data_5403 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5403 _Entry.Title ; Backbone resonance assignments of the 91 kDa oligomeric TRAP protein from Bacillus staerothermophilus in complex with L-tryptophan ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2002-06-26 _Entry.Accession_date 2002-06-26 _Entry.Last_release_date 2002-06-26 _Entry.Original_release_date 2002-06-26 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.6.0 _Entry.NMR_STAR_dict_location . _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.ORCID _Entry_author.Entry_ID 1 Craig McElroy . A. . . 5403 2 Amanda Manfredo . . . . 5403 3 Alice Wendt . . . . 5403 4 Paul Gollnick . . . . 5403 5 Mark Foster . P. . . 5403 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 5403 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 148 5403 '15N chemical shifts' 57 5403 '1H chemical shifts' 57 5403 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 . . 2020-06-09 2002-06-26 update author 'update assignments' 5403 1 . . 2003-04-10 2002-06-26 original author 'original release' 5403 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5403 _Citation.ID 1 _Citation.Name . _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22269622 _Citation.PubMed_ID 12381302 _Citation.DOI . _Citation.Full_citation . _Citation.Title ; TROSY-NMR Studies of the 91 kDa TRAP Protein reveal Allosteric Control of a Gene Regulatory Protein by Ligand-altered Flexibility ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 323 _Citation.Journal_issue 3 _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 463 _Citation.Page_last 473 _Citation.Year 2002 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Craig McElroy . A. . . 5403 1 2 Amanda Manfredo . . . . 5403 1 3 Alice Wendt . . . . 5403 1 4 Paul Gollnick . . . . 5403 1 5 Mark Foster . P. . . 5403 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'Bacillus stearothermophilus' 5403 1 'NMR assignments' 5403 1 TROSY 5403 1 'trp RNA-binding attenuation protein' 5403 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5403 _Citation.ID 2 _Citation.Name . _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID 7525975 _Citation.DOI . _Citation.Full_citation ; Antson, A. A., Brzozowski, A. M., Dodson, E. J., Dauter, Z., Wilson, K. S., Kurecki, T., Otridge, J. & Gollnick, P. (1994). J. Mol. Biol. 244, 1-5. ; _Citation.Title ; 11-fold symmetry of the trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis determined by X-ray analysis. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 244 _Citation.Journal_issue 1 _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 1 _Citation.Page_last 5 _Citation.Year 1994 _Citation.Details ; The trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis has been crystallized and examined by crystallography using X-ray synchrotron radiation diffraction data. Crystals of TRAP complexed with L-tryptophan belong to space group C2 with a = 156.8 A, b = 114.05 A, c = 105.9 A, beta = 118.2 degrees. Crystals of a potential heavy-atom derivative of TRAP complexed with 5-bromo-L-tryptophan grow in the same space group with similar cell dimensions. X-ray data for the native crystals and for the derivative have been collected to 2.9 A and 2.2 A resolution, respectively. Peaks in the self-rotation function and in the Patterson synthesis could only be explained by two 11-subunit oligomers (each formed by an 11-fold axis of symmetry) in the asymmetric unit lying with the 11-fold rotation axes parallel to each other. The consequence is that the TRAP molecule has 11-fold symmetry and contains 11 subunits. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 A.A. Antson A. A. . . 5403 2 2 A.M. Brzozowski A. M. . . 5403 2 3 E.J. Dodson E. J. . . 5403 2 4 Z. Dauter Z. . . . 5403 2 5 K.S. Wilson K. S. . . 5403 2 6 T. Kurecki T. . . . 5403 2 7 J. Otridge J. . . . 5403 2 8 P. Gollnick P. . . . 5403 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5403 _Citation.ID 3 _Citation.Name . _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID 10499579 _Citation.DOI . _Citation.Full_citation ; Antson, A. A., Dodson, E. J., Dodson, G., Greaves, R. B., Chen, X. & Gollnick, P. (1999). Nature 401, 235-42. ; _Citation.Title ; Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Nature _Citation.Journal_name_full Nature _Citation.Journal_volume 401 _Citation.Journal_issue 6750 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0028-0836 _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 235 _Citation.Page_last 242 _Citation.Year 1999 _Citation.Details ; The trp RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes of several bacilli by binding single-stranded RNA. The binding sequence is composed of eleven triplet repeats, predominantly GAG, separated by two or three non-conserved nucleotides. Here we present the crystal structure of a complex of TRAP and a 53-base single-stranded RNA containing eleven GAG triplets, revealing that each triplet is accommodated in a binding pocket formed by beta-strands. In the complex, the RNA has an extended structure without any base-pairing and binds to the protein mostly by specific protein-base interactions. Eleven binding pockets on the circular TRAP 11-mer form a belt with a diameter of about 80 A. This simple but elegant mechanism of arresting the RNA segment by encircling it around a protein disk is applicable to both transcription, when TRAP binds the nascent RNA, and to translation, when TRAP binds the same sequence within a non-coding leader region of the messenger RNA. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 A.A. Antson A. A. . . 5403 3 2 E.J. Dodson E. J. . . 5403 3 3 G. Dodson G. . . . 5403 3 4 R.B. Greaves R. B. . . 5403 3 5 X. Chen X. . . . 5403 3 6 P. Gollnick P. . . . 5403 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 5403 _Citation.ID 4 _Citation.Name . _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID 7715723 _Citation.DOI . _Citation.Full_citation ; Antson, A. A., Otridge, J., Brzozowski, A. M., Dodson, E. J., Dodson, G. G., Wilson, K. S., Smith, T. M., Yang, M., Kurecki, T. & Gollnick, P. (1995). Nature 374, 693-700. ; _Citation.Title ; The structure of trp RNA-binding attenuation protein. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Nature _Citation.Journal_name_full Nature _Citation.Journal_volume 374 _Citation.Journal_issue 6524 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0028-0836 _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 693 _Citation.Page_last 700 _Citation.Year 1995 _Citation.Details ; The crystal structure of the trp RNA-binding attenuation protein of Bacclius subtilis solved at 1.8 A resolution reveals a novel structural arrangement in which the eleven subunits are stabilized through eleven intersubunit beta-sheets to form a beta-wheel with a large central hole. The nature of the binding of L-tryptophan in clefts between adjacent beta-sheets in the beta-wheel suggests that this binding induces conformational changes in the flexible residues 25-33 and 49-52. It is argued that upon binding, the messenger RNA target forms a matching circle in which eleven U/GAG repeats are bound to the surface of the protein ondecamer modified by the binding of L-tryptophan. