data_4875 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4875 _Entry.Title ; 1H NMR Analysis of the partly-folded non-native two-disulphide intermediates (30-51, 5-14) and (30-51, 5-38) in the folding pathway of bovine pancreatic trypsin inhibitor ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2000-10-23 _Entry.Accession_date 2000-10-23 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Carlo 'van Mierlo' . P.M. . 4875 2 Johan Kemmink . . . 4875 3 David Neuhaus . . . 4875 4 Nigel Darby . J. . 4875 5 Thomas Creighton . E. . 4875 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4875 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 370 4875 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 2 . . 2000-11-29 . original author 'Original release.' 4875 1 . . 2002-08-12 . update BMRB 'Modify the saveframe name.' 4875 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 2169 '(5-55)Ser BPTI folding intermediate' 4875 BMRB 4855 '(14-38, 30-51)Ser BPTI folding intermediate' 4875 BMRB 4868 BPTI-R52 4875 BMRB 4873 '(30-51)Ser BPTI folding intermediate' 4875 BMRB 4877 '(30-51, 5-38)Ser BPTI folding intermediate' 4875 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4875 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 94118338 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; 1H NMR Analysis of the partly-folded non-native two-disulphide intermediates (30-51, 5-14) and (30-51, 5-38) in the folding pathway of bovine pancreatic trypsin inhibitor ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 235 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 1044 _Citation.Page_last 1061 _Citation.Year 1994 _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 Carlo 'van Mierlo' . P.M. . 4875 1 2 Johan Kemmink . . . 4875 1 3 David Neuhaus . . . 4875 1 4 Nigel Darby . J. . 4875 1 5 Thomas Creighton . E. . 4875 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'bovine pancreatic trypsin inhibitor (BPTI)' 4875 1 'disulphide bonds' 4875 1 'folding intermediate' 4875 1 NMR 4875 1 'protein folding' 4875 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4875 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1960732 _Citation.Full_citation ; van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE. Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor. J Mol Biol. 1991 Nov 20;222(2):373-90. ; _Citation.Title 'Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 222 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _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 373 _Citation.Page_last 390 _Citation.Year 1991 _Citation.Details ; An analogue of the bovine pancreatic trypsin inhibitor (BPTI) folding intermediate that contains only the disulphide bond between Cys5 and Cys55 has been prepared in Escherichia coli by protein engineering methods, with the other four Cys residues replaced by Ser. Two-dimensional 1H nuclear magnetic resonance studies of the analogue have resulted in essentially complete resonance assignments of the folded form of the protein. The folded protein has a compact conformation that is structurally very similar to that of native BPTI, although there are subtle differences and the folded conformation is not very stable. Approximately half of the protein molecules are unfolded at 3 degrees C, and this proportion increases at higher temperatures. The folded and unfolded conformations are in slow exchange. The conformational properties of the analogue can explain many aspects of the kinetic role that the normal (5-55) intermediate plays in the folding of BPTI. ; 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 'C. P.' 'van Mierlo' C. P. . 4875 2 2 'N. J.' Darby N. J. . 4875 2 3 D. Neuhaus D. . . 4875 2 4 'T. E.' Creighton T. E. . 4875 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4875 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1704858 _Citation.Full_citation ; Darby NJ, van Mierlo CP, Creighton TE. The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor. FEBS Lett. 1991 Feb 11;279(1):61-4. ; _Citation.Title 'The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'FEBS Lett.' _Citation.Journal_name_full 'FEBS letters' _Citation.Journal_volume 279 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0014-5793 _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 61 _Citation.Page_last 64 _Citation.Year 1991 _Citation.Details ; An analogue of the BPT1 folding intermediate that contains only the disulphide bond between Cys-5 and Cys-55 has been prepared by mutation of the other four Cys residues to Ser. On the basis of its circular dichroism and 1H-nuclear magnetic resonance spectra and its electrophoretic mobility, this intermediate is shown to be at least partially folded at low temperatures. This probably accounts for several of the unique properties of this intermediate observed during folding. ; 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 'N. J.' Darby N. J. . 4875 3 2 'C. P.' 'van Mierlo' C. P. . 4875 3 3 'T. E.' Creighton T. E. . 