data_4997 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4997 _Entry.Title ; 1H, 13C Chemical Shift Assignment of PT-insulin in H2O and 35% TFE ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-04-23 _Entry.Accession_date 2001-04-23 _Entry.Last_release_date 2001-04-23 _Entry.Original_release_date 2001-04-23 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 2.1 _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 Danielle Keller . . . . 4997 2 R. Clausen . . . . 4997 3 Knud Josefsen . . . . 4997 4 Jens Led . J. . . 4997 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 4 4997 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 109 4997 '1H chemical shifts' 546 4997 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2001-05-21 . original BMRB . 4997 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4997 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21415430 _Citation.DOI . _Citation.PubMed_ID 11524020 _Citation.Full_citation . _Citation.Title ; Flexibility and Bioactivity of Insulin: an NMR Investigation of the Solution Structure and Folding of an Unusually Flexible Human Insulin Mutant with Increased Biological Activity ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 40 _Citation.Journal_issue 35 _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 10732 _Citation.Page_last 10740 _Citation.Year 2001 _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 Danielle Keller . . . . 4997 1 2 R. Clausen . . . . 4997 1 3 Knud Josefsen . . . . 4997 1 4 Jens Led . J. . . 4997 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID Insulin 4997 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_PT-insulin _Assembly.Sf_category assembly _Assembly.Sf_framecode system_PT-insulin _Assembly.Entry_ID 4997 _Assembly.ID 1 _Assembly.Name [Thr(B27)->Pro,Pro(B28)->Thr]-insulin _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 4997 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 'PT-insulin A chain' 1 $PT-insulin_A_chain . . . native . . . . . 4997 1 2 'PT-insulin B chain' 2 $PT-insulin_B_chain . . . native . . . . . 4997 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 20 20 SG . 2 . 2 CYS 19 19 SG . . . . . . . . . . . . 4997 1 2 disulfide single . 1 . 1 CYS 6 6 SG . 1 . 1 CYS 11 11 SG . . . . . . . . . . . . 4997 1 3 disulfide single . 1 . 1 CYS 7 7 SG . 2 . 2 CYS 7 7 SG . . . . . . . . . . . . 4997 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID PT-insulin abbreviation 4997 1 [Thr(B27)->Pro,Pro(B28)->Thr]-insulin system 4997 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'Peptide hormone' 4997 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_PT-insulin_A_chain _Entity.Sf_category entity _Entity.Sf_framecode PT-insulin_A_chain _Entity.Entry_ID 4997 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Insulin _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 2008-08-19 _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 . no BMRB 1000 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1002 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1004 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1006 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1008 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1010 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1012 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1014 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1016 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1018 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1020 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1022 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1023 . 'insulin B chain' . . . . . 95.24 42 100.00 100.00 1.97e-02 . . . . 4997 1 . no BMRB 11016 . 'Chain A' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1344 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 15464 . entity_1 . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1585 . 'insulin A chain' . . . . . 95.24 20 100.00 100.00 2.46e-02 . . . . 4997 1 . no BMRB 1587 . 'insulin A chain' . . . . . 95.24 20 100.00 100.00 2.46e-02 . . . . 4997 1 . no BMRB 1632 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 1761 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 4266 . [D-AlaB26]destetra(B27-B30)insulin-B26-amide . . . . . 100.00 47 100.00 100.00 3.04e-03 . . . . 4997 1 . no BMRB 554 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 556 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 6203 . 'ThrB12-DKP-insulin, chain A' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 6204 . 'AlaB12-DKP-insulin, chain A' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 6205 . 'AbaB12-DKP-insulin, chain A' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 936 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 994 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 996 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no BMRB 998 . 'insulin A chain' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1A7F . 'Insulin Mutant B16 Glu, B24 Gly, Des-B30, Nmr, 20 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1AI0 . 'R6 Human Insulin Hexamer (Non-Symmetric), Nmr, 10 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1AIY . 'R6 Human Insulin Hexamer (Symmetric), Nmr, 10 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1B17 . 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 5.00 Coordinates)' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1B18 . 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 5.53 Coordinates)' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1B19 . 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 5.80 Coordinates)' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1B2A . 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.00 Coordinates)' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1B2B . 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.16 Coordinates)' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1B2C . 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.26 Coordinates)' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1B2D . 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.35 Coordinates)' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1B2E . 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.50 Coordinates)' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1B2F . 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.98 Coordinates)' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1B2G . 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 9.00 Coordinates)' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1B9E . 'Human Insulin Mutant Serb9glu' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1BEN . 'Insulin Complexed With 4-Hydroxybenzamide' . . . . . 95.24 21 100.00 100.00 2.46e-02 . . . . 4997 1 . no PDB 1BZV . '[d-Alab26]-Des(B27-B30)-Insulin-B26-Amide A Superpotent Single-Replacement Insulin Analogue, Nmr, Minimized Average Structure' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1DEI . 'Desheptapeptide (B24-B30) Insulin' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1EFE . 'An Active Mini-Proinsulin, M2pi' . . . . . 100.00 60 100.00 100.00 2.27e-03 . . . . 4997 1 . no PDB 1EV3 . 'Structure Of The Rhombohedral Form Of The M-CresolINSULIN R6 Hexamer' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1EV6 . 'Structure Of The Monoclinic Form Of The M-CresolINSULIN R6 Hexamer' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1EVR . 'The Structure Of The ResorcinolINSULIN R6 HEXAMER' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1FU2 . 'First Protein Structure Determined From X-Ray Powder Diffraction Data' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1FUB . 'First Protein Structure Determined From X-Ray Powder Diffraction Data' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1G7A . '1.2 A Structure Of T3r3 Human Insulin At 100 K' . . . . . 95.24 21 100.00 100.00 2.46e-02 . . . . 4997 1 . no PDB 1GUJ . 'Insulin At Ph 2: Structural Analysis Of The Conditions Promoting Insulin Fibre Formation.' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1HIQ . 'Paradoxical Structure And Function In A Mutant Human Insulin Associated With Diabetes Mellitus' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1HIS . 'Structure And Dynamics Of Des-Pentapeptide-Insulin In Solution: The Molten-Globule Hypothesis' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1HIT . 'Receptor Binding Redefined By A Structural Switch In A Mutant Human Insulin' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1HLS . 'Nmr Structure Of The Human Insulin-His(B16)' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1HTV . 'Crystal Structure Of Destripeptide (B28-B30) Insulin' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1HUI . 'Insulin Mutant (B1, B10, B16, B27)glu, Des-B30, Nmr, 25 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1IZA . 