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 A.A. Antson A. A. . . 5403 4 2 J. Otridge J. . . . 5403 4 3 A.M. Brzozowski A. M. . . 5403 4 4 E.J. Dodson E. J. . . 5403 4 5 G.G. Dodson G. G. . . 5403 4 6 K.S. Wilson K. S. . . 5403 4 7 T.M. Smith T. M. . . 5403 4 8 M. Yang M. . . . 5403 4 9 T. Kurecki T. . . . 5403 4 10 P. Gollnick P. . . . 5403 4 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 5403 _Citation.ID 5 _Citation.Name . _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID 9383185 _Citation.DOI . _Citation.Full_citation ; Babitzke, P. (1997). Mol. Microbiol. 26, 1-9. ; _Citation.Title ; Regulation of tryptophan biosynthesis: Trp-ing the TRAP or how Bacillus subtilis reinvented the wheel. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Mol. Microbiol.' _Citation.Journal_name_full 'Molecular microbiology' _Citation.Journal_volume 26 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0950-382X _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 1 _Citation.Page_last 9 _Citation.Year 1997 _Citation.Details ; The Bacillus subtilis tryptophan biosynthetic genes are regulated by TRAP. Radiographic crystallography indicates that the TRAP complex contains 11 identical subunits arranged in a doughnut-like structure termed the beta-wheel. The trpEDCFBA operon is regulated by an attenuation mechanism in which tryptophan-activated TRAP binds to 11 (G/U)AG repeats in the trp leader transcript. TRAP binding blocks formation of an anti-terminator structure, thereby promoting the formation of an overlapping terminator, resulting in transcription termination preceding the structural genes. When TRAP is not activated, it is unable to bind to the transcript, which allows anti-terminator formation and, hence, transcription of the operon. TRAP is also responsible for regulating translation of trpEand trpG. TRAP binding to trp operon readthrough transcripts promotes refolding of the RNA such that the trpE Shine-Dalgarno sequence is sequestered in a hairpin, thus inhibiting TrpE synthesis. In the case of trpG, TRAP binds to nine repeats that overlap the ribosome-binding site, thereby blocking translation. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 P. Babitzke P. . . . 5403 5 stop_ save_ save_ref_5 _Citation.Sf_category citations _Citation.Sf_framecode ref_5 _Citation.Entry_ID 5403 _Citation.ID 6 _Citation.Name . _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID . _Citation.DOI . _Citation.Full_citation ; Cavanagh, J. (1996). Protein NMR spectroscopy : principles and practice, Academic Press, San Diego. ; _Citation.Title . _Citation.Status published _Citation.Type book _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _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 . _Citation.Page_last . _Citation.Year . _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 . . . . . . 5403 6 stop_ save_ save_ref_6 _Citation.Sf_category citations _Citation.Sf_framecode ref_6 _Citation.Entry_ID 5403 _Citation.ID 7 _Citation.Name . _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID 10369778 _Citation.DOI . _Citation.Full_citation ; Chen, X., Antson, A. A., Yang, M., Li, P., Baumann, C., Dodson, E. J., Dodson, G. G. & Gollnick, P. (1999). J. Mol. Biol. 289, 1003-16. ; _Citation.Title ; Regulatory features of the trp operon and the crystal structure of the trp RNA-binding attenuation protein from Bacillus stearothermophilus. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 289 _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 1003 _Citation.Page_last 1016 _Citation.Year 1999 _Citation.Details ; Characterization of both the cis and trans -acting regulatory elements indicates that the Bacillus stearothermophilustrp operon is regulated by an attenuation mechanism similar to that which controls the trp operon in Bacillus subtilis. Secondary structure predictions indicate that the leader region of the trp mRNA is capable of folding into terminator and anti- terminator RNA structures. B. stearothermophilus also encodes an RNA-binding protein with 77% sequence identity with the RNA-binding protein (TRAP) that regulates attenuation in B. subtilis. The X-ray structure of this protein has been determined in complex with L-tryptophan at 2.5 A resolution. Like the B. subtilis protein, B. stearothermophilus TRAP has 11 subunits arranged in a ring-like structure. The central cavities in these two structures have different sizes and opposite charge distributions, and packing within the B. stearothermophilus TRAP crystal form does not generate the head-to-head dimers seen in the B. subtilis protein, suggesting that neither of these properties is functionally important. However, the mode of L-tryptophan binding and the proposed RNA binding surfaces are similar, indicating that both proteins are activated by l -tryptophan and bind RNA in essentially the same way. As expected, the TRAP:RNA complex from B. stearothermophilus is significantly more thermostable than that from B. subtilis, with optimal binding occurring at 70 degrees C. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 X.P. Chen X. . . . 5403 7 2 A.A. Antson A. A. . . 5403 7 3 M. Yang M. . . . 5403 7 4 P. Li P. . . . 5403 7 5 C. Baumann C. . . . 5403 7 6 E.J. Dodson E. J. . . 5403 7 7 G.G. Dodson G. G. . . 5403 7 8 P. Gollnick P. . . . 5403 7 stop_ save_ save_ref_7 _Citation.Sf_category citations _Citation.Sf_framecode ref_7 _Citation.Entry_ID 5403 _Citation.ID 8 _Citation.Name . _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID 7836324 _Citation.DOI . _Citation.Full_citation ; Hoffman, R. J. & Gollnick, P. (1995). J. Bacteriol. 177, 839-42. ; _Citation.Title ; The mtrB gene of Bacillus pumilus encodes a protein with sequence and functional homology to the trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Bacteriol.' _Citation.Journal_name_full 'Journal of bacteriology' _Citation.Journal_volume 177 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0021-9193 _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 839 _Citation.Page_last 842 _Citation.Year 1995 _Citation.Details ; The mtrB gene from Bacillus pumilus encodes a 76-amino-acid polypeptide with 77% identity to the trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis. B. pumilus TRAP binds trp leader RNA from either B. subtilis or B. pumilus in a tryptophan-dependent manner. Altering threonine 52 to alanine eliminated RNA-binding activity of B. pumilus TRAP. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 R.J. Hoffman R. J. . . 5403 8 2 P. Gollnick P. . . . 5403 8 stop_ save_ save_ref_8 _Citation.Sf_category citations _Citation.Sf_framecode ref_8 _Citation.Entry_ID 5403 _Citation.ID 9 _Citation.Name . _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID 3133360 _Citation.DOI . _Citation.Full_citation ; Kuroda, M. I., Henner, D. & Yanofsky, C. (1988). J. Bacteriol. 170, 3080-8. ; _Citation.Title ; cis-acting sites in the transcript of the Bacillus subtilis trp operon regulate expression of the operon. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Bacteriol.' _Citation.Journal_name_full 'Journal of bacteriology' _Citation.Journal_volume 170 _Citation.Journal_issue 7 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0021-9193 _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 3080 _Citation.Page_last 3088 _Citation.Year 1988 _Citation.Details ; Transcription of the trp operon of Bacillus subtilis is regulated by attenuation. A trpE'-'lacZ gene fusion preceded by the wild-type trp promoter-leader region was used to analyze regulation. Overproduction of the trp leader transcript in trans from a multicopy plasmid caused constitutive expression of the chromosomal trpE'-'lacZ fusion, presumably by titrating a negative regulatory factor encoded by the mtr locus. Subsegments of the trp leader region cloned onto the multicopy plasmid were examined for their abilities to elevate beta-galactosidase activity. An RNA segment spanning the portion of the leader transcript that forms the promoter-proximal strand of the proposed antiterminator structure was most active in this trans test. The data suggest that the mtr gene product, when activated by tryptophan, binds to this RNA segment and prevents formation of the antiterminator. In this manner, the trans-acting factor promotes formation of the RNA structure that causes transcription termination. Secondary-structure predictions for the leader segment of the trp operon transcript suggest that if the mtr factor bound this RNA segment in a nonterminated transcript, the ribosome-binding site for the first structural gene, trpE, could be sequestered in a stable RNA structure. We tested this possibility by comparing transcriptional and translational fusions containing the initial segments of the trp operon. Our findings suggest that the mtr product causes both transcription attenuation and inhibition of translation of trpE mRNA. Inhibition of translation initiation would reduce ribosome density on trpE mRNA, perhaps making it more labile. Consistent with this interpretation, the addition of tryptophan to mtr+ cultures increased the rate of trpE'-'lacZ mRNA decay. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 M.I. Kuroda M. I. . . 5403 9 2 D. Henner D. . . . 5403 9 3 C. Yanofsky C. . . . 5403 9 stop_ save_ save_ref_9 _Citation.Sf_category citations _Citation.Sf_framecode ref_9 _Citation.Entry_ID 5403 _Citation.ID 10 _Citation.Name . _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID 9811843 _Citation.DOI . _Citation.Full_citation ; Salzmann, M., Pervushin, K., Wider, G., Senn, H. & Wuthrich, K. (1998). Proc. Natl. Acad. Sci. U. S. A. 95, 13585-90. ; _Citation.Title ; TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. ; _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 95 _Citation.Journal_issue 23 _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 13585 _Citation.Page_last 13590 _Citation.Year 1998 _Citation.Details ; The NMR assignment of 13C, 15N-labeled proteins with the use of triple resonance experiments is limited to molecular weights below approximately 25,000 Daltons, mainly because of low sensitivity due to rapid transverse nuclear spin relaxation during the evolution and recording periods. For experiments that exclusively correlate the amide proton (1HN), the amide nitrogen (15N), and 13C atoms, this size limit has been previously extended by additional labeling with deuterium (2H). The present paper shows that the implementation of transverse relaxation-optimized spectroscopy ([15N,1H]-TROSY) into triple resonance experiments results in several-fold improved sensitivity for 2H/13C/15N-labeled proteins and approximately twofold sensitivity gain for 13C/15N-labeled proteins. Pulse schemes and spectra recorded with deuterated and protonated proteins are presented for the [15N, 1H]-TROSY-HNCA and [15N, 1H]-TROSY-HNCO experiments. A theoretical analysis of the HNCA experiment shows that the primary TROSY effect is on the transverse relaxation of 15N, which is only little affected by deuteration, and predicts sensitivity enhancements that are in close agreement with the experimental data. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 M. Salzmann M. . . . 5403 10 2 K. Pervushin K. . . . 5403 10 3 G. Wider G. . . . 5403 10 4 H. Senn H. . . . 5403 10 5 K. Wuthrich K. . . . 5403 10 stop_ save_ save_ref_10 _Citation.Sf_category citations _Citation.Sf_framecode ref_10 _Citation.Entry_ID 5403 _Citation.ID 11 _Citation.Name . _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID 10605091 _Citation.DOI . _Citation.Full_citation ; Salzmann, M., Wider, G., Pervushin, K. & Wuthrich, K. (1999). J. Biomol. NMR 15, 181-4. ; _Citation.Title ; Improved sensitivity and coherence selection for [15N,1H]-TROSY elements in triple resonance experiments. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 15 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _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 181 _Citation.Page_last 184 _Citation.Year 1999 _Citation.Details ; In experiments with proteins of molecular weights around 100 kDa the implementation of [15N,1H]-TROSY-elements in [15N]-constant-time triple resonance experiments yields sensitivity enhancements of one to two orders of magnitude. An additional gain of 10 to 20% may be obtained with the use of 'sensitivity enhancement elements'. This paper describes a novel sensitivity enhancement scheme which is based on concatenation of the 13C alpha-->15N magnetization transfer with the ST2-PT element, and which enables proper TROSY selection of the 15N multiplet components. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 M. Salzmann M. . . . 5403 11 2 G. Wider G. . . . 5403 11 3 K. Pervushin K. . . . 5403 11 4 K. Wuthrich K. . . . 