4875 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4875 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1960731 _Citation.Full_citation ; van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE (14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study. J Mol Biol. 1991 Nov 20;222(2):353-71. ; _Citation.Title '(14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 222 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _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 353 _Citation.Page_last 371 _Citation.Year 1991 _Citation.Details ; An analogue of the BPTI folding intermediate that contains only the disulphide bonds between Cys14 and Cys38 and between Cys30 and Cys51 has been prepared in Escherichia coli by protein engineering methods. The other two Cys residues of native BPTI (at positions 5 and 55) have been replaced by Ser. Essentially complete proton resonance assignments of the analogue were obtained by employing two-dimensional 1H nuclear magnetic resonance techniques. The intermediate has a more extended conformation in the N-terminal (residues 1 to 7) region and there are other differences in the C-terminal (residues 55 to 58) region. The remainder of the protein is substantially identical to native BPTI. The conformational properties of the analogue can explain several aspects of the kinetic role that the normal (14-38, 30-51) intermediate plays in the folding of BPTI. ; 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 'C. P.' 'van Mierlo' C. P. . 4875 4 2 'N. J.' Darby N. J. . 4875 4 3 D. Neuhaus D. . . 4875 4 4 'T. E.' Creighton T. E. . 4875 4 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 4875 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1373775 _Citation.Full_citation ; Darby NJ, van Mierlo CP, Scott GH, Neuhaus D, Creighton TE. Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor. J Mol Biol. 1992 Apr 20;224(4):905-11. ; _Citation.Title 'Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 224 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _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 905 _Citation.Page_last 911 _Citation.Year 1992 _Citation.Details ; The most productive folding pathway of reduced bovine pancreatic trypsin inhibitor (BPTI) proceeds through the disulphide intermediates (30-51), (30-51, 5-14), and (30-51, 5-38); these are important kinetic intermediates in folding, even though the latter pair contain non-native disulphide bonds. Analogues of these intermediates have been prepared by protein engineering methods and their conformational properties examined by circular dichroism and 1H-nuclear magnetic resonance. The (30-51), (30-51, 5-14) and (30-51, 5-38) analogues exhibit comparable degrees of stable structure, which cannot include those portions of the polypeptide chain involving Cys5, Cys14 and Cys38. These properties are consistent with the roles of (30-51, 5-14) and (30-51, 5-38) in the folding pathway of BPTI, which demand that they exhibit a considerable degree of conformational flexibility in part of the molecule. ; 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 'N. J.' Darby N. J. . 4875 5 2 'C. P.' 'van Mierlo' C. P. . 4875 5 3 'G. H.' Scott G. H. . 4875 5 4 D. Neuhaus D. . . 4875 5 5 'T. E.' Creighton T. E. . 4875 5 stop_ save_ save_ref_5 _Citation.Sf_category citations _Citation.Sf_framecode ref_5 _Citation.Entry_ID 4875 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1379719 _Citation.Full_citation ; van Mierlo CP, Darby NJ, Creighton TE. The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):6775-9. ; _Citation.Title 'The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proc. Natl. Acad. Sci. U.S.A.' _Citation.Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Citation.Journal_volume 89 _Citation.Journal_issue 15 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0027-8424 _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 6775 _Citation.Page_last 6779 _Citation.Year 1992 _Citation.Details ; The best-characterized protein folding pathway is that of bovine pancreatic trypsin inhibitor, which folds from the reduced form through a series of disulfide bond intermediates. The crucial one-disulfide intermediate of bovine pancreatic trypsin inhibitor with the disulfide bond between Cys-30 and Cys-51 is shown here to have a partially folded conformation in which the major elements of secondary structure interact via a core of apolar side chains, which resembles part of the native conformation. The stability of this structure can account for the predominance of this one-disulfide intermediate during folding. Much of the remaining one-third of the polypeptide chain, in particular the N-terminal 14 residues, is largely disordered; this accounts for the ability of this intermediate to form readily any of the three possible second disulfide bonds involving Cys-5, -14, and -38. The partially folded conformation of this intermediate provides direct evidence for the importance of native-like interactions between elements of secondary structure in directing protein folding, which is assumed in many studies. ; 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 'C. P.' 'van Mierlo' C. P. . 4875 6 2 'N. J.' Darby N. J. . 4875 6 3 'T. E.' Creighton T. E. . 4875 6 stop_ save_ save_ref_6 _Citation.Sf_category citations _Citation.Sf_framecode ref_6 _Citation.Entry_ID 4875 _Citation.ID 7 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7680380 _Citation.Full_citation ; van Mierlo CP, Darby NJ, Keeler J, Neuhaus D, Creighton TE. Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements. J Mol Biol. 1993 Feb 20;229(4):1125-46. ; _Citation.Title 'Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 229 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _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 1125 _Citation.Page_last 1146 _Citation.Year 1993 _Citation.Details ; An analogue of the important folding intermediate of BPTI with only the disulphide bond between Cys30 and Cys51 has been characterized by 1H and 15N NMR techniques. In particular, the dynamics of the polypeptide backbone were characterized using (1H)-15N NOE and 15N T1 and T2 relaxation data. The intermediate is partially folded, with part of the polypeptide chain stably folded and the remainder flexible or unfolded. The folded portion consists of the major elements of native-like secondary structure interacting through the hydrophobic core of the molecule. The 15N relaxation data show that the N-terminal 15 residues are very flexible, and the (1H, 1H) NOESY data show that these residues have no NOE interactions with the remainder of the molecule. The segment of residues 37 to 41 is also flexible. These observations explain why during folding this intermediate most readily forms any of the possible disulphide bonds between Cys5, Cys14 and Cys38, including the non-native 5-14 and 5-38 bonds. The native-like folded portion of the molecule limits the possible disulphide bonds that can be formed to those in the remainder of the polypeptide chain. Also, forming the non-native disulphide bonds need not involve any disruption of that folded structure, as the Cys residues involved are in flexible regions of the molecule. ; 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 'C P' 'van Mierlo' C. P. . 4875 7 2 'N J' Darby N. J. . 4875 7 3 J Keeler J. . . 4875 7 4 D Neuhaus D. . . 4875 7 5 'T E' Creighton T. E. . 4875 7 stop_ save_ save_ref_7 _Citation.Sf_category citations _Citation.Sf_framecode ref_7 _Citation.Entry_ID 4875 _Citation.ID 8 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7507172 _Citation.Full_citation ; van Mierlo CP, Kemmink J, Neuhaus D, Darby NJ, Creighton TE. 1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor. J Mol Biol. 1994 Jan 21;235(3):1044-61. ; _Citation.Title '1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 235 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _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 1044 _Citation.Page_last 1061 _Citation.Year 1994 _Citation.Details ; The conformational properties of analogues of the (30-51,5-14) and (30-51,5-38) disulphide intermediates in refolding of reduced BPTI, with non-native second disulphide bonds, have been characterized in detail by 1H NMR analysis. They are shown to have partly-folded conformations, very similar to that of the (30-51) one-disulphide intermediate from which they arise during folding. The non-native disulphide bonds are formed in flexible or unfolded parts of the polypeptide chain; they do not disrupt the folded portion nor do they introduce substantial non-native conformation. The conformational properties of these intermediates explain their important roles in the folding pathway. ; 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 'C P' 'van Mierlo' C. P. . 4875 8 2 J Kemmink J. . . 4875 8 3 D Neuhaus D. . . 4875 8 4 'N J' Darby N. J. . 4875 8 5 'T E' Creighton T. E. . 4875 8 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_(30-51_5-14)Ser_BPTI_folding_intermediate _Assembly.Sf_category assembly _Assembly.Sf_framecode (30-51_5-14)Ser_BPTI_folding_intermediate _Assembly.Entry_ID 4875 _Assembly.ID 1 _Assembly.Name '(30-51, 5-14)Ser BPTI folding intermediate' _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 4875 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 '(30-51, 5-14) BPTI' 1 $(30-51_5-14)_BPTI . . . native . . . . . 4875 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_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_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 5 5 SG . 1 . 1 CYS 14 14 SG . . . . . . . . . . 4875 1 2 disulfide single . 1 . 1 CYS 30 30 SG . 1 . 1 CYS 51 51 SG . . . . . . . . . . 4875 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID '(30-51, 5-14)Ser BPTI folding intermediate' abbreviation 4875 1 '(30-51, 5-14)Ser BPTI folding intermediate' system 4875 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID ; The species discussed is a stable mimick of the (30-51, 5-14) folding intermediate in BPTI folding" ; 4875 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_(30-51_5-14)_BPTI _Entity.Sf_category entity _Entity.Sf_framecode (30-51_5-14)_BPTI _Entity.Entry_ID 4875 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name '(30-51, 5-14)Ser BPTI folding intermediate' _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 ; RPDFCLEPPYTGPCKARIIR YFYNAKAGLCQTFVYGGSRA KRNNFKSAEDCRRTSGGA ; _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 58 _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 . _Entity.DB_query_revised_last_date 2005-12-09 loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID '(30-51, 5-14) BPTI' abbreviation 4875 1 '(30-51, 5-14)Ser BPTI folding intermediate' common 4875 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 . ARG . 4875 1 2 . PRO . 4875 1 3 . ASP . 4875 1 4 . PHE . 4875 1 5 . CYS . 4875 1 6 . LEU . 4875 1 7 . GLU . 4875 1 8 . PRO . 4875 1 9 . PRO . 4875 1 10 . TYR . 4875 1 11 . THR . 4875 1 12 . GLY . 4875 1 13 . PRO . 4875 1 14 . CYS . 4875 1 15 . LYS . 4875 1 16 . ALA . 4875 1 17 . ARG . 4875 1 18 . ILE . 4875 1 19 . ILE . 4875 1 20 . ARG . 4875 1 21 . TYR . 4875 1 22 . PHE . 4875 1 23 . TYR . 4875 1 24 . ASN . 4875 1 25 . ALA . 4875 1 26 . LYS . 4875 1 27 . ALA . 4875 1 28 . GLY . 4875 1 29 . LEU . 4875 1 30 . CYS . 4875 1 31 . GLN . 4875 1 32 . THR . 4875 1 33 . PHE . 4875 1 34 . VAL . 4875 1 35 . TYR . 4875 1 36 . GLY . 4875 1 37 . GLY . 4875 1 38 . SER . 4875 1 39 . ARG . 4875 1 40 . ALA . 4875 1 41 . LYS . 4875 1 42 . ARG . 4875 1 43 . ASN . 4875 1 44 . ASN . 4875 1 45 . PHE . 4875 1 46 . LYS . 4875 1 47 . SER . 4875 1 48 . ALA . 4875 1 49 . GLU . 4875 1 50 . ASP . 4875 1 51 . CYS . 4875 1 52 . ARG . 4875 1 53 . ARG . 4875 1 54 . THR . 4875 1 55 . SER . 4875 1 56 . GLY . 4875 1 57 . GLY . 4875 1 58 . ALA . 