data_6205 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H chemical shift assignments for AbaB12-DKP-insulin ; _BMRB_accession_number 6205 _BMRB_flat_file_name bmr6205.str _Entry_type original _Submission_date 2004-05-10 _Accession_date 2004-05-10 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Huang K. . . 2 Xu B. . . 3 Hu S. Q. . 4 Chu Y. C. . 5 Hua Q. X. . 6 Whittaker J. . . 7 Nakagawa S. H. . 8 DeMeyts P. . . 9 Katsoyannis P. G. . 10 Weiss M. A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 275 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-15 update BMRB 'Updating non-standard residue' stop_ loop_ _Related_BMRB_accession_number _Relationship 6203 AlaB12-DKP-insulin 6204 AbaB12-DKP-insulin stop_ _Original_release_date 2004-05-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; How Insulin Binds: the B-Chain alpha-Helix Contacts the L1 beta -Helix of the Insulin Receptor. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Huang K. . . 2 Xu B. . . 3 Hu S. Q. . 4 Chu Y. C. . 5 Hua Q. X. . 6 Qu Y. . . 7 Li B. . . 8 Wang S. . . 9 Wang R. Y. . 10 Nakagawa S. H. . 11 Theede A. M. . 12 Whittaker J. . . 13 'De Meyts' P. . . 14 Katsoyannis P. G. . 15 Weiss M. A. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 341 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 529 _Page_last 550 _Year 2004 _Details . loop_ _Keyword Ala-B12-DKP-insulin 'insulin receptor' 'protein unfolding' 'receptor binding' stop_ save_ ################################## # Molecular system description # ################################## save_DKP-HI _Saveframe_category molecular_system _Mol_system_name 'insulin analogue' _Abbreviation_common DKP-HI _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'insulin analogue chain A' $DKP_HI_A 'insulin analogue chain B' $DKP_HI_B stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DKP_HI_A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'AbaB12-DKP-insulin, chain A' _Name_variant 'Aba-B12-Val, Asp-B10-His, Lys-B28-Pro, Pro-B29-Lys insulin' _Abbreviation_common DKP_HI_A _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 21 _Mol_residue_sequence ; GIVEQCCTSICSLYQLENYC N ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ILE 3 VAL 4 GLU 5 GLN 6 CYS 7 CYS 8 THR 9 SER 10 ILE 11 CYS 12 SER 13 LEU 14 TYR 15 GLN 16 LEU 17 GLU 18 ASN 19 TYR 20 CYS 21 ASN stop_ _Sequence_homology_query_date 2008-03-24 _Sequence_homology_query_revised_last_date 2008-03-03 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 1761 'insulin A chain' 100.00 21 100 100 2e-05 BMRB 4997 Insulin 100.00 21 100 100 2e-05 BMRB 6203 'ThrB12-DKP-insulin, chain A' 100.00 21 100 100 2e-05 BMRB 6204 'AlaB12-DKP-insulin, chain A' 100.00 21 100 100 2e-05 BMRB 4266 [D-AlaB26]destetra(B27-B30)insulin-B26-amide 44.68 47 100 100 2e-05 PDB 1A7F 'A Chain A, Insulin Mutant B16 Glu, B24 Gly,Des-B30, Nmr, 20 Structures' 100.00 21 100 100 2e-05 PDB 1AI0 'A Chain A, R6 Human Insulin Hexamer(Non-Symmetric), Nmr, 10 Structures' 100.00 21 100 100 2e-05 PDB 1AIY 'A Chain A, R6 Human Insulin Hexamer(Symmetric), Nmr, 10 Structures' 100.00 21 100 100 2e-05 PDB 1B17 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 5.00Coordinates)' 100.00 21 100 100 2e-05 PDB 1B18 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 5.53Coordinates)' 100.00 21 100 100 2e-05 PDB 1B19 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 