5403 11 stop_ save_ save_ref_11 _Citation.Sf_category citations _Citation.Sf_framecode ref_11 _Citation.Entry_ID 5403 _Citation.ID 12 _Citation.Name . _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID 11914485 _Citation.DOI . _Citation.Full_citation ; Hopcroft NH, Wendt AL, Gollnick P, Antson AA. Specificity of TRAP-RNA interactions: crystal structures of two complexes with different RNA sequences. Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):615-21. ; _Citation.Title ; Specificity of TRAP-RNA interactions: crystal structures of two complexes with different RNA sequences. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Acta Crystallogr. D Biol. Crystallogr.' _Citation.Journal_name_full 'Acta crystallographica. Section D, Biological crystallography' _Citation.Journal_volume 58 _Citation.Journal_issue 'Pt 4' _Citation.Journal_ASTM . _Citation.Journal_ISSN 0907-4449 _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 615 _Citation.Page_last 621 _Citation.Year 2002 _Citation.Details ; The trp RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes in bacilli by binding to the leader region of the nascent trp operon mRNA. When activated by binding tryptophan, the 11-subunit circular TRAP molecule binds to a target sequence consisting of 11 (G/U)AG repeats, separated by two or three variable 'spacer' nucleotides. Reported here are two crystal structures of TRAP bound to RNAs containing 11 GAG repeats separated by UU and CC spacer nucleotides, determined at 1.75 and 2.50 A resolution, respectively. These show the spacer regions of the RNA molecules to be highly flexible, making no direct hydrogen-bonding contacts with the protein. Comparison of these structures with the previous structure of TRAP bound to (GAGAU)(10)GAG RNA, in which the spacer nucleotides stack with each other close to the protein surface, shows that the RNA can adopt different conformations depending on the sequence of the spacer regions. This gives insight into the structural basis of the specificity of TRAP and into the mechanism of binding. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'Nicholas H.' Hopcroft N. H. . . 5403 12 2 'Alice L.' Wendt A. L. . . 5403 12 3 Paul Gollnick P. . . . 5403 12 4 'Alfred A.' Antson A. A. . . 5403 12 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_TRAP _Assembly.Sf_category assembly _Assembly.Sf_framecode system_TRAP _Assembly.Entry_ID 5403 _Assembly.ID 1 _Assembly.Name 'trp RNA-binding attenuation protein undecamer' _Assembly.BMRB_code . _Assembly.Number_of_components 22 _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 'not present' _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 undecamer 5403 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 'TRAP subunit A' 1 $TRAP . . . native . . 1 . . 5403 1 2 'TRAP subunit B' 1 $TRAP . . . native . . 1 . . 5403 1 3 'TRAP subunit C' 1 $TRAP . . . native . . 1 . . 5403 1 4 'TRAP subunit D' 1 $TRAP . . . native . . 1 . . 5403 1 5 'TRAP subunit E' 1 $TRAP . . . native . . 1 . . 5403 1 6 'TRAP subunit F' 1 $TRAP . . . native . . 1 . . 5403 1 7 'TRAP subunit G' 1 $TRAP . . . native . . 1 . . 5403 1 8 'TRAP subunit H' 1 $TRAP . . . native . . 1 . . 5403 1 9 'TRAP subunit I' 1 $TRAP . . . native . . 1 . . 5403 1 10 'TRAP subunit J' 1 $TRAP . . . native . . 1 . . 5403 1 11 'TRAP subunit K' 1 $TRAP . . . native . . 1 . . 5403 1 12 'L-tryptophan, 1' 2 $entity_TRP . . . native . . 2 . . 5403 1 13 'L-tryptophan, 2' 2 $entity_TRP . . . native . . 2 . . 5403 1 14 'L-tryptophan, 3' 2 $entity_TRP . . . native . . 2 . . 5403 1 15 'L-tryptophan, 4' 2 $entity_TRP . . . native . . 2 . . 5403 1 16 'L-tryptophan, 5' 2 $entity_TRP . . . native . . 2 . . 5403 1 17 'L-tryptophan, 6' 2 $entity_TRP . . . native . . 2 . . 5403 1 18 'L-tryptophan, 7' 2 $entity_TRP . . . native . . 2 . . 5403 1 19 'L-tryptophan, 8' 2 $entity_TRP . . . native . . 2 . . 5403 1 20 'L-tryptophan, 9' 2 $entity_TRP . . . native . . 2 . . 5403 1 21 'L-tryptophan, 10' 2 $entity_TRP . . . native . . 2 . . 5403 1 22 'L-tryptophan, 11' 2 $entity_TRP . . . native . . 2 . . 5403 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1C9S . . . . . ; No RNA is present it's in solution ; 5403 1 yes PDB 1GTF . . . . . ; No RNA is present it's in solution ; 5403 1 yes PDB 1GTN . . . . . ; No RNA is present it's in solution ; 5403 1 yes PDB 1QAW . . . . . "it's in solution" 5403 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID TRAP abbreviation 5403 1 'trp RNA-binding attenuation protein undecamer' system 5403 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'transcriptional regulation' 5403 1 'translational regulation' 5403 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_TRAP _Entity.Sf_category entity _Entity.Sf_framecode TRAP _Entity.Entry_ID 5403 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'trp RNA-binding attenuation protein' _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 ; MYTNSDFVVIKALEDGVNVI GLTRGADTRFHHSEKLDKGE VLIAQFTEHTSAIKVRGKAY IQTRHGVIESEGKK ; _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 74 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 8243 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; undecamer mass 90673 undecamer mass with ligand bound 92920 ; _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1C9S . ; Crystal Structure Of A Complex Of Trp Rna-Binding Attenuation Protein With A 53-Base Single Stranded Rna Containing Eleven Gag Triplets Separated By Au Dinucleotides ; . . . . . 100.00 74 100.00 100.00 4.24e-35 . . . . 5403 1 2 no PDB 1GTF . 'The Structure Of The Trp Rna-Binding Attenuation Protein (Trap) Bound To A 53-Nucleotide Rna Molecule Containing Gaguu Repeats' . . . . . 100.00 74 100.00 100.00 4.24e-35 . . . . 5403 1 3 no PDB 1GTN . 'Structure Of The Trp Rna-Binding Attenuation Protein (Trap) Bound To An Rna Molecule Containing 11 Gagcc Repeats' . . . . . 100.00 74 100.00 100.00 4.24e-35 . . . . 5403 1 4 no PDB 1QAW . ; Regulatory Features Of The Trp Operon And The Crystal Structure Of The Trp Rna-Binding Attenuation Protein From Bacillus Stearothermophilus. ; . . . . . 100.00 74 100.00 100.00 4.24e-35 . . . . 5403 1 5 no PDB 1UTD . 'The Structure Of The Trp Ran-Binding Attenuation Protein (Trap) Bound To A 63-Nucleotide Rna Molecule Containing Gaguuu Repeats' . . . . . 100.00 74 100.00 100.00 4.24e-35 . . . . 5403 1 6 no PDB 1UTF . 'The Structure Of The Trp Rna-Binding Attenuation Protein (Trap) Bound To A Rna Molecule Containing Uagau Repeats (Part I)' . . . . . 100.00 74 100.00 100.00 4.24e-35 . . . . 5403 1 7 no PDB 1UTV . 'The Structure Of The Trp Rna-Binding Attenuation Protein (Trap) Bound To A Rna Molecule Containing Uagau Repeats (Part Ii)' . . . . . 100.00 74 100.00 100.00 4.24e-35 . . . . 5403 1 8 no PDB 2EXS . 'Trap3 (Engineered Trap)' . . . . . 98.65 77 98.63 98.63 8.92e-34 . . . . 5403 1 9 no PDB 2EXT . 'Trap4 (Engineered Trap)' . . . . . 98.65 77 100.00 100.00 1.61e-34 . . . . 