data_1444 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 1444 _Entry.Title ; 2D 1H NMR Studies of Monomeric Insulin ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-04-13 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Kerry Higgins . A. . 1444 2 David Craik . J. . 1444 3 Jon Hall . G. . 1444 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 1444 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 217 1444 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 5 . . 2010-06-14 . revision BMRB 'Complete natural source information' 1444 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1444 3 . . 1996-04-13 . revision BMRB 'Link to the Protein Data Bank added' 1444 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1444 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 1444 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 1444 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Higgins, Kerry A., Craik, David J., Hall, Jon G., "2D 1H NMR Studies of Monomeric Insulin," Biochem. Int. 22 (4), 627-637 (1990). ; _Citation.Title '2D 1H NMR Studies of Monomeric Insulin' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochem. Int.' _Citation.Journal_name_full . _Citation.Journal_volume 22 _Citation.Journal_issue 4 _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 627 _Citation.Page_last 637 _Citation.Year 1990 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Kerry Higgins . A. . 1444 1 2 David Craik . J. . 1444 1 3 Jon Hall . G. . 1444 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_insulin_B_chain _Assembly.Sf_category assembly _Assembly.Sf_framecode system_insulin_B_chain _Assembly.Entry_ID 1444 _Assembly.ID 1 _Assembly.Name 'insulin B chain' _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 . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'insulin B chain' 1 $insulin_B_chain . . . . . . . . . 1444 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'insulin B chain' system 1444 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_insulin_B_chain _Entity.Sf_category entity _Entity.Sf_framecode insulin_B_chain _Entity.Entry_ID 1444 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'insulin B chain' _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 ; FVNQHLCGSHLVEALYLVCG ERGFFYTPKA ; _Entity.Polymer_seq_one_letter_code ; FVNQHLCGSHLVEALYLVCG ERGFFYTPKA ; _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 . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-26 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 1023 . "insulin B chain" . . . . . 73.33 42 100.00 100.00 6.83e-06 . . . . 1444 1 2 no BMRB 4266 . [D-AlaB26]destetra(B27-B30)insulin-B26-amide . . . . . 83.33 47 100.00 100.00 3.10e-08 . . . . 1444 1 3 no PDB 1APH . "Conformational Changes In Cubic Insulin Crystals In The Ph Range 7-11" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 4 no PDB 1B17 . "Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 5.00 Coordinates)" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 5 no PDB 1B18 . "Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 5.53 Coordinates)" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 6 no PDB 1B19 . "Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 5.80 Coordinates)" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 7 no PDB 1B2A . "Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.00 Coordinates)" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 8 no PDB 1B2B . "Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.16 Coordinates)" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 9 no PDB 1B2C . "Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.26 Coordinates)" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 10 no PDB 1B2D . "Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.35 Coordinates)" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 11 no PDB 1B2E . "Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.50 Coordinates)" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 12 no PDB 1B2F . "Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.98 Coordinates)" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 13 no PDB 1B2G . "Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 9.00 Coordinates)" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 14 no PDB 1BPH . "Conformational Changes In Cubic Insulin Crystals In The Ph Range 7-11" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 15 no PDB 1BZV . "[d-Alab26]-Des(B27-B30)-Insulin-B26-Amide A Superpotent Single-Replacement Insulin Analogue, Nmr, Minimized Average Structure" . . . . . 