A 124 ? 0.23892 0.18572 0.21509 0.00332  -0.02583 -0.01995 124 MET A N   
1456 C CA  . MET A 124 ? 0.27732 0.23399 0.25725 0.00385  -0.02921 -0.02005 124 MET A CA  
1457 C C   . MET A 124 ? 0.24446 0.19948 0.21844 0.00975  -0.02820 -0.01905 124 MET A C   
1458 O O   . MET A 124 ? 0.27630 0.23128 0.24482 0.01040  -0.03091 -0.02045 124 MET A O   
1459 C CB  . MET A 124 ? 0.23566 0.20393 0.22715 0.00379  -0.02888 -0.01754 124 MET A CB  
1460 C CG  . MET A 124 ? 0.24941 0.22721 0.24501 0.00538  -0.03194 -0.01697 124 MET A CG  
1461 S SD  . MET A 124 ? 0.25164 0.24019 0.25910 0.00699  -0.03026 -0.01410 124 MET A SD  
1462 C CE  . MET A 124 ? 0.21916 0.20361 0.22390 0.01230  -0.02626 -0.01183 124 MET A CE  
1463 N N   . LEU A 125 ? 0.24663 0.20085 0.22168 0.01407  -0.02428 -0.01650 125 LEU A N   
1464 C CA  . LEU A 125 ? 0.25436 0.20838 0.22588 0.01924  -0.02230 -0.01503 125 LEU A CA  
1465 C C   . LEU A 125 ? 0.26573 0.20925 0.22500 0.02115  -0.02135 -0.01718 125 LEU A C   
1466 O O   . LEU A 125 ? 0.28418 0.22710 0.23757 0.02400  -0.02116 -0.01705 125 LEU A O   
1467 C CB  . LEU A 125 ? 0.24864 0.20527 0.22577 0.02252  -0.01854 -0.01231 125 LEU A CB  
1468 C CG  . LEU A 125 ? 0.27942 0.24558 0.26725 0.02147  -0.01894 -0.01052 125 LEU A CG  
1469 C CD1 . LEU A 125 ? 0.26261 0.23105 0.25500 0.02429  -0.01600 -0.00868 125 LEU A CD1 
1470 C CD2 . LEU A 125 ? 0.25034 0.22252 0.24110 0.02191  -0.02040 -0.00957 125 LEU A CD2 
1471 N N   . LEU A 126 ? 0.29443 0.22856 0.24881 0.02010  -0.02015 -0.01899 126 LEU A N   
1472 C CA  . LEU A 126 ? 0.29697 0.21928 0.23860 0.02216  -0.01883 -0.02165 126 LEU A CA  
1473 C C   . LEU A 126 ? 0.32558 0.24621 0.25987 0.01902  -0.02337 -0.02523 126 LEU A C   
1474 O O   . LEU A 126 ? 0.31627 0.23233 0.24034 0.02224  -0.02283 -0.02647 126 LEU A O   
1475 C CB  . LEU A 126 ? 0.31556 0.22650 0.25314 0.02105  -0.01698 -0.02310 126 LEU A CB  
1476 C CG  . LEU A 126 ? 0.39868 0.29477 0.32218 0.02275  -0.01544 -0.02668 126 LEU A CG  
1477 C CD1 . LEU A 126 ? 0.45731 0.35284 0.37641 0.03047  -0.01106 -0.02504 126 LEU A CD1 
1478 C CD2 . LEU A 126 ? 0.45993 0.34394 0.38053 0.02146  -0.01333 -0.02742 126 LEU A CD2 
1479 N N   . ILE A 127 ? 0.30108 0.22622 0.24050 0.01284  -0.02794 -0.02690 127 ILE A N   
1480 C CA  . ILE A 127 ? 0.30922 0.23522 0.24328 0.00946  -0.03351 -0.03051 127 ILE A CA  
1481 C C   . ILE A 127 ? 0.31833 0.25273 0.25190 0.01358  -0.03502 -0.02817 127 ILE A C   
1482 O O   . ILE A 127 ? 0.31430 0.24501 0.23662 0.01516  -0.03718 -0.03024 127 ILE A O   
1483 C CB  . ILE A 127 ? 0.28972 0.22173 0.23270 0.00187  -0.03781 -0.03229 127 ILE A CB  
1484 C CG1 . ILE A 127 ? 0.32821 0.24823 0.26812 -0.00267 -0.03599 -0.03501 127 ILE A CG1 
1485 C CG2 . ILE A 127 ? 0.32571 0.26362 0.26654 -0.00118 -0.04471 -0.03542 127 ILE A CG2 
1486 C CD1 . ILE A 127 ? 0.32986 0.25537 0.28073 -0.01011 -0.03759 -0.03536 127 ILE A CD1 
1487 N N   . GLY A 128 ? 0.27595 0.22060 0.22056 0.01551  -0.03369 -0.02381 128 GLY A N   
1488 C CA  . GLY A 128 ? 0.28846 0.23915 0.23252 0.01979  -0.03398 -0.02081 128 GLY A CA  
1489 C C   . GLY A 128 ? 0.29148 0.23479 0.22479 0.02533  -0.02952 -0.01976 128 GLY A C   
1490 O O   . GLY A 128 ? 0.30019 0.24311 0.22506 0.02809  -0.03075 -0.01925 128 GLY A O   
1491 N N   . TYR A 129 ? 0.27391 0.21166 0.20724 0.02742  -0.02411 -0.01917 129 TYR A N   
1492 C CA  . TYR A 129 ? 0.28957 0.22159 0.21434 0.03296  -0.01892 -0.01798 129 TYR A CA  
1493 C C   . TYR A 129 ? 0.31978 0.24167 0.22796 0.03357  -0.02043 -0.02208 129 TYR A C   
1494 O O   . TYR A 129 ? 0.34260 0.26239 0.24102 0.03754  -0.01882 -0.02116 129 TYR A O   
1495 C CB  . TYR A 129 ? 0.29038 0.21960 0.21959 0.03522  -0.01350 -0.01692 129 TYR A CB  
1496 C CG  . TYR A 129 ? 0.34549 0.27055 0.26813 0.04121  -0.00735 -0.01551 129 TYR A CG  
1497 C CD1 . TYR A 129 ? 0.35285 0.28522 0.28183 0.04417  -0.00348 -0.01119 129 TYR A CD1 
1498 C CD2 . TYR A 129 ? 0.41847 0.33204 0.32883 0.04377  -0.00492 -0.01854 129 TYR A CD2 
1499 C CE1 . TYR A 129 ? 0.36863 0.29853 0.29304 0.04932  0.00287  -0.00958 129 TYR A CE1 
1500 C CE2 . TYR A 129 ? 0.41747 0.32808 0.32226 0.04984  0.00156  -0.01708 129 TYR A CE2 
1501 C CZ  . TYR A 129 ? 0.40353 0.32328 0.31619 0.05241  0.00548  -0.01238 129 TYR A CZ  
1502 O OH  . TYR A 129 ? 0.62498 0.54311 0.53365 0.05805  0.01262  -0.01060 129 TYR A OH  
1503 N N   . LEU A 130 ? 0.29686 0.21169 0.20092 0.02941  -0.02339 -0.02676 130 LEU A N   
1504 C CA  . LEU A 130 ? 0.36011 0.26466 0.24804 0.02871  -0.02596 -0.03192 130 LEU A CA  
1505 C C   . LEU A 130 ? 0.35751 0.26789 0.24021 0.02805  -0.03191 -0.03243 130 LEU A C   
1506 O O   . LEU A 130 ? 0.38140 0.28544 0.24880 0.03104  -0.03211 -0.03433 130 LEU A O   
1507 C CB  . LEU A 130 ? 0.35939 0.25606 0.24648 0.02269  -0.02863 -0.03686 130 LEU A CB  
1508 C CG  . LEU A 130 ? 0.38273 0.27016 0.27090 0.02444  -0.02273 -0.03653 130 LEU A CG  
1509 C CD1 . LEU A 130 ? 0.42648 0.30628 0.31482 0.01761  -0.02544 -0.04058 130 LEU A CD1 
1510 C CD2 . LEU A 130 ? 0.42229 0.29781 0.29671 0.03105  -0.01702 -0.03770 130 LEU A CD2 
1511 N N   . GLY A 131 ? 0.32974 0.25222 0.22437 0.02481  -0.03667 -0.03060 131 GLY A N   
1512 C CA  . GLY A 131 ? 0.33157 0.26083 0.22217 0.02528  -0.04262 -0.03031 131 GLY A CA  
1513 C C   . GLY A 131 ? 0.32928 0.26073 0.21590 0.03217  -0.03875 -0.02486 131 GLY A C   
1514 O O   . GLY A 131 ? 0.36624 0.29624 0.24017 0.03502  -0.04139 -0.02501 131 GLY A O   
1515 N N   A GLU A 132 ? 0.33117 0.26618 0.22848 0.03456  -0.03269 -0.01999 132 GLU A N   
1516 N N   B GLU A 132 ? 0.33458 0.26908 0.23137 0.03468  -0.03244 -0.02006 132 GLU A N   
1517 C CA  A GLU A 132 ? 0.33895 0.27627 0.23494 0.04001  -0.02840 -0.01439 132 GLU A CA  
1518 C CA  B GLU A 132 ? 0.35587 0.29130 0.24978 0.04044  -0.02751 -0.01475 132 GLU A CA  
1519 C C   A GLU A 132 ? 0.36485 0.29238 0.24489 0.04479  -0.02323 -0.01455 132 GLU A C   
1520 C C   B GLU A 132 ? 0.40171 0.32662 0.27893 0.04479  -0.02283 -0.01578 132 GLU A C   
1521 O O   A GLU A 132 ? 0.39407 0.32122 0.26597 0.04908  -0.02153 -0.01106 132 GLU A O   
1522 O O   B GLU A 132 ? 0.43037 0.35367 0.29662 0.04893  -0.02191 -0.01337 132 GLU A O   
1523 C CB  A GLU A 132 ? 0.37139 0.31427 0.28322 0.04025  -0.02318 -0.01026 132 GLU A CB  
1524 C CB  B GLU A 132 ? 0.31359 0.25402 0.22256 0.04105  -0.02175 -0.01053 132 GLU A CB  
1525 C CG  A GLU A 132 ? 0.36776 0.31397 0.28212 0.04421  -0.01903 -0.00434 132 GLU A CG  
1526 C CG  B GLU A 132 ? 0.36069 0.30422 0.27113 0.04512  -0.01764 -0.00469 132 GLU A CG  
1527 C CD  A GLU A 132 ? 0.36760 0.31825 0.27950 0.04536  -0.02415 -0.00217 132 GLU A CD  
1528 C CD  B GLU A 132 ? 0.32731 0.27538 0.23541 0.04592  -0.02310 -0.00273 132 GLU A CD  
1529 O OE1 A GLU A 132 ? 0.27375 0.23174 0.19531 0.04251  -0.02938 -0.00279 132 GLU A OE1 
1530 O OE1 B GLU A 132 ? 0.33455 0.28928 0.25088 0.04259  -0.02910 -0.00421 132 GLU A OE1 
1531 O OE2 A GLU A 132 ? 0.39424 0.34116 0.29438 0.04966  -0.02257 0.00053  132 GLU A OE2 
1532 O OE2 B GLU A 132 ? 0.38064 0.32579 0.27853 0.05028  -0.02114 0.00059  132 GLU A OE2 
1533 N N   A THR A 133 ? 0.36912 0.28802 0.24385 0.04455  -0.02026 -0.01835 133 THR A N   
1534 N N   B THR A 133 ? 0.37055 0.28761 0.24485 0.04442  -0.01947 -0.01916 133 THR A N   
1535 C CA  A THR A 133 ? 0.34233 0.25109 0.20143 0.04942  -0.01472 -0.01931 133 THR A CA  
1536 C CA  B THR A 133 ? 0.40275 0.30874 0.26055 0.04872  -0.01481 -0.02114 133 THR A CA  
1537 C C   A THR A 133 ? 0.42466 0.32432 0.26518 0.04855  -0.01985 -0.02542 133 THR A C   
1538 C C   B THR A 133 ? 0.42291 0.32102 0.26348 0.04712  -0.02097 -0.02720 133 THR A C   
1539 O O   A THR A 133 ? 0.45130 0.34075 0.27651 0.05256  -0.01546 -0.02737 133 THR A O   
1540 O O   B THR A 133 ? 0.44590 0.33253 0.27145 0.04989  -0.01768 -0.03062 133 THR A O   
1541 C CB  A THR A 133 ? 0.37636 0.28075 0.24041 0.05108  -0.00761 -0.01956 133 THR A CB  
1542 C CB  B THR A 133 ? 0.41105 0.31133 0.27255 0.04987  -0.00870 -0.02233 133 THR A CB  
1543 O OG1 A THR A 133 ? 0.39400 0.29402 0.26056 0.04664  -0.01112 -0.02434 133 THR A OG1 
1544 O OG1 B THR A 133 ? 0.36717 0.26504 0.23352 0.04448  -0.01318 -0.02653 133 THR A OG1 
1545 C CG2 A THR A 133 ? 0.42888 0.34300 0.31057 0.05192  -0.00294 -0.01394 133 THR A CG2 
1546 C CG2 B THR A 133 ? 0.39331 0.30211 0.27063 0.05196  -0.00269 -0.01661 133 THR A CG2 
1547 N N   A LYS A 134 ? 0.41237 0.31587 0.25420 0.04331  -0.02897 -0.02875 134 LYS A N   
1548 N N   B LYS A 134 ? 0.42137 0.32574 0.26424 0.04269  -0.02984 -0.02892 134 LYS A N   
1549 C CA  A LYS A 134 ? 0.44800 0.34565 0.27317 0.04167  -0.03581 -0.03463 134 LYS A CA  
1550 C CA  B LYS A 134 ? 0.43816 0.33785 0.26622 0.04031  -0.03745 -0.03489 134 LYS A CA  
1551 C C   A LYS A 134 ? 0.44820 0.33217 0.26358 0.03915  -0.03520 -0.04187 134 LYS A C   
1552 C C   B LYS A 134 ? 0.48360 0.37017 0.30276 0.03717  -0.03739 -0.04224 134 LYS A C   
1553 O O   A LYS A 134 ? 0.51315 0.38765 0.30971 0.03990  -0.03754 -0.04696 134 LYS A O   
1554 O O   B LYS A 134 ? 0.52147 0.39997 0.32363 0.03639  -0.04158 -0.04798 134 LYS A O   
1555 C CB  A LYS A 134 ? 0.51805 0.41393 0.32639 0.04768  -0.03542 -0.03231 134 LYS A CB  
1556 C CB  B LYS A 134 ? 0.53107 0.42847 0.34150 0.04610  -0.03756 -0.03314 134 LYS A CB  
1557 C CG  A LYS A 134 ? 0.55535 0.46295 0.37234 0.05035  -0.03608 -0.02483 134 LYS A CG  
1558 C CG  B LYS A 134 ? 0.55524 0.46439 0.37295 0.04872  -0.03921 -0.02617 134 LYS A CG  
1559 C CD  A LYS A 134 ? 0.66604 0.57093 0.46421 0.05605  -0.03694 -0.02260 134 LYS A CD  
1560 C CD  B LYS A 134 ? 0.66977 0.57461 0.46914 0.05559  -0.03681 -0.02293 134 LYS A CD  
1561 C CE  A LYS A 134 ? 0.69849 0.61175 0.50386 0.05989  -0.03516 -0.01410 134 LYS A CE  
1562 C CE  B LYS A 134 ? 0.67601 0.59081 0.48107 0.05837  -0.03910 -0.01596 134 LYS A CE  
1563 N NZ  A LYS A 134 ? 0.70645 0.61640 0.49176 0.06577  -0.03659 -0.01145 134 LYS A NZ  
1564 N NZ  B LYS A 134 ? 0.71144 0.62089 0.49725 0.06541  -0.03619 -0.01193 134 LYS A NZ  
1565 N N   A GLN A 135 ? 0.45240 0.33442 0.27955 0.03622  -0.03224 -0.04247 135 GLN A N   
1566 N N   B GLN A 135 ? 0.47009 0.35364 0.29975 0.03548  -0.03283 -0.04224 135 GLN A N   
1567 C CA  A GLN A 135 ? 0.50438 0.37272 0.32435 0.03315  -0.03186 -0.04895 135 GLN A CA  
1568 C CA  B GLN A 135 ? 0.50335 0.37283 0.32509 0.03273  -0.03216 -0.04867 135 GLN A CA  
1569 C C   A GLN A 135 ? 0.60007 0.46964 0.42357 0.02411  -0.04074 -0.05442 135 GLN A C   
1570 C C   B GLN A 135 ? 0.59109 0.46121 0.41514 0.02380  -0.04112 -0.05444 135 GLN A C   
1571 O O   A GLN A 135 ? 0.59956 0.45613 0.41239 0.02056  -0.04237 -0.06128 135 GLN A O   
1572 O O   B GLN A 135 ? 0.58564 0.44283 0.39748 0.02059  -0.04306 -0.06143 135 GLN A O   
1573 C CB  A GLN A 135 ? 0.49105 0.35604 0.32098 0.03526  -0.02405 -0.04624 135 GLN A CB  
1574 C CB  B GLN A 135 ? 0.49430 0.36062 0.32632 0.03456  -0.02461 -0.04602 135 GLN A CB  
1575 C CG  A GLN A 135 ? 0.44248 0.30804 0.27075 0.04368  -0.01534 -0.04115 135 GLN A CG  
1576 C CG  B GLN A 135 ? 0.63963 0.48824 0.45919 0.03613  -0.02029 -0.05093 135 GLN A CG  
1577 C CD  A GLN A 135 ? 0.70596 0.57068 0.54496 0.04652  -0.00832 -0.03821 135 GLN A CD  
1578 C CD  B GLN A 135 ? 0.61190 0.45861 0.43946 0.04127  -0.01178 -0.04689 135 GLN A CD  
1579 O OE1 A GLN A 135 ? 0.59445 0.46999 0.44672 0.04891  -0.00487 -0.03235 135 GLN A OE1 
1580 O OE1 B GLN A 135 ? 0.70748 0.56307 0.54226 0.04651  -0.00687 -0.04108 135 GLN A OE1 
1581 N NE2 A GLN A 135 ? 0.64997 0.50136 0.48263 0.04663  -0.00615 -0.04232 135 GLN A NE2 
1582 N NE2 B GLN A 135 ? 0.75076 0.58582 0.57719 0.03977  -0.01007 -0.04989 135 GLN A NE2 
1583 N N   A ILE A 136 ? 0.50248 0.38723 0.34094 0.02031  -0.04613 -0.05163 136 ILE A N   
1584 N N   B ILE A 136 ? 0.49692 0.38183 0.33680 0.01960  -0.04629 -0.05180 136 ILE A N   
1585 C CA  A ILE A 136 ? 0.43966 0.33008 0.28372 0.01190  -0.05504 -0.05603 136 ILE A CA  
1586 C CA  B ILE A 136 ? 0.45353 0.34346 0.29800 0.01119  -0.05524 -0.05650 136 ILE A CA  
1587 C C   A ILE A 136 ? 0.48526 0.39104 0.33298 0.01304  -0.06154 -0.05315 136 ILE A C   
1588 C C   B ILE A 136 ? 0.47187 0.37777 0.32121 0.01209  -0.06171 -0.05348 136 ILE A C   
1589 O O   A ILE A 136 ? 0.46662 0.37841 0.31608 0.01948  -0.05823 -0.04688 136 ILE A O   
1590 O O   B ILE A 136 ? 0.46076 0.37333 0.31304 0.01833  -0.05845 -0.04706 136 ILE A O   
1591 C CB  A ILE A 136 ? 0.42719 0.32182 0.28954 0.00594  -0.05416 -0.05501 136 ILE A CB  
1592 C CB  B ILE A 136 ? 0.45229 0.34509 0.31383 0.00464  -0.05467 -0.05626 136 ILE A CB  
1593 C CG1 A ILE A 136 ? 0.35257 0.25916 0.23057 0.00977  -0.04996 -0.04717 136 ILE A CG1 
1594 C CG1 B ILE A 136 ? 0.51003 0.39990 0.37869 0.00918  -0.04565 -0.05104 136 ILE A CG1 
1595 C CG2 A ILE A 136 ? 0.41383 0.29187 0.27140 0.00431  -0.04881 -0.05818 136 ILE A CG2 
1596 C CG2 B ILE A 136 ? 0.56460 0.44542 0.42019 -0.00310 -0.05757 -0.06393 136 ILE A CG2 