5403 1 10 no PDB 2ZCZ . 'Crytal Structures And Thermostability Of Mutant Trap3 A7 (Engineered Trap)' . . . . . 100.00 81 100.00 100.00 1.51e-35 . . . . 5403 1 11 no PDB 2ZD0 . 'Crytal Structures And Thermostability Of Mutant Trap3 A5 (Engineered Trap)' . . . . . 100.00 79 100.00 100.00 2.05e-35 . . . . 5403 1 12 no DBJ BAD76498 . ; transcription attenuation protein (tryptophan RNA-binding attenuator protein) (trp RNA-binding attenuation protein) [Geobacillus kaustophilus HTA426] ; . . . . . 100.00 74 98.65 100.00 6.07e-35 . . . . 5403 1 13 no GenBank AAD33793 . 'trp RNA-binding attenuation protein [Geobacillus stearothermophilus]' . . . . . 100.00 74 100.00 100.00 4.24e-35 . . . . 5403 1 14 no GenBank ABO67499 . 'Trp RNA-binding attenuation protein [Geobacillus thermodenitrificans NG80-2]' . . . . . 100.00 75 98.65 98.65 1.04e-34 . . . . 5403 1 15 no REF YP_001126244 . 'transcription attenuation protein MtrB [Geobacillus thermodenitrificans NG80-2]' . . . . . 100.00 75 98.65 98.65 1.04e-34 . . . . 5403 1 16 no REF YP_148066 . 'transcription attenuation protein MtrB [Geobacillus kaustophilus HTA426]' . . . . . 100.00 74 98.65 100.00 6.07e-35 . . . . 5403 1 17 no SWISS-PROT Q9X6J6 . 'Transcription attenuation protein mtrB (Tryptophan RNA-binding attenuator protein) (Trp RNA-binding attenuation protein) (TRAP)' . . . . . 100.00 74 100.00 100.00 4.24e-35 . . . . 5403 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID TRAP abbreviation 5403 1 'trp RNA-binding attenuation protein' common 5403 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 . MET . 5403 1 2 . TYR . 5403 1 3 . THR . 5403 1 4 . ASN . 5403 1 5 . SER . 5403 1 6 . ASP . 5403 1 7 . PHE . 5403 1 8 . VAL . 5403 1 9 . VAL . 5403 1 10 . ILE . 5403 1 11 . LYS . 5403 1 12 . ALA . 5403 1 13 . LEU . 5403 1 14 . GLU . 5403 1 15 . ASP . 5403 1 16 . GLY . 5403 1 17 . VAL . 5403 1 18 . ASN . 5403 1 19 . VAL . 5403 1 20 . ILE . 5403 1 21 . GLY . 5403 1 22 . LEU . 5403 1 23 . THR . 5403 1 24 . ARG . 5403 1 25 . GLY . 5403 1 26 . ALA . 5403 1 27 . ASP . 5403 1 28 . THR . 5403 1 29 . ARG . 5403 1 30 . PHE . 5403 1 31 . HIS . 5403 1 32 . HIS . 5403 1 33 . SER . 5403 1 34 . GLU . 5403 1 35 . LYS . 5403 1 36 . LEU . 5403 1 37 . ASP . 5403 1 38 . LYS . 5403 1 39 . GLY . 5403 1 40 . GLU . 5403 1 41 . VAL . 5403 1 42 . LEU . 5403 1 43 . ILE . 5403 1 44 . ALA . 5403 1 45 . GLN . 5403 1 46 . PHE . 5403 1 47 . THR . 5403 1 48 . GLU . 5403 1 49 . HIS . 5403 1 50 . THR . 5403 1 51 . SER . 5403 1 52 . ALA . 5403 1 53 . ILE . 5403 1 54 . LYS . 5403 1 55 . VAL . 5403 1 56 . ARG . 5403 1 57 . GLY . 5403 1 58 . LYS . 5403 1 59 . ALA . 5403 1 60 . TYR . 5403 1 61 . ILE . 5403 1 62 . GLN . 5403 1 63 . THR . 5403 1 64 . ARG . 5403 1 65 . HIS . 5403 1 66 . GLY . 5403 1 67 . VAL . 5403 1 68 . ILE . 5403 1 69 . GLU . 5403 1 70 . SER . 5403 1 71 . GLU . 5403 1 72 . GLY . 5403 1 73 . LYS . 5403 1 74 . LYS . 5403 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 . MET 1 1 5403 1 . TYR 2 2 5403 1 . THR 3 3 5403 1 . ASN 4 4 5403 1 . SER 5 5 5403 1 . ASP 6 6 5403 1 . PHE 7 7 5403 1 . VAL 8 8 5403 1 . VAL 9 9 5403 1 . ILE 10 10 5403 1 . LYS 11 11 5403 1 . ALA 12 12 5403 1 . LEU 13 13 5403 1 . GLU 14 14 5403 1 . ASP 15 15 5403 1 . GLY 16 16 5403 1 . VAL 17 17 5403 1 . ASN 18 18 5403 1 . VAL 19 19 5403 1 . ILE 20 20 5403 1 . GLY 21 21 5403 1 . LEU 22 22 5403 1 . THR 23 23 5403 1 . ARG 24 24 5403 1 . GLY 25 25 5403 1 . ALA 26 26 5403 1 . ASP 27 27 5403 1 . THR 28 28 5403 1 . ARG 29 29 5403 1 . PHE 30 30 5403 1 . HIS 31 31 5403 1 . HIS 32 32 5403 1 . SER 33 33 5403 1 . GLU 34 34 5403 1 . LYS 35 35 5403 1 . LEU 36 36 5403 1 . ASP 37 37 5403 1 . LYS 38 38 5403 1 . GLY 39 39 5403 1 . GLU 40 40 5403 1 . VAL 41 41 5403 1 . LEU 42 42 5403 1 . ILE 43 43 5403 1 . ALA 44 44 5403 1 . GLN 45 45 5403 1 . PHE 46 46 5403 1 . THR 47 47 5403 1 . GLU 48 48 5403 1 . HIS 49 49 5403 1 . THR 50 50 5403 1 . SER 51 51 5403 1 . ALA 52 52 5403 1 . ILE 53 53 5403 1 . LYS 54 54 5403 1 . VAL 55 55 5403 1 . ARG 56 56 5403 1 . GLY 57 57 5403 1 . LYS 58 58 5403 1 . ALA 59 59 5403 1 . TYR 60 60 5403 1 . ILE 61 61 5403 1 . GLN 62 62 5403 1 . THR 63 63 5403 1 . ARG 64 64 5403 1 . HIS 65 65 5403 1 . GLY 66 66 5403 1 . VAL 67 67 5403 1 . ILE 68 68 5403 1 . GLU 69 69 5403 1 . SER 70 70 5403 1 . GLU 71 71 5403 1 . GLY 72 72 5403 1 . LYS 73 73 5403 1 . LYS 74 74 5403 1 stop_ save_ save_entity_TRP _Entity.Sf_category entity _Entity.Sf_framecode entity_TRP _Entity.Entry_ID 5403 _Entity.ID 2 _Entity.BMRB_code TRP _Entity.Name TRYPTOPHAN _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _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 TRP _Entity.Nonpolymer_comp_label $chem_comp_TRP _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components 1 _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 204.225 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID TRYPTOPHAN BMRB 5403 2 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID TRYPTOPHAN BMRB 5403 2 TRP 'Three letter code' 5403 2 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 TRP $chem_comp_TRP 5403 2 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 5403 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $TRAP . 1422 organism . 'Bacillus stearothermophilus' 'Geobacillus stearothermophilus' . . Bacteria . Bacillus stearothermophilus . . . . . . . . . . . . . 5403 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 5403 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $TRAP . 'recombinant technology' . . . . . . . . . . . . . . . . 5403 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_TRP _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_TRP _Chem_comp.Entry_ID 5403 _Chem_comp.ID TRP _Chem_comp.Provenance PDB _Chem_comp.Name TRYPTOPHAN _Chem_comp.Type 'L-PEPTIDE LINKING' _Chem_comp.BMRB_code TRP _Chem_comp.PDB_code TRP _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2012-11-20 _Chem_comp.Modified_date 2012-11-20 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces LTR _Chem_comp.One_letter_code W _Chem_comp.Three_letter_code TRP _Chem_comp.Number_atoms_all 27 _Chem_comp.Number_atoms_nh 15 _Chem_comp.Atom_nomenclature_source . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/C11H12N2O2/c12-9(11(14)15)5-7-6-13-10-4-2-1-3-8(7)10/h1-4,6,9,13H,5,12H2,(H,14,15)/t9-/m0/s1 _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic yes _Chem_comp.Formula 'C11 H12 N2 O2' _Chem_comp.Formula_weight 204.225 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site EBI _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID InChI=1S/C11H12N2O2/c12-9(11(14)15)5-7-6-13-10-4-2-1-3-8(7)10/h1-4,6,9,13H,5,12H2,(H,14,15)/t9-/m0/s1 InChI InChI 1.03 5403 TRP N[C@@H](Cc1c[nH]c2ccccc12)C(O)=O SMILES_CANONICAL CACTVS 3.341 5403 TRP N[CH](Cc1c[nH]c2ccccc12)C(O)=O SMILES CACTVS 3.341 5403 TRP O=C(O)C(N)Cc2c1ccccc1nc2 SMILES ACDLabs 10.04 5403 TRP QIVBCDIJIAJPQS-VIFPVBQESA-N InChIKey InChI 1.03 5403 TRP c1ccc2c(c1)c(c[nH]2)CC(C(=O)O)N SMILES 'OpenEye OEToolkits' 1.5.0 5403 TRP c1ccc2c(c1)c(c[nH]2)C[C@@H](C(=O)O)N SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5403 TRP stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID '(2S)-2-amino-3-(1H-indol-3-yl)propanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5403 TRP L-tryptophan 'SYSTEMATIC NAME' ACDLabs 10.04 5403 TRP stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID N N N N . N . . N 0 . . . 1 no no . . . . 74.708 . 60.512 . 32.843 . 1.278 1.121 2.059 1 . 5403 TRP CA CA CA CA . C . . S 0 . . . 1 no no . . . . 74.400 . 61.735 . 32.114 . -0.008 0.417 1.970 2 . 5403 TRP C C C C . C . . N 0 . . . 1 no no . . . . 73.588 . 61.411 . 30.840 . -0.490 0.076 3.357 3 . 5403 TRP O O O O . O . . N 0 . . . 1 no no . . . . 72.939 . 62.292 . 30.277 . 0.308 -0.130 4.240 4 . 5403 TRP CB CB CB CB . C . . N 0 . . . 1 no no . . . . 75.684 . 62.473 . 31.706 . 0.168 -0.868 1.161 5 . 5403 TRP CG CG CG CG . C . . N 0 . . . 1 yes no . . . . 76.675 . 62.727 . 32.832 . 0.650 -0.526 -0.225 6 . 5403 TRP CD1 CD1 CD1 CD1 . C . . N 0 . . . 1 yes no . . . . 77.753 . 61.964 . 33.157 . 1.928 -0.418 -0.622 7 . 5403 TRP CD2 CD2 CD2 CD2 . C . . N 0 . . . 1 yes no . . . . 76.646 . 63.805 . 33.777 . -0.186 -0.256 -1.396 8 . 5403 TRP NE1 NE1 NE1 NE1 . N . . N 0 . . . 1 yes no . . . . 78.403 . 62.494 . 34.247 . 1.978 -0.095 -1.951 9 . 5403 TRP CE2 CE2 CE2 CE2 . C . . N 0 . . . 1 yes no . . . . 77.741 . 63.625 . 34.650 . 0.701 0.014 -2.454 10 . 5403 TRP CE3 CE3 CE3 CE3 . C . . N 0 . . . 1 yes no . . . . 75.796 . 64.902 . 33.974 . -1.564 -0.210 -1.615 11 . 5403 TRP CZ2 CZ2 CZ2 CZ2 . C . . N 0 . . . 1 yes no . . . . 78.014 . 64.499 . 35.709 . 0.190 0.314 -3.712 12 . 5403 TRP CZ3 CZ3 CZ3 CZ3 . C . . N 0 . . . 1 yes no . . . . 76.065 . 65.776 . 35.031 . -2.044 0.086 -2.859 13 . 5403 TRP CH2 CH2 CH2 CH2 . C . . N 0 . . . 1 yes no . . . . 77.168 . 65.565 . 35.884 . -1.173 0.348 -3.907 14 . 5403 TRP OXT OXT OXT OXT . O . . N 0 . . . 1 no yes . . . . 73.495 . 60.470 . 30.438 . -1.806 0.001 3.610 15 . 5403 TRP H H H H . H . . N 0 . . . 1 no no . . . . 75.244 . 60.725 . 33.684 . 1.921 0.493 2.518 16 . 5403 TRP H2 H2 H2 HN2 . H . . N 0 . . . 1 no yes . . . . 75.182 . 59.827 . 32.253 . 1.611 1.237 1.113 17 . 5403 TRP HA HA HA HA . H . . N 0 . . . 1 no no . . . . 73.801 . 62.387 . 32.790 . -0.740 1.058 1.479 18 . 5403 TRP HB2 HB2 HB2 1HB . H . . N 0 . . . 1 no no . . . . 76.185 . 61.933 . 30.869 . 0.900 -1.509 1.652 19 . 5403 TRP HB3 HB3 HB3 2HB . H . . N 0 . . . 1 no no . . . . 75.429 . 63.431 . 31.197 . -0.786 -1.390 1.095 20 . 5403 TRP HD1 HD1 HD1 HD1 . H . . N 0 . . . 1 no no . . . . 78.055 . 61.051 . 32.616 . 2.789 -0.564 0.012 21 . 5403 TRP HE1 HE1 HE1 HE1 . H . . N 0 . . . 1 no no . . . . 79.240 . 62.110 . 34.685 . 2.791 0.036 -2.462 22 . 5403 TRP HE3 HE3 HE3 HE3 . H . . N 0 . . . 1 no no . . . . 74.932 . 65.074 . 33.310 . -2.248 -0.413 -0.804 23 . 5403 TRP HZ2 HZ2 HZ2 HZ2 . H . . N 0 . . . 1 no no . . . . 78.871 . 64.351 . 36.386 . 0.860 0.521 -4.534 24 . 5403 TRP HZ3 HZ3 HZ3 HZ3 . H . . N 0 . . . 1 no no . . . . 75.400 . 66.641 . 35.193 . -3.110 0.116 -3.029 25 . 5403 TRP HH2 HH2 HH2 HH2 . H . . N 0 . . . 1 no no . . . . 77.376 . 66.257 . 36.716 . -1.567 0.582 -4.885 26 . 5403 TRP HXT HXT HXT HXT . H . . N 0 . . . 1 no yes . . . . 72.995 . 60.270 . 29.654 . -2.115 -0.217 4.500 27 . 5403 TRP stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING N CA no N 1 . 5403 TRP 2 . SING N H no N 2 . 5403 TRP 3 . SING N H2 no N 3 . 5403 TRP 4 . SING CA C no N 4 . 5403 TRP 5 . SING CA CB no N 5 . 5403 TRP 6 . SING CA HA no N 6 . 5403 TRP 7 . DOUB C O no N 7 . 5403 TRP 8 . SING C OXT no N 8 . 5403 TRP 9 . SING CB CG no N 9 . 5403 TRP 10 . SING CB HB2 no N 10 . 5403 TRP 11 . SING CB HB3 no N 11 . 5403 TRP 12 . DOUB CG CD1 yes N 12 . 5403 TRP 13 . SING CG CD2 yes N 13 . 5403 TRP 14 . SING CD1 NE1 yes N 14 . 5403 TRP 15 . SING CD1 HD1 no N 15 . 5403 TRP 16 . DOUB CD2 CE2 yes N 16 . 5403 TRP 17 . SING CD2 CE3 yes N 17 . 5403 TRP 18 . SING NE1 CE2 yes N 18 . 5403 TRP 19 . SING NE1 HE1 no N 19 . 5403 TRP 20 . SING CE2 CZ2 yes N 20 . 5403 TRP 21 . DOUB CE3 CZ3 yes N 21 . 5403 TRP 22 . SING CE3 HE3 no N 22 . 5403 TRP 23 . DOUB CZ2 CH2 yes N 23 . 5403 TRP 24 . SING CZ2 HZ2 no N 24 . 5403 TRP 25 . SING CZ3 CH2 yes N 25 . 5403 TRP 26 . SING CZ3 HZ3 no N 26 . 5403 TRP 27 . SING CH2 HH2 no N 27 . 5403 TRP 28 . SING OXT HXT no N 28 . 5403 TRP stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5403 _Sample.ID 1 _Sample.Name . _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 'trp RNA-binding attenuation protein' '[U-2H; U-13C; U-15N]' . . 1 $TRAP . . 6.6 . . mM . . . . 5403 1 2 L-TRYPTOPHAN '[U-2H; U-13C; U-15N]' . . 2 $entity_TRP . . 6.6 . . mM . . . . 5403 1 stop_ save_ ####################### # Sample conditions # ####################### save_condition_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition_1 _Sample_condition_list.Entry_ID 5403 _Sample_condition_list.ID 1 _Sample_condition_list.Name . _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 8.0 0.1 pH 5403 1 temperature 328 0.5 K 5403 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5403 _NMR_spectrometer.ID 1 _NMR_spectrometer.Name . _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5403 _NMR_spectrometer_list.ID 1 _NMR_spectrometer_list.Name . loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer Bruker DRX . 800 . . . 5403 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 5403 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 TROSY . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5403 1 2 TROSY-HNCA . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5403 1 3 TROSY-HN(CO)CA . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5403 1 4 TROSY-HNCACB . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5403 1 5 TROSY-HNCO . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5403 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 5403 _Chem_shift_reference.ID 1 _Chem_shift_reference.Name . _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . 5403 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . 5403 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . 5403 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5403 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Name . _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 TROSY 1 $sample_1 . 5403 1 2 TROSY-HNCA 1 $sample_1 . 5403 1 3 TROSY-HN(CO)CA 1 $sample_1 . 5403 1 4 TROSY-HNCACB 1 $sample_1 . 5403 1 5 TROSY-HNCO 1 $sample_1 . 