data_4653 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4653 _Entry.Title ; Solution structure of third intradiskal loop of bovine rhodopsin (residues 268-293) ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2000-01-28 _Entry.Accession_date 2001-03-16 _Entry.Last_release_date 2001-05-09 _Entry.Original_release_date 2001-05-09 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 P. Yeagle . L. . 4653 2 A. Salloum . . . 4653 3 A. Chopra . . . 4653 4 N. Bhawsar . . . 4653 5 L. Ali . . . 4653 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4653 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 159 4653 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2001-05-09 2000-01-28 original author . 4653 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4653 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10888202 _Citation.Full_citation . _Citation.Title ; Structures of the intradiskal loops and amino terminus of the G-protein receptor, rhodopsin ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Pept. Res.' _Citation.Journal_name_full . _Citation.Journal_volume 55 _Citation.Journal_issue 6 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 455 _Citation.Page_last 465 _Citation.Year 2000 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 P. Yeagle . L. . 4653 1 2 A. Salloum . . . 4653 1 3 A. Chopra . . . 4653 1 4 N. Bhawsar . . . 4653 1 5 L. Ali . . . 4653 1 6 G. Kuzmanovski . . . 4653 1 7 J. Alderfer . L. . 4653 1 8 A. Albert . D. . 4653 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID helix 4653 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_RHODOPSIN _Assembly.Sf_category assembly _Assembly.Sf_framecode system_RHODOPSIN _Assembly.Entry_ID 4653 _Assembly.ID 1 _Assembly.Name 'Third intradiskal loop of RHODOPSIN (Residues 268-293)' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4653 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 RHODOPSIN 1 $RHODOPSIN . . . native . . . . . 4653 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID . PDB 1EDW . . . . . . 4653 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Third intradiskal loop of RHODOPSIN (Residues 268-293)' system 4653 1 RHODOPSIN abbreviation 4653 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_RHODOPSIN _Entity.Sf_category entity _Entity.Sf_framecode RHODOPSIN _Entity.Entry_ID 4653 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name RHODOPSIN _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; YAGVAFYIFTHQGSDFGPIF MTIPAF ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 26 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1EDW . "Solution Structure Of Third Intradiskal Loop Of Bovine Rhodopsin (Residues 268-293)" . . . . . 100.00 26 100.00 100.00 2.46e-08 . . . . 4653 1 2 no PDB 1F88 . "Crystal Structure Of Bovine Rhodopsin" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 3 no PDB 1GZM . "Structure Of Bovine Rhodopsin In A Trigonal Crystal Form" . . . . . 