83.33 26 100.00 100.00 3.66e-08 . . . . 1444 1 16 no PDB 1CPH . "Conformational Changes In Cubic Insulin Crystals In The Ph Range 7-11" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 17 no PDB 1DEI . "Desheptapeptide (B24-B30) Insulin" . . . . . 76.67 23 100.00 100.00 1.25e-06 . . . . 1444 1 18 no PDB 1DPH . "Conformational Changes In Cubic Insulin Crystals In The Ph Range 7-11" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 19 no PDB 1HIS . "Structure And Dynamics Of Des-Pentapeptide-Insulin In Solution: The Molten-Globule Hypothesis" . . . . . 83.33 25 100.00 100.00 3.65e-08 . . . . 1444 1 20 no PDB 1HTV . "Crystal Structure Of Destripeptide (B28-B30) Insulin" . . . . . 90.00 27 100.00 100.00 7.55e-10 . . . . 1444 1 21 no PDB 1LPH . "Lys(B28)pro(B29)-Human Insulin" . . . . . 90.00 30 100.00 100.00 6.34e-10 . . . . 1444 1 22 no PDB 1M5A . "Crystal Structure Of 2-Co(2+)-Insulin At 1.2a Resolution" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 23 no PDB 1MPJ . "X-Ray Crystallographic Studies On Hexameric Insulins In The Presence Of Helix-Stabilizing Agents, Thiocyanate, Methylparaben An" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 24 no PDB 1PID . "Bovine Despentapeptide Insulin" . . . . . 83.33 25 100.00 100.00 3.65e-08 . . . . 1444 1 25 no PDB 1SDB . "Porcine Desb1-2 Despentapeptide(B26-B30) Insulin" . . . . . 76.67 23 100.00 100.00 8.60e-07 . . . . 1444 1 26 no PDB 1UZ9 . "Crystallographic And Solution Studies Of N-Lithocholyl Insulin: A New Generation Of Prolonged-Acting Insulins." . . . . . 96.67 29 100.00 100.00 8.48e-12 . . . . 1444 1 27 no PDB 1WAV . "Crystal Structure Of Form B Monoclinic Crystal Of Insulin" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 28 no PDB 1XDA . "Structure Of Insulin" . . . . . 96.67 29 100.00 100.00 8.48e-12 . . . . 1444 1 29 no PDB 1ZNI . Insulin . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 30 no PDB 2A3G . "The Structure Of T6 Bovine Insulin" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 31 no PDB 2BN1 . "Insulin After A High Dose X-ray Burn" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 32 no PDB 2BN3 . "Insulin Before A High Dose X-Ray Burn" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 33 no PDB 2C8Q . "Insuline(1sec) And Uv Laser Excited Fluorescence" . . . . . 96.67 29 100.00 100.00 8.48e-12 . . . . 1444 1 34 no PDB 2C8R . "Insuline(60sec) And Uv Laser Excited Fluorescence" . . . . . 96.67 29 100.00 100.00 8.48e-12 . . . . 1444 1 35 no PDB 2CEU . "Despentapeptide Insulin In Acetic Acid (Ph 2)" . . . . . 83.33 25 100.00 100.00 3.65e-08 . . . . 1444 1 36 no PDB 2EFA . "Neutron Crystal Structure Of Cubic Insulin At Pd6.6" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 37 no PDB 2G4M . "Insulin Collected At 2.0 A Wavelength" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 38 no PDB 2INS . "The Structure Of Des-Phe B1 Bovine Insulin" . . . . . 96.67 29 100.00 100.00 9.86e-12 . . . . 1444 1 39 no PDB 2KJJ . "Dynamics Of Insulin Probed By 1h-Nmr Amide Proton Exchange A Flexibility Of The Receptor-Binding Surface" . . . . . 90.00 30 100.00 100.00 6.34e-10 . . . . 1444 1 40 no PDB 2M1D . "Biosynthetic Engineered B28k-b29p Human Insulin Monomer Structure In In Water/acetonitrile Solutions." . . . . . 90.00 30 100.00 100.00 6.34e-10 . . . . 1444 1 41 no PDB 2M1E . "Biosynthetic Engineered B28k-b29p Human Insulin Monomer Structure In In Water Solutions" . . . . . 90.00 30 100.00 100.00 6.34e-10 . . . . 1444 1 42 no PDB 2TCI . "X-Ray Crystallographic Studies On Hexameric Insulins In The Presence Of Helix-Stabilizing Agents, Thiocyanate, Methylparaben An" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 43 no PDB 2W44 . "Structure Deltaa1-a4 Insulin" . . . . . 96.67 29 100.00 100.00 8.48e-12 . . . . 1444 1 44 no PDB 2WBY . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Insulin" . . . . . 63.33 19 100.00 100.00 2.26e-03 . . . . 1444 1 45 no PDB 2WRU . "Semi-synthetic Highly Active Analogue Of Human Insulin Nmealab26-dti-nh2" . . . . . 