data_5376 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5376 _Entry.Title ; C-terminal peptide of alpha-subunit of transducin ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2002-05-15 _Entry.Accession_date 2002-05-15 _Entry.Last_release_date 2003-01-06 _Entry.Original_release_date 2003-01-06 _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 Bernd Koenig . W. . 5376 2 Georg Kontaxis . . . 5376 3 Drake Mitchell . C. . 5376 4 John Louis . M. . 5376 5 Burton Litman . J. . 5376 6 Ad Bax . . . 5376 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5376 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 81 5376 '13C chemical shifts' 36 5376 '15N chemical shifts' 10 5376 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 . . 2003-01-06 2002-05-15 original author . 5376 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5376 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22206956 _Citation.DOI . _Citation.PubMed_ID 12217702 _Citation.Full_citation . _Citation.Title ; Structure and Orientation of a G Protein Fragment in the Receptor Bound State from Residual Dipolar Couplings ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 322 _Citation.Journal_issue 2 _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 441 _Citation.Page_last 461 _Citation.Year 2002 _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 Bernd Koenig . W. . 5376 1 2 Georg Kontaxis . . . 5376 1 3 Drake Mitchell . C. . 5376 1 4 John Louis . M. . 5376 1 5 Burton Litman . J. . 5376 1 6 Ad Bax . . . 5376 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID NMR 5376 1 'membrane protein' 5376 1 rhodopsin 5376 1 transducin 5376 1 'transferred dipolar couplings' 5376 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_Gt_alpha340-350 _Assembly.Sf_category assembly _Assembly.Sf_framecode Gt_alpha340-350 _Assembly.Entry_ID 5376 _Assembly.ID 1 _Assembly.Name 'complex of transducin peptide and rhodopsin' _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 'peptide analog of C-terminal binding region of alpha subunit of transducin' _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5376 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 'S2 peptide' 1 $S2 . . . native . . . . . 5376 1 2 rhodopsin 2 $rhodopsin . . . native . . . . . 5376 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'complex of transducin peptide and rhodopsin' system 5376 1 Gt-alpha(340-350) abbreviation 5376 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'signal transduction in the visual system' 5376 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_S2 _Entity.Sf_category entity _Entity.Sf_framecode S2 _Entity.Entry_ID 5376 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Gt-alpha(340-350) _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 IRENLKDSGLF _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 11 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _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 2015-01-28 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 1F88 . "Crystal Structure Of Bovine Rhodopsin" . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 2 no PDB 1GZM . "Structure Of Bovine Rhodopsin In A Trigonal Crystal Form" . . . . . 100.00 349 100.00 100.00 0.00e+00 . . . . 5376 1 3 no PDB 1HZX . "Crystal Structure Of Bovine Rhodopsin" . . . . . 100.00 349 100.00 100.00 0.00e+00 . . . . 5376 1 4 no PDB 1JFP . "Structure Of Bovine Rhodopsin (Dark Adapted)" . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 5 no PDB 1L9H . "Crystal Structure Of Bovine Rhodopsin At 2.6 Angstroms Resolution" . . . . . 100.00 349 100.00 100.00 0.00e+00 . . . . 5376 1 6 no PDB 1LN6 . "Structure Of Bovine Rhodopsin (Metarhodopsin Ii)" . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 7 no PDB 1U19 . "Crystal Structure Of Bovine Rhodopsin At 2.2 Angstroms Resolution" . . . . . 100.00 349 100.00 100.00 0.00e+00 . . . . 5376 1 8 no PDB 2G87 . "Crystallographic Model Of Bathorhodopsin" . . . . . 100.00 349 100.00 100.00 0.00e+00 . . . . 5376 1 9 no PDB 2HPY . "Crystallographic Model Of Lumirhodopsin" . . . . . 100.00 349 100.00 100.00 0.00e+00 . . . . 5376 1 10 no PDB 2I35 . "Crystal Structure Of Rhombohedral Crystal Form Of Ground-State Rhodopsin" . . . . . 100.00 349 100.00 100.00 0.00e+00 . . . . 5376 1 11 no PDB 2I36 . "Crystal Structure Of Trigonal Crystal Form Of Ground-State Rhodopsin" . . . . . 100.00 349 100.00 100.00 0.00e+00 . . . . 5376 1 12 no PDB 2I37 . "Crystal Structure Of A Photoactivated Rhodopsin" . . . . . 100.00 349 100.00 100.00 0.00e+00 . . . . 5376 1 13 no PDB 2J4Y . "Crystal Structure Of A Rhodopsin Stabilizing Mutant Expressed In Mammalian Cells" . . . . . 100.00 349 99.43 99.43 0.00e+00 . . . . 