100.00 349 100.00 100.00 8.97e-08 . . . . 4653 1 4 no PDB 1HZX . "Crystal Structure Of Bovine Rhodopsin" . . . . . 100.00 349 100.00 100.00 8.97e-08 . . . . 4653 1 5 no PDB 1JFP . "Structure Of Bovine Rhodopsin (Dark Adapted)" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 6 no PDB 1L9H . "Crystal Structure Of Bovine Rhodopsin At 2.6 Angstroms Resolution" . . . . . 100.00 349 100.00 100.00 8.97e-08 . . . . 4653 1 7 no PDB 1LN6 . "Structure Of Bovine Rhodopsin (Metarhodopsin Ii)" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 8 no PDB 1U19 . "Crystal Structure Of Bovine Rhodopsin At 2.2 Angstroms Resolution" . . . . . 100.00 349 100.00 100.00 8.97e-08 . . . . 4653 1 9 no PDB 2G87 . "Crystallographic Model Of Bathorhodopsin" . . . . . 100.00 349 100.00 100.00 8.97e-08 . . . . 4653 1 10 no PDB 2HPY . "Crystallographic Model Of Lumirhodopsin" . . . . . 100.00 349 100.00 100.00 8.97e-08 . . . . 4653 1 11 no PDB 2I35 . "Crystal Structure Of Rhombohedral Crystal Form Of Ground-State Rhodopsin" . . . . . 100.00 349 100.00 100.00 8.97e-08 . . . . 4653 1 12 no PDB 2I36 . "Crystal Structure Of Trigonal Crystal Form Of Ground-State Rhodopsin" . . . . . 100.00 349 100.00 100.00 8.97e-08 . . . . 4653 1 13 no PDB 2I37 . "Crystal Structure Of A Photoactivated Rhodopsin" . . . . . 100.00 349 100.00 100.00 8.97e-08 . . . . 4653 1 14 no PDB 2PED . "Crystallographic Model Of 9-Cis-Rhodopsin" . . . . . 100.00 349 100.00 100.00 8.97e-08 . . . . 4653 1 15 no PDB 3C9L . "Structure Of Ground-State Bovine Rhodospin In A Hexagonal Crystal Form" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 16 no PDB 3CAP . "Crystal Structure Of Native Opsin: The G Protein-Coupled Receptor Rhodopsin In Its Ligand-Free State" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 17 no PDB 3DQB . "Crystal Structure Of The Active G-protein-coupled Receptor Opsin In Complex With A C-terminal Peptide Derived From The Galpha S" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 18 no PDB 3OAX . "Crystal Structure Of Bovine Rhodopsin With Beta-Ionone" . . . . . 100.00 349 100.00 100.00 8.97e-08 . . . . 4653 1 19 no PDB 3PQR . "Crystal Structure Of Metarhodopsin Ii In Complex With A C-Terminal Peptide Derived From The Galpha Subunit Of Transducin" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 20 no PDB 3PXO . "Crystal Structure Of Metarhodopsin Ii" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 21 no PDB 4J4Q . "Crystal Structure Of Active Conformation Of Gpcr Opsin Stabilized By Octylglucoside" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 22 no PDB 4PXF . "Crystal Structure Of The Active G-protein-coupled Receptor Opsin In Complex With The Finger-loop Peptide Derived From The Full-" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 23 no PDB 4X1H . "Opsin/g(alpha) Peptide Complex Stabilized By Nonyl-glucoside" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 24 no DBJ BAB83621 . "rhodopsin [synthetic construct]" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 25 no GB AAA30674 . "rhodopsin [Bos taurus]" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 26 no GB ADB43478 . "rhodopsin, partial [Tragelaphus eurycerus]" . . . . . 