'Role Of B13 Glu In Insulin Assembly: The Hexamer Structure Of Recombinant Mutant (B13 Glu-> Gln) Insulin' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1IZB . 'Role Of B13 Glu In Insulin Assembly: The Hexamer Structure Of Recombinant Mutant (B13 Glu-> Gln) Insulin' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1JCO . 'Solution Structure Of The Monomeric [thr(B27)->pro,Pro(B28)- >thr] Insulin Mutant (Pt Insulin)' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1LPH . 'Lys(B28)pro(B29)-Human Insulin' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1M5A . 'Crystal Structure Of 2-Co(2+)-Insulin At 1.2a Resolution' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1MHJ . ; Solution Structure Of The Superactive Monomeric Des- [phe(B25)] Human Insulin Mutant. Elucidation Of The Structural Basis For The Monomerization Of The Des- [phe(B25)] Insulin And The Dimerization Of Native Insulin ; . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1MPJ . ; X-Ray Crystallographic Studies On Hexameric Insulins In The Presence Of Helix-Stabilizing Agents, Thiocyanate, Methylparaben And Phenol ; . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1OS3 . 'Dehydrated T6 Human Insulin At 100 K' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1OS4 . 'Dehydrated T6 Human Insulin At 295 K' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1QIY . 'Human Insulin Hexamers With Chain B His Mutated To Tyr Complexed With Phenol' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1QIZ . 'Human Insulin Hexamers With Chain B His Mutated To Tyr Complexed With Resorcinol' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1QJ0 . 'Human Insulin Hexamers With Chain B His Mutated To Tyr' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1SDB . 'Porcine Desb1-2 Despentapeptide(B26-B30) Insulin' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1SF1 . 'Nmr Structure Of Human Insulin Under Amyloidogenic Condition, 15 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1SJT . 'Mini-Proinsulin, Two Chain Insulin Analog Mutant: Des B30, His(B 10)asp, Pro(B 28)asp, Nmr, 20 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1SJU . ; Mini-Proinsulin, Single Chain Insulin Analog Mutant: Des B30, His(B 10)asp, Pro(B 28)asp And Peptide Bond Between Lys B 29 And Gly A 1, Nmr, 20 Structures ; . . . . . 100.00 50 100.00 100.00 3.11e-03 . . . . 4997 1 . no PDB 1T1K . 'Nmr Structure Of Human Insulin Mutant His-B10-Asp, Val-B12- Ala, Pro-B28-Lys, Lys-B29-Pro, 15 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1T1P . 'Nmr Structure Of Human Insulin Mutant His-B10-Asp, Val-B12- Thr, Pro-B28-Lys, Lys-B29-Pro, 15 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1T1Q . 'Nmr Structure Of Human Insulin Mutant His-B10-Asp, Val-B12- Aba, Pro-B28-Lys, Lys-B29-Pro, 15 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1TRZ . 'Crystallographic Evidence For Dual Coordination Around Zinc In The T3r3 Human Insulin Hexamer' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1TYL . "The Structure Of A Complex Of Hexameric Insulin And 4'- Hydroxyacetanilide" . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1TYM . "The Structure Of A Complex Of Hexameric Insulin And 4'- Hydroxyacetanilide" . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1UZ9 . 'Crystallographic And Solution Studies Of N-Lithocholyl Insulin: A New Generation Of Prolonged-Acting Insulins.' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1W8P . 'Structural Properties Of The B25tyr-Nme-B26phe Insulin Mutant.' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1WAV . 'Crystal Structure Of Form B Monoclinic Crystal Of Insulin' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1XDA . 'Structure Of Insulin' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1XGL . 'Human Insulin Disulfide Isomer, Nmr, 10 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1ZEG . 'Structure Of B28 Asp Insulin In Complex With Phenol' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1ZEH . 'Structure Of Insulin' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1ZEI . 'Cross-Linked B28 Asp Insulin' . . . . . 100.00 53 100.00 100.00 2.36e-03 . . . . 4997 1 . no PDB 1ZNI . Insulin . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 1ZNJ . 'Insulin, Monoclinic Crystal Form' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2AIY . 'R6 Human Insulin Hexamer (Symmetric), Nmr, 20 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2C8Q . 'Insuline(1sec) And Uv Laser Excited Fluorescence' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2C8R . 'Insuline(60sec) And Uv Laser Excited Fluorescence' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2CEU . 'Despentapeptide Insulin In Acetic Acid (Ph 2)' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2G4M . 'Insulin Collected At 2.0 A Wavelength' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2H67 . 'Nmr Structure Of Human Insulin Mutant His-B5-Ala, His-B10- Asp Pro-B28-Lys, Lys-B29-Pro, 20 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2HH4 . 'Nmr Structure Of Human Insulin Mutant Gly-B8-D-Ser, His-B10- Asp Pro-B28-Lys, Lys-B29-Pro, 20 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2HHO . 'Nmr Structure Of Human Insulin Mutant Gly-B8-Ser, His-B10- Asp Pro-B28-Lys, Lys-B29-Pro, 20 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2HIU . 'Nmr Structure Of Human Insulin In 20% Acetic Acid, Zinc- Free, 10 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2JMN . 'Nmr Structure Of Human Insulin Mutant His-B10-Asp, Pro-B28- Lys, Lys-B29-Pro, 20 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2JV1 . 'Nmr Structure Of Human Insulin Monomer In 35% Cd3cn Zinc Free, 50 Structures' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2OLY . 'Structure Of Human Insulin In Presence Of Urea At Ph 7.0' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2OLZ . 'Structure Of Human Insulin In Presence Of Thiocyanate At Ph 7.0' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2OM0 . 'Structure Of Human Insulin In Presence Of Urea At Ph 6.5' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2OM1 . 'Structure Of Human Insulin In Presence Of Thiocyanate At Ph 6.5' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2OMG . 'Structure Of Human Insulin Cocrystallized With Protamine And Urea' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2OMH . 'Structure Of Human Insulin Cocrystallized With Arg-12 Peptide In Presence Of Urea' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2OMI . 'Structure Of Human Insulin Cocrystallized With Protamine' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 2QIU . 'Structure Of Human Arg-Insulin' . . . . . 100.00 22 100.00 100.00 4.10e-03 . . . . 4997 1 . no PDB 2TCI . ; X-Ray Crystallographic Studies On Hexameric Insulins In The Presence Of Helix-Stabilizing Agents, Thiocyanate, Methylparaben And Phenol ; . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 3AIY . 'R6 Human Insulin Hexamer (Symmetric), Nmr, Refined Average Structure' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 3BXQ . 'The Structure Of A Mutant Insulin Uncouples Receptor Binding From Protein Allostery. An Electrostatic Block To The Tr Transition' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 3MTH . ; X-Ray Crystallographic Studies On Hexameric Insulins In The Presence Of Helix-Stabilizing Agents, Thiocyanate, Methylparaben And Phenol ; . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 4AIY . "R6 Human Insulin Hexamer (Symmetric), Nmr, 'green' Substate, Average Structure" . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 4INS . 'The Structure Of 2zn Pig Insulin Crystals At 1.5 Angstroms Resolution' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 5AIY . "R6 Human Insulin Hexamer (Symmetric), Nmr, 'red' Substate, Average Structure" . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 6INS . 'X-Ray Analysis Of The Single Chain B29-A1 Peptide-Linked Insulin Molecule. A Completely Inactive Analogue' . . . . . 100.00 50 100.00 100.00 3.11e-03 . . . . 4997 1 . no PDB 7INS . 'Structure Of Porcine Insulin Cocrystallized With Clupeine Z' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PDB 9INS . 'Monovalent Cation Binding In Cubic Insulin Crystals' . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no EMBL CAA23424 . 'unnamed protein product [synthetic construct]' . . . . . 100.00 87 100.00 100.00 1.29e-03 . . . . 4997 1 . no EMBL CAA23475 . 'preproinsulin [Canis sp.]' . . . . . 100.00 110 100.00 100.00 8.40e-04 . . . . 4997 1 . no EMBL CAA23828 . 'preproinsulin [Homo sapiens]' . . . . . 100.00 110 100.00 100.00 1.16e-03 . . . . 4997 1 . no EMBL CAA43403 . 'Preproinsulin [Pan troglodytes]' . . . . . 100.00 110 100.00 100.00 7.79e-04 . . . . 4997 1 . no EMBL CAA43405 . 'Preproinsulin [Chlorocebus aethiops]' . . . . . 100.00 110 100.00 100.00 8.40e-04 . . . . 4997 1 . no GenBank AAA17540 . insulin . . . . . 