5.80Coordinates)' 100.00 21 100 100 2e-05 PDB 1B2A 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 6.00Coordinates)' 100.00 21 100 100 2e-05 PDB 1B2B 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 6.16Coordinates)' 100.00 21 100 100 2e-05 PDB 1B2C 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 6.26Coordinates)' 100.00 21 100 100 2e-05 PDB 1B2D 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 6.35Coordinates)' 100.00 21 100 100 2e-05 PDB 1B2E 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 6.50Coordinates)' 100.00 21 100 100 2e-05 PDB 1B2F 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 6.98Coordinates)' 100.00 21 100 100 2e-05 PDB 1B2G 'A Chain A, Ph Affects Glu B13 Switching AndSulfate Binding In Cubic Insulin Crystals (Ph 9.00Coordinates)' 100.00 21 100 100 2e-05 PDB 1B9E 'A Chain A, Human Insulin Mutant Serb9glu' 100.00 21 100 100 2e-05 PDB 1BEN 'A Chain A, Insulin Complexed With4-Hydroxybenzamide' 100.00 21 100 100 1e-04 PDB 1BZV 'A Chain A,[d-Alab26]-Des(B27-B30)-Insulin-B26-Amide A SuperpotentSingle-Replacement Insulin Analogue, Nmr, MinimizedAver' 100.00 21 100 100 2e-05 PDB 1DEI 'A Chain A, Desheptapeptide (B24-B30) Insulin' 100.00 21 100 100 2e-05 PDB 1EV3 'A Chain A, Structure Of The RhombohedralForm Of The M-CresolINSULIN R6 Hexamer' 100.00 21 100 100 2e-05 PDB 1EV6 'A Chain A, Structure Of The Monoclinic FormOf The M-CresolINSULIN R6 Hexamer' 100.00 21 100 100 2e-05 PDB 1EVR 'A Chain A, The Structure Of TheResorcinolINSULIN R6 HEXAMER' 100.00 21 100 100 2e-05 PDB 1FU2 'A Chain A, First Protein StructureDetermined From X-Ray Powder Diffraction Data' 100.00 21 100 100 2e-05 PDB 1FUB 'A Chain A, First Protein StructureDetermined From X-Ray Powder Diffraction Data' 100.00 21 100 100 2e-05 PDB 1G7A 'A Chain A, 1.2 A Structure Of T3r3 HumanInsulin At 100 K' 100.00 21 100 100 1e-04 PDB 1G7B 'A Chain A, 1.3 A Structure Of T3r3 HumanInsulin At 100 K' 100.00 21 100 100 1e-04 PDB 1GUJ 'A Chain A, Insulin At Ph 2: StructuralAnalysis Of The Conditions Promoting Insulin FibreFormation.' 100.00 21 100 100 2e-05 PDB 1HIQ 'A Chain A, Paradoxical Structure AndFunction In A Mutant Human Insulin Associated WithDiabetes Mellitus' 100.00 21 100 100 2e-05 PDB 1HIS 'A Chain A, Structure And Dynamics OfDes-Pentapeptide-Insulin In Solution: TheMolten-Globule Hypothesis' 100.00 21 100 100 2e-05 PDB 1HIT 'A Chain A, Receptor Binding Redefined By AStructural Switch In A Mutant Human Insulin' 100.00 21 100 100 2e-05 PDB 1HLS 'A Chain A, Nmr Structure Of The HumanInsulin-His(B16)' 100.00 21 100 100 2e-05 PDB 1HTV 'A Chain A, Crystal Structure OfDestripeptide (B28-B30) Insulin' 100.00 21 100 100 2e-05 PDB 1HUI 'A Chain A, Insulin Mutant (B1, B10, B16,B27)glu, Des-B30, Nmr, 25 Structures' 100.00 21 100 100 2e-05 PDB 1IZA 'A Chain A, Role Of B13 Glu In InsulinAssembly: The Hexamer Structure Of Recombinant Mutant(B13 Glu-> Gln) Insulin' 100.00 21 100 100 2e-05 PDB 1IZB 'A Chain A, Role Of B13 Glu In InsulinAssembly: The Hexamer Structure Of Recombinant Mutant(B13 Glu-> Gln) Insulin' 100.00 21 100 100 2e-05 PDB 1JCO 'A Chain A, Solution Structure Of TheMonomeric [thr(B27)->pro,Pro(B28)- >thr] Insulin Mutant(Pt Insulin)' 100.00 21 100 100 2e-05 PDB 1LKQ 'A Chain A, Nmr Structure Of Human InsulinMutant Ile-A2-Gly, Val-A3- Gly, His-B10-Asp,Pro-B28-Lys, Lys-B29-Pro, 20 Struct' 