1597 C CD1 A ILE A 136 ? 0.37827 0.29092 0.27342 0.00420  -0.04981 -0.04592 136 ILE A CD1 
1598 C CD1 B ILE A 136 ? 0.49824 0.37001 0.35573 0.01112  -0.03978 -0.05398 136 ILE A CD1 
1599 N N   A ASN A 137 ? 0.47049 0.38279 0.31999 0.00670  -0.07086 -0.05767 137 ASN A N   
1600 N N   B ASN A 137 ? 0.46445 0.37654 0.31524 0.00571  -0.07095 -0.05812 137 ASN A N   
1601 C CA  A ASN A 137 ? 0.43902 0.36605 0.29104 0.00868  -0.07780 -0.05502 137 ASN A CA  
1602 C CA  B ASN A 137 ? 0.43405 0.36159 0.28874 0.00710  -0.07815 -0.05563 137 ASN A CA  
1603 C C   A ASN A 137 ? 0.48124 0.42405 0.35526 0.00829  -0.07746 -0.04898 137 ASN A C   
1604 C C   B ASN A 137 ? 0.49253 0.43496 0.36880 0.00734  -0.07676 -0.04914 137 ASN A C   
1605 O O   A ASN A 137 ? 0.44807 0.39175 0.33583 0.00451  -0.07368 -0.04816 137 ASN A O   
1606 O O   B ASN A 137 ? 0.41837 0.36060 0.30736 0.00425  -0.07218 -0.04796 137 ASN A O   
1607 C CB  A ASN A 137 ? 0.48414 0.41451 0.33015 0.00265  -0.08883 -0.06221 137 ASN A CB  
1608 C CB  B ASN A 137 ? 0.51127 0.44333 0.36371 -0.00021 -0.08900 -0.06277 137 ASN A CB  
1609 C CG  A ASN A 137 ? 0.57193 0.50828 0.43417 -0.00756 -0.09282 -0.06616 137 ASN A CG  
1610 C CG  B ASN A 137 ? 0.54178 0.47738 0.41051 -0.00997 -0.09067 -0.06603 137 ASN A CG  
1611 O OD1 A ASN A 137 ? 0.50339 0.45546 0.38431 -0.00944 -0.09494 -0.06256 137 ASN A OD1 
1612 O OD1 B ASN A 137 ? 0.52301 0.47455 0.40990 -0.01267 -0.09368 -0.06325 137 ASN A OD1 
1613 N ND2 A ASN A 137 ? 0.72412 0.64728 0.57901 -0.01422 -0.09336 -0.07359 137 ASN A ND2 
1614 N ND2 B ASN A 137 ? 0.64620 0.56621 0.50824 -0.01504 -0.08801 -0.07169 137 ASN A ND2 
1615 N N   A LYS A 138 ? 0.50890 0.46352 0.38503 0.01281  -0.08130 -0.04462 138 LYS A N   
1616 N N   B LYS A 138 ? 0.48682 0.44157 0.36601 0.01154  -0.08074 -0.04489 138 LYS A N   
1617 C CA  A LYS A 138 ? 0.41829 0.38663 0.31341 0.01402  -0.08027 -0.03862 138 LYS A CA  
1618 C CA  B LYS A 138 ? 0.40246 0.37028 0.30037 0.01296  -0.07910 -0.03873 138 LYS A CA  
1619 C C   A LYS A 138 ? 0.45785 0.43653 0.37016 0.00595  -0.08470 -0.04146 138 LYS A C   
1620 C C   B LYS A 138 ? 0.45741 0.43676 0.37262 0.00527  -0.08403 -0.04124 138 LYS A C   
1621 O O   A LYS A 138 ? 0.39880 0.38301 0.32676 0.00490  -0.08052 -0.03816 138 LYS A O   
1622 O O   B LYS A 138 ? 0.39662 0.38212 0.32755 0.00443  -0.08008 -0.03779 138 LYS A O   
1623 C CB  A LYS A 138 ? 0.49184 0.46956 0.38444 0.02062  -0.08422 -0.03378 138 LYS A CB  
1624 C CB  B LYS A 138 ? 0.50364 0.47947 0.39859 0.02030  -0.08152 -0.03328 138 LYS A CB  
1625 C CG  A LYS A 138 ? 0.47911 0.44909 0.36112 0.02898  -0.07701 -0.02800 138 LYS A CG  
1626 C CG  B LYS A 138 ? 0.47797 0.46078 0.36529 0.01979  -0.09218 -0.03651 138 LYS A CG  
1627 C CD  A LYS A 138 ? 0.58481 0.56448 0.47047 0.03525  -0.07878 -0.02127 138 LYS A CD  
1628 C CD  B LYS A 138 ? 0.51769 0.50284 0.39469 0.02871  -0.09346 -0.03092 138 LYS A CD  
1629 C CE  A LYS A 138 ? 0.71307 0.68455 0.59194 0.04215  -0.06967 -0.01496 138 LYS A CE  
1630 C CE  B LYS A 138 ? 0.58872 0.57971 0.45492 0.02852  -0.10484 -0.03484 138 LYS A CE  
1631 N NZ  A LYS A 138 ? 0.56395 0.54275 0.45562 0.04592  -0.06693 -0.00799 138 LYS A NZ  
1632 N NZ  B LYS A 138 ? 0.56068 0.55136 0.41241 0.03788  -0.10606 -0.02934 138 LYS A NZ  
1633 N N   A MET A 139 ? 0.43747 0.41914 0.34710 -0.00006 -0.09308 -0.04775 139 MET A N   
1634 N N   B MET A 139 ? 0.44820 0.43094 0.36090 -0.00060 -0.09248 -0.04736 139 MET A N   
1635 C CA  A MET A 139 ? 0.45259 0.44596 0.37998 -0.00821 -0.09724 -0.05024 139 MET A CA  
1636 C CA  B MET A 139 ? 0.42750 0.42148 0.35767 -0.00890 -0.09647 -0.04998 139 MET A CA  
1637 C C   A MET A 139 ? 0.41298 0.39721 0.34680 -0.01405 -0.09044 -0.05175 139 MET A C   
1638 C C   B MET A 139 ? 0.42536 0.40966 0.36126 -0.01450 -0.08952 -0.05142 139 MET A C   
1639 O O   A MET A 139 ? 0.43534 0.42818 0.38629 -0.01695 -0.08806 -0.04929 139 MET A O   
1640 O O   B MET A 139 ? 0.43129 0.42344 0.38382 -0.01703 -0.08658 -0.04871 139 MET A O   
1641 C CB  A MET A 139 ? 0.50763 0.50672 0.43116 -0.01413 -0.10809 -0.05714 139 MET A CB  
1642 C CB  B MET A 139 ? 0.53657 0.53559 0.46268 -0.01503 -0.10706 -0.05701 139 MET A CB  
1643 C CG  A MET A 139 ? 0.65119 0.66972 0.59588 -0.02037 -0.11399 -0.05790 139 MET A CG  
1644 C CG  B MET A 139 ? 0.52363 0.53066 0.46648 -0.02577 -0.10991 -0.06113 139 MET A CG  
1645 S SD  A MET A 139 ? 0.92208 0.95155 0.86445 -0.02705 -0.12829 -0.06583 139 MET A SD  
1646 S SD  B MET A 139 ? 0.84533 0.86545 0.78917 -0.03295 -0.12399 -0.06859 139 MET A SD  
1647 C CE  A MET A 139 ? 0.66173 0.67667 0.57392 -0.01979 -0.13111 -0.06784 139 MET A CE  
1648 C CE  B MET A 139 ? 0.73724 0.77830 0.68755 -0.02315 -0.12978 -0.06185 139 MET A CE  
1649 N N   A LEU A 140 ? 0.44618 0.41236 0.36560 -0.01496 -0.08671 -0.05537 140 LEU A N   
1650 N N   B LEU A 140 ? 0.44587 0.41238 0.36715 -0.01581 -0.08644 -0.05544 140 LEU A N   
1651 C CA  A LEU A 140 ? 0.41046 0.36606 0.33395 -0.01911 -0.07985 -0.05606 140 LEU A CA  
1652 C CA  B LEU A 140 ? 0.41657 0.37189 0.34112 -0.01954 -0.07932 -0.05597 140 LEU A CA  
1653 C C   A LEU A 140 ? 0.41457 0.37203 0.34679 -0.01356 -0.07178 -0.04892 140 LEU A C   
1654 C C   B LEU A 140 ? 0.42084 0.37719 0.35271 -0.01346 -0.07115 -0.04885 140 LEU A C   
1655 O O   A LEU A 140 ? 0.41623 0.37466 0.35991 -0.01713 -0.06794 -0.04750 140 LEU A O   
1656 O O   B LEU A 140 ? 0.39530 0.35099 0.33734 -0.01652 -0.06665 -0.04733 140 LEU A O   
1657 C CB  A LEU A 140 ? 0.48958 0.42468 0.39437 -0.01918 -0.07717 -0.06090 140 LEU A CB  
1658 C CB  B LEU A 140 ? 0.47719 0.41224 0.38313 -0.02011 -0.07718 -0.06119 140 LEU A CB  
1659 C CG  A LEU A 140 ? 0.50450 0.42613 0.41089 -0.02244 -0.07008 -0.06153 140 LEU A CG  
1660 C CG  B LEU A 140 ? 0.52452 0.44546 0.43131 -0.02461 -0.07103 -0.06289 140 LEU A CG  
1661 C CD1 A LEU A 140 ? 0.59274 0.52058 0.51388 -0.03239 -0.07250 -0.06356 140 LEU A CD1 
1662 C CD1 B LEU A 140 ? 0.53633 0.44974 0.44149 -0.01705 -0.06173 -0.05740 140 LEU A CD1 
1663 C CD2 A LEU A 140 ? 0.56109 0.46193 0.44822 -0.02218 -0.06805 -0.06702 140 LEU A CD2 
1664 C CD2 B LEU A 140 ? 0.57213 0.50227 0.49691 -0.03311 -0.07226 -0.06287 140 LEU A CD2 
1665 N N   . THR A 141 ? 0.39266 0.35029 0.31907 -0.00505 -0.06906 -0.04445 141 THR A N   
1666 C CA  . THR A 141 ? 0.35616 0.31579 0.29063 -0.00014 -0.06197 -0.03826 141 THR A CA  
1667 C C   . THR A 141 ? 0.30526 0.28020 0.25786 -0.00194 -0.06333 -0.03516 141 THR A C   
1668 O O   . THR A 141 ? 0.31976 0.29555 0.28206 -0.00281 -0.05843 -0.03275 141 THR A O   
1669 C CB  . THR A 141 ? 0.37387 0.33202 0.29954 0.00833  -0.05942 -0.03426 141 THR A CB  
1670 O OG1 . THR A 141 ? 0.38134 0.32587 0.28941 0.01052  -0.05781 -0.03724 141 THR A OG1 
1671 C CG2 . THR A 141 ? 0.31261 0.27180 0.24662 0.01246  -0.05198 -0.02868 141 THR A CG2 
1672 N N   A LEU A 142 ? 0.33111 0.31845 0.28815 -0.00222 -0.07005 -0.03529 142 LEU A N   
1673 N N   B LEU A 142 ? 0.33839 0.32576 0.29519 -0.00175 -0.06991 -0.03502 142 LEU A N   
1674 C CA  A LEU A 142 ? 0.35805 0.36034 0.33230 -0.00263 -0.07079 -0.03212 142 LEU A CA  
1675 C CA  B LEU A 142 ? 0.36087 0.36329 0.33480 -0.00208 -0.07076 -0.03183 142 LEU A CA  
1676 C C   A LEU A 142 ? 0.33703 0.34325 0.32323 -0.01095 -0.07088 -0.03482 142 LEU A C   
1677 C C   B LEU A 142 ? 0.33692 0.34343 0.32285 -0.01037 -0.07094 -0.03456 142 LEU A C   
1678 O O   A LEU A 142 ? 0.34307 0.35546 0.34179 -0.01127 -0.06699 -0.03186 142 LEU A O   
1679 O O   B LEU A 142 ? 0.35088 0.36343 0.34929 -0.01072 -0.06702 -0.03162 142 LEU A O   
1680 C CB  A LEU A 142 ? 0.35571 0.37064 0.33160 0.00047  -0.07794 -0.03108 142 LEU A CB  
1681 C CB  B LEU A 142 ? 0.35867 0.37368 0.33408 0.00107  -0.07796 -0.03078 142 LEU A CB  
1682 C CG  A LEU A 142 ? 0.33061 0.34316 0.29761 0.00953  -0.07636 -0.02630 142 LEU A CG  
1683 C CG  B LEU A 142 ? 0.32202 0.35267 0.31435 0.00303  -0.07847 -0.02681 142 LEU A CG  
1684 C CD1 A LEU A 142 ? 0.36890 0.39234 0.33452 0.01227  -0.08471 -0.02596 142 LEU A CD1 
1685 C CD1 B LEU A 142 ? 0.29226 0.31950 0.28724 0.00888  -0.07084 -0.02138 142 LEU A CD1 
1686 C CD2 A LEU A 142 ? 0.33854 0.35330 0.31519 0.01393  -0.06962 -0.02058 142 LEU A CD2 
1687 C CD2 B LEU A 142 ? 0.29363 0.33639 0.28638 0.00672  -0.08638 -0.02589 142 LEU A CD2 
1688 N N   A PHE A 143 ? 0.35959 0.36148 0.34159 -0.01796 -0.07479 -0.04050 143 PHE A N   
1689 N N   B PHE A 143 ? 0.35291 0.35541 0.33469 -0.01734 -0.07503 -0.04025 143 PHE A N   
1690 C CA  A PHE A 143 ? 0.39466 0.39946 0.38823 -0.02662 -0.07409 -0.04275 143 PHE A CA  
1691 C CA  B PHE A 143 ? 0.39607 0.40049 0.38867 -0.02607 -0.07418 -0.04267 143 PHE A CA  
1692 C C   A PHE A 143 ? 0.35031 0.34143 0.34161 -0.02772 -0.06589 -0.04159 143 PHE A C   
1693 C C   B PHE A 143 ? 0.35109 0.34296 0.34229 -0.02628 -0.06563 -0.04081 143 PHE A C   
1694 O O   A PHE A 143 ? 0.36107 0.35642 0.36385 -0.03082 -0.06207 -0.03961 143 PHE A O   
1695 O O   B PHE A 143 ? 0.31907 0.31646 0.32198 -0.02744 -0.06148 -0.03782 143 PHE A O   
1696 C CB  A PHE A 143 ? 0.47442 0.47945 0.46569 -0.03485 -0.08118 -0.04948 143 PHE A CB  
1697 C CB  B PHE A 143 ? 0.44057 0.44096 0.42788 -0.03418 -0.08012 -0.04968 143 PHE A CB  
1698 C CG  A PHE A 143 ? 0.44151 0.46606 0.44295 -0.03601 -0.08960 -0.05034 143 PHE A CG  
1699 C CG  B PHE A 143 ? 0.44801 0.44551 0.44387 -0.04371 -0.07754 -0.05209 143 PHE A CG  
1700 C CD1 A PHE A 143 ? 0.47160 0.51301 0.49271 -0.03825 -0.08935 -0.04787 143 PHE A CD1 
1701 C CD1 B PHE A 143 ? 0.54521 0.55889 0.55982 -0.04855 -0.07831 -0.05093 143 PHE A CD1 
1702 C CD2 A PHE A 143 ? 0.54472 0.57132 0.53581 -0.03409 -0.09767 -0.05336 143 PHE A CD2 
1703 C CD2 B PHE A 143 ? 0.52111 0.49931 0.50640 -0.04734 -0.07346 -0.05498 143 PHE A CD2 
1704 C CE1 A PHE A 143 ? 0.53497 0.59581 0.56675 -0.03841 -0.09712 -0.04833 143 PHE A CE1 
1705 C CE1 B PHE A 143 ? 0.56512 0.57579 0.58760 -0.05753 -0.07488 -0.05250 143 PHE A CE1 
1706 C CE2 A PHE A 143 ? 0.54945 0.59522 0.55013 -0.03429 -0.10607 -0.05376 143 PHE A CE2 
1707 C CE2 B PHE A 143 ? 0.52482 0.49882 0.51736 -0.05601 -0.07030 -0.05645 143 PHE A CE2 
1708 C CZ  A PHE A 143 ? 0.62399 0.68736 0.64580 -0.03635 -0.10584 -0.05118 143 PHE A CZ  
1709 C CZ  B PHE A 143 ? 0.54377 0.53403 0.55484 -0.06140 -0.07088 -0.05511 143 PHE A CZ  
1710 N N   . GLY A 144 ? 0.36434 0.33932 0.34062 -0.02465 -0.06292 -0.04253 144 GLY A N   
1711 C CA  . GLY A 144 ? 0.39458 0.35719 0.36843 -0.02429 -0.05552 -0.04088 144 GLY A CA  
1712 C C   . GLY A 144 ? 0.36130 0.32897 0.34171 -0.01812 -0.05036 -0.03496 144 GLY A C   
1713 O O   . GLY A 144 ? 0.32768 0.29419 0.31422 -0.01967 -0.04580 -0.03285 144 GLY A O   
1714 N N   . GLY A 145 ? 0.28787 0.26049 0.26632 -0.01123 -0.05093 -0.03228 145 GLY A N   
1715 C CA  . GLY A 145 ? 0.27709 0.25433 0.26202 -0.00608 -0.04640 -0.02731 145 GLY A CA  
1716 C C   . GLY A 145 ? 0.28052 0.27069 0.28031 -0.00839 -0.04657 -0.02549 145 GLY A C   
1717 O O   . GLY A 145 ? 0.29117 0.28170 0.29632 -0.00754 -0.04195 -0.02296 145 GLY A O   
1718 N N   . SER A 146 ? 0.27556 0.27696 0.28204 -0.01110 -0.05195 -0.02690 146 SER A N   
1719 C CA  . SER A 146 ? 0.23826 0.25301 0.25975 -0.01297 -0.05169 -0.02530 146 SER A CA  
1720 C C   . SER A 146 ? 0.27283 0.28503 0.29953 -0.01978 -0.04835 -0.02640 146 SER A C   
1721 O O   . SER A 146 ? 0.25928 0.27654 0.29452 -0.01961 -0.04424 -0.02389 146 SER A O   
1722 C CB  . SER A 146 ? 0.37774 0.40641 0.40609 -0.01391 -0.05853 -0.02651 146 SER A CB  
1723 O OG  . SER A 146 ? 0.39657 0.42773 0.42024 -0.00664 -0.06092 -0.02425 146 SER A OG  
1724 N N   . PHE A 147 ? 0.29358 0.29647 0.31406 -0.02565 -0.04950 -0.03006 147 PHE A N   
1725 C CA  . PHE A 147 ? 0.29692 0.29445 0.32067 -0.03200 -0.04531 -0.03045 147 PHE A CA  
1726 C C   . PHE A 147 ? 0.30528 0.29523 0.32602 -0.02778 -0.03846 -0.02663 147 PHE A C   
1727 O O   . PHE A 147 ? 0.27844 0.27256 0.30679 -0.02940 -0.03448 -0.02435 147 PHE A O   
1728 C CB  . PHE A 147 ? 0.31031 0.29480 0.32519 -0.03819 -0.04682 -0.03493 147 PHE A CB  
1729 C CG  . PHE A 147 ? 0.34382 0.31910 0.35978 -0.04401 -0.04136 -0.03449 147 PHE A CG  
1730 C CD1 . PHE A 147 ? 0.42159 0.40499 0.44953 -0.05225 -0.04130 -0.03540 147 PHE A CD1 
1731 C CD2 . PHE A 147 ? 0.35306 0.31249 0.35872 -0.04080 -0.03599 -0.03261 147 PHE A CD2 
1732 C CE1 . PHE A 147 ? 0.52550 0.49956 0.55380 -0.05763 -0.03548 -0.03430 147 PHE A CE1 
1733 C CE2 . PHE A 147 ? 0.38385 0.33386 0.38933 -0.04539 -0.03075 -0.03140 147 PHE A CE2 
1734 C CZ  . PHE A 147 ? 0.48026 0.43684 0.49648 -0.05395 -0.03023 -0.03212 147 PHE A CZ  
1735 N N   . PHE A 148 ? 0.26592 0.24550 0.27557 -0.02209 -0.03707 -0.02588 148 PHE A N   
1736 C CA  . PHE A 148 ? 0.24279 0.21663 0.24995 -0.01779 -0.03158 -0.02248 148 PHE A CA  
1737 C C   . PHE A 148 ? 0.24676 0.23172 0.26205 -0.01347 -0.03017 -0.01933 148 PHE A C   