88.46 72 100.00 100.00 9.68e-07 . . . . 4653 1 27 no GB AGL13378 . "rhodopsin, partial [Hippopotamus amphibius]" . . . . . 100.00 135 100.00 100.00 1.36e-08 . . . . 4653 1 28 no GB ELR51227 . "Rhodopsin, partial [Bos mutus]" . . . . . 100.00 351 100.00 100.00 8.44e-08 . . . . 4653 1 29 no PRF 0811197A . rhodopsin . . . . . 100.00 347 100.00 100.00 8.46e-08 . . . . 4653 1 30 no PRF 0901188A . rhodopsin . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 31 no PRF 0901212A . rhodopsin . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 32 no PRF 0906201A . rhodopsin . . . . . 100.00 299 100.00 100.00 7.64e-08 . . . . 4653 1 33 no PRF 1001148A . rhodopsin . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 34 no REF NP_001014890 . "rhodopsin [Bos taurus]" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 35 no REF XP_004018583 . "PREDICTED: rhodopsin isoform X4 [Ovis aries]" . . . . . 100.00 348 100.00 100.00 8.01e-08 . . . . 4653 1 36 no REF XP_005902896 . "PREDICTED: rhodopsin [Bos mutus]" . . . . . 100.00 348 100.00 100.00 8.33e-08 . . . . 4653 1 37 no REF XP_005955807 . "PREDICTED: LOW QUALITY PROTEIN: rhodopsin [Pantholops hodgsonii]" . . . . . 100.00 375 100.00 100.00 9.91e-08 . . . . 4653 1 38 no REF XP_006078962 . "PREDICTED: rhodopsin [Bubalus bubalis]" . . . . . 100.00 348 100.00 100.00 8.67e-08 . . . . 4653 1 39 no SP P02699 . "RecName: Full=Rhodopsin" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 40 no SP P02700 . "RecName: Full=Rhodopsin" . . . . . 100.00 348 100.00 100.00 7.93e-08 . . . . 4653 1 41 no TPG DAA16827 . "TPA: rhodopsin [Bos taurus]" . . . . . 100.00 348 100.00 100.00 8.93e-08 . . . . 4653 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID RHODOPSIN common 4653 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 268 TYR . 4653 1 2 269 ALA . 4653 1 3 270 GLY . 4653 1 4 271 VAL . 4653 1 5 272 ALA . 4653 1 6 273 PHE . 4653 1 7 274 TYR . 4653 1 8 275 ILE . 4653 1 9 276 PHE . 4653 1 10 277 THR . 4653 1 11 278 HIS . 4653 1 12 279 GLN . 4653 1 13 280 GLY . 4653 1 14 281 SER . 4653 1 15 282 ASP . 4653 1 16 283 PHE . 4653 1 17 284 GLY . 4653 1 18 285 PRO . 4653 1 19 286 ILE . 4653 1 20 287 PHE . 4653 1 21 288 MET . 4653 1 22 289 THR . 4653 1 23 290 ILE . 4653 1 24 291 PRO . 4653 1 25 292 ALA . 4653 1 26 293 PHE . 4653 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . TYR 1 1 4653 1 . ALA 2 2 4653 1 . GLY 3 3 4653 1 . VAL 4 4 4653 1 . ALA 5 5 4653 1 . PHE 6 6 4653 1 . TYR 7 7 4653 1 . ILE 8 8 4653 1 . PHE 9 9 4653 1 . THR 10 10 4653 1 . HIS 11 11 4653 1 . GLN 12 12 4653 1 . GLY 13 13 4653 1 . SER 14 14 4653 1 . ASP 15 15 4653 1 . PHE 16 16 4653 1 . GLY 17 17 4653 1 . PRO 18 18 4653 1 . ILE 19 19 4653 1 . PHE 20 20 4653 1 . MET 21 21 4653 1 . THR 22 22 4653 1 . ILE 23 23 4653 1 . PRO 24 24 4653 1 . ALA 25 25 4653 1 . PHE 26 26 4653 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4653 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $RHODOPSIN . 