100.00 21 100 100 8e-04 PDB 1LPH 'A Chain A, Lys(B28)pro(B29)-Human Insulin' 100.00 21 100 100 2e-05 PDB 1M5A 'A Chain A, Crystal Structure Of2-Co(2+)-Insulin At 1.2a Resolution' 100.00 21 100 100 2e-05 PDB 1MHI 'A Chain A, Three-Dimensional SolutionStructure Of An Insulin Dimer. A Study Of The B9(Asp)Mutant Of Human Insulin Using' 100.00 21 100 100 1e-04 PDB 1MHJ 'A Chain A, Solution Structure Of TheSuperactive Monomeric Des- [phe(B25)] Human InsulinMutant. Elucidation Of The Struct' 100.00 21 100 100 2e-05 PDB 1MPJ 'A Chain A, X-Ray Crystallographic Studies OnHexameric Insulins In The Presence Of Helix-StabilizingAgents, Thiocyanate,' 100.00 21 100 100 2e-05 PDB 1MSO 'A Chain A, T6 Human Insulin At 1.0 AResolution' 100.00 21 100 100 1e-04 PDB 1OS3 'A Chain A, Dehydrated T6 Human Insulin At100 K' 100.00 21 100 100 2e-05 PDB 1OS4 'A Chain A, Dehydrated T6 Human Insulin At295 K' 100.00 21 100 100 2e-05 PDB 1QIY 'A Chain A, Human Insulin Hexamers With ChainB His Mutated To Tyr Complexed With Phenol' 100.00 21 100 100 2e-05 PDB 1QIZ 'A Chain A, Human Insulin Hexamers With ChainB His Mutated To Tyr Complexed With Resorcinol' 100.00 21 100 100 2e-05 PDB 1QJ0 'A Chain A, Human Insulin Hexamers With ChainB His Mutated To Tyr' 100.00 21 100 100 2e-05 PDB 1SDB 'A Chain A, Porcine Desb1-2Despentapeptide(B26-B30) Insulin' 100.00 21 100 100 2e-05 PDB 1SF1 'A Chain A, Nmr Structure Of Human InsulinUnder Amyloidogenic Condition, 15 Structures' 100.00 21 100 100 2e-05 PDB 1SJT 'A Chain A, Mini-Proinsulin, Two ChainInsulin Analog Mutant: Des B30, His(B 10)asp, Pro(B28)asp, Nmr, 20 Structures' 100.00 21 100 100 2e-05 PDB 1T1K 'A Chain A, Nmr Structure Of Human InsulinMutant His-B10-Asp, Val-B12- Ala, Pro-B28-Lys,Lys-B29-Pro, 15 Structures' 100.00 21 100 100 2e-05 PDB 1T1P 'A Chain A, Nmr Structure Of Human InsulinMutant His-B10-Asp, Val-B12- Thr, Pro-B28-Lys,Lys-B29-Pro, 15 Structures' 100.00 21 100 100 2e-05 PDB 1T1Q 'A Chain A, Nmr Structure Of Human InsulinMutant His-B10-Asp, Val-B12- Aba, Pro-B28-Lys,Lys-B29-Pro, 15 Structures' 100.00 21 100 100 2e-05 PDB 1TRZ 'A Chain A, Crystallographic Evidence For DualCoordination Around Zinc In The T3r3 Human InsulinHexamer' 100.00 21 100 100 2e-05 PDB 1TYL "A Chain A, The Structure Of A Complex OfHexameric Insulin And 4'- Hydroxyacetanilide" 100.00 21 100 100 2e-05 PDB 1TYM "A Chain A, The Structure Of A Complex OfHexameric Insulin And 4'- Hydroxyacetanilide" 100.00 21 100 100 2e-05 PDB 1UZ9 'A Chain A, Crystallographic And SolutionStudies Of N-Lithocholyl Insulin: A New Generation OfProlonged-Acting Insulins.' 100.00 21 100 100 2e-05 PDB 1W8P 'A Chain A, Structural Properties Of TheB25tyr-Nme-B26phe Insulin Mutant.' 100.00 21 100 100 2e-05 PDB 1WAV 'A Chain A, Crystal Structure Of Form BMonoclinic Crystal Of Insulin' 100.00 21 100 100 2e-05 PDB 1XDA 'A Chain A, Structure Of Insulin' 100.00 21 100 100 2e-05 PDB 1XGL 'A Chain A, Human Insulin Disulfide Isomer,Nmr, 10 Structures' 100.00 21 100 100 2e-05 PDB 1ZEG 'A Chain A, Structure Of B28 Asp Insulin InComplex With Phenol' 100.00 21 100 100 2e-05 PDB 1ZEH 'A Chain A, Structure Of Insulin' 100.00 21 100 100 2e-05 PDB 1ZNI 'A Chain A, Insulin' 100.00 21 100 100 2e-05 PDB 1ZNJ 'A Chain A, Insulin, Monoclinic Crystal Form' 100.00 21 100 100 2e-05 PDB 2AIY 'A Chain A, R6 Human Insulin Hexamer(Symmetric), Nmr, 20 Structures' 100.00 