83.33 26 100.00 100.00 3.66e-08 . . . . 1444 1 46 no PDB 2WRV . "Semi-Synthetic Highly Active Analogue Of Human Insulin Nmehisb26-Dti-Nh2" . . . . . 83.33 26 100.00 100.00 3.66e-08 . . . . 1444 1 47 no PDB 2WRW . "Semi-Synthetic Highly Active Analogue Of Human Insulin D- Prob26-Dti-Nh2" . . . . . 83.33 26 100.00 100.00 3.66e-08 . . . . 1444 1 48 no PDB 2WS4 . "Semi-Synthetic Analogue Of Human Insulin Prob26-Dti In Monomer Form" . . . . . 83.33 26 100.00 100.00 3.86e-08 . . . . 1444 1 49 no PDB 2WS7 . "Semi-Synthetic Analogue Of Human Insulin Prob26-Dti" . . . . . 83.33 26 100.00 100.00 3.86e-08 . . . . 1444 1 50 no PDB 2ZP6 . "Crystal Structure Of Bovine Insulin (Hexameric Form)" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 51 no PDB 2ZPP . "Neutron Crystal Structure Of Cubic Insulin At Pd9" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 52 no PDB 3E7Y . "Structure Of Human Insulin" . . . . . 96.67 29 100.00 100.00 8.48e-12 . . . . 1444 1 53 no PDB 3E7Z . "Structure Of Human Insulin" . . . . . 96.67 29 100.00 100.00 8.48e-12 . . . . 1444 1 54 no PDB 3FHP . "A Neutron Crystallographic Analysis Of A Porcine 2zn Insulin At 2.0 A Resolution" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 55 no PDB 3GKY . "The Structural Basis Of An Er Stress-Associated Bottleneck In A Protein Folding Landscape" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 56 no PDB 3I3Z . "Human Insulin" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 57 no PDB 3I40 . "Human Insulin" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 58 no PDB 3INS . "Structure Of Insulin. Results Of Joint Neutron And X-ray Refinement" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 59 no PDB 3MTH . "X-Ray Crystallographic Studies On Hexameric Insulins In The Presence Of Helix-Stabilizing Agents, Thiocyanate, Methylparaben An" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 60 no PDB 3RTO . "Acoustically Mounted Porcine Insulin Microcrystals Yield An X-Ray Sad Structure" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 61 no PDB 3T2A . "Tmao-Grown Cubic Insulin (Porcine)" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 62 no PDB 3W12 . "Insulin Receptor Ectodomain Construct Comprising Domains L1-cr In Complex With High-affinity Insulin Analogue [d-pro-b26]-dti-n" . . . . . 83.33 26 100.00 100.00 3.66e-08 . . . . 1444 1 63 no PDB 3W13 . "Insulin Receptor Ectodomain Construct Comprising Domains L1-cr In Complex With High-affinity Insulin Analogue [d-pro-b26]-dti-n" . . . . . 83.33 26 100.00 100.00 3.66e-08 . . . . 1444 1 64 no PDB 3W14 . "Insulin Receptor Ectodomain Construct Comprising Domains L1,cr,l2, Fniii-1 And Alphact Peptide In Complex With Bovine Insulin A" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 65 no PDB 4A7E . "X-Ray Crystal Structure Of Porcine Insulin Flash-Cooled At High Pressure" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 66 no PDB 4AJX . "Ligand Controlled Assembly Of Hexamers, Dihexamers, And Linear Multihexamer Structures By An Engineered Acylated Insulin" . . . . . 96.67 29 100.00 100.00 8.48e-12 . . . . 1444 1 67 no PDB 4AJZ . "Ligand Controlled Assembly Of Hexamers, Dihexamers, And Linear Multihexamer Structures By An Engineered Acylated Insulin" . . . . . 96.67 29 100.00 100.00 8.48e-12 . . . . 1444 1 68 no PDB 4AK0 . "Ligand Controlled Assembly Of Hexamers, Dihexamers, And Linear Multihexamer Structures By An Engineered Acylated Insulin" . . . . . 96.67 29 100.00 100.00 8.48e-12 . . . . 1444 1 69 no PDB 4AKJ . "Ligand Controlled Assembly Of Hexamers, Dihexamers, And Linear Multihexamer Structures By An Engineered Acylated Insulin" . . . . . 96.67 29 100.00 100.00 8.48e-12 . . . . 