data_6205 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 6205 _Entry.Title ; 1H chemical shift assignments for AbaB12-DKP-insulin ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2004-05-10 _Entry.Accession_date 2004-05-10 _Entry.Last_release_date 2004-05-10 _Entry.Original_release_date 2004-05-10 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 3.2.0.16 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _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.ORCID _Entry_author.Entry_ID 1 K. Huang . . . . 6205 2 B. Xu . . . . 6205 3 S. Hu . Q. . . 6205 4 Y. Chu . C. . . 6205 5 Q. Hua . X. . . 6205 6 J. Whittaker . . . . 6205 7 S. Nakagawa . H. . . 6205 8 P. DeMeyts . . . . 6205 9 P. Katsoyannis . G. . . 6205 10 M. Weiss . A. . . 6205 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 6205 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 275 6205 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 . . 2008-07-15 . update BMRB 'Updating non-standard residue' 6205 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 6203 AlaB12-DKP-insulin 6205 BMRB 6204 AbaB12-DKP-insulin 6205 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 6205 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; How Insulin Binds: the B-Chain alpha-Helix Contacts the L1 beta -Helix of the Insulin Receptor. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 341 _Citation.Journal_issue . _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 529 _Citation.Page_last 550 _Citation.Year 2004 _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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 K. Huang . . . . 6205 1 2 B. Xu . . . . 6205 1 3 S. Hu . Q. . . 6205 1 4 Y. Chu . C. . . 6205 1 5 Q. Hua . X. . . 6205 1 6 Y. Qu . . . . 6205 1 7 B. Li . . . . 6205 1 8 S. Wang . . . . 6205 1 9 R. Wang . Y. . . 6205 1 10 S. Nakagawa . H. . . 6205 1 11 A. Theede . M. . . 6205 1 12 J. Whittaker . . . . 6205 1 13 P. 'De Meyts' . . . . 6205 1 14 P. Katsoyannis . G. . . 6205 1 15 M. Weiss . A. . . 6205 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID Ala-B12-DKP-insulin 6205 1 'insulin receptor' 6205 1 'protein unfolding' 6205 1 'receptor binding' 6205 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_DKP-HI _Assembly.Sf_category assembly _Assembly.Sf_framecode DKP-HI _Assembly.Entry_ID 6205 _Assembly.ID 1 _Assembly.Name 'insulin analogue' _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 'all disulfide bound' _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 6205 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 'insulin analogue chain A' 1 $DKP_HI_A . . . native . . . . . 6205 1 2 'insulin analogue chain B' 2 $DKP_HI_B . . . native . . . . . 6205 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_asym_ID_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_asym_ID_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 6 6 SG . 1 . 1 CYS 11 11 SG . . . . . . . . . . . . 6205 1 2 disulfide single . 1 . 1 CYS 7 7 SG . 2 . 2 CYS 7 7 SG . . . . . . . . . . . . 6205 1 3 disulfide single . 1 . 1 CYS 20 20 SG . 2 . 2 CYS 19 19 SG . . . . . . . . . . . . 6205 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 yes PDB 1T1Q . . . . . . 6205 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID DKP-HI abbreviation 6205 1 'insulin analogue' system 6205 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_DKP_HI_A _Entity.Sf_category entity _Entity.Sf_framecode DKP_HI_A _Entity.Entry_ID 6205 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'AbaB12-DKP-insulin, chain A' _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 ; GIVEQCCTSICSLYQLENYC N ; _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 21 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _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 2008-03-24 _Entity.DB_query_revised_last_date 2008-03-03 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 . . BMRB 1761 . 'insulin A chain' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . BMRB 4997 . Insulin . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . BMRB 6203 . 'ThrB12-DKP-insulin, chain A' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . BMRB 6204 . 'AlaB12-DKP-insulin, chain A' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . BMRB 4266 . [D-AlaB26]destetra(B27-B30)insulin-B26-amide . . . . . 44.68 47 100 100 2e-05 . . . . 6205 1 . . PDB 1A7F . 'A Chain A, Insulin Mutant B16 Glu, B24 Gly,Des-B30, Nmr, 20 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1AI0 . 'A Chain A, R6 Human Insulin Hexamer(Non-Symmetric), Nmr, 10 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1AIY . 'A Chain A, R6 Human Insulin Hexamer(Symmetric), Nmr, 10 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1B17 . 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 5.00Coordinates)' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1B18 . 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 5.53Coordinates)' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1B19 . 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 5.80Coordinates)' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1B2A . 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 6.00Coordinates)' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1B2B . 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 6.16Coordinates)' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1B2C . 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 6.26Coordinates)' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1B2D . 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 6.35Coordinates)' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1B2E . 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 6.50Coordinates)' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1B2F . 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 6.98Coordinates)' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1B2G . 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 9.00Coordinates)' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1B9E . 'A Chain A, Human Insulin Mutant Serb9glu' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1BEN . 'A Chain A, Insulin Complexed With4-Hydroxybenzamide' . . . . . 100.00 21 100 100 1e-04 . . . . 6205 1 . . PDB 1BZV . 'A Chain A,[d-Alab26]-Des(B27-B30)-Insulin-B26-Amide A SuperpotentSingle-Replacement Insulin Analogue, Nmr, MinimizedAver' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1DEI . 'A Chain A, Desheptapeptide (B24-B30) Insulin' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1EV3 . 'A Chain A, Structure Of The RhombohedralForm Of The M-CresolINSULIN R6 Hexamer' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1EV6 . 