1738 O O   . PHE A 148 ? 0.25256 0.23675 0.26969 -0.01259 -0.02604 -0.01702 148 PHE A O   
1739 C CB  . PHE A 148 ? 0.28209 0.24314 0.27691 -0.01317 -0.03031 -0.02269 148 PHE A CB  
1740 C CG  . PHE A 148 ? 0.27432 0.22105 0.26078 -0.01711 -0.02930 -0.02514 148 PHE A CG  
1741 C CD1 . PHE A 148 ? 0.32487 0.26399 0.31072 -0.01906 -0.02489 -0.02336 148 PHE A CD1 
1742 C CD2 . PHE A 148 ? 0.31913 0.25922 0.29769 -0.01905 -0.03266 -0.02928 148 PHE A CD2 
1743 C CE1 . PHE A 148 ? 0.35471 0.27880 0.33256 -0.02274 -0.02346 -0.02540 148 PHE A CE1 
1744 C CE2 . PHE A 148 ? 0.34771 0.27271 0.31800 -0.02303 -0.03144 -0.03210 148 PHE A CE2 
1745 C CZ  . PHE A 148 ? 0.32859 0.24522 0.29886 -0.02489 -0.02666 -0.03003 148 PHE A CZ  
1746 N N   . LEU A 149 ? 0.22736 0.22166 0.24655 -0.01051 -0.03338 -0.01918 149 LEU A N   
1747 C CA  . LEU A 149 ? 0.22370 0.22731 0.25081 -0.00683 -0.03169 -0.01659 149 LEU A CA  
1748 C C   . LEU A 149 ? 0.21486 0.22623 0.25193 -0.01089 -0.02974 -0.01621 149 LEU A C   
1749 O O   . LEU A 149 ? 0.23896 0.25174 0.27879 -0.00917 -0.02574 -0.01431 149 LEU A O   
1750 C CB  . LEU A 149 ? 0.21742 0.22905 0.24719 -0.00319 -0.03547 -0.01625 149 LEU A CB  
1751 C CG  . LEU A 149 ? 0.20196 0.22203 0.23991 0.00070  -0.03360 -0.01386 149 LEU A CG  
1752 C CD1 . LEU A 149 ? 0.25771 0.27165 0.29132 0.00524  -0.03008 -0.01210 149 LEU A CD1 
1753 C CD2 . LEU A 149 ? 0.27557 0.30525 0.31831 0.00334  -0.03788 -0.01339 149 LEU A CD2 
1754 N N   A PHE A 150 ? 0.23200 0.24893 0.27456 -0.01644 -0.03249 -0.01820 150 PHE A N   
1755 N N   B PHE A 150 ? 0.23179 0.24824 0.27410 -0.01662 -0.03235 -0.01822 150 PHE A N   
1756 C CA  A PHE A 150 ? 0.24098 0.26611 0.29407 -0.02094 -0.02996 -0.01776 150 PHE A CA  
1757 C CA  B PHE A 150 ? 0.24062 0.26589 0.29385 -0.02093 -0.02993 -0.01773 150 PHE A CA  
1758 C C   A PHE A 150 ? 0.24023 0.25562 0.28886 -0.02326 -0.02423 -0.01642 150 PHE A C   
1759 C C   B PHE A 150 ? 0.25567 0.27160 0.30512 -0.02419 -0.02438 -0.01665 150 PHE A C   
1760 O O   A PHE A 150 ? 0.20708 0.22637 0.26007 -0.02238 -0.01978 -0.01432 150 PHE A O   
1761 O O   B PHE A 150 ? 0.22359 0.24464 0.27922 -0.02511 -0.02007 -0.01488 150 PHE A O   
1762 C CB  A PHE A 150 ? 0.24303 0.27519 0.30278 -0.02762 -0.03427 -0.02059 150 PHE A CB  
1763 C CB  B PHE A 150 ? 0.25402 0.28815 0.31497 -0.02690 -0.03454 -0.02040 150 PHE A CB  
1764 C CG  A PHE A 150 ? 0.26553 0.31008 0.33100 -0.02477 -0.04028 -0.02134 150 PHE A CG  
1765 C CG  B PHE A 150 ? 0.26890 0.31791 0.33859 -0.02335 -0.03898 -0.02021 150 PHE A CG  
1766 C CD1 A PHE A 150 ? 0.26784 0.31730 0.33457 -0.01697 -0.04010 -0.01884 150 PHE A CD1 
1767 C CD1 B PHE A 150 ? 0.34551 0.39313 0.40862 -0.01767 -0.04316 -0.02014 150 PHE A CD1 
1768 C CD2 A PHE A 150 ? 0.26717 0.31806 0.33643 -0.02982 -0.04623 -0.02451 150 PHE A CD2 
1769 C CD2 B PHE A 150 ? 0.28935 0.35363 0.37370 -0.02514 -0.03848 -0.01967 150 PHE A CD2 
1770 C CE1 A PHE A 150 ? 0.30759 0.36727 0.37856 -0.01348 -0.04534 -0.01876 150 PHE A CE1 
1771 C CE1 B PHE A 150 ? 0.32352 0.38370 0.39355 -0.01359 -0.04716 -0.01929 150 PHE A CE1 
1772 C CE2 A PHE A 150 ? 0.25586 0.31863 0.32960 -0.02636 -0.05231 -0.02477 150 PHE A CE2 
1773 C CE2 B PHE A 150 ? 0.32155 0.39965 0.41409 -0.02084 -0.04265 -0.01910 150 PHE A CE2 
1774 C CZ  A PHE A 150 ? 0.31283 0.37972 0.38719 -0.01780 -0.05167 -0.02152 150 PHE A CZ  
1775 C CZ  B PHE A 150 ? 0.30782 0.38337 0.39275 -0.01489 -0.04715 -0.01876 150 PHE A CZ  
1776 N N   . LEU A 151 ? 0.24650 0.24828 0.28519 -0.02549 -0.02407 -0.01747 151 LEU A N   
1777 C CA  . LEU A 151 ? 0.23975 0.23091 0.27306 -0.02734 -0.01883 -0.01571 151 LEU A CA  
1778 C C   . LEU A 151 ? 0.24948 0.23915 0.27911 -0.02080 -0.01552 -0.01275 151 LEU A C   
1779 O O   . LEU A 151 ? 0.25888 0.24835 0.28924 -0.02133 -0.01101 -0.01052 151 LEU A O   
1780 C CB  . LEU A 151 ? 0.29350 0.26906 0.31603 -0.02965 -0.01937 -0.01739 151 LEU A CB  
1781 C CG  . LEU A 151 ? 0.27735 0.23953 0.29223 -0.03003 -0.01395 -0.01487 151 LEU A CG  
1782 C CD1 . LEU A 151 ? 0.32135 0.28656 0.34316 -0.03661 -0.00997 -0.01357 151 LEU A CD1 
1783 C CD2 . LEU A 151 ? 0.31414 0.26000 0.31793 -0.03092 -0.01440 -0.01663 151 LEU A CD2 
1784 N N   . THR A 152 ? 0.22487 0.21433 0.25086 -0.01481 -0.01774 -0.01280 152 THR A N   
1785 C CA  . THR A 152 ? 0.21224 0.20122 0.23563 -0.00920 -0.01544 -0.01071 152 THR A CA  
1786 C C   . THR A 152 ? 0.22245 0.22172 0.25385 -0.00872 -0.01331 -0.00980 152 THR A C   
1787 O O   . THR A 152 ? 0.23284 0.23046 0.26196 -0.00765 -0.00971 -0.00817 152 THR A O   
1788 C CB  . THR A 152 ? 0.23087 0.21995 0.25170 -0.00401 -0.01814 -0.01118 152 THR A CB  
1789 O OG1 . THR A 152 ? 0.24313 0.22214 0.25558 -0.00358 -0.01917 -0.01198 152 THR A OG1 
1790 C CG2 . THR A 152 ? 0.22553 0.21614 0.24591 0.00091  -0.01634 -0.00968 152 THR A CG2 
1791 N N   . PHE A 153 ? 0.20161 0.21140 0.24181 -0.00916 -0.01546 -0.01083 153 PHE A N   
1792 C CA  . PHE A 153 ? 0.19458 0.21404 0.24256 -0.00766 -0.01311 -0.01015 153 PHE A CA  
1793 C C   . PHE A 153 ? 0.21767 0.24011 0.27003 -0.01233 -0.00897 -0.00936 153 PHE A C   
1794 O O   . PHE A 153 ? 0.22184 0.24757 0.27582 -0.01060 -0.00492 -0.00832 153 PHE A O   
1795 C CB  . PHE A 153 ? 0.21568 0.24489 0.27132 -0.00526 -0.01654 -0.01094 153 PHE A CB  
1796 C CG  . PHE A 153 ? 0.20448 0.23101 0.25631 0.00051  -0.01765 -0.01064 153 PHE A CG  
1797 C CD1 . PHE A 153 ? 0.22135 0.24089 0.26609 0.00186  -0.02037 -0.01090 153 PHE A CD1 
1798 C CD2 . PHE A 153 ? 0.23637 0.26626 0.29113 0.00435  -0.01525 -0.01022 153 PHE A CD2 
1799 C CE1 . PHE A 153 ? 0.26319 0.28040 0.30527 0.00654  -0.02060 -0.01034 153 PHE A CE1 
1800 C CE2 . PHE A 153 ? 0.25834 0.28479 0.30999 0.00871  -0.01591 -0.01012 153 PHE A CE2 
1801 C CZ  . PHE A 153 ? 0.25864 0.27907 0.30441 0.00953  -0.01848 -0.00997 153 PHE A CZ  
1802 N N   . TYR A 154 ? 0.22294 0.24363 0.27674 -0.01847 -0.00952 -0.00997 154 TYR A N   
1803 C CA  . TYR A 154 ? 0.26459 0.28689 0.32247 -0.02381 -0.00465 -0.00879 154 TYR A CA  
1804 C C   . TYR A 154 ? 0.23040 0.24167 0.27779 -0.02249 0.00029  -0.00630 154 TYR A C   
1805 O O   . TYR A 154 ? 0.24049 0.25473 0.28931 -0.02258 0.00550  -0.00451 154 TYR A O   
1806 C CB  . TYR A 154 ? 0.25847 0.27885 0.31910 -0.03145 -0.00651 -0.01036 154 TYR A CB  
1807 C CG  . TYR A 154 ? 0.31018 0.33012 0.37447 -0.03787 -0.00061 -0.00875 154 TYR A CG  
1808 C CD1 . TYR A 154 ? 0.41113 0.44554 0.48865 -0.04021 0.00226  -0.00826 154 TYR A CD1 
1809 C CD2 . TYR A 154 ? 0.34353 0.34833 0.39793 -0.04100 0.00275  -0.00727 154 TYR A CD2 
1810 C CE1 . TYR A 154 ? 0.35994 0.39435 0.44124 -0.04630 0.00862  -0.00640 154 TYR A CE1 
1811 C CE2 . TYR A 154 ? 0.42287 0.42607 0.47997 -0.04704 0.00905  -0.00513 154 TYR A CE2 
1812 C CZ  . TYR A 154 ? 0.40679 0.42518 0.47751 -0.04988 0.01212  -0.00471 154 TYR A CZ  
1813 O OH  . TYR A 154 ? 0.55291 0.57051 0.62712 -0.05619 0.01930  -0.00227 154 TYR A OH  
1814 N N   . LEU A 155 ? 0.26196 0.26060 0.29828 -0.02076 -0.00119 -0.00601 155 LEU A N   
1815 C CA  . LEU A 155 ? 0.25333 0.24191 0.27896 -0.01812 0.00247  -0.00333 155 LEU A CA  
1816 C C   . LEU A 155 ? 0.24868 0.24250 0.27331 -0.01248 0.00377  -0.00270 155 LEU A C   
1817 O O   . LEU A 155 ? 0.24258 0.23412 0.26239 -0.01170 0.00815  -0.00055 155 LEU A O   
1818 C CB  . LEU A 155 ? 0.25867 0.23509 0.27415 -0.01548 -0.00008 -0.00330 155 LEU A CB  
1819 C CG  . LEU A 155 ? 0.29117 0.25799 0.30403 -0.02082 -0.00042 -0.00406 155 LEU A CG  
1820 C CD1 . LEU A 155 ? 0.34401 0.30008 0.34744 -0.01667 -0.00294 -0.00450 155 LEU A CD1 
1821 C CD2 . LEU A 155 ? 0.33884 0.29787 0.34823 -0.02508 0.00523  -0.00121 155 LEU A CD2 
1822 N N   A LEU A 156 ? 0.23828 0.23793 0.26622 -0.00850 0.00009  -0.00462 156 LEU A N   
1823 N N   B LEU A 156 ? 0.24211 0.24238 0.27061 -0.00860 0.00021  -0.00465 156 LEU A N   
1824 C CA  A LEU A 156 ? 0.23547 0.23982 0.26336 -0.00394 0.00115  -0.00494 156 LEU A CA  
1825 C CA  B LEU A 156 ? 0.24075 0.24476 0.26813 -0.00384 0.00132  -0.00484 156 LEU A CA  
1826 C C   A LEU A 156 ? 0.20253 0.21448 0.23628 -0.00545 0.00584  -0.00452 156 LEU A C   
1827 C C   B LEU A 156 ? 0.23923 0.25218 0.27369 -0.00477 0.00538  -0.00487 156 LEU A C   
1828 O O   A LEU A 156 ? 0.20745 0.21801 0.23578 -0.00351 0.00957  -0.00359 156 LEU A O   
1829 O O   B LEU A 156 ? 0.24938 0.26279 0.28003 -0.00179 0.00821  -0.00475 156 LEU A O   
1830 C CB  A LEU A 156 ? 0.22212 0.23137 0.25474 -0.00077 -0.00303 -0.00701 156 LEU A CB  
1831 C CB  B LEU A 156 ? 0.25481 0.26125 0.28396 0.00020  -0.00297 -0.00674 156 LEU A CB  
1832 C CG  A LEU A 156 ? 0.20061 0.21388 0.23423 0.00349  -0.00239 -0.00813 156 LEU A CG  
1833 C CG  B LEU A 156 ? 0.17053 0.17326 0.19289 0.00471  -0.00387 -0.00699 156 LEU A CG  
1834 C CD1 A LEU A 156 ? 0.23397 0.24115 0.25798 0.00592  -0.00147 -0.00770 156 LEU A CD1 
1835 C CD1 B LEU A 156 ? 0.38500 0.38329 0.40476 0.00629  -0.00758 -0.00722 156 LEU A CD1 
1836 C CD2 A LEU A 156 ? 0.25360 0.26924 0.29118 0.00604  -0.00619 -0.00948 156 LEU A CD2 
1837 C CD2 B LEU A 156 ? 0.35358 0.36220 0.37976 0.00751  -0.00347 -0.00881 156 LEU A CD2 
1838 N N   . TYR A 157 ? 0.22632 0.24695 0.27110 -0.00868 0.00566  -0.00525 157 TYR A N   
1839 C CA  . TYR A 157 ? 0.22479 0.25548 0.27801 -0.00915 0.01000  -0.00509 157 TYR A CA  
1840 C C   . TYR A 157 ? 0.23018 0.25740 0.27919 -0.01219 0.01647  -0.00266 157 TYR A C   
1841 O O   . TYR A 157 ? 0.25617 0.28547 0.30298 -0.00962 0.02126  -0.00210 157 TYR A O   
1842 C CB  . TYR A 157 ? 0.21205 0.25385 0.27894 -0.01237 0.00783  -0.00606 157 TYR A CB  
1843 C CG  . TYR A 157 ? 0.23806 0.29235 0.31553 -0.01114 0.01204  -0.00599 157 TYR A CG  
1844 C CD1 . TYR A 157 ? 0.28045 0.33911 0.36263 -0.01538 0.01817  -0.00441 157 TYR A CD1 
1845 C CD2 . TYR A 157 ? 0.24374 0.30467 0.32614 -0.00537 0.01058  -0.00726 157 TYR A CD2 
1846 C CE1 . TYR A 157 ? 0.22905 0.30000 0.32155 -0.01366 0.02276  -0.00428 157 TYR A CE1 
1847 C CE2 . TYR A 157 ? 0.24621 0.31820 0.33823 -0.00318 0.01490  -0.00721 157 TYR A CE2 
1848 C CZ  . TYR A 157 ? 0.23370 0.31129 0.33100 -0.00718 0.02102  -0.00579 157 TYR A CZ  
1849 O OH  . TYR A 157 ? 0.31124 0.40063 0.41870 -0.00447 0.02599  -0.00568 157 TYR A OH  
1850 N N   . VAL A 158 ? 0.22729 0.24773 0.27374 -0.01748 0.01703  -0.00115 158 VAL A N   
1851 C CA  . VAL A 158 ? 0.28185 0.29922 0.32598 -0.02149 0.02400  0.00176  158 VAL A CA  
1852 C C   . VAL A 158 ? 0.35089 0.35778 0.37980 -0.01753 0.02718  0.00418  158 VAL A C   
1853 O O   . VAL A 158 ? 0.37909 0.38448 0.40454 -0.01895 0.03395  0.00691  158 VAL A O   
1854 C CB  . VAL A 158 ? 0.28229 0.29481 0.32909 -0.02928 0.02432  0.00258  158 VAL A CB  
1855 C CG1 . VAL A 158 ? 0.32098 0.34630 0.38353 -0.03354 0.02098  -0.00007 158 VAL A CG1 
1856 C CG2 . VAL A 158 ? 0.27350 0.27137 0.30878 -0.02847 0.02040  0.00272  158 VAL A CG2 
1857 N N   . LYS A 159 ? 0.25184 0.25178 0.27144 -0.01262 0.02258  0.00348  159 LYS A N   
1858 C CA  . LYS A 159 ? 0.23872 0.23031 0.24412 -0.00839 0.02442  0.00559  159 LYS A CA  
1859 C C   . LYS A 159 ? 0.29099 0.28803 0.29413 -0.00289 0.02410  0.00346  159 LYS A C   
1860 O O   . LYS A 159 ? 0.30328 0.29733 0.29680 -0.00054 0.02793  0.00497  159 LYS A O   
1861 C CB  . LYS A 159 ? 0.30789 0.28894 0.30438 -0.00615 0.01983  0.00632  159 LYS A CB  
1862 C CG  . LYS A 159 ? 0.45420 0.42679 0.43589 -0.00196 0.02170  0.00937  159 LYS A CG  
1863 C CD  . LYS A 159 ? 0.50782 0.46939 0.48119 0.00002  0.01875  0.01132  159 LYS A CD  
1864 C CE  . LYS A 159 ? 0.41447 0.36821 0.37315 0.00461  0.02046  0.01504  159 LYS A CE  
1865 N NZ  . LYS A 159 ? 0.51581 0.46200 0.46873 0.00117  0.02776  0.01956  159 LYS A NZ  
1866 N N   . TYR A 160 ? 0.26681 0.27106 0.27787 -0.00086 0.01997  -0.00006 160 TYR A N   
1867 C CA  . TYR A 160 ? 0.24456 0.25040 0.25153 0.00431  0.01843  -0.00261 160 TYR A CA  
1868 C C   . TYR A 160 ? 0.26185 0.27667 0.27682 0.00571  0.02107  -0.00507 160 TYR A C   
1869 O O   . TYR A 160 ? 0.28628 0.30074 0.29608 0.00961  0.02119  -0.00742 160 TYR A O   
1870 C CB  . TYR A 160 ? 0.23752 0.24105 0.24368 0.00677  0.01167  -0.00450 160 TYR A CB  
1871 C CG  . TYR A 160 ? 0.22304 0.21774 0.21934 0.00750  0.00963  -0.00220 160 TYR A CG  
1872 C CD1 . TYR A 160 ? 0.23916 0.22924 0.22347 0.01049  0.01056  -0.00097 160 TYR A CD1 
1873 C CD2 . TYR A 160 ? 0.28154 0.27226 0.27970 0.00577  0.00680  -0.00122 160 TYR A CD2 
1874 C CE1 . TYR A 160 ? 0.27220 0.25449 0.24753 0.01225  0.00853  0.00172  160 TYR A CE1 
1875 C CE2 . TYR A 160 ? 0.27439 0.25658 0.26363 0.00740  0.00542  0.00105  160 TYR A CE2 
1876 C CZ  . TYR A 160 ? 0.28680 0.26519 0.26522 0.01086  0.00621  0.00274  160 TYR A CZ  
1877 O OH  . TYR A 160 ? 0.28978 0.26026 0.25986 0.01342  0.00464  0.00543  160 TYR A OH  
1878 N N   . THR A 161 ? 0.26989 0.29274 0.29729 0.00296  0.02285  -0.00489 161 THR A N   
1879 C CA  . THR A 161 ? 0.24263 0.27412 0.27794 0.00561  0.02536  -0.00700 161 THR A CA  