1444 1 70 no PDB 4BS3 . "Bovin Insulin Structure Determined By In Situ Crystal Analysis And Sulfur-sad Phasing At Room Temperature" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 71 no PDB 4E7T . "The Structure Of T6 Bovine Insulin" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 72 no PDB 4E7U . "The Structure Of T3r3 Bovine Insulin" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 73 no PDB 4E7V . "The Structure Of R6 Bovine Insulin" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 74 no PDB 4I5Y . "Insulin Protein Crystallization Via Langmuir-blodgett" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 75 no PDB 4I5Z . "Insulin Protein Crystallization Via Langmuir-blodgett" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 76 no PDB 4IDW . "Polycrystalline T6 Bovine Insulin: Anisotropic Lattice Evolution And Novel Structure Refinement Strategy" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 77 no PDB 4IHN . "High Resolution Insulin By Langmuir-blodgett Modified Hanging Drop Vapour Diffusion" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 78 no PDB 4INS . "The Structure Of 2zn Pig Insulin Crystals At 1.5 Angstroms Resolution" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 79 no PDB 4IYD . "Insulin Glargine Crystal Structure 1" . . . . . 96.67 29 100.00 100.00 8.48e-12 . . . . 1444 1 80 no PDB 4IYF . "Insulin Glargine Crystal Structure 2" . . . . . 96.67 29 100.00 100.00 8.48e-12 . . . . 1444 1 81 no PDB 4M4F . "Radiation Damage Study Of Cu T6-insulin - 0.01 Mgy" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 82 no PDB 4M4H . "Radiation Damage Study Of Cu T6-insulin - 0.06 Mgy" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 83 no PDB 4M4I . "Radiation Damage Study Of Cu T6-insulin - 0.12 Mgy" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 84 no PDB 4M4J . "Radiation Damage Study Of Cu T6-insulin - 0.30 Mgy" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 85 no PDB 4M4L . "The Structure Of Cu T6 Bovine Insulin" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 86 no PDB 4M4M . "The Structure Of Ni T6 Bovine Insulin" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 87 no PDB 4Q5Z . "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Insulin" . . . . . 63.33 19 100.00 100.00 2.26e-03 . . . . 1444 1 88 no PDB 7INS . "Structure Of Porcine Insulin Cocrystallized With Clupeine Z" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 89 no PDB 9INS . "Monovalent Cation Binding In Cubic Insulin Crystals" . . . . . 100.00 30 100.00 100.00 1.73e-12 . . . . 1444 1 90 no DBJ BAB84110 . "preproinsulin [Felis catus]" . . . . . 100.00 110 100.00 100.00 2.18e-12 . . . . 1444 1 91 no DBJ BAE80772 . "proinsulin [Bubalus bubalis]" . . . . . 100.00 81 100.00 100.00 3.63e-12 . . . . 1444 1 92 no DBJ BAJ17943 . "insulin [synthetic construct]" . . . . . 96.67 110 100.00 100.00 9.50e-12 . . . . 1444 1 93 no EMBL CAA08766 . "insulin [Homo sapiens]" . . . . . 96.67 59 100.00 100.00 2.04e-12 . . . . 1444 1 94 no EMBL CAA23475 . "preproinsulin [Canis sp.]" . . . . . 100.00 110 100.00 100.00 2.07e-12 . . . . 1444 1 95 no EMBL CAA23828 . "preproinsulin [Homo sapiens]" . . . . . 96.67 110 100.00 100.00 9.50e-12 . . . . 1444 1 96 no EMBL CAA49913 . "pre-proinsulin [Homo sapiens]" . . . . . 96.67 110 100.00 100.00 9.50e-12 . . . . 1444 1 97 no EMBL CAA66897 . "preproinsulin [Psammomys obesus]" . . . . . 96.67 110 100.00 100.00 1.34e-11 . . . . 1444 1 98 no GB AAA30722 . "preproinsulin [Bos taurus]" . . . . . 100.00 105 100.00 100.00 3.04e-12 . . . . 1444 1 99 no GB AAA36849 . "preproinsulin [Macaca fascicularis]" . . . . . 96.67 110 100.00 100.00 1.00e-11 . . . . 1444 1 100 no GB AAA59172 . "insulin [Homo sapiens]" . . . . . 96.67 110 100.00 100.00 9.50e-12 . . . . 1444 1 101 no GB AAA59173 . "insulin [Homo sapiens]" . . . . . 96.67 110 100.00 100.00 9.50e-12 . . . . 1444 1 102 no GB AAA59179 . "insulin [Homo sapiens]" . . . . . 96.67 107 100.00 100.00 9.21e-12 . . . . 1444 1 103 no PIR A59151 . "insulin precursor - jack bean (fragments)" . . . . . 100.00 51 100.00 100.00 1.93e-12 . . . . 1444 1 104 no PIR S15778 . "insulin chain B - bovine (fragments)" . . . . . 56.67 17 100.00 100.00 2.46e-02 . . . . 1444 1 105 no PRF 0601246A . insulin,prepro . . . . . 96.67 110 100.00 100.00 9.50e-12 . . . . 1444 1 106 no PRF 550085A . insulin . . . . . 100.00 51 100.00 100.00 1.93e-12 . . . . 1444 1 107 no PRF 550086A . insulin . . . . . 100.00 51 100.00 100.00 1.95e-12 . . . . 1444 1 108 no PRF 550086B . insulin . . . . . 100.00 51 100.00 100.00 2.55e-12 . . . . 1444 1 109 no PRF 560164A . insulin . . . . . 100.00 51 100.00 100.00 2.42e-12 . . . . 1444 1 110 no REF NP_000198 . "insulin preproprotein [Homo sapiens]" . . . . . 96.67 110 100.00 100.00 9.50e-12 . . . . 1444 1 111 no REF NP_001009272 . "insulin precursor [Felis catus]" . . . . . 100.00 110 100.00 100.00 2.18e-12 . . . . 