21 100 100 2e-05 PDB 2C8Q 'A Chain A, Insuline(1sec) And Uv LaserExcited Fluorescence' 100.00 21 100 100 2e-05 PDB 2C8R 'A Chain A, Insuline(60sec) And Uv LaserExcited Fluorescence' 100.00 21 100 100 2e-05 PDB 2CEU 'A Chain A, Despentapeptide Insulin In AceticAcid (Ph 2)' 100.00 21 100 100 2e-05 PDB 2EFA 'A Chain A, Neutron Crystal Structure OfCubic Insulin At Pd6.6' 100.00 21 100 100 5e-04 PDB 2G4M 'A Chain A, Insulin Collected At 2.0 AWavelength' 100.00 21 100 100 2e-05 PDB 2H67 'A Chain A, Nmr Structure Of Human InsulinMutant His-B5-Ala, His-B10- Asp Pro-B28-Lys,Lys-B29-Pro, 20 Structures' 100.00 21 100 100 2e-05 PDB 2HH4 'A Chain A, Nmr Structure Of Human InsulinMutant Gly-B8-D-Ser, His-B10- Asp Pro-B28-Lys,Lys-B29-Pro, 20 Structures' 100.00 21 100 100 2e-05 PDB 2HHO 'A Chain A, Nmr Structure Of Human InsulinMutant Gly-B8-Ser, His-B10- Asp Pro-B28-Lys,Lys-B29-Pro, 20 Structures' 100.00 21 100 100 2e-05 PDB 2HIU 'A Chain A, Nmr Structure Of Human InsulinIn 20% Acetic Acid, Zinc- Free, 10 Structures' 100.00 21 100 100 2e-05 PDB 2JMN 'A Chain A, Nmr Structure Of Human InsulinMutant His-B10-Asp, Pro-B28- Lys, Lys-B29-Pro, 20Structures' 100.00 21 100 100 2e-05 PDB 2JV1 'A Chain A, Nmr Structure Of Human InsulinMonomer In 35% Cd3cn Zinc Free, 50 Structures' 100.00 21 100 100 2e-05 PDB 2OLY 'A Chain A, Structure Of Human Insulin InPresence Of Urea At Ph 7.0' 100.00 21 100 100 2e-05 PDB 2OLZ 'A Chain A, Structure Of Human Insulin InPresence Of Thiocyanate At Ph 7.0' 100.00 21 100 100 2e-05 PDB 2OM0 '1 Chain 1, Structure Of Human Insulin InPresence Of Urea At Ph 6.5' 100.00 21 100 100 2e-05 PDB 2OM1 '1 Chain 1, Structure Of Human Insulin InPresence Of Thiocyanate At Ph 6.5' 100.00 21 100 100 2e-05 PDB 2OMG 'A Chain A, Structure Of Human InsulinCocrystallized With Protamine And Urea' 100.00 21 100 100 2e-05 PDB 2OMH 'A Chain A, Structure Of Human InsulinCocrystallized With Arg-12 Peptide In Presence Of Urea' 100.00 21 100 100 2e-05 PDB 2OMI 'A Chain A, Structure Of Human InsulinCocrystallized With Protamine' 100.00 21 100 100 2e-05 PDB 2TCI 'A Chain A, X-Ray Crystallographic Studies OnHexameric Insulins In The Presence Of Helix-StabilizingAgents, Thiocyanate,' 100.00 21 100 100 2e-05 PDB 3AIY 'A Chain A, R6 Human Insulin Hexamer(Symmetric), Nmr, Refined Average Structure' 100.00 21 100 100 2e-05 PDB 3INS 'A Chain A, Structure Of Insulin. Results OfJoint Neutron And X-Ray Refinement' 100.00 21 100 100 5e-04 PDB 3MTH 'A Chain A, X-Ray Crystallographic Studies OnHexameric Insulins In The Presence Of Helix-StabilizingAgents, Thiocyanate,' 100.00 21 100 100 2e-05 PDB 4AIY "A Chain A, R6 Human Insulin Hexamer(Symmetric), Nmr, 'green' Substate, Average Structure" 100.00 21 100 100 2e-05 PDB 4INS 'A Chain A, The Structure Of 2zn Pig InsulinCrystals At 1.5 Angstroms Resolution' 100.00 21 100 100 2e-05 PDB 5AIY "A Chain A, R6 Human Insulin Hexamer(Symmetric), Nmr, 'red' Substate, Average Structure" 100.00 21 100 100 2e-05 PDB 7INS 'A Chain A, Structure Of Porcine InsulinCocrystallized With Clupeine Z' 100.00 21 100 100 2e-05 PDB 9INS 'A Chain A, Monovalent Cation Binding In CubicInsulin Crystals' 100.00 21 100 100 2e-05 PDB 1SJU 'A Chain A, Mini-Proinsulin, Single ChainInsulin Analog Mutant: Des B30, His(B 10)asp, Pro(B28)asp And Peptide Bond Betwe' 42.00 50 100 100 2e-05 PDB 6INS 'E Chain E, X-Ray Analysis Of The