5376 1 14 no PDB 2PED . "Crystallographic Model Of 9-Cis-Rhodopsin" . . . . . 100.00 349 100.00 100.00 0.00e+00 . . . . 5376 1 15 no PDB 2X72 . "Crystal Structure Of The Constitutively Active E113q,N2c, D282c Rhodopsin Mutant With Bound Galphact Peptide" . . . . . 100.00 349 99.14 99.43 0.00e+00 . . . . 5376 1 16 no PDB 3C9L . "Structure Of Ground-State Bovine Rhodospin In A Hexagonal Crystal Form" . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 17 no PDB 3C9M . "Structure Of A Mutant Bovine Rhodopsin In Hexagonal Crystal Form" . . . . . 100.00 348 99.43 99.43 0.00e+00 . . . . 5376 1 18 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 0.00e+00 . . . . 5376 1 19 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 0.00e+00 . . . . 5376 1 20 no PDB 3OAX . "Crystal Structure Of Bovine Rhodopsin With Beta-Ionone" . . . . . 100.00 349 100.00 100.00 0.00e+00 . . . . 5376 1 21 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 0.00e+00 . . . . 5376 1 22 no PDB 3PXO . "Crystal Structure Of Metarhodopsin Ii" . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 23 no PDB 4A4M . "Crystal Structure Of The Light-Activated Constitutively Active N2c,M257y,D282c Rhodopsin Mutant In Complex With A Peptide Resem" . . . . . 100.00 349 99.14 99.14 0.00e+00 . . . . 5376 1 24 no PDB 4BEY . "Night Blindness Causing G90d Rhodopsin In Complex With Gact2 Peptide" . . . . . 100.00 349 99.14 99.14 0.00e+00 . . . . 5376 1 25 no PDB 4BEZ . "Night Blindness Causing G90d Rhodopsin In The Active Conformation" . . . . . 100.00 349 99.14 99.14 0.00e+00 . . . . 5376 1 26 no PDB 4J4Q . "Crystal Structure Of Active Conformation Of Gpcr Opsin Stabilized By Octylglucoside" . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 27 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 0.00e+00 . . . . 5376 1 28 no DBJ BAB83621 . "rhodopsin [synthetic construct]" . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 29 no GB AAA30674 . "rhodopsin [Bos taurus]" . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 30 no GB AAA30675 . "rhodopsin, partial [Bos taurus]" . . . . . 98.56 343 99.71 99.71 0.00e+00 . . . . 5376 1 31 no GB ELR51227 . "Rhodopsin, partial [Bos mutus]" . . . . . 100.00 351 99.43 99.71 0.00e+00 . . . . 5376 1 32 no PRF 0811197A . rhodopsin . . . . . 100.00 347 99.71 99.71 0.00e+00 . . . . 5376 1 33 no PRF 0901188A . rhodopsin . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 34 no PRF 0901212A . rhodopsin . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 35 no PRF 1001148A . rhodopsin . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 36 no REF NP_001014890 . "rhodopsin [Bos taurus]" . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 37 no REF XP_004018583 . "PREDICTED: rhodopsin [Ovis aries]" . . . . . 100.00 348 97.41 98.56 0.00e+00 . . . . 5376 1 38 no REF XP_005902896 . "PREDICTED: rhodopsin [Bos mutus]" . . . . . 100.00 348 99.43 99.71 0.00e+00 . . . . 5376 1 39 no REF XP_006078962 . "PREDICTED: rhodopsin [Bubalus bubalis]" . . . . . 100.00 348 98.85 99.14 0.00e+00 . . . . 5376 1 40 no REF XP_010860750 . "PREDICTED: rhodopsin [Bison bison bison]" . . . . . 100.00 348 99.43 100.00 0.00e+00 . . . . 5376 1 41 no SP P02699 . "RecName: Full=Rhodopsin [Bos taurus]" . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 42 no TPG DAA16827 . "TPA: rhodopsin [Bos taurus]" . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID Gt-alpha(340-350) common 5376 1 Gt-alpha(340-350)K341R,C347S variant 5376 1 S2 abbreviation 5376 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 . ILE . 5376 1 2 . ARG . 5376 1 3 . GLU . 5376 1 4 . ASN . 5376 1 5 . LEU . 5376 1 6 . LYS . 5376 1 7 . ASP . 5376 1 8 . SER . 5376 1 9 . GLY . 5376 1 10 . LEU . 5376 1 11 . PHE . 5376 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 . ILE 1 1 5376 1 . ARG 2 2 5376 1 . GLU 3 3 5376 1 . ASN 4 4 5376 1 . LEU 5 5 5376 1 . LYS 6 6 5376 1 . ASP 7 7 5376 1 . SER 8 8 5376 1 . GLY 9 9 5376 1 . LEU 10 10 5376 1 . PHE 11 11 5376 1 stop_ save_ save_rhodopsin _Entity.Sf_category entity _Entity.Sf_framecode rhodopsin _Entity.Entry_ID 5376 _Entity.ID 2 _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 ; MNGTEGPNFYVPFSNKTGVV RSPFEAPQYYLAEPWQFSML AAYMFLLIMLGFPINFLTLY VTVQHKKLRTPLNYILLNLA VADLFMVFGGFTTTLYTSLH GYFVFGPTGCNLEGFFATLG GEIALWSLVVLAIERYVVVC KPMSNFRFGENHAIMGVAFT WVMALACAAPPLVGWSRYIP EGMQCSCGIDYYTPHEETNN ESFVIYMFVVHFIIPLIVIF FCYGQLVFTVKEAAAQQQES ATTQKAEKEVTRMVIIMVIA FLICWLPYAGVAFYIFTHQG SDFGPIFMTIPAFFAKTSAV YNPVIYIMMNKQFRNCMVTT LCCGKNPLGDDEASTTVSKT ETSQVAPA ; _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 348 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not reported' _Entity.Src_method . _Entity.Parent_entity_ID . _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 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 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 . . REF NP_001014890 . 