5403 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_assembly_asym_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Ambiguity_set_ID _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 . 1 8 8 VAL H H 1 7.8960 0.0153 . 1 . . . . . 8 VAL H . 5403 1 2 . 1 . 1 8 8 VAL C C 13 179.1400 0.0000 . 1 . . . . . 8 VAL C . 5403 1 3 . 1 . 1 8 8 VAL CA C 13 58.6250 0.3660 . 1 . . . . . 8 VAL CA . 5403 1 4 . 1 . 1 8 8 VAL N N 15 115.3860 0.0578 . 1 . . . . . 8 VAL N . 5403 1 5 . 1 . 1 9 9 VAL H H 1 8.5410 0.0153 . 1 . . . . . 9 VAL H . 5403 1 6 . 1 . 1 9 9 VAL C C 13 177.9188 0.0000 . 1 . . . . . 9 VAL C . 5403 1 7 . 1 . 1 9 9 VAL CA C 13 61.4830 0.3660 . 1 . . . . . 9 VAL CA . 5403 1 8 . 1 . 1 9 9 VAL CB C 13 33.9580 2.1390 . 1 . . . . . 9 VAL CB . 5403 1 9 . 1 . 1 9 9 VAL N N 15 124.9350 0.0578 . 1 . . . . . 9 VAL N . 5403 1 10 . 1 . 1 10 10 ILE H H 1 9.2200 0.0153 . 1 . . . . . 10 ILE H . 5403 1 11 . 1 . 1 10 10 ILE CA C 13 60.2440 0.3660 . 1 . . . . . 10 ILE CA . 5403 1 12 . 1 . 1 10 10 ILE CB C 13 40.8660 2.1390 . 1 . . . . . 10 ILE CB . 5403 1 13 . 1 . 1 10 10 ILE N N 15 126.9940 0.0578 . 1 . . . . . 10 ILE N . 5403 1 14 . 1 . 1 11 11 LYS H H 1 9.3550 0.0153 . 1 . . . . . 11 LYS H . 5403 1 15 . 1 . 1 11 11 LYS C C 13 176.2136 0.0000 . 1 . . . . . 11 LYS C . 5403 1 16 . 1 . 1 11 11 LYS CA C 13 53.1010 0.3660 . 1 . . . . . 11 LYS CA . 5403 1 17 . 1 . 1 11 11 LYS CB C 13 35.8780 2.1390 . 1 . . . . . 11 LYS CB . 5403 1 18 . 1 . 1 11 11 LYS N N 15 128.1160 0.0578 . 1 . . . . . 11 LYS N . 5403 1 19 . 1 . 1 12 12 ALA H H 1 8.3090 0.0153 . 1 . . . . . 12 ALA H . 5403 1 20 . 1 . 1 12 12 ALA C C 13 174.2298 0.0000 . 1 . . . . . 12 ALA C . 5403 1 21 . 1 . 1 12 12 ALA CA C 13 53.0670 0.3660 . 1 . . . . . 12 ALA CA . 5403 1 22 . 1 . 1 12 12 ALA CB C 13 19.9210 2.1390 . 1 . . . . . 12 ALA CB . 5403 1 23 . 1 . 1 12 12 ALA N N 15 130.4230 0.0578 . 1 . . . . . 12 ALA N . 5403 1 24 . 1 . 1 13 13 LEU H H 1 8.9810 0.0153 . 1 . . . . . 13 LEU H . 5403 1 25 . 1 . 1 13 13 LEU C C 13 177.1714 0.0000 . 1 . . . . . 13 LEU C . 5403 1 26 . 1 . 1 13 13 LEU CA C 13 53.6260 0.3660 . 1 . . . . . 13 LEU CA . 5403 1 27 . 1 . 1 13 13 LEU CB C 13 41.1800 2.1390 . 1 . . . . . 13 LEU CB . 5403 1 28 . 1 . 1 13 13 LEU N N 15 124.4500 0.0578 . 1 . . . . . 13 LEU N . 5403 1 29 . 1 . 1 14 14 GLU H H 1 7.6930 0.0153 . 1 . . . . . 14 GLU H . 5403 1 30 . 1 . 1 14 14 GLU C C 13 179.6025 0.0000 . 1 . . . . . 14 GLU C . 5403 1 31 . 1 . 1 14 14 GLU CA C 13 53.3300 0.3660 . 1 . . . . . 14 GLU CA . 5403 1 32 . 1 . 1 14 14 GLU CB C 13 31.7490 2.1390 . 1 . . . . . 14 GLU CB . 5403 1 33 . 1 . 1 14 14 GLU N N 15 117.1640 0.0578 . 1 . . . . . 14 GLU N . 5403 1 34 . 1 . 1 15 15 ASP H H 1 8.2880 0.0153 . 1 . . . . . 15 ASP H . 5403 1 35 . 1 . 1 15 15 ASP CA C 13 54.9860 0.3660 . 1 . . . . . 15 ASP CA . 5403 1 36 . 1 . 1 15 15 ASP CB C 13 40.5970 2.1390 . 1 . . . . . 15 ASP CB . 5403 1 37 . 1 . 1 15 15 ASP N N 15 118.3370 0.0578 . 1 . . . . . 15 ASP N . 5403 1 38 . 1 . 1 16 16 GLY C C 13 177.2614 0.0000 . 1 . . . . . 16 GLY C . 5403 1 39 . 1 . 1 16 16 GLY CA C 13 46.1480 0.3660 . 1 . . . . . 16 GLY CA . 5403 1 40 . 1 . 1 17 17 VAL H H 1 7.6550 0.0153 . 1 . . . . . 17 VAL H . 5403 1 41 . 1 . 1 17 17 VAL C C 13 176.8610 0.0000 . 1 . . . . . 17 VAL C . 5403 1 42 . 1 . 1 17 17 VAL CA C 13 63.3660 0.3660 . 1 . . . . . 17 VAL CA . 5403 1 43 . 1 . 1 17 17 VAL CB C 13 32.1030 2.1390 . 1 . . . . . 17 VAL CB . 5403 1 44 . 1 . 1 17 17 VAL N N 15 124.0820 0.0578 . 1 . . . . . 17 VAL N . 5403 1 45 . 1 . 1 18 18 ASN H H 1 8.6590 0.0153 . 1 . . . . . 18 ASN H . 5403 1 46 . 1 . 1 18 18 ASN C C 13 179.3636 0.0000 . 1 . . . . . 18 ASN C . 5403 1 47 . 1 . 1 18 18 ASN CA C 13 51.7920 0.3660 . 1 . . . . . 18 ASN CA . 5403 1 48 . 1 . 1 18 18 ASN CB C 13 41.8560 2.1390 . 1 . . . . . 18 ASN CB . 5403 1 49 . 1 . 1 18 18 ASN N N 15 125.2680 0.0578 . 1 . . . . . 18 ASN N . 5403 1 50 . 1 . 1 19 19 VAL H H 1 8.4800 0.0153 . 1 . . . . . 19 VAL H . 5403 1 51 . 1 . 1 19 19 VAL C C 13 178.3280 0.0000 . 1 . . . . . 19 VAL C . 5403 1 52 . 1 . 1 19 19 VAL CA C 13 61.7620 0.3660 . 1 . . . . . 19 VAL CA . 5403 1 53 . 1 . 1 19 19 VAL CB C 13 31.6880 2.1390 . 1 . . . . . 19 VAL CB . 5403 1 54 . 1 . 1 19 19 VAL N N 15 124.6440 0.0578 . 1 . . . . . 19 VAL N . 5403 1 55 . 1 . 1 20 20 ILE H H 1 9.3260 0.0153 . 1 . . . . . 20 ILE H . 5403 1 56 . 1 . 1 20 20 ILE CA C 13 59.9260 0.3660 . 1 . . . . . 20 ILE CA . 5403 1 57 . 1 . 1 20 20 ILE CB C 13 40.0430 2.1390 . 1 . . . . . 20 ILE CB . 5403 1 58 . 1 . 1 20 20 ILE N N 15 129.2550 0.0578 . 1 . . . . . 20 ILE N . 5403 1 59 . 1 . 1 21 21 GLY H H 1 8.7900 0.0153 . 1 . . . . . 21 GLY H . 5403 1 60 . 1 . 1 21 21 GLY CA C 13 45.3640 0.3660 . 1 . . . . . 21 GLY CA . 5403 1 61 . 1 . 1 21 21 GLY N N 15 114.2960 0.0578 . 1 . . . . . 21 GLY N . 5403 1 62 . 1 . 1 22 22 LEU H H 1 8.5150 0.0153 . 1 . . . . . 22 LEU H . 5403 1 63 . 1 . 1 22 22 LEU CA C 13 54.2210 0.3660 . 1 . . . . . 22 LEU CA . 5403 1 64 . 1 . 1 22 22 LEU CB C 13 41.4570 2.1390 . 1 . . . . . 22 LEU CB . 5403 1 65 . 1 . 1 22 22 LEU N N 15 127.5260 0.0578 . 1 . . . . . 22 LEU N . 5403 1 66 . 1 . 1 23 23 THR H H 1 8.5820 0.0153 . 1 . . . . . 23 THR H . 5403 1 67 . 1 . 1 23 23 THR CA C 13 60.4440 0.3660 . 1 . . . . . 23 THR CA . 5403 1 68 . 1 . 1 23 23 THR CB C 13 69.6270 2.1390 . 1 . . . . . 23 THR CB . 5403 1 69 . 1 . 1 23 23 THR N N 15 110.6970 0.0578 . 1 . . . . . 23 THR N . 5403 1 70 . 1 . 1 24 24 ARG H H 1 7.3360 0.0153 . 1 . . . . . 24 ARG H . 5403 1 71 . 1 . 1 24 24 ARG CA C 13 55.8410 0.3660 . 1 . . . . . 24 ARG CA . 5403 1 72 . 1 . 1 24 24 ARG CB C 13 30.3970 2.1390 . 1 . . . . . 24 ARG CB . 5403 1 73 . 1 . 1 24 24 ARG N N 15 124.6140 0.0578 . 1 . . . . . 24 ARG N . 5403 1 74 . 1 . 1 25 25 GLY H H 1 7.9690 0.0153 . 1 . . . . . 25 GLY H . 5403 1 75 . 1 . 1 25 25 GLY CA C 13 43.3750 0.3660 . 1 . . . . . 25 GLY CA . 5403 1 76 . 1 . 1 25 25 GLY N N 15 115.4110 0.0578 . 1 . . . . . 25 GLY N . 5403 1 77 . 1 . 1 30 30 PHE C C 13 175.1916 0.0000 . 1 . . . . . 30 PHE C . 5403 1 78 . 1 . 1 30 30 PHE CA C 13 54.7750 0.3660 . 1 . . . . . 30 PHE CA . 5403 1 79 . 1 . 1 30 30 PHE CB C 13 37.3400 2.1390 . 1 . . . . . 30 PHE CB . 5403 1 80 . 1 . 1 31 31 HIS H H 1 8.4290 0.0153 . 1 . . . . . 31 HIS H . 5403 1 81 . 1 . 1 31 31 HIS CA C 13 55.8460 0.3660 . 1 . . . . . 31 HIS CA . 5403 1 82 . 1 . 1 31 31 HIS CB C 13 32.3020 2.1390 . 1 . . . . . 31 HIS CB . 5403 1 83 . 1 . 1 31 31 HIS N N 15 122.5620 0.0578 . 1 . . . . . 31 HIS N . 5403 1 84 . 1 . 1 32 32 HIS H H 1 9.6870 0.0153 . 1 . . . . . 32 HIS H . 5403 1 85 . 1 . 1 32 32 HIS CA C 13 57.4380 0.3660 . 1 . . . . . 32 HIS CA . 5403 1 86 . 1 . 1 32 32 HIS CB C 13 33.7150 2.1390 . 1 . . . . . 32 HIS CB . 5403 1 87 . 1 . 1 32 32 HIS N N 15 119.4710 0.0578 . 1 . . . . . 32 HIS N . 5403 1 88 . 1 . 