9913 organism . 'Bos taurus' cow . . Eukaryota Metazoa Bos taurus . . . . . . . . . . . . . . . . . . . . . 4653 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 4653 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $RHODOPSIN . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4653 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4653 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 RHODOPSIN . . . 1 $RHODOPSIN . . 2 . . mM . . . . 4653 1 2 DMSO . . . . . . . . . . % . . . . 4653 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_1 _Sample_condition_list.Entry_ID 4653 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID temperature 303 . K 4653 1 pressure 1 . atm 4653 1 stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 4653 _Software.ID 1 _Software.Name FELIX _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 4653 1 stop_ save_ save_DIANA _Software.Sf_category software _Software.Sf_framecode DIANA _Software.Entry_ID 4653 _Software.ID 2 _Software.Name DIANA _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 4653 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 4653 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4653 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker AMX . 600 . . . 4653 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 4653 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D NOESY' . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4653 1 2 DQF-COSY . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4653 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_ref_1 _Chem_shift_reference.Entry_ID 4653 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 . . . . . . ppm . . . . . . . 1 $entry_citation . . 1 $entry_citation 4653 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_set_1 _Assigned_chem_shift_list.Entry_ID 4653 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_ref_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_1 . 4653 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 TYR H H 1 7.87 . . . . . . . . . . . 4653 1 2 . 1 1 1 1 TYR HA H 1 4.53 . . . . . . . . . . . 4653 1 3 . 1 1 1 1 TYR HB2 H 1 2.62 . . . . . . . . . . . 4653 1 4 . 1 1 1 1 TYR HB3 H 1 2.77 . . . . . . . . . . . 4653 1 5 . 1 1 1 1 TYR HD1 H 1 7.04 . . . . . . . . . . . 4653 1 6 . 1 1 1 1 TYR HD2 H 1 7.04 . . . . . . . . . . . 4653 1 7 . 1 1 2 2 ALA H H 1 8.09 . . . . . . . . . . . 4653 1 8 . 1 1 2 2 ALA HA H 1 4.49 . . . . . . . . . . . 4653 1 9 . 1 1 2 2 ALA HB1 H 1 1.36 . . . . . . . . . . . 4653 1 10 . 1 1 2 2 ALA HB2 H 1 1.36 . . . . . . . . . . . 4653 1 11 . 1 1 2 2 ALA HB3 H 1 1.36 . . . . . . . . . . . 4653 1 12 . 1 1 3 3 GLY H H 1 8.56 . . . . . . . . . . . 4653 1 13 . 1 1 3 3 GLY HA2 H 1 3.89 . . . . . . . . . . . 