100.00 55 100.00 100.00 1.35e-03 . . . . 4997 1 . no GenBank AAA19033 . insulin . . . . . 100.00 110 100.00 100.00 8.33e-04 . . . . 4997 1 . no GenBank AAA36849 . preproinsulin . . . . . 100.00 110 100.00 100.00 7.99e-04 . . . . 4997 1 . no GenBank AAA59172 . 'insulin [Homo sapiens]' . . . . . 100.00 110 100.00 100.00 1.16e-03 . . . . 4997 1 . no GenBank AAA59173 . 'insulin [Homo sapiens]' . . . . . 100.00 110 100.00 100.00 1.16e-03 . . . . 4997 1 . no PRF 0601246A . insulin,prepro . . . . . 100.00 110 100.00 100.00 1.16e-03 . . . . 4997 1 . no PRF 1006230A . insulin,pro- . . . . . 100.00 86 100.00 100.00 1.29e-03 . . . . 4997 1 . no PRF 550086A . insulin . . . . . 100.00 51 100.00 100.00 2.86e-03 . . . . 4997 1 . no PRF 560164B . insulin . . . . . 100.00 21 100.00 100.00 4.53e-03 . . . . 4997 1 . no PRF 580107B . insulin . . . . . 100.00 50 100.00 100.00 2.77e-03 . . . . 4997 1 . no REF NP_000198 . 'proinsulin precursor [Homo sapiens]' . . . . . 100.00 110 100.00 100.00 1.16e-03 . . . . 4997 1 . no REF NP_001008996 . 'proinsulin precursor [Pan troglodytes]' . . . . . 100.00 110 100.00 100.00 7.79e-04 . . . . 4997 1 . no REF NP_001075804 . 'insulin [Oryctolagus cuniculus]' . . . . . 100.00 110 100.00 100.00 8.33e-04 . . . . 4997 1 . no REF NP_001103242 . 'insulin [Sus scrofa]' . . . . . 100.00 108 100.00 100.00 1.13e-03 . . . . 4997 1 . no REF NP_001123565 . 'proinsulin [Canis lupus familiaris]' . . . . . 100.00 110 100.00 100.00 8.40e-04 . . . . 4997 1 . no SWISS-PROT P01308 . 'Insulin precursor [Contains: Insulin B chain; Insulin A chain]' . . . . . 100.00 110 100.00 100.00 1.16e-03 . . . . 4997 1 . no SWISS-PROT P01311 . 'Insulin precursor [Contains: Insulin B chain; Insulin A chain]' . . . . . 100.00 110 100.00 100.00 8.33e-04 . . . . 4997 1 . no SWISS-PROT P01315 . 'Insulin precursor [Contains: Insulin B chain; Insulin A chain]' . . . . . 100.00 108 100.00 100.00 1.13e-03 . . . . 4997 1 . no SWISS-PROT P01321 . 'Insulin precursor [Contains: Insulin B chain; Insulin A chain]' . . . . . 100.00 110 100.00 100.00 8.40e-04 . . . . 4997 1 . no SWISS-PROT P30406 . 'Insulin precursor [Contains: Insulin B chain; Insulin A chain]' . . . . . 100.00 110 100.00 100.00 7.99e-04 . . . . 4997 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID Insulin abbreviation 4997 1 Insulin common 4997 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 1 GLY . 4997 1 2 2 ILE . 4997 1 3 3 VAL . 4997 1 4 4 GLU . 4997 1 5 5 GLN . 4997 1 6 6 CYS . 4997 1 7 7 CYS . 4997 1 8 8 THR . 4997 1 9 9 SER . 4997 1 10 10 ILE . 4997 1 11 11 CYS . 4997 1 12 12 SER . 4997 1 13 13 LEU . 4997 1 14 14 TYR . 4997 1 15 15 GLN . 4997 1 16 16 LEU . 4997 1 17 17 GLU . 4997 1 18 18 ASN . 4997 1 19 19 TYR . 4997 1 20 20 CYS . 4997 1 21 21 ASN . 4997 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 4997 1 . ILE 2 2 4997 1 . VAL 3 3 4997 1 . GLU 4 4 4997 1 . GLN 5 5 4997 1 . CYS 6 6 4997 1 . CYS 7 7 4997 1 . THR 8 8 4997 1 . SER 9 9 4997 1 . ILE 10 10 4997 1 . CYS 11 11 4997 1 . SER 12 12 4997 1 . LEU 13 13 4997 1 . TYR 14 14 4997 1 . GLN 15 15 4997 1 . LEU 16 16 4997 1 . GLU 17 17 4997 1 . ASN 18 18 4997 1 . TYR 19 19 4997 1 . CYS 20 20 4997 1 . ASN 21 21 4997 1 stop_ save_ save_PT-insulin_B_chain _Entity.Sf_category entity _Entity.Sf_framecode PT-insulin_B_chain _Entity.Entry_ID 4997 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name Insulin _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 ; FVNQHLCGSHLVEALYLVCG ERGFFYPTKT ; _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 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 . _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 . no PDB 1JCO . 'Solution Structure Of The Monomeric [thr(B27)->pro,Pro(B28)- >thr] Insulin Mutant (Pt Insulin)' . . . . . 100.00 30 100.00 100.00 2.23e-09 . . . . 4997 2 . no PRF 640291A . insulin . . . . . 86.67 51 100.00 100.00 8.54e-07 . . . . 4997 2 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID Insulin abbreviation 4997 2 Insulin common 4997 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 22 PHE . 4997 2 2 23 VAL . 4997 2 3 24 ASN . 4997 2 4 25 GLN . 4997 2 5 26 HIS . 4997 2 6 27 LEU . 4997 2 7 28 CYS . 4997 2 8 29 GLY . 4997 2 9 30 SER . 4997 2 10 31 HIS . 4997 2 11 32 LEU . 4997 2 12 33 VAL . 4997 2 13 34 GLU . 4997 2 14 35 ALA . 4997 2 15 36 LEU . 4997 2 16 37 TYR . 4997 2 17 38 LEU . 4997 2 18 39 VAL . 4997 2 19 40 CYS . 4997 2 20 41 GLY . 4997 2 21 42 GLU . 4997 2 22 43 ARG . 4997 2 23 44 GLY . 4997 2 24 45 PHE . 4997 2 25 46 PHE . 4997 2 26 47 TYR . 4997 2 27 48 PRO . 4997 2 28 49 THR . 4997 2 29 50 LYS . 4997 2 30 51 THR . 4997 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 4997 2 . VAL 2 2 4997 2 . ASN 3 3 4997 2 . GLN 4 4 4997 2 . HIS 5 5 4997 2 . LEU 6 6 4997 2 . CYS 7 7 4997 2 . GLY 8 8 4997 2 . SER 9 9 4997 2 . HIS 10 10 4997 2 . LEU 11 11 4997 2 . VAL 12 12 4997 2 . GLU 13 13 4997 2 . ALA 14 14 4997 2 . LEU 15 15 4997 2 . TYR 16 16 4997 2 . LEU 17 17 4997 2 . VAL 18 18 4997 2 . CYS 19 19 4997 2 . GLY 20 20 4997 2 . GLU 21 21 4997 2 . ARG 22 22 4997 2 . GLY 23 23 4997 2 . PHE 24 24 4997 2 . PHE 25 25 4997 2 . TYR 26 26 4997 2 . PRO 27 27 4997 2 . THR 28 28 4997 2 . LYS 29 29 4997 2 . THR 30 30 4997 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 4997 _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 $PT-insulin_A_chain . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . pancreas . . . 4997 1 2 2 $PT-insulin_B_chain . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . pancreas . . . 4997 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 4997 _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 $PT-insulin_A_chain . 'recombinant technology' 'Pichia pastoris' 'Pichia pastoris' . . Pichia pastoris . . . plasmid . . pPIC9 . . . 4997 1 2 2 $PT-insulin_B_chain . 'recombinant technology' 'Pichia pastoris' 'Pichia pastoris' . . Pichia pastoris . . . plasmid . . pPIC9 . . . 4997 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4997 _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 Insulin . . . 1 $PT-insulin_A_chain . . 2.8 . . mM . . . . 4997 1 2 Insulin . . . 2 $PT-insulin_B_chain . . 2.8 . . mM . . . . 4997 1 3 H2O . . . . . . . 90 . . % . . . . 4997 1 4 D2O . . . . . . . 10 . . % . . . . 4997 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 4997 _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 Insulin . . . 1 $PT-insulin_A_chain . . 2.8 . . mM . . . . 4997 2 2 Insulin . . . 2 $PT-insulin_B_chain . . 2.8 . . mM . . . . 4997 2 3 H2O . . . . . . . 65 . . % . . . . 4997 2 4 TFE . . . . . . . 35 . . % . . . . 4997 2 stop_ save_ ####################### # Sample conditions # ####################### save_cond_H2O _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond_H2O _Sample_condition_list.Entry_ID 4997 _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 3.13 0.1 n/a 4997 1 temperature 298 0.1 K 4997 1 stop_ save_ save_cond_TFE _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond_TFE _Sample_condition_list.Entry_ID 4997 _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 3.23 0.1 n/a 4997 2 temperature 298 0.1 K 4997 2 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 4997 _Software.ID 1 _Software.Type . _Software.Name NMRPipe _Software.Version . _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Fourier Transformation' 4997 1 stop_ save_ save_XEASY _Software.Sf_category software _Software.Sf_framecode XEASY _Software.Entry_ID 4997 _Software.ID 2 _Software.Type . _Software.Name XEASY _Software.Version . _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Cross peak integration' 4997 2 'Resonance assignment' 4997 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 4997 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 4997 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_NMR_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_3 _NMR_spectrometer.Entry_ID 4997 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4997 _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 Varian INOVA . 500 . . . 4997 1 2 NMR_spectrometer_2 Varian INOVA . 750 . . . 4997 1 3 NMR_spectrometer_3 Varian INOVA . 800 . . . 4997 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 4997 _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 'COSY with DQF' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4997 1 2 'TOCSY/NOESY with WaterGate' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4997 1 3 'HSQC: Gradient enhanced' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4997 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 4997 _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 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . 4997 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . 4997 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_CS_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode CS_1 _Assigned_chem_shift_list.Entry_ID 4997 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $cond_H2O _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 'COSY with DQF' 1 $sample_1 . 