'A Chain A, Structure Of The Monoclinic FormOf The M-CresolINSULIN R6 Hexamer' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1EVR . 'A Chain A, The Structure Of TheResorcinolINSULIN R6 HEXAMER' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1FU2 . 'A Chain A, First Protein StructureDetermined From X-Ray Powder Diffraction Data' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1FUB . 'A Chain A, First Protein StructureDetermined From X-Ray Powder Diffraction Data' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1G7A . 'A Chain A, 1.2 A Structure Of T3r3 HumanInsulin At 100 K' . . . . . 100.00 21 100 100 1e-04 . . . . 6205 1 . . PDB 1G7B . 'A Chain A, 1.3 A Structure Of T3r3 HumanInsulin At 100 K' . . . . . 100.00 21 100 100 1e-04 . . . . 6205 1 . . PDB 1GUJ . 'A Chain A, Insulin At Ph 2: StructuralAnalysis Of The Conditions Promoting Insulin FibreFormation.' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1HIQ . 'A Chain A, Paradoxical Structure AndFunction In A Mutant Human Insulin Associated WithDiabetes Mellitus' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1HIS . 'A Chain A, Structure And Dynamics OfDes-Pentapeptide-Insulin In Solution: TheMolten-Globule Hypothesis' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1HIT . 'A Chain A, Receptor Binding Redefined By AStructural Switch In A Mutant Human Insulin' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1HLS . 'A Chain A, Nmr Structure Of The HumanInsulin-His(B16)' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1HTV . 'A Chain A, Crystal Structure OfDestripeptide (B28-B30) Insulin' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1HUI . 'A Chain A, Insulin Mutant (B1, B10, B16,B27)glu, Des-B30, Nmr, 25 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1IZA . 'A Chain A, Role Of B13 Glu In InsulinAssembly: The Hexamer Structure Of Recombinant Mutant(B13 Glu-> Gln) Insulin' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1IZB . 'A Chain A, Role Of B13 Glu In InsulinAssembly: The Hexamer Structure Of Recombinant Mutant(B13 Glu-> Gln) Insulin' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1JCO . 'A Chain A, Solution Structure Of TheMonomeric [thr(B27)->pro,Pro(B28)- >thr] Insulin Mutant(Pt Insulin)' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1LKQ . 'A Chain A, Nmr Structure Of Human InsulinMutant Ile-A2-Gly, Val-A3- Gly, His-B10-Asp,Pro-B28-Lys, Lys-B29-Pro, 20 Struct' . . . . . 100.00 21 100 100 8e-04 . . . . 6205 1 . . PDB 1LPH . 'A Chain A, Lys(B28)pro(B29)-Human Insulin' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1M5A . 'A Chain A, Crystal Structure Of2-Co(2+)-Insulin At 1.2a Resolution' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1MHI . 'A Chain A, Three-Dimensional SolutionStructure Of An Insulin Dimer. A Study Of The B9(Asp)Mutant Of Human Insulin Using' . . . . . 100.00 21 100 100 1e-04 . . . . 6205 1 . . PDB 1MHJ . 'A Chain A, Solution Structure Of TheSuperactive Monomeric Des- [phe(B25)] Human InsulinMutant. Elucidation Of The Struct' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1MPJ . 'A Chain A, X-Ray Crystallographic Studies OnHexameric Insulins In The Presence Of Helix-StabilizingAgents, Thiocyanate,' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1MSO . 'A Chain A, T6 Human Insulin At 1.0 AResolution' . . . . . 100.00 21 100 100 1e-04 . . . . 6205 1 . . PDB 1OS3 . 'A Chain A, Dehydrated T6 Human Insulin At100 K' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1OS4 . 'A Chain A, Dehydrated T6 Human Insulin At295 K' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1QIY . 'A Chain A, Human Insulin Hexamers With ChainB His Mutated To Tyr Complexed With Phenol' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1QIZ . 'A Chain A, Human Insulin Hexamers With ChainB His Mutated To Tyr Complexed With Resorcinol' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1QJ0 . 'A Chain A, Human Insulin Hexamers With ChainB His Mutated To Tyr' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1SDB . 'A Chain A, Porcine Desb1-2Despentapeptide(B26-B30) Insulin' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1SF1 . 'A Chain A, Nmr Structure Of Human InsulinUnder Amyloidogenic Condition, 15 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1SJT . 'A Chain A, Mini-Proinsulin, Two ChainInsulin Analog Mutant: Des B30, His(B 10)asp, Pro(B28)asp, Nmr, 20 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1T1K . 'A Chain A, Nmr Structure Of Human InsulinMutant His-B10-Asp, Val-B12- Ala, Pro-B28-Lys,Lys-B29-Pro, 15 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1T1P . 'A Chain A, Nmr Structure Of Human InsulinMutant His-B10-Asp, Val-B12- Thr, Pro-B28-Lys,Lys-B29-Pro, 15 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1T1Q . 'A Chain A, Nmr Structure Of Human InsulinMutant His-B10-Asp, Val-B12- Aba, Pro-B28-Lys,Lys-B29-Pro, 15 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1TRZ . 'A Chain A, Crystallographic Evidence For DualCoordination Around Zinc In The T3r3 Human InsulinHexamer' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1TYL . "A Chain A, The Structure Of A Complex OfHexameric Insulin And 4'- Hydroxyacetanilide" . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1TYM . "A Chain A, The Structure Of A Complex OfHexameric Insulin And 4'- Hydroxyacetanilide" . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1UZ9 . 'A Chain A, Crystallographic And SolutionStudies Of N-Lithocholyl Insulin: A New Generation OfProlonged-Acting Insulins.' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1W8P . 'A Chain A, Structural Properties Of TheB25tyr-Nme-B26phe Insulin Mutant.' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1WAV . 'A Chain A, Crystal Structure Of Form BMonoclinic Crystal Of Insulin' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1XDA . 'A Chain A, Structure Of Insulin' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1XGL . 'A Chain A, Human Insulin Disulfide Isomer,Nmr, 10 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1ZEG . 'A Chain A, Structure Of B28 Asp Insulin InComplex With Phenol' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1ZEH . 'A Chain A, Structure Of Insulin' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1ZNI . 'A Chain A, Insulin' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1ZNJ . 'A Chain A, Insulin, Monoclinic Crystal Form' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2AIY . 'A Chain A, R6 Human Insulin Hexamer(Symmetric), Nmr, 20 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2C8Q . 'A Chain A, Insuline(1sec) And Uv LaserExcited Fluorescence' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2C8R . 