1444 1 112 no REF NP_001035835 . "insulin, isoform 2 precursor [Homo sapiens]" . . . . . 96.67 200 100.00 100.00 2.29e-13 . . . . 1444 1 113 no REF NP_001103242 . "insulin precursor [Sus scrofa]" . . . . . 100.00 108 100.00 100.00 2.34e-12 . . . . 1444 1 114 no REF NP_001123565 . "insulin precursor [Canis lupus familiaris]" . . . . . 100.00 110 100.00 100.00 2.07e-12 . . . . 1444 1 115 no SP F8WCM5 . "RecName: Full=Insulin, isoform 2; AltName: Full=INS-IGF2 readthrough transcript protein" . . . . . 96.67 200 100.00 100.00 2.29e-13 . . . . 1444 1 116 no SP P01308 . "RecName: Full=Insulin; Contains: RecName: Full=Insulin B chain; Contains: RecName: Full=Insulin A chain; Flags: Precursor" . . . . . 96.67 110 100.00 100.00 9.50e-12 . . . . 1444 1 117 no SP P01310 . "RecName: Full=Insulin; Contains: RecName: Full=Insulin B chain; Contains: RecName: Full=Insulin A chain; Flags: Precursor" . . . . . 100.00 86 100.00 100.00 3.49e-12 . . . . 1444 1 118 no SP P01314 . "RecName: Full=Insulin; Contains: RecName: Full=Insulin B chain; Contains: RecName: Full=Insulin A chain" . . . . . 100.00 51 100.00 100.00 1.87e-12 . . . . 1444 1 119 no SP P01315 . "RecName: Full=Insulin; Contains: RecName: Full=Insulin B chain; Contains: RecName: Full=Insulin A chain; Flags: Precursor" . . . . . 100.00 108 100.00 100.00 2.34e-12 . . . . 1444 1 120 no TPG DAA13523 . "TPA: proinsulin precursor [Bos taurus]" . . . . . 100.00 105 100.00 100.00 2.62e-12 . . . . 1444 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'insulin B chain' common 1444 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 . PHE . 1444 1 2 . VAL . 1444 1 3 . ASN . 1444 1 4 . GLN . 1444 1 5 . HIS . 1444 1 6 . LEU . 1444 1 7 . CYS . 1444 1 8 . GLY . 1444 1 9 . SER . 1444 1 10 . HIS . 1444 1 11 . LEU . 1444 1 12 . VAL . 1444 1 13 . GLU . 1444 1 14 . ALA . 1444 1 15 . LEU . 1444 1 16 . TYR . 1444 1 17 . LEU . 1444 1 18 . VAL . 1444 1 19 . CYS . 1444 1 20 . GLY . 1444 1 21 . GLU . 1444 1 22 . ARG . 1444 1 23 . GLY . 1444 1 24 . PHE . 1444 1 25 . PHE . 1444 1 26 . TYR . 1444 1 27 . THR . 1444 1 28 . PRO . 1444 1 29 . LYS . 1444 1 30 . ALA . 1444 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 . PHE 1 1 1444 1 . VAL 2 2 1444 1 . ASN 3 3 1444 1 . GLN 4 4 1444 1 . HIS 5 5 1444 1 . LEU 6 6 1444 1 . CYS 7 7 1444 1 . GLY 8 8 1444 1 . SER 9 9 1444 1 . HIS 10 10 1444 1 . LEU 11 11 1444 1 . VAL 12 12 1444 1 . GLU 13 13 1444 1 . ALA 14 14 1444 1 . LEU 15 15 1444 1 . TYR 16 16 1444 1 . LEU 17 17 1444 1 . VAL 18 18 1444 1 . CYS 19 19 1444 1 . GLY 20 20 1444 1 . GLU 21 21 1444 1 . ARG 22 22 1444 1 . GLY 23 23 1444 1 . PHE 24 24 1444 1 . PHE 25 25 1444 1 . TYR 26 26 1444 1 . THR 27 27 1444 1 . PRO 28 28 1444 1 . LYS 29 29 1444 1 . ALA 30 30 1444 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 1444 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $insulin_B_chain . 9909 organism . 'Bos primigenius' cow . . Eukaryota Metazoa Bos primigenius . . . . pancreas . . . . . . . . . . . . . . . . 1444 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 1444 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $insulin_B_chain . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1444 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 1444 _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 . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 1444 _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 2.6 . na 1444 1 temperature 298 . K 1444 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 1444 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 1444 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 1444 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 1444 _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 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 1444 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 1444 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H . DSS . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 1444 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 1444 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 1444 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 PHE HA H 1 4.52 . . 1 . . . . . . . . 1444 1 2 . 1 1 1 1 PHE HB2 H 1 3.22 . . 2 . . . . . . . . 1444 1 3 . 1 1 1 1 PHE HB3 H 1 3.28 . . 2 . . . . . . . . 1444 1 4 . 1 1 1 1 PHE HD1 H 1 7.39 . . 