'rhodopsin [Bos taurus]' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . SWISS-PROT P02699 . Rhodopsin . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PRF 0901212A . rhodopsin . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PRF 1001148A . rhodopsin . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PRF 0811197A . rhodopsin . . . . . 100.00 347 99.71 99.71 0.00e+00 . . . . 5376 2 . . PRF 0901188A . rhodopsin . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . GenBank AAA30674 . rhodopsin . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . GenBank AAA30675 . rhodopsin . . . . . 98.56 343 99.71 99.71 0.00e+00 . . . . 5376 2 . . 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 0.00e+00 . . . . 5376 2 . . DBJ BAB83621 . 'rhodopsin [synthetic construct]' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 3C9L . 'Structure Of Ground-State Bovine Rhodospin In A Hexagonal Crystal Form' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 3C9M . 'Structure Of A Mutant Bovine Rhodopsin In Hexagonal Crystal Form' . . . . . 100.00 348 99.43 99.43 0.00e+00 . . . . 5376 2 . . PDB 2J4Y . 'Crystal Structure Of A Rhodopsin Stabilizing Mutant Expressed In Mammalian Cells' . . . . . 99.43 348 99.42 99.42 0.00e+00 . . . . 5376 2 . . PDB 2PED . 'Crystallographic Model Of 9-Cis-Rhodopsin' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 2I36 . 'Crystal Structure Of Trigonal Crystal Form Of Ground-State Rhodopsin' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 2I37 . 'Crystal Structure Of A Photoactivated Rhodopsin' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 2HPY . 'Crystallographic Model Of Lumirhodopsin' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 2I35 . 'Crystal Structure Of Rhombohedral Crystal Form Of Ground- State Rhodopsin' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 1U19 . 'Crystal Structure Of Bovine Rhodopsin At 2.2 Angstroms Resolution' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 2G87 . 'Crystallographic Model Of Bathorhodopsin' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 1L9H . 'Crystal Structure Of Bovine Rhodopsin At 2.6 Angstroms Resolution' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 1LN6 . 'Structure Of Bovine Rhodopsin (Metarhodopsin Ii)' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 1HZX . 'Crystal Structure Of Bovine Rhodopsin' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 1JFP . 'Structure Of Bovine Rhodopsin (Dark Adapted)' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 1F88 . 'Crystal Structure Of Bovine Rhodopsin' . . . . . 99.71 348 100.00 100.00 0.00e+00 . . . . 5376 2 . . PDB 1GZM . 'Structure Of Bovine Rhodopsin In A Trigonal Crystal Form' . . . . . 100.00 348 100.00 100.00 0.00e+00 . . . . 5376 2 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID rhodopsin common 5376 2 rhodopsin variant 5376 2 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 . MET . 5376 2 2 . ASN . 5376 2 3 . GLY . 5376 2 4 . THR . 5376 2 5 . GLU . 5376 2 6 . GLY . 5376 2 7 . PRO . 5376 2 8 . ASN . 5376 2 9 . PHE . 5376 2 10 . TYR . 5376 2 11 . VAL . 5376 2 12 . PRO . 5376 2 13 . PHE . 5376 2 14 . SER . 5376 2 15 . ASN . 5376 2 16 . LYS . 5376 2 17 . THR . 5376 2 18 . GLY . 5376 2 19 . VAL . 5376 2 20 . VAL . 5376 2 21 . ARG . 5376 2 22 . SER . 5376 2 23 . PRO . 5376 2 24 . PHE . 5376 2 25 . GLU . 5376 2 26 . ALA . 5376 2 27 . PRO . 5376 2 28 . GLN . 5376 2 29 . TYR . 5376 2 30 . TYR . 5376 2 31 . LEU . 5376 2 32 . ALA . 5376 2 33 . GLU . 5376 2 34 . PRO . 5376 2 35 . TRP . 5376 2 36 . GLN . 5376 2 37 . PHE . 5376 2 38 . SER . 5376 2 39 . MET . 5376 2 40 . LEU . 5376 2 41 . ALA . 5376 2 42 . ALA . 5376 2 43 . TYR . 5376 2 44 . MET . 5376 2 45 . PHE . 5376 2 46 . LEU . 5376 2 47 . LEU . 5376 2 48 . ILE . 5376 2 49 . MET . 5376 2 50 . LEU . 5376 2 51 . GLY . 5376 2 52 . PHE . 5376 2 53 . PRO . 5376 2 54 . ILE . 5376 2 55 . ASN . 5376 2 56 . PHE . 5376 2 57 . LEU . 5376 2 58 . THR . 5376 2 59 . LEU . 5376 2 60 . TYR . 5376 2 61 . VAL . 5376 2 62 . THR . 5376 2 63 . VAL . 5376 2 64 . GLN . 5376 2 65 . HIS . 5376 2 66 . LYS . 5376 2 67 . LYS . 5376 2 68 . LEU . 5376 2 69 . ARG . 5376 2 70 . THR . 5376 2 71 . PRO . 5376 2 72 . LEU . 5376 2 73 . ASN . 5376 2 74 . TYR . 5376 2 75 . ILE . 5376 2 76 . LEU . 5376 2 77 . LEU . 5376 2 78 . ASN . 5376 2 79 . LEU . 5376 2 80 . ALA . 5376 2 81 . VAL . 5376 2 82 . ALA . 5376 2 83 . ASP . 5376 2 84 . LEU . 5376 2 85 . PHE . 5376 2 86 . MET . 5376 2 87 . VAL . 5376 2 88 . PHE . 5376 2 89 . GLY . 5376 2 90 . GLY . 5376 2 91 . PHE . 5376 2 92 . THR . 5376 2 93 . THR . 5376 2 94 . THR . 5376 2 95 . LEU . 