1880 C C   . THR A 161 ? 0.27114 0.30593 0.30559 0.00535  0.03347  -0.00574 161 THR A C   
1881 O O   . THR A 161 ? 0.29641 0.32781 0.32612 0.00200  0.03749  -0.00267 161 THR A O   
1882 C CB  . THR A 161 ? 0.24365 0.28445 0.29398 0.00414  0.02277  -0.00747 161 THR A CB  
1883 O OG1 . THR A 161 ? 0.25579 0.30133 0.31342 -0.00151 0.02516  -0.00523 161 THR A OG1 
1884 C CG2 . THR A 161 ? 0.23459 0.27181 0.28469 0.00461  0.01557  -0.00843 161 THR A CG2 
1885 N N   A LYS A 162 ? 0.24396 0.28459 0.28249 0.00923  0.03651  -0.00797 162 LYS A N   
1886 N N   B LYS A 162 ? 0.25368 0.29450 0.29252 0.00919  0.03650  -0.00796 162 LYS A N   
1887 C CA  A LYS A 162 ? 0.24183 0.28885 0.28375 0.00948  0.04488  -0.00702 162 LYS A CA  
1888 C CA  B LYS A 162 ? 0.24787 0.29486 0.28970 0.00956  0.04490  -0.00706 162 LYS A CA  
1889 C C   A LYS A 162 ? 0.26253 0.32241 0.32197 0.01051  0.04532  -0.00790 162 LYS A C   
1890 C C   B LYS A 162 ? 0.25300 0.31259 0.31164 0.01118  0.04569  -0.00819 162 LYS A C   
1891 O O   A LYS A 162 ? 0.22700 0.28873 0.29253 0.01223  0.03925  -0.00951 162 LYS A O   
1892 O O   B LYS A 162 ? 0.21860 0.27942 0.28207 0.01400  0.04034  -0.01027 162 LYS A O   
1893 C CB  A LYS A 162 ? 0.30781 0.34961 0.33687 0.01450  0.04905  -0.00919 162 LYS A CB  
1894 C CB  B LYS A 162 ? 0.31411 0.35517 0.34212 0.01429  0.04897  -0.00901 162 LYS A CB  
1895 C CG  A LYS A 162 ? 0.34858 0.37950 0.35983 0.01396  0.04944  -0.00765 162 LYS A CG  
1896 C CG  B LYS A 162 ? 0.34412 0.37448 0.35497 0.01340  0.04920  -0.00718 162 LYS A CG  
1897 C CD  A LYS A 162 ? 0.38496 0.41074 0.38208 0.01898  0.05226  -0.01060 162 LYS A CD  
1898 C CD  B LYS A 162 ? 0.39997 0.42625 0.39712 0.01773  0.05433  -0.00894 162 LYS A CD  
1899 C CE  A LYS A 162 ? 0.56833 0.59964 0.56718 0.02094  0.06187  -0.01061 162 LYS A CE  
1900 C CE  B LYS A 162 ? 0.36056 0.37702 0.34007 0.01738  0.05451  -0.00634 162 LYS A CE  
1901 N NZ  A LYS A 162 ? 0.50894 0.53319 0.49075 0.02569  0.06427  -0.01386 162 LYS A NZ  
1902 N NZ  B LYS A 162 ? 0.37517 0.38704 0.33891 0.02198  0.05803  -0.00872 162 LYS A NZ  
1903 N N   . GLU A 163 ? 0.22997 0.29926 0.29777 0.00965  0.05270  -0.00643 163 GLU A N   
1904 C CA  . GLU A 163 ? 0.22446 0.30840 0.31068 0.01088  0.05332  -0.00674 163 GLU A CA  
1905 C C   . GLU A 163 ? 0.24013 0.32559 0.32603 0.01880  0.05655  -0.00955 163 GLU A C   
1906 O O   . GLU A 163 ? 0.25969 0.35036 0.34746 0.02129  0.06488  -0.00943 163 GLU A O   
1907 C CB  . GLU A 163 ? 0.26189 0.35706 0.35990 0.00560  0.05965  -0.00376 163 GLU A CB  
1908 C CG  . GLU A 163 ? 0.27508 0.36836 0.37510 -0.00275 0.05624  -0.00153 163 GLU A CG  
1909 C CD  . GLU A 163 ? 0.26033 0.35890 0.37073 -0.00440 0.04707  -0.00270 163 GLU A CD  
1910 O OE1 . GLU A 163 ? 0.28512 0.39630 0.40911 -0.00094 0.04541  -0.00378 163 GLU A OE1 
1911 O OE2 . GLU A 163 ? 0.28036 0.37020 0.38459 -0.00868 0.04178  -0.00238 163 GLU A OE2 
1912 N N   . ASN A 164 ? 0.21276 0.29258 0.29569 0.02289  0.05043  -0.01215 164 ASN A N   
1913 C CA  . ASN A 164 ? 0.26449 0.34424 0.34785 0.03035  0.05311  -0.01505 164 ASN A CA  
1914 C C   . ASN A 164 ? 0.22529 0.30268 0.31228 0.03313  0.04556  -0.01631 164 ASN A C   
1915 O O   . ASN A 164 ? 0.20321 0.27719 0.28893 0.02952  0.03863  -0.01542 164 ASN A O   
1916 C CB  . ASN A 164 ? 0.28490 0.35337 0.35116 0.03331  0.05776  -0.01790 164 ASN A CB  
1917 C CG  . ASN A 164 ? 0.29169 0.34685 0.34305 0.03138  0.05164  -0.01944 164 ASN A CG  
1918 O OD1 . ASN A 164 ? 0.25943 0.31108 0.31225 0.03138  0.04463  -0.02035 164 ASN A OD1 
1919 N ND2 . ASN A 164 ? 0.30895 0.35712 0.34584 0.02990  0.05439  -0.01941 164 ASN A ND2 
1920 N N   . TRP A 165 ? 0.22742 0.30592 0.31846 0.03999  0.04758  -0.01818 165 TRP A N   
1921 C CA  . TRP A 165 ? 0.23570 0.31298 0.33183 0.04310  0.04139  -0.01832 165 TRP A CA  
1922 C C   . TRP A 165 ? 0.28393 0.34663 0.36758 0.04199  0.03599  -0.02037 165 TRP A C   
1923 O O   . TRP A 165 ? 0.22392 0.28554 0.31054 0.04149  0.02982  -0.01920 165 TRP A O   
1924 C CB  . TRP A 165 ? 0.21096 0.29313 0.31579 0.05126  0.04505  -0.01897 165 TRP A CB  
1925 C CG  . TRP A 165 ? 0.24979 0.35062 0.37249 0.05193  0.04676  -0.01582 165 TRP A CG  
1926 C CD1 . TRP A 165 ? 0.32778 0.43936 0.45756 0.05242  0.05442  -0.01515 165 TRP A CD1 
1927 C CD2 . TRP A 165 ? 0.24254 0.35429 0.37833 0.05163  0.04039  -0.01300 165 TRP A CD2 
1928 N NE1 . TRP A 165 ? 0.27276 0.40245 0.42104 0.05208  0.05306  -0.01219 165 TRP A NE1 
1929 C CE2 . TRP A 165 ? 0.27954 0.40951 0.43120 0.05167  0.04400  -0.01102 165 TRP A CE2 
1930 C CE3 . TRP A 165 ? 0.25941 0.36754 0.39462 0.05136  0.03203  -0.01197 165 TRP A CE3 
1931 C CZ2 . TRP A 165 ? 0.28670 0.43188 0.45386 0.05141  0.03864  -0.00850 165 TRP A CZ2 
1932 C CZ3 . TRP A 165 ? 0.24250 0.36459 0.39132 0.05151  0.02701  -0.00927 165 TRP A CZ3 
1933 C CH2 . TRP A 165 ? 0.26058 0.40122 0.42524 0.05137  0.02984  -0.00777 165 TRP A CH2 
1934 N N   A MET A 166 ? 0.24182 0.29386 0.31154 0.04144  0.03795  -0.02336 166 MET A N   
1935 N N   B MET A 166 ? 0.24222 0.29431 0.31220 0.04187  0.03823  -0.02349 166 MET A N   
1936 C CA  A MET A 166 ? 0.22635 0.26686 0.28648 0.03971  0.03233  -0.02526 166 MET A CA  
1937 C CA  B MET A 166 ? 0.22859 0.26918 0.28836 0.03971  0.03273  -0.02533 166 MET A CA  
1938 C C   A MET A 166 ? 0.22010 0.26108 0.27888 0.03382  0.02695  -0.02266 166 MET A C   
1939 C C   B MET A 166 ? 0.20430 0.24682 0.26525 0.03415  0.02705  -0.02230 166 MET A C   
1940 O O   A MET A 166 ? 0.28338 0.31846 0.33920 0.03253  0.02156  -0.02297 166 MET A O   
1941 O O   B MET A 166 ? 0.16977 0.20921 0.23191 0.03353  0.02157  -0.02179 166 MET A O   
1942 C CB  A MET A 166 ? 0.27875 0.30888 0.32476 0.04058  0.03475  -0.02965 166 MET A CB  
1943 C CB  B MET A 166 ? 0.28815 0.31972 0.33323 0.03945  0.03531  -0.02897 166 MET A CB  
1944 C CG  A MET A 166 ? 0.30787 0.33837 0.34494 0.03778  0.03785  -0.02921 166 MET A CG  
1945 C CG  B MET A 166 ? 0.40420 0.43062 0.44551 0.04496  0.04041  -0.03321 166 MET A CG  
1946 S SD  A MET A 166 ? 0.36346 0.38133 0.38186 0.03837  0.03763  -0.03465 166 MET A SD  
1947 S SD  B MET A 166 ? 0.58500 0.60405 0.60860 0.04484  0.04477  -0.03725 166 MET A SD  
1948 C CE  A MET A 166 ? 0.52270 0.53465 0.54233 0.04410  0.04038  -0.03968 166 MET A CE  
1949 C CE  B MET A 166 ? 0.49022 0.49687 0.50306 0.04238  0.03734  -0.04159 166 MET A CE  
1950 N N   . ASN A 167 ? 0.19891 0.24610 0.25957 0.03019  0.02892  -0.02010 167 ASN A N   
1951 C CA  . ASN A 167 ? 0.21304 0.26081 0.27432 0.02500  0.02420  -0.01747 167 ASN A CA  
1952 C C   . ASN A 167 ? 0.19140 0.24641 0.26461 0.02471  0.02000  -0.01560 167 ASN A C   
1953 O O   . ASN A 167 ? 0.22223 0.27377 0.29382 0.02257  0.01443  -0.01485 167 ASN A O   
1954 C CB  . ASN A 167 ? 0.20747 0.25806 0.26691 0.02084  0.02812  -0.01525 167 ASN A CB  
1955 C CG  . ASN A 167 ? 0.23584 0.27679 0.27988 0.02013  0.02932  -0.01601 167 ASN A CG  
1956 O OD1 . ASN A 167 ? 0.24249 0.27834 0.28053 0.01690  0.02599  -0.01447 167 ASN A OD1 
1957 N ND2 . ASN A 167 ? 0.24477 0.28291 0.28170 0.02362  0.03381  -0.01848 167 ASN A ND2 
1958 N N   . TYR A 168 ? 0.21218 0.27801 0.29724 0.02692  0.02256  -0.01469 168 TYR A N   
1959 C CA  . TYR A 168 ? 0.21126 0.28532 0.30730 0.02688  0.01780  -0.01287 168 TYR A CA  
1960 C C   . TYR A 168 ? 0.19572 0.26299 0.28895 0.03055  0.01310  -0.01339 168 TYR A C   
1961 O O   . TYR A 168 ? 0.20314 0.27080 0.29770 0.02893  0.00748  -0.01204 168 TYR A O   
1962 C CB  . TYR A 168 ? 0.18744 0.27582 0.29773 0.02975  0.02109  -0.01184 168 TYR A CB  
1963 C CG  . TYR A 168 ? 0.17205 0.26863 0.28715 0.02583  0.02696  -0.01096 168 TYR A CG  
1964 C CD1 . TYR A 168 ? 0.21458 0.30758 0.32425 0.01863  0.02694  -0.01007 168 TYR A CD1 
1965 C CD2 . TYR A 168 ? 0.21860 0.32566 0.34333 0.02963  0.03317  -0.01078 168 TYR A CD2 
1966 C CE1 . TYR A 168 ? 0.21711 0.31649 0.33085 0.01471  0.03326  -0.00873 168 TYR A CE1 
1967 C CE2 . TYR A 168 ? 0.24189 0.35640 0.37111 0.02598  0.03961  -0.00969 168 TYR A CE2 
1968 C CZ  . TYR A 168 ? 0.22597 0.33651 0.34972 0.01827  0.03973  -0.00854 168 TYR A CZ  
1969 O OH  . TYR A 168 ? 0.23235 0.35004 0.36102 0.01460  0.04709  -0.00695 168 TYR A OH  
1970 N N   . ILE A 169 ? 0.19487 0.25519 0.28370 0.03537  0.01570  -0.01541 169 ILE A N   
1971 C CA  . ILE A 169 ? 0.20966 0.26213 0.29572 0.03840  0.01223  -0.01568 169 ILE A CA  
1972 C C   . ILE A 169 ? 0.18668 0.23135 0.26468 0.03401  0.00768  -0.01567 169 ILE A C   
1973 O O   . ILE A 169 ? 0.22715 0.27125 0.30638 0.03390  0.00323  -0.01390 169 ILE A O   
1974 C CB  . ILE A 169 ? 0.22005 0.26430 0.30184 0.04324  0.01634  -0.01854 169 ILE A CB  
1975 C CG1 . ILE A 169 ? 0.22923 0.28099 0.32009 0.04934  0.02070  -0.01805 169 ILE A CG1 
1976 C CG2 . ILE A 169 ? 0.26123 0.29506 0.33904 0.04476  0.01314  -0.01879 169 ILE A CG2 
1977 C CD1 . ILE A 169 ? 0.26465 0.30728 0.34998 0.05401  0.02605  -0.02164 169 ILE A CD1 
1978 N N   . VAL A 170 ? 0.19102 0.22968 0.26022 0.03094  0.00882  -0.01752 170 VAL A N   
1979 C CA  . VAL A 170 ? 0.23351 0.26548 0.29573 0.02762  0.00484  -0.01751 170 VAL A CA  
1980 C C   . VAL A 170 ? 0.21405 0.25032 0.27880 0.02412  0.00138  -0.01491 170 VAL A C   
1981 O O   . VAL A 170 ? 0.22612 0.25943 0.28955 0.02350  -0.00253 -0.01393 170 VAL A O   
1982 C CB  . VAL A 170 ? 0.27226 0.29870 0.32497 0.02583  0.00653  -0.01979 170 VAL A CB  
1983 C CG1 . VAL A 170 ? 0.30550 0.32693 0.35232 0.02294  0.00246  -0.01942 170 VAL A CG1 
1984 C CG2 . VAL A 170 ? 0.27217 0.29332 0.32148 0.02897  0.00924  -0.02331 170 VAL A CG2 
1985 N N   . PHE A 171 ? 0.18510 0.22821 0.25364 0.02167  0.00313  -0.01388 171 PHE A N   
1986 C CA  . PHE A 171 ? 0.20213 0.24759 0.27194 0.01734  0.00004  -0.01219 171 PHE A CA  
1987 C C   . PHE A 171 ? 0.20175 0.25258 0.27845 0.01846  -0.00415 -0.01102 171 PHE A C   
1988 O O   . PHE A 171 ? 0.19564 0.24284 0.26889 0.01697  -0.00825 -0.01046 171 PHE A O   
1989 C CB  . PHE A 171 ? 0.18911 0.23999 0.26187 0.01354  0.00343  -0.01142 171 PHE A CB  
1990 C CG  . PHE A 171 ? 0.17749 0.22904 0.25117 0.00835  0.00040  -0.01026 171 PHE A CG  
1991 C CD1 . PHE A 171 ? 0.18993 0.23219 0.25412 0.00549  -0.00053 -0.00993 171 PHE A CD1 
1992 C CD2 . PHE A 171 ? 0.20472 0.26590 0.28853 0.00662  -0.00201 -0.00974 171 PHE A CD2 
1993 C CE1 . PHE A 171 ? 0.21531 0.25603 0.27926 0.00088  -0.00304 -0.00932 171 PHE A CE1 
1994 C CE2 . PHE A 171 ? 0.33233 0.39295 0.41614 0.00125  -0.00521 -0.00955 171 PHE A CE2 
1995 C CZ  . PHE A 171 ? 0.21948 0.26902 0.29302 -0.00170 -0.00536 -0.00944 171 PHE A CZ  
1996 N N   . TYR A 172 ? 0.19637 0.25621 0.28245 0.02151  -0.00317 -0.01052 172 TYR A N   
1997 C CA  . TYR A 172 ? 0.17110 0.23770 0.26368 0.02285  -0.00782 -0.00910 172 TYR A CA  
1998 C C   . TYR A 172 ? 0.20716 0.26696 0.29533 0.02722  -0.01048 -0.00837 172 TYR A C   
1999 O O   . TYR A 172 ? 0.20939 0.27051 0.29741 0.02734  -0.01517 -0.00711 172 TYR A O   
2000 C CB  . TYR A 172 ? 0.20598 0.28623 0.31116 0.02498  -0.00643 -0.00839 172 TYR A CB  
2001 C CG  . TYR A 172 ? 0.18641 0.27455 0.29723 0.01894  -0.00488 -0.00859 172 TYR A CG  
2002 C CD1 . TYR A 172 ? 0.20346 0.29524 0.31633 0.01341  -0.00960 -0.00850 172 TYR A CD1 
2003 C CD2 . TYR A 172 ? 0.17717 0.26819 0.29057 0.01847  0.00171  -0.00898 172 TYR A CD2 
2004 C CE1 . TYR A 172 ? 0.25943 0.35721 0.37776 0.00703  -0.00774 -0.00875 172 TYR A CE1 
2005 C CE2 . TYR A 172 ? 0.27476 0.37270 0.39374 0.01243  0.00415  -0.00865 172 TYR A CE2 
2006 C CZ  . TYR A 172 ? 0.26061 0.36161 0.38240 0.00638  -0.00063 -0.00851 172 TYR A CZ  
2007 O OH  . TYR A 172 ? 0.27323 0.38004 0.40099 -0.00052 0.00202  -0.00826 172 TYR A OH  
2008 N N   A PHE A 173 ? 0.19171 0.24446 0.27651 0.03092  -0.00739 -0.00913 173 PHE A N   
2009 N N   B PHE A 173 ? 0.15301 0.20431 0.23620 0.03005  -0.00755 -0.00932 173 PHE A N   
2010 C CA  A PHE A 173 ? 0.19907 0.24401 0.27955 0.03413  -0.00917 -0.00816 173 PHE A CA  
2011 C CA  B PHE A 173 ? 0.16454 0.20768 0.24295 0.03282  -0.00935 -0.00848 173 PHE A CA  
2012 C C   A PHE A 173 ? 0.20574 0.24479 0.27890 0.03036  -0.01232 -0.00792 173 PHE A C   
2013 C C   B PHE A 173 ? 0.22259 0.25985 0.29369 0.02899  -0.01226 -0.00836 173 PHE A C   
2014 O O   A PHE A 173 ? 0.19345 0.23178 0.26505 0.03143  -0.01573 -0.00610 173 PHE A O   
2015 O O   B PHE A 173 ? 0.14810 0.18312 0.21688 0.03015  -0.01525 -0.00668 173 PHE A O   
2016 C CB  A PHE A 173 ? 0.22714 0.26390 0.30459 0.03686  -0.00500 -0.00993 173 PHE A CB  
2017 C CB  B PHE A 173 ? 0.24358 0.27854 0.31881 0.03539  -0.00543 -0.01024 173 PHE A CB  
2018 C CG  A PHE A 173 ? 0.24104 0.26880 0.31506 0.03981  -0.00552 -0.00889 173 PHE A CG  
2019 C CG  B PHE A 173 ? 0.25718 0.28339 0.32867 0.03763  -0.00630 -0.00924 173 PHE A CG  
2020 C CD1 A PHE A 173 ? 0.28751 0.31565 0.36160 0.04175  -0.00887 -0.00575 173 PHE A CD1 
2021 C CD1 B PHE A 173 ? 0.37986 0.39855 0.44497 0.03452  -0.00701 -0.01005 173 PHE A CD1 