1 . . . . . . . . 1444 1 5 . 1 1 1 1 PHE HD2 H 1 7.39 . . 1 . . . . . . . . 1444 1 6 . 1 1 1 1 PHE HE1 H 1 7.52 . . 1 . . . . . . . . 1444 1 7 . 1 1 1 1 PHE HE2 H 1 7.52 . . 1 . . . . . . . . 1444 1 8 . 1 1 1 1 PHE HZ H 1 7.4 . . 1 . . . . . . . . 1444 1 9 . 1 1 2 2 VAL H H 1 8.25 . . 1 . . . . . . . . 1444 1 10 . 1 1 2 2 VAL HA H 1 4.18 . . 1 . . . . . . . . 1444 1 11 . 1 1 2 2 VAL HB H 1 1.87 . . 1 . . . . . . . . 1444 1 12 . 1 1 2 2 VAL HG11 H 1 .84 . . 2 . . . . . . . . 1444 1 13 . 1 1 2 2 VAL HG12 H 1 .84 . . 2 . . . . . . . . 1444 1 14 . 1 1 2 2 VAL HG13 H 1 .84 . . 2 . . . . . . . . 1444 1 15 . 1 1 2 2 VAL HG21 H 1 .96 . . 2 . . . . . . . . 1444 1 16 . 1 1 2 2 VAL HG22 H 1 .96 . . 2 . . . . . . . . 1444 1 17 . 1 1 2 2 VAL HG23 H 1 .96 . . 2 . . . . . . . . 1444 1 18 . 1 1 3 3 ASN H H 1 8.42 . . 1 . . . . . . . . 1444 1 19 . 1 1 3 3 ASN HA H 1 4.8 . . 1 . . . . . . . . 1444 1 20 . 1 1 3 3 ASN HB2 H 1 2.93 . . 2 . . . . . . . . 1444 1 21 . 1 1 3 3 ASN HB3 H 1 2.99 . . 2 . . . . . . . . 1444 1 22 . 1 1 3 3 ASN HD21 H 1 6.88 . . 2 . . . . . . . . 1444 1 23 . 1 1 3 3 ASN HD22 H 1 7.65 . . 2 . . . . . . . . 1444 1 24 . 1 1 4 4 GLN H H 1 8.44 . . 1 . . . . . . . . 1444 1 25 . 1 1 4 4 GLN HA H 1 4.52 . . 1 . . . . . . . . 1444 1 26 . 1 1 4 4 GLN HB2 H 1 1.91 . . 2 . . . . . . . . 1444 1 27 . 1 1 4 4 GLN HB3 H 1 2.15 . . 2 . . . . . . . . 1444 1 28 . 1 1 4 4 GLN HG2 H 1 2.42 . . 1 . . . . . . . . 1444 1 29 . 1 1 4 4 GLN HG3 H 1 2.42 . . 1 . . . . . . . . 1444 1 30 . 1 1 4 4 GLN HE21 H 1 6.7 . . 2 . . . . . . . . 1444 1 31 . 1 1 4 4 GLN HE22 H 1 7.43 . . 2 . . . . . . . . 1444 1 32 . 1 1 5 5 HIS H H 1 8.6 . . 1 . . . . . . . . 1444 1 33 . 1 1 5 5 HIS HA H 1 4.73 . . 1 . . . . . . . . 1444 1 34 . 1 1 5 5 HIS HB2 H 1 3.41 . . 2 . . . . . . . . 1444 1 35 . 1 1 5 5 HIS HB3 H 1 3.64 . . 2 . . . . . . . . 1444 1 36 . 1 1 5 5 HIS HD2 H 1 7.48 . . 1 . . . . . . . . 1444 1 37 . 1 1 5 5 HIS HE1 H 1 8.63 . . 1 . . . . . . . . 1444 1 38 . 1 1 6 6 LEU H H 1 8.42 . . 1 . . . . . . . . 1444 1 39 . 1 1 6 6 LEU HA H 1 4.26 . . 1 . . . . . . . . 1444 1 40 . 1 1 6 6 LEU HB2 H 1 2.14 . . 1 . . . . . . . . 1444 1 41 . 1 1 6 6 LEU HB3 H 1 2.14 . . 1 . . . . . . . . 1444 1 42 . 1 1 6 6 LEU HG H 1 2.06 . . 1 . . . . . . . . 1444 1 43 . 1 1 6 6 LEU HD11 H 1 .94 . . 2 . . . . . . . . 1444 1 44 . 1 1 6 6 LEU HD12 H 1 .94 . . 2 . . . . . . . . 1444 1 45 . 1 1 6 6 LEU HD13 H 1 .94 . . 2 . . . . . . . . 1444 1 46 . 1 1 6 6 LEU HD21 H 1 1.03 . . 2 . . . . . . . . 1444 1 47 . 1 1 6 6 LEU HD22 H 1 1.03 . . 2 . . . . . . . . 1444 1 48 . 1 1 6 6 LEU HD23 H 1 1.03 . . 2 . . . . . . . . 1444 1 49 . 1 1 7 7 CYS H H 1 8.88 . . 1 . . . . . . . . 1444 1 50 . 1 1 7 7 CYS HA H 1 4.92 . . 1 . . . . . . . . 1444 1 51 . 1 1 7 7 CYS HB2 H 1 3.1 . . 2 . . . . . . . . 1444 1 52 . 1 1 7 7 CYS HB3 H 1 3.34 . . 2 . . . . . . . . 1444 1 53 . 1 1 8 8 GLY H H 1 7.4 . . 1 . . . . . . . . 1444 1 54 . 1 1 8 8 GLY HA2 H 1 4.2 . . 2 . . . . . . . . 1444 1 55 . 1 1 8 8 GLY HA3 H 1 4.25 . . 2 . . . . . . . . 1444 1 56 . 1 1 9 9 SER H H 1 8.6 . . 1 . . . . . . . . 1444 1 57 . 1 1 9 9 SER HA H 1 4.8 . . 1 . . . . . . . . 1444 1 58 . 1 1 9 9 SER HB2 H 1 3.92 . . 2 . . . . . . . . 1444 1 59 . 1 1 9 9 SER HB3 H 1 4.18 . . 2 . . . . . . . . 1444 1 60 . 1 1 10 10 HIS H H 1 7.96 . . 1 . . . . . . . . 1444 1 61 . 1 1 10 10 HIS HA H 1 4.63 . . 1 . . . . . . . . 1444 1 62 . 1 1 10 10 HIS HB2 H 1 3.46 . . 2 . . . . . . . . 1444 1 63 . 1 1 10 10 HIS HB3 H 1 3.66 . . 2 . . . . . . . . 1444 1 64 . 1 1 10 10 HIS HD2 H 1 7.5 . . 1 . . . . . . . . 1444 1 65 . 1 1 10 10 HIS HE1 H 1 8.6 . . 1 . . . . . . . . 1444 1 66 . 1 1 11 11 LEU H H 1 8.61 . . 1 . . . . . . . . 1444 1 67 . 1 1 11 11 LEU HA H 1 4.16 . . 1 . . . . . . . . 1444 1 68 . 1 1 11 11 LEU HB2 H 1 1.66 . . 1 . . . . . . . . 1444 1 69 . 1 1 11 11 LEU HB3 H 1 1.66 . . 1 . . . . . . . . 1444 1 70 . 1 1 11 11 LEU HG H 1 1.56 . . 1 . . . . . . . . 1444 1 71 . 1 1 11 11 LEU HD11 H 1 .94 . . 1 . . . . . . . . 1444 1 72 . 1 1 11 11 LEU HD12 H 1 .94 . . 1 . . . . . . . . 1444 1 73 . 1 1 11 11 LEU HD13 H 1 .94 . . 1 . . . . . . . . 1444 1 74 . 1 1 11 11 LEU HD21 H 1 .94 . . 1 . . . . . . . . 1444 1 75 . 1 1 11 11 LEU HD22 H 1 .94 . . 1 . . . . . . . . 1444 1 76 . 1 1 11 11 LEU HD23 H 1 .94 . . 1 . . . . . . . . 1444 1 77 . 1 1 12 12 VAL H H 1 7.4 . . 1 . . . . . . . . 