'A Chain A, Insuline(60sec) And Uv LaserExcited Fluorescence' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2CEU . 'A Chain A, Despentapeptide Insulin In AceticAcid (Ph 2)' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2EFA . 'A Chain A, Neutron Crystal Structure OfCubic Insulin At Pd6.6' . . . . . 100.00 21 100 100 5e-04 . . . . 6205 1 . . PDB 2G4M . 'A Chain A, Insulin Collected At 2.0 AWavelength' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2H67 . 'A Chain A, Nmr Structure Of Human InsulinMutant His-B5-Ala, His-B10- Asp Pro-B28-Lys,Lys-B29-Pro, 20 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2HH4 . 'A Chain A, Nmr Structure Of Human InsulinMutant Gly-B8-D-Ser, His-B10- Asp Pro-B28-Lys,Lys-B29-Pro, 20 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2HHO . 'A Chain A, Nmr Structure Of Human InsulinMutant Gly-B8-Ser, His-B10- Asp Pro-B28-Lys,Lys-B29-Pro, 20 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2HIU . 'A Chain A, Nmr Structure Of Human InsulinIn 20% Acetic Acid, Zinc- Free, 10 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2JMN . 'A Chain A, Nmr Structure Of Human InsulinMutant His-B10-Asp, Pro-B28- Lys, Lys-B29-Pro, 20Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2JV1 . 'A Chain A, Nmr Structure Of Human InsulinMonomer In 35% Cd3cn Zinc Free, 50 Structures' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2OLY . 'A Chain A, Structure Of Human Insulin InPresence Of Urea At Ph 7.0' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2OLZ . 'A Chain A, Structure Of Human Insulin InPresence Of Thiocyanate At Ph 7.0' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2OM0 . '1 Chain 1, Structure Of Human Insulin InPresence Of Urea At Ph 6.5' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2OM1 . '1 Chain 1, Structure Of Human Insulin InPresence Of Thiocyanate At Ph 6.5' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2OMG . 'A Chain A, Structure Of Human InsulinCocrystallized With Protamine And Urea' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2OMH . 'A Chain A, Structure Of Human InsulinCocrystallized With Arg-12 Peptide In Presence Of Urea' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2OMI . 'A Chain A, Structure Of Human InsulinCocrystallized With Protamine' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 2TCI . 'A Chain A, X-Ray Crystallographic Studies OnHexameric Insulins In The Presence Of Helix-StabilizingAgents, Thiocyanate,' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 3AIY . 'A Chain A, R6 Human Insulin Hexamer(Symmetric), Nmr, Refined Average Structure' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 3INS . 'A Chain A, Structure Of Insulin. Results OfJoint Neutron And X-Ray Refinement' . . . . . 100.00 21 100 100 5e-04 . . . . 6205 1 . . PDB 3MTH . 'A Chain A, X-Ray Crystallographic Studies OnHexameric Insulins In The Presence Of Helix-StabilizingAgents, Thiocyanate,' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 4AIY . "A Chain A, R6 Human Insulin Hexamer(Symmetric), Nmr, 'green' Substate, Average Structure" . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 4INS . 'A Chain A, The Structure Of 2zn Pig InsulinCrystals At 1.5 Angstroms Resolution' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 5AIY . "A Chain A, R6 Human Insulin Hexamer(Symmetric), Nmr, 'red' Substate, Average Structure" . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 7INS . 'A Chain A, Structure Of Porcine InsulinCocrystallized With Clupeine Z' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 9INS . 'A Chain A, Monovalent Cation Binding In CubicInsulin Crystals' . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PDB 1SJU . 'A Chain A, Mini-Proinsulin, Single ChainInsulin Analog Mutant: Des B30, His(B 10)asp, Pro(B28)asp And Peptide Bond Betwe' . . . . . 42.00 50 100 100 2e-05 . . . . 6205 1 . . PDB 6INS . 'E Chain E, X-Ray Analysis Of The Single ChainB29-A1 Peptide-Linked Insulin Molecule. A CompletelyInactive Analogue' . . . . . 42.00 50 100 100 2e-05 . . . . 6205 1 . . PDB 1ZEI . 'A Chain A, Cross-Linked B28 Asp Insulin' . . . . . 39.62 53 100 100 2e-05 . . . . 6205 1 . . PDB 1EFE . 'A Chain A, An Active Mini-Proinsulin, M2pi' . . . . . 35.00 60 100 100 2e-05 . . . . 6205 1 . . EMBL CAA23475.1 . 'preproinsulin [Canis sp.]' . . . . . 19.09 110 100 100 2e-05 . . . . 6205 1 . . EMBL CAA23828.1 . 'preproinsulin [Homo sapiens]' . . . . . 19.09 110 100 100 2e-05 . . . . 6205 1 . . EMBL CAA43403.1 . 'Preproinsulin [Pan troglodytes]' . . . . . 19.09 110 100 100 2e-05 . . . . 6205 1 . . EMBL CAA43405.1 . 'Preproinsulin [Chlorocebus aethiops]' . . . . . 19.09 110 100 100 2e-05 . . . . 6205 1 . . EMBL CAA49913.1 . 'pre-proinsulin [Homo sapiens]' . . . . . 19.09 110 100 100 2e-05 . . . . 6205 1 . . GenBank ABP93829.1 . 'mini-proinsulin [synthetic construct]' . . . . . 35.59 59 100 100 2e-05 . . . . 6205 1 . . GenBank ABI63346.1 . 'insulin [Homo sapiens]' . . . . . 21.43 98 100 100 2e-05 . . . . 6205 1 . . GenBank AAP36446.1 . 'Homo sapiens insulin [syntheticconstruct]' . . . . . 18.92 111 100 100 2e-05 . . . . 6205 1 . . GenBank AAX29480.1 . 'insulin [synthetic construct]' . . . . . 18.92 111 100 100 2e-05 . . . . 6205 1 . . GenBank AAX29481.1 . 'insulin [synthetic construct]' . . . . . 18.92 111 100 100 2e-05 . . . . 6205 1 . . PRF 560164B . insulin . . . . . 100.00 21 100 100 2e-05 . . . . 6205 1 . . PRF 580107B . insulin . . . . . 42.00 50 100 100 2e-05 . . . . 6205 1 . . PRF 600165A . insulin . . . . . 41.18 51 100 100 2e-05 . . . . 6205 1 . . PRF 1006230A . insulin,pro- . . . . . 24.42 86 100 100 2e-05 . . . . 6205 1 . . PRF 0601246A . insulin,prepro . . . . . 19.09 110 100 100 2e-05 . . . . 6205 1 . . REF NP_000198.1 . 'proinsulin precursor [Homo sapiens]' . . . . . 19.09 110 100 100 2e-05 . . . . 6205 1 . . REF NP_001008996.1 . 'proinsulin precursor [Pantroglodytes]' . . . . . 19.09 110 100 100 2e-05 . . . . 6205 1 . . REF NP_001075804.1 . 'insulin [Oryctolagus cuniculus]' . . . . . 19.09 110 100 100 2e-05 . . . . 6205 1 . . REF XP_540786.1 . 'PREDICTED: similar to Insulinprecursor [Canis familiaris]' . . . . . 19.09 110 100 100 2e-05 . . . . 6205 1 . . SWISS-PROT P67973 . 'INS_BALPH Insulin [Contains: Insulin Bchain; Insulin A chain]' . . . . . 41.18 51 100 100 2e-05 . . . . 6205 1 . . SWISS-PROT P67974 . 'INS_PHYCA Insulin [Contains: Insulin Bchain; Insulin A chain]' . . . . . 41.18 51 100 100 2e-05 . . . . 6205 1 . . SWISS-PROT P30406 . 'INS_MACFA Insulin precursor [Contains: InsulinB chain; Insulin A chain]' . . . . . 19.09 110 100 100 2e-05 . . . . 6205 1 . . SWISS-PROT P30410 . 