4875 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 . ARG 1 1 4875 1 . PRO 2 2 4875 1 . ASP 3 3 4875 1 . PHE 4 4 4875 1 . CYS 5 5 4875 1 . LEU 6 6 4875 1 . GLU 7 7 4875 1 . PRO 8 8 4875 1 . PRO 9 9 4875 1 . TYR 10 10 4875 1 . THR 11 11 4875 1 . GLY 12 12 4875 1 . PRO 13 13 4875 1 . CYS 14 14 4875 1 . LYS 15 15 4875 1 . ALA 16 16 4875 1 . ARG 17 17 4875 1 . ILE 18 18 4875 1 . ILE 19 19 4875 1 . ARG 20 20 4875 1 . TYR 21 21 4875 1 . PHE 22 22 4875 1 . TYR 23 23 4875 1 . ASN 24 24 4875 1 . ALA 25 25 4875 1 . LYS 26 26 4875 1 . ALA 27 27 4875 1 . GLY 28 28 4875 1 . LEU 29 29 4875 1 . CYS 30 30 4875 1 . GLN 31 31 4875 1 . THR 32 32 4875 1 . PHE 33 33 4875 1 . VAL 34 34 4875 1 . TYR 35 35 4875 1 . GLY 36 36 4875 1 . GLY 37 37 4875 1 . SER 38 38 4875 1 . ARG 39 39 4875 1 . ALA 40 40 4875 1 . LYS 41 41 4875 1 . ARG 42 42 4875 1 . ASN 43 43 4875 1 . ASN 44 44 4875 1 . PHE 45 45 4875 1 . LYS 46 46 4875 1 . SER 47 47 4875 1 . ALA 48 48 4875 1 . GLU 49 49 4875 1 . ASP 50 50 4875 1 . CYS 51 51 4875 1 . ARG 52 52 4875 1 . ARG 53 53 4875 1 . THR 54 54 4875 1 . SER 55 55 4875 1 . GLY 56 56 4875 1 . GLY 57 57 4875 1 . ALA 58 58 4875 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 4875 _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 $(30-51_5-14)_BPTI . 9913 organism . 'Bos taurus' cow . . Eukaryota Metazoa Bos taurus . . . . . . . . . . . . . . . . . . . . . 4875 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 4875 _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 $(30-51_5-14)_BPTI . 'recombinant technology' 'Escherichia coli' 'E. coli' . . 'Escherichia coli' . . . . . . . . . . . . . . . . . . . . . ; See: Darby et al. (1991) FEBS Letters, 279, 61-64; Darby and Creighton (1993) J. Mol. Biol. 232, 873 - 896; van Mierlo et al. (1993) J. Mol. Biol. 229, 1125 - 1146. ; . . 4875 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4875 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details ; no salt was added to the sample, pH 4.6, the pH was adjusted by adding small amounts of NaOH ; _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 '(30-51, 5-14)Ser BPTI folding intermediate' . . . 1 $(30-51_5-14)_BPTI . . . 1.5 3 mM . . . . 4875 1 2 H2O . . . . . . . 90 . . % . . . . 4875 1 3 D2O . . . . . . . 10 . . % . . . . 4875 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 4875 _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 '(30-51, 5-14)Ser BPTI folding intermediate' . . . 1 $(30-51_5-14)_BPTI . . . 1.5 3 mM . . . . 4875 2 2 D2O . . . . . . . 100 . . % . . . . 4875 2 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 4875 _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 4.6 0.1 n/a 4875 1 temperature 271 0.5 K 4875 1 stop_ save_ ############################ # Computer software used # ############################ save_UXNMR _Software.Sf_category software _Software.Sf_framecode UXNMR _Software.Entry_ID 4875 _Software.ID 1 _Software.Name UXNMR _Software.Version . _Software.Details 'Software versions as availabe in 1991 - 1992.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data acquisition' 4875 1 'data processing' 4875 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 4875 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4875 _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 Bruker AMX . 500 . . . 4875 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 4875 _Experiment_list.ID 1 _Experiment_list.Details ; DQ = double quantum coherence experiment (Mareci and Freeman (1983) J. Magn. Reson. 51, 531 - 535; Wagner and Zuiderweg (1983) Biochem. Biophys. Res. Commun. 113, 854 - 860). ; 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 'DQ = double quantum coherence experiment' . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4875 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 4875 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 TSP methyl . . . . ppm 0.00 internal direct . internal . . . . . . . . 4875 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_CSR_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode CSR_1 _Assigned_chem_shift_list.Entry_ID 4875 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details ; The N-terminal part of the molecule is flexible. In addition, two major species of the N-terminal part, referred to here as A and B, were apparant from doubling of the proton resonances for residues 2 to 13. A population ratio of approximately 37 % A: 63 % B is observed. Assignments for species A are given here, for assignments of species B, see van Mierlo et al. J. Mol. Biol. (1994) 235, 1044 - 1061. The HE1, HE2 and HZ protons of Phe4 resonate between 7.20 - 7.40 ppm, it was not possible to determine their exact resonance position due to near coincidence of these resonances. ; _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_1 . 4875 1 . . 2 $sample_2 . 4875 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 ARG HA H 1 4.42 0.01 . 1 . . . . . . . . 4875 1 2 . 1 1 1 1 ARG HB2 H 1 1.96 0.01 . 2 . . . . . . . . 4875 1 3 . 1 1 1 1 ARG HG2 H 1 1.70 0.01 . 1 . . . . . . . . 4875 1 4 . 1 1 1 1 ARG HG3 H 1 1.70 0.01 . 1 . . . . . . . . 4875 1 5 . 1 1 1 1 ARG HD2 H 1 3.20 0.01 . 1 . . . . . . . . 4875 1 6 . 1 1 1 1 ARG HD3 H 1 3.20 0.01 . 1 . . . . . . . . 4875 1 7 . 1 1 1 1 ARG HE H 1 7.34 0.01 . 1 . . . . . . . . 4875 1 8 . 1 1 2 2 PRO HA H 1 4.46 0.01 . 1 . . . . . . . . 4875 1 9 . 1 1 2 2 PRO HB2 H 1 1.70 0.01 . 4 . . . . . . . . 4875 1 10 . 1 1 2 2 PRO HB3 H 1 2.25 0.01 . 2 . . . . . . . . 4875 1 11 . 1 1 2 2 PRO HG2 H 1 1.98 0.01 . 1 . . . . . . . . 4875 1 12 . 1 1 2 2 PRO HG3 H 1 1.98 0.01 . 9 . . . . . . . . 4875 1 13 . 1 1 2 2 PRO HD2 H 1 3.59 0.01 . 2 . . . . . . . . 4875 1 14 . 1 1 2 2 PRO HD3 H 1 3.77 0.01 . 2 . . . . . . . . 4875 1 15 . 1 1 3 3 ASP H H 1 8.55 0.01 . 1 . . . . . . . . 4875 1 16 . 1 1 3 3 ASP HA H 1 4.51 0.01 . 1 . . . . . . . . 4875 1 17 . 