4997 1 2 'TOCSY/NOESY with WaterGate' 1 $sample_1 . 4997 1 3 'HSQC: Gradient enhanced' 1 $sample_1 . 4997 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 8.58 0.02 . 1 . . . . . . . . . 4997 1 2 . 1 1 2 2 ILE HA H 1 3.95 0.02 . 1 . . . . . . . . . 4997 1 3 . 1 1 2 2 ILE HB H 1 1.42 0.02 . 1 . . . . . . . . . 4997 1 4 . 1 1 2 2 ILE HG12 H 1 1.17 0.02 . 2 . . . . . . . . . 4997 1 5 . 1 1 2 2 ILE HG13 H 1 0.87 0.02 . 2 . . . . . . . . . 4997 1 6 . 1 1 2 2 ILE HG21 H 1 0.63 0.02 . 1 . . . . . . . . . 4997 1 7 . 1 1 2 2 ILE HG22 H 1 0.63 0.02 . 1 . . . . . . . . . 4997 1 8 . 1 1 2 2 ILE HG23 H 1 0.63 0.02 . 1 . . . . . . . . . 4997 1 9 . 1 1 2 2 ILE HD11 H 1 0.52 0.02 . 1 . . . . . . . . . 4997 1 10 . 1 1 2 2 ILE HD12 H 1 0.52 0.02 . 1 . . . . . . . . . 4997 1 11 . 1 1 2 2 ILE HD13 H 1 0.52 0.02 . 1 . . . . . . . . . 4997 1 12 . 1 1 3 3 VAL H H 1 8.21 0.02 . 1 . . . . . . . . . 4997 1 13 . 1 1 3 3 VAL HA H 1 3.69 0.02 . 1 . . . . . . . . . 4997 1 14 . 1 1 3 3 VAL HB H 1 1.95 0.02 . 1 . . . . . . . . . 4997 1 15 . 1 1 3 3 VAL HG11 H 1 1.00 0.02 . 2 . . . . . . . . . 4997 1 16 . 1 1 3 3 VAL HG12 H 1 1.00 0.02 . 2 . . . . . . . . . 4997 1 17 . 1 1 3 3 VAL HG13 H 1 1.00 0.02 . 2 . . . . . . . . . 4997 1 18 . 1 1 3 3 VAL HG21 H 1 0.92 0.02 . 2 . . . . . . . . . 4997 1 19 . 1 1 3 3 VAL HG22 H 1 0.92 0.02 . 2 . . . . . . . . . 4997 1 20 . 1 1 3 3 VAL HG23 H 1 0.92 0.02 . 2 . . . . . . . . . 4997 1 21 . 1 1 4 4 GLU H H 1 8.32 0.02 . 1 . . . . . . . . . 4997 1 22 . 1 1 4 4 GLU HA H 1 4.01 0.02 . 1 . . . . . . . . . 4997 1 23 . 1 1 5 5 GLN HB2 H 1 2.01 0.02 . 2 . . . . . . . . . 4997 1 24 . 1 1 5 5 GLN HB3 H 1 2.08 0.02 . 2 . . . . . . . . . 4997 1 25 . 1 1 5 5 GLN HG2 H 1 2.34 0.02 . 2 . . . . . . . . . 4997 1 26 . 1 1 5 5 GLN HG3 H 1 2.43 0.02 . 2 . . . . . . . . . 4997 1 27 . 1 1 5 5 GLN HE21 H 1 7.45 0.02 . 2 . . . . . . . . . 4997 1 28 . 1 1 5 5 GLN HE22 H 1 6.84 0.02 . 2 . . . . . . . . . 4997 1 29 . 1 1 6 6 CYS H H 1 8.32 0.02 . 1 . . . . . . . . . 4997 1 30 . 1 1 6 6 CYS HA H 1 4.85 0.02 . 1 . . . . . . . . . 4997 1 31 . 1 1 6 6 CYS HB2 H 1 3.35 0.02 . 2 . . . . . . . . . 4997 1 32 . 1 1 7 7 CYS HA H 1 4.82 0.02 . 1 . . . . . . . . . 4997 1 33 . 1 1 8 8 THR H H 1 8.36 0.02 . 1 . . . . . . . . . 4997 1 34 . 1 1 8 8 THR HA H 1 3.96 0.02 . 1 . . . . . . . . . 4997 1 35 . 1 1 8 8 THR HB H 1 4.34 0.02 . 1 . . . . . . . . . 4997 1 36 . 1 1 8 8 THR HG21 H 1 1.24 0.02 . 1 . . . . . . . . . 4997 1 37 . 1 1 8 8 THR HG22 H 1 1.24 0.02 . 1 . . . . . . . . . 4997 1 38 . 1 1 8 8 THR HG23 H 1 1.24 0.02 . 1 . . . . . . . . . 4997 1 39 . 1 1 9 9 SER HA H 1 4.09 0.02 . 1 . . . . . . . . . 4997 1 40 . 1 1 9 9 SER HB2 H 1 4.03 0.02 . 2 . . . . . . . . . 4997 1 41 . 1 1 9 9 SER HB3 H 1 3.87 0.02 . 2 . . . . . . . . . 4997 1 42 . 1 1 10 10 ILE H H 1 7.87 0.02 . 1 . . . . . . . . . 4997 1 43 . 1 1 10 10 ILE HA H 1 4.36 0.02 . 1 . . . . . . . . . 4997 1 44 . 1 1 10 10 ILE HB H 1 1.55 0.02 . 1 . . . . . . . . . 4997 1 45 . 1 1 10 10 ILE HG12 H 1 1.05 0.02 . 2 . . . . . . . . . 4997 1 46 . 1 1 10 10 ILE HG13 H 1 1.23 0.02 . 2 . . . . . . . . . 4997 1 47 . 1 1 10 10 ILE HG21 H 1 0.61 0.02 . 1 . . . . . . . . . 4997 1 48 . 1 1 10 10 ILE HG22 H 1 0.61 0.02 . 1 . . . . . . . . . 4997 1 49 . 1 1 10 10 ILE HG23 H 1 0.61 0.02 . 1 . . . . . . . . . 4997 1 50 . 1 1 10 10 ILE HD11 H 1 0.43 0.02 . 1 . . . . . . . . . 4997 1 51 . 1 1 10 10 ILE HD12 H 1 0.43 0.02 . 1 . . . . . . . . . 4997 1 52 . 1 1 10 10 ILE HD13 H 1 0.43 0.02 . 1 . . . . . . . . . 4997 1 53 . 1 1 11 11 CYS H H 1 9.79 0.02 . 1 . . . . . . . . . 4997 1 54 . 1 1 11 11 CYS HA H 1 4.95 0.02 . 1 . . . . . . . . . 4997 1 55 . 1 1 12 12 SER H H 1 8.73 0.02 . 1 . . . . . . . . . 4997 1 56 . 1 1 12 12 SER HA H 1 4.57 0.02 . 1 . . . . . . . . . 4997 1 57 . 1 1 12 12 SER HB2 H 1 4.25 0.02 . 2 . . . . . . . . . 4997 1 58 . 1 1 12 12 SER HB3 H 1 3.98 0.02 . 2 . . . . . . . . . 4997 1 59 . 1 1 13 13 LEU H H 1 8.62 0.02 . 1 . . . . . . . . . 4997 1 60 . 1 1 13 13 LEU HA H 1 3.73 0.02 . 1 . . . . . . . . . 4997 1 61 . 1 1 13 13 LEU HB2 H 1 1.33 0.02 . 2 . . . . . . . . . 4997 1 62 . 1 1 13 13 LEU HB3 H 1 1.21 0.02 . 2 . . . . . . . . . 4997 1 63 . 1 1 13 13 LEU HG H 1 0.93 0.02 . 1 . . . . . . . . . 4997 1 64 . 1 1 13 13 LEU HD11 H 1 0.78 0.02 . 1 . . . . . . . . . 4997 1 65 . 1 1 13 13 LEU HD12 H 1 0.78 0.02 . 1 . . . . . . . . . 4997 1 66 . 1 1 13 13 LEU HD13 H 1 0.78 0.02 . 1 . . . . . . . . . 4997 1 67 . 1 1 13 13 LEU HD21 H 1 0.71 0.02 . 1 . . . . . . . . . 4997 1 68 . 1 1 13 13 LEU HD22 H 1 0.71 0.02 . 1 . . . . . . . . . 4997 1 69 . 1 1 13 13 LEU HD23 H 1 0.71 0.02 . 1 . . . . . . . . . 4997 1 70 . 1 1 14 14 TYR H H 1 7.56 0.02 . 1 . . . . . . . . . 4997 1 71 . 1 1 14 14 TYR HA H 1 4.11 0.02 . 1 . . . . . . . . . 4997 1 72 . 1 1 14 14 TYR HB2 H 1 2.99 0.02 . 2 . . . . . . . . . 4997 1 73 . 1 1 14 14 TYR HB3 H 1 2.94 0.02 . 2 . . . . . . . . . 4997 1 74 . 1 1 14 14 TYR HD1 H 1 6.89 0.02 . 3 . . . . . . . . . 4997 1 75 . 1 1 14 14 TYR HE1 H 1 7.05 0.02 . 3 . . . . . . . . . 4997 1 76 . 1 1 15 15 GLN H H 1 7.51 0.02 . 1 . . . . . . . . . 4997 1 77 . 1 1 15 15 GLN HA H 1 3.94 0.02 . 1 . . . . . . . . . 4997 1 78 . 1 1 15 15 GLN HB2 H 1 2.01 0.02 . 2 . . . . . . . . . 4997 1 79 . 1 1 15 15 GLN HG2 H 1 2.33 0.02 . 2 . . . . . . . . . 4997 1 80 . 1 1 15 15 GLN HG3 H 1 2.38 0.02 . 2 . . . . . . . . . 4997 1 81 . 1 1 15 15 GLN HE21 H 1 6.84 0.02 . 2 . . . . . . . . . 4997 1 82 . 1 1 15 15 GLN HE22 H 1 7.05 0.02 . 2 . . . . . . . . . 4997 1 83 . 1 1 16 16 LEU H H 1 7.90 0.02 . 1 . . . . . . . . . 4997 1 84 . 1 1 16 16 LEU HA H 1 4.11 0.02 . 1 . . . . . . . . . 4997 1 85 . 1 1 16 16 LEU HB2 H 1 1.71 0.02 . 2 . . . . . . . . . 4997 1 86 . 1 1 17 17 GLU H H 1 8.07 0.02 . 1 . . . . . . . . . 4997 1 87 . 1 1 17 17 GLU HA H 1 4.28 0.02 . 1 . . . . . . . . . 4997 1 88 . 1 1 17 17 GLU HB2 H 1 2.06 0.02 . 2 . . . . . . . . . 4997 1 89 . 1 1 17 17 GLU HG2 H 1 2.29 0.02 . 2 . . . . . . . . . 4997 1 90 . 1 1 17 17 GLU HG3 H 1 2.54 0.02 . 2 . . . . . . . . . 4997 1 91 . 1 1 18 18 ASN H H 1 7.36 0.02 . 1 . . . . . . . . . 4997 1 92 . 1 1 18 18 ASN HA H 1 4.48 0.02 . 1 . . . . . . . . . 4997 1 93 . 1 1 18 18 ASN HB2 H 1 2.62 0.02 . 2 . . . . . . . . . 4997 1 94 . 1 1 18 18 ASN HB3 H 1 2.53 0.02 . 2 . . . . . . . . . 4997 1 95 . 1 1 18 18 ASN HD21 H 1 6.58 0.02 . 2 . . . . . . . . . 4997 1 96 . 1 1 18 18 ASN HD22 H 1 7.15 0.02 . 2 . . . . . . . . . 4997 1 97 . 1 1 19 19 TYR H H 1 7.90 0.02 . 1 . . . . . . . . . 4997 1 98 . 1 1 19 19 TYR HA H 1 4.38 0.02 . 1 . . . . . . . . . 4997 1 99 . 1 1 19 19 TYR HB2 H 1 2.93 0.02 . 2 . . . . . . . . . 4997 1 100 . 1 1 19 19 TYR HB3 H 1 3.51 0.02 . 2 . . . . . . . . . 4997 1 101 . 1 1 19 19 TYR HD1 H 1 6.74 0.02 . 3 . . . . . . . . . 4997 1 102 . 1 1 19 19 TYR HE1 H 1 7.23 0.02 . 3 . . . . . . . . . 4997 1 103 . 1 1 20 20 CYS H H 1 7.29 0.02 . 1 . . . . . . . . . 4997 1 104 . 1 1 20 20 CYS HA H 1 5.23 0.02 . 1 . . . . . . . . . 4997 1 105 . 1 1 20 20 CYS HB2 H 1 3.32 0.02 . 2 . . . . . . . . . 4997 1 106 . 1 1 20 20 CYS HB3 H 1 2.18 0.02 . 2 . . . . . . . . . 4997 1 107 . 1 1 21 21 ASN HD21 H 1 6.27 0.02 . 2 . . . . . . . . . 4997 1 108 . 1 1 21 21 ASN HD22 H 1 7.48 0.02 . 2 . . . . . . . . . 4997 1 stop_ save_ save_CS_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode CS_2 _Assigned_chem_shift_list.Entry_ID 4997 _Assigned_chem_shift_list.ID 2 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $cond_H2O _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 'COSY with DQF' 1 $sample_1 . 4997 2 2 'TOCSY/NOESY with WaterGate' 1 $sample_1 . 4997 2 3 'HSQC: Gradient enhanced' 1 $sample_1 . 4997 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 4.19 0.02 . 1 . . . . . . . . . 4997 2 2 . 2 2 1 1 PHE HB2 H 1 3.13 0.02 . 1 . . . . . . . . . 4997 2 3 . 2 2 1 1 PHE HB3 H 1 3.08 0.02 . 2 . . . . . . . . . 4997 2 4 . 2 2 1 1 PHE HD1 H 1 7.18 0.02 . 2 . . . . . . . . . 4997 2 5 . 2 2 1 1 PHE HE1 H 1 7.3 0.02 . 3 . . . . . . . . . 4997 2 6 . 2 2 1 1 PHE HZ H 1 7.21 0.02 . 1 . . . . . . . . . 4997 2 7 . 2 2 2 2 VAL H H 1 7.99 0.02 . 1 . . . . . . . . . 4997 2 8 . 2 2 2 2 VAL HA H 1 4.01 0.02 . 1 . . . . . . . . . 4997 2 9 . 2 2 2 2 VAL HB H 1 1.99 0.02 . 1 . . . . . . . . . 4997 2 10 . 2 2 2 2 VAL HG11 H 1 0.78 0.02 . 2 . . . . . . . . . 4997 2 11 . 2 2 2 2 VAL HG12 H 1 0.78 0.02 . 2 . . . . . . . . . 4997 2 12 . 2 2 2 2 VAL HG13 H 1 0.78 0.02 . 2 . . . . . . . . . 4997 2 13 . 2 2 3 3 ASN H H 1 8.45 0.02 . 1 . . . . . . . . . 4997 2 14 . 2 2 3 3 ASN HA H 1 4.64 0.02 . 1 . . . . . . . . . 4997 2 15 . 2 2 3 3 ASN HB2 H 1 2.66 0.02 . 2 . . . . . . . . . 4997 2 16 . 2 2 3 3 ASN HD21 H 1 6.82 0.02 . 2 . . . . . . . . . 4997 2 17 . 2 2 3 3 ASN HD22 H 1 7.49 0.02 . 2 . . . . . . . . . 4997 2 18 . 2 2 4 4 GLN H H 1 8.36 0.02 . 1 . . . . . . . . . 4997 2 19 . 2 2 4 4 GLN HA H 1 4.43 0.02 . 1 . . . . . . . . . 4997 2 20 . 2 2 4 4 GLN HB2 H 1 2.04 0.02 . 2 . . . . . . . . . 