Single ChainB29-A1 Peptide-Linked Insulin Molecule. A CompletelyInactive Analogue' 42.00 50 100 100 2e-05 PDB 1ZEI 'A Chain A, Cross-Linked B28 Asp Insulin' 39.62 53 100 100 2e-05 PDB 1EFE 'A Chain A, An Active Mini-Proinsulin, M2pi' 35.00 60 100 100 2e-05 EMBL CAA23475.1 'preproinsulin [Canis sp.]' 19.09 110 100 100 2e-05 EMBL CAA23828.1 'preproinsulin [Homo sapiens]' 19.09 110 100 100 2e-05 EMBL CAA43403.1 'Preproinsulin [Pan troglodytes]' 19.09 110 100 100 2e-05 EMBL CAA43405.1 'Preproinsulin [Chlorocebus aethiops]' 19.09 110 100 100 2e-05 EMBL CAA49913.1 'pre-proinsulin [Homo sapiens]' 19.09 110 100 100 2e-05 GenBank ABP93829.1 'mini-proinsulin [synthetic construct]' 35.59 59 100 100 2e-05 GenBank ABI63346.1 'insulin [Homo sapiens]' 21.43 98 100 100 2e-05 GenBank AAP36446.1 'Homo sapiens insulin [syntheticconstruct]' 18.92 111 100 100 2e-05 GenBank AAX29480.1 'insulin [synthetic construct]' 18.92 111 100 100 2e-05 GenBank AAX29481.1 'insulin [synthetic construct]' 18.92 111 100 100 2e-05 PRF 560164B insulin 100.00 21 100 100 2e-05 PRF 580107B insulin 42.00 50 100 100 2e-05 PRF 600165A insulin 41.18 51 100 100 2e-05 PRF 1006230A insulin,pro- 24.42 86 100 100 2e-05 PRF 0601246A insulin,prepro 19.09 110 100 100 2e-05 REF NP_000198.1 'proinsulin precursor [Homo sapiens]' 19.09 110 100 100 2e-05 REF NP_001008996.1 'proinsulin precursor [Pantroglodytes]' 19.09 110 100 100 2e-05 REF NP_001075804.1 'insulin [Oryctolagus cuniculus]' 19.09 110 100 100 2e-05 REF XP_540786.1 'PREDICTED: similar to Insulinprecursor [Canis familiaris]' 19.09 110 100 100 2e-05 SWISS-PROT P67973 'INS_BALPH Insulin [Contains: Insulin Bchain; Insulin A chain]' 41.18 51 100 100 2e-05 SWISS-PROT P67974 'INS_PHYCA Insulin [Contains: Insulin Bchain; Insulin A chain]' 41.18 51 100 100 2e-05 SWISS-PROT P30406 'INS_MACFA Insulin precursor [Contains: InsulinB chain; Insulin A chain]' 19.09 110 100 100 2e-05 SWISS-PROT P30410 'INS_PANTR Insulin precursor [Contains: InsulinB chain; Insulin A chain]' 19.09 110 100 100 2e-05 SWISS-PROT Q91XI3 'INS_SPETR Insulin precursor [Contains:Insulin B chain; Insulin A chain]' 19.09 110 100 100 2e-05 stop_ save_ save_DKP_HI_B _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'AbaB12-DKP-insulin, chain B' _Name_variant 'Aba-B12-Val, Asp-B10-His, Lys-B28-Pro, Pro-B29-Lys insulin' _Abbreviation_common DKP_HI_B _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details ; an non-standard amino acid alpha-amino-butyric acid replace the valineB12 in B-chain ; _Residue_count 30 _Mol_residue_sequence ; FVNQHLCGSDLXEALYLVCG ERGFFYTKPT ; loop_ _Residue_seq_code _Residue_label 1 PHE 2 VAL 3 ASN 4 GLN 5 HIS 6 LEU 7 CYS 8 GLY 9 SER 10 ASP 11 LEU 12 ABA 13 GLU 14 ALA 15 LEU 16 TYR 17 LEU 18 VAL 19 CYS 20 GLY 21 GLU 22 ARG 23 GLY 24 PHE 25 PHE 26 TYR 27 THR 28 LYS 29 PRO 30 THR stop_ _Sequence_homology_query_date 2008-03-24 _Sequence_homology_query_revised_last_date 2008-01-16 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1T1Q 'B Chain B, Nmr Structure Of Human InsulinMutant His-B10-Asp, Val-B12- Aba, Pro-B28-Lys,Lys-B29-Pro, 15 Structures' 100.00 30 100 100 4e-10 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_ABA _Saveframe_category polymer_residue _Mol_type 'L-peptide linking' _Name_common 'ALPHA-AMINOBUTYRIC ACID' _BMRB_code . _PDB_code ABA _Standard_residue_derivative . _Molecular_mass 103.120 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Aug 1 09:46:43 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HN2 HN2 H . 