1 1 3 3 ASP HB2 H 1 2.56 0.01 . 2 . . . . . . . . 4875 1 18 . 1 1 3 3 ASP HB3 H 1 2.67 0.01 . 2 . . . . . . . . 4875 1 19 . 1 1 4 4 PHE H H 1 8.36 0.01 . 1 . . . . . . . . 4875 1 20 . 1 1 4 4 PHE HA H 1 4.86 0.01 . 1 . . . . . . . . 4875 1 21 . 1 1 4 4 PHE HB2 H 1 2.99 0.01 . 2 . . . . . . . . 4875 1 22 . 1 1 4 4 PHE HB3 H 1 3.31 0.01 . 2 . . . . . . . . 4875 1 23 . 1 1 4 4 PHE HD1 H 1 7.27 0.01 . 1 . . . . . . . . 4875 1 24 . 1 1 4 4 PHE HD2 H 1 7.27 0.01 . 1 . . . . . . . . 4875 1 25 . 1 1 4 4 PHE HE1 H 1 7.20 0.01 . 3 . . . . . . . . 4875 1 26 . 1 1 4 4 PHE HE2 H 1 7.40 0.01 . 3 . . . . . . . . 4875 1 27 . 1 1 4 4 PHE HZ H 1 7.20 0.01 . 3 . . . . . . . . 4875 1 28 . 1 1 5 5 CYS H H 1 8.94 0.01 . 1 . . . . . . . . 4875 1 29 . 1 1 5 5 CYS HA H 1 4.86 0.01 . 9 . . . . . . . . 4875 1 30 . 1 1 5 5 CYS HB2 H 1 3.07 0.01 . 9 . . . . . . . . 4875 1 31 . 1 1 5 5 CYS HB3 H 1 3.60 0.01 . 9 . . . . . . . . 4875 1 32 . 1 1 6 6 LEU HA H 1 4.37 0.01 . 1 . . . . . . . . 4875 1 33 . 1 1 6 6 LEU HB2 H 1 1.74 0.01 . 1 . . . . . . . . 4875 1 34 . 1 1 6 6 LEU HB3 H 1 1.74 0.01 . 1 . . . . . . . . 4875 1 35 . 1 1 6 6 LEU HG H 1 1.74 0.01 . 1 . . . . . . . . 4875 1 36 . 1 1 6 6 LEU HD11 H 1 0.91 0.01 . 2 . . . . . . . . 4875 1 37 . 1 1 6 6 LEU HD12 H 1 0.91 0.01 . 2 . . . . . . . . 4875 1 38 . 1 1 6 6 LEU HD13 H 1 0.91 0.01 . 2 . . . . . . . . 4875 1 39 . 1 1 6 6 LEU HD21 H 1 0.98 0.01 . 2 . . . . . . . . 4875 1 40 . 1 1 6 6 LEU HD22 H 1 0.98 0.01 . 2 . . . . . . . . 4875 1 41 . 1 1 6 6 LEU HD23 H 1 0.98 0.01 . 2 . . . . . . . . 4875 1 42 . 1 1 7 7 GLU H H 1 7.61 0.01 . 1 . . . . . . . . 4875 1 43 . 1 1 7 7 GLU HA H 1 4.78 0.01 . 1 . . . . . . . . 4875 1 44 . 1 1 7 7 GLU HB2 H 1 1.84 0.01 . 2 . . . . . . . . 4875 1 45 . 1 1 7 7 GLU HB3 H 1 2.03 0.01 . 2 . . . . . . . . 4875 1 46 . 1 1 7 7 GLU HG2 H 1 2.19 0.01 . 1 . . . . . . . . 4875 1 47 . 1 1 7 7 GLU HG3 H 1 2.19 0.01 . 1 . . . . . . . . 4875 1 48 . 1 1 8 8 PRO HA H 1 3.60 0.01 . 9 . . . . . . . . 4875 1 49 . 1 1 8 8 PRO HB2 H 1 1.72 0.01 . 9 . . . . . . . . 4875 1 50 . 1 1 8 8 PRO HB3 H 1 2.01 0.01 . 9 . . . . . . . . 4875 1 51 . 1 1 9 9 PRO HA H 1 4.45 0.01 . 1 . . . . . . . . 4875 1 52 . 1 1 10 10 TYR H H 1 8.79 0.01 . 1 . . . . . . . . 4875 1 53 . 1 1 10 10 TYR HA H 1 4.22 0.01 . 1 . . . . . . . . 4875 1 54 . 1 1 10 10 TYR HB2 H 1 3.13 0.01 . 2 . . . . . . . . 4875 1 55 . 1 1 10 10 TYR HD1 H 1 7.10 0.01 . 1 . . . . . . . . 4875 1 56 . 1 1 10 10 TYR HD2 H 1 7.10 0.01 . 1 . . . . . . . . 4875 1 57 . 1 1 10 10 TYR HE1 H 1 6.70 0.01 . 1 . . . . . . . . 4875 1 58 . 1 1 10 10 TYR HE2 H 1 6.70 0.01 . 1 . . . . . . . . 4875 1 59 . 1 1 11 11 THR H H 1 7.84 0.01 . 1 . . . . . . . . 4875 1 60 . 1 1 11 11 THR HA H 1 4.46 0.01 . 1 . . . . . . . . 4875 1 61 . 1 1 11 11 THR HB H 1 4.52 0.01 . 1 . . . . . . . . 4875 1 62 . 1 1 11 11 THR HG21 H 1 1.32 0.01 . 1 . . . . . . . . 4875 1 63 . 1 1 11 11 THR HG22 H 1 1.32 0.01 . 1 . . . . . . . . 4875 1 64 . 1 1 11 11 THR HG23 H 1 1.32 0.01 . 1 . . . . . . . . 4875 1 65 . 1 1 12 12 GLY HA2 H 1 3.78 0.01 . 9 . . . . . . . . 4875 1 66 . 1 1 12 12 GLY HA3 H 1 4.30 0.01 . 9 . . . . . . . . 4875 1 67 . 1 1 13 13 PRO HA H 1 4.66 0.01 . 1 . . . . . . . . 4875 1 68 . 1 1 13 13 PRO HB2 H 1 2.08 0.01 . 2 . . . . . . . . 4875 1 69 . 1 1 13 13 PRO HB3 H 1 2.46 0.01 . 2 . . . . . . . . 4875 1 70 . 1 1 13 13 PRO HG2 H 1 1.95 0.01 . 2 . . . . . . . . 4875 1 71 . 1 1 13 13 PRO HD2 H 1 3.55 0.01 . 2 . . . . . . . . 4875 1 72 . 1 1 13 13 PRO HD3 H 1 3.62 0.01 . 2 . . . . . . . . 4875 1 73 . 1 1 14 14 CYS H H 1 9.29 0.01 . 1 . . . . . . . . 4875 1 74 . 1 1 14 14 CYS HA H 1 4.99 0.01 . 1 . . . . . . . . 4875 1 75 . 1 1 14 14 CYS HB2 H 1 2.79 0.01 . 2 . . . . . . . . 4875 1 76 . 1 1 14 14 CYS HB3 H 1 3.49 0.01 . 2 . . . . . . . . 4875 1 77 . 1 1 15 15 LYS H H 1 9.00 0.01 . 1 . . . . . . . . 4875 1 78 . 1 1 15 15 LYS HA H 1 4.27 0.01 . 1 . . . . . . . . 4875 1 79 . 1 1 15 15 LYS HB2 H 1 1.74 0.01 . 4 . . . . . . . . 4875 1 80 . 1 1 15 15 LYS HG2 H 1 1.49 0.01 . 9 . . . . . . . . 4875 1 81 . 1 1 15 15 LYS HD2 H 1 1.69 0.01 . 9 . . . . . . . . 4875 1 82 . 1 1 15 15 LYS HD3 H 1 1.69 0.01 . 9 . . . . . . . . 4875 1 83 . 1 1 15 15 LYS HE2 H 1 3.00 0.01 . 9 . . . . . . . . 4875 1 84 . 1 1 15 15 LYS HE3 H 1 3.00 0.01 . 9 . . . . . . . . 4875 1 85 . 1 1 15 15 LYS HZ1 H 1 7.62 0.01 . 9 . . . . . . . . 4875 1 86 . 1 1 15 15 LYS HZ2 H 1 7.62 0.01 . 9 . . . . . . . . 4875 1 87 . 1 1 15 15 LYS HZ3 H 1 7.62 0.01 . 9 . . . . . . . . 4875 1 88 . 1 1 16 16 ALA H H 1 8.58 0.01 . 1 . . . . . . . . 4875 1 89 . 1 1 16 16 ALA HA H 1 4.26 0.01 . 1 . . . . . . . . 4875 1 90 . 1 1 16 16 ALA HB1 H 1 1.37 0.01 . 1 . . . . . . . . 4875 1 91 . 1 1 16 16 ALA HB2 H 1 1.37 0.01 . 1 . . . . . . . . 4875 1 92 . 1 1 16 16 ALA HB3 H 1 1.37 0.01 . 1 . . . . . . . . 4875 1 93 . 1 1 17 17 ARG H H 1 8.52 0.01 . 1 . . . . . . . . 4875 1 94 . 1 1 17 17 ARG HA H 1 4.36 0.01 . 1 . . . . . . . . 4875 1 95 . 1 1 17 17 ARG HB2 H 1 1.74 0.01 . 2 . . . . . . . . 4875 1 96 . 1 1 17 17 ARG HG2 H 1 1.54 0.01 . 4 . . . . . . . . 4875 1 97 . 1 1 17 17 ARG HD2 H 1 3.16 0.01 . 1 . . . . . . . . 4875 1 98 . 1 1 17 17 ARG HD3 H 1 3.16 0.01 . 1 . . . . . . . . 4875 1 99 . 1 1 18 18 ILE H H 1 8.73 0.01 . 1 . . . . . . . . 4875 1 100 . 1 1 18 18 ILE HA H 1 4.21 0.01 . 1 . . . . . . . . 4875 1 101 . 1 1 18 18 ILE HB H 1 1.95 0.01 . 1 . . . . . . . . 4875 1 102 . 1 1 18 18 ILE HG12 H 1 1.20 0.01 . 2 . . . . . . . . 4875 1 103 . 1 1 18 18 ILE HG13 H 1 1.54 0.01 . 2 . . . . . . . . 4875 1 104 . 1 1 18 18 ILE HG21 H 1 0.87 0.01 . 1 . . . . . . . . 4875 1 105 . 1 1 18 18 ILE HG22 H 1 0.87 0.01 . 1 . . . . . . . . 4875 1 106 . 1 1 18 18 ILE HG23 H 1 0.87 0.01 . 1 . . . . . . . . 4875 1 107 . 1 1 18 18 ILE HD11 H 1 0.88 0.01 . 