4997 2 21 . 2 2 4 4 GLN HB3 H 1 1.87 0.02 . 2 . . . . . . . . . 4997 2 22 . 2 2 4 4 GLN HG2 H 1 2.21 0.02 . 2 . . . . . . . . . 4997 2 23 . 2 2 4 4 GLN HE21 H 1 7.37 0.02 . 2 . . . . . . . . . 4997 2 24 . 2 2 4 4 GLN HE22 H 1 6.76 0.02 . 2 . . . . . . . . . 4997 2 25 . 2 2 5 5 HIS H H 1 8.69 0.02 . 1 . . . . . . . . . 4997 2 26 . 2 2 5 5 HIS HA H 1 4.43 0.02 . 1 . . . . . . . . . 4997 2 27 . 2 2 5 5 HIS HB2 H 1 3.55 0.02 . 2 . . . . . . . . . 4997 2 28 . 2 2 5 5 HIS HB3 H 1 3.24 0.02 . 2 . . . . . . . . . 4997 2 29 . 2 2 5 5 HIS HD2 H 1 7.34 0.02 . 1 . . . . . . . . . 4997 2 30 . 2 2 5 5 HIS HE1 H 1 8.56 0.02 . 1 . . . . . . . . . 4997 2 31 . 2 2 6 6 LEU H H 1 9.08 0.02 . 1 . . . . . . . . . 4997 2 32 . 2 2 6 6 LEU HA H 1 4.47 0.02 . 1 . . . . . . . . . 4997 2 33 . 2 2 6 6 LEU HB2 H 1 1.75 0.02 . 2 . . . . . . . . . 4997 2 34 . 2 2 6 6 LEU HB3 H 1 1.56 0.02 . 2 . . . . . . . . . 4997 2 35 . 2 2 6 6 LEU HG H 1 0.87 0.02 . 1 . . . . . . . . . 4997 2 36 . 2 2 6 6 LEU HD11 H 1 0.73 0.02 . 2 . . . . . . . . . 4997 2 37 . 2 2 6 6 LEU HD12 H 1 0.73 0.02 . 2 . . . . . . . . . 4997 2 38 . 2 2 6 6 LEU HD13 H 1 0.73 0.02 . 2 . . . . . . . . . 4997 2 39 . 2 2 6 6 LEU HD21 H 1 0.66 0.02 . 2 . . . . . . . . . 4997 2 40 . 2 2 6 6 LEU HD22 H 1 0.66 0.02 . 2 . . . . . . . . . 4997 2 41 . 2 2 6 6 LEU HD23 H 1 0.66 0.02 . 2 . . . . . . . . . 4997 2 42 . 2 2 7 7 CYS H H 1 8.52 0.02 . 1 . . . . . . . . . 4997 2 43 . 2 2 7 7 CYS HA H 1 4.97 0.02 . 1 . . . . . . . . . 4997 2 44 . 2 2 7 7 CYS HB2 H 1 3.23 0.02 . 2 . . . . . . . . . 4997 2 45 . 2 2 7 7 CYS HB3 H 1 2.94 0.02 . 2 . . . . . . . . . 4997 2 46 . 2 2 8 8 GLY H H 1 9.43 0.02 . 1 . . . . . . . . . 4997 2 47 . 2 2 8 8 GLY HA2 H 1 3.95 0.02 . 2 . . . . . . . . . 4997 2 48 . 2 2 8 8 GLY HA3 H 1 3.85 0.02 . 2 . . . . . . . . . 4997 2 49 . 2 2 9 9 SER H H 1 9.15 0.02 . 1 . . . . . . . . . 4997 2 50 . 2 2 9 9 SER HA H 1 3.72 0.02 . 1 . . . . . . . . . 4997 2 51 . 2 2 10 10 HIS H H 1 7.92 0.02 . 1 . . . . . . . . . 4997 2 52 . 2 2 10 10 HIS HA H 1 4.38 0.02 . 1 . . . . . . . . . 4997 2 53 . 2 2 10 10 HIS HB2 H 1 3.51 0.02 . 2 . . . . . . . . . 4997 2 54 . 2 2 10 10 HIS HB3 H 1 3.23 0.02 . 2 . . . . . . . . . 4997 2 55 . 2 2 10 10 HIS HD2 H 1 7.44 0.02 . 1 . . . . . . . . . 4997 2 56 . 2 2 10 10 HIS HE1 H 1 8.58 0.02 . 1 . . . . . . . . . 4997 2 57 . 2 2 12 12 VAL HA H 1 3.55 0.02 . 1 . . . . . . . . . 4997 2 58 . 2 2 12 12 VAL HB H 1 1.9 0.02 . 1 . . . . . . . . . 4997 2 59 . 2 2 12 12 VAL HG11 H 1 0.86 0.02 . 2 . . . . . . . . . 4997 2 60 . 2 2 12 12 VAL HG12 H 1 0.86 0.02 . 2 . . . . . . . . . 4997 2 61 . 2 2 12 12 VAL HG13 H 1 0.86 0.02 . 2 . . . . . . . . . 4997 2 62 . 2 2 14 14 ALA HA H 1 4.05 0.02 . 1 . . . . . . . . . 4997 2 63 . 2 2 14 14 ALA HB1 H 1 1.42 0.02 . 1 . . . . . . . . . 4997 2 64 . 2 2 14 14 ALA HB2 H 1 1.42 0.02 . 1 . . . . . . . . . 4997 2 65 . 2 2 14 14 ALA HB3 H 1 1.42 0.02 . 1 . . . . . . . . . 4997 2 66 . 2 2 15 15 LEU H H 1 7.83 0.02 . 1 . . . . . . . . . 4997 2 67 . 2 2 15 15 LEU HA H 1 3.61 0.02 . 1 . . . . . . . . . 4997 2 68 . 2 2 15 15 LEU HB2 H 1 1.98 0.02 . 2 . . . . . . . . . 4997 2 69 . 2 2 15 15 LEU HG H 1 1.28 0.02 . 1 . . . . . . . . . 4997 2 70 . 2 2 15 15 LEU HD11 H 1 0.48 0.02 . 2 . . . . . . . . . 4997 2 71 . 2 2 15 15 LEU HD12 H 1 0.48 0.02 . 2 . . . . . . . . . 4997 2 72 . 2 2 15 15 LEU HD13 H 1 0.48 0.02 . 2 . . . . . . . . . 4997 2 73 . 2 2 15 15 LEU HD21 H 1 0.02 0.02 . 2 . . . . . . . . . 4997 2 74 . 2 2 15 15 LEU HD22 H 1 0.02 0.02 . 2 . . . . . . . . . 4997 2 75 . 2 2 15 15 LEU HD23 H 1 0.02 0.02 . 2 . . . . . . . . . 4997 2 76 . 2 2 17 17 LEU H H 1 7.74 0.02 . 1 . . . . . . . . . 4997 2 77 . 2 2 17 17 LEU HA H 1 3.9 0.02 . 1 . . . . . . . . . 4997 2 78 . 2 2 17 17 LEU HB2 H 1 1.85 0.02 . 2 . . . . . . . . . 4997 2 79 . 2 2 17 17 LEU HB3 H 1 1.56 0.02 . 2 . . . . . . . . . 4997 2 80 . 2 2 18 18 VAL H H 1 8.51 0.02 . 1 . . . . . . . . . 4997 2 81 . 2 2 18 18 VAL HA H 1 3.74 0.02 . 1 . . . . . . . . . 4997 2 82 . 2 2 18 18 VAL HB H 1 1.99 0.02 . 1 . . . . . . . . . 4997 2 83 . 2 2 18 18 VAL HG11 H 1 0.78 0.02 . 2 . . . . . . . . . 4997 2 84 . 2 2 18 18 VAL HG12 H 1 0.78 0.02 . 2 . . . . . . . . . 4997 2 85 . 2 2 18 18 VAL HG13 H 1 0.78 0.02 . 2 . . . . . . . . . 4997 2 86 . 2 2 18 18 VAL HG21 H 1 0.93 0.02 . 2 . . . . . . . . . 4997 2 87 . 2 2 18 18 VAL HG22 H 1 0.93 0.02 . 2 . . . . . . . . . 4997 2 88 . 2 2 18 18 VAL HG23 H 1 0.93 0.02 . 2 . . . . . . . . . 4997 2 89 . 2 2 19 19 CYS H H 1 8.7 0.02 . 1 . . . . . . . . . 4997 2 90 . 2 2 19 19 CYS HA H 1 4.76 0.02 . 1 . . . . . . . . . 4997 2 91 . 2 2 19 19 CYS HB2 H 1 2.92 0.02 . 2 . . . . . . . . . 4997 2 92 . 2 2 19 19 CYS HB3 H 1 3.35 0.02 . 2 . . . . . . . . . 4997 2 93 . 2 2 20 20 GLY H H 1 7.74 0.02 . 1 . . . . . . . . . 4997 2 94 . 2 2 20 20 GLY HA2 H 1 3.77 0.02 . 2 . . . . . . . . . 4997 2 95 . 2 2 20 20 GLY HA3 H 1 3.91 0.02 . 2 . . . . . . . . . 4997 2 96 . 2 2 21 21 GLU H H 1 8.98 0.02 . 1 . . . . . . . . . 4997 2 97 . 2 2 21 21 GLU HA H 1 4.19 0.02 . 1 . . . . . . . . . 4997 2 98 . 2 2 21 21 GLU HB2 H 1 2.25 0.02 . 2 . . . . . . . . . 4997 2 99 . 2 2 21 21 GLU HB3 H 1 1.99 0.02 . 2 . . . . . . . . . 4997 2 100 . 2 2 21 21 GLU HG2 H 1 2.54 0.02 . 2 . . . . . . . . . 4997 2 101 . 2 2 21 21 GLU HG3 H 1 2.11 0.02 . 2 . . . . . . . . . 4997 2 102 . 2 2 22 22 ARG H H 1 8.13 0.02 . 1 . . . . . . . . . 4997 2 103 . 2 2 22 22 ARG HA H 1 4.15 0.02 . 1 . . . . . . . . . 4997 2 104 . 2 2 22 22 ARG HG2 H 1 1.84 0.02 . 4 . . . . . . . . . 4997 2 105 . 2 2 22 22 ARG HE H 1 7.15 0.02 . 1 . . . . . . . . . 4997 2 106 . 2 2 23 23 GLY HA2 H 1 4.38 0.02 . 2 . . . . . . . . . 4997 2 107 . 2 2 23 23 GLY HA3 H 1 4.1 0.02 . 2 . . . . . . . . . 4997 2 108 . 2 2 24 24 PHE H H 1 8.39 0.02 . 1 . . . . . . . . . 4997 2 109 . 2 2 24 24 PHE HA H 1 4.99 0.02 . 1 . . . . . . . . . 4997 2 110 . 2 2 24 24 PHE HB2 H 1 2.93 0.02 . 2 . . . . . . . . . 4997 2 111 . 2 2 24 24 PHE HB3 H 1 3.22 0.02 . 2 . . . . . . . . . 4997 2 112 . 2 2 24 24 PHE HD1 H 1 6.89 0.02 . 3 . . . . . . . . . 4997 2 113 . 2 2 25 25 PHE H H 1 9.58 0.02 . 1 . . . . . . . . . 4997 2 114 . 2 2 25 25 PHE HB2 H 1 3.92 0.02 . 2 . . . . . . . . . 4997 2 115 . 2 2 25 25 PHE HB3 H 1 3.8 0.02 . 2 . . . . . . . . . 4997 2 116 . 2 2 28 28 THR H H 1 8.13 0.02 . 1 . . . . . . . . . 4997 2 117 . 2 2 28 28 THR HA H 1 4.15 0.02 . 1 . . . . . . . . . 4997 2 118 . 2 2 28 28 THR HG21 H 1 1.24 0.02 . 1 . . . . . . . . . 4997 2 119 . 2 2 28 28 THR HG22 H 1 1.24 0.02 . 1 . . . . . . . . . 4997 2 120 . 2 2 28 28 THR HG23 H 1 1.24 0.02 . 1 . . . . . . . . . 4997 2 121 . 2 2 29 29 LYS H H 1 8.29 0.02 . 1 . . . . . . . . . 4997 2 122 . 2 2 29 29 LYS HA H 1 4.38 0.02 . 1 . . . . . . . . . 4997 2 123 . 2 2 29 29 LYS HB2 H 1 1.88 0.02 . 2 . . . . . . . . . 4997 2 124 . 2 2 29 29 LYS HG2 H 1 1.46 0.02 . 2 . . . . . . . . . 4997 2 125 . 2 2 29 29 LYS HD2 H 1 1.68 0.02 . 4 . . . . . . . . . 4997 2 126 . 2 2 29 29 LYS HE2 H 1 3 0.02 . 2 . . . . . . . . . 4997 2 127 . 2 2 29 29 LYS HZ1 H 1 7.52 0.02 . 1 . . . . . . . . . 4997 2 128 . 2 2 29 29 LYS HZ2 H 1 7.52 0.02 . 1 . . . . . . . . . 4997 2 129 . 2 2 29 29 LYS HZ3 H 1 7.52 0.02 . 1 . . . . . . . . . 4997 2 130 . 2 2 30 30 THR HA H 1 4.28 0.02 . 1 . . . . . . . . . 4997 2 131 . 2 2 30 30 THR HB H 1 4.23 0.02 . 1 . . . . . . . . . 4997 2 132 . 2 2 30 30 THR HG21 H 1 1.15 0.02 . 1 . . . . . . . . . 4997 2 133 . 2 2 30 30 THR HG22 H 1 1.15 0.02 . 1 . . . . . . . . . 4997 2 134 . 2 2 30 30 THR HG23 H 1 1.15 0.02 . 1 . . . . . . . . . 4997 2 stop_ save_ save_CS_3 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode CS_3 _Assigned_chem_shift_list.Entry_ID 4997 _Assigned_chem_shift_list.ID 3 _Assigned_chem_shift_list.Sample_condition_list_ID 2 _Assigned_chem_shift_list.Sample_condition_list_label $cond_TFE _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 'COSY with DQF' 2 $sample_2 . 4997 3 2 'TOCSY/NOESY with WaterGate' 2 $sample_2 . 4997 3 3 'HSQC: Gradient enhanced' 2 $sample_2 . 4997 3 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 1 1 GLY HA2 H 1 4.09 0.02 . 2 . . . . . . . . . 4997 3 2 . 1 1 1 1 GLY HA3 H 1 4.01 0.02 . 2 . . . . . . . . . 4997 3 3 . 1 1 1 1 GLY CA C 13 43.75 0.02 . 1 . . . . . . . . . 4997 3 4 . 1 1 2 2 ILE H H 1 8.52 0.02 . 1 . . . . . . . . . 4997 3 5 . 1 1 2 2 ILE HA H 1 3.95 0.02 . 1 . . . . . . . . . 4997 3 6 . 1 1 2 2 ILE HB H 1 0.95 0.02 . 1 . . . . . . . . . 4997 3 7 . 1 1 2 2 ILE HG12 H 1 1.30 0.02 . 2 . . . . . . . . . 4997 3 8 . 1 1 2 2 ILE HG13 H 1 1.23 0.02 . 2 . . . . . . . . . 4997 3 9 . 1 1 2 2 ILE HG21 H 1 0.76 0.02 . 1 . . . . . . . . . 4997 3 10 . 1 1 2 2 ILE HG22 H 1 0.76 0.02 . 1 . . . . . . . . . 4997 3 11 . 1 1 2 2 ILE HG23 H 1 0.76 0.02 . 1 . . . . . . . . . 4997 3 12 . 1 1 2 2 ILE HD11 H 1 0.68 0.02 . 1 . . . . . . . . . 4997 3 13 . 1 1 2 2 ILE HD12 H 1 0.68 0.02 . 1 . . . . . . . . . 4997 3 14 . 1 1 2 2 ILE HD13 H 1 0.68 0.02 . 1 . . . . . . . . . 4997 3 15 . 1 1 2 2 ILE CA C 13 63.31 0.02 . 1 . . . . . . . . . 