5376 2 96 . TYR . 5376 2 97 . THR . 5376 2 98 . SER . 5376 2 99 . LEU . 5376 2 100 . HIS . 5376 2 101 . GLY . 5376 2 102 . TYR . 5376 2 103 . PHE . 5376 2 104 . VAL . 5376 2 105 . PHE . 5376 2 106 . GLY . 5376 2 107 . PRO . 5376 2 108 . THR . 5376 2 109 . GLY . 5376 2 110 . CYS . 5376 2 111 . ASN . 5376 2 112 . LEU . 5376 2 113 . GLU . 5376 2 114 . GLY . 5376 2 115 . PHE . 5376 2 116 . PHE . 5376 2 117 . ALA . 5376 2 118 . THR . 5376 2 119 . LEU . 5376 2 120 . GLY . 5376 2 121 . GLY . 5376 2 122 . GLU . 5376 2 123 . ILE . 5376 2 124 . ALA . 5376 2 125 . LEU . 5376 2 126 . TRP . 5376 2 127 . SER . 5376 2 128 . LEU . 5376 2 129 . VAL . 5376 2 130 . VAL . 5376 2 131 . LEU . 5376 2 132 . ALA . 5376 2 133 . ILE . 5376 2 134 . GLU . 5376 2 135 . ARG . 5376 2 136 . TYR . 5376 2 137 . VAL . 5376 2 138 . VAL . 5376 2 139 . VAL . 5376 2 140 . CYS . 5376 2 141 . LYS . 5376 2 142 . PRO . 5376 2 143 . MET . 5376 2 144 . SER . 5376 2 145 . ASN . 5376 2 146 . PHE . 5376 2 147 . ARG . 5376 2 148 . PHE . 5376 2 149 . GLY . 5376 2 150 . GLU . 5376 2 151 . ASN . 5376 2 152 . HIS . 5376 2 153 . ALA . 5376 2 154 . ILE . 5376 2 155 . MET . 5376 2 156 . GLY . 5376 2 157 . VAL . 5376 2 158 . ALA . 5376 2 159 . PHE . 5376 2 160 . THR . 5376 2 161 . TRP . 5376 2 162 . VAL . 5376 2 163 . MET . 5376 2 164 . ALA . 5376 2 165 . LEU . 5376 2 166 . ALA . 5376 2 167 . CYS . 5376 2 168 . ALA . 5376 2 169 . ALA . 5376 2 170 . PRO . 5376 2 171 . PRO . 5376 2 172 . LEU . 5376 2 173 . VAL . 5376 2 174 . GLY . 5376 2 175 . TRP . 5376 2 176 . SER . 5376 2 177 . ARG . 5376 2 178 . TYR . 5376 2 179 . ILE . 5376 2 180 . PRO . 5376 2 181 . GLU . 5376 2 182 . GLY . 5376 2 183 . MET . 5376 2 184 . GLN . 5376 2 185 . CYS . 5376 2 186 . SER . 5376 2 187 . CYS . 5376 2 188 . GLY . 5376 2 189 . ILE . 5376 2 190 . ASP . 5376 2 191 . TYR . 5376 2 192 . TYR . 5376 2 193 . THR . 5376 2 194 . PRO . 5376 2 195 . HIS . 5376 2 196 . GLU . 5376 2 197 . GLU . 5376 2 198 . THR . 5376 2 199 . ASN . 5376 2 200 . ASN . 5376 2 201 . GLU . 5376 2 202 . SER . 5376 2 203 . PHE . 5376 2 204 . VAL . 5376 2 205 . ILE . 5376 2 206 . TYR . 5376 2 207 . MET . 5376 2 208 . PHE . 5376 2 209 . VAL . 5376 2 210 . VAL . 5376 2 211 . HIS . 5376 2 212 . PHE . 5376 2 213 . ILE . 5376 2 214 . ILE . 5376 2 215 . PRO . 5376 2 216 . LEU . 5376 2 217 . ILE . 5376 2 218 . VAL . 5376 2 219 . ILE . 5376 2 220 . PHE . 5376 2 221 . PHE . 5376 2 222 . CYS . 5376 2 223 . TYR . 5376 2 224 . GLY . 5376 2 225 . GLN . 5376 2 226 . LEU . 5376 2 227 . VAL . 5376 2 228 . PHE . 5376 2 229 . THR . 5376 2 230 . VAL . 5376 2 231 . LYS . 5376 2 232 . GLU . 5376 2 233 . ALA . 5376 2 234 . ALA . 5376 2 235 . ALA . 5376 2 236 . GLN . 5376 2 237 . GLN . 5376 2 238 . GLN . 5376 2 239 . GLU . 5376 2 240 . SER . 5376 2 241 . ALA . 5376 2 242 . THR . 5376 2 243 . THR . 5376 2 244 . GLN . 5376 2 245 . LYS . 5376 2 246 . ALA . 5376 2 247 . GLU . 5376 2 248 . LYS . 5376 2 249 . GLU . 5376 2 250 . VAL . 5376 2 251 . THR . 5376 2 252 . ARG . 5376 2 253 . MET . 5376 2 254 . VAL . 5376 2 255 . ILE . 5376 2 256 . ILE . 5376 2 257 . MET . 5376 2 258 . VAL . 5376 2 259 . ILE . 5376 2 260 . ALA . 5376 2 261 . PHE . 5376 2 262 . LEU . 5376 2 263 . ILE . 5376 2 264 . CYS . 5376 2 265 . TRP . 5376 2 266 . LEU . 5376 2 267 . PRO . 5376 2 268 . TYR . 5376 2 269 . ALA . 5376 2 270 . GLY . 5376 2 271 . VAL . 5376 2 272 . ALA . 5376 2 273 . PHE . 5376 2 274 . TYR . 5376 2 275 . ILE . 5376 2 276 . PHE . 5376 2 277 . THR . 5376 2 278 . HIS . 5376 2 279 . GLN . 5376 2 280 . GLY . 5376 2 281 . SER . 5376 2 282 . ASP . 5376 2 283 . PHE . 5376 2 284 . GLY . 5376 2 285 . PRO . 5376 2 286 . ILE . 5376 2 287 . PHE . 5376 2 288 . MET . 5376 2 289 . THR . 5376 2 290 . ILE . 5376 2 291 . PRO . 5376 2 292 . ALA . 5376 2 293 . PHE . 5376 2 294 . PHE . 5376 2 295 . ALA . 5376 2 296 . LYS . 5376 2 297 . THR . 5376 2 298 . SER . 5376 2 299 . ALA . 5376 2 300 . VAL . 5376 2 301 . TYR . 5376 2 302 . ASN . 5376 2 303 . PRO . 5376 2 304 . VAL . 5376 2 305 . ILE . 5376 2 306 . TYR . 5376 2 307 . ILE . 5376 2 308 . MET . 5376 2 309 . MET . 5376 2 310 . ASN . 5376 2 311 . LYS . 5376 2 312 . GLN . 5376 2 313 . PHE . 5376 2 314 . ARG . 5376 2 315 . ASN . 5376 2 316 . CYS . 5376 2 317 . MET . 5376 2 318 . VAL . 5376 2 319 . THR . 5376 2 320 . THR . 5376 2 321 . LEU . 5376 2 322 . CYS . 5376 2 323 . CYS . 5376 2 324 . GLY . 5376 2 325 . LYS . 5376 2 326 . ASN . 5376 2 327 . PRO . 5376 2 328 . LEU . 5376 2 329 . GLY . 5376 2 330 . ASP . 5376 2 331 . ASP . 5376 2 332 . GLU . 5376 2 333 . ALA . 5376 2 334 . SER . 5376 2 335 . THR . 5376 2 336 . THR . 5376 2 337 . VAL . 5376 2 338 . SER . 5376 2 339 . LYS . 5376 2 340 . THR . 5376 2 341 . GLU . 5376 2 342 . THR . 5376 2 343 . SER . 5376 2 344 . GLN . 5376 2 345 . VAL . 