'INS_PANTR Insulin precursor [Contains: InsulinB chain; Insulin A chain]' . . . . . 19.09 110 100 100 2e-05 . . . . 6205 1 . . SWISS-PROT Q91XI3 . 'INS_SPETR Insulin precursor [Contains:Insulin B chain; Insulin A chain]' . . . . . 19.09 110 100 100 2e-05 . . . . 6205 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Aba-B12-Val, Asp-B10-His, Lys-B28-Pro, Pro-B29-Lys insulin' variant 6205 1 'AbaB12-DKP-insulin, chain A' common 6205 1 DKP_HI_A abbreviation 6205 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 . GLY . 6205 1 2 . ILE . 6205 1 3 . VAL . 6205 1 4 . GLU . 6205 1 5 . GLN . 6205 1 6 . CYS . 6205 1 7 . CYS . 6205 1 8 . THR . 6205 1 9 . SER . 6205 1 10 . ILE . 6205 1 11 . CYS . 6205 1 12 . SER . 6205 1 13 . LEU . 6205 1 14 . TYR . 6205 1 15 . GLN . 6205 1 16 . LEU . 6205 1 17 . GLU . 6205 1 18 . ASN . 6205 1 19 . TYR . 6205 1 20 . CYS . 6205 1 21 . ASN . 6205 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 . GLY 1 1 6205 1 . ILE 2 2 6205 1 . VAL 3 3 6205 1 . GLU 4 4 6205 1 . GLN 5 5 6205 1 . CYS 6 6 6205 1 . CYS 7 7 6205 1 . THR 8 8 6205 1 . SER 9 9 6205 1 . ILE 10 10 6205 1 . CYS 11 11 6205 1 . SER 12 12 6205 1 . LEU 13 13 6205 1 . TYR 14 14 6205 1 . GLN 15 15 6205 1 . LEU 16 16 6205 1 . GLU 17 17 6205 1 . ASN 18 18 6205 1 . TYR 19 19 6205 1 . CYS 20 20 6205 1 . ASN 21 21 6205 1 stop_ save_ save_DKP_HI_B _Entity.Sf_category entity _Entity.Sf_framecode DKP_HI_B _Entity.Entry_ID 6205 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name 'AbaB12-DKP-insulin, chain B' _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 ; FVNQHLCGSDLXEALYLVCG ERGFFYTKPT ; _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 ABA _Entity.Nonpolymer_comp_label $chem_comp_ABA _Entity.Number_of_monomers 30 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID 2 _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 ; an non-standard amino acid alpha-amino-butyric acid replace the valineB12 in B-chain ; _Entity.DB_query_date 2008-03-24 _Entity.DB_query_revised_last_date 2008-01-16 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 . yes PDB 1T1Q . 'B Chain B, Nmr Structure Of Human InsulinMutant His-B10-Asp, Val-B12- Aba, Pro-B28-Lys,Lys-B29-Pro, 15 Structures' . . . . . 100.00 30 100 100 4e-10 . . . . 6205 2 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Aba-B12-Val, Asp-B10-His, Lys-B28-Pro, Pro-B29-Lys insulin' variant 6205 2 'AbaB12-DKP-insulin, chain B' common 6205 2 DKP_HI_B abbreviation 6205 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 . PHE . 6205 2 2 . VAL . 6205 2 3 . ASN . 6205 2 4 . GLN . 6205 2 5 . HIS . 6205 2 6 . LEU . 6205 2 7 . CYS . 6205 2 8 . GLY . 6205 2 9 . SER . 6205 2 10 . ASP . 6205 2 11 . LEU . 6205 2 12 . ABA . 6205 2 13 . GLU . 6205 2 14 . ALA . 6205 2 15 . LEU . 6205 2 16 . TYR . 6205 2 17 . LEU . 6205 2 18 . VAL . 6205 2 19 . CYS . 6205 2 20 . GLY . 6205 2 21 . GLU . 6205 2 22 . ARG . 6205 2 23 . GLY . 6205 2 24 . PHE . 6205 2 25 . PHE . 6205 2 26 . TYR . 6205 2 27 . THR . 6205 2 28 . LYS . 6205 2 29 . PRO . 6205 2 30 . THR . 6205 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 . PHE 1 1 6205 2 . VAL 2 2 6205 2 . ASN 3 3 6205 2 . GLN 4 4 6205 2 . HIS 5 5 6205 2 . LEU 6 6 6205 2 . CYS 7 7 6205 2 . GLY 8 8 6205 2 . SER 9 9 6205 2 . ASP 10 10 6205 2 . LEU 11 11 6205 2 . ABA 12 12 6205 2 . GLU 13 13 6205 2 . ALA 14 14 6205 2 . LEU 15 15 6205 2 . TYR 16 16 6205 2 . LEU 17 17 6205 2 . VAL 18 18 6205 2 . CYS 19 19 6205 2 . GLY 20 20 6205 2 . GLU 21 21 6205 2 . ARG 22 22 6205 2 . GLY 23 23 6205 2 . PHE 24 24 6205 2 . PHE 25 25 6205 2 . TYR 26 26 6205 2 . THR 27 27 6205 2 . LYS 28 28 6205 2 . PRO 29 29 6205 2 . THR 30 30 6205 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 6205 _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.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.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $DKP_HI_A . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 6205 1 2 2 $DKP_HI_B . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 6205 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 6205 _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_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.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $DKP_HI_A . 'chemical synthesis' . . . . . . . . . . . . . . . . 6205 1 2 2 $DKP_HI_B . 'chemical synthesis' . . . . . . . . . . . . . . . . 6205 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_ABA _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_ABA _Chem_comp.Entry_ID 6205 _Chem_comp.ID ABA _Chem_comp.Provenance PDB _Chem_comp.Name 'ALPHA-AMINOBUTYRIC ACID' _Chem_comp.Type 'L-peptide linking' _Chem_comp.BMRB_code . _Chem_comp.PDB_code ABA _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces AA3 _Chem_comp.One_letter_code A _Chem_comp.Three_letter_code ABA _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.Atom_nomenclature_source . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID ALA _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'C4 H9 N O2' _Chem_comp.Formula_weight 103.120 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 1CWC _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Aug 1 09:46:43 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID CCC(C(=O)O)N SMILES 'OpenEye OEToolkits' 1.5.0 6205 ABA CC[C@@H](C(=O)O)N SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 6205 ABA CC[C@H](N)C(O)=O SMILES_CANONICAL CACTVS 3.341 6205 ABA CC[CH](N)C(O)=O SMILES CACTVS 3.341 6205 ABA InChI=1S/C4H9NO2/c1-2-3(5)4(6)7/h3H,2,5H2,1H3,(H,6,7)/t3-/m0/s1 InChI InChI 1.03 6205 ABA O=C(O)C(N)CC SMILES ACDLabs 10.04 6205 ABA QWCKQJZIFLGMSD-VKHMYHEASA-N InChIKey InChI 1.03 6205 ABA stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID '(2S)-2-aminobutanoic acid' 'SYSTEMATIC NAME' ACDLabs 10.04 6205 ABA '(2S)-2-aminobutanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 6205 ABA stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID N . N . . N . . N 0 . . . . no no . . . . 8.872 . 35.101 . 18.829 . -0.644 1.545 0.393 1 . 6205 ABA CA . CA . . C . . S 0 . . . . no no . . . . 10.112 . 35.739 . 19.276 . -0.299 0.117 0.432 2 . 6205 ABA C . C . . C . . N 0 . . . . no no . . . . 10.743 . 36.533 . 18.128 . 1.141 -0.063 0.030 3 . 6205 ABA O . O . . O . . N 0 . . . . no no . . . . 11.507 . 35.962 . 17.351 . 1.707 0.803 -0.595 4 . 6205 ABA CB . CB . . C . . N 0 . . . . no no . . . . 11.098 . 34.657 . 19.740 . -1.200 -0.651 -0.537 5 . 6205 ABA CG . CG . . C . . N 0 . . . . no no . . . . 10.518 . 33.684 . 20.758 . -2.651 -0.572 -0.057 6 . 6205 ABA OXT . OXT . . O . . N 0 . . . . no yes . . . . 10.475 . 37.838 . 18.044 . 1.796 -1.186 0.364 7 . 6205 ABA H . H . . H . . N 0 . . . . no no . . . . 