1 . . . . . . . . 4875 1 108 . 1 1 18 18 ILE HD12 H 1 0.88 0.01 . 1 . . . . . . . . 4875 1 109 . 1 1 18 18 ILE HD13 H 1 0.88 0.01 . 1 . . . . . . . . 4875 1 110 . 1 1 19 19 ILE H H 1 8.61 0.01 . 1 . . . . . . . . 4875 1 111 . 1 1 19 19 ILE HA H 1 4.46 0.01 . 1 . . . . . . . . 4875 1 112 . 1 1 19 19 ILE HB H 1 1.85 0.01 . 1 . . . . . . . . 4875 1 113 . 1 1 19 19 ILE HG12 H 1 1.28 0.01 . 2 . . . . . . . . 4875 1 114 . 1 1 19 19 ILE HG13 H 1 1.45 0.01 . 2 . . . . . . . . 4875 1 115 . 1 1 19 19 ILE HG21 H 1 0.71 0.01 . 1 . . . . . . . . 4875 1 116 . 1 1 19 19 ILE HG22 H 1 0.71 0.01 . 1 . . . . . . . . 4875 1 117 . 1 1 19 19 ILE HG23 H 1 0.71 0.01 . 1 . . . . . . . . 4875 1 118 . 1 1 19 19 ILE HD11 H 1 0.72 0.01 . 1 . . . . . . . . 4875 1 119 . 1 1 19 19 ILE HD12 H 1 0.72 0.01 . 1 . . . . . . . . 4875 1 120 . 1 1 19 19 ILE HD13 H 1 0.72 0.01 . 1 . . . . . . . . 4875 1 121 . 1 1 20 20 ARG H H 1 8.36 0.01 . 1 . . . . . . . . 4875 1 122 . 1 1 20 20 ARG HA H 1 4.72 0.01 . 1 . . . . . . . . 4875 1 123 . 1 1 20 20 ARG HB2 H 1 1.01 0.01 . 2 . . . . . . . . 4875 1 124 . 1 1 20 20 ARG HB3 H 1 1.94 0.01 . 9 . . . . . . . . 4875 1 125 . 1 1 20 20 ARG HG2 H 1 1.31 0.01 . 4 . . . . . . . . 4875 1 126 . 1 1 20 20 ARG HD2 H 1 2.89 0.01 . 9 . . . . . . . . 4875 1 127 . 1 1 20 20 ARG HD3 H 1 3.05 0.01 . 9 . . . . . . . . 4875 1 128 . 1 1 21 21 TYR H H 1 9.01 0.01 . 1 . . . . . . . . 4875 1 129 . 1 1 21 21 TYR HA H 1 5.73 0.01 . 1 . . . . . . . . 4875 1 130 . 1 1 21 21 TYR HB2 H 1 2.72 0.01 . 1 . . . . . . . . 4875 1 131 . 1 1 21 21 TYR HB3 H 1 2.72 0.01 . 1 . . . . . . . . 4875 1 132 . 1 1 21 21 TYR HD1 H 1 6.71 0.01 . 1 . . . . . . . . 4875 1 133 . 1 1 21 21 TYR HD2 H 1 6.71 0.01 . 1 . . . . . . . . 4875 1 134 . 1 1 21 21 TYR HE1 H 1 6.78 0.01 . 1 . . . . . . . . 4875 1 135 . 1 1 21 21 TYR HE2 H 1 6.78 0.01 . 1 . . . . . . . . 4875 1 136 . 1 1 22 22 PHE H H 1 9.90 0.01 . 1 . . . . . . . . 4875 1 137 . 1 1 22 22 PHE HA H 1 5.40 0.01 . 1 . . . . . . . . 4875 1 138 . 1 1 22 22 PHE HB2 H 1 3.02 0.01 . 2 . . . . . . . . 4875 1 139 . 1 1 22 22 PHE HB3 H 1 3.16 0.01 . 2 . . . . . . . . 4875 1 140 . 1 1 22 22 PHE HD1 H 1 7.15 0.01 . 1 . . . . . . . . 4875 1 141 . 1 1 22 22 PHE HD2 H 1 7.15 0.01 . 1 . . . . . . . . 4875 1 142 . 1 1 22 22 PHE HE1 H 1 7.26 0.01 . 1 . . . . . . . . 4875 1 143 . 1 1 22 22 PHE HE2 H 1 7.26 0.01 . 1 . . . . . . . . 4875 1 144 . 1 1 22 22 PHE HZ H 1 7.34 0.01 . 1 . . . . . . . . 4875 1 145 . 1 1 23 23 TYR H H 1 9.80 0.01 . 1 . . . . . . . . 4875 1 146 . 1 1 23 23 TYR HA H 1 4.46 0.01 . 1 . . . . . . . . 4875 1 147 . 1 1 23 23 TYR HB2 H 1 3.00 0.01 . 2 . . . . . . . . 4875 1 148 . 1 1 23 23 TYR HB3 H 1 3.09 0.01 . 2 . . . . . . . . 4875 1 149 . 1 1 23 23 TYR HD1 H 1 7.01 0.01 . 1 . . . . . . . . 4875 1 150 . 1 1 23 23 TYR HD2 H 1 7.01 0.01 . 1 . . . . . . . . 4875 1 151 . 1 1 23 23 TYR HE1 H 1 6.55 0.01 . 1 . . . . . . . . 4875 1 152 . 1 1 23 23 TYR HE2 H 1 6.55 0.01 . 1 . . . . . . . . 4875 1 153 . 1 1 24 24 ASN H H 1 8.02 0.01 . 1 . . . . . . . . 4875 1 154 . 1 1 24 24 ASN HA H 1 4.54 0.01 . 1 . . . . . . . . 4875 1 155 . 1 1 24 24 ASN HB2 H 1 2.25 0.01 . 2 . . . . . . . . 4875 1 156 . 1 1 24 24 ASN HB3 H 1 2.92 0.01 . 2 . . . . . . . . 4875 1 157 . 1 1 24 24 ASN HD21 H 1 8.14 0.01 . 9 . . . . . . . . 4875 1 158 . 1 1 24 24 ASN HD22 H 1 7.32 0.01 . 9 . . . . . . . . 4875 1 159 . 1 1 25 25 ALA H H 1 8.51 0.01 . 1 . . . . . . . . 4875 1 160 . 1 1 25 25 ALA HA H 1 3.63 0.01 . 1 . . . . . . . . 4875 1 161 . 1 1 25 25 ALA HB1 H 1 1.52 0.01 . 1 . . . . . . . . 4875 1 162 . 1 1 25 25 ALA HB2 H 1 1.52 0.01 . 1 . . . . . . . . 4875 1 163 . 1 1 25 25 ALA HB3 H 1 1.52 0.01 . 1 . . . . . . . . 4875 1 164 . 1 1 26 26 LYS H H 1 8.02 0.01 . 1 . . . . . . . . 4875 1 165 . 1 1 26 26 LYS HA H 1 4.09 0.01 . 1 . . . . . . . . 4875 1 166 . 1 1 26 26 LYS HB2 H 1 1.91 0.01 . 1 . . . . . . . . 4875 1 167 . 1 1 26 26 LYS HB3 H 1 1.91 0.01 . 1 . . . . . . . . 4875 1 168 . 1 1 26 26 LYS HG2 H 1 1.45 0.01 . 2 . . . . . . . . 4875 1 169 . 1 1 26 26 LYS HG3 H 1 1.52 0.01 . 2 . . . . . . . . 4875 1 170 . 1 1 26 26 LYS HD2 H 1 1.72 0.01 . 1 . . . . . . . . 4875 1 171 . 1 1 26 26 LYS HD3 H 1 1.72 0.01 . 1 . . . . . . . . 4875 1 172 . 1 1 26 26 LYS HE2 H 1 3.00 0.01 . 1 . . . . . . . . 4875 1 173 . 1 1 26 26 LYS HE3 H 1 3.00 0.01 . 1 . . . . . . . . 4875 1 174 . 1 1 26 26 LYS HZ1 H 1 7.65 0.01 . 1 . . . . . . . . 4875 1 175 . 1 1 26 26 LYS HZ2 H 1 7.65 0.01 . 1 . . . . . . . . 4875 1 176 . 1 1 26 26 LYS HZ3 H 1 7.65 0.01 . 1 . . . . . . . . 4875 1 177 . 1 1 27 27 ALA H H 1 6.94 0.01 . 1 . . . . . . . . 4875 1 178 . 1 1 27 27 ALA HA H 1 4.28 0.01 . 1 . . . . . . . . 4875 1 179 . 1 1 27 27 ALA HB1 H 1 1.22 0.01 . 1 . . . . . . . . 4875 1 180 . 1 1 27 27 ALA HB2 H 1 1.22 0.01 . 1 . . . . . . . . 4875 1 181 . 1 1 27 27 ALA HB3 H 1 1.22 0.01 . 1 . . . . . . . . 4875 1 182 . 1 1 28 28 GLY H H 1 8.20 0.01 . 1 . . . . . . . . 4875 1 183 . 1 1 28 28 GLY HA2 H 1 3.77 0.01 . 2 . . . . . . . . 4875 1 184 . 1 1 28 28 GLY HA3 H 1 3.97 0.01 . 2 . . . . . . . . 4875 1 185 . 1 1 29 29 LEU H H 1 6.95 0.01 . 1 . . . . . . . . 4875 1 186 . 1 1 29 29 LEU HA H 1 4.91 0.01 . 1 . . . . . . . . 4875 1 187 . 1 1 29 29 LEU HB2 H 1 1.38 0.01 . 2 . . . . . . . . 4875 1 188 . 1 1 29 29 LEU HB3 H 1 1.58 0.01 . 2 . . . . . . . . 4875 1 189 . 1 1 29 29 LEU HG H 1 1.46 0.01 . 1 . . . . . . . . 4875 1 190 . 1 1 29 29 LEU HD11 H 1 0.84 0.01 . 2 . . . . . . . . 4875 1 191 . 1 1 29 29 LEU HD12 H 1 0.84 0.01 . 2 . . . . . . . . 4875 1 192 . 1 1 29 29 LEU HD13 H 1 0.84 0.01 . 2 . . . . . . . . 4875 1 193 . 1 1 29 29 LEU HD21 H 1 0.89 0.01 . 2 . . . . . . . . 4875 1 194 . 1 1 29 29 LEU HD22 H 1 0.89 0.01 . 2 . . . . . . . . 4875 1 195 . 