5376 2 346 . ALA . 5376 2 347 . PRO . 5376 2 348 . ALA . 5376 2 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 . MET 1 1 5376 2 . ASN 2 2 5376 2 . GLY 3 3 5376 2 . THR 4 4 5376 2 . GLU 5 5 5376 2 . GLY 6 6 5376 2 . PRO 7 7 5376 2 . ASN 8 8 5376 2 . PHE 9 9 5376 2 . TYR 10 10 5376 2 . VAL 11 11 5376 2 . PRO 12 12 5376 2 . PHE 13 13 5376 2 . SER 14 14 5376 2 . ASN 15 15 5376 2 . LYS 16 16 5376 2 . THR 17 17 5376 2 . GLY 18 18 5376 2 . VAL 19 19 5376 2 . VAL 20 20 5376 2 . ARG 21 21 5376 2 . SER 22 22 5376 2 . PRO 23 23 5376 2 . PHE 24 24 5376 2 . GLU 25 25 5376 2 . ALA 26 26 5376 2 . PRO 27 27 5376 2 . GLN 28 28 5376 2 . TYR 29 29 5376 2 . TYR 30 30 5376 2 . LEU 31 31 5376 2 . ALA 32 32 5376 2 . GLU 33 33 5376 2 . PRO 34 34 5376 2 . TRP 35 35 5376 2 . GLN 36 36 5376 2 . PHE 37 37 5376 2 . SER 38 38 5376 2 . MET 39 39 5376 2 . LEU 40 40 5376 2 . ALA 41 41 5376 2 . ALA 42 42 5376 2 . TYR 43 43 5376 2 . MET 44 44 5376 2 . PHE 45 45 5376 2 . LEU 46 46 5376 2 . LEU 47 47 5376 2 . ILE 48 48 5376 2 . MET 49 49 5376 2 . LEU 50 50 5376 2 . GLY 51 51 5376 2 . PHE 52 52 5376 2 . PRO 53 53 5376 2 . ILE 54 54 5376 2 . ASN 55 55 5376 2 . PHE 56 56 5376 2 . LEU 57 57 5376 2 . THR 58 58 5376 2 . LEU 59 59 5376 2 . TYR 60 60 5376 2 . VAL 61 61 5376 2 . THR 62 62 5376 2 . VAL 63 63 5376 2 . GLN 64 64 5376 2 . HIS 65 65 5376 2 . LYS 66 66 5376 2 . LYS 67 67 5376 2 . LEU 68 68 5376 2 . ARG 69 69 5376 2 . THR 70 70 5376 2 . PRO 71 71 5376 2 . LEU 72 72 5376 2 . ASN 73 73 5376 2 . TYR 74 74 5376 2 . ILE 75 75 5376 2 . LEU 76 76 5376 2 . LEU 77 77 5376 2 . ASN 78 78 5376 2 . LEU 79 79 5376 2 . ALA 80 80 5376 2 . VAL 81 81 5376 2 . ALA 82 82 5376 2 . ASP 83 83 5376 2 . LEU 84 84 5376 2 . PHE 85 85 5376 2 . MET 86 86 5376 2 . VAL 87 87 5376 2 . PHE 88 88 5376 2 . GLY 89 89 5376 2 . GLY 90 90 5376 2 . PHE 91 91 5376 2 . THR 92 92 5376 2 . THR 93 93 5376 2 . THR 94 94 5376 2 . LEU 95 95 5376 2 . TYR 96 96 5376 2 . THR 97 97 5376 2 . SER 98 98 5376 2 . LEU 99 99 5376 2 . HIS 100 100 5376 2 . GLY 101 101 5376 2 . TYR 102 102 5376 2 . PHE 103 103 5376 2 . VAL 104 104 5376 2 . PHE 105 105 5376 2 . GLY 106 106 5376 2 . PRO 107 107 5376 2 . THR 108 108 5376 2 . GLY 109 109 5376 2 . CYS 110 110 5376 2 . ASN 111 111 5376 2 . LEU 112 112 5376 2 . GLU 113 113 5376 2 . GLY 114 114 5376 2 . PHE 115 115 5376 2 . PHE 116 116 5376 2 . ALA 117 117 5376 2 . THR 118 118 5376 2 . LEU 119 119 5376 2 . GLY 120 120 5376 2 . GLY 121 121 5376 2 . GLU 122 122 5376 2 . ILE 123 123 5376 2 . ALA 124 124 5376 2 . LEU 125 125 5376 2 . TRP 126 126 5376 2 . SER 127 127 5376 2 . LEU 128 128 5376 2 . VAL 129 129 5376 2 . VAL 130 130 5376 2 . LEU 131 131 5376 2 . ALA 132 132 5376 2 . ILE 133 133 5376 2 . GLU 134 134 5376 2 . ARG 135 135 5376 2 . TYR 136 136 5376 2 . VAL 137 137 5376 2 . VAL 138 138 5376 2 . VAL 139 139 5376 2 . CYS 140 140 5376 2 . LYS 141 141 5376 2 . PRO 142 142 5376 2 . MET 143 143 5376 2 . SER 144 144 5376 2 . ASN 145 145 5376 2 . PHE 146 146 5376 2 . ARG 147 147 5376 2 . PHE 148 148 5376 2 . GLY 149 149 5376 2 . GLU 150 150 5376 2 . ASN 151 151 5376 2 . HIS 152 152 5376 2 . ALA 153 153 5376 2 . ILE 154 154 5376 2 . MET 155 155 5376 2 . GLY 156 156 5376 2 . VAL 157 157 5376 2 . ALA 158 158 5376 2 . PHE 159 159 5376 2 . THR 160 160 5376 2 . TRP 161 161 5376 2 . VAL 162 162 5376 2 . MET 163 163 5376 2 . ALA 164 164 5376 2 . LEU 165 165 5376 2 . ALA 166 166 5376 2 . CYS 167 167 5376 2 . ALA 168 168 5376 2 . ALA 169 169 5376 2 . PRO 170 170 5376 2 . PRO 171 171 5376 2 . LEU 172 172 5376 2 . VAL 173 173 5376 2 . GLY 174 174 5376 2 . TRP 175 175 5376 2 . SER 176 176 5376 2 . ARG 177 177 5376 2 . TYR 178 178 5376 2 . ILE 179 179 5376 2 . PRO 180 180 5376 2 . GLU 181 181 5376 2 . GLY 182 182 5376 2 . MET 183 183 5376 2 . GLN 184 184 5376 2 . CYS 185 185 5376 2 . SER 186 186 5376 2 . CYS 187 187 5376 2 . GLY 188 188 5376 2 . ILE 189 189 5376 2 . ASP 190 190 5376 2 . TYR 191 191 5376 2 . TYR 192 192 5376 2 . THR 193 193 5376 2 . PRO 194 194 5376 2 . HIS 195 195 5376 2 . GLU 196 196 5376 2 . GLU 197 197 5376 2 . THR 198 198 5376 2 . ASN 199 199 5376 2 . ASN 200 200 5376 2 . GLU 201 201 5376 2 . SER 202 202 5376 2 . PHE 203 203 5376 2 . VAL 204 204 5376 2 . ILE 205 205 5376 2 . TYR 206 206 5376 2 . MET 207 207 5376 2 . PHE 208 208 5376 2 . VAL 209 209 5376 2 . VAL 210 210 5376 2 . HIS 211 211 5376 2 . PHE 212 212 5376 2 . ILE 213 213 5376 2 . ILE 214 214 5376 2 . PRO 215 215 5376 2 . LEU 216 216 5376 2 . ILE 217 217 5376 2 . VAL 218 218 5376 2 . ILE 219 219 5376 2 . PHE 220 220 5376 2 . PHE 221 221 5376 2 . CYS 222 222 5376 2 . TYR 223 223 5376 2 . GLY 224 224 5376 2 . GLN 225 225 5376 2 . LEU 226 226 5376 2 . VAL 227 227 5376 2 . PHE 228 228 5376 2 . THR 229 229 5376 2 . VAL 230 230 5376 2 . LYS 231 231 