0 . ? HA HA H . 0 . ? HB3 HB3 H . 0 . ? HB2 HB2 H . 0 . ? HG1 HG1 H . 0 . ? HG3 HG3 H . 0 . ? HG2 HG2 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N HN2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING CB CG ? ? SING CB HB3 ? ? SING CB HB2 ? ? SING CG HG1 ? ? SING CG HG3 ? ? SING CG HG2 ? ? SING OXT HXT ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DKP_HI_A Human 9606 Eukaryota Metazoa Homo sapiens $DKP_HI_B Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $DKP_HI_A 'chemical synthesis' . . . . . $DKP_HI_B 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DKP_HI_A 1.2 mM . $DKP_HI_B 1.2 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DKP_HI_A 1.2 mM . $DKP_HI_B 1.2 mM . D2O 100 % . stop_ save_ ############################ # Computer software used # ############################ save_DGII _Saveframe_category software _Name DGII _Version 'INSIGHTII 2000' loop_ _Task 'structure solution' stop_ _Details 'Molecular Simulations INC.' save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.85 loop_ _Task 'simulated annealing refinement' stop_ _Details Brunger save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer .Bruker _Model .DRX _Field_strength .800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 n/a pressure 1 . atm temperature 298 1 K stop_ save_ save_sample_cond_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.6 0.1 n/a pressure 1 . atm temperature 305 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D NOESY' '2D TOCSY' DQF-COSY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'insulin analogue chain A' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 ILE H H 7.84 0.02 1 2 . 2 ILE HA H 3.88 0.02 1 3 . 2 ILE HB H 1.11 0.02 1 4 . 2 ILE HG12 H 0.86 0.02 1 5 . 2 ILE HG13 H 0.86 0.02 1 6 . 2 ILE HG2 H 0.69 0.02 1 7 . 2 ILE HD1 H 0.49 0.02 1 8 . 3 VAL H H 8.23 0.02 1 9 . 3 VAL HA H 3.59 0.02 1 10 . 3 VAL HB H 1.93 0.02 1 11 . 3 VAL HG1 H 0.92 0.02 2 12 . 3 VAL HG2 H 0.88 0.02 2 13 . 4 GLU H H 8.33 0.02 1 14 . 4 GLU HA H 4.12 0.02 1 15 . 4 GLU HB2 H 2.16 0.02 2 16 . 4 GLU HB3 H 2.04 0.02 2 17 . 4 GLU HG2 H 2.48 0.02 1 18 . 4 GLU HG3 H 2.48 0.02 1 19 . 5 GLN H H 8.34 0.02 1 20 . 5 GLN HA H 4.04 0.02 1 21 . 5 GLN HB2 H 2.07 0.02 2 22 . 5 GLN HB3 H 2.13 0.02 2 23 . 5 GLN HG2 H 2.48 0.02 2 24 . 5 GLN HG3 H 2.38 0.02 2 25 . 6 CYS H H 8.36 0.02 1 26 . 6 CYS HA H 5.04 0.02 1 27 . 6 CYS HB2 H 3.36 0.02 2 28 . 6 CYS HB3 H 2.83 0.02 2 29 . 7 CYS H H 8.19 0.02 1 30 . 7 CYS HA H 4.86 0.02 1 31 . 7 CYS HB2 H 3.75 0.02 2 32 . 7 CYS HB3 H 3.29 0.02 2 33 . 8 THR H H 8.13 0.02 1 34 . 8 THR HA H 4.06 0.02 1 35 . 8 THR HB H 4.41 0.02 1 36 . 8 THR HG2 H 1.25 0.02 1 37 . 9 SER HA H 4.73 0.02 1 38 . 9 SER HB2 H 3.83 0.02 2 39 . 9 SER HB3 H 4.00 0.02 2 40 . 10 ILE H H 7.86 0.02 1 41 . 10 ILE HA H 4.27 0.02 1 42 . 10 ILE HB H 1.57 0.02 1 43 . 10 ILE HG12 H 1.12 0.02 2 44 . 10 ILE HG13 H 0.43 0.02 2 45 . 10 ILE HG2 H 0.66 0.02 1 46 . 10 ILE HD1 H 0.49 0.02 1 47 . 11 CYS H H 9.70 0.02 1 48 . 11 CYS HA H 4.94 0.02 1 49 . 11 CYS HB2 H 3.29 0.02 2 50 . 11 CYS HB3 H 2.96 0.02 2 51 . 12 SER H H 8.69 0.02 1 52 . 12 SER HA H 4.62 0.02 1 53 . 12 SER HB2 H 4.00 0.02 2 54 . 12 SER HB3 H 4.16 0.02 2 55 . 13 LEU H H 8.69 0.02 1 56 . 13 LEU HA H 3.86 0.02 1 57 . 