1444 1 78 . 1 1 12 12 VAL HA H 1 3.56 . . 1 . . . . . . . . 1444 1 79 . 1 1 12 12 VAL HB H 1 2.07 . . 1 . . . . . . . . 1444 1 80 . 1 1 12 12 VAL HG11 H 1 .76 . . 2 . . . . . . . . 1444 1 81 . 1 1 12 12 VAL HG12 H 1 .76 . . 2 . . . . . . . . 1444 1 82 . 1 1 12 12 VAL HG13 H 1 .76 . . 2 . . . . . . . . 1444 1 83 . 1 1 12 12 VAL HG21 H 1 .97 . . 2 . . . . . . . . 1444 1 84 . 1 1 12 12 VAL HG22 H 1 .97 . . 2 . . . . . . . . 1444 1 85 . 1 1 12 12 VAL HG23 H 1 .97 . . 2 . . . . . . . . 1444 1 86 . 1 1 13 13 GLU H H 1 7.93 . . 1 . . . . . . . . 1444 1 87 . 1 1 13 13 GLU HA H 1 4.06 . . 1 . . . . . . . . 1444 1 88 . 1 1 13 13 GLU HB2 H 1 2.23 . . 1 . . . . . . . . 1444 1 89 . 1 1 13 13 GLU HB3 H 1 2.23 . . 1 . . . . . . . . 1444 1 90 . 1 1 13 13 GLU HG2 H 1 2.34 . . 1 . . . . . . . . 1444 1 91 . 1 1 13 13 GLU HG3 H 1 2.34 . . 1 . . . . . . . . 1444 1 92 . 1 1 14 14 ALA H H 1 7.93 . . 1 . . . . . . . . 1444 1 93 . 1 1 14 14 ALA HA H 1 4.2 . . 1 . . . . . . . . 1444 1 94 . 1 1 14 14 ALA HB1 H 1 1.65 . . 1 . . . . . . . . 1444 1 95 . 1 1 14 14 ALA HB2 H 1 1.65 . . 1 . . . . . . . . 1444 1 96 . 1 1 14 14 ALA HB3 H 1 1.65 . . 1 . . . . . . . . 1444 1 97 . 1 1 15 15 LEU H H 1 8.32 . . 1 . . . . . . . . 1444 1 98 . 1 1 15 15 LEU HA H 1 4.09 . . 1 . . . . . . . . 1444 1 99 . 1 1 15 15 LEU HB2 H 1 1.74 . . 1 . . . . . . . . 1444 1 100 . 1 1 15 15 LEU HB3 H 1 1.74 . . 1 . . . . . . . . 1444 1 101 . 1 1 15 15 LEU HG H 1 1.34 . . 1 . . . . . . . . 1444 1 102 . 1 1 15 15 LEU HD11 H 1 .76 . . 2 . . . . . . . . 1444 1 103 . 1 1 15 15 LEU HD12 H 1 .76 . . 2 . . . . . . . . 1444 1 104 . 1 1 15 15 LEU HD13 H 1 .76 . . 2 . . . . . . . . 1444 1 105 . 1 1 15 15 LEU HD21 H 1 .86 . . 2 . . . . . . . . 1444 1 106 . 1 1 15 15 LEU HD22 H 1 .86 . . 2 . . . . . . . . 1444 1 107 . 1 1 15 15 LEU HD23 H 1 .86 . . 2 . . . . . . . . 1444 1 108 . 1 1 16 16 TYR H H 1 8.44 . . 1 . . . . . . . . 1444 1 109 . 1 1 16 16 TYR HA H 1 4.18 . . 1 . . . . . . . . 1444 1 110 . 1 1 16 16 TYR HB2 H 1 3.32 . . 1 . . . . . . . . 1444 1 111 . 1 1 16 16 TYR HB3 H 1 3.32 . . 1 . . . . . . . . 1444 1 112 . 1 1 16 16 TYR HD1 H 1 7.16 . . 1 . . . . . . . . 1444 1 113 . 1 1 16 16 TYR HD2 H 1 7.16 . . 1 . . . . . . . . 1444 1 114 . 1 1 16 16 TYR HE1 H 1 6.87 . . 1 . . . . . . . . 1444 1 115 . 1 1 16 16 TYR HE2 H 1 6.87 . . 1 . . . . . . . . 1444 1 116 . 1 1 17 17 LEU H H 1 8.24 . . 1 . . . . . . . . 1444 1 117 . 1 1 17 17 LEU HA H 1 4.24 . . 1 . . . . . . . . 1444 1 118 . 1 1 17 17 LEU HB2 H 1 2.05 . . 1 . . . . . . . . 1444 1 119 . 1 1 17 17 LEU HB3 H 1 2.05 . . 1 . . . . . . . . 1444 1 120 . 1 1 17 17 LEU HG H 1 1.76 . . 1 . . . . . . . . 1444 1 121 . 1 1 17 17 LEU HD11 H 1 .96 . . 2 . . . . . . . . 1444 1 122 . 1 1 17 17 LEU HD12 H 1 .96 . . 2 . . . . . . . . 1444 1 123 . 1 1 17 17 LEU HD13 H 1 .96 . . 2 . . . . . . . . 1444 1 124 . 1 1 17 17 LEU HD21 H 1 1.03 . . 2 . . . . . . . . 1444 1 125 . 1 1 17 17 LEU HD22 H 1 1.03 . . 2 . . . . . . . . 1444 1 126 . 1 1 17 17 LEU HD23 H 1 1.03 . . 2 . . . . . . . . 1444 1 127 . 1 1 18 18 VAL H H 1 8.88 . . 1 . . . . . . . . 1444 1 128 . 1 1 18 18 VAL HA H 1 3.9 . . 1 . . . . . . . . 1444 1 129 . 1 1 18 18 VAL HB H 1 2.25 . . 1 . . . . . . . . 1444 1 130 . 1 1 18 18 VAL HG11 H 1 1.03 . . 2 . . . . . . . . 1444 1 131 . 1 1 18 18 VAL HG12 H 1 1.03 . . 2 . . . . . . . . 1444 1 132 . 1 1 18 18 VAL HG13 H 1 1.03 . . 2 . . . . . . . . 1444 1 133 . 1 1 18 18 VAL HG21 H 1 1.17 . . 2 . . . . . . . . 1444 1 134 . 1 1 18 18 VAL HG22 H 1 1.17 . . 2 . . . . . . . . 1444 1 135 . 1 1 18 18 VAL HG23 H 1 1.17 . . 2 . . . . . . . . 1444 1 136 . 1 1 19 19 CYS H H 1 7.95 . . 1 . . . . . . . . 1444 1 137 . 1 1 19 19 CYS HA H 1 4.92 . . 1 . . . . . . . . 1444 1 138 . 1 1 19 19 CYS HB2 H 1 3.32 . . 1 . . . . . . . . 1444 1 139 . 1 1 19 19 CYS HB3 H 1 3.32 . . 1 . . . . . . . . 1444 1 140 . 1 1 20 20 GLY H H 1 8.89 . . 1 . . . . . . . . 1444 1 141 . 1 1 20 20 GLY HA2 H 1 3.9 . . 2 . . . . . . . . 1444 1 142 . 1 1 20 20 GLY HA3 H 1 4.07 . . 2 . . . . . . . . 1444 1 143 . 1 1 21 21 GLU H H 1 8.35 . . 1 . . . . . . . . 1444 1 144 . 1 1 21 21 GLU HA H 1 4.36 . . 1 . . . . . . . . 1444 1 145 . 1 1 21 21 GLU HB2 H 1 2.2 . . 2 . . . . . . . . 1444 1 146 . 1 1 21 21 GLU HB3 H 1 2.28 . . 2 . . . . . . . . 1444 1 147 . 1 1 21 21 GLU HG2 H 1 2.57 . . 1 . . . . . . . . 1444 1 148 . 