5376 2 . GLU 232 232 5376 2 . ALA 233 233 5376 2 . ALA 234 234 5376 2 . ALA 235 235 5376 2 . GLN 236 236 5376 2 . GLN 237 237 5376 2 . GLN 238 238 5376 2 . GLU 239 239 5376 2 . SER 240 240 5376 2 . ALA 241 241 5376 2 . THR 242 242 5376 2 . THR 243 243 5376 2 . GLN 244 244 5376 2 . LYS 245 245 5376 2 . ALA 246 246 5376 2 . GLU 247 247 5376 2 . LYS 248 248 5376 2 . GLU 249 249 5376 2 . VAL 250 250 5376 2 . THR 251 251 5376 2 . ARG 252 252 5376 2 . MET 253 253 5376 2 . VAL 254 254 5376 2 . ILE 255 255 5376 2 . ILE 256 256 5376 2 . MET 257 257 5376 2 . VAL 258 258 5376 2 . ILE 259 259 5376 2 . ALA 260 260 5376 2 . PHE 261 261 5376 2 . LEU 262 262 5376 2 . ILE 263 263 5376 2 . CYS 264 264 5376 2 . TRP 265 265 5376 2 . LEU 266 266 5376 2 . PRO 267 267 5376 2 . TYR 268 268 5376 2 . ALA 269 269 5376 2 . GLY 270 270 5376 2 . VAL 271 271 5376 2 . ALA 272 272 5376 2 . PHE 273 273 5376 2 . TYR 274 274 5376 2 . ILE 275 275 5376 2 . PHE 276 276 5376 2 . THR 277 277 5376 2 . HIS 278 278 5376 2 . GLN 279 279 5376 2 . GLY 280 280 5376 2 . SER 281 281 5376 2 . ASP 282 282 5376 2 . PHE 283 283 5376 2 . GLY 284 284 5376 2 . PRO 285 285 5376 2 . ILE 286 286 5376 2 . PHE 287 287 5376 2 . MET 288 288 5376 2 . THR 289 289 5376 2 . ILE 290 290 5376 2 . PRO 291 291 5376 2 . ALA 292 292 5376 2 . PHE 293 293 5376 2 . PHE 294 294 5376 2 . ALA 295 295 5376 2 . LYS 296 296 5376 2 . THR 297 297 5376 2 . SER 298 298 5376 2 . ALA 299 299 5376 2 . VAL 300 300 5376 2 . TYR 301 301 5376 2 . ASN 302 302 5376 2 . PRO 303 303 5376 2 . VAL 304 304 5376 2 . ILE 305 305 5376 2 . TYR 306 306 5376 2 . ILE 307 307 5376 2 . MET 308 308 5376 2 . MET 309 309 5376 2 . ASN 310 310 5376 2 . LYS 311 311 5376 2 . GLN 312 312 5376 2 . PHE 313 313 5376 2 . ARG 314 314 5376 2 . ASN 315 315 5376 2 . CYS 316 316 5376 2 . MET 317 317 5376 2 . VAL 318 318 5376 2 . THR 319 319 5376 2 . THR 320 320 5376 2 . LEU 321 321 5376 2 . CYS 322 322 5376 2 . CYS 323 323 5376 2 . GLY 324 324 5376 2 . LYS 325 325 5376 2 . ASN 326 326 5376 2 . PRO 327 327 5376 2 . LEU 328 328 5376 2 . GLY 329 329 5376 2 . ASP 330 330 5376 2 . ASP 331 331 5376 2 . GLU 332 332 5376 2 . ALA 333 333 5376 2 . SER 334 334 5376 2 . THR 335 335 5376 2 . THR 336 336 5376 2 . VAL 337 337 5376 2 . SER 338 338 5376 2 . LYS 339 339 5376 2 . THR 340 340 5376 2 . GLU 341 341 5376 2 . THR 342 342 5376 2 . SER 343 343 5376 2 . GLN 344 344 5376 2 . VAL 345 345 5376 2 . ALA 346 346 5376 2 . PRO 347 347 5376 2 . ALA 348 348 5376 2 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 5376 _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 $S2 . 9913 . . 'Bos taurus' cow . . Eukaryota Metazoa Bos taurus . . . eye retina . . . . . . . . . . . . . . . . 5376 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 5376 _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 $S2 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli . . . . . . . . . . . . . plasmid . . GEV-S2 . . . . . . 5376 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5376 _Sample.ID 1 _Sample.Type emulsion _Sample.Sub_type . _Sample.Details ; sample contains individual, intact rhodopsin rich disk membranes isolated from the rod outer segment of bovine retina; S2 peptide is in fast exchange between a free form in solution and a rhodopsin bound form ; _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 Gt-alpha(340-350) '[U-15N; U-13C]' . . 1 $S2 . . 2.6 . . mM . . . . 5376 1 2 rhodopsin . . . 2 $rhodopsin . . 0.063 . . mM . . . . 5376 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5376 _Sample.ID 2 _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 Gt-alpha(340-350) . . . 1 $S2 . . 2.6 . . mM . . . . 5376 2 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 5376 _Sample_condition_list.ID 1 _Sample_condition_list.Details ; sample was studied in dark adapted state and after photo activation of rhodopsin by illuminating the sample for 60s with a focussed microscope light, chemical shifts of S2 are identical in both states, TrNOEs and TrDCs are difference values between the dark and light-activated states ; 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 pH 6.6 0.2 na 5376 1 temperature 283 0.5 K 5376 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 5376 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details 'Delaglio, F. et al. (1995) J. Biomol. NMR 6(3), 277-293' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'raw spectral data processing' 5376 1 'peak picking' 5376 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5376 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer2 _NMR_spectrometer.Entry_ID 5376 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5376 _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 NMR_spectrometer Bruker DMX . 