13 LEU HB2 H 1.41 0.02 2 58 . 13 LEU HB3 H 1.47 0.02 2 59 . 13 LEU HG H 1.52 0.02 1 60 . 13 LEU HD1 H 0.84 0.02 2 61 . 13 LEU HD2 H 0.76 0.02 2 62 . 14 TYR H H 7.65 0.02 1 63 . 14 TYR HA H 4.33 0.02 1 64 . 14 TYR HB2 H 2.99 0.02 2 65 . 14 TYR HB3 H 3.01 0.02 2 66 . 14 TYR HD1 H 7.12 0.02 1 67 . 14 TYR HD2 H 7.12 0.02 1 68 . 14 TYR HE1 H 6.86 0.02 1 69 . 14 TYR HE2 H 6.86 0.02 1 70 . 15 GLN H H 7.46 0.02 1 71 . 15 GLN HA H 3.98 0.02 1 72 . 15 GLN HB2 H 2.22 0.02 2 73 . 15 GLN HB3 H 2.33 0.02 2 74 . 15 GLN HG2 H 2.39 0.02 2 75 . 15 GLN HG3 H 2.35 0.02 2 76 . 16 LEU H H 7.86 0.02 1 77 . 16 LEU HA H 4.08 0.02 1 78 . 16 LEU HB2 H 1.34 0.02 2 79 . 16 LEU HB3 H 1.97 0.02 2 80 . 16 LEU HG H 1.74 0.02 1 81 . 16 LEU HD1 H 0.76 0.02 2 82 . 16 LEU HD2 H 0.72 0.02 2 83 . 17 GLU H H 7.96 0.02 1 84 . 17 GLU HA H 4.24 0.02 1 85 . 17 GLU HB2 H 2.04 0.02 1 86 . 17 GLU HB3 H 2.04 0.02 1 87 . 17 GLU HG2 H 2.48 0.02 2 88 . 17 GLU HG3 H 2.26 0.02 2 89 . 18 ASN H H 7.30 0.02 1 90 . 18 ASN HA H 4.48 0.02 1 91 . 18 ASN HB2 H 2.67 0.02 2 92 . 18 ASN HB3 H 2.56 0.02 2 93 . 18 ASN HD21 H 7.22 0.02 2 94 . 18 ASN HD22 H 6.59 0.02 2 95 . 19 TYR H H 7.97 0.02 1 96 . 19 TYR HA H 4.24 0.02 1 97 . 19 TYR HB2 H 3.48 0.02 2 98 . 19 TYR HB3 H 2.79 0.02 2 99 . 19 TYR HD1 H 7.32 0.02 1 100 . 19 TYR HD2 H 7.32 0.02 1 101 . 19 TYR HE1 H 6.80 0.02 1 102 . 19 TYR HE2 H 6.80 0.02 1 103 . 20 CYS H H 7.24 0.02 1 104 . 20 CYS HA H 5.16 0.02 1 105 . 20 CYS HB2 H 3.31 0.02 2 106 . 20 CYS HB3 H 2.81 0.02 2 107 . 21 ASN H H 8.03 0.02 1 108 . 21 ASN HA H 4.49 0.02 1 109 . 21 ASN HB2 H 2.77 0.02 2 110 . 21 ASN HB3 H 2.64 0.02 2 111 . 21 ASN HD21 H 7.49 0.02 2 112 . 21 ASN HD22 H 6.80 0.02 2 stop_ save_ save_chemical_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D NOESY' '2D TOCSY' DQF-COSY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'insulin analogue chain B' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 PHE HA H 4.08 0.02 1 2 . 1 PHE HB2 H 3.10 0.02 1 3 . 1 PHE HB3 H 3.10 0.02 1 4 . 1 PHE HD1 H 7.22 0.02 1 5 . 1 PHE HD2 H 7.22 0.02 1 6 . 1 PHE HE1 H 7.31 0.02 1 7 . 1 PHE HE2 H 7.31 0.02 1 8 . 2 VAL HA H 4.09 0.02 1 9 . 2 VAL HB H 1.95 0.02 1 10 . 2 VAL HG1 H 0.93 0.02 1 11 . 2 VAL HG2 H 0.93 0.02 1 12 . 3 ASN H H 8.54 0.02 1 13 . 3 ASN HA H 4.59 0.02 1 14 . 3 ASN HB2 H 2.81 0.02 2 15 . 3 ASN HB3 H 2.73 0.02 2 16 . 4 GLN HA H 4.48 0.02 1 17 . 4 GLN HB2 H 2.08 0.02 2 18 . 4 GLN HB3 H 1.93 0.02 2 19 . 4 GLN HG2 H 2.20 0.02 2 20 . 4 GLN HG3 H 2.17 0.02 2 21 . 5 HIS H H 8.49 0.02 1 22 . 5 HIS HA H 4.43 0.02 1 23 . 5 HIS HB2 H 3.44 0.02 2 24 . 5 HIS HB3 H 3.10 0.02 2 25 . 6 LEU H H 8.96 0.02 1 26 . 6 LEU HA H 4.61 0.02 1 27 . 6 LEU HB2 H 1.73 0.02 2 28 . 6 LEU HB3 H 0.82 0.02 2 29 . 6 LEU HG H 1.62 0.02 2 30 . 6 LEU HD1 H 0.85 0.02 2 31 . 6 LEU HD2 H 0.74 0.02 2 32 . 7 CYS H H 8.86 0.02 1 33 . 7 CYS HA H 4.94 0.02 1 34 . 7 CYS HB2 H 3.23 0.02 2 35 . 7 CYS HB3 H 2.97 0.02 2 36 . 8 GLY HA2 H 3.96 0.02 2 37 . 8 GLY HA3 H 3.79 0.02 2 38 . 9 SER H H 8.04 0.02 1 39 . 9 SER HA H 4.21 0.02 1 40 . 9 SER HB2 H 3.93 0.02 2 41 . 9 SER HB3 H 4.06 0.02 2 42 . 10 ASP H H 8.07 0.02 1 43 . 10 ASP HA H 4.40 0.02 2 44 . 10 ASP HB2 H 3.02 0.02 2 45 . 10 ASP HB3 H 2.66 0.02 2 46 . 11 LEU H H 6.96 0.02 1 47 . 11 LEU HA H 3.93 0.02 1 48 . 11 LEU HB2 H 1.82 0.02 2 49 . 11 LEU HB3 H 1.16 0.02 2 50 . 11 LEU HG H 1.25 0.02 1 51 . 11 LEU HD1 H 0.72 0.02 2 52 . 