4653 1 14 . 1 1 3 3 GLY HA3 H 1 3.89 . . . . . . . . . . . 4653 1 15 . 1 1 4 4 VAL H H 1 7.89 . . . . . . . . . . . 4653 1 16 . 1 1 4 4 VAL HA H 1 4.19 . . . . . . . . . . . 4653 1 17 . 1 1 4 4 VAL HB H 1 1.91 . . . . . . . . . . . 4653 1 18 . 1 1 4 4 VAL HG11 H 1 0.77 . . . . . . . . . . . 4653 1 19 . 1 1 4 4 VAL HG12 H 1 0.77 . . . . . . . . . . . 4653 1 20 . 1 1 4 4 VAL HG13 H 1 0.77 . . . . . . . . . . . 4653 1 21 . 1 1 4 4 VAL HG21 H 1 0.77 . . . . . . . . . . . 4653 1 22 . 1 1 4 4 VAL HG22 H 1 0.77 . . . . . . . . . . . 4653 1 23 . 1 1 4 4 VAL HG23 H 1 0.77 . . . . . . . . . . . 4653 1 24 . 1 1 5 5 ALA H H 1 8.03 . . . . . . . . . . . 4653 1 25 . 1 1 5 5 ALA HA H 1 4.24 . . . . . . . . . . . 4653 1 26 . 1 1 5 5 ALA HB1 H 1 1.13 . . . . . . . . . . . 4653 1 27 . 1 1 5 5 ALA HB2 H 1 1.13 . . . . . . . . . . . 4653 1 28 . 1 1 5 5 ALA HB3 H 1 1.13 . . . . . . . . . . . 4653 1 29 . 1 1 6 6 PHE H H 1 7.79 . . . . . . . . . . . 4653 1 30 . 1 1 6 6 PHE HA H 1 4.46 . . . . . . . . . . . 4653 1 31 . 1 1 6 6 PHE HB2 H 1 2.75 . . . . . . . . . . . 4653 1 32 . 1 1 6 6 PHE HB3 H 1 2.95 . . . . . . . . . . . 4653 1 33 . 1 1 6 6 PHE HD1 H 1 7.14 . . . . . . . . . . . 4653 1 34 . 1 1 6 6 PHE HD2 H 1 7.14 . . . . . . . . . . . 4653 1 35 . 1 1 7 7 TYR H H 1 7.99 . . . . . . . . . . . 4653 1 36 . 1 1 7 7 TYR HA H 1 4.49 . . . . . . . . . . . 4653 1 37 . 1 1 7 7 TYR HB2 H 1 2.64 . . . . . . . . . . . 4653 1 38 . 1 1 7 7 TYR HB3 H 1 2.81 . . . . . . . . . . . 4653 1 39 . 1 1 7 7 TYR HD1 H 1 6.99 . . . . . . . . . . . 4653 1 40 . 1 1 7 7 TYR HD2 H 1 6.99 . . . . . . . . . . . 4653 1 41 . 1 1 8 8 ILE H H 1 7.86 . . . . . . . . . . . 4653 1 42 . 1 1 8 8 ILE HA H 1 4.21 . . . . . . . . . . . 4653 1 43 . 1 1 8 8 ILE HB H 1 1.67 . . . . . . . . . . . 4653 1 44 . 1 1 8 8 ILE HG12 H 1 0.76 . . . . . . . . . . . 4653 1 45 . 1 1 8 8 ILE HG13 H 1 0.76 . . . . . . . . . . . 4653 1 46 . 1 1 8 8 ILE HG21 H 1 1.02 . . . . . . . . . . . 4653 1 47 . 1 1 8 8 ILE HG22 H 1 1.02 . . . . . . . . . . . 4653 1 48 . 1 1 8 8 ILE HG23 H 1 1.02 . . . . . . . . . . . 4653 1 49 . 1 1 8 8 ILE HD11 H 1 1.36 . . . . . . . . . . . 4653 1 50 . 1 1 8 8 ILE HD12 H 1 1.36 . . . . . . . . . . . 4653 1 51 . 1 1 8 8 ILE HD13 H 1 1.36 . . . . . . . . . . . 4653 1 52 . 1 1 9 9 PHE H H 1 8.09 . . . . . . . . . . . 4653 1 53 . 1 1 9 9 PHE HA H 1 4.63 . . . . . . . . . . . 4653 1 54 . 1 1 9 9 PHE HB2 H 1 2.8 . . . . . . . . . . . 4653 1 55 . 1 1 9 9 PHE HB3 H 1 3.02 . . . . . . . . . . . 4653 1 56 . 1 1 9 9 PHE HD1 H 1 7.25 . . . . . . . . . . . 4653 1 57 . 1 1 9 9 PHE HD2 H 1 7.25 . . . . . . . . . . . 4653 1 58 . 1 1 10 10 THR H H 1 7.924 . . . . . . . . . . . 4653 1 59 . 1 1 10 10 THR HA H 1 4.25 . . . . . . . . . . . 4653 1 60 . 1 1 10 10 THR HG21 H 1 1.02 . . . . . . . . . . . 4653 1 61 . 1 1 10 10 THR HG22 H 1 1.02 . . . . . . . . . . . 4653 1 62 . 1 1 10 10 THR HG23 H 1 1.02 . . . . . . . . . . . 4653 1 63 . 1 1 11 11 HIS H H 1 8.07 . . . . . . . . . . . 