8.270 . 34.956 . 19.614 . -0.517 1.922 -0.535 8 . 6205 ABA HN2 . HN2 . . H . . N 0 . . . . no yes . . . . 8.415 . 35.691 . 18.163 . -1.586 1.699 0.720 9 . 6205 ABA HA . HA . . H . . N 0 . . . . no no . . . . 9.884 . 36.424 . 20.105 . -0.445 -0.263 1.443 10 . 6205 ABA HB3 . HB3 . . H . . N 0 . . . . no no . . . . 11.408 . 34.079 . 18.857 . -1.122 -0.213 -1.531 11 . 6205 ABA HB2 . HB2 . . H . . N 0 . . . . no no . . . . 11.934 . 35.175 . 20.233 . -0.887 -1.695 -0.574 12 . 6205 ABA HG1 . HG1 . . H . . N 0 . . . . no no . . . . 10.378 . 32.700 . 20.287 . -2.729 -1.010 0.938 13 . 6205 ABA HG3 . HG3 . . H . . N 0 . . . . no no . . . . 11.209 . 33.588 . 21.609 . -2.964 0.472 -0.020 14 . 6205 ABA HG2 . HG2 . . H . . N 0 . . . . no no . . . . 9.548 . 34.061 . 21.114 . -3.292 -1.119 -0.747 15 . 6205 ABA HXT . HXT . . H . . N 0 . . . . no yes . . . . 10.956 . 38.214 . 17.317 . 2.719 -1.256 0.084 16 . 6205 ABA stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING N CA no N 1 . 6205 ABA 2 . SING N H no N 2 . 6205 ABA 3 . SING N HN2 no N 3 . 6205 ABA 4 . SING CA C no N 4 . 6205 ABA 5 . SING CA CB no N 5 . 6205 ABA 6 . SING CA HA no N 6 . 6205 ABA 7 . DOUB C O no N 7 . 6205 ABA 8 . SING C OXT no N 8 . 6205 ABA 9 . SING CB CG no N 9 . 6205 ABA 10 . SING CB HB3 no N 10 . 6205 ABA 11 . SING CB HB2 no N 11 . 6205 ABA 12 . SING CG HG1 no N 12 . 6205 ABA 13 . SING CG HG3 no N 13 . 6205 ABA 14 . SING CG HG2 no N 14 . 6205 ABA 15 . SING OXT HXT no N 15 . 6205 ABA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 6205 _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 'AbaB12-DKP-insulin, chain A' . . . 1 $DKP_HI_A . . 1.2 . . mM . . . . 6205 1 2 'AbaB12-DKP-insulin, chain B' . . . 2 $DKP_HI_B . . 1.2 . . mM . . . . 6205 1 3 H2O . . . . . . . 90 . . % . . . . 6205 1 4 D2O . . . . . . . 10 . . % . . . . 6205 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 6205 _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 'AbaB12-DKP-insulin, chain A' . . . 1 $DKP_HI_A . . 1.2 . . mM . . . . 6205 2 2 'AbaB12-DKP-insulin, chain B' . . . 2 $DKP_HI_B . . 1.2 . . mM . . . . 6205 2 3 D2O . . . . . . . 100 . . % . . . . 6205 2 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 6205 _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 pH 7.0 0.1 n/a 6205 1 pressure 1 . atm 6205 1 temperature 298 1 K 6205 1 stop_ save_ save_sample_cond_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_2 _Sample_condition_list.Entry_ID 6205 _Sample_condition_list.ID 2 _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 pH 7.6 0.1 n/a 6205 2 pressure 1 . atm 6205 2 temperature 305 1 K 6205 2 stop_ save_ ############################ # Computer software used # ############################ save_DGII _Software.Sf_category software _Software.Sf_framecode DGII _Software.Entry_ID 6205 _Software.ID 1 _Software.Type . _Software.Name DGII _Software.Version 'INSIGHTII 2000' _Software.DOI . _Software.Details 'Molecular Simulations INC.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 6205 1 stop_ save_ save_X-PLOR _Software.Sf_category software _Software.Sf_framecode X-PLOR _Software.Entry_ID 6205 _Software.ID 2 _Software.Type . _Software.Name X-PLOR _Software.Version 3.85 _Software.DOI . _Software.Details Brunger loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'simulated annealing refinement' 6205 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 6205 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer .Bruker _NMR_spectrometer.Model .DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength .800 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 6205 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _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 6205 _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_1 .Bruker .DRX . .800 . . . 6205 1 2 NMR_spectrometer_2 Varian INOVA . 600 . . . 6205 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 6205 _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' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 6205 1 2 '2D TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 6205 1 3 DQF-COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 6205 1 stop_ 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 6205 _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.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . 6205 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 6205 _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_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 NOESY' 1 $sample_1 . 6205 1 2 '2D TOCSY' 1 $sample_1 . 6205 1 3 DQF-COSY 1 $sample_1 . 6205 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.Ambiguity_set_ID _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 2 2 ILE H H 1 7.84 0.02 . 1 . . . . . . . . . 6205 1 2 . 1 1 2 2 ILE HA H 1 3.88 0.02 . 1 . . . . . . . . . 6205 1 3 . 1 1 2 2 ILE HB H 1 1.11 0.02 . 1 . . . . . . . . . 6205 1 4 . 1 1 2 2 ILE HG12 H 1 0.86 0.02 . 1 . . . . . . . . . 6205 1 5 . 1 1 2 2 ILE HG13 H 1 0.86 0.02 . 1 . . . . . . . . . 6205 1 6 . 1 1 2 2 ILE HG21 H 1 0.69 0.02 . 1 . . . . . . . . . 6205 1 7 . 1 1 2 2 ILE HG22 H 1 0.69 0.02 . 1 . . . . . . . . . 6205 1 8 . 1 1 2 2 ILE HG23 H 1 0.69 0.02 . 1 . . . . . . . . . 6205 1 9 . 1 1 2 2 ILE HD11 H 1 0.49 0.02 . 1 . . . . . . . . . 6205 1 10 . 1 1 2 2 ILE HD12 H 1 0.49 0.02 . 1 . . . . . . . . . 6205 1 11 . 1 1 2 2 ILE HD13 H 1 0.49 0.02 . 1 . . . . . . . . . 6205 1 12 . 1 1 3 3 VAL H H 1 8.23 0.02 . 1 . . . . . . . . . 6205 1 13 . 1 1 3 3 VAL HA H 1 3.59 0.02 . 1 . . . . . . . . . 6205 1 14 . 1 1 3 3 VAL HB H 1 1.93 0.02 . 1 . . . . . . . . . 6205 1 15 . 1 1 3 3 VAL HG11 H 1 0.92 0.02 . 2 . . . . . . . . . 6205 1 16 . 1 1 3 3 VAL HG12 H 1 0.92 0.02 . 2 . . . . . . . . . 6205 1 17 . 1 1 3 3 VAL HG13 H 1 0.92 0.02 . 2 . . . . . . . . . 6205 1 18 . 1 1 3 3 VAL HG21 H 1 0.88 0.02 . 2 . . . . . . . . . 6205 1 19 . 1 1 3 3 VAL HG22 H 1 0.88 0.02 . 2 . . . . . . . . . 6205 1 20 . 1 1 3 3 VAL HG23 H 1 0.88 0.02 . 2 . . . . . . . . . 6205 1 21 . 1 1 4 4 GLU H H 1 8.33 0.02 . 1 . . . . . . . . . 6205 1 22 . 1 1 4 4 GLU HA H 1 4.12 0.02 . 1 . . . . . . . . . 6205 1 23 . 1 1 4 4 GLU HB2 H 1 2.16 0.02 . 2 . . . . . . . . . 6205 1 24 . 1 1 4 4 GLU HB3 H 1 2.04 0.02 . 2 . . . . . . . . . 6205 1 25 . 1 1 4 4 GLU HG2 H 1 2.48 0.02 . 1 . . . . . . . . . 6205 1 26 . 1 1 4 4 GLU HG3 H 1 2.48 0.02 . 1 . . . . . . . . . 6205 1 27 . 1 1 5 5 GLN H H 1 8.34 0.02 . 1 . . . . . . . . . 6205 1 28 . 1 1 5 5 GLN HA H 1 4.04 0.02 . 1 . . . . . . . . . 6205 1 29 . 1 1 5 5 GLN HB2 H 1 2.07 0.02 . 2 . . . . . . . . . 6205 1 30 . 1 1 5 5 GLN HB3 H 1 2.13 0.02 . 2 . . . . . . . . . 6205 1 31 . 