1 1 29 29 LEU HD23 H 1 0.89 0.01 . 2 . . . . . . . . 4875 1 196 . 1 1 30 30 CYS H H 1 9.28 0.01 . 1 . . . . . . . . 4875 1 197 . 1 1 30 30 CYS HA H 1 5.42 0.01 . 1 . . . . . . . . 4875 1 198 . 1 1 30 30 CYS HB2 H 1 2.60 0.01 . 2 . . . . . . . . 4875 1 199 . 1 1 30 30 CYS HB3 H 1 3.58 0.01 . 2 . . . . . . . . 4875 1 200 . 1 1 31 31 GLN H H 1 9.24 0.01 . 1 . . . . . . . . 4875 1 201 . 1 1 31 31 GLN HA H 1 4.90 0.01 . 1 . . . . . . . . 4875 1 202 . 1 1 31 31 GLN HB2 H 1 1.75 0.01 . 2 . . . . . . . . 4875 1 203 . 1 1 31 31 GLN HB3 H 1 2.09 0.01 . 2 . . . . . . . . 4875 1 204 . 1 1 31 31 GLN HG2 H 1 2.07 0.01 . 2 . . . . . . . . 4875 1 205 . 1 1 31 31 GLN HG3 H 1 2.27 0.01 . 2 . . . . . . . . 4875 1 206 . 1 1 31 31 GLN HE21 H 1 7.64 0.01 . 9 . . . . . . . . 4875 1 207 . 1 1 31 31 GLN HE22 H 1 7.27 0.01 . 9 . . . . . . . . 4875 1 208 . 1 1 32 32 THR H H 1 8.34 0.01 . 1 . . . . . . . . 4875 1 209 . 1 1 32 32 THR HA H 1 4.84 0.01 . 1 . . . . . . . . 4875 1 210 . 1 1 32 32 THR HB H 1 4.03 0.01 . 1 . . . . . . . . 4875 1 211 . 1 1 32 32 THR HG21 H 1 0.79 0.01 . 1 . . . . . . . . 4875 1 212 . 1 1 32 32 THR HG22 H 1 0.79 0.01 . 1 . . . . . . . . 4875 1 213 . 1 1 32 32 THR HG23 H 1 0.79 0.01 . 1 . . . . . . . . 4875 1 214 . 1 1 33 33 PHE H H 1 8.90 0.01 . 1 . . . . . . . . 4875 1 215 . 1 1 33 33 PHE HA H 1 4.83 0.01 . 1 . . . . . . . . 4875 1 216 . 1 1 33 33 PHE HB2 H 1 2.94 0.01 . 2 . . . . . . . . 4875 1 217 . 1 1 33 33 PHE HB3 H 1 3.15 0.01 . 2 . . . . . . . . 4875 1 218 . 1 1 33 33 PHE HD1 H 1 7.11 0.01 . 1 . . . . . . . . 4875 1 219 . 1 1 33 33 PHE HD2 H 1 7.11 0.01 . 1 . . . . . . . . 4875 1 220 . 1 1 33 33 PHE HE1 H 1 7.29 0.01 . 9 . . . . . . . . 4875 1 221 . 1 1 33 33 PHE HE2 H 1 7.29 0.01 . 9 . . . . . . . . 4875 1 222 . 1 1 33 33 PHE HZ H 1 7.18 0.01 . 9 . . . . . . . . 4875 1 223 . 1 1 34 34 VAL H H 1 8.49 0.01 . 1 . . . . . . . . 4875 1 224 . 1 1 34 34 VAL HA H 1 4.05 0.01 . 1 . . . . . . . . 4875 1 225 . 1 1 34 34 VAL HB H 1 1.91 0.01 . 1 . . . . . . . . 4875 1 226 . 1 1 34 34 VAL HG11 H 1 0.82 0.01 . 2 . . . . . . . . 4875 1 227 . 1 1 34 34 VAL HG12 H 1 0.82 0.01 . 2 . . . . . . . . 4875 1 228 . 1 1 34 34 VAL HG13 H 1 0.82 0.01 . 2 . . . . . . . . 4875 1 229 . 1 1 34 34 VAL HG21 H 1 0.85 0.01 . 2 . . . . . . . . 4875 1 230 . 1 1 34 34 VAL HG22 H 1 0.85 0.01 . 2 . . . . . . . . 4875 1 231 . 1 1 34 34 VAL HG23 H 1 0.85 0.01 . 2 . . . . . . . . 4875 1 232 . 1 1 35 35 TYR H H 1 8.78 0.01 . 1 . . . . . . . . 4875 1 233 . 1 1 35 35 TYR HA H 1 4.38 0.01 . 1 . . . . . . . . 4875 1 234 . 1 1 35 35 TYR HB2 H 1 2.48 0.01 . 2 . . . . . . . . 4875 1 235 . 1 1 35 35 TYR HB3 H 1 2.77 0.01 . 2 . . . . . . . . 4875 1 236 . 1 1 35 35 TYR HD1 H 1 7.09 0.01 . 1 . . . . . . . . 4875 1 237 . 1 1 35 35 TYR HD2 H 1 7.09 0.01 . 1 . . . . . . . . 4875 1 238 . 1 1 35 35 TYR HE1 H 1 6.88 0.01 . 1 . . . . . . . . 4875 1 239 . 1 1 35 35 TYR HE2 H 1 6.88 0.01 . 1 . . . . . . . . 4875 1 240 . 1 1 36 36 GLY H H 1 8.36 0.01 . 1 . . . . . . . . 4875 1 241 . 1 1 36 36 GLY HA2 H 1 3.84 0.01 . 2 . . . . . . . . 4875 1 242 . 1 1 37 37 GLY H H 1 7.23 0.01 . 1 . . . . . . . . 4875 1 243 . 1 1 37 37 GLY HA2 H 1 3.77 0.01 . 2 . . . . . . . . 4875 1 244 . 1 1 37 37 GLY HA3 H 1 3.98 0.01 . 2 . . . . . . . . 4875 1 245 . 1 1 38 38 SER H H 1 8.32 0.01 . 1 . . . . . . . . 4875 1 246 . 1 1 38 38 SER HA H 1 4.40 0.01 . 1 . . . . . . . . 4875 1 247 . 1 1 38 38 SER HB2 H 1 3.84 0.01 . 2 . . . . . . . . 4875 1 248 . 1 1 38 38 SER HB3 H 1 3.92 0.01 . 2 . . . . . . . . 4875 1 249 . 1 1 39 39 ARG H H 1 8.52 0.01 . 1 . . . . . . . . 4875 1 250 . 1 1 39 39 ARG HA H 1 4.29 0.01 . 1 . . . . . . . . 4875 1 251 . 1 1 39 39 ARG HB2 H 1 1.75 0.01 . 9 . . . . . . . . 4875 1 252 . 1 1 39 39 ARG HB3 H 1 1.84 0.01 . 9 . . . . . . . . 4875 1 253 . 1 1 39 39 ARG HG2 H 1 1.63 0.01 . 4 . . . . . . . . 4875 1 254 . 1 1 39 39 ARG HD2 H 1 3.06 0.01 . 9 . . . . . . . . 4875 1 255 . 1 1 39 39 ARG HD3 H 1 3.06 0.01 . 9 . . . . . . . . 4875 1 256 . 1 1 39 39 ARG HE H 1 7.16 0.01 . 9 . . . . . . . . 4875 1 257 . 1 1 40 40 ALA H H 1 8.29 0.01 . 1 . . . . . . . . 4875 1 258 . 1 1 40 40 ALA HA H 1 4.25 0.01 . 1 . . . . . . . . 4875 1 259 . 1 1 40 40 ALA HB1 H 1 1.35 0.01 . 1 . . . . . . . . 4875 1 260 . 1 1 40 40 ALA HB2 H 1 1.35 0.01 . 1 . . . . . . . . 4875 1 261 . 1 1 40 40 ALA HB3 H 1 1.35 0.01 . 1 . . . . . . . . 4875 1 262 . 1 1 41 41 LYS H H 1 8.33 0.01 . 1 . . . . . . . . 4875 1 263 . 1 1 41 41 LYS HA H 1 4.27 0.01 . 1 . . . . . . . . 4875 1 264 . 1 1 41 41 LYS HB2 H 1 1.71 0.01 . 9 . . . . . . . . 4875 1 265 . 1 1 41 41 LYS HB3 H 1 1.84 0.01 . 9 . . . . . . . . 4875 1 266 . 1 1 42 42 ARG H H 1 8.13 0.01 . 1 . . . . . . . . 4875 1 267 . 1 1 42 42 ARG HA H 1 4.29 0.01 . 1 . . . . . . . . 4875 1 268 . 1 1 42 42 ARG HB2 H 1 1.82 0.01 . 9 . . . . . . . . 4875 1 269 . 1 1 42 42 ARG HG2 H 1 1.57 0.01 . 9 . . . . . . . . 4875 1 270 . 1 1 42 42 ARG HD2 H 1 2.86 0.01 . 9 . . . . . . . . 4875 1 271 . 1 1 42 42 ARG HD3 H 1 2.95 0.01 . 9 . . . . . . . . 4875 1 272 . 1 1 42 42 ARG HE H 1 7.17 0.01 . 9 . . . . . . . . 4875 1 273 . 1 1 43 43 ASN H H 1 8.66 0.01 . 1 . . . . . . . . 4875 1 274 . 1 1 43 43 ASN HA H 1 4.65 0.01 . 1 . . . . . . . . 4875 1 275 . 1 1 43 43 ASN HB2 H 1 2.73 0.01 . 2 . . . . . . . . 4875 1 276 . 1 1 43 43 ASN HB3 H 1 2.88 0.01 . 2 . . . . . . . . 4875 1 277 . 1 1 43 43 ASN HD21 H 1 7.94 0.01 . 9 . . . . . . . . 4875 1 278 . 1 1 43 43 ASN HD22 H 1 7.46 0.01 . 9 . . . . . . . . 4875 1 279 . 1 1 44 44 ASN H H 1 7.85 0.01 . 1 . . . . . . . . 4875 1 280 . 1 1 44 44 ASN HA H 1 5.32 0.01 . 1 . . . . . . . . 4875 1 281 . 1 1 44 44 ASN HB2 H 1 2.74 0.01 . 1 . . . . . . . . 4875 1 282 . 1 1 44 44 ASN HB3 H 1 2.74 0.01 . 1 . . . . . . . . 4875 1 283 . 