4653 1 64 . 1 1 11 11 HIS HA H 1 4.62 . . . . . . . . . . . 4653 1 65 . 1 1 11 11 HIS HB2 H 1 3.02 . . . . . . . . . . . 4653 1 66 . 1 1 11 11 HIS HB3 H 1 3.12 . . . . . . . . . . . 4653 1 67 . 1 1 11 11 HIS HD1 H 1 7.36 . . . . . . . . . . . 4653 1 68 . 1 1 12 12 GLN H H 1 8.18 . . . . . . . . . . . 4653 1 69 . 1 1 12 12 GLN HA H 1 4.25 . . . . . . . . . . . 4653 1 70 . 1 1 12 12 GLN HB2 H 1 1.79 . . . . . . . . . . . 4653 1 71 . 1 1 12 12 GLN HB3 H 1 1.91 . . . . . . . . . . . 4653 1 72 . 1 1 12 12 GLN HG2 H 1 2.13 . . . . . . . . . . . 4653 1 73 . 1 1 12 12 GLN HG3 H 1 2.13 . . . . . . . . . . . 4653 1 74 . 1 1 12 12 GLN HE21 H 1 6.77 . . . . . . . . . . . 4653 1 75 . 1 1 12 12 GLN HE22 H 1 6.77 . . . . . . . . . . . 4653 1 76 . 1 1 13 13 GLY HA2 H 1 3.76 . . . . . . . . . . . 4653 1 77 . 1 1 13 13 GLY HA3 H 1 3.87 . . . . . . . . . . . 4653 1 78 . 1 1 14 14 SER H H 1 7.98 . . . . . . . . . . . 4653 1 79 . 1 1 14 14 SER HA H 1 4.4 . . . . . . . . . . . 4653 1 80 . 1 1 14 14 SER HB2 H 1 3.57 . . . . . . . . . . . 4653 1 81 . 1 1 14 14 SER HB3 H 1 3.57 . . . . . . . . . . . 4653 1 82 . 1 1 15 15 ASP H H 1 8.34 . . . . . . . . . . . 4653 1 83 . 1 1 15 15 ASP HA H 1 4.54 . . . . . . . . . . . 4653 1 84 . 1 1 15 15 ASP HB2 H 1 2.39 . . . . . . . . . . . 4653 1 85 . 1 1 15 15 ASP HB3 H 1 2.62 . . . . . . . . . . . 4653 1 86 . 1 1 16 16 PHE H H 1 7.88 . . . . . . . . . . . 4653 1 87 . 1 1 16 16 PHE HA H 1 4.54 . . . . . . . . . . . 4653 1 88 . 1 1 16 16 PHE HB2 H 1 2.77 . . . . . . . . . . . 4653 1 89 . 1 1 16 16 PHE HB3 H 1 3.04 . . . . . . . . . . . 4653 1 90 . 1 1 16 16 PHE HD1 H 1 7.23 . . . . . . . . . . . 4653 1 91 . 1 1 16 16 PHE HD2 H 1 7.23 . . . . . . . . . . . 4653 1 92 . 1 1 17 17 GLY H H 1 8.13 . . . . . . . . . . . 4653 1 93 . 1 1 17 17 GLY HA2 H 1 3.74 . . . . . . . . . . . 4653 1 94 . 1 1 17 17 GLY HA3 H 1 3.81 . . . . . . . . . . . 4653 1 95 . 1 1 18 18 PRO HA H 1 4.32 . . . . . . . . . . . 4653 1 96 . 1 1 18 18 PRO HB2 H 1 1.78 . . . . . . . . . . . 4653 1 97 . 1 1 18 18 PRO HB3 H 1 1.94 . . . . . . . . . . . 4653 1 98 . 1 1 18 18 PRO HG2 H 1 3.50 . . . . . . . . . . . 4653 1 99 . 1 1 18 18 PRO HG3 H 1 3.50 . . . . . . . . . . . 4653 1 100 . 1 1 18 18 PRO HD2 H 1 3.44 . . . . . . . . . . . 4653 1 101 . 1 1 18 18 PRO HD3 H 1 3.44 . . . . . . . . . . . 4653 1 102 . 1 1 19 19 ILE H H 1 7.81 . . . . . . . . . . . 4653 1 103 . 1 1 19 19 ILE HA H 1 4.06 . . . . . . . . . . . 4653 1 104 . 1 1 19 19 ILE HB H 1 1.64 . . . . . . . . . . . 4653 1 105 . 1 1 19 19 ILE HG12 H 1 0.72 . . . . . . . . . . . 4653 1 106 . 1 1 19 19 ILE HG13 H 1 0.76 . . . . . . . . . . . 4653 1 107 . 1 1 19 19 ILE HG21 H 1 0.99 . . . . . . . . . . . 4653 1 108 . 1 1 19 19 ILE HG22 H 1 0.99 . . . . . . . . . . . 4653 1 109 . 1 1 19 19 ILE HG23 H 1 0.99 . . . . . . . . . . . 4653 1 110 . 1 1 19 19 ILE HD11 H 1 1.35 . . . . . . . . . . . 4653 1 111 . 1 1 19 19 ILE HD12 H 1 1.35 . . . . . . . . . . . 4653 1 112 . 