1 1 5 5 GLN HG2 H 1 2.48 0.02 . 2 . . . . . . . . . 6205 1 32 . 1 1 5 5 GLN HG3 H 1 2.38 0.02 . 2 . . . . . . . . . 6205 1 33 . 1 1 6 6 CYS H H 1 8.36 0.02 . 1 . . . . . . . . . 6205 1 34 . 1 1 6 6 CYS HA H 1 5.04 0.02 . 1 . . . . . . . . . 6205 1 35 . 1 1 6 6 CYS HB2 H 1 3.36 0.02 . 2 . . . . . . . . . 6205 1 36 . 1 1 6 6 CYS HB3 H 1 2.83 0.02 . 2 . . . . . . . . . 6205 1 37 . 1 1 7 7 CYS H H 1 8.19 0.02 . 1 . . . . . . . . . 6205 1 38 . 1 1 7 7 CYS HA H 1 4.86 0.02 . 1 . . . . . . . . . 6205 1 39 . 1 1 7 7 CYS HB2 H 1 3.75 0.02 . 2 . . . . . . . . . 6205 1 40 . 1 1 7 7 CYS HB3 H 1 3.29 0.02 . 2 . . . . . . . . . 6205 1 41 . 1 1 8 8 THR H H 1 8.13 0.02 . 1 . . . . . . . . . 6205 1 42 . 1 1 8 8 THR HA H 1 4.06 0.02 . 1 . . . . . . . . . 6205 1 43 . 1 1 8 8 THR HB H 1 4.41 0.02 . 1 . . . . . . . . . 6205 1 44 . 1 1 8 8 THR HG21 H 1 1.25 0.02 . 1 . . . . . . . . . 6205 1 45 . 1 1 8 8 THR HG22 H 1 1.25 0.02 . 1 . . . . . . . . . 6205 1 46 . 1 1 8 8 THR HG23 H 1 1.25 0.02 . 1 . . . . . . . . . 6205 1 47 . 1 1 9 9 SER HA H 1 4.73 0.02 . 1 . . . . . . . . . 6205 1 48 . 1 1 9 9 SER HB2 H 1 3.83 0.02 . 2 . . . . . . . . . 6205 1 49 . 1 1 9 9 SER HB3 H 1 4.00 0.02 . 2 . . . . . . . . . 6205 1 50 . 1 1 10 10 ILE H H 1 7.86 0.02 . 1 . . . . . . . . . 6205 1 51 . 1 1 10 10 ILE HA H 1 4.27 0.02 . 1 . . . . . . . . . 6205 1 52 . 1 1 10 10 ILE HB H 1 1.57 0.02 . 1 . . . . . . . . . 6205 1 53 . 1 1 10 10 ILE HG12 H 1 1.12 0.02 . 2 . . . . . . . . . 6205 1 54 . 1 1 10 10 ILE HG13 H 1 0.43 0.02 . 2 . . . . . . . . . 6205 1 55 . 1 1 10 10 ILE HG21 H 1 0.66 0.02 . 1 . . . . . . . . . 6205 1 56 . 1 1 10 10 ILE HG22 H 1 0.66 0.02 . 1 . . . . . . . . . 6205 1 57 . 1 1 10 10 ILE HG23 H 1 0.66 0.02 . 1 . . . . . . . . . 6205 1 58 . 1 1 10 10 ILE HD11 H 1 0.49 0.02 . 1 . . . . . . . . . 6205 1 59 . 1 1 10 10 ILE HD12 H 1 0.49 0.02 . 1 . . . . . . . . . 6205 1 60 . 1 1 10 10 ILE HD13 H 1 0.49 0.02 . 1 . . . . . . . . . 6205 1 61 . 1 1 11 11 CYS H H 1 9.70 0.02 . 1 . . . . . . . . . 6205 1 62 . 1 1 11 11 CYS HA H 1 4.94 0.02 . 1 . . . . . . . . . 6205 1 63 . 1 1 11 11 CYS HB2 H 1 3.29 0.02 . 2 . . . . . . . . . 6205 1 64 . 1 1 11 11 CYS HB3 H 1 2.96 0.02 . 2 . . . . . . . . . 6205 1 65 . 1 1 12 12 SER H H 1 8.69 0.02 . 1 . . . . . . . . . 6205 1 66 . 1 1 12 12 SER HA H 1 4.62 0.02 . 1 . . . . . . . . . 6205 1 67 . 1 1 12 12 SER HB2 H 1 4.00 0.02 . 2 . . . . . . . . . 6205 1 68 . 1 1 12 12 SER HB3 H 1 4.16 0.02 . 2 . . . . . . . . . 6205 1 69 . 1 1 13 13 LEU H H 1 8.69 0.02 . 1 . . . . . . . . . 6205 1 70 . 1 1 13 13 LEU HA H 1 3.86 0.02 . 1 . . . . . . . . . 6205 1 71 . 1 1 13 13 LEU HB2 H 1 1.41 0.02 . 2 . . . . . . . . . 6205 1 72 . 1 1 13 13 LEU HB3 H 1 1.47 0.02 . 2 . . . . . . . . . 6205 1 73 . 1 1 13 13 LEU HG H 1 1.52 0.02 . 1 . . . . . . . . . 6205 1 74 . 1 1 13 13 LEU HD11 H 1 0.84 0.02 . 2 . . . . . . . . . 6205 1 75 . 1 1 13 13 LEU HD12 H 1 0.84 0.02 . 2 . . . . . . . . . 6205 1 76 . 1 1 13 13 LEU HD13 H 1 0.84 0.02 . 2 . . . . . . . . . 6205 1 77 . 1 1 13 13 LEU HD21 H 1 0.76 0.02 . 2 . . . . . . . . . 6205 1 78 . 1 1 13 13 LEU HD22 H 1 0.76 0.02 . 2 . . . . . . . . . 6205 1 79 . 1 1 13 13 LEU HD23 H 1 0.76 0.02 . 2 . . . . . . . . . 6205 1 80 . 1 1 14 14 TYR H H 1 7.65 0.02 . 1 . . . . . . . . . 6205 1 81 . 1 1 14 14 TYR HA H 1 4.33 0.02 . 1 . . . . . . . . . 6205 1 82 . 1 1 14 14 TYR HB2 H 1 2.99 0.02 . 2 . . . . . . . . . 6205 1 83 . 1 1 14 14 TYR HB3 H 1 3.01 0.02 . 2 . . . . . . . . . 6205 1 84 . 1 1 14 14 TYR HD1 H 1 7.12 0.02 . 1 . . . . . . . . . 6205 1 85 . 1 1 14 14 TYR HD2 H 1 7.12 0.02 . 1 . . . . . . . . . 6205 1 86 . 1 1 14 14 TYR HE1 H 1 6.86 0.02 . 1 . . . . . . . . . 6205 1 87 . 1 1 14 14 TYR HE2 H 1 6.86 0.02 . 1 . . . . . . . . . 6205 1 88 . 1 1 15 15 GLN H H 1 7.46 0.02 . 1 . . . . . . . . . 6205 1 89 . 1 1 15 15 GLN HA H 1 3.98 0.02 . 1 . . . . . . . . . 6205 1 90 . 1 1 15 15 GLN HB2 H 1 2.22 0.02 . 2 . . . . . . . . . 6205 1 91 . 1 1 15 15 GLN HB3 H 1 2.33 0.02 . 2 . . . . . . . . . 6205 1 92 . 1 1 15 15 GLN HG2 H 1 2.39 0.02 . 2 . . . . . . . . . 6205 1 93 . 1 1 15 15 GLN HG3 H 1 2.35 0.02 . 2 . . . . . . . . . 6205 1 94 . 1 1 16 16 LEU H H 1 7.86 0.02 . 1 . . . . . . . . . 6205 1 95 . 1 1 16 16 LEU HA H 1 4.08 0.02 . 1 . . . . . . . . . 6205 1 96 . 1 1 16 16 LEU HB2 H 1 1.34 0.02 . 2 . . . . . . . . . 6205 1 97 . 1 1 16 16 LEU HB3 H 1 1.97 0.02 . 2 . . . . . . . . . 6205 1 98 . 1 1 16 16 LEU HG H 1 1.74 0.02 . 1 . . . . . . . . . 6205 1 99 . 1 1 16 16 LEU HD11 H 1 0.76 0.02 . 2 . . . . . . . . . 6205 1 100 . 1 1 16 16 LEU HD12 H 1 0.76 0.02 . 2 . . . . . . . . . 6205 1 101 . 1 1 16 16 LEU HD13 H 1 0.76 0.02 . 2 . . . . . . . . . 6205 1 102 . 1 1 16 16 LEU HD21 H 1 0.72 0.02 . 2 . . . . . . . . . 6205 1 103 . 1 1 16 16 LEU HD22 H 1 0.72 0.02 . 2 . . . . . . . . . 6205 1 104 . 1 1 16 16 LEU HD23 H 1 0.72 0.02 . 2 . . . . . . . . . 6205 1 105 . 1 1 17 17 GLU H H 1 7.96 0.02 . 1 . . . . . . . . . 6205 1 106 . 1 1 17 17 GLU HA H 1 4.24 0.02 . 1 . . . . . . . . . 6205 1 107 . 1 1 17 17 GLU HB2 H 1 2.04 0.02 . 1 . . . . . . . . . 6205 1 108 . 1 1 17 17 GLU HB3 H 1 2.04 0.02 . 1 . . . . . . . . . 6205 1 109 . 1 1 17 17 GLU HG2 H 1 2.48 0.02 . 2 . . . . . . . . . 6205 1 110 . 1 1 17 17 GLU HG3 H 1 2.26 0.02 . 2 . . . . . . . . . 6205 1 111 . 1 1 18 18 ASN H H 1 7.30 0.02 . 1 . . . . . . . . . 6205 1 112 . 1 1 18 18 ASN HA H 1 4.48 0.02 . 1 . . . . . . . . . 6205 1 113 . 1 1 18 18 ASN HB2 H 1 2.67 0.02 . 2 . . . . . . . . . 6205 1 114 . 1 1 18 18 ASN HB3 H 1 2.56 0.02 . 2 . . . . . . . . . 6205 1 115 . 1 1 18 18 ASN HD21 H 1 7.22 0.02 . 2 . . . . . . . . . 6205 1 116 . 1 1 18 18 ASN HD22 H 1 6.59 0.02 . 2 . . . . . . . . . 6205 1 117 . 1 1 19 19 TYR H H 1 7.97 0.02 . 1 . . . . . . . . . 6205 1 118 . 1 1 19 19 TYR HA H 1 4.24 0.02 . 1 . . . . . . . . . 6205 1 119 . 1 1 19 19 TYR HB2 H 1 3.48 0.02 . 2 . . . . . . . . . 6205 1 120 . 1 1 19 19 TYR HB3 H 1 2.79 0.02 . 2 . . . . . . . . . 6205 1 121 . 1 1 19 19 TYR HD1 H 1 7.32 0.02 . 1 . . . . . . . . . 6205 1 122 . 1 1 19 19 TYR HD2 H 1 7.32 0.02 . 1 . . . . . . . . . 6205 1 123 . 1 1 19 19 TYR HE1 H 1 6.80 0.02 . 1 . . . . . . . . . 6205 1 124 . 1 1 19 19 TYR HE2 H 1 6.80 0.02 . 1 . . . . . . . . . 6205 1 125 . 1 1 20 20 CYS H H 1 7.24 0.02 . 1 . . . . . . . . . 6205 1 126 . 1 1 20 20 CYS HA H 1 5.16 0.02 . 1 . . . . . . . . . 6205 1 127 . 1 1 20 20 CYS HB2 H 1 3.31 0.02 . 2 . . . . . . . . . 6205 1 128 . 1 1 20 20 CYS HB3 H 1 2.81 0.02 . 2 . . . . . . . . . 6205 1 129 . 1 1 21 21 ASN H H 1 8.03 0.02 . 1 . . . . . . . . . 6205 1 130 . 1 1 21 21 ASN HA H 1 4.49 0.02 . 1 . . . . . . . . . 6205 1 131 . 1 1 21 21 ASN HB2 H 1 2.77 0.02 . 2 . . . . . . . . . 6205 1 132 . 1 1 21 21 ASN HB3 H 1 2.64 0.02 . 