2022 C CD2 A PHE A 173 ? 0.39108 0.40945 0.46128 0.04037  -0.00235 -0.01122 173 PHE A CD2 
2023 C CD2 B PHE A 173 ? 0.32306 0.34883 0.39784 0.04308  -0.00606 -0.00709 173 PHE A CD2 
2024 C CE1 A PHE A 173 ? 0.41509 0.43395 0.48551 0.04434  -0.00829 -0.00423 173 PHE A CE1 
2025 C CE1 B PHE A 173 ? 0.37877 0.38985 0.44145 0.03604  -0.00699 -0.00885 173 PHE A CE1 
2026 C CE2 A PHE A 173 ? 0.40522 0.41455 0.47293 0.04220  -0.00205 -0.01026 173 PHE A CE2 
2027 C CE2 B PHE A 173 ? 0.37856 0.39512 0.44949 0.04495  -0.00602 -0.00559 173 PHE A CE2 
2028 C CZ  A PHE A 173 ? 0.37125 0.38066 0.43912 0.04428  -0.00463 -0.00637 173 PHE A CZ  
2029 C CZ  B PHE A 173 ? 0.32173 0.33108 0.38690 0.04101  -0.00625 -0.00655 173 PHE A CZ  
2030 N N   A MET A 174 ? 0.15497 0.19012 0.22319 0.02637  -0.01113 -0.00958 174 MET A N   
2031 N N   B MET A 174 ? 0.19808 0.23229 0.26474 0.02506  -0.01104 -0.00993 174 MET A N   
2032 C CA  A MET A 174 ? 0.13980 0.16946 0.20140 0.02349  -0.01353 -0.00937 174 MET A CA  
2033 C CA  B MET A 174 ? 0.20511 0.23393 0.26523 0.02219  -0.01333 -0.00976 174 MET A CA  
2034 C C   A MET A 174 ? 0.14899 0.18286 0.21130 0.02119  -0.01720 -0.00839 174 MET A C   
2035 C C   B MET A 174 ? 0.23167 0.26445 0.29267 0.02010  -0.01694 -0.00871 174 MET A C   
2036 O O   A MET A 174 ? 0.15759 0.18816 0.21580 0.02162  -0.01997 -0.00744 174 MET A O   
2037 O O   B MET A 174 ? 0.16664 0.19542 0.22290 0.01996  -0.01950 -0.00802 174 MET A O   
2038 C CB  A MET A 174 ? 0.18627 0.21188 0.24288 0.02060  -0.01159 -0.01101 174 MET A CB  
2039 C CB  B MET A 174 ? 0.18639 0.21193 0.24186 0.01929  -0.01138 -0.01121 174 MET A CB  
2040 C CG  A MET A 174 ? 0.12378 0.14399 0.17402 0.01843  -0.01361 -0.01068 174 MET A CG  
2041 C CG  B MET A 174 ? 0.41398 0.43346 0.46539 0.02048  -0.00997 -0.01269 174 MET A CG  
2042 S SD  A MET A 174 ? 0.20029 0.21695 0.24485 0.01621  -0.01179 -0.01187 174 MET A SD  
2043 S SD  B MET A 174 ? 0.37038 0.38527 0.41428 0.01776  -0.01059 -0.01320 174 MET A SD  
2044 C CE  A MET A 174 ? 0.20762 0.21845 0.24637 0.01576  -0.01407 -0.01113 174 MET A CE  
2045 C CE  B MET A 174 ? 0.13320 0.14981 0.17660 0.01480  -0.01203 -0.01149 174 MET A CE  
2046 N N   . PHE A 175 ? 0.20544 0.24637 0.27266 0.01839  -0.01707 -0.00882 175 PHE A N   
2047 C CA  . PHE A 175 ? 0.19109 0.23602 0.25948 0.01511  -0.02088 -0.00873 175 PHE A CA  
2048 C C   . PHE A 175 ? 0.18752 0.23609 0.25752 0.01846  -0.02509 -0.00747 175 PHE A C   
2049 O O   . PHE A 175 ? 0.20878 0.25415 0.27318 0.01736  -0.02866 -0.00748 175 PHE A O   
2050 C CB  . PHE A 175 ? 0.15771 0.21157 0.23413 0.01161  -0.01939 -0.00928 175 PHE A CB  
2051 C CG  . PHE A 175 ? 0.17709 0.23476 0.25542 0.00622  -0.02301 -0.01004 175 PHE A CG  
2052 C CD1 . PHE A 175 ? 0.20091 0.25068 0.27079 0.00386  -0.02617 -0.01081 175 PHE A CD1 
2053 C CD2 . PHE A 175 ? 0.32684 0.39603 0.41587 0.00323  -0.02276 -0.01033 175 PHE A CD2 
2054 C CE1 . PHE A 175 ? 0.29296 0.34490 0.36390 -0.00144 -0.02942 -0.01227 175 PHE A CE1 
2055 C CE2 . PHE A 175 ? 0.39252 0.46537 0.48422 -0.00272 -0.02619 -0.01162 175 PHE A CE2 
2056 C CZ  . PHE A 175 ? 0.38996 0.45342 0.47201 -0.00520 -0.02969 -0.01284 175 PHE A CZ  
2057 N N   . LEU A 176 ? 0.17823 0.23261 0.25470 0.02321  -0.02451 -0.00623 176 LEU A N   
2058 C CA  . LEU A 176 ? 0.17991 0.23727 0.25691 0.02755  -0.02851 -0.00426 176 LEU A CA  
2059 C C   . LEU A 176 ? 0.19010 0.23645 0.25695 0.02957  -0.02899 -0.00303 176 LEU A C   
2060 O O   . LEU A 176 ? 0.20580 0.25152 0.26767 0.03004  -0.03307 -0.00216 176 LEU A O   
2061 C CB  . LEU A 176 ? 0.16786 0.23160 0.25295 0.03345  -0.02696 -0.00267 176 LEU A CB  
2062 C CG  . LEU A 176 ? 0.21692 0.28220 0.30137 0.03958  -0.03064 0.00033  176 LEU A CG  
2063 C CD1 . LEU A 176 ? 0.25270 0.32685 0.33820 0.03784  -0.03749 0.00040  176 LEU A CD1 
2064 C CD2 . LEU A 176 ? 0.33840 0.40885 0.43109 0.04614  -0.02813 0.00198  176 LEU A CD2 
2065 N N   . VAL A 177 ? 0.18093 0.21889 0.24458 0.03061  -0.02479 -0.00311 177 VAL A N   
2066 C CA  . VAL A 177 ? 0.17966 0.20807 0.23552 0.03216  -0.02428 -0.00175 177 VAL A CA  
2067 C C   . VAL A 177 ? 0.18177 0.20658 0.23036 0.02866  -0.02637 -0.00253 177 VAL A C   
2068 O O   . VAL A 177 ? 0.19809 0.21929 0.24045 0.03038  -0.02810 -0.00094 177 VAL A O   
2069 C CB  . VAL A 177 ? 0.18718 0.20867 0.24261 0.03249  -0.01968 -0.00254 177 VAL A CB  
2070 C CG1 . VAL A 177 ? 0.21852 0.23159 0.26746 0.03248  -0.01878 -0.00146 177 VAL A CG1 
2071 C CG2 . VAL A 177 ? 0.22200 0.24425 0.28267 0.03705  -0.01744 -0.00165 177 VAL A CG2 
2072 N N   A TRP A 178 ? 0.17768 0.20249 0.22601 0.02418  -0.02582 -0.00481 178 TRP A N   
2073 N N   B TRP A 178 ? 0.17781 0.20267 0.22619 0.02416  -0.02581 -0.00482 178 TRP A N   
2074 C CA  A TRP A 178 ? 0.18669 0.20680 0.22775 0.02145  -0.02739 -0.00566 178 TRP A CA  
2075 C CA  B TRP A 178 ? 0.19248 0.21279 0.23377 0.02126  -0.02737 -0.00576 178 TRP A CA  
2076 C C   A TRP A 178 ? 0.19996 0.22384 0.23927 0.02067  -0.03217 -0.00593 178 TRP A C   
2077 C C   B TRP A 178 ? 0.20429 0.22820 0.24369 0.02062  -0.03213 -0.00596 178 TRP A C   
2078 O O   A TRP A 178 ? 0.19224 0.21118 0.22348 0.02136  -0.03387 -0.00572 178 TRP A O   
2079 O O   B TRP A 178 ? 0.19512 0.21387 0.22637 0.02118  -0.03373 -0.00580 178 TRP A O   
2080 C CB  A TRP A 178 ? 0.18118 0.19921 0.22175 0.01748  -0.02550 -0.00752 178 TRP A CB  
2081 C CB  B TRP A 178 ? 0.17372 0.19277 0.21511 0.01708  -0.02569 -0.00767 178 TRP A CB  
2082 C CG  A TRP A 178 ? 0.16137 0.17460 0.20065 0.01840  -0.02198 -0.00753 178 TRP A CG  
2083 C CG  B TRP A 178 ? 0.21602 0.23017 0.25584 0.01767  -0.02218 -0.00780 178 TRP A CG  
2084 C CD1 A TRP A 178 ? 0.16502 0.17833 0.20757 0.02078  -0.01975 -0.00717 178 TRP A CD1 
2085 C CD1 B TRP A 178 ? 0.15447 0.16886 0.19754 0.01992  -0.01984 -0.00755 178 TRP A CD1 
2086 C CD2 A TRP A 178 ? 0.16907 0.17690 0.20345 0.01696  -0.02078 -0.00818 178 TRP A CD2 
2087 C CD2 B TRP A 178 ? 0.23255 0.24110 0.26721 0.01607  -0.02104 -0.00846 178 TRP A CD2 
2088 N NE1 A TRP A 178 ? 0.17378 0.18303 0.21414 0.02020  -0.01777 -0.00798 178 TRP A NE1 
2089 N NE1 B TRP A 178 ? 0.19293 0.20325 0.23349 0.01925  -0.01790 -0.00838 178 TRP A NE1 
2090 C CE2 A TRP A 178 ? 0.18335 0.18995 0.21903 0.01830  -0.01846 -0.00831 178 TRP A CE2 
2091 C CE2 B TRP A 178 ? 0.22038 0.22769 0.25607 0.01734  -0.01866 -0.00861 178 TRP A CE2 
2092 C CE3 A TRP A 178 ? 0.20340 0.20702 0.23236 0.01484  -0.02149 -0.00879 178 TRP A CE3 
2093 C CE3 B TRP A 178 ? 0.19556 0.19964 0.22464 0.01394  -0.02188 -0.00904 178 TRP A CE3 
2094 C CZ2 A TRP A 178 ? 0.19521 0.19847 0.22774 0.01789  -0.01746 -0.00876 178 TRP A CZ2 
2095 C CZ2 B TRP A 178 ? 0.23760 0.24121 0.26968 0.01693  -0.01766 -0.00899 178 TRP A CZ2 
2096 C CZ3 A TRP A 178 ? 0.19264 0.19160 0.21793 0.01513  -0.01982 -0.00882 178 TRP A CZ3 
2097 C CZ3 B TRP A 178 ? 0.16024 0.15926 0.18531 0.01412  -0.02015 -0.00906 178 TRP A CZ3 
2098 C CH2 A TRP A 178 ? 0.21705 0.21687 0.24457 0.01679  -0.01811 -0.00869 178 TRP A CH2 
2099 C CH2 B TRP A 178 ? 0.18788 0.18765 0.21486 0.01576  -0.01834 -0.00888 178 TRP A CH2 
2100 N N   . PHE A 179 ? 0.19381 0.22716 0.24076 0.01953  -0.03448 -0.00649 179 PHE A N   
2101 C CA  . PHE A 179 ? 0.20135 0.24010 0.24766 0.01868  -0.04010 -0.00712 179 PHE A CA  
2102 C C   . PHE A 179 ? 0.22478 0.26184 0.26516 0.02412  -0.04254 -0.00467 179 PHE A C   
2103 O O   . PHE A 179 ? 0.20936 0.24472 0.24212 0.02371  -0.04658 -0.00541 179 PHE A O   
2104 C CB  . PHE A 179 ? 0.23916 0.29088 0.29749 0.01774  -0.04176 -0.00744 179 PHE A CB  
2105 C CG  . PHE A 179 ? 0.33789 0.39769 0.39767 0.01609  -0.04838 -0.00863 179 PHE A CG  
2106 C CD1 . PHE A 179 ? 0.36988 0.42902 0.42792 0.00924  -0.05080 -0.01196 179 PHE A CD1 
2107 C CD2 . PHE A 179 ? 0.40434 0.47164 0.46640 0.02144  -0.05246 -0.00651 179 PHE A CD2 
2108 C CE1 . PHE A 179 ? 0.54348 0.61031 0.60282 0.00685  -0.05765 -0.01392 179 PHE A CE1 
2109 C CE2 . PHE A 179 ? 0.44138 0.51740 0.50455 0.01994  -0.05965 -0.00793 179 PHE A CE2 
2110 C CZ  . PHE A 179 ? 0.47346 0.54956 0.53547 0.01223  -0.06246 -0.01200 179 PHE A CZ  
2111 N N   . LEU A 180 ? 0.21467 0.25015 0.25671 0.02923  -0.03960 -0.00176 180 LEU A N   
2112 C CA  . LEU A 180 ? 0.21630 0.24886 0.25210 0.03472  -0.04103 0.00145  180 LEU A CA  
2113 C C   . LEU A 180 ? 0.19593 0.21781 0.21966 0.03465  -0.03961 0.00184  180 LEU A C   
2114 O O   . LEU A 180 ? 0.22486 0.24416 0.24081 0.03844  -0.04140 0.00422  180 LEU A O   
2115 C CB  . LEU A 180 ? 0.21192 0.24386 0.25261 0.03994  -0.03759 0.00454  180 LEU A CB  
2116 C CG  . LEU A 180 ? 0.22715 0.27070 0.27886 0.04226  -0.03955 0.00491  180 LEU A CG  
2117 C CD1 . LEU A 180 ? 0.21045 0.25028 0.26634 0.04692  -0.03454 0.00704  180 LEU A CD1 
2118 C CD2 . LEU A 180 ? 0.22250 0.27426 0.27330 0.04559  -0.04632 0.00656  180 LEU A CD2 
2119 N N   A TYR A 181 ? 0.18135 0.19739 0.20300 0.03098  -0.03638 -0.00019 181 TYR A N   
2120 N N   B TYR A 181 ? 0.18478 0.20058 0.20670 0.03122  -0.03600 0.00001  181 TYR A N   
2121 C CA  A TYR A 181 ? 0.19886 0.20626 0.20976 0.03116  -0.03506 -0.00008 181 TYR A CA  
2122 C CA  B TYR A 181 ? 0.20488 0.21235 0.21613 0.03102  -0.03495 -0.00016 181 TYR A CA  
2123 C C   A TYR A 181 ? 0.24559 0.25310 0.24881 0.02940  -0.03995 -0.00239 181 TYR A C   
2124 C C   B TYR A 181 ? 0.22920 0.23761 0.23308 0.02978  -0.04026 -0.00211 181 TYR A C   
2125 O O   A TYR A 181 ? 0.23221 0.23390 0.22459 0.03152  -0.04022 -0.00170 181 TYR A O   
2126 O O   B TYR A 181 ? 0.23992 0.24436 0.23389 0.03282  -0.04143 -0.00070 181 TYR A O   
2127 C CB  A TYR A 181 ? 0.18643 0.18890 0.19811 0.02835  -0.03078 -0.00162 181 TYR A CB  
2128 C CB  B TYR A 181 ? 0.20293 0.20556 0.21450 0.02778  -0.03112 -0.00207 181 TYR A CB  
2129 C CG  A TYR A 181 ? 0.21907 0.21934 0.23524 0.02989  -0.02604 0.00018  181 TYR A CG  
2130 C CG  B TYR A 181 ? 0.16374 0.16339 0.17900 0.02914  -0.02606 -0.00042 181 TYR A CG  
2131 C CD1 A TYR A 181 ? 0.15241 0.15683 0.17747 0.02963  -0.02499 -0.00005 181 TYR A CD1 
2132 C CD1 B TYR A 181 ? 0.18870 0.19203 0.21266 0.02879  -0.02466 -0.00058 181 TYR A CD1 
2133 C CD2 A TYR A 181 ? 0.21426 0.20835 0.22601 0.03131  -0.02234 0.00175  181 TYR A CD2 
2134 C CD2 B TYR A 181 ? 0.18862 0.18207 0.19892 0.03050  -0.02253 0.00095  181 TYR A CD2 
2135 C CE1 A TYR A 181 ? 0.23874 0.24019 0.26720 0.03039  -0.02098 0.00071  181 TYR A CE1 
2136 C CE1 B TYR A 181 ? 0.14558 0.14592 0.17263 0.02932  -0.02065 0.00007  181 TYR A CE1 
2137 C CE2 A TYR A 181 ? 0.18316 0.17562 0.19998 0.03166  -0.01830 0.00284  181 TYR A CE2 
2138 C CE2 B TYR A 181 ? 0.19558 0.18743 0.21080 0.03076  -0.01831 0.00199  181 TYR A CE2 
2139 C CZ  A TYR A 181 ? 0.16679 0.16248 0.19154 0.03102  -0.01795 0.00206  181 TYR A CZ  
2140 C CZ  B TYR A 181 ? 0.20627 0.20127 0.22954 0.02992  -0.01778 0.00126  181 TYR A CZ  
2141 O OH  A TYR A 181 ? 0.19895 0.19217 0.22800 0.03078  -0.01431 0.00234  181 TYR A OH  
2142 O OH  B TYR A 181 ? 0.14765 0.14080 0.17550 0.02948  -0.01425 0.00139  181 TYR A OH  
2143 N N   . GLY A 182 ? 0.23784 0.25134 0.24613 0.02510  -0.04348 -0.00545 182 GLY A N   
2144 C CA  . GLY A 182 ? 0.23537 0.24984 0.23737 0.02280  -0.04909 -0.00824 182 GLY A CA  
2145 C C   . GLY A 182 ? 0.24585 0.26643 0.24554 0.02682  -0.05435 -0.00646 182 GLY A C   
2146 O O   . GLY A 182 ? 0.28459 0.30222 0.27323 0.02750  -0.05818 -0.00763 182 GLY A O   
2147 N N   . PHE A 183 ? 0.23883 0.26792 0.24824 0.03000  -0.05481 -0.00366 183 PHE A N   
2148 C CA  . PHE A 183 ? 0.22815 0.26298 0.23525 0.03530  -0.05969 -0.00099 183 PHE A CA  
2149 C C   . PHE A 183 ? 0.24594 0.27057 0.23915 0.04063  -0.05757 0.00246  183 PHE A C   
2150 O O   . PHE A 183 ? 0.26512 0.28990 0.24824 0.04333  -0.06240 0.00298  183 PHE A O   
2151 C CB  . PHE A 183 ? 0.26456 0.30822 0.28462 0.03887  -0.05879 0.00192  183 PHE A CB  
2152 C CG  . PHE A 183 ? 0.30898 0.35988 0.32851 0.04536  -0.06396 0.00529  183 PHE A CG  
2153 C CD1 . PHE A 183 ? 0.31546 0.37697 0.33562 0.04422  -0.07228 0.00318  183 PHE A CD1 
2154 C CD2 . PHE A 183 ? 0.26742 0.31469 0.28637 0.05258  -0.06064 0.01054  183 PHE A CD2 
2155 C CE1 . PHE A 183 ? 0.35692 0.42629 0.37684 0.05096  -0.07763 0.00659  183 PHE A CE1 
2156 C CE2 . PHE A 183 ? 0.29131 0.34450 0.30928 0.05956  -0.06517 0.01436  183 PHE A CE2 
2157 C CZ  . PHE A 183 ? 0.34497 0.40992 0.36340 0.05917  -0.07398 0.01255  183 PHE A CZ  
2158 N N   . ALA A 184 ? 0.25155 0.26741 0.24378 0.04186  -0.05029 0.00469  184 ALA A N   
2159 C CA  . ALA A 184 ? 0.23931 0.24550 0.21958 0.04628  -0.04686 0.00829  184 ALA A CA  
2160 C C   . ALA A 184 ? 0.25005 0.24993 0.21624 0.04496  -0.04821 0.00582  184 ALA A C   
2161 O O   . ALA A 184 ? 0.25850 0.25304 0.21227 0.04934  -0.04797 0.00860  184 ALA A O   
2162 C CB  . ALA A 184 ? 0.23614 0.23544 0.22033 0.04621  -0.03877 0.01021  184 ALA A CB  