11 LEU HD2 H 0.64 0.02 2 53 . 12 ABA H H 7.08 0.02 1 54 . 12 ABA HA H 3.48 0.02 1 55 . 12 ABA HB2 H 1.92 0.02 2 56 . 12 ABA HB3 H 1.84 0.02 2 57 . 12 ABA HG H 1.04 0.02 2 58 . 13 GLU H H 7.91 0.02 1 59 . 13 GLU HA H 4.08 0.02 1 60 . 13 GLU HB2 H 2.32 0.02 2 61 . 13 GLU HB3 H 2.09 0.02 2 62 . 13 GLU HG2 H 2.47 0.02 1 63 . 13 GLU HG3 H 2.47 0.02 1 64 . 14 ALA H H 7.58 0.02 1 65 . 14 ALA HA H 4.07 0.02 1 66 . 14 ALA HB H 1.38 0.02 1 67 . 15 LEU H H 8.05 0.02 2 68 . 15 LEU HA H 3.69 0.02 1 69 . 15 LEU HB2 H 0.88 0.02 2 70 . 15 LEU HB3 H 1.25 0.02 2 71 . 15 LEU HG H 1.24 0.02 1 72 . 15 LEU HD1 H 0.54 0.02 2 73 . 15 LEU HD2 H 0.18 0.02 2 74 . 16 TYR H H 8.03 0.02 1 75 . 16 TYR HA H 4.39 0.02 1 76 . 16 TYR HB2 H 3.20 0.02 2 77 . 16 TYR HB3 H 3.17 0.02 2 78 . 16 TYR HD1 H 7.26 0.02 1 79 . 16 TYR HD2 H 7.26 0.02 1 80 . 16 TYR HE1 H 6.85 0.02 1 81 . 16 TYR HE2 H 6.85 0.02 1 82 . 17 LEU H H 7.77 0.02 1 83 . 17 LEU HA H 4.04 0.02 1 84 . 17 LEU HB2 H 1.80 0.02 2 85 . 17 LEU HB3 H 1.93 0.02 2 86 . 17 LEU HG H 1.92 0.02 2 87 . 17 LEU HD1 H 0.94 0.02 1 88 . 17 LEU HD2 H 0.94 0.02 1 89 . 18 VAL H H 8.33 0.02 1 90 . 18 VAL HA H 3.73 0.02 1 91 . 18 VAL HB H 1.97 0.02 1 92 . 18 VAL HG1 H 0.99 0.02 2 93 . 18 VAL HG2 H 0.83 0.02 2 94 . 19 CYS H H 8.76 0.02 1 95 . 19 CYS HA H 4.81 0.02 1 96 . 19 CYS HB2 H 3.28 0.02 2 97 . 19 CYS HB3 H 2.88 0.02 2 98 . 20 GLY H H 7.81 0.02 1 99 . 20 GLY HA2 H 3.96 0.02 2 100 . 20 GLY HA3 H 3.79 0.02 2 101 . 21 GLU H H 9.09 0.02 1 102 . 21 GLU HA H 4.18 0.02 1 103 . 21 GLU HB2 H 2.21 0.02 2 104 . 21 GLU HB3 H 2.05 0.02 2 105 . 21 GLU HG2 H 2.38 0.02 1 106 . 21 GLU HG3 H 2.38 0.02 1 107 . 22 ARG H H 8.08 0.02 1 108 . 22 ARG HA H 4.16 0.02 1 109 . 22 ARG HB2 H 2.17 0.02 2 110 . 22 ARG HB3 H 2.08 0.02 2 111 . 22 ARG HG2 H 1.88 0.02 2 112 . 22 ARG HG3 H 1.85 0.02 2 113 . 22 ARG HD2 H 3.31 0.02 1 114 . 22 ARG HD3 H 3.31 0.02 1 115 . 23 GLY H H 7.33 0.02 1 116 . 23 GLY HA2 H 4.14 0.02 2 117 . 23 GLY HA3 H 3.82 0.02 2 118 . 24 PHE H H 7.62 0.02 1 119 . 24 PHE HA H 5.28 0.02 1 120 . 24 PHE HB2 H 3.21 0.02 2 121 . 24 PHE HB3 H 2.90 0.02 2 122 . 24 PHE HD1 H 6.71 0.02 1 123 . 24 PHE HD2 H 6.71 0.02 1 124 . 24 PHE HE1 H 6.92 0.02 1 125 . 24 PHE HE2 H 6.92 0.02 1 126 . 24 PHE HZ H 7.04 0.02 1 127 . 25 PHE H H 8.56 0.02 1 128 . 25 PHE HA H 4.87 0.02 1 129 . 25 PHE HB2 H 3.21 0.02 2 130 . 25 PHE HB3 H 3.23 0.02 2 131 . 25 PHE HD1 H 7.22 0.02 1 132 . 25 PHE HD2 H 7.22 0.02 1 133 . 25 PHE HE1 H 7.36 0.02 1 134 . 25 PHE HE2 H 7.36 0.02 1 135 . 26 TYR H H 8.21 0.02 1 136 . 26 TYR HA H 4.68 0.02 1 137 . 26 TYR HB2 H 2.99 0.02 2 138 . 26 TYR HB3 H 2.97 0.02 2 139 . 26 TYR HD1 H 6.98 0.02 1 140 . 26 TYR HD2 H 6.98 0.02 1 141 . 26 TYR HE1 H 6.68 0.02 1 142 . 26 TYR HE2 H 6.68 0.02 1 143 . 27 THR H H 7.77 0.02 1 144 . 27 THR HA H 4.46 0.02 1 145 . 27 THR HB H 4.11 0.02 2 146 . 27 THR HG2 H 1.20 0.02 1 147 . 28 LYS H H 8.40 0.02 1 148 . 28 LYS HA H 4.37 0.02 1 149 . 28 LYS HB2 H 1.72 0.02 2 150 . 28 LYS HB3 H 1.79 0.02 2 151 . 28 LYS HG2 H 1.42 0.02 1 152 . 28 LYS HG3 H 1.42 0.02 1 153 . 28 LYS HE2 H 2.92 0.02 1 154 . 28 LYS HE3 H 2.92 0.02 1 155 . 29 PRO HA H 4.45 0.02 1 156 . 29 PRO HB2 H 2.29 0.02 2 157 . 29 PRO HB3 H 2.04 0.02 2 158 . 29 PRO HG2 H 1.96 0.02 1 159 . 29 PRO HG3 H 1.96 0.02 1 160 . 30 THR H H 7.80 0.02 1 161 . 30 THR HA H 4.13 0.02 1 162 . 30 THR HB H 4.24 0.02 1 163 . 30 THR HG2 H 1.20 0.02 1 stop_ save_