2 . . . . . . . . . 6205 1 133 . 1 1 21 21 ASN HD21 H 1 7.49 0.02 . 2 . . . . . . . . . 6205 1 134 . 1 1 21 21 ASN HD22 H 1 6.80 0.02 . 2 . . . . . . . . . 6205 1 stop_ save_ save_chemical_shift_set_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_set_2 _Assigned_chem_shift_list.Entry_ID 6205 _Assigned_chem_shift_list.ID 2 _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_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 NOESY' 1 $sample_1 . 6205 2 2 '2D TOCSY' 1 $sample_1 . 6205 2 3 DQF-COSY 1 $sample_1 . 6205 2 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.Ambiguity_set_ID _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 . 2 2 1 1 PHE HA H 1 4.08 0.02 . 1 . . . . . . . . . 6205 2 2 . 2 2 1 1 PHE HB2 H 1 3.10 0.02 . 1 . . . . . . . . . 6205 2 3 . 2 2 1 1 PHE HB3 H 1 3.10 0.02 . 1 . . . . . . . . . 6205 2 4 . 2 2 1 1 PHE HD1 H 1 7.22 0.02 . 1 . . . . . . . . . 6205 2 5 . 2 2 1 1 PHE HD2 H 1 7.22 0.02 . 1 . . . . . . . . . 6205 2 6 . 2 2 1 1 PHE HE1 H 1 7.31 0.02 . 1 . . . . . . . . . 6205 2 7 . 2 2 1 1 PHE HE2 H 1 7.31 0.02 . 1 . . . . . . . . . 6205 2 8 . 2 2 2 2 VAL HA H 1 4.09 0.02 . 1 . . . . . . . . . 6205 2 9 . 2 2 2 2 VAL HB H 1 1.95 0.02 . 1 . . . . . . . . . 6205 2 10 . 2 2 2 2 VAL HG11 H 1 0.93 0.02 . 1 . . . . . . . . . 6205 2 11 . 2 2 2 2 VAL HG12 H 1 0.93 0.02 . 1 . . . . . . . . . 6205 2 12 . 2 2 2 2 VAL HG13 H 1 0.93 0.02 . 1 . . . . . . . . . 6205 2 13 . 2 2 2 2 VAL HG21 H 1 0.93 0.02 . 1 . . . . . . . . . 6205 2 14 . 2 2 2 2 VAL HG22 H 1 0.93 0.02 . 1 . . . . . . . . . 6205 2 15 . 2 2 2 2 VAL HG23 H 1 0.93 0.02 . 1 . . . . . . . . . 6205 2 16 . 2 2 3 3 ASN H H 1 8.54 0.02 . 1 . . . . . . . . . 6205 2 17 . 2 2 3 3 ASN HA H 1 4.59 0.02 . 1 . . . . . . . . . 6205 2 18 . 2 2 3 3 ASN HB2 H 1 2.81 0.02 . 2 . . . . . . . . . 6205 2 19 . 2 2 3 3 ASN HB3 H 1 2.73 0.02 . 2 . . . . . . . . . 6205 2 20 . 2 2 4 4 GLN HA H 1 4.48 0.02 . 1 . . . . . . . . . 6205 2 21 . 2 2 4 4 GLN HB2 H 1 2.08 0.02 . 2 . . . . . . . . . 6205 2 22 . 2 2 4 4 GLN HB3 H 1 1.93 0.02 . 2 . . . . . . . . . 6205 2 23 . 2 2 4 4 GLN HG2 H 1 2.20 0.02 . 2 . . . . . . . . . 6205 2 24 . 2 2 4 4 GLN HG3 H 1 2.17 0.02 . 2 . . . . . . . . . 6205 2 25 . 2 2 5 5 HIS H H 1 8.49 0.02 . 1 . . . . . . . . . 6205 2 26 . 2 2 5 5 HIS HA H 1 4.43 0.02 . 1 . . . . . . . . . 6205 2 27 . 2 2 5 5 HIS HB2 H 1 3.44 0.02 . 2 . . . . . . . . . 6205 2 28 . 2 2 5 5 HIS HB3 H 1 3.10 0.02 . 2 . . . . . . . . . 6205 2 29 . 2 2 6 6 LEU H H 1 8.96 0.02 . 1 . . . . . . . . . 6205 2 30 . 2 2 6 6 LEU HA H 1 4.61 0.02 . 1 . . . . . . . . . 6205 2 31 . 2 2 6 6 LEU HB2 H 1 1.73 0.02 . 2 . . . . . . . . . 6205 2 32 . 2 2 6 6 LEU HB3 H 1 0.82 0.02 . 2 . . . . . . . . . 6205 2 33 . 2 2 6 6 LEU HG H 1 1.62 0.02 . 2 . . . . . . . . . 6205 2 34 . 2 2 6 6 LEU HD11 H 1 0.85 0.02 . 2 . . . . . . . . . 6205 2 35 . 2 2 6 6 LEU HD12 H 1 0.85 0.02 . 2 . . . . . . . . . 6205 2 36 . 2 2 6 6 LEU HD13 H 1 0.85 0.02 . 2 . . . . . . . . . 6205 2 37 . 2 2 6 6 LEU HD21 H 1 0.74 0.02 . 2 . . . . . . . . . 6205 2 38 . 2 2 6 6 LEU HD22 H 1 0.74 0.02 . 2 . . . . . . . . . 6205 2 39 . 2 2 6 6 LEU HD23 H 1 0.74 0.02 . 2 . . . . . . . . . 6205 2 40 . 2 2 7 7 CYS H H 1 8.86 0.02 . 1 . . . . . . . . . 6205 2 41 . 2 2 7 7 CYS HA H 1 4.94 0.02 . 1 . . . . . . . . . 6205 2 42 . 2 2 7 7 CYS HB2 H 1 3.23 0.02 . 2 . . . . . . . . . 6205 2 43 . 2 2 7 7 CYS HB3 H 1 2.97 0.02 . 2 . . . . . . . . . 6205 2 44 . 2 2 8 8 GLY HA2 H 1 3.96 0.02 . 2 . . . . . . . . . 6205 2 45 . 2 2 8 8 GLY HA3 H 1 3.79 0.02 . 2 . . . . . . . . . 6205 2 46 . 2 2 9 9 SER H H 1 8.04 0.02 . 1 . . . . . . . . . 6205 2 47 . 2 2 9 9 SER HA H 1 4.21 0.02 . 1 . . . . . . . . . 6205 2 48 . 2 2 9 9 SER HB2 H 1 3.93 0.02 . 2 . . . . . . . . . 6205 2 49 . 2 2 9 9 SER HB3 H 1 4.06 0.02 . 2 . . . . . . . . . 6205 2 50 . 2 2 10 10 ASP H H 1 8.07 0.02 . 1 . . . . . . . . . 6205 2 51 . 2 2 10 10 ASP HA H 1 4.40 0.02 . 2 . . . . . . . . . 6205 2 52 . 2 2 10 10 ASP HB2 H 1 3.02 0.02 . 2 . . . . . . . . . 6205 2 53 . 2 2 10 10 ASP HB3 H 1 2.66 0.02 . 2 . . . . . . . . . 6205 2 54 . 2 2 11 11 LEU H H 1 6.96 0.02 . 1 . . . . . . . . . 6205 2 55 . 2 2 11 11 LEU HA H 1 3.93 0.02 . 1 . . . . . . . . . 6205 2 56 . 2 2 11 11 LEU HB2 H 1 1.82 0.02 . 2 . . . . . . . . . 6205 2 57 . 2 2 11 11 LEU HB3 H 1 1.16 0.02 . 2 . . . . . . . . . 6205 2 58 . 2 2 11 11 LEU HG H 1 1.25 0.02 . 1 . . . . . . . . . 6205 2 59 . 2 2 11 11 LEU HD11 H 1 0.72 0.02 . 2 . . . . . . . . . 6205 2 60 . 2 2 11 11 LEU HD12 H 1 0.72 0.02 . 2 . . . . . . . . . 6205 2 61 . 2 2 11 11 LEU HD13 H 1 0.72 0.02 . 2 . . . . . . . . . 6205 2 62 . 2 2 11 11 LEU HD21 H 1 0.64 0.02 . 2 . . . . . . . . . 6205 2 63 . 2 2 11 11 LEU HD22 H 1 0.64 0.02 . 2 . . . . . . . . . 6205 2 64 . 2 2 11 11 LEU HD23 H 1 0.64 0.02 . 2 . . . . . . . . . 6205 2 65 . 2 2 12 12 ABA H H 1 7.08 0.02 . 1 . . . . . . . . . 6205 2 66 . 2 2 12 12 ABA HA H 1 3.48 0.02 . 1 . . . . . . . . . 6205 2 67 . 2 2 12 12 ABA HB2 H 1 1.92 0.02 . 2 . . . . . . . . . 6205 2 68 . 2 2 12 12 ABA HB3 H 1 1.84 0.02 . 2 . . . . . . . . . 6205 2 69 . 2 2 12 12 ABA HG H 1 1.04 0.02 . 2 . . . . . . . . . 6205 2 70 . 2 2 13 13 GLU H H 1 7.91 0.02 . 1 . . . . . . . . . 6205 2 71 . 2 2 13 13 GLU HA H 1 4.08 0.02 . 1 . . . . . . . . . 6205 2 72 . 2 2 13 13 GLU HB2 H 1 2.32 0.02 . 2 . . . . . . . . . 6205 2 73 . 2 2 13 13 GLU HB3 H 1 2.09 0.02 . 2 . . . . . . . . . 6205 2 74 . 2 2 13 13 GLU HG2 H 1 2.47 0.02 . 1 . . . . . . . . . 6205 2 75 . 2 2 13 13 GLU HG3 H 1 2.47 0.02 . 1 . . . . . . . . . 6205 2 76 . 2 2 14 14 ALA H H 1 7.58 0.02 . 1 . . . . . . . . . 6205 2 77 . 2 2 14 14 ALA HA H 1 4.07 0.02 . 1 . . . . . . . . . 6205 2 78 . 2 2 14 14 ALA HB1 H 1 1.38 0.02 . 1 . . . . . . . . . 6205 2 79 . 2 2 14 14 ALA HB2 H 1 1.38 0.02 . 1 . . . . . . . . . 6205 2 80 . 2 2 14 14 ALA HB3 H 1 1.38 0.02 . 1 . . . . . . . . . 6205 2 81 . 2 2 15 15 LEU H H 1 8.05 0.02 . 2 . . . . . . . . . 6205 2 82 . 2 2 15 15 LEU HA H 1 3.69 0.02 . 1 . . . . . . . . . 6205 2 83 . 2 2 15 15 LEU HB2 H 1 0.88 0.02 . 2 . . . . . . . . . 6205 2 84 . 2 2 15 15 LEU HB3 H 1 1.25 0.02 . 2 . . . . . . . . . 6205 2 85 . 2 2 15 15 LEU HG H 1 1.24 0.02 . 1 . . . . . . . . . 6205 2 86 . 2 2 15 15 LEU HD11 H 1 0.54 0.02 . 2 . . . . . . . . . 6205 2 87 . 2 2 15 15 LEU HD12 H 1 0.54 0.02 . 2 . . . . . . . . . 6205 2 88 . 2 2 15 15 LEU HD13 H 1 0.54 0.02 . 2 . . . . . . . . . 6205 2 89 . 2 2 15 15 LEU HD21 H 1 0.18 0.02 . 2 . . . . . . . . . 6205 2 90 . 2 2 15 15 LEU HD22 H 1 0.18 0.02 . 2 . . . . . . . . . 6205 2 91 . 2 2 15 15 LEU HD23 H 1 0.18 0.02 . 2 . . . . . . . . . 6205 2 92 . 2 2 16 16 TYR H H 1 8.03 0.02 . 1 . . . . . . . . . 6205 2 93 . 2 2 16 16 TYR HA H 1 4.39 0.02 . 1 . . . . . . . . . 6205 2 94 . 