2163 N N   . PHE A 185 ? 0.26372 0.26282 0.23065 0.03933  -0.04896 0.00081  185 PHE A N   
2164 C CA  . PHE A 185 ? 0.26385 0.25552 0.21704 0.03808  -0.04986 -0.00230 185 PHE A CA  
2165 C C   . PHE A 185 ? 0.31076 0.30435 0.25273 0.04040  -0.05681 -0.00290 185 PHE A C   
2166 O O   . PHE A 185 ? 0.35077 0.33633 0.27746 0.04191  -0.05656 -0.00397 185 PHE A O   
2167 C CB  . PHE A 185 ? 0.32230 0.31366 0.27989 0.03146  -0.05070 -0.00767 185 PHE A CB  
2168 C CG  . PHE A 185 ? 0.27897 0.26199 0.22294 0.02964  -0.05211 -0.01190 185 PHE A CG  
2169 C CD1 . PHE A 185 ? 0.34792 0.33380 0.28682 0.02674  -0.05974 -0.01611 185 PHE A CD1 
2170 C CD2 . PHE A 185 ? 0.37521 0.34786 0.31192 0.03076  -0.04594 -0.01206 185 PHE A CD2 
2171 C CE1 . PHE A 185 ? 0.35547 0.33201 0.28049 0.02493  -0.06103 -0.02075 185 PHE A CE1 
2172 C CE2 . PHE A 185 ? 0.36739 0.33102 0.29065 0.02970  -0.04669 -0.01628 185 PHE A CE2 
2173 C CZ  . PHE A 185 ? 0.36038 0.32505 0.27703 0.02674  -0.05415 -0.02078 185 PHE A CZ  
2174 N N   A MET A 186 ? 0.32234 0.32698 0.27132 0.04105  -0.06320 -0.00236 186 MET A N   
2175 N N   B MET A 186 ? 0.32241 0.32697 0.27133 0.04123  -0.06309 -0.00220 186 MET A N   
2176 C CA  A MET A 186 ? 0.37586 0.38455 0.31506 0.04314  -0.07134 -0.00331 186 MET A CA  
2177 C CA  B MET A 186 ? 0.37713 0.38655 0.31730 0.04313  -0.07150 -0.00322 186 MET A CA  
2178 C C   A MET A 186 ? 0.36096 0.36349 0.28584 0.05096  -0.06977 0.00209  186 MET A C   
2179 C C   B MET A 186 ? 0.38700 0.39278 0.31511 0.05136  -0.07105 0.00261  186 MET A C   
2180 O O   A MET A 186 ? 0.40515 0.40546 0.31487 0.05292  -0.07466 0.00080  186 MET A O   
2181 O O   B MET A 186 ? 0.32162 0.33077 0.23974 0.05403  -0.07832 0.00224  186 MET A O   
2182 C CB  A MET A 186 ? 0.36047 0.38466 0.31333 0.04277  -0.07820 -0.00326 186 MET A CB  
2183 C CB  B MET A 186 ? 0.34077 0.36568 0.29575 0.04126  -0.07826 -0.00425 186 MET A CB  
2184 C CG  A MET A 186 ? 0.47335 0.50472 0.43883 0.03453  -0.08075 -0.00881 186 MET A CG  
2185 C CG  B MET A 186 ? 0.40098 0.43050 0.36805 0.03286  -0.07893 -0.00957 186 MET A CG  
2186 S SD  A MET A 186 ? 0.62380 0.67491 0.60079 0.03373  -0.09141 -0.01020 186 MET A SD  
2187 S SD  B MET A 186 ? 0.38353 0.43341 0.36747 0.03137  -0.08718 -0.01039 186 MET A SD  
2188 C CE  A MET A 186 ? 0.33566 0.39396 0.32399 0.04207  -0.08827 -0.00265 186 MET A CE  
2189 C CE  B MET A 186 ? 0.43228 0.48617 0.40239 0.03261  -0.09818 -0.01307 186 MET A CE  
2190 N N   . PHE A 187 ? 0.30817 0.30722 0.23688 0.05527  -0.06289 0.00804  187 PHE A N   
2191 C CA  . PHE A 187 ? 0.31969 0.31462 0.23854 0.06300  -0.06134 0.01461  187 PHE A CA  
2192 C C   . PHE A 187 ? 0.30091 0.28265 0.20329 0.06512  -0.05494 0.01626  187 PHE A C   
2193 O O   . PHE A 187 ? 0.33000 0.30576 0.23197 0.06118  -0.04988 0.01316  187 PHE A O   
2194 C CB  . PHE A 187 ? 0.32838 0.32466 0.25995 0.06599  -0.05640 0.01998  187 PHE A CB  
2195 C CG  . PHE A 187 ? 0.29755 0.30689 0.24259 0.06693  -0.06251 0.02004  187 PHE A CG  
2196 C CD1 . PHE A 187 ? 0.27169 0.28914 0.23246 0.06102  -0.06348 0.01559  187 PHE A CD1 
2197 C CD2 . PHE A 187 ? 0.30354 0.31736 0.24518 0.07425  -0.06709 0.02485  187 PHE A CD2 
2198 C CE1 . PHE A 187 ? 0.29235 0.32291 0.26638 0.06204  -0.06835 0.01566  187 PHE A CE1 
2199 C CE2 . PHE A 187 ? 0.36875 0.39583 0.32406 0.07582  -0.07237 0.02503  187 PHE A CE2 
2200 C CZ  . PHE A 187 ? 0.29306 0.32885 0.26485 0.06963  -0.07280 0.02034  187 PHE A CZ  
2201 N N   . PRO A 188 ? 0.35729 0.33448 0.24535 0.07184  -0.05493 0.02139  188 PRO A N   
2202 C CA  . PRO A 188 ? 0.41752 0.38239 0.28965 0.07427  -0.04776 0.02357  188 PRO A CA  
2203 C C   . PRO A 188 ? 0.38847 0.34741 0.26968 0.07323  -0.03680 0.02696  188 PRO A C   
2204 O O   . PRO A 188 ? 0.35090 0.31358 0.24759 0.07227  -0.03492 0.02896  188 PRO A O   
2205 C CB  . PRO A 188 ? 0.42221 0.38446 0.27887 0.08228  -0.04999 0.02973  188 PRO A CB  
2206 C CG  . PRO A 188 ? 0.49670 0.47129 0.35932 0.08383  -0.06083 0.02911  188 PRO A CG  
2207 C CD  . PRO A 188 ? 0.36049 0.34387 0.24595 0.07803  -0.06135 0.02574  188 PRO A CD  
2208 N N   . PHE A 189 ? 0.32384 0.27112 0.29765 0.05577  -0.02319 -0.01470 189 PHE A N   
2209 C CA  . PHE A 189 ? 0.27442 0.23211 0.25172 0.04508  -0.01515 -0.01649 189 PHE A CA  
2210 C C   . PHE A 189 ? 0.28883 0.23683 0.25513 0.03791  -0.00869 -0.01535 189 PHE A C   
2211 O O   . PHE A 189 ? 0.27576 0.23514 0.25299 0.03199  -0.00772 -0.01516 189 PHE A O   
2212 C CB  . PHE A 189 ? 0.29280 0.24845 0.26115 0.04274  -0.00891 -0.01905 189 PHE A CB  
2213 C CG  . PHE A 189 ? 0.28065 0.24692 0.25315 0.03178  -0.00058 -0.02062 189 PHE A CG  
2214 C CD1 . PHE A 189 ? 0.29958 0.28852 0.29381 0.02812  -0.00260 -0.02179 189 PHE A CD1 
2215 C CD2 . PHE A 189 ? 0.32177 0.27567 0.27735 0.02507  0.00893  -0.02074 189 PHE A CD2 
2216 C CE1 . PHE A 189 ? 0.32681 0.32572 0.32587 0.01797  0.00453  -0.02310 189 PHE A CE1 
2217 C CE2 . PHE A 189 ? 0.31537 0.27921 0.27599 0.01477  0.01620  -0.02185 189 PHE A CE2 
2218 C CZ  . PHE A 189 ? 0.33584 0.32218 0.31829 0.01118  0.01391  -0.02307 189 PHE A CZ  
2219 N N   . SER A 190 ? 0.30720 0.23406 0.25148 0.03811  -0.00408 -0.01471 190 SER A N   
2220 C CA  . SER A 190 ? 0.30512 0.22261 0.23796 0.03031  0.00290  -0.01407 190 SER A CA  
2221 C C   . SER A 190 ? 0.30306 0.22006 0.24064 0.03179  -0.00134 -0.01161 190 SER A C   
2222 O O   . SER A 190 ? 0.31833 0.24173 0.26087 0.02486  0.00141  -0.01163 190 SER A O   
2223 C CB  . SER A 190 ? 0.36842 0.26302 0.27639 0.03053  0.00870  -0.01384 190 SER A CB  
2224 O OG  . SER A 190 ? 0.42956 0.31445 0.32638 0.02302  0.01502  -0.01313 190 SER A OG  
2225 N N   . ILE A 191 ? 0.32216 0.23146 0.25841 0.04109  -0.00820 -0.00930 191 ILE A N   
2226 C CA  . ILE A 191 ? 0.30877 0.21678 0.24907 0.04361  -0.01211 -0.00632 191 ILE A CA  
2227 C C   . ILE A 191 ? 0.27751 0.20815 0.24135 0.04200  -0.01595 -0.00619 191 ILE A C   
2228 O O   . ILE A 191 ? 0.28300 0.21663 0.24999 0.03839  -0.01480 -0.00503 191 ILE A O   
2229 C CB  . ILE A 191 ? 0.33402 0.23115 0.27089 0.05448  -0.01931 -0.00360 191 ILE A CB  
2230 C CG1 . ILE A 191 ? 0.43530 0.30858 0.34743 0.05593  -0.01530 -0.00364 191 ILE A CG1 
2231 C CG2 . ILE A 191 ? 0.37411 0.27198 0.31791 0.05816  -0.02382 0.00015  191 ILE A CG2 
2232 C CD1 . ILE A 191 ? 0.56511 0.42704 0.47341 0.06667  -0.02264 -0.00130 191 ILE A CD1 
2233 N N   . LYS A 192 ? 0.25216 0.19847 0.23247 0.04523  -0.02092 -0.00729 192 LYS A N   
2234 C CA  . LYS A 192 ? 0.23413 0.20298 0.23772 0.04391  -0.02476 -0.00735 192 LYS A CA  
2235 C C   . LYS A 192 ? 0.24133 0.21857 0.24724 0.03315  -0.01809 -0.00931 192 LYS A C   
2236 O O   . LYS A 192 ? 0.24029 0.22668 0.25640 0.03110  -0.01936 -0.00818 192 LYS A O   
2237 C CB  . LYS A 192 ? 0.23722 0.21953 0.25497 0.04815  -0.02999 -0.00891 192 LYS A CB  
2238 C CG  . LYS A 192 ? 0.21038 0.21715 0.25249 0.04619  -0.03350 -0.00955 192 LYS A CG  
2239 C CD  . LYS A 192 ? 0.20763 0.22523 0.26279 0.05229  -0.04016 -0.01057 192 LYS A CD  
2240 C CE  . LYS A 192 ? 0.27391 0.28616 0.31759 0.05004  -0.03518 -0.01389 192 LYS A CE  
2241 N NZ  . LYS A 192 ? 0.34302 0.36585 0.39874 0.05593  -0.04158 -0.01527 192 LYS A NZ  
2242 N N   A ASN A 193 ? 0.22159 0.19554 0.21809 0.02633  -0.01097 -0.01205 193 ASN A N   
2243 N N   B ASN A 193 ? 0.22151 0.19528 0.21782 0.02626  -0.01090 -0.01204 193 ASN A N   
2244 C CA  A ASN A 193 ? 0.22468 0.20688 0.22443 0.01579  -0.00498 -0.01390 193 ASN A CA  
2245 C CA  B ASN A 193 ? 0.22648 0.20918 0.22674 0.01577  -0.00507 -0.01391 193 ASN A CA  
2246 C C   A ASN A 193 ? 0.23940 0.20858 0.22618 0.01132  -0.00102 -0.01265 193 ASN A C   
2247 C C   B ASN A 193 ? 0.23743 0.20633 0.22339 0.01057  -0.00031 -0.01290 193 ASN A C   
2248 O O   A ASN A 193 ? 0.24764 0.22541 0.24181 0.00537  0.00015  -0.01305 193 ASN A O   
2249 O O   B ASN A 193 ? 0.25353 0.23030 0.24538 0.00335  0.00205  -0.01369 193 ASN A O   
2250 C CB  A ASN A 193 ? 0.24927 0.23209 0.24394 0.01025  0.00135  -0.01659 193 ASN A CB  
2251 C CB  B ASN A 193 ? 0.28352 0.27020 0.28209 0.01039  0.00053  -0.01676 193 ASN A CB  
2252 C CG  A ASN A 193 ? 0.26872 0.27084 0.28151 0.01194  -0.00208 -0.01830 193 ASN A CG  
2253 C CG  B ASN A 193 ? 0.26432 0.27122 0.28256 0.01281  -0.00388 -0.01829 193 ASN A CG  
2254 O OD1 A ASN A 193 ? 0.23594 0.25565 0.26440 0.00636  -0.00178 -0.01959 193 ASN A OD1 
2255 O OD1 B ASN A 193 ? 0.28798 0.29337 0.30440 0.01816  -0.00559 -0.01900 193 ASN A OD1 
2256 N ND2 A ASN A 193 ? 0.24708 0.24640 0.25877 0.02019  -0.00628 -0.01827 193 ASN A ND2 
2257 N ND2 B ASN A 193 ? 0.21280 0.23840 0.24961 0.00908  -0.00594 -0.01885 193 ASN A ND2 
2258 N N   . GLN A 194 ? 0.26898 0.21700 0.23592 0.01410  0.00097  -0.01127 194 GLN A N   
2259 C CA  . GLN A 194 ? 0.26415 0.19894 0.21859 0.01124  0.00369  -0.00979 194 GLN A CA  
2260 C C   . GLN A 194 ? 0.26201 0.20488 0.22852 0.01517  -0.00201 -0.00752 194 GLN A C   
2261 O O   . GLN A 194 ? 0.26752 0.21143 0.23396 0.01011  -0.00010 -0.00742 194 GLN A O   
2262 C CB  . GLN A 194 ? 0.30309 0.21451 0.23592 0.01558  0.00527  -0.00827 194 GLN A CB  
2263 C CG  . GLN A 194 ? 0.30014 0.20041 0.21744 0.01071  0.01241  -0.01010 194 GLN A CG  
2264 C CD  . GLN A 194 ? 0.43834 0.31593 0.33504 0.01589  0.01322  -0.00850 194 GLN A CD  
2265 O OE1 . GLN A 194 ? 0.43581 0.30013 0.32096 0.01550  0.01433  -0.00687 194 GLN A OE1 
2266 N NE2 . GLN A 194 ? 0.43753 0.31019 0.32923 0.02115  0.01238  -0.00895 194 GLN A NE2 
2267 N N   A MET A 195 ? 0.26525 0.21488 0.24332 0.02422  -0.00923 -0.00560 195 MET A N   
2268 N N   B MET A 195 ? 0.26695 0.21497 0.24362 0.02453  -0.00917 -0.00542 195 MET A N   
2269 C CA  A MET A 195 ? 0.23780 0.19509 0.22784 0.02886  -0.01457 -0.00272 195 MET A CA  
2270 C CA  B MET A 195 ? 0.23818 0.19595 0.22869 0.02888  -0.01466 -0.00275 195 MET A CA  
2271 C C   A MET A 195 ? 0.20556 0.18413 0.21449 0.02380  -0.01528 -0.00413 195 MET A C   
2272 C C   B MET A 195 ? 0.20518 0.18240 0.21194 0.02243  -0.01415 -0.00453 195 MET A C   
2273 O O   A MET A 195 ? 0.21209 0.19368 0.22476 0.02321  -0.01600 -0.00262 195 MET A O   
2274 O O   B MET A 195 ? 0.20482 0.18233 0.21124 0.01944  -0.01296 -0.00377 195 MET A O   
2275 C CB  A MET A 195 ? 0.22148 0.18032 0.21984 0.03981  -0.02230 0.00013  195 MET A CB  
2276 C CB  B MET A 195 ? 0.22672 0.19100 0.22997 0.03913  -0.02277 -0.00044 195 MET A CB  
2277 C CG  A MET A 195 ? 0.23625 0.17340 0.21676 0.04581  -0.02268 0.00245  195 MET A CG  
2278 C CG  B MET A 195 ? 0.26548 0.21104 0.25528 0.04694  -0.02501 0.00255  195 MET A CG  
2279 S SD  A MET A 195 ? 0.23376 0.17547 0.22754 0.05800  -0.03267 0.00540  195 MET A SD  
2280 S SD  B MET A 195 ? 0.23268 0.18558 0.23848 0.05870  -0.03527 0.00547  195 MET A SD  
2281 C CE  A MET A 195 ? 0.25222 0.16804 0.22547 0.06470  -0.03312 0.00892  195 MET A CE  
2282 C CE  B MET A 195 ? 0.28115 0.20886 0.26747 0.06586  -0.03622 0.00899  195 MET A CE  
2283 N N   . TYR A 196 ? 0.21219 0.20536 0.23277 0.02036  -0.01509 -0.00698 196 TYR A N   
2284 C CA  . TYR A 196 ? 0.18719 0.20021 0.22503 0.01466  -0.01527 -0.00863 196 TYR A CA  
2285 C C   . TYR A 196 ? 0.23095 0.23887 0.25941 0.00478  -0.00882 -0.01031 196 TYR A C   
2286 O O   . TYR A 196 ? 0.21864 0.23581 0.25585 0.00179  -0.00964 -0.01027 196 TYR A O   
2287 C CB  . TYR A 196 ? 0.17576 0.20440 0.22684 0.01294  -0.01600 -0.01138 196 TYR A CB  
2288 C CG  . TYR A 196 ? 0.18495 0.22324 0.25047 0.02241  -0.02392 -0.00988 196 TYR A CG  
2289 C CD1 . TYR A 196 ? 0.19080 0.23532 0.26810 0.02912  -0.03034 -0.00654 196 TYR A CD1 
2290 C CD2 . TYR A 196 ? 0.19319 0.23487 0.26129 0.02468  -0.02512 -0.01167 196 TYR A CD2 
2291 C CE1 . TYR A 196 ? 0.18555 0.23917 0.27740 0.03764  -0.03810 -0.00484 196 TYR A CE1 
2292 C CE2 . TYR A 196 ? 0.19911 0.24912 0.28062 0.03344  -0.03315 -0.01036 196 TYR A CE2 
2293 C CZ  . TYR A 196 ? 0.22094 0.27710 0.31481 0.03959  -0.03972 -0.00690 196 TYR A CZ  
2294 O OH  . TYR A 196 ? 0.24391 0.30853 0.35218 0.04795  -0.04799 -0.00529 196 TYR A OH  
2295 N N   . ASN A 197 ? 0.21491 0.20795 0.22564 -0.00031 -0.00257 -0.01172 197 ASN A N   
2296 C CA  . ASN A 197 ? 0.23806 0.22567 0.24010 -0.01015 0.00330  -0.01325 197 ASN A CA  
2297 C C   . ASN A 197 ? 0.26409 0.24286 0.25920 -0.00902 0.00228  -0.01122 197 ASN A C   
2298 O O   . ASN A 197 ? 0.26613 0.24919 0.26391 -0.01533 0.00364  -0.01227 197 ASN A O   
2299 C CB  . ASN A 197 ? 0.25822 0.22921 0.24128 -0.01458 0.00994  -0.01429 197 ASN A CB  
2300 C CG  . ASN A 197 ? 0.26789 0.24804 0.25693 -0.01798 0.01276  -0.01656 197 ASN A CG  
2301 O OD1 . ASN A 197 ? 0.24334 0.24281 0.25081 -0.01865 0.01025  -0.01784 197 ASN A OD1 
2302 N ND2 . ASN A 197 ? 0.30763 0.27356 0.28062 -0.01990 0.01823  -0.01692 197 ASN A ND2 
2303 N N   . ILE A 198 ? 0.23530 0.20074 0.22059 -0.00092 -0.00004 -0.00827 198 ILE A N   
2304 C CA  . ILE A 198 ? 0.27293 0.22838 0.25003 0.00137  -0.00079 -0.00591 198 ILE A CA  