4997 3 16 . 1 1 2 2 ILE CG2 C 13 17.08 0.02 . 1 . . . . . . . . . 4997 3 17 . 1 1 2 2 ILE CD1 C 13 12.59 0.02 . 1 . . . . . . . . . 4997 3 18 . 1 1 3 3 VAL H H 1 8.11 0.02 . 1 . . . . . . . . . 4997 3 19 . 1 1 3 3 VAL HA H 1 3.38 0.02 . 1 . . . . . . . . . 4997 3 20 . 1 1 3 3 VAL HB H 1 1.95 0.02 . 1 . . . . . . . . . 4997 3 21 . 1 1 3 3 VAL HG11 H 1 0.95 0.02 . 2 . . . . . . . . . 4997 3 22 . 1 1 3 3 VAL HG12 H 1 0.95 0.02 . 2 . . . . . . . . . 4997 3 23 . 1 1 3 3 VAL HG13 H 1 0.95 0.02 . 2 . . . . . . . . . 4997 3 24 . 1 1 3 3 VAL HG21 H 1 0.91 0.02 . 2 . . . . . . . . . 4997 3 25 . 1 1 3 3 VAL HG22 H 1 0.91 0.02 . 2 . . . . . . . . . 4997 3 26 . 1 1 3 3 VAL HG23 H 1 0.91 0.02 . 2 . . . . . . . . . 4997 3 27 . 1 1 3 3 VAL CA C 13 66.15 0.02 . 1 . . . . . . . . . 4997 3 28 . 1 1 3 3 VAL CB C 13 27.34 0.02 . 1 . . . . . . . . . 4997 3 29 . 1 1 4 4 GLU H H 1 8.19 0.02 . 1 . . . . . . . . . 4997 3 30 . 1 1 4 4 GLU HA H 1 4.11 0.02 . 1 . . . . . . . . . 4997 3 31 . 1 1 4 4 GLU HB2 H 1 2.18 0.02 . 2 . . . . . . . . . 4997 3 32 . 1 1 4 4 GLU HB3 H 1 2.07 0.02 . 2 . . . . . . . . . 4997 3 33 . 1 1 4 4 GLU HG2 H 1 2.58 0.02 . 2 . . . . . . . . . 4997 3 34 . 1 1 4 4 GLU HG3 H 1 2.40 0.02 . 2 . . . . . . . . . 4997 3 35 . 1 1 4 4 GLU CA C 13 61.49 0.02 . 1 . . . . . . . . . 4997 3 36 . 1 1 4 4 GLU CG C 13 34.94 0.02 . 1 . . . . . . . . . 4997 3 37 . 1 1 5 5 GLN H H 1 8.26 0.02 . 1 . . . . . . . . . 4997 3 38 . 1 1 5 5 GLN HA H 1 4.05 0.02 . 1 . . . . . . . . . 4997 3 39 . 1 1 5 5 GLN HB2 H 1 2.88 0.02 . 2 . . . . . . . . . 4997 3 40 . 1 1 5 5 GLN HB3 H 1 2.10 0.02 . 2 . . . . . . . . . 4997 3 41 . 1 1 5 5 GLN HG2 H 1 2.49 0.02 . 2 . . . . . . . . . 4997 3 42 . 1 1 5 5 GLN HG3 H 1 2.42 0.02 . 2 . . . . . . . . . 4997 3 43 . 1 1 5 5 GLN HE21 H 1 7.54 0.02 . 2 . . . . . . . . . 4997 3 44 . 1 1 5 5 GLN CA C 13 59.08 0.02 . 1 . . . . . . . . . 4997 3 45 . 1 1 5 5 GLN CG C 13 33.17 0.02 . 1 . . . . . . . . . 4997 3 46 . 1 1 6 6 CYS H H 1 8.38 0.02 . 1 . . . . . . . . . 4997 3 47 . 1 1 6 6 CYS HA H 1 4.95 0.02 . 1 . . . . . . . . . 4997 3 48 . 1 1 6 6 CYS HB2 H 1 3.37 0.02 . 2 . . . . . . . . . 4997 3 49 . 1 1 6 6 CYS HB3 H 1 2.96 0.02 . 2 . . . . . . . . . 4997 3 50 . 1 1 6 6 CYS CA C 13 55.37 0.02 . 1 . . . . . . . . . 4997 3 51 . 1 1 7 7 CYS H H 1 8.29 0.02 . 1 . . . . . . . . . 4997 3 52 . 1 1 7 7 CYS HA H 1 4.89 0.02 . 1 . . . . . . . . . 4997 3 53 . 1 1 7 7 CYS HB2 H 1 3.73 0.02 . 2 . . . . . . . . . 4997 3 54 . 1 1 7 7 CYS HB3 H 1 3.32 0.02 . 2 . . . . . . . . . 4997 3 55 . 1 1 7 7 CYS CA C 13 57.41 0.02 . 1 . . . . . . . . . 4997 3 56 . 1 1 8 8 THR HA H 1 4.20 0.02 . 1 . . . . . . . . . 4997 3 57 . 1 1 8 8 THR HB H 1 4.44 0.02 . 1 . . . . . . . . . 4997 3 58 . 1 1 8 8 THR HG21 H 1 1.27 0.02 . 1 . . . . . . . . . 4997 3 59 . 1 1 8 8 THR HG22 H 1 1.27 0.02 . 1 . . . . . . . . . 4997 3 60 . 1 1 8 8 THR HG23 H 1 1.27 0.02 . 1 . . . . . . . . . 4997 3 61 . 1 1 8 8 THR CA C 13 60.47 0.02 . 1 . . . . . . . . . 4997 3 62 . 1 1 8 8 THR CB C 13 69.45 0.02 . 1 . . . . . . . . . 4997 3 63 . 1 1 8 8 THR CG2 C 13 21.99 0.02 . 1 . . . . . . . . . 4997 3 64 . 1 1 9 9 SER HA H 1 4.76 0.02 . 1 . . . . . . . . . 4997 3 65 . 1 1 9 9 SER HB2 H 1 4.08 0.02 . 2 . . . . . . . . . 4997 3 66 . 1 1 9 9 SER HB3 H 1 3.92 0.02 . 2 . . . . . . . . . 4997 3 67 . 1 1 9 9 SER CA C 13 53.44 0.02 . 1 . . . . . . . . . 4997 3 68 . 1 1 10 10 ILE H H 1 7.92 0.02 . 1 . . . . . . . . . 4997 3 69 . 1 1 10 10 ILE HA H 1 4.53 0.02 . 1 . . . . . . . . . 4997 3 70 . 1 1 10 10 ILE HB H 1 1.69 0.02 . 1 . . . . . . . . . 4997 3 71 . 1 1 10 10 ILE HG12 H 1 1.30 0.02 . 2 . . . . . . . . . 4997 3 72 . 1 1 10 10 ILE HG21 H 1 0.77 0.02 . 1 . . . . . . . . . 4997 3 73 . 1 1 10 10 ILE HG22 H 1 0.77 0.02 . 1 . . . . . . . . . 4997 3 74 . 1 1 10 10 ILE HG23 H 1 0.77 0.02 . 1 . . . . . . . . . 4997 3 75 . 1 1 10 10 ILE HD11 H 1 0.66 0.02 . 1 . . . . . . . . . 4997 3 76 . 1 1 10 10 ILE HD12 H 1 0.66 0.02 . 1 . . . . . . . . . 4997 3 77 . 1 1 10 10 ILE HD13 H 1 0.66 0.02 . 1 . . . . . . . . . 4997 3 78 . 1 1 10 10 ILE CA C 13 56.59 0.02 . 1 . . . . . . . . . 4997 3 79 . 1 1 10 10 ILE CB C 13 39.46 0.02 . 1 . . . . . . . . . 4997 3 80 . 1 1 10 10 ILE CG2 C 13 17.48 0.02 . 1 . . . . . . . . . 4997 3 81 . 1 1 10 10 ILE CD1 C 13 14.19 0.02 . 1 . . . . . . . . . 4997 3 82 . 1 1 11 11 CYS H H 1 9.37 0.02 . 1 . . . . . . . . . 4997 3 83 . 1 1 11 11 CYS HA H 1 5.08 0.02 . 1 . . . . . . . . . 4997 3 84 . 1 1 11 11 CYS CA C 13 53.62 0.02 . 1 . . . . . . . . . 4997 3 85 . 1 1 12 12 SER H H 1 8.71 0.02 . 1 . . . . . . . . . 4997 3 86 . 1 1 12 12 SER HA H 1 4.66 0.02 . 1 . . . . . . . . . 4997 3 87 . 1 1 12 12 SER HB2 H 1 4.29 0.02 . 2 . . . . . . . . . 4997 3 88 . 1 1 12 12 SER HB3 H 1 4.03 0.02 . 2 . . . . . . . . . 4997 3 89 . 1 1 12 12 SER CB C 13 66.11 0.02 . 1 . . . . . . . . . 4997 3 90 . 1 1 13 13 LEU H H 1 8.59 0.02 . 1 . . . . . . . . . 4997 3 91 . 1 1 13 13 LEU HA H 1 4.08 0.02 . 1 . . . . . . . . . 4997 3 92 . 1 1 13 13 LEU HB2 H 1 1.51 0.02 . 2 . . . . . . . . . 4997 3 93 . 1 1 13 13 LEU HB3 H 1 1.46 0.02 . 2 . . . . . . . . . 4997 3 94 . 1 1 13 13 LEU HG H 1 1.57 0.02 . 1 . . . . . . . . . 4997 3 95 . 1 1 13 13 LEU HD11 H 1 0.90 0.02 . 2 . . . . . . . . . 4997 3 96 . 1 1 13 13 LEU HD12 H 1 0.90 0.02 . 2 . . . . . . . . . 4997 3 97 . 1 1 13 13 LEU HD13 H 1 0.90 0.02 . 2 . . . . . . . . . 4997 3 98 . 1 1 13 13 LEU HD21 H 1 0.82 0.02 . 2 . . . . . . . . . 4997 3 99 . 1 1 13 13 LEU HD22 H 1 0.82 0.02 . 2 . . . . . . . . . 4997 3 100 . 1 1 13 13 LEU HD23 H 1 0.82 0.02 . 2 . . . . . . . . . 4997 3 101 . 1 1 13 13 LEU CA C 13 59.37 0.02 . 1 . . . . . . . . . 4997 3 102 . 1 1 13 13 LEU CB C 13 41.88 0.02 . 1 . . . . . . . . . 4997 3 103 . 1 1 14 14 TYR H H 1 7.42 0.02 . 1 . . . . . . . . . 4997 3 104 . 1 1 14 14 TYR HA H 1 4.19 0.02 . 1 . . . . . . . . . 4997 3 105 . 1 1 14 14 TYR HB2 H 1 3.03 0.02 . 2 . . . . . . . . . 4997 3 106 . 1 1 14 14 TYR HB3 H 1 2.96 0.02 . 2 . . . . . . . . . 4997 3 107 . 1 1 14 14 TYR HD1 H 1 7.12 0.02 . 3 . . . . . . . . . 4997 3 108 . 1 1 14 14 TYR HE1 H 1 6.89 0.02 . . . . . . . . . . . 4997 3 109 . 1 1 14 14 TYR CA C 13 60.47 0.02 . 1 . . . . . . . . . 4997 3 110 . 1 1 14 14 TYR CB C 13 37.89 0.02 . 1 . . . . . . . . . 4997 3 111 . 1 1 14 14 TYR CD1 C 13 132.90 0.02 . 3 . . . . . . . . . 4997 3 112 . 1 1 14 14 TYR CE1 C 13 118.59 0.02 . 3 . . . . . . . . . 4997 3 113 . 1 1 15 15 GLN H H 1 7.57 0.02 . 1 . . . . . . . . . 4997 3 114 . 1 1 15 15 GLN HA H 1 4.01 0.02 . 1 . . . . . . . . . 4997 3 115 . 1 1 15 15 GLN HG2 H 1 2.48 0.02 . 2 . . . . . . . . . 4997 3 116 . 1 1 15 15 GLN HG3 H 1 2.41 0.02 . 2 . . . . . . . . . 4997 3 117 . 1 1 15 15 GLN HE21 H 1 7.49 0.02 . 2 . . . . . . . . . 4997 3 118 . 1 1 15 15 GLN HE22 H 1 6.95 0.02 . 2 . . . . . . . . . 4997 3 119 . 1 1 15 15 GLN CA C 13 58.65 0.02 . 1 . . . . . . . . . 4997 3 120 . 1 1 15 15 GLN CB C 13 28.00 0.02 . 1 . . . . . . . . . 4997 3 121 . 1 1 16 16 LEU H H 1 7.98 0.02 . 1 . . . . . . . . . 4997 3 122 . 1 1 16 16 LEU HA H 1 4.18 0.02 . 1 . . . . . . . . . 4997 3 123 . 1 1 16 16 LEU HB2 H 1 1.98 0.02 . 2 . . . . . . . . . 4997 3 124 . 1 1 16 16 LEU HB3 H 1 1.79 0.02 . 2 . . . . . . . . . 4997 3 125 . 1 1 16 16 LEU HG H 1 1.59 0.02 . 1 . . . . . . . . . 4997 3 126 . 1 1 16 16 LEU HD11 H 1 0.88 0.02 . 2 . . . . . . . . . 4997 3 127 . 1 1 16 16 LEU HD12 H 1 0.88 0.02 . 2 . . . . . . . . . 4997 3 128 . 1 1 16 16 LEU HD13 H 1 0.88 0.02 . 2 . . . . . . . . . 4997 3 129 . 1 1 16 16 LEU HD21 H 1 0.83 0.02 . 2 . . . . . . . . . 4997 3 130 . 1 1 16 16 LEU HD22 H 1 0.83 0.02 . 2 . . . . . . . . . 4997 3 131 . 1 1 16 16 LEU HD23 H 1 0.83 0.02 . 2 . . . . . . . . . 4997 3 132 . 1 1 16 16 LEU CA C 13 58.48 0.02 . 1 . . . . . . . . . 4997 3 133 . 1 1 17 17 GLU H H 1 8.21 0.02 . 1 . . . . . . . . . 4997 3 134 . 1 1 17 17 GLU HA H 1 4.20 0.02 . 1 . . . . . . . . . 4997 3 135 . 1 1 17 17 GLU HB2 H 1 2.14 0.02 . 2 . . . . . . . . . 4997 3 136 . 1 1 17 17 GLU HB3 H 1 2.08 0.02 . 2 . . . . . . . . . 4997 3 137 . 1 1 17 17 GLU HG2 H 1 2.57 0.02 . 2 . . . . . . . . . 4997 3 138 . 1 1 17 17 GLU HG3 H 1 2.43 0.02 . 2 . . . . . . . . . 4997 3 139 . 1 1 17 17 GLU CA C 13 58.43 0.02 . 1 . . . . . . . . . 4997 3 140 . 1 1 17 17 GLU CG C 13 33.41 0.02 . 1 . . . . . . . . . 4997 3 141 . 1 1 18 18 ASN H H 1 7.48 0.02 . 1 . . . . . . . . . 4997 3 142 . 1 1 18 18 ASN HA H 1 4.47 0.02 . 1 . . . . . . . . . 4997 3 143 . 1 1 18 18 ASN HB2 H 1 2.65 0.02 . 2 . . . . . . . . . 4997 3 144 . 1 1 18 18 ASN HB3 H 1 2.57 0.02 . 2 . . . . . . . . . 4997 3 145 . 1 1 18 18 ASN HD21 H 1 7.20 0.02 . 2 . . . . . . . . . 4997 3 146 . 1 1 18 18 ASN CA C 13 60.49 0.02 . 1 . . . . . . . . . 4997 3 147 . 1 1 18 18 ASN CB C 13 39.06 0.02 . 1 . . . . . . . . . 4997 3 148 . 1 1 19 19 TYR H H 1 8.01 0.02 . 1 . . . . . . . . . 4997 3 149 . 1 1 19 19 TYR HA H 1 4.51 0.02 . 1 . . . . . . . . . 4997 3 150 . 1 1 19 19 TYR HB2 H 1 3.39 0.02 . 2 . . . . . . . . . 4997 3 151 . 1 1 19 19 TYR HB3 H 1 3.06 0.02 . 