1 1 19 19 ILE HD13 H 1 1.35 . . . . . . . . . . . 4653 1 113 . 1 1 20 20 PHE H H 1 7.9 . . . . . . . . . . . 4653 1 114 . 1 1 20 20 PHE HA H 1 4.5 . . . . . . . . . . . 4653 1 115 . 1 1 20 20 PHE HB2 H 1 2.8 . . . . . . . . . . . 4653 1 116 . 1 1 20 20 PHE HB3 H 1 3.00 . . . . . . . . . . . 4653 1 117 . 1 1 20 20 PHE HD1 H 1 7.06 . . . . . . . . . . . 4653 1 118 . 1 1 20 20 PHE HD2 H 1 7.06 . . . . . . . . . . . 4653 1 119 . 1 1 21 21 MET H H 1 8.1 . . . . . . . . . . . 4653 1 120 . 1 1 21 21 MET HA H 1 4.47 . . . . . . . . . . . 4653 1 121 . 1 1 21 21 MET HB2 H 1 1.79 . . . . . . . . . . . 4653 1 122 . 1 1 21 21 MET HB3 H 1 1.94 . . . . . . . . . . . 4653 1 123 . 1 1 21 21 MET HG2 H 1 2.44 . . . . . . . . . . . 4653 1 124 . 1 1 21 21 MET HG3 H 1 2.44 . . . . . . . . . . . 4653 1 125 . 1 1 22 22 THR H H 1 7.83 . . . . . . . . . . . 4653 1 126 . 1 1 22 22 THR HA H 1 4.25 . . . . . . . . . . . 4653 1 127 . 1 1 22 22 THR HB H 1 3.95 . . . . . . . . . . . 4653 1 128 . 1 1 22 22 THR HG21 H 1 1.02 . . . . . . . . . . . 4653 1 129 . 1 1 22 22 THR HG22 H 1 1.02 . . . . . . . . . . . 4653 1 130 . 1 1 22 22 THR HG23 H 1 1.02 . . . . . . . . . . . 4653 1 131 . 1 1 23 23 ILE H H 1 7.72 . . . . . . . . . . . 4653 1 132 . 1 1 23 23 ILE HA H 1 4.37 . . . . . . . . . . . 4653 1 133 . 1 1 23 23 ILE HB H 1 1.74 . . . . . . . . . . . 4653 1 134 . 1 1 23 23 ILE HG12 H 1 0.89 . . . . . . . . . . . 4653 1 135 . 1 1 23 23 ILE HG13 H 1 0.89 . . . . . . . . . . . 4653 1 136 . 1 1 23 23 ILE HG21 H 1 1.08 . . . . . . . . . . . 4653 1 137 . 1 1 23 23 ILE HG22 H 1 1.08 . . . . . . . . . . . 4653 1 138 . 1 1 23 23 ILE HG23 H 1 1.08 . . . . . . . . . . . 4653 1 139 . 1 1 23 23 ILE HD11 H 1 1.52 . . . . . . . . . . . 4653 1 140 . 1 1 23 23 ILE HD12 H 1 1.52 . . . . . . . . . . . 4653 1 141 . 1 1 23 23 ILE HD13 H 1 1.52 . . . . . . . . . . . 4653 1 142 . 1 1 24 24 PRO HA H 1 4.39 . . . . . . . . . . . 4653 1 143 . 1 1 24 24 PRO HB2 H 1 1.86 . . . . . . . . . . . 4653 1 144 . 1 1 24 24 PRO HB3 H 1 1.93 . . . . . . . . . . . 4653 1 145 . 1 1 24 24 PRO HG2 H 1 3.38 . . . . . . . . . . . 4653 1 146 . 1 1 24 24 PRO HG3 H 1 3.38 . . . . . . . . . . . 4653 1 147 . 1 1 24 24 PRO HD2 H 1 3.43 . . . . . . . . . . . 4653 1 148 . 1 1 24 24 PRO HD3 H 1 3.43 . . . . . . . . . . . 4653 1 149 . 1 1 25 25 ALA H H 1 8.67 . . . . . . . . . . . 4653 1 150 . 1 1 25 25 ALA HA H 1 4.39 . . . . . . . . . . . 4653 1 151 . 1 1 25 25 ALA HB1 H 1 1.27 . . . . . . . . . . . 4653 1 152 . 1 1 25 25 ALA HB2 H 1 1.27 . . . . . . . . . . . 4653 1 153 . 1 1 25 25 ALA HB3 H 1 1.27 . . . . . . . . . . . 4653 1 154 . 1 1 26 26 PHE H H 1 8.08 . . . . . . . . . . . 4653 1 155 . 1 1 26 26 PHE HA H 1 4.71 . . . . . . . . . . . 4653 1 156 . 1 1 26 26 PHE HB2 H 1 2.82 . . . . . . . . . . . 4653 1 157 . 1 1 26 26 PHE HB3 H 1 3.04 . . . . . . . . . . . 4653 1 158 . 1 1 26 26 PHE HD1 H 1 7.25 . . . . . . . . . . . 4653 1 159 . 1 1 26 26 PHE HD2 H 1 7.25 . . . . . . . . . . . 4653 1 stop_ save_