2305 C C   . ILE A 198 ? 0.25395 0.22512 0.24915 0.00669  -0.00661 -0.00389 198 ILE A C   
2306 O O   . ILE A 198 ? 0.24203 0.21387 0.23713 0.00478  -0.00650 -0.00342 198 ILE A O   
2307 C CB  . ILE A 198 ? 0.28850 0.22310 0.24768 0.00783  -0.00056 -0.00332 198 ILE A CB  
2308 C CG1 . ILE A 198 ? 0.31129 0.22977 0.25179 0.00244  0.00558  -0.00519 198 ILE A CG1 
2309 C CG2 . ILE A 198 ? 0.30966 0.23411 0.26037 0.01062  -0.00119 -0.00067 198 ILE A CG2 
2310 C CD1 . ILE A 198 ? 0.39733 0.31023 0.32869 -0.00810 0.01121  -0.00736 198 ILE A CD1 
2311 N N   . LEU A 199 ? 0.23510 0.21901 0.24604 0.01353  -0.01187 -0.00262 199 LEU A N   
2312 C CA  . LEU A 199 ? 0.21028 0.21100 0.24050 0.01834  -0.01735 -0.00055 199 LEU A CA  
2313 C C   . LEU A 199 ? 0.21074 0.22627 0.25180 0.01057  -0.01611 -0.00318 199 LEU A C   
2314 O O   . LEU A 199 ? 0.21798 0.23997 0.26612 0.01242  -0.01830 -0.00154 199 LEU A O   
2315 C CB  . LEU A 199 ? 0.21194 0.22606 0.25927 0.02512  -0.02313 0.00048  199 LEU A CB  
2316 C CG  . LEU A 199 ? 0.22634 0.22885 0.26816 0.03517  -0.02686 0.00434  199 LEU A CG  
2317 C CD1 . LEU A 199 ? 0.22377 0.23687 0.27950 0.04028  -0.03213 0.00421  199 LEU A CD1 
2318 C CD2 . LEU A 199 ? 0.23435 0.23710 0.28071 0.04199  -0.03023 0.00902  199 LEU A CD2 
2319 N N   A ASP A 200 ? 0.20022 0.22121 0.24277 0.00199  -0.01256 -0.00710 200 ASP A N   
2320 N N   B ASP A 200 ? 0.20291 0.22449 0.24621 0.00240  -0.01283 -0.00704 200 ASP A N   
2321 C CA  A ASP A 200 ? 0.21244 0.24720 0.26551 -0.00583 -0.01154 -0.00966 200 ASP A CA  
2322 C CA  B ASP A 200 ? 0.21587 0.24931 0.26744 -0.00626 -0.01104 -0.00985 200 ASP A CA  
2323 C C   A ASP A 200 ? 0.21660 0.24017 0.25706 -0.01024 -0.00882 -0.00970 200 ASP A C   
2324 C C   B ASP A 200 ? 0.20841 0.23170 0.24900 -0.00908 -0.00925 -0.00930 200 ASP A C   
2325 O O   A ASP A 200 ? 0.20833 0.24233 0.25801 -0.01316 -0.01009 -0.01044 200 ASP A O   
2326 O O   B ASP A 200 ? 0.26362 0.29755 0.31450 -0.00925 -0.01164 -0.00905 200 ASP A O   
2327 C CB  A ASP A 200 ? 0.22839 0.26940 0.28419 -0.01441 -0.00767 -0.01347 200 ASP A CB  
2328 C CB  B ASP A 200 ? 0.25365 0.28643 0.30102 -0.01517 -0.00586 -0.01343 200 ASP A CB  
2329 C CG  A ASP A 200 ? 0.15492 0.21196 0.22721 -0.01105 -0.01085 -0.01415 200 ASP A CG  
2330 C CG  B ASP A 200 ? 0.29718 0.35201 0.36454 -0.01980 -0.00687 -0.01599 200 ASP A CG  
2331 O OD1 A ASP A 200 ? 0.16614 0.23454 0.25282 -0.00361 -0.01675 -0.01221 200 ASP A OD1 
2332 O OD1 B ASP A 200 ? 0.34134 0.40621 0.41769 -0.02405 -0.00768 -0.01693 200 ASP A OD1 
2333 O OD2 A ASP A 200 ? 0.23553 0.29414 0.30671 -0.01612 -0.00728 -0.01663 200 ASP A OD2 
2334 O OD2 B ASP A 200 ? 0.25014 0.31180 0.32366 -0.01913 -0.00684 -0.01712 200 ASP A OD2 
2335 N N   . ILE A 201 ? 0.24282 0.24495 0.26190 -0.01101 -0.00517 -0.00912 201 ILE A N   
2336 C CA  . ILE A 201 ? 0.23557 0.22543 0.24155 -0.01386 -0.00333 -0.00884 201 ILE A CA  
2337 C C   . ILE A 201 ? 0.25145 0.24541 0.26354 -0.00578 -0.00777 -0.00557 201 ILE A C   
2338 O O   . ILE A 201 ? 0.29094 0.28776 0.30446 -0.00815 -0.00827 -0.00600 201 ILE A O   
2339 C CB  . ILE A 201 ? 0.29629 0.26178 0.27827 -0.01423 0.00067  -0.00816 201 ILE A CB  
2340 C CG1 . ILE A 201 ? 0.28691 0.24807 0.26257 -0.02220 0.00560  -0.01099 201 ILE A CG1 
2341 C CG2 . ILE A 201 ? 0.30366 0.25593 0.27182 -0.01626 0.00190  -0.00774 201 ILE A CG2 
2342 C CD1 . ILE A 201 ? 0.33790 0.27547 0.29055 -0.02179 0.00949  -0.01010 201 ILE A CD1 
2343 N N   . VAL A 202 ? 0.23184 0.22634 0.24808 0.00408  -0.01121 -0.00208 202 VAL A N   
2344 C CA  . VAL A 202 ? 0.21450 0.21119 0.23558 0.01274  -0.01498 0.00200  202 VAL A CA  
2345 C C   . VAL A 202 ? 0.24878 0.26879 0.29310 0.01378  -0.01899 0.00204  202 VAL A C   
2346 O O   . VAL A 202 ? 0.27481 0.29896 0.32253 0.01532  -0.02022 0.00330  202 VAL A O   
2347 C CB  . VAL A 202 ? 0.24553 0.23441 0.26374 0.02275  -0.01741 0.00612  202 VAL A CB  
2348 C CG1 . VAL A 202 ? 0.28432 0.27504 0.30761 0.03203  -0.02087 0.01111  202 VAL A CG1 
2349 C CG2 . VAL A 202 ? 0.27665 0.24210 0.27135 0.02154  -0.01335 0.00589  202 VAL A CG2 
2350 N N   . SER A 203 ? 0.20873 0.24437 0.26923 0.01309  -0.02109 0.00060  203 SER A N   
2351 C CA  . SER A 203 ? 0.19102 0.24905 0.27453 0.01525  -0.02546 0.00113  203 SER A CA  
2352 C C   . SER A 203 ? 0.21099 0.27931 0.30036 0.00637  -0.02393 -0.00253 203 SER A C   
2353 O O   . SER A 203 ? 0.23515 0.31730 0.33833 0.00850  -0.02695 -0.00152 203 SER A O   
2354 C CB  . SER A 203 ? 0.19121 0.26257 0.29034 0.01778  -0.02873 0.00076  203 SER A CB  
2355 O OG  . SER A 203 ? 0.17077 0.24454 0.26859 0.00895  -0.02537 -0.00385 203 SER A OG  
2356 N N   A LYS A 204 ? 0.18589 0.24847 0.26617 -0.00343 -0.01951 -0.00659 204 LYS A N   
2357 N N   B LYS A 204 ? 0.19106 0.25202 0.26968 -0.00340 -0.01931 -0.00648 204 LYS A N   
2358 N N   C LYS A 204 ? 0.18818 0.24997 0.26767 -0.00339 -0.01942 -0.00653 204 LYS A N   
2359 C CA  A LYS A 204 ? 0.19130 0.26212 0.27644 -0.01229 -0.01823 -0.00998 204 LYS A CA  
2360 C CA  B LYS A 204 ? 0.19464 0.26576 0.28002 -0.01279 -0.01801 -0.01024 204 LYS A CA  
2361 C CA  C LYS A 204 ? 0.19533 0.26602 0.28029 -0.01263 -0.01804 -0.01014 204 LYS A CA  
2362 C C   A LYS A 204 ? 0.21543 0.26938 0.28215 -0.01612 -0.01540 -0.01046 204 LYS A C   
2363 C C   B LYS A 204 ? 0.20547 0.26194 0.27413 -0.01896 -0.01475 -0.01168 204 LYS A C   
2364 C C   C LYS A 204 ? 0.22268 0.27762 0.29020 -0.01701 -0.01524 -0.01085 204 LYS A C   
2365 O O   A LYS A 204 ? 0.17801 0.23527 0.24725 -0.01518 -0.01719 -0.00993 204 LYS A O   
2366 O O   B LYS A 204 ? 0.24603 0.31019 0.32075 -0.02283 -0.01576 -0.01316 204 LYS A O   
2367 O O   C LYS A 204 ? 0.20519 0.26536 0.27684 -0.01758 -0.01690 -0.01098 204 LYS A O   
2368 C CB  A LYS A 204 ? 0.18261 0.26084 0.27310 -0.02104 -0.01559 -0.01393 204 LYS A CB  
2369 C CB  B LYS A 204 ? 0.19081 0.27036 0.28305 -0.01977 -0.01593 -0.01370 204 LYS A CB  
2370 C CB  C LYS A 204 ? 0.19011 0.26607 0.27840 -0.02108 -0.01508 -0.01394 204 LYS A CB  
2371 C CG  A LYS A 204 ? 0.16672 0.26481 0.27794 -0.01798 -0.01896 -0.01411 204 LYS A CG  
2372 C CG  B LYS A 204 ? 0.18634 0.27599 0.29091 -0.01313 -0.01906 -0.01240 204 LYS A CG  
2373 C CG  C LYS A 204 ? 0.20662 0.30061 0.31382 -0.01808 -0.01805 -0.01414 204 LYS A CG  
2374 C CD  A LYS A 204 ? 0.11808 0.21886 0.22989 -0.02531 -0.01541 -0.01742 204 LYS A CD  
2375 C CD  B LYS A 204 ? 0.19603 0.30123 0.31421 -0.01868 -0.01852 -0.01563 204 LYS A CD  
2376 C CD  C LYS A 204 ? 0.12627 0.22449 0.23520 -0.02656 -0.01437 -0.01779 204 LYS A CD  
2377 C CE  A LYS A 204 ? 0.16368 0.28505 0.29634 -0.02308 -0.01876 -0.01815 204 LYS A CE  
2378 C CE  B LYS A 204 ? 0.16487 0.27094 0.28587 -0.01273 -0.02015 -0.01475 204 LYS A CE  
2379 C CE  C LYS A 204 ? 0.24038 0.35224 0.36383 -0.02228 -0.01710 -0.01782 204 LYS A CE  
2380 N NZ  A LYS A 204 ? 0.11663 0.23480 0.24872 -0.01489 -0.02092 -0.01623 204 LYS A NZ  
2381 N NZ  B LYS A 204 ? 0.18397 0.31107 0.32734 -0.00867 -0.02530 -0.01468 204 LYS A NZ  
2382 N NZ  C LYS A 204 ? 0.16475 0.29008 0.30450 -0.01390 -0.02345 -0.01524 204 LYS A NZ  
2383 N N   . ASN A 205 ? 0.20008 0.23526 0.24766 -0.02005 -0.01115 -0.01137 205 ASN A N   
2384 C CA  . ASN A 205 ? 0.24207 0.26215 0.27307 -0.02604 -0.00839 -0.01280 205 ASN A CA  
2385 C C   . ASN A 205 ? 0.30974 0.31908 0.33068 -0.01871 -0.01006 -0.00967 205 ASN A C   
2386 O O   . ASN A 205 ? 0.28089 0.28731 0.29743 -0.02159 -0.01039 -0.01069 205 ASN A O   
2387 C CB  . ASN A 205 ? 0.26384 0.26626 0.27707 -0.03160 -0.00346 -0.01412 205 ASN A CB  
2388 C CG  . ASN A 205 ? 0.30465 0.31632 0.32617 -0.03891 -0.00099 -0.01692 205 ASN A CG  
2389 O OD1 . ASN A 205 ? 0.36426 0.36575 0.37582 -0.04002 0.00238  -0.01698 205 ASN A OD1 
2390 N ND2 . ASN A 205 ? 0.30656 0.33731 0.34600 -0.04369 -0.00245 -0.01912 205 ASN A ND2 
2391 N N   . ILE A 206 ? 0.23379 0.23620 0.25017 -0.00911 -0.01111 -0.00577 206 ILE A N   
2392 C CA  . ILE A 206 ? 0.26658 0.25966 0.27432 -0.00139 -0.01246 -0.00225 206 ILE A CA  
2393 C C   . ILE A 206 ? 0.31285 0.32252 0.33636 0.00162  -0.01607 -0.00137 206 ILE A C   
2394 O O   . ILE A 206 ? 0.28909 0.29238 0.30477 0.00319  -0.01636 -0.00062 206 ILE A O   
2395 C CB  . ILE A 206 ? 0.35865 0.34310 0.36127 0.00864  -0.01322 0.00223  206 ILE A CB  
2396 C CG1 . ILE A 206 ? 0.38345 0.34618 0.36450 0.00571  -0.00917 0.00143  206 ILE A CG1 
2397 C CG2 . ILE A 206 ? 0.39076 0.37249 0.39190 0.01833  -0.01541 0.00684  206 ILE A CG2 
2398 C CD1 . ILE A 206 ? 0.41010 0.36270 0.38483 0.01521  -0.00992 0.00567  206 ILE A CD1 
2399 N N   A TYR A 207 ? 0.24435 0.27528 0.28987 0.00250  -0.01891 -0.00154 207 TYR A N   
2400 N N   B TYR A 207 ? 0.24898 0.28000 0.29455 0.00240  -0.01890 -0.00159 207 TYR A N   
2401 C CA  A TYR A 207 ? 0.22986 0.27760 0.29142 0.00521  -0.02232 -0.00071 207 TYR A CA  
2402 C CA  B TYR A 207 ? 0.23006 0.27792 0.29176 0.00531  -0.02236 -0.00067 207 TYR A CA  
2403 C C   A TYR A 207 ? 0.25966 0.30755 0.31784 -0.00345 -0.02138 -0.00466 207 TYR A C   
2404 C C   B TYR A 207 ? 0.26688 0.31580 0.32611 -0.00343 -0.02152 -0.00468 207 TYR A C   
2405 O O   A TYR A 207 ? 0.26795 0.31579 0.32476 -0.00045 -0.02284 -0.00356 207 TYR A O   
2406 O O   B TYR A 207 ? 0.27851 0.32944 0.33843 -0.00047 -0.02322 -0.00364 207 TYR A O   
2407 C CB  A TYR A 207 ? 0.25806 0.32846 0.34389 0.00692  -0.02558 -0.00054 207 TYR A CB  
2408 C CB  B TYR A 207 ? 0.25839 0.32867 0.34431 0.00755  -0.02571 -0.00025 207 TYR A CB  
2409 C CG  A TYR A 207 ? 0.25553 0.34302 0.35843 0.01181  -0.02939 0.00146  207 TYR A CG  
2410 C CG  B TYR A 207 ? 0.30322 0.38905 0.40579 0.01527  -0.02984 0.00317  207 TYR A CG  
2411 C CD1 A TYR A 207 ? 0.33829 0.42562 0.44377 0.02297  -0.03168 0.00705  207 TYR A CD1 
2412 C CD1 B TYR A 207 ? 0.32733 0.42244 0.43625 0.01226  -0.03084 0.00154  207 TYR A CD1 
2413 C CD2 A TYR A 207 ? 0.27597 0.37953 0.39240 0.00546  -0.03057 -0.00193 207 TYR A CD2 
2414 C CD2 B TYR A 207 ? 0.34520 0.43631 0.45746 0.02565  -0.03288 0.00823  207 TYR A CD2 
2415 C CE1 A TYR A 207 ? 0.48012 0.58305 0.60125 0.02787  -0.03486 0.00935  207 TYR A CE1 
2416 C CE1 B TYR A 207 ? 0.29439 0.40367 0.41833 0.01956  -0.03433 0.00489  207 TYR A CE1 
2417 C CE2 A TYR A 207 ? 0.24479 0.36395 0.37672 0.01020  -0.03402 0.00000  207 TYR A CE2 
2418 C CE2 B TYR A 207 ? 0.37431 0.47990 0.50251 0.03279  -0.03645 0.01186  207 TYR A CE2 
2419 C CZ  A TYR A 207 ? 0.33475 0.45340 0.46873 0.02151  -0.03603 0.00572  207 TYR A CZ  
2420 C CZ  B TYR A 207 ? 0.32922 0.44392 0.46299 0.02979  -0.03695 0.01018  207 TYR A CZ  
2421 O OH  A TYR A 207 ? 0.33330 0.46551 0.47880 0.02625  -0.03816 0.00784  207 TYR A OH  
2422 O OH  B TYR A 207 ? 0.34652 0.46918 0.48245 0.03551  -0.03694 0.01199  207 TYR A OH  
2423 N N   . SER A 208 ? 0.22544 0.27246 0.28148 -0.01406 -0.01894 -0.00909 208 SER A N   
2424 C CA  . SER A 208 ? 0.22744 0.27361 0.28033 -0.02290 -0.01839 -0.01282 208 SER A CA  
2425 C C   . SER A 208 ? 0.28797 0.31269 0.31866 -0.02219 -0.01716 -0.01229 208 SER A C   
2426 O O   . SER A 208 ? 0.25825 0.28300 0.28739 -0.02323 -0.01883 -0.01326 208 SER A O   
2427 C CB  . SER A 208 ? 0.37432 0.42151 0.42794 -0.03419 -0.01550 -0.01692 208 SER A CB  
2428 O OG  . SER A 208 ? 0.33581 0.40459 0.41097 -0.03602 -0.01695 -0.01815 208 SER A OG  
2429 N N   . ILE A 209 ? 0.27326 0.27891 0.28595 -0.02042 -0.01437 -0.01090 209 ILE A N   
2430 C CA  . ILE A 209 ? 0.31630 0.30049 0.30688 -0.01930 -0.01322 -0.01029 209 ILE A CA  
2431 C C   . ILE A 209 ? 0.27623 0.26133 0.26705 -0.00875 -0.01588 -0.00653 209 ILE A C   
2432 O O   . ILE A 209 ? 0.26369 0.23979 0.24376 -0.00874 -0.01654 -0.00708 209 ILE A O   
2433 C CB  . ILE A 209 ? 0.34494 0.30963 0.31749 -0.01850 -0.00979 -0.00911 209 ILE A CB  
2434 C CG1 . ILE A 209 ? 0.31186 0.27491 0.28314 -0.02925 -0.00669 -0.01271 209 ILE A CG1 
2435 C CG2 . ILE A 209 ? 0.34323 0.28528 0.29251 -0.01627 -0.00883 -0.00814 209 ILE A CG2 
2436 C CD1 . ILE A 209 ? 0.40708 0.35440 0.36409 -0.02812 -0.00326 -0.01146 209 ILE A CD1 
2437 N N   . PHE A 210 ? 0.27948 0.27463 0.28201 0.00069  -0.01747 -0.00241 210 PHE A N   
2438 C CA  . PHE A 210 ? 0.23882 0.23771 0.24493 0.01130  -0.01983 0.00194  210 PHE A CA  
2439 C C   . PHE A 210 ? 0.26287 0.27425 0.27883 0.00914  -0.02230 0.00007  210 PHE A C   
2440 O O   . PHE A 210 ? 0.25590 0.25944 0.26202 0.01297  -0.02289 0.00115  210 PHE A O   
2441 C CB  . PHE A 210 ? 0.20199 0.21423 0.22476 0.01984  -0.02171 0.00625  210 PHE A CB  
2442 C CG  . PHE A 210 ? 0.24640 0.26803 0.27910 0.03030  -0.02439 0.01108  210 PHE A CG  
2443 C CD1 . PHE A 210 ? 0.27350 0.28070 0.29163 0.03863  -0.02352 0.01520  210 PHE A CD1 
2444 C CD2 . PHE A 210 ? 0.28326 0.32799 0.33981 0.03219  -0.02759 0.01183  210 PHE A CD2 
2445 C CE1 . PHE A 210 ? 0.28915 0.30520 0.31673 0.04886  -0.02554 0.02030  210 PHE A CE1 