600 . . . 5376 1 2 NMR_spectrometer2 Bruker DMX . 750 . . . 5376 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 5376 _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 1H-1H NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5376 1 2 '2D 1H-1H TOCSY (15N separated)' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5376 1 3 '2D 1H-15N HSQC (w/o 1H decoupling)' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5376 1 4 '2D 1H-13C CT-HSQC (w/o 1H decoupling)' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5376 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 5376 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '2D 1H-1H NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5376 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '2D 1H-1H TOCSY (15N separated)' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5376 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '2D 1H-15N HSQC (w/o 1H decoupling)' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5376 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '2D 1H-13C CT-HSQC (w/o 1H decoupling)' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5376 _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 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . . . . . 5376 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5376 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5376 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_S2_shift_set _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode S2_shift_set _Assigned_chem_shift_list.Entry_ID 5376 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _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 '2D 1H-1H NOESY' . . . 5376 1 2 '2D 1H-1H TOCSY (15N separated)' . . . 5376 1 3 '2D 1H-15N HSQC (w/o 1H decoupling)' . . . 5376 1 4 '2D 1H-13C CT-HSQC (w/o 1H decoupling)' . . . 5376 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 ILE HA H 1 3.86 . . 1 . . . . . . . . 5376 1 2 . 1 1 1 1 ILE HB H 1 1.95 . . 1 . . . . . . . . 5376 1 3 . 1 1 1 1 ILE HG12 H 1 1.47 . . 2 . . . . . . . . 5376 1 4 . 1 1 1 1 ILE HG13 H 1 1.21 . . 2 . . . . . . . . 5376 1 5 . 1 1 1 1 ILE HG21 H 1 0.99 . . 1 . . . . . . . . 5376 1 6 . 1 1 1 1 ILE HG22 H 1 0.99 . . 1 . . . . . . . . 5376 1 7 . 1 1 1 1 ILE HG23 H 1 0.99 . . 1 . . . . . . . . 5376 1 8 . 1 1 1 1 ILE HD11 H 1 0.92 . . 1 . . . . . . . . 5376 1 9 . 1 1 1 1 ILE HD12 H 1 0.92 . . 1 . . . . . . . . 5376 1 10 . 1 1 1 1 ILE HD13 H 1 0.92 . . 1 . . . . . . . . 5376 1 11 . 1 1 1 1 ILE CA C 13 60.5 . . 1 . . . . . . . . 5376 1 12 . 1 1 1 1 ILE CB C 13 39.3 . . 1 . . . . . . . . 5376 1 13 . 1 1 1 1 ILE CG1 C 13 26.7 . . 1 . . . . . . . . 5376 1 14 . 1 1 1 1 ILE CG2 C 13 16.9 . . 1 . . . . . . . . 5376 1 15 . 1 1 1 1 ILE CD1 C 13 13.3 . . 1 . . . . . . . . 5376 1 16 . 1 1 2 2 ARG HA H 1 4.32 . . 1 . . . . . . . . 5376 1 17 . 1 1 2 2 ARG HB2 H 1 1.86 . . 2 . . . . . . . . 5376 1 18 . 1 1 2 2 ARG HB3 H 1 1.79 . . 2 . . . . . . . . 5376 1 19 . 1 1 2 2 ARG HG2 H 1 1.63 . . 1 . . . . . . . . 5376 1 20 . 1 1 2 2 ARG HG3 H 1 1.63 . . 1 . . . . . . . . 5376 1 21 . 1 1 2 2 ARG HD2 H 1 3.20 . . 1 . . . . . . . . 5376 1 22 . 1 1 2 2 ARG HD3 H 1 3.20 . . 1 . . . . . . . . 5376 1 23 . 1 1 2 2 ARG CA C 13 56.4 . . 1 . . . . . . . . 5376 1 24 . 1 1 2 2 ARG CB C 13 30.4 . . 1 . . . . . . . . 5376 1 25 . 1 1 2 2 ARG CG C 13 27.2 . . 1 . . . . . . . . 5376 1 26 . 1 1 2 2 ARG CD C 13 43.3 . . 1 . . . . . . . . 5376 1 27 . 1 1 3 3 GLU H H 1 8.76 . . 1 . . . . . . . . 5376 1 28 . 1 1 3 3 GLU HA H 1 4.23 . . 1 . . . . . . . . 5376 1 29 . 1 1 3 3 GLU HB2 H 1 2.00 . . 2 . . . . . . . . 5376 1 30 . 1 1 3 3 GLU HB3 H 1 1.92 . . 2 . . . . . . . . 5376 1 31 . 1 1 3 3 GLU HG2 H 1 2.26 . . 1 . . . . . . . . 5376 1 32 . 1 1 3 3 GLU HG3 H 1 2.26 . . 1 . . . . . . . . 5376 1 33 . 1 1 3 3 GLU CA C 13 56.9 . . 1 . . . . . . . . 5376 1 34 . 1 1 3 3 GLU CB C 13 30.4 . . 1 . . . . . . . . 5376 1 35 . 1 1 3 3 GLU CG C 13 36.3 . . 1 . . . . . . . . 5376 1 36 . 1 1 3 3 GLU N N 15 123.4 . . 1 . . . . . . . . 5376 1 37 . 1 1 4 4 ASN H H 1 8.65 . . 1 . . . . . . . . 5376 1 38 . 1 1 4 4 ASN HA H 1 4.67 . . 1 . . . . . . . . 5376 1 39 . 1 1 4 4 ASN HB2 H 1 2.85 . . 2 . . . . . . . . 5376 1 40 . 1 1 4 4 ASN HB3 H 1 2.75 . . 2 . . . . . . . . 5376 1 41 . 1 1 4 4 ASN HD21 H 1 7.68 . . 2 . . . . . . . . 5376 1 42 . 1 1 4 4 ASN HD22 H 1 6.97 . . 2 . . . . . . . . 5376 1 43 . 1 1 4 4 ASN CA C 13 53.1 . . 1 . . . . . . . . 5376 1 44 . 1 1 4 4 ASN CB C 13 38.6 . . 1 . . . . . . . . 5376 1 45 . 1 1 4 4 ASN N N 15 119.7 . . 1 . . . . . . . . 5376 1 46 . 1 1 4 4 ASN ND2 N 15 113.2 . . 1 . . . . . . . . 5376 1 47 . 1 1 5 5 LEU H H 1 8.35 . . 1 . . . . . . . . 5376 1 48 . 1 1 5 5 LEU HA H 1 4.31 . . 1 . . . . . . . . 5376 1 49 . 