2 . . . . . . . . . 4997 3 152 . 1 1 19 19 TYR HD1 H 1 7.34 0.02 . 3 . . . . . . . . . 4997 3 153 . 1 1 19 19 TYR HE1 H 1 6.83 0.02 . 3 . . . . . . . . . 4997 3 154 . 1 1 19 19 TYR CA C 13 55.42 0.02 . 1 . . . . . . . . . 4997 3 155 . 1 1 19 19 TYR CB C 13 38.52 0.02 . 1 . . . . . . . . . 4997 3 156 . 1 1 19 19 TYR CD1 C 13 130.76 0.02 . 3 . . . . . . . . . 4997 3 157 . 1 1 19 19 TYR CE1 C 13 118.27 0.02 . 3 . . . . . . . . . 4997 3 158 . 1 1 20 20 CYS H H 1 7.46 0.02 . 1 . . . . . . . . . 4997 3 159 . 1 1 20 20 CYS HA H 1 4.87 0.02 . 1 . . . . . . . . . 4997 3 160 . 1 1 20 20 CYS HB2 H 1 3.28 0.02 . 2 . . . . . . . . . 4997 3 161 . 1 1 20 20 CYS HB3 H 1 2.89 0.02 . 2 . . . . . . . . . 4997 3 162 . 1 1 20 20 CYS CA C 13 54.93 0.02 . 1 . . . . . . . . . 4997 3 163 . 1 1 21 21 ASN H H 1 8.13 0.02 . 1 . . . . . . . . . 4997 3 164 . 1 1 21 21 ASN HA H 1 4.66 0.02 . 1 . . . . . . . . . 4997 3 165 . 1 1 21 21 ASN HB2 H 1 2.87 0.02 . 2 . . . . . . . . . 4997 3 166 . 1 1 21 21 ASN HB3 H 1 2.76 0.02 . 2 . . . . . . . . . 4997 3 167 . 1 1 21 21 ASN HD21 H 1 7.48 0.02 . 2 . . . . . . . . . 4997 3 168 . 1 1 21 21 ASN CA C 13 56.82 0.02 . 1 . . . . . . . . . 4997 3 169 . 1 1 21 21 ASN CB C 13 39.27 0.02 . 1 . . . . . . . . . 4997 3 stop_ save_ save_CS_4 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode CS_4 _Assigned_chem_shift_list.Entry_ID 4997 _Assigned_chem_shift_list.ID 4 _Assigned_chem_shift_list.Sample_condition_list_ID 2 _Assigned_chem_shift_list.Sample_condition_list_label $cond_TFE _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 'COSY with DQF' 2 $sample_2 . 4997 4 2 'TOCSY/NOESY with WaterGate' 2 $sample_2 . 4997 4 3 'HSQC: Gradient enhanced' 2 $sample_2 . 4997 4 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 4.33 0.02 . 1 . . . . . . . . . 4997 4 2 . 2 2 1 1 PHE HB2 H 1 3.27 0.02 . 2 . . . . . . . . . 4997 4 3 . 2 2 1 1 PHE HB3 H 1 3.2 0.02 . 2 . . . . . . . . . 4997 4 4 . 2 2 1 1 PHE HD1 H 1 7.32 0.02 . 3 . . . . . . . . . 4997 4 5 . 2 2 1 1 PHE HE1 H 1 7.38 0.02 . 3 . . . . . . . . . 4997 4 6 . 2 2 1 1 PHE HZ H 1 7.42 0.02 . 1 . . . . . . . . . 4997 4 7 . 2 2 1 1 PHE CA C 13 57.41 0.02 . 1 . . . . . . . . . 4997 4 8 . 2 2 1 1 PHE CB C 13 39.85 0.02 . 1 . . . . . . . . . 4997 4 9 . 2 2 1 1 PHE CD1 C 13 132.24 0.02 . 3 . . . . . . . . . 4997 4 10 . 2 2 1 1 PHE CE1 C 13 131.97 0.02 . 3 . . . . . . . . . 4997 4 11 . 2 2 2 2 VAL H H 1 8.17 0.02 . 1 . . . . . . . . . 4997 4 12 . 2 2 2 2 VAL HA H 1 4.14 0.02 . 1 . . . . . . . . . 4997 4 13 . 2 2 2 2 VAL HB H 1 2.01 0.02 . 1 . . . . . . . . . 4997 4 14 . 2 2 2 2 VAL HG11 H 1 0.92 0.02 . 2 . . . . . . . . . 4997 4 15 . 2 2 2 2 VAL HG12 H 1 0.92 0.02 . 2 . . . . . . . . . 4997 4 16 . 2 2 2 2 VAL HG13 H 1 0.92 0.02 . 2 . . . . . . . . . 4997 4 17 . 2 2 2 2 VAL CA C 13 62.51 0.02 . 1 . . . . . . . . . 4997 4 18 . 2 2 3 3 ASN H H 1 8.37 0.02 . 1 . . . . . . . . . 4997 4 19 . 2 2 3 3 ASN HA H 1 4.73 0.02 . 1 . . . . . . . . . 4997 4 20 . 2 2 3 3 ASN HB2 H 1 2.83 0.02 . 2 . . . . . . . . . 4997 4 21 . 2 2 3 3 ASN HB3 H 1 2.78 0.02 . 2 . . . . . . . . . 4997 4 22 . 2 2 3 3 ASN HD21 H 1 7.57 0.02 . 2 . . . . . . . . . 4997 4 23 . 2 2 3 3 ASN HD22 H 1 6.88 0.02 . 2 . . . . . . . . . 4997 4 24 . 2 2 3 3 ASN CA C 13 56.63 0.02 . 1 . . . . . . . . . 4997 4 25 . 2 2 3 3 ASN CB C 13 39.03 0.02 . 1 . . . . . . . . . 4997 4 26 . 2 2 4 4 GLN H H 1 8.39 0.02 . 1 . . . . . . . . . 4997 4 27 . 2 2 4 4 GLN HA H 1 4.41 0.02 . 1 . . . . . . . . . 4997 4 28 . 2 2 4 4 GLN HB2 H 1 2.15 0.02 . 2 . . . . . . . . . 4997 4 29 . 2 2 4 4 GLN HB3 H 1 1.92 0.02 . 2 . . . . . . . . . 4997 4 30 . 2 2 4 4 GLN HG2 H 1 2.32 0.02 . 2 . . . . . . . . . 4997 4 31 . 2 2 4 4 GLN HG3 H 1 2.26 0.02 . 2 . . . . . . . . . 4997 4 32 . 2 2 4 4 GLN HE21 H 1 7.27 0.02 . 2 . . . . . . . . . 4997 4 33 . 2 2 4 4 GLN HE22 H 1 6.69 0.02 . 2 . . . . . . . . . 4997 4 34 . 2 2 4 4 GLN CA C 13 56.5 0.02 . 1 . . . . . . . . . 4997 4 35 . 2 2 4 4 GLN CB C 13 31.86 0.02 . 1 . . . . . . . . . 4997 4 36 . 2 2 5 5 HIS H H 1 8.57 0.02 . 1 . . . . . . . . . 4997 4 37 . 2 2 5 5 HIS HA H 1 4.58 0.02 . 1 . . . . . . . . . 4997 4 38 . 2 2 5 5 HIS HB2 H 1 3.58 0.02 . 2 . . . . . . . . . 4997 4 39 . 2 2 5 5 HIS HB3 H 1 3.32 0.02 . 2 . . . . . . . . . 4997 4 40 . 2 2 5 5 HIS HD2 H 1 7.42 0.02 . 1 . . . . . . . . . 4997 4 41 . 2 2 5 5 HIS HE1 H 1 8.56 0.02 . 1 . . . . . . . . . 4997 4 42 . 2 2 5 5 HIS CA C 13 57.7 0.02 . 1 . . . . . . . . . 4997 4 43 . 2 2 5 5 HIS CB C 13 28.57 0.02 . 1 . . . . . . . . . 4997 4 44 . 2 2 5 5 HIS CD2 C 13 120.72 0.02 . 1 . . . . . . . . . 4997 4 45 . 2 2 5 5 HIS CE1 C 13 136.23 0.02 . 1 . . . . . . . . . 4997 4 46 . 2 2 6 6 LEU H H 1 8.76 0.02 . 1 . . . . . . . . . 4997 4 47 . 2 2 6 6 LEU HA H 1 4.48 0.02 . 1 . . . . . . . . . 4997 4 48 . 2 2 6 6 LEU HB2 H 1 1.78 0.02 . 2 . . . . . . . . . 4997 4 49 . 2 2 6 6 LEU HB3 H 1 1.62 0.02 . 2 . . . . . . . . . 4997 4 50 . 2 2 6 6 LEU HG H 1 1.2 0.02 . 1 . . . . . . . . . 4997 4 51 . 2 2 6 6 LEU HD11 H 1 0.83 0.02 . 2 . . . . . . . . . 4997 4 52 . 2 2 6 6 LEU HD12 H 1 0.83 0.02 . 2 . . . . . . . . . 4997 4 53 . 2 2 6 6 LEU HD13 H 1 0.83 0.02 . 2 . . . . . . . . . 4997 4 54 . 2 2 6 6 LEU HD21 H 1 0.93 0.02 . 2 . . . . . . . . . 4997 4 55 . 2 2 6 6 LEU HD22 H 1 0.93 0.02 . 2 . . . . . . . . . 4997 4 56 . 2 2 6 6 LEU HD23 H 1 0.93 0.02 . 2 . . . . . . . . . 4997 4 57 . 2 2 6 6 LEU CA C 13 59.42 0.02 . 1 . . . . . . . . . 4997 4 58 . 2 2 7 7 CYS H H 1 8.25 0.02 . 1 . . . . . . . . . 4997 4 59 . 2 2 7 7 CYS HA H 1 4.46 0.02 . 1 . . . . . . . . . 4997 4 60 . 2 2 7 7 CYS HB2 H 1 3.18 0.02 . 2 . . . . . . . . . 4997 4 61 . 2 2 7 7 CYS HB3 H 1 3.07 0.02 . 2 . . . . . . . . . 4997 4 62 . 2 2 7 7 CYS CA C 13 56.01 0.02 . 1 . . . . . . . . . 4997 4 63 . 2 2 8 8 GLY H H 1 8.92 0.02 . 1 . . . . . . . . . 4997 4 64 . 2 2 8 8 GLY HA2 H 1 3.99 0.02 . 2 . . . . . . . . . 4997 4 65 . 2 2 8 8 GLY HA3 H 1 3.79 0.02 . 2 . . . . . . . . . 4997 4 66 . 2 2 8 8 GLY CA C 13 45.41 0.02 . 1 . . . . . . . . . 4997 4 67 . 2 2 9 9 SER H H 1 8.75 0.02 . 1 . . . . . . . . . 4997 4 68 . 2 2 9 9 SER HA H 1 4.08 0.02 . 1 . . . . . . . . . 4997 4 69 . 2 2 9 9 SER HB2 H 1 3.92 0.02 . 2 . . . . . . . . . 4997 4 70 . 2 2 9 9 SER CA C 13 59.64 0.02 . 1 . . . . . . . . . 4997 4 71 . 2 2 9 9 SER CB C 13 64.33 0.02 . 1 . . . . . . . . . 4997 4 72 . 2 2 10 10 HIS H H 1 7.93 0.02 . 1 . . . . . . . . . 4997 4 73 . 2 2 10 10 HIS HA H 1 4.55 0.02 . 1 . . . . . . . . . 4997 4 74 . 2 2 10 10 HIS HB2 H 1 3.53 0.02 . 2 . . . . . . . . . 4997 4 75 . 2 2 10 10 HIS HB3 H 1 3.33 0.02 . 2 . . . . . . . . . 4997 4 76 . 2 2 10 10 HIS HD2 H 1 7.77 0.02 . 1 . . . . . . . . . 4997 4 77 . 2 2 10 10 HIS HE1 H 1 8.66 0.02 . 1 . . . . . . . . . 4997 4 78 . 2 2 10 10 HIS CA C 13 58.06 0.02 . 1 . . . . . . . . . 4997 4 79 . 2 2 10 10 HIS CB C 13 28.19 0.02 . 1 . . . . . . . . . 4997 4 80 . 2 2 10 10 HIS CD2 C 13 119.93 0.02 . 1 . . . . . . . . . 4997 4 81 . 2 2 10 10 HIS CE1 C 13 136.53 0.02 . 1 . . . . . . . . . 4997 4 82 . 2 2 11 11 LEU HA H 1 3.94 0.02 . 1 . . . . . . . . . 4997 4 83 . 2 2 11 11 LEU CA C 13 58.25 0.02 . 1 . . . . . . . . . 4997 4 84 . 2 2 12 12 VAL H H 1 7.16 0.02 . 1 . . . . . . . . . 4997 4 85 . 2 2 12 12 VAL HA H 1 3.41 0.02 . 1 . . . . . . . . . 4997 4 86 . 2 2 12 12 VAL HB H 1 2.07 0.02 . 1 . . . . . . . . . 4997 4 87 . 2 2 12 12 VAL HG11 H 1 0.96 0.02 . 2 . . . . . . . . . 4997 4 88 . 2 2 12 12 VAL HG12 H 1 0.96 0.02 . 2 . . . . . . . . . 4997 4 89 . 2 2 12 12 VAL HG13 H 1 0.96 0.02 . 2 . . . . . . . . . 4997 4 90 . 2 2 12 12 VAL CA C 13 67.17 0.02 . 1 . . . . . . . . . 4997 4 91 . 2 2 12 12 VAL CB C 13 28.21 0.02 . 1 . . . . . . . . . 4997 4 92 . 2 2 13 13 GLU H H 1 7.88 0.02 . 1 . . . . . . . . . 4997 4 93 . 2 2 13 13 GLU HA H 1 4.01 0.02 . 1 . . . . . . . . . 4997 4 94 . 2 2 13 13 GLU HB2 H 1 2.24 0.02 . 2 . . . . . . . . . 4997 4 95 . 2 2 13 13 GLU HB3 H 1 2.11 0.02 . 2 . . . . . . . . . 4997 4 96 . 2 2 13 13 GLU HG2 H 1 2.6 0.02 . 2 . . . . . . . . . 4997 4 97 . 2 2 13 13 GLU HG3 H 1 2.44 0.02 . 2 . . . . . . . . . 4997 4 98 . 2 2 13 13 GLU CA C 13 59.01 0.02 . 1 . . . . . . . . . 4997 4 99 . 2 2 13 13 GLU CB C 13 29.45 0.02 . 1 . . . . . . . . . 4997 4 100 . 2 2 14 14 ALA H H 1 7.86 0.02 . 1 . . . . . . . . . 4997 4 101 . 2 2 14 14 ALA HA H 1 4.09 0.02 . 1 . . . . . . . . . 4997 4 102 . 2 2 14 14 ALA HB1 H 1 1.52 0.02 . 1 . . . . . . . . . 4997 4 103 . 2 2 14 14 ALA HB2 H 1 1.52 0.02 . 1 . . . . . . . . . 4997 4 104 . 2 2 14 14 ALA HB3 H 1 1.52 0.02 . 1 . . . . . . . . . 4997 4 105 . 2 2 14 14 ALA CA C 13 55.66 0.02 . 1 . . . . . . . . . 4997 4 106 . 2 2 14 14 ALA CB C 13 18.52 0.02 . 1 . . . . . . . . . 4997 4 107 . 2 2 15 15 LEU H H 1 8.23 0.02 . 1 . . . . . . . . . 4997 4 108 . 2 2 15 15 LEU HA H 1 3.94 0.02 . 1 . . . . . . . . . 4997 4 109 . 2 2 15 15 LEU HB2 H 1 1.54 0.02 . 2 . . . . . . . . . 4997 4 110 . 2 2 15 15 LEU HB3 H 1 1.5 0.02 . 2 . . . . . . . . . 4997 4 111 . 2 2 15 15 LEU HG H 1 1.6 0.02 . 1 . . . . . . . . . 4997 4 112 . 