1 1 44 44 ASN HD21 H 1 7.71 0.01 . 9 . . . . . . . . 4875 1 284 . 1 1 44 44 ASN HD22 H 1 6.58 0.01 . 9 . . . . . . . . 4875 1 285 . 1 1 45 45 PHE H H 1 9.48 0.01 . 1 . . . . . . . . 4875 1 286 . 1 1 45 45 PHE HA H 1 5.05 0.01 . 1 . . . . . . . . 4875 1 287 . 1 1 45 45 PHE HB2 H 1 2.72 0.01 . 2 . . . . . . . . 4875 1 288 . 1 1 45 45 PHE HB3 H 1 3.40 0.01 . 2 . . . . . . . . 4875 1 289 . 1 1 45 45 PHE HD1 H 1 7.23 0.01 . 1 . . . . . . . . 4875 1 290 . 1 1 45 45 PHE HD2 H 1 7.23 0.01 . 1 . . . . . . . . 4875 1 291 . 1 1 45 45 PHE HE1 H 1 7.49 0.01 . 1 . . . . . . . . 4875 1 292 . 1 1 45 45 PHE HE2 H 1 7.49 0.01 . 1 . . . . . . . . 4875 1 293 . 1 1 45 45 PHE HZ H 1 7.36 0.01 . 1 . . . . . . . . 4875 1 294 . 1 1 46 46 LYS H H 1 9.95 0.01 . 1 . . . . . . . . 4875 1 295 . 1 1 46 46 LYS HA H 1 4.40 0.01 . 1 . . . . . . . . 4875 1 296 . 1 1 46 46 LYS HB2 H 1 2.04 0.01 . 1 . . . . . . . . 4875 1 297 . 1 1 46 46 LYS HB3 H 1 2.04 0.01 . 1 . . . . . . . . 4875 1 298 . 1 1 46 46 LYS HG2 H 1 1.55 0.01 . 1 . . . . . . . . 4875 1 299 . 1 1 46 46 LYS HG3 H 1 1.55 0.01 . 9 . . . . . . . . 4875 1 300 . 1 1 46 46 LYS HD2 H 1 1.78 0.01 . 9 . . . . . . . . 4875 1 301 . 1 1 46 46 LYS HD3 H 1 1.78 0.01 . 9 . . . . . . . . 4875 1 302 . 1 1 46 46 LYS HE2 H 1 3.05 0.01 . 9 . . . . . . . . 4875 1 303 . 1 1 46 46 LYS HE3 H 1 3.05 0.01 . 9 . . . . . . . . 4875 1 304 . 1 1 46 46 LYS HZ1 H 1 7.72 0.01 . 9 . . . . . . . . 4875 1 305 . 1 1 46 46 LYS HZ2 H 1 7.72 0.01 . 9 . . . . . . . . 4875 1 306 . 1 1 46 46 LYS HZ3 H 1 7.72 0.01 . 9 . . . . . . . . 4875 1 307 . 1 1 47 47 SER H H 1 7.51 0.01 . 1 . . . . . . . . 4875 1 308 . 1 1 47 47 SER HA H 1 4.59 0.01 . 1 . . . . . . . . 4875 1 309 . 1 1 47 47 SER HB2 H 1 3.84 0.01 . 2 . . . . . . . . 4875 1 310 . 1 1 47 47 SER HB3 H 1 4.11 0.01 . 2 . . . . . . . . 4875 1 311 . 1 1 48 48 ALA H H 1 8.37 0.01 . 1 . . . . . . . . 4875 1 312 . 1 1 48 48 ALA HA H 1 3.00 0.01 . 1 . . . . . . . . 4875 1 313 . 1 1 48 48 ALA HB1 H 1 1.02 0.01 . 1 . . . . . . . . 4875 1 314 . 1 1 48 48 ALA HB2 H 1 1.02 0.01 . 1 . . . . . . . . 4875 1 315 . 1 1 48 48 ALA HB3 H 1 1.02 0.01 . 1 . . . . . . . . 4875 1 316 . 1 1 49 49 GLU H H 1 8.77 0.01 . 1 . . . . . . . . 4875 1 317 . 1 1 49 49 GLU HA H 1 3.84 0.01 . 1 . . . . . . . . 4875 1 318 . 1 1 49 49 GLU HB2 H 1 1.81 0.01 . 2 . . . . . . . . 4875 1 319 . 1 1 49 49 GLU HB3 H 1 2.01 0.01 . 2 . . . . . . . . 4875 1 320 . 1 1 49 49 GLU HG2 H 1 2.20 0.01 . 2 . . . . . . . . 4875 1 321 . 1 1 49 49 GLU HG3 H 1 2.36 0.01 . 2 . . . . . . . . 4875 1 322 . 1 1 50 50 ASP H H 1 7.91 0.01 . 1 . . . . . . . . 4875 1 323 . 1 1 50 50 ASP HA H 1 4.28 0.01 . 1 . . . . . . . . 4875 1 324 . 1 1 50 50 ASP HB2 H 1 2.72 0.01 . 2 . . . . . . . . 4875 1 325 . 1 1 50 50 ASP HB3 H 1 2.85 0.01 . 2 . . . . . . . . 4875 1 326 . 1 1 51 51 CYS H H 1 7.14 0.01 . 1 . . . . . . . . 4875 1 327 . 1 1 51 51 CYS HA H 1 1.85 0.01 . 1 . . . . . . . . 4875 1 328 . 1 1 51 51 CYS HB2 H 1 2.69 0.01 . 2 . . . . . . . . 4875 1 329 . 1 1 51 51 CYS HB3 H 1 3.10 0.01 . 2 . . . . . . . . 4875 1 330 . 1 1 52 52 ARG H H 1 8.70 0.01 . 1 . . . . . . . . 4875 1 331 . 1 1 52 52 ARG HA H 1 3.75 0.01 . 1 . . . . . . . . 4875 1 332 . 1 1 52 52 ARG HB2 H 1 1.75 0.01 . 1 . . . . . . . . 4875 1 333 . 1 1 52 52 ARG HB3 H 1 1.75 0.01 . 1 . . . . . . . . 4875 1 334 . 1 1 52 52 ARG HG2 H 1 1.49 0.01 . 2 . . . . . . . . 4875 1 335 . 1 1 52 52 ARG HG3 H 1 1.66 0.01 . 2 . . . . . . . . 4875 1 336 . 1 1 52 52 ARG HD2 H 1 3.06 0.01 . 2 . . . . . . . . 4875 1 337 . 1 1 52 52 ARG HD3 H 1 3.12 0.01 . 2 . . . . . . . . 4875 1 338 . 1 1 52 52 ARG HE H 1 7.46 0.01 . 1 . . . . . . . . 4875 1 339 . 1 1 52 52 ARG HH11 H 1 6.74 0.01 . 9 . . . . . . . . 4875 1 340 . 1 1 52 52 ARG HH12 H 1 6.96 0.01 . 9 . . . . . . . . 4875 1 341 . 1 1 53 53 ARG H H 1 8.07 0.01 . 1 . . . . . . . . 4875 1 342 . 1 1 53 53 ARG HA H 1 3.96 0.01 . 1 . . . . . . . . 4875 1 343 . 1 1 53 53 ARG HB2 H 1 1.81 0.01 . 2 . . . . . . . . 4875 1 344 . 1 1 53 53 ARG HB3 H 1 1.91 0.01 . 2 . . . . . . . . 4875 1 345 . 1 1 53 53 ARG HG2 H 1 1.58 0.01 . 2 . . . . . . . . 4875 1 346 . 1 1 53 53 ARG HG3 H 1 1.71 0.01 . 2 . . . . . . . . 4875 1 347 . 1 1 53 53 ARG HD2 H 1 3.20 0.01 . 1 . . . . . . . . 4875 1 348 . 1 1 53 53 ARG HD3 H 1 3.20 0.01 . 1 . . . . . . . . 4875 1 349 . 1 1 53 53 ARG HE H 1 7.38 0.01 . 1 . . . . . . . . 4875 1 350 . 1 1 54 54 THR H H 1 7.49 0.01 . 1 . . . . . . . . 4875 1 351 . 1 1 54 54 THR HA H 1 4.13 0.01 . 1 . . . . . . . . 4875 1 352 . 1 1 54 54 THR HB H 1 3.98 0.01 . 1 . . . . . . . . 4875 1 353 . 1 1 54 54 THR HG21 H 1 1.37 0.01 . 1 . . . . . . . . 4875 1 354 . 1 1 54 54 THR HG22 H 1 1.37 0.01 . 1 . . . . . . . . 4875 1 355 . 1 1 54 54 THR HG23 H 1 1.37 0.01 . 1 . . . . . . . . 4875 1 356 . 1 1 55 55 SER H H 1 7.90 0.01 . 1 . . . . . . . . 4875 1 357 . 1 1 55 55 SER HA H 1 4.10 0.01 . 1 . . . . . . . . 4875 1 358 . 1 1 55 55 SER HB2 H 1 3.13 0.01 . 1 . . . . . . . . 4875 1 359 . 1 1 55 55 SER HB3 H 1 3.13 0.01 . 1 . . . . . . . . 4875 1 360 . 1 1 56 56 GLY H H 1 7.91 0.01 . 1 . . . . . . . . 4875 1 361 . 1 1 56 56 GLY HA2 H 1 3.82 0.01 . 2 . . . . . . . . 4875 1 362 . 1 1 56 56 GLY HA3 H 1 3.97 0.01 . 2 . . . . . . . . 4875 1 363 . 1 1 57 57 GLY H H 1 8.14 0.01 . 1 . . . . . . . . 4875 1 364 . 1 1 57 57 GLY HA2 H 1 3.83 0.01 . 2 . . . . . . . . 4875 1 365 . 1 1 57 57 GLY HA3 H 1 3.98 0.01 . 2 . . . . . . . . 4875 1 366 . 1 1 58 58 ALA H H 1 7.97 0.01 . 1 . . . . . . . . 4875 1 367 . 1 1 58 58 ALA HA H 1 4.19 0.01 . 1 . . . . . . . . 4875 1 368 . 1 1 58 58 ALA HB1 H 1 1.38 0.01 . 1 . . . . . . . . 4875 1 369 . 1 1 58 58 ALA HB2 H 1 1.38 0.01 . 1 . . . . . . . . 4875 1 370 . 1 1 58 58 ALA HB3 H 1 1.38 0.01 . 1 . . . . . . . . 4875 1 stop_ save_