2 2 16 16 TYR HB2 H 1 3.20 0.02 . 2 . . . . . . . . . 6205 2 95 . 2 2 16 16 TYR HB3 H 1 3.17 0.02 . 2 . . . . . . . . . 6205 2 96 . 2 2 16 16 TYR HD1 H 1 7.26 0.02 . 1 . . . . . . . . . 6205 2 97 . 2 2 16 16 TYR HD2 H 1 7.26 0.02 . 1 . . . . . . . . . 6205 2 98 . 2 2 16 16 TYR HE1 H 1 6.85 0.02 . 1 . . . . . . . . . 6205 2 99 . 2 2 16 16 TYR HE2 H 1 6.85 0.02 . 1 . . . . . . . . . 6205 2 100 . 2 2 17 17 LEU H H 1 7.77 0.02 . 1 . . . . . . . . . 6205 2 101 . 2 2 17 17 LEU HA H 1 4.04 0.02 . 1 . . . . . . . . . 6205 2 102 . 2 2 17 17 LEU HB2 H 1 1.80 0.02 . 2 . . . . . . . . . 6205 2 103 . 2 2 17 17 LEU HB3 H 1 1.93 0.02 . 2 . . . . . . . . . 6205 2 104 . 2 2 17 17 LEU HG H 1 1.92 0.02 . 2 . . . . . . . . . 6205 2 105 . 2 2 17 17 LEU HD11 H 1 0.94 0.02 . 1 . . . . . . . . . 6205 2 106 . 2 2 17 17 LEU HD12 H 1 0.94 0.02 . 1 . . . . . . . . . 6205 2 107 . 2 2 17 17 LEU HD13 H 1 0.94 0.02 . 1 . . . . . . . . . 6205 2 108 . 2 2 17 17 LEU HD21 H 1 0.94 0.02 . 1 . . . . . . . . . 6205 2 109 . 2 2 17 17 LEU HD22 H 1 0.94 0.02 . 1 . . . . . . . . . 6205 2 110 . 2 2 17 17 LEU HD23 H 1 0.94 0.02 . 1 . . . . . . . . . 6205 2 111 . 2 2 18 18 VAL H H 1 8.33 0.02 . 1 . . . . . . . . . 6205 2 112 . 2 2 18 18 VAL HA H 1 3.73 0.02 . 1 . . . . . . . . . 6205 2 113 . 2 2 18 18 VAL HB H 1 1.97 0.02 . 1 . . . . . . . . . 6205 2 114 . 2 2 18 18 VAL HG11 H 1 0.99 0.02 . 2 . . . . . . . . . 6205 2 115 . 2 2 18 18 VAL HG12 H 1 0.99 0.02 . 2 . . . . . . . . . 6205 2 116 . 2 2 18 18 VAL HG13 H 1 0.99 0.02 . 2 . . . . . . . . . 6205 2 117 . 2 2 18 18 VAL HG21 H 1 0.83 0.02 . 2 . . . . . . . . . 6205 2 118 . 2 2 18 18 VAL HG22 H 1 0.83 0.02 . 2 . . . . . . . . . 6205 2 119 . 2 2 18 18 VAL HG23 H 1 0.83 0.02 . 2 . . . . . . . . . 6205 2 120 . 2 2 19 19 CYS H H 1 8.76 0.02 . 1 . . . . . . . . . 6205 2 121 . 2 2 19 19 CYS HA H 1 4.81 0.02 . 1 . . . . . . . . . 6205 2 122 . 2 2 19 19 CYS HB2 H 1 3.28 0.02 . 2 . . . . . . . . . 6205 2 123 . 2 2 19 19 CYS HB3 H 1 2.88 0.02 . 2 . . . . . . . . . 6205 2 124 . 2 2 20 20 GLY H H 1 7.81 0.02 . 1 . . . . . . . . . 6205 2 125 . 2 2 20 20 GLY HA2 H 1 3.96 0.02 . 2 . . . . . . . . . 6205 2 126 . 2 2 20 20 GLY HA3 H 1 3.79 0.02 . 2 . . . . . . . . . 6205 2 127 . 2 2 21 21 GLU H H 1 9.09 0.02 . 1 . . . . . . . . . 6205 2 128 . 2 2 21 21 GLU HA H 1 4.18 0.02 . 1 . . . . . . . . . 6205 2 129 . 2 2 21 21 GLU HB2 H 1 2.21 0.02 . 2 . . . . . . . . . 6205 2 130 . 2 2 21 21 GLU HB3 H 1 2.05 0.02 . 2 . . . . . . . . . 6205 2 131 . 2 2 21 21 GLU HG2 H 1 2.38 0.02 . 1 . . . . . . . . . 6205 2 132 . 2 2 21 21 GLU HG3 H 1 2.38 0.02 . 1 . . . . . . . . . 6205 2 133 . 2 2 22 22 ARG H H 1 8.08 0.02 . 1 . . . . . . . . . 6205 2 134 . 2 2 22 22 ARG HA H 1 4.16 0.02 . 1 . . . . . . . . . 6205 2 135 . 2 2 22 22 ARG HB2 H 1 2.17 0.02 . 2 . . . . . . . . . 6205 2 136 . 2 2 22 22 ARG HB3 H 1 2.08 0.02 . 2 . . . . . . . . . 6205 2 137 . 2 2 22 22 ARG HG2 H 1 1.88 0.02 . 2 . . . . . . . . . 6205 2 138 . 2 2 22 22 ARG HG3 H 1 1.85 0.02 . 2 . . . . . . . . . 6205 2 139 . 2 2 22 22 ARG HD2 H 1 3.31 0.02 . 1 . . . . . . . . . 6205 2 140 . 2 2 22 22 ARG HD3 H 1 3.31 0.02 . 1 . . . . . . . . . 6205 2 141 . 2 2 23 23 GLY H H 1 7.33 0.02 . 1 . . . . . . . . . 6205 2 142 . 2 2 23 23 GLY HA2 H 1 4.14 0.02 . 2 . . . . . . . . . 6205 2 143 . 2 2 23 23 GLY HA3 H 1 3.82 0.02 . 2 . . . . . . . . . 6205 2 144 . 2 2 24 24 PHE H H 1 7.62 0.02 . 1 . . . . . . . . . 6205 2 145 . 2 2 24 24 PHE HA H 1 5.28 0.02 . 1 . . . . . . . . . 6205 2 146 . 2 2 24 24 PHE HB2 H 1 3.21 0.02 . 2 . . . . . . . . . 6205 2 147 . 2 2 24 24 PHE HB3 H 1 2.90 0.02 . 2 . . . . . . . . . 6205 2 148 . 2 2 24 24 PHE HD1 H 1 6.71 0.02 . 1 . . . . . . . . . 6205 2 149 . 2 2 24 24 PHE HD2 H 1 6.71 0.02 . 1 . . . . . . . . . 6205 2 150 . 2 2 24 24 PHE HE1 H 1 6.92 0.02 . 1 . . . . . . . . . 6205 2 151 . 2 2 24 24 PHE HE2 H 1 6.92 0.02 . 1 . . . . . . . . . 6205 2 152 . 2 2 24 24 PHE HZ H 1 7.04 0.02 . 1 . . . . . . . . . 6205 2 153 . 2 2 25 25 PHE H H 1 8.56 0.02 . 1 . . . . . . . . . 6205 2 154 . 2 2 25 25 PHE HA H 1 4.87 0.02 . 1 . . . . . . . . . 6205 2 155 . 2 2 25 25 PHE HB2 H 1 3.21 0.02 . 2 . . . . . . . . . 6205 2 156 . 2 2 25 25 PHE HB3 H 1 3.23 0.02 . 2 . . . . . . . . . 6205 2 157 . 2 2 25 25 PHE HD1 H 1 7.22 0.02 . 1 . . . . . . . . . 6205 2 158 . 2 2 25 25 PHE HD2 H 1 7.22 0.02 . 1 . . . . . . . . . 6205 2 159 . 2 2 25 25 PHE HE1 H 1 7.36 0.02 . 1 . . . . . . . . . 6205 2 160 . 2 2 25 25 PHE HE2 H 1 7.36 0.02 . 1 . . . . . . . . . 6205 2 161 . 2 2 26 26 TYR H H 1 8.21 0.02 . 1 . . . . . . . . . 6205 2 162 . 2 2 26 26 TYR HA H 1 4.68 0.02 . 1 . . . . . . . . . 6205 2 163 . 2 2 26 26 TYR HB2 H 1 2.99 0.02 . 2 . . . . . . . . . 6205 2 164 . 2 2 26 26 TYR HB3 H 1 2.97 0.02 . 2 . . . . . . . . . 6205 2 165 . 2 2 26 26 TYR HD1 H 1 6.98 0.02 . 1 . . . . . . . . . 6205 2 166 . 2 2 26 26 TYR HD2 H 1 6.98 0.02 . 1 . . . . . . . . . 6205 2 167 . 2 2 26 26 TYR HE1 H 1 6.68 0.02 . 1 . . . . . . . . . 6205 2 168 . 2 2 26 26 TYR HE2 H 1 6.68 0.02 . 1 . . . . . . . . . 6205 2 169 . 2 2 27 27 THR H H 1 7.77 0.02 . 1 . . . . . . . . . 6205 2 170 . 2 2 27 27 THR HA H 1 4.46 0.02 . 1 . . . . . . . . . 6205 2 171 . 2 2 27 27 THR HB H 1 4.11 0.02 . 2 . . . . . . . . . 6205 2 172 . 2 2 27 27 THR HG21 H 1 1.20 0.02 . 1 . . . . . . . . . 6205 2 173 . 2 2 27 27 THR HG22 H 1 1.20 0.02 . 1 . . . . . . . . . 6205 2 174 . 2 2 27 27 THR HG23 H 1 1.20 0.02 . 1 . . . . . . . . . 6205 2 175 . 2 2 28 28 LYS H H 1 8.40 0.02 . 1 . . . . . . . . . 6205 2 176 . 2 2 28 28 LYS HA H 1 4.37 0.02 . 1 . . . . . . . . . 6205 2 177 . 2 2 28 28 LYS HB2 H 1 1.72 0.02 . 2 . . . . . . . . . 6205 2 178 . 2 2 28 28 LYS HB3 H 1 1.79 0.02 . 2 . . . . . . . . . 6205 2 179 . 2 2 28 28 LYS HG2 H 1 1.42 0.02 . 1 . . . . . . . . . 6205 2 180 . 2 2 28 28 LYS HG3 H 1 1.42 0.02 . 1 . . . . . . . . . 6205 2 181 . 2 2 28 28 LYS HE2 H 1 2.92 0.02 . 1 . . . . . . . . . 6205 2 182 . 2 2 28 28 LYS HE3 H 1 2.92 0.02 . 1 . . . . . . . . . 6205 2 183 . 2 2 29 29 PRO HA H 1 4.45 0.02 . 1 . . . . . . . . . 6205 2 184 . 2 2 29 29 PRO HB2 H 1 2.29 0.02 . 2 . . . . . . . . . 6205 2 185 . 2 2 29 29 PRO HB3 H 1 2.04 0.02 . 2 . . . . . . . . . 6205 2 186 . 2 2 29 29 PRO HG2 H 1 1.96 0.02 . 1 . . . . . . . . . 6205 2 187 . 2 2 29 29 PRO HG3 H 1 1.96 0.02 . 1 . . . . . . . . . 6205 2 188 . 2 2 30 30 THR H H 1 7.80 0.02 . 1 . . . . . . . . . 6205 2 189 . 2 2 30 30 THR HA H 1 4.13 0.02 . 1 . . . . . . . . . 6205 2 190 . 2 2 30 30 THR HB H 1 4.24 0.02 . 1 . . . . . . . . . 6205 2 191 . 2 2 30 30 THR HG21 H 1 1.20 0.02 . 1 . . . . . . . . . 6205 2 192 . 2 2 30 30 THR HG22 H 1 1.20 0.02 . 1 . . . . . . . . . 6205 2 193 . 2 2 30 30 THR HG23 H 1 1.20 0.02 . 1 . . . . . . . . . 6205 2 stop_ save_