2446 C CE2 . PHE A 210 ? 0.26186 0.31564 0.32822 0.04210  -0.02986 0.01677  210 PHE A CE2 
2447 C CZ  . PHE A 210 ? 0.23028 0.26957 0.28203 0.05061  -0.02866 0.02120  210 PHE A CZ  
2448 N N   . ILE A 211 ? 0.23902 0.26961 0.27405 0.00322  -0.02383 -0.00278 211 ILE A N   
2449 C CA  . ILE A 211 ? 0.21123 0.25459 0.25673 0.00069  -0.02638 -0.00481 211 ILE A CA  
2450 C C   . ILE A 211 ? 0.24030 0.26864 0.26864 -0.00644 -0.02562 -0.00852 211 ILE A C   
2451 O O   . ILE A 211 ? 0.23048 0.25837 0.25625 -0.00401 -0.02756 -0.00850 211 ILE A O   
2452 C CB  . ILE A 211 ? 0.17670 0.24239 0.24498 -0.00539 -0.02786 -0.00755 211 ILE A CB  
2453 C CG1 . ILE A 211 ? 0.19655 0.27765 0.28278 0.00293  -0.02966 -0.00354 211 ILE A CG1 
2454 C CG2 . ILE A 211 ? 0.19072 0.26801 0.26827 -0.00992 -0.03033 -0.01049 211 ILE A CG2 
2455 C CD1 . ILE A 211 ? 0.18405 0.27384 0.27911 0.01360  -0.03242 0.00110  211 ILE A CD1 
2456 N N   . PHE A 212 ? 0.23247 0.24858 0.24934 -0.01550 -0.02303 -0.01180 212 PHE A N   
2457 C CA  . PHE A 212 ? 0.23358 0.23399 0.23379 -0.02262 -0.02268 -0.01518 212 PHE A CA  
2458 C C   . PHE A 212 ? 0.29800 0.28027 0.27867 -0.01462 -0.02290 -0.01256 212 PHE A C   
2459 O O   . PHE A 212 ? 0.28903 0.26584 0.26250 -0.01553 -0.02488 -0.01417 212 PHE A O   
2460 C CB  . PHE A 212 ? 0.28338 0.27198 0.27360 -0.03208 -0.01937 -0.01785 212 PHE A CB  
2461 C CG  . PHE A 212 ? 0.32860 0.29886 0.30060 -0.03905 -0.01915 -0.02079 212 PHE A CG  
2462 C CD1 . PHE A 212 ? 0.29957 0.27558 0.27768 -0.04851 -0.02105 -0.02487 212 PHE A CD1 
2463 C CD2 . PHE A 212 ? 0.36040 0.30762 0.30944 -0.03567 -0.01755 -0.01932 212 PHE A CD2 
2464 C CE1 . PHE A 212 ? 0.34954 0.30829 0.31140 -0.05497 -0.02162 -0.02753 212 PHE A CE1 
2465 C CE2 . PHE A 212 ? 0.42699 0.35664 0.35899 -0.04199 -0.01789 -0.02206 212 PHE A CE2 
2466 C CZ  . PHE A 212 ? 0.37414 0.30950 0.31274 -0.05176 -0.02014 -0.02619 212 PHE A CZ  
2467 N N   . ILE A 213 ? 0.25543 0.22766 0.22690 -0.00652 -0.02098 -0.00849 213 ILE A N   
2468 C CA  . ILE A 213 ? 0.29153 0.24592 0.24380 0.00168  -0.02073 -0.00559 213 ILE A CA  
2469 C C   . ILE A 213 ? 0.29665 0.26141 0.25711 0.01082  -0.02343 -0.00271 213 ILE A C   
2470 O O   . ILE A 213 ? 0.31046 0.26378 0.25709 0.01399  -0.02431 -0.00261 213 ILE A O   
2471 C CB  . ILE A 213 ? 0.30000 0.24227 0.24206 0.00820  -0.01799 -0.00164 213 ILE A CB  
2472 C CG1 . ILE A 213 ? 0.34656 0.27522 0.27661 -0.00092 -0.01509 -0.00468 213 ILE A CG1 
2473 C CG2 . ILE A 213 ? 0.37010 0.29657 0.29492 0.01815  -0.01772 0.00213  213 ILE A CG2 
2474 C CD1 . ILE A 213 ? 0.34825 0.26661 0.27019 0.00459  -0.01247 -0.00122 213 ILE A CD1 
2475 N N   . VAL A 214 ? 0.27681 0.26296 0.25951 0.01548  -0.02484 -0.00019 214 VAL A N   
2476 C CA  . VAL A 214 ? 0.25005 0.24837 0.24297 0.02336  -0.02737 0.00246  214 VAL A CA  
2477 C C   . VAL A 214 ? 0.29756 0.29792 0.28977 0.01664  -0.02966 -0.00220 214 VAL A C   
2478 O O   . VAL A 214 ? 0.26833 0.26259 0.25172 0.02204  -0.03088 -0.00117 214 VAL A O   
2479 C CB  . VAL A 214 ? 0.23349 0.25553 0.25223 0.02806  -0.02885 0.00555  214 VAL A CB  
2480 C CG1 . VAL A 214 ? 0.25685 0.29245 0.28713 0.03531  -0.03141 0.00811  214 VAL A CG1 
2481 C CG2 . VAL A 214 ? 0.26291 0.28044 0.28053 0.03643  -0.02724 0.01091  214 VAL A CG2 
2482 N N   . ILE A 215 ? 0.22717 0.23521 0.22790 0.00481  -0.03029 -0.00734 215 ILE A N   
2483 C CA  . ILE A 215 ? 0.23094 0.24099 0.23200 -0.00236 -0.03287 -0.01191 215 ILE A CA  
2484 C C   . ILE A 215 ? 0.24514 0.23078 0.22056 -0.00355 -0.03284 -0.01358 215 ILE A C   
2485 O O   . ILE A 215 ? 0.28759 0.27018 0.25757 -0.00136 -0.03541 -0.01446 215 ILE A O   
2486 C CB  . ILE A 215 ? 0.26327 0.28419 0.27715 -0.01526 -0.03299 -0.01674 215 ILE A CB  
2487 C CG1 . ILE A 215 ? 0.21130 0.25828 0.25173 -0.01355 -0.03413 -0.01554 215 ILE A CG1 
2488 C CG2 . ILE A 215 ? 0.27396 0.29043 0.28293 -0.02444 -0.03544 -0.02181 215 ILE A CG2 
2489 C CD1 . ILE A 215 ? 0.21820 0.27623 0.27157 -0.02513 -0.03351 -0.01959 215 ILE A CD1 
2490 N N   A LEU A 216 ? 0.28737 0.25500 0.24650 -0.00736 -0.03017 -0.01428 216 LEU A N   
2491 N N   B LEU A 216 ? 0.28983 0.25719 0.24865 -0.00713 -0.03015 -0.01419 216 LEU A N   
2492 C CA  A LEU A 216 ? 0.28884 0.23270 0.22363 -0.00964 -0.03045 -0.01629 216 LEU A CA  
2493 C CA  B LEU A 216 ? 0.30588 0.24881 0.23950 -0.00797 -0.03029 -0.01562 216 LEU A CA  
2494 C C   A LEU A 216 ? 0.32818 0.26124 0.24911 0.00299  -0.03085 -0.01233 216 LEU A C   
2495 C C   B LEU A 216 ? 0.34756 0.28239 0.26993 0.00510  -0.03081 -0.01144 216 LEU A C   
2496 O O   A LEU A 216 ? 0.36887 0.29026 0.27620 0.00339  -0.03312 -0.01413 216 LEU A O   
2497 O O   B LEU A 216 ? 0.38476 0.31059 0.29589 0.00626  -0.03325 -0.01298 216 LEU A O   
2498 C CB  A LEU A 216 ? 0.38559 0.31336 0.30691 -0.01526 -0.02715 -0.01710 216 LEU A CB  
2499 C CB  B LEU A 216 ? 0.37876 0.30412 0.29718 -0.01209 -0.02690 -0.01590 216 LEU A CB  
2500 C CG  A LEU A 216 ? 0.43647 0.33823 0.33201 -0.01826 -0.02724 -0.01908 216 LEU A CG  
2501 C CG  B LEU A 216 ? 0.41232 0.33206 0.32801 -0.02619 -0.02641 -0.02083 216 LEU A CG  
2502 C CD1 A LEU A 216 ? 0.59723 0.49804 0.49301 -0.02899 -0.03052 -0.02438 216 LEU A CD1 
2503 C CD1 B LEU A 216 ? 0.48919 0.38738 0.38497 -0.02735 -0.02310 -0.02015 216 LEU A CD1 
2504 C CD2 A LEU A 216 ? 0.50916 0.39702 0.39329 -0.02175 -0.02342 -0.01870 216 LEU A CD2 
2505 C CD2 B LEU A 216 ? 0.43098 0.34546 0.34141 -0.03276 -0.03012 -0.02504 216 LEU A CD2 
2506 N N   A ASN A 217 ? 0.35418 0.29153 0.27916 0.01371  -0.02886 -0.00675 217 ASN A N   
2507 N N   B ASN A 217 ? 0.35794 0.29603 0.28360 0.01536  -0.02865 -0.00592 217 ASN A N   
2508 C CA  A ASN A 217 ? 0.40637 0.33521 0.32013 0.02680  -0.02864 -0.00197 217 ASN A CA  
2509 C CA  B ASN A 217 ? 0.41221 0.34225 0.32722 0.02852  -0.02838 -0.00102 217 ASN A CA  
2510 C C   A ASN A 217 ? 0.40927 0.35082 0.33267 0.03181  -0.03166 -0.00143 217 ASN A C   
2511 C C   B ASN A 217 ? 0.40495 0.34741 0.32928 0.03341  -0.03137 -0.00053 217 ASN A C   
2512 O O   A ASN A 217 ? 0.43152 0.36090 0.33960 0.03781  -0.03263 -0.00070 217 ASN A O   
2513 O O   B ASN A 217 ? 0.43077 0.36175 0.34046 0.04085  -0.03200 0.00105  217 ASN A O   
2514 C CB  A ASN A 217 ? 0.43698 0.36936 0.35603 0.03625  -0.02593 0.00417  217 ASN A CB  
2515 C CB  B ASN A 217 ? 0.44173 0.37649 0.36330 0.03789  -0.02582 0.00512  217 ASN A CB  
2516 C CG  A ASN A 217 ? 0.59545 0.52434 0.50875 0.05069  -0.02550 0.01022  217 ASN A CG  
2517 C CG  B ASN A 217 ? 0.57795 0.50905 0.49368 0.05223  -0.02537 0.01118  217 ASN A CG  
2518 O OD1 A ASN A 217 ? 0.62905 0.57536 0.56001 0.05841  -0.02607 0.01454  217 ASN A OD1 
2519 O OD1 B ASN A 217 ? 0.60596 0.55464 0.53918 0.05964  -0.02623 0.01513  217 ASN A OD1 
2520 N ND2 A ASN A 217 ? 0.55469 0.46098 0.44341 0.05456  -0.02444 0.01080  217 ASN A ND2 
2521 N ND2 B ASN A 217 ? 0.54791 0.45612 0.43911 0.05638  -0.02394 0.01215  217 ASN A ND2 
2522 N N   . GLN A 218 ? 0.31363 0.27928 0.26182 0.02965  -0.03321 -0.00182 218 GLN A N   
2523 C CA  . GLN A 218 ? 0.33413 0.31264 0.29229 0.03424  -0.03605 -0.00131 218 GLN A CA  
2524 C C   . GLN A 218 ? 0.42376 0.39395 0.37173 0.02701  -0.03918 -0.00698 218 GLN A C   
2525 O O   . GLN A 218 ? 0.40785 0.37800 0.35244 0.03306  -0.04130 -0.00632 218 GLN A O   
2526 C CB  . GLN A 218 ? 0.28682 0.29302 0.27421 0.03218  -0.03728 -0.00106 218 GLN A CB  
2527 C CG  . GLN A 218 ? 0.31220 0.32982 0.31312 0.04142  -0.03548 0.00527  218 GLN A CG  
2528 C CD  . GLN A 218 ? 0.43471 0.44882 0.43007 0.05575  -0.03483 0.01162  218 GLN A CD  
2529 O OE1 . GLN A 218 ? 0.55293 0.57853 0.55744 0.06089  -0.03667 0.01310  218 GLN A OE1 
2530 N NE2 . GLN A 218 ? 0.49525 0.49295 0.47499 0.06237  -0.03205 0.01551  218 GLN A NE2 
2531 N N   . SER A 219 ? 0.34161 0.30445 0.28464 0.01436  -0.03964 -0.01236 219 SER A N   
2532 C CA  . SER A 219 ? 0.44532 0.40507 0.38501 0.00577  -0.04340 -0.01797 219 SER A CA  
2533 C C   . SER A 219 ? 0.56962 0.50241 0.48285 0.00185  -0.04404 -0.02086 219 SER A C   
2534 O O   . SER A 219 ? 0.61305 0.54116 0.52252 -0.00617 -0.04761 -0.02570 219 SER A O   
2535 C CB  . SER A 219 ? 0.44027 0.41611 0.39933 -0.00706 -0.04422 -0.02216 219 SER A CB  
2536 O OG  . SER A 219 ? 0.50661 0.50672 0.48993 -0.00385 -0.04352 -0.01956 219 SER A OG  
2537 N N   A TYR A 220 ? 0.49694 0.41171 0.39199 0.00719  -0.04101 -0.01800 220 TYR A N   
2538 N N   B TYR A 220 ? 0.49687 0.41164 0.39191 0.00725  -0.04102 -0.01799 220 TYR A N   
2539 C CA  A TYR A 220 ? 0.69148 0.58115 0.56295 0.00143  -0.04142 -0.02111 220 TYR A CA  
2540 C CA  B TYR A 220 ? 0.69144 0.58107 0.56286 0.00152  -0.04138 -0.02106 220 TYR A CA  
2541 C C   A TYR A 220 ? 0.86910 0.74544 0.72507 0.00281  -0.04575 -0.02374 220 TYR A C   
2542 C C   B TYR A 220 ? 0.86942 0.74532 0.72491 0.00303  -0.04566 -0.02364 220 TYR A C   
2543 O O   A TYR A 220 ? 0.96670 0.82716 0.80930 -0.00579 -0.04806 -0.02809 220 TYR A O   
2544 O O   B TYR A 220 ? 0.96870 0.82796 0.80999 -0.00522 -0.04786 -0.02785 220 TYR A O   
2545 C CB  A TYR A 220 ? 0.69979 0.57266 0.55440 0.00782  -0.03741 -0.01732 220 TYR A CB  
2546 C CB  B TYR A 220 ? 0.69976 0.57315 0.55488 0.00802  -0.03731 -0.01718 220 TYR A CB  
2547 C CG  A TYR A 220 ? 0.82525 0.67307 0.65697 0.00091  -0.03762 -0.02055 220 TYR A CG  
2548 C CG  B TYR A 220 ? 0.68594 0.55115 0.52869 0.02287  -0.03661 -0.01228 220 TYR A CG  
2549 C CD1 A TYR A 220 ? 0.81657 0.66286 0.65121 -0.01145 -0.03646 -0.02367 220 TYR A CD1 
2550 C CD1 B TYR A 220 ? 0.71222 0.59429 0.56995 0.03341  -0.03514 -0.00694 220 TYR A CD1 
2551 C CD2 A TYR A 220 ? 0.84278 0.66837 0.64995 0.00694  -0.03898 -0.02031 220 TYR A CD2 
2552 C CD2 B TYR A 220 ? 0.81406 0.65447 0.63020 0.02656  -0.03740 -0.01275 220 TYR A CD2 
2553 C CE1 A TYR A 220 ? 0.90339 0.72695 0.71782 -0.01789 -0.03673 -0.02632 220 TYR A CE1 
2554 C CE1 B TYR A 220 ? 0.90462 0.77955 0.75168 0.04729  -0.03407 -0.00185 220 TYR A CE1 
2555 C CE2 A TYR A 220 ? 1.00140 0.80382 0.78779 0.00061  -0.03959 -0.02325 220 TYR A CE2 
2556 C CE2 B TYR A 220 ? 0.89969 0.73240 0.70405 0.04060  -0.03636 -0.00799 220 TYR A CE2 
2557 C CZ  A TYR A 220 ? 1.01507 0.81674 0.80558 -0.01196 -0.03850 -0.02618 220 TYR A CZ  
2558 C CZ  B TYR A 220 ? 0.92597 0.77621 0.74607 0.05095  -0.03448 -0.00238 220 TYR A CZ  
2559 O OH  A TYR A 220 ? 1.19646 0.97518 0.96691 -0.01831 -0.03917 -0.02879 220 TYR A OH  
2560 O OH  B TYR A 220 ? 1.06317 0.90611 0.87218 0.06522  -0.03305 0.00294  220 TYR A OH  
2561 N N   . LYS A 221 ? 0.95381 0.83601 0.81129 0.01360  -0.04709 -0.02109 221 LYS A N   
2562 C CA  . LYS A 221 ? 0.89773 0.76769 0.74057 0.01546  -0.05155 -0.02375 221 LYS A CA  
2563 C C   . LYS A 221 ? 0.99242 0.87229 0.84771 0.00385  -0.05627 -0.02950 221 LYS A C   
2564 O O   . LYS A 221 ? 1.07550 0.94010 0.91669 -0.00115 -0.06054 -0.03377 221 LYS A O   
2565 C CB  . LYS A 221 ? 0.84759 0.72129 0.68858 0.03070  -0.05126 -0.01899 221 LYS A CB  
2566 C CG  . LYS A 221 ? 0.86706 0.72637 0.69125 0.04273  -0.04718 -0.01338 221 LYS A CG  
2567 N N   . LEU A 222 ? 0.89749 0.80255 0.77925 -0.00060 -0.05586 -0.02966 222 LEU A N   
2568 C CA  . LEU A 222 ? 0.98684 0.90223 0.88203 -0.01260 -0.05990 -0.03498 222 LEU A CA  
2569 C C   . LEU A 222 ? 1.10388 1.00854 0.99412 -0.02649 -0.06011 -0.03909 222 LEU A C   
2570 O O   . LEU A 222 ? 1.14313 1.04829 1.03726 -0.03662 -0.06426 -0.04380 222 LEU A O   
2571 C CB  . LEU A 222 ? 0.88343 0.82835 0.80817 -0.01390 -0.05893 -0.03392 222 LEU A CB  
2572 C CG  . LEU A 222 ? 0.75888 0.71891 0.69399 -0.00104 -0.05842 -0.02934 222 LEU A CG  
2573 C CD1 . LEU A 222 ? 0.60272 0.59087 0.56723 -0.00431 -0.05745 -0.02868 222 LEU A CD1 
2574 C CD2 . LEU A 222 ? 0.81744 0.77359 0.74544 0.00331  -0.06302 -0.03096 222 LEU A CD2 
2575 N N   . LEU A 223 ? 1.06104 0.95628 0.94341 -0.02716 -0.05575 -0.03718 223 LEU A N   
2576 C CA  . LEU A 223 ? 1.19048 1.07479 1.06743 -0.03979 -0.05539 -0.04047 223 LEU A CA  
2577 C C   . LEU A 223 ? 1.41699 1.27281 1.26665 -0.04052 -0.05807 -0.04249 223 LEU A C   
2578 O O   . LEU A 223 ? 1.58318 1.43073 1.42942 -0.05142 -0.06156 -0.04679 223 LEU A O   
2579 C CB  . LEU A 223 ? 0.98541 0.87227 0.86604 -0.04026 -0.04954 -0.03760 223 LEU A CB  
2580 C CG  . LEU A 223 ? 0.87609 0.78716 0.78274 -0.04634 -0.04725 -0.03761 223 LEU A CG  
2581 C CD1 . LEU A 223 ? 0.81574 0.72469 0.72083 -0.04453 -0.04182 -0.03449 223 LEU A CD1 
2582 C CD2 . LEU A 223 ? 0.77016 0.68538 0.68598 -0.06109 -0.04949 -0.04242 223 LEU A CD2 
2583 N N   . LEU A 224 ? 1.29840 1.13880 1.12871 -0.02903 -0.05660 -0.03927 224 LEU A N   
2584 C CA  . LEU A 224 ? 1.33189 1.14414 1.13480 -0.02855 -0.05897 -0.04090 224 LEU A CA  
2585 C C   . LEU A 224 ? 1.46737 1.27326 1.26155 -0.02435 -0.06490 -0.04310 224 LEU A C   
2586 O O   . LEU A 224 ? 1.21997 1.04259 1.02745 -0.01907 -0.06618 -0.04226 224 LEU A O   
2587 C CB  . LEU A 224 ? 1.27733 1.07502 1.06249 -0.01789 -0.05457 -0.03638 224 LEU A CB  
# 