2 2 15 15 LEU HD11 H 1 0.76 0.02 . 2 . . . . . . . . . 4997 4 113 . 2 2 15 15 LEU HD12 H 1 0.76 0.02 . 2 . . . . . . . . . 4997 4 114 . 2 2 15 15 LEU HD13 H 1 0.76 0.02 . 2 . . . . . . . . . 4997 4 115 . 2 2 15 15 LEU HD21 H 1 0.61 0.02 . 2 . . . . . . . . . 4997 4 116 . 2 2 15 15 LEU HD22 H 1 0.61 0.02 . 2 . . . . . . . . . 4997 4 117 . 2 2 15 15 LEU HD23 H 1 0.61 0.02 . 2 . . . . . . . . . 4997 4 118 . 2 2 15 15 LEU CA C 13 62.8 0.02 . 1 . . . . . . . . . 4997 4 119 . 2 2 15 15 LEU CD1 C 13 24.34 0.02 . 2 . . . . . . . . . 4997 4 120 . 2 2 15 15 LEU CD2 C 13 25.58 0.02 . 2 . . . . . . . . . 4997 4 121 . 2 2 16 16 TYR H H 1 8.36 0.02 . 1 . . . . . . . . . 4997 4 122 . 2 2 16 16 TYR HA H 1 4.2 0.02 . 1 . . . . . . . . . 4997 4 123 . 2 2 16 16 TYR HB2 H 1 3.19 0.02 . 2 . . . . . . . . . 4997 4 124 . 2 2 16 16 TYR HD1 H 1 7.14 0.02 . 3 . . . . . . . . . 4997 4 125 . 2 2 16 16 TYR HE1 H 1 6.9 0.02 . 3 . . . . . . . . . 4997 4 126 . 2 2 16 16 TYR CA C 13 61.85 0.02 . 1 . . . . . . . . . 4997 4 127 . 2 2 16 16 TYR CB C 13 38.09 0.02 . 1 . . . . . . . . . 4997 4 128 . 2 2 16 16 TYR CD1 C 13 133 0.02 . 3 . . . . . . . . . 4997 4 129 . 2 2 16 16 TYR CE1 C 13 118.14 0.02 . 3 . . . . . . . . . 4997 4 130 . 2 2 17 17 LEU H H 1 8.12 0.02 . 1 . . . . . . . . . 4997 4 131 . 2 2 17 17 LEU HA H 1 4.07 0.02 . 1 . . . . . . . . . 4997 4 132 . 2 2 17 17 LEU HB2 H 1 1.98 0.02 . 2 . . . . . . . . . 4997 4 133 . 2 2 17 17 LEU HB3 H 1 1.92 0.02 . 2 . . . . . . . . . 4997 4 134 . 2 2 17 17 LEU HG H 1 1.63 0.02 . 1 . . . . . . . . . 4997 4 135 . 2 2 17 17 LEU HD11 H 1 0.93 0.02 . 2 . . . . . . . . . 4997 4 136 . 2 2 17 17 LEU HD12 H 1 0.93 0.02 . 2 . . . . . . . . . 4997 4 137 . 2 2 17 17 LEU HD13 H 1 0.93 0.02 . 2 . . . . . . . . . 4997 4 138 . 2 2 17 17 LEU CA C 13 58.14 0.02 . 1 . . . . . . . . . 4997 4 139 . 2 2 18 18 VAL H H 1 8.82 0.02 . 1 . . . . . . . . . 4997 4 140 . 2 2 18 18 VAL HA H 1 3.77 0.02 . 1 . . . . . . . . . 4997 4 141 . 2 2 18 18 VAL HB H 1 2.13 0.02 . 1 . . . . . . . . . 4997 4 142 . 2 2 18 18 VAL HG11 H 1 1.06 0.02 . 2 . . . . . . . . . 4997 4 143 . 2 2 18 18 VAL HG12 H 1 1.06 0.02 . 2 . . . . . . . . . 4997 4 144 . 2 2 18 18 VAL HG13 H 1 1.06 0.02 . 2 . . . . . . . . . 4997 4 145 . 2 2 18 18 VAL HG21 H 1 0.91 0.02 . 2 . . . . . . . . . 4997 4 146 . 2 2 18 18 VAL HG22 H 1 0.91 0.02 . 2 . . . . . . . . . 4997 4 147 . 2 2 18 18 VAL HG23 H 1 0.91 0.02 . 2 . . . . . . . . . 4997 4 148 . 2 2 18 18 VAL CA C 13 66 0.02 . 1 . . . . . . . . . 4997 4 149 . 2 2 18 18 VAL CB C 13 32.65 0.02 . 1 . . . . . . . . . 4997 4 150 . 2 2 19 19 CYS H H 1 8.82 0.02 . 1 . . . . . . . . . 4997 4 151 . 2 2 19 19 CYS HA H 1 4.83 0.02 . 1 . . . . . . . . . 4997 4 152 . 2 2 19 19 CYS HB2 H 1 3.26 0.02 . 2 . . . . . . . . . 4997 4 153 . 2 2 19 19 CYS HB3 H 1 3.03 0.02 . 2 . . . . . . . . . 4997 4 154 . 2 2 19 19 CYS CA C 13 54.27 0.02 . 1 . . . . . . . . . 4997 4 155 . 2 2 20 20 GLY H H 1 7.82 0.02 . 1 . . . . . . . . . 4997 4 156 . 2 2 20 20 GLY HA2 H 1 3.94 0.02 . 2 . . . . . . . . . 4997 4 157 . 2 2 20 20 GLY CA C 13 46.76 0.02 . 1 . . . . . . . . . 4997 4 158 . 2 2 21 21 GLU H H 1 8.43 0.02 . 1 . . . . . . . . . 4997 4 159 . 2 2 21 21 GLU HA H 1 4.23 0.02 . 1 . . . . . . . . . 4997 4 160 . 2 2 21 21 GLU HB2 H 1 2.24 0.02 . 2 . . . . . . . . . 4997 4 161 . 2 2 21 21 GLU HB3 H 1 2.13 0.02 . 2 . . . . . . . . . 4997 4 162 . 2 2 21 21 GLU HG2 H 1 2.56 0.02 . 2 . . . . . . . . . 4997 4 163 . 2 2 21 21 GLU HG3 H 1 2.51 0.02 . 2 . . . . . . . . . 4997 4 164 . 2 2 21 21 GLU CA C 13 57.17 0.02 . 1 . . . . . . . . . 4997 4 165 . 2 2 21 21 GLU CB C 13 28.23 0.02 . 1 . . . . . . . . . 4997 4 166 . 2 2 22 22 ARG H H 1 7.96 0.02 . 1 . . . . . . . . . 4997 4 167 . 2 2 22 22 ARG HA H 1 4.22 0.02 . 1 . . . . . . . . . 4997 4 168 . 2 2 22 22 ARG HB2 H 1 2.06 0.02 . 2 . . . . . . . . . 4997 4 169 . 2 2 22 22 ARG HB3 H 1 2.03 0.02 . 2 . . . . . . . . . 4997 4 170 . 2 2 22 22 ARG HG2 H 1 1.84 0.02 . 2 . . . . . . . . . 4997 4 171 . 2 2 22 22 ARG HG3 H 1 1.78 0.02 . 2 . . . . . . . . . 4997 4 172 . 2 2 22 22 ARG HD2 H 1 3.29 0.02 . 2 . . . . . . . . . 4997 4 173 . 2 2 22 22 ARG HE H 1 7.32 0.02 . 1 . . . . . . . . . 4997 4 174 . 2 2 22 22 ARG CA C 13 57.58 0.02 . 1 . . . . . . . . . 4997 4 175 . 2 2 22 22 ARG CD C 13 43.82 0.02 . 1 . . . . . . . . . 4997 4 176 . 2 2 23 23 GLY H H 1 7.75 0.02 . 1 . . . . . . . . . 4997 4 177 . 2 2 23 23 GLY HA2 H 1 3.99 0.02 . 2 . . . . . . . . . 4997 4 178 . 2 2 23 23 GLY HA3 H 1 3.87 0.02 . 2 . . . . . . . . . 4997 4 179 . 2 2 23 23 GLY CA C 13 47.05 0.02 . 1 . . . . . . . . . 4997 4 180 . 2 2 24 24 PHE H H 1 7.68 0.02 . 1 . . . . . . . . . 4997 4 181 . 2 2 24 24 PHE HA H 1 4.77 0.02 . 1 . . . . . . . . . 4997 4 182 . 2 2 24 24 PHE HB2 H 1 3.15 0.02 . 2 . . . . . . . . . 4997 4 183 . 2 2 24 24 PHE HB3 H 1 2.99 0.02 . 2 . . . . . . . . . 4997 4 184 . 2 2 24 24 PHE HD1 H 1 7.16 0.02 . 3 . . . . . . . . . 4997 4 185 . 2 2 24 24 PHE HE1 H 1 7 0.02 . 3 . . . . . . . . . 4997 4 186 . 2 2 24 24 PHE CB C 13 40.46 0.02 . 1 . . . . . . . . . 4997 4 187 . 2 2 24 24 PHE CD1 C 13 132.21 0.02 . 3 . . . . . . . . . 4997 4 188 . 2 2 24 24 PHE CE1 C 13 131.21 0.02 . 3 . . . . . . . . . 4997 4 189 . 2 2 25 25 PHE H H 1 8.13 0.02 . 1 . . . . . . . . . 4997 4 190 . 2 2 25 25 PHE HA H 1 4.63 0.02 . 1 . . . . . . . . . 4997 4 191 . 2 2 25 25 PHE HB2 H 1 3.07 0.02 . 2 . . . . . . . . . 4997 4 192 . 2 2 25 25 PHE HB3 H 1 3.02 0.02 . 2 . . . . . . . . . 4997 4 193 . 2 2 25 25 PHE HD1 H 1 7.23 0.02 . 3 . . . . . . . . . 4997 4 194 . 2 2 25 25 PHE HE1 H 1 7.32 0.02 . 3 . . . . . . . . . 4997 4 195 . 2 2 25 25 PHE HZ H 1 7.27 0.02 . 1 . . . . . . . . . 4997 4 196 . 2 2 25 25 PHE CA C 13 56.97 0.02 . 1 . . . . . . . . . 4997 4 197 . 2 2 25 25 PHE CB C 13 40.1 0.02 . 1 . . . . . . . . . 4997 4 198 . 2 2 25 25 PHE CD1 C 13 131.97 0.02 . 3 . . . . . . . . . 4997 4 199 . 2 2 25 25 PHE CE1 C 13 133.58 0.02 . 3 . . . . . . . . . 4997 4 200 . 2 2 26 26 TYR H H 1 7.86 0.02 . 1 . . . . . . . . . 4997 4 201 . 2 2 26 26 TYR HA H 1 4.76 0.02 . 1 . . . . . . . . . 4997 4 202 . 2 2 26 26 TYR HB2 H 1 3.02 0.02 . 2 . . . . . . . . . 4997 4 203 . 2 2 26 26 TYR HB3 H 1 2.86 0.02 . 2 . . . . . . . . . 4997 4 204 . 2 2 26 26 TYR CA C 13 56.01 0.02 . 1 . . . . . . . . . 4997 4 205 . 2 2 26 26 TYR CB C 13 39.2 0.02 . 1 . . . . . . . . . 4997 4 206 . 2 2 26 26 TYR CE1 C 13 118.08 0.02 . 3 . . . . . . . . . 4997 4 207 . 2 2 27 27 PRO HA H 1 4.45 0.02 . 1 . . . . . . . . . 4997 4 208 . 2 2 27 27 PRO HB2 H 1 2.22 0.02 . 2 . . . . . . . . . 4997 4 209 . 2 2 27 27 PRO HG2 H 1 1.97 0.02 . 2 . . . . . . . . . 4997 4 210 . 2 2 27 27 PRO HG3 H 1 1.92 0.02 . 2 . . . . . . . . . 4997 4 211 . 2 2 27 27 PRO HD2 H 1 3.51 0.02 . 2 . . . . . . . . . 4997 4 212 . 2 2 27 27 PRO HD3 H 1 3.26 0.02 . 2 . . . . . . . . . 4997 4 213 . 2 2 27 27 PRO CA C 13 55.44 0.02 . 1 . . . . . . . . . 4997 4 214 . 2 2 27 27 PRO CD C 13 50.54 0.02 . 1 . . . . . . . . . 4997 4 215 . 2 2 28 28 THR H H 1 7.89 0.02 . 1 . . . . . . . . . 4997 4 216 . 2 2 28 28 THR HA H 1 4.4 0.02 . 1 . . . . . . . . . 4997 4 217 . 2 2 28 28 THR HB H 1 4.29 0.02 . 1 . . . . . . . . . 4997 4 218 . 2 2 28 28 THR HG21 H 1 1.27 0.02 . 1 . . . . . . . . . 4997 4 219 . 2 2 28 28 THR HG22 H 1 1.27 0.02 . 1 . . . . . . . . . 4997 4 220 . 2 2 28 28 THR HG23 H 1 1.27 0.02 . 1 . . . . . . . . . 4997 4 221 . 2 2 28 28 THR CA C 13 61.86 0.02 . 1 . . . . . . . . . 4997 4 222 . 2 2 28 28 THR CB C 13 70.14 0.02 . 1 . . . . . . . . . 4997 4 223 . 2 2 28 28 THR CG2 C 13 21.64 0.02 . 1 . . . . . . . . . 4997 4 224 . 2 2 29 29 LYS H H 1 8.16 0.02 . 1 . . . . . . . . . 4997 4 225 . 2 2 29 29 LYS HA H 1 4.49 0.02 . 1 . . . . . . . . . 4997 4 226 . 2 2 29 29 LYS HB2 H 1 1.95 0.02 . 2 . . . . . . . . . 4997 4 227 . 2 2 29 29 LYS HB3 H 1 1.82 0.02 . 2 . . . . . . . . . 4997 4 228 . 2 2 29 29 LYS HG2 H 1 1.51 0.02 . 2 . . . . . . . . . 4997 4 229 . 2 2 29 29 LYS HD2 H 1 1.74 0.02 . 2 . . . . . . . . . 4997 4 230 . 2 2 29 29 LYS HE2 H 1 3.01 0.02 . 2 . . . . . . . . . 4997 4 231 . 2 2 29 29 LYS HZ1 H 1 7.57 0.02 . 1 . . . . . . . . . 4997 4 232 . 2 2 29 29 LYS HZ2 H 1 7.57 0.02 . 1 . . . . . . . . . 4997 4 233 . 2 2 29 29 LYS HZ3 H 1 7.57 0.02 . 1 . . . . . . . . . 4997 4 234 . 2 2 29 29 LYS CA C 13 55.44 0.02 . 1 . . . . . . . . . 4997 4 235 . 2 2 29 29 LYS CB C 13 33.53 0.02 . 1 . . . . . . . . . 4997 4 236 . 2 2 29 29 LYS CE C 13 42.38 0.02 . 1 . . . . . . . . . 4997 4 237 . 2 2 30 30 THR H H 1 7.98 0.02 . 1 . . . . . . . . . 4997 4 238 . 2 2 30 30 THR HA H 1 4.38 0.02 . 1 . . . . . . . . . 4997 4 239 . 2 2 30 30 THR HG21 H 1 1.22 0.02 . 1 . . . . . . . . . 4997 4 240 . 2 2 30 30 THR HG22 H 1 1.22 0.02 . 1 . . . . . . . . . 4997 4 241 . 2 2 30 30 THR HG23 H 1 1.22 0.02 . 1 . . . . . . . . . 4997 4 242 . 2 2 30 30 THR CA C 13 61.85 0.02 . 1 . . . . . . . . . 4997 4 243 . 2 2 30 30 THR CB C 13 70.52 0.02 . 1 . . . . . . . . . 4997 4 244 . 2 2 30 30 THR CG2 C 13 21.85 0.02 . 1 . . . . . . . . . 4997 4 stop_ save_