1 1 21 21 GLU HG3 H 1 2.57 . . 1 . . . . . . . . 1444 1 149 . 1 1 22 22 ARG H H 1 7.96 . . 1 . . . . . . . . 1444 1 150 . 1 1 22 22 ARG HA H 1 4.35 . . 1 . . . . . . . . 1444 1 151 . 1 1 22 22 ARG HB2 H 1 2.08 . . 1 . . . . . . . . 1444 1 152 . 1 1 22 22 ARG HB3 H 1 2.08 . . 1 . . . . . . . . 1444 1 153 . 1 1 22 22 ARG HG2 H 1 1.86 . . 1 . . . . . . . . 1444 1 154 . 1 1 22 22 ARG HG3 H 1 1.86 . . 1 . . . . . . . . 1444 1 155 . 1 1 22 22 ARG HD2 H 1 3.39 . . 1 . . . . . . . . 1444 1 156 . 1 1 22 22 ARG HD3 H 1 3.39 . . 1 . . . . . . . . 1444 1 157 . 1 1 22 22 ARG HE H 1 7.27 . . 1 . . . . . . . . 1444 1 158 . 1 1 23 23 GLY H H 1 7.93 . . 1 . . . . . . . . 1444 1 159 . 1 1 23 23 GLY HA2 H 1 3.98 . . 2 . . . . . . . . 1444 1 160 . 1 1 23 23 GLY HA3 H 1 4.01 . . 2 . . . . . . . . 1444 1 161 . 1 1 24 24 PHE H H 1 7.82 . . 1 . . . . . . . . 1444 1 162 . 1 1 24 24 PHE HA H 1 4.6 . . 1 . . . . . . . . 1444 1 163 . 1 1 24 24 PHE HB2 H 1 3.08 . . 2 . . . . . . . . 1444 1 164 . 1 1 24 24 PHE HB3 H 1 2.98 . . 2 . . . . . . . . 1444 1 165 . 1 1 24 24 PHE HD1 H 1 7.25 . . 1 . . . . . . . . 1444 1 166 . 1 1 24 24 PHE HD2 H 1 7.25 . . 1 . . . . . . . . 1444 1 167 . 1 1 24 24 PHE HE1 H 1 7.41 . . 1 . . . . . . . . 1444 1 168 . 1 1 24 24 PHE HE2 H 1 7.41 . . 1 . . . . . . . . 1444 1 169 . 1 1 24 24 PHE HZ H 1 7.35 . . 1 . . . . . . . . 1444 1 170 . 1 1 25 25 PHE H H 1 8.04 . . 1 . . . . . . . . 1444 1 171 . 1 1 25 25 PHE HA H 1 4.7 . . 1 . . . . . . . . 1444 1 172 . 1 1 25 25 PHE HB2 H 1 3.09 . . 2 . . . . . . . . 1444 1 173 . 1 1 25 25 PHE HB3 H 1 3.19 . . 2 . . . . . . . . 1444 1 174 . 1 1 25 25 PHE HD1 H 1 7.08 . . 1 . . . . . . . . 1444 1 175 . 1 1 25 25 PHE HD2 H 1 7.08 . . 1 . . . . . . . . 1444 1 176 . 1 1 25 25 PHE HE1 H 1 7.26 . . 1 . . . . . . . . 1444 1 177 . 1 1 25 25 PHE HE2 H 1 7.26 . . 1 . . . . . . . . 1444 1 178 . 1 1 25 25 PHE HZ H 1 7.2 . . 1 . . . . . . . . 1444 1 179 . 1 1 26 26 TYR H H 1 7.82 . . 1 . . . . . . . . 1444 1 180 . 1 1 26 26 TYR HA H 1 4.72 . . 1 . . . . . . . . 1444 1 181 . 1 1 26 26 TYR HB2 H 1 3.08 . . 1 . . . . . . . . 1444 1 182 . 1 1 26 26 TYR HB3 H 1 3.08 . . 1 . . . . . . . . 1444 1 183 . 1 1 26 26 TYR HD1 H 1 7.16 . . 1 . . . . . . . . 1444 1 184 . 1 1 26 26 TYR HD2 H 1 7.16 . . 1 . . . . . . . . 1444 1 185 . 1 1 26 26 TYR HE1 H 1 6.87 . . 1 . . . . . . . . 1444 1 186 . 1 1 26 26 TYR HE2 H 1 6.87 . . 1 . . . . . . . . 1444 1 187 . 1 1 27 27 THR H H 1 7.62 . . 1 . . . . . . . . 1444 1 188 . 1 1 27 27 THR HA H 1 4.59 . . 1 . . . . . . . . 1444 1 189 . 1 1 27 27 THR HB H 1 4.24 . . 1 . . . . . . . . 1444 1 190 . 1 1 27 27 THR HG21 H 1 1.34 . . 1 . . . . . . . . 1444 1 191 . 1 1 27 27 THR HG22 H 1 1.34 . . 1 . . . . . . . . 1444 1 192 . 1 1 27 27 THR HG23 H 1 1.34 . . 1 . . . . . . . . 1444 1 193 . 1 1 28 28 PRO HA H 1 4.47 . . 1 . . . . . . . . 1444 1 194 . 1 1 28 28 PRO HB2 H 1 2.1 . . 2 . . . . . . . . 1444 1 195 . 1 1 28 28 PRO HB3 H 1 2.42 . . 2 . . . . . . . . 1444 1 196 . 1 1 28 28 PRO HG2 H 1 2.03 . . 1 . . . . . . . . 1444 1 197 . 1 1 28 28 PRO HG3 H 1 2.03 . . 1 . . . . . . . . 1444 1 198 . 1 1 28 28 PRO HD2 H 1 3.76 . . 1 . . . . . . . . 1444 1 199 . 1 1 28 28 PRO HD3 H 1 3.76 . . 1 . . . . . . . . 1444 1 200 . 1 1 29 29 LYS H H 1 8.11 . . 1 . . . . . . . . 1444 1 201 . 1 1 29 29 LYS HA H 1 4.5 . . 1 . . . . . . . . 1444 1 202 . 1 1 29 29 LYS HB2 H 1 1.83 . . 1 . . . . . . . . 1444 1 203 . 1 1 29 29 LYS HB3 H 1 1.83 . . 1 . . . . . . . . 1444 1 204 . 1 1 29 29 LYS HG2 H 1 1.52 . . 1 . . . . . . . . 1444 1 205 . 1 1 29 29 LYS HG3 H 1 1.52 . . 1 . . . . . . . . 1444 1 206 . 1 1 29 29 LYS HD2 H 1 1.76 . . 1 . . . . . . . . 1444 1 207 . 1 1 29 29 LYS HD3 H 1 1.76 . . 1 . . . . . . . . 1444 1 208 . 1 1 29 29 LYS HE2 H 1 2.98 . . 1 . . . . . . . . 1444 1 209 . 1 1 29 29 LYS HE3 H 1 2.98 . . 1 . . . . . . . . 1444 1 210 . 1 1 29 29 LYS HZ1 H 1 7.65 . . 1 . . . . . . . . 1444 1 211 . 1 1 29 29 LYS HZ2 H 1 7.65 . . 1 . . . . . . . . 1444 1 212 . 1 1 29 29 LYS HZ3 H 1 7.65 . . 1 . . . . . . . . 1444 1 213 . 1 1 30 30 ALA H H 1 8.12 . . 1 . . . . . . . . 1444 1 214 . 1 1 30 30 ALA HA H 1 4.5 . . 1 . . . . . . . . 1444 1 215 . 1 1 30 30 ALA HB1 H 1 1.5 . . 1 . . . . . . . . 1444 1 216 . 1 1 30 30 ALA HB2 H 1 1.5 . . 1 . . . . . . . . 1444 1 217 . 1 1 30 30 ALA HB3 H 1 1.5 . . 1 . . . . . . . . 1444 1 stop_ save_