1 1 5 5 LEU HB2 H 1 1.65 . . 2 . . . . . . . . 5376 1 50 . 1 1 5 5 LEU HB3 H 1 1.59 . . 2 . . . . . . . . 5376 1 51 . 1 1 5 5 LEU HG H 1 1.60 . . 1 . . . . . . . . 5376 1 52 . 1 1 5 5 LEU HD11 H 1 0.92 . . 1 . . . . . . . . 5376 1 53 . 1 1 5 5 LEU HD12 H 1 0.92 . . 1 . . . . . . . . 5376 1 54 . 1 1 5 5 LEU HD13 H 1 0.92 . . 1 . . . . . . . . 5376 1 55 . 1 1 5 5 LEU HD21 H 1 0.86 . . 1 . . . . . . . . 5376 1 56 . 1 1 5 5 LEU HD22 H 1 0.86 . . 1 . . . . . . . . 5376 1 57 . 1 1 5 5 LEU HD23 H 1 0.86 . . 1 . . . . . . . . 5376 1 58 . 1 1 5 5 LEU CA C 13 55.4 . . 1 . . . . . . . . 5376 1 59 . 1 1 5 5 LEU CB C 13 42.2 . . 1 . . . . . . . . 5376 1 60 . 1 1 5 5 LEU CG C 13 27.0 . . 1 . . . . . . . . 5376 1 61 . 1 1 5 5 LEU CD1 C 13 25.0 . . 1 . . . . . . . . 5376 1 62 . 1 1 5 5 LEU CD2 C 13 23.2 . . 1 . . . . . . . . 5376 1 63 . 1 1 5 5 LEU N N 15 122.9 . . 1 . . . . . . . . 5376 1 64 . 1 1 6 6 LYS H H 1 8.36 . . 1 . . . . . . . . 5376 1 65 . 1 1 6 6 LYS HA H 1 4.27 . . 1 . . . . . . . . 5376 1 66 . 1 1 6 6 LYS HB2 H 1 1.82 . . 2 . . . . . . . . 5376 1 67 . 1 1 6 6 LYS HB3 H 1 1.78 . . 2 . . . . . . . . 5376 1 68 . 1 1 6 6 LYS HG2 H 1 1.43 . . 2 . . . . . . . . 5376 1 69 . 1 1 6 6 LYS HG3 H 1 1.39 . . 2 . . . . . . . . 5376 1 70 . 1 1 6 6 LYS HD2 H 1 1.66 . . 1 . . . . . . . . 5376 1 71 . 1 1 6 6 LYS HD3 H 1 1.66 . . 1 . . . . . . . . 5376 1 72 . 1 1 6 6 LYS HE2 H 1 2.97 . . 1 . . . . . . . . 5376 1 73 . 1 1 6 6 LYS HE3 H 1 2.97 . . 1 . . . . . . . . 5376 1 74 . 1 1 6 6 LYS CA C 13 56.7 . . 1 . . . . . . . . 5376 1 75 . 1 1 6 6 LYS CB C 13 32.9 . . 1 . . . . . . . . 5376 1 76 . 1 1 6 6 LYS CG C 13 24.7 . . 1 . . . . . . . . 5376 1 77 . 1 1 6 6 LYS CD C 13 29.1 . . 1 . . . . . . . . 5376 1 78 . 1 1 6 6 LYS CE C 13 42.1 . . 1 . . . . . . . . 5376 1 79 . 1 1 6 6 LYS N N 15 121.8 . . 1 . . . . . . . . 5376 1 80 . 1 1 7 7 ASP H H 1 8.36 . . 1 . . . . . . . . 5376 1 81 . 1 1 7 7 ASP HA H 1 4.61 . . 1 . . . . . . . . 5376 1 82 . 1 1 7 7 ASP HB2 H 1 2.75 . . 2 . . . . . . . . 5376 1 83 . 1 1 7 7 ASP HB3 H 1 2.66 . . 2 . . . . . . . . 5376 1 84 . 1 1 7 7 ASP CA C 13 54.5 . . 1 . . . . . . . . 5376 1 85 . 1 1 7 7 ASP CB C 13 41.1 . . 1 . . . . . . . . 5376 1 86 . 1 1 7 7 ASP N N 15 121.4 . . 1 . . . . . . . . 5376 1 87 . 1 1 8 8 SER H H 1 8.31 . . 1 . . . . . . . . 5376 1 88 . 1 1 8 8 SER HA H 1 4.37 . . 1 . . . . . . . . 5376 1 89 . 1 1 8 8 SER HB2 H 1 3.93 . . 2 . . . . . . . . 5376 1 90 . 1 1 8 8 SER HB3 H 1 3.89 . . 2 . . . . . . . . 5376 1 91 . 1 1 8 8 SER CA C 13 58.9 . . 1 . . . . . . . . 5376 1 92 . 1 1 8 8 SER CB C 13 63.8 . . 1 . . . . . . . . 5376 1 93 . 1 1 8 8 SER N N 15 116.3 . . 1 . . . . . . . . 5376 1 94 . 1 1 9 9 GLY H H 1 8.53 . . 1 . . . . . . . . 5376 1 95 . 1 1 9 9 GLY HA2 H 1 3.93 . . 1 . . . . . . . . 5376 1 96 . 1 1 9 9 GLY HA3 H 1 3.93 . . 1 . . . . . . . . 5376 1 97 . 1 1 9 9 GLY CA C 13 45.4 . . 1 . . . . . . . . 5376 1 98 . 1 1 9 9 GLY N N 15 110.8 . . 1 . . . . . . . . 5376 1 99 . 1 1 10 10 LEU H H 1 7.94 . . 1 . . . . . . . . 5376 1 100 . 1 1 10 10 LEU HA H 1 4.30 . . 1 . . . . . . . . 5376 1 101 . 1 1 10 10 LEU HB2 H 1 1.50 . . 2 . . . . . . . . 5376 1 102 . 1 1 10 10 LEU HB3 H 1 1.44 . . 2 . . . . . . . . 5376 1 103 . 1 1 10 10 LEU HG H 1 1.50 . . 1 . . . . . . . . 5376 1 104 . 1 1 10 10 LEU HD11 H 1 0.88 . . 1 . . . . . . . . 5376 1 105 . 1 1 10 10 LEU HD12 H 1 0.88 . . 1 . . . . . . . . 5376 1 106 . 1 1 10 10 LEU HD13 H 1 0.88 . . 1 . . . . . . . . 5376 1 107 . 1 1 10 10 LEU HD21 H 1 0.81 . . 1 . . . . . . . . 5376 1 108 . 1 1 10 10 LEU HD22 H 1 0.81 . . 1 . . . . . . . . 5376 1 109 . 1 1 10 10 LEU HD23 H 1 0.81 . . 1 . . . . . . . . 5376 1 110 . 1 1 10 10 LEU CA C 13 55.0 . . 1 . . . . . . . . 5376 1 111 . 1 1 10 10 LEU CB C 13 42.4 . . 1 . . . . . . . . 5376 1 112 . 1 1 10 10 LEU CG C 13 26.8 . . 1 . . . . . . . . 5376 1 113 . 1 1 10 10 LEU CD1 C 13 25.0 . . 1 . . . . . . . . 5376 1 114 . 1 1 10 10 LEU CD2 C 13 23.1 . . 1 . . . . . . . . 5376 1 115 . 1 1 10 10 LEU N N 15 121.4 . . 1 . . . . . . . . 5376 1 116 . 1 1 11 11 PHE H H 1 7.71 . . 1 . . . . . . . . 5376 1 117 . 1 1 11 11 PHE HA H 1 4.43 . . 1 . . . . . . . . 5376 1 118 . 1 1 11 11 PHE HB2 H 1 3.17 . . 2 . . . . . . . . 5376 1 119 . 1 1 11 11 PHE HB3 H 1 2.94 . . 2 . . . . . . . . 5376 1 120 . 1 1 11 11 PHE HD1 H 1 7.22 . . 1 . . . . . . . . 5376 1 121 . 1 1 11 11 PHE HD2 H 1 7.22 . . 1 . . . . . . . . 5376 1 122 . 1 1 11 11 PHE HE1 H 1 7.33 . . 1 . . . . . . . . 5376 1 123 . 1 1 11 11 PHE HE2 H 1 7.33 . . 1 . . . . . . . . 5376 1 124 . 1 1 11 11 PHE HZ H 1 7.27 . . 1 . . . . . . . . 5376 1 125 . 1 1 11 11 PHE CA C 13 58.9 . . 1 . . . . . . . . 5376 1 126 . 1 1 11 11 PHE CB C 13 40.4 . . 1 . . . . . . . . 5376 1 127 . 1 1 11 11 PHE N N 15 124.9 . . 1 . . . . . . . . 5376 1 stop_ save_