1 33 33 SER H H 1 6.9490 0.0153 . 1 . . . . . 33 SER H . 5403 1 89 . 1 . 1 33 33 SER C C 13 179.7877 0.0000 . 1 . . . . . 33 SER C . 5403 1 90 . 1 . 1 33 33 SER CA C 13 55.4420 0.3660 . 1 . . . . . 33 SER CA . 5403 1 91 . 1 . 1 33 33 SER CB C 13 63.6370 2.1390 . 1 . . . . . 33 SER CB . 5403 1 92 . 1 . 1 33 33 SER N N 15 121.2170 0.0578 . 1 . . . . . 33 SER N . 5403 1 93 . 1 . 1 34 34 GLU H H 1 9.2040 0.0153 . 1 . . . . . 34 GLU H . 5403 1 94 . 1 . 1 34 34 GLU C C 13 177.8255 0.0000 . 1 . . . . . 34 GLU C . 5403 1 95 . 1 . 1 34 34 GLU CA C 13 53.8340 0.3660 . 1 . . . . . 34 GLU CA . 5403 1 96 . 1 . 1 34 34 GLU CB C 13 30.7050 2.1390 . 1 . . . . . 34 GLU CB . 5403 1 97 . 1 . 1 34 34 GLU N N 15 129.8480 0.0578 . 1 . . . . . 34 GLU N . 5403 1 98 . 1 . 1 35 35 LYS H H 1 8.0380 0.0153 . 1 . . . . . 35 LYS H . 5403 1 99 . 1 . 1 35 35 LYS C C 13 176.4405 0.0000 . 1 . . . . . 35 LYS C . 5403 1 100 . 1 . 1 35 35 LYS CA C 13 54.9550 0.3660 . 1 . . . . . 35 LYS CA . 5403 1 101 . 1 . 1 35 35 LYS CB C 13 31.8720 2.1390 . 1 . . . . . 35 LYS CB . 5403 1 102 . 1 . 1 35 35 LYS N N 15 129.2580 0.0578 . 1 . . . . . 35 LYS N . 5403 1 103 . 1 . 1 36 36 LEU H H 1 9.0440 0.0153 . 1 . . . . . 36 LEU H . 5403 1 104 . 1 . 1 36 36 LEU C C 13 177.1515 0.0000 . 1 . . . . . 36 LEU C . 5403 1 105 . 1 . 1 36 36 LEU CA C 13 53.1260 0.3660 . 1 . . . . . 36 LEU CA . 5403 1 106 . 1 . 1 36 36 LEU CB C 13 45.3180 2.1390 . 1 . . . . . 36 LEU CB . 5403 1 107 . 1 . 1 36 36 LEU N N 15 128.7120 0.0578 . 1 . . . . . 36 LEU N . 5403 1 108 . 1 . 1 37 37 ASP H H 1 8.4720 0.0153 . 1 . . . . . 37 ASP H . 5403 1 109 . 1 . 1 37 37 ASP C C 13 176.7482 0.0000 . 1 . . . . . 37 ASP C . 5403 1 110 . 1 . 1 37 37 ASP CA C 13 52.4330 0.3660 . 1 . . . . . 37 ASP CA . 5403 1 111 . 1 . 1 37 37 ASP CB C 13 41.8260 2.1390 . 1 . . . . . 37 ASP CB . 5403 1 112 . 1 . 1 37 37 ASP N N 15 123.4800 0.0578 . 1 . . . . . 37 ASP N . 5403 1 113 . 1 . 1 38 38 LYS H H 1 8.7100 0.0153 . 1 . . . . . 38 LYS H . 5403 1 114 . 1 . 1 38 38 LYS C C 13 175.0256 0.0000 . 1 . . . . . 38 LYS C . 5403 1 115 . 1 . 1 38 38 LYS CA C 13 59.3760 0.3660 . 1 . . . . . 38 LYS CA . 5403 1 116 . 1 . 1 38 38 LYS CB C 13 31.8100 2.1390 . 1 . . . . . 38 LYS CB . 5403 1 117 . 1 . 1 38 38 LYS N N 15 119.4840 0.0578 . 1 . . . . . 38 LYS N . 5403 1 118 . 1 . 1 39 39 GLY H H 1 8.5570 0.0153 . 1 . . . . . 39 GLY H . 5403 1 119 . 1 . 1 39 39 GLY C C 13 178.2853 0.0000 . 1 . . . . . 39 GLY C . 5403 1 120 . 1 . 1 39 39 GLY CA C 13 45.1750 0.3660 . 1 . . . . . 39 GLY CA . 5403 1 121 . 1 . 1 39 39 GLY N N 15 115.5460 0.0578 . 1 . . . . . 39 GLY N . 5403 1 122 . 1 . 1 40 40 GLU H H 1 8.1230 0.0153 . 1 . . . . . 40 GLU H . 5403 1 123 . 1 . 1 40 40 GLU C C 13 176.8562 0.0000 . 1 . . . . . 40 GLU C . 5403 1 124 . 1 . 1 40 40 GLU CA C 13 56.7890 0.3660 . 1 . . . . . 40 GLU CA . 5403 1 125 . 1 . 1 40 40 GLU CB C 13 31.8100 2.1390 . 1 . . . . . 40 GLU CB . 5403 1 126 . 1 . 1 40 40 GLU N N 15 120.7060 0.0578 . 1 . . . . . 40 GLU N . 5403 1 127 . 1 . 1 41 41 VAL H H 1 7.4540 0.0153 . 1 . . . . . 41 VAL H . 5403 1 128 . 1 . 1 41 41 VAL C C 13 178.7112 0.0000 . 1 . . . . . 41 VAL C . 5403 1 129 . 1 . 1 41 41 VAL CA C 13 59.6140 0.3660 . 1 . . . . . 41 VAL CA . 5403 1 130 . 1 . 1 41 41 VAL CB C 13 35.6190 2.1390 . 1 . . . . . 41 VAL CB . 5403 1 131 . 1 . 1 41 41 VAL N N 15 118.9090 0.0578 . 1 . . . . . 41 VAL N . 5403 1 132 . 1 . 1 42 42 LEU H H 1 9.2580 0.0153 . 1 . . . . . 42 LEU H . 5403 1 133 . 1 . 1 42 42 LEU C C 13 178.5874 0.0000 . 1 . . . . . 42 LEU C . 5403 1 134 . 1 . 1 42 42 LEU CA C 13 52.3890 0.3660 . 1 . . . . . 42 LEU CA . 5403 1 135 . 1 . 1 42 42 LEU CB C 13 46.6180 2.1390 . 1 . . . . . 42 LEU CB . 5403 1 136 . 1 . 1 42 42 LEU N N 15 128.7260 0.0578 . 1 . . . . . 42 LEU N . 5403 1 137 . 1 . 1 43 43 ILE H H 1 9.3880 0.0153 . 1 . . . . . 43 ILE H . 5403 1 138 . 1 . 1 43 43 ILE C C 13 177.0136 0.0000 . 1 . . . . . 43 ILE C . 5403 1 139 . 1 . 1 43 43 ILE CA C 13 60.2960 0.3660 . 1 . . . . . 43 ILE CA . 5403 1 140 . 1 . 1 43 43 ILE CB C 13 38.2620 2.1390 . 1 . . . . . 43 ILE CB . 5403 1 141 . 1 . 1 43 43 ILE N N 15 128.6980 0.0578 . 1 . . . . . 43 ILE N . 5403 1 142 . 1 . 1 44 44 ALA H H 1 8.7840 0.0153 . 1 . . . . . 44 ALA H . 5403 1 143 . 1 . 1 44 44 ALA C C 13 182.0850 0.0000 . 1 . . . . . 44 ALA C . 5403 1 144 . 1 . 1 44 44 ALA CA C 13 50.6710 0.3660 . 1 . . . . . 44 ALA CA . 5403 1 145 . 1 . 1 44 44 ALA CB C 13 21.5200 2.1390 . 1 . . . . . 44 ALA CB . 5403 1 146 . 1 . 1 44 44 ALA N N 15 128.7040 0.0578 . 1 . . . . . 44 ALA N . 5403 1 147 . 1 . 1 45 45 GLN H H 1 7.6970 0.0153 . 1 . . . . . 45 GLN H . 5403 1 148 . 1 . 1 45 45 GLN C C 13 176.9307 0.0000 . 1 . . . . . 45 GLN C . 5403 1 149 . 1 . 1 45 45 GLN CA C 13 55.4030 0.3660 . 1 . . . . . 45 GLN CA . 5403 1 150 . 1 . 1 45 45 GLN CB C 13 31.1350 2.1390 . 1 . . . . . 45 GLN CB . 5403 1 151 . 1 . 1 45 45 GLN N N 15 120.6360 0.0578 . 1 . . . . . 45 GLN N . 5403 1 152 . 1 . 1 46 46 PHE H H 1 7.1240 0.0153 . 1 . . . . . 46 PHE H . 5403 1 153 . 1 . 1 46 46 PHE CA C 13 59.4950 0.3660 . 1 . . . . . 46 PHE CA . 5403 1 154 . 1 . 1 46 46 PHE CB C 13 39.5390 2.1390 . 1 . . . . . 46 PHE CB . 5403 1 155 . 1 . 1 46 46 PHE N N 15 117.2200 0.0578 . 1 . . . . . 46 PHE N . 5403 1 156 . 1 . 1 47 47 THR CA C 13 59.4350 0.3660 . 1 . . . . . 47 THR CA . 5403 1 157 . 1 . 1 48 48 GLU H H 1 8.0990 0.0153 . 1 . . . . . 48 GLU H . 5403 1 158 . 1 . 1 48 48 GLU CA C 13 54.2930 0.3660 . 1 . . . . . 48 GLU CA . 5403 1 159 . 1 . 1 48 48 GLU N N 15 113.0970 0.0578 . 1 . . . . . 48 GLU N . 5403 1 160 . 1 . 1 49 49 HIS H H 1 8.6780 0.0153 . 1 . . . . . 49 HIS H . 5403 1 161 . 1 . 1 49 49 HIS C C 13 176.4905 0.0000 . 1 . . . . . 49 HIS C . 5403 1 162 . 1 . 1 49 49 HIS CA C 13 58.5530 0.3660 . 1 . . . . . 49 HIS CA . 5403 1 163 . 1 . 1 49 49 HIS N N 15 117.1130 0.0578 . 1 . . . . . 49 HIS N . 5403 1 164 . 1 . 1 50 50 THR H H 1 7.7820 0.0153 . 1 . . . . . 50 THR H . 5403 1 165 . 1 . 1 50 50 THR CA C 13 60.2170 0.3660 . 1 . . . . . 50 THR CA . 5403 1 166 . 1 . 1 50 50 THR CB C 13 69.1440 2.1390 . 1 . . . . . 50 THR CB . 5403 1 167 . 1 . 1 50 50 THR N N 15 120.7180 0.0578 . 1 . . . . . 50 THR N . 5403 1 168 . 1 . 1 51 51 SER H H 1 7.5880 0.0153 . 1 . . . . . 51 SER H . 5403 1 169 . 1 . 1 51 51 SER C C 13 180.6995 0.0000 . 1 . . . . . 51 SER C . 5403 1 170 . 1 . 1 51 51 SER CA C 13 56.3740 0.3660 . 1 . . . . . 51 SER CA . 5403 1 171 . 1 . 1 51 51 SER CB C 13 64.9580 2.1390 . 1 . . . . . 51 SER CB . 5403 1 172 . 1 . 1 51 51 SER N N 15 118.2790 0.0578 . 1 . . . . . 51 SER N . 5403 1 173 . 1 . 1 52 52 ALA H H 1 7.5750 0.0153 . 1 . . . . . 52 ALA H . 5403 1 174 . 1 . 1 52 52 ALA C C 13 178.2423 0.0000 . 1 . . . . . 52 ALA C . 5403 1 175 . 1 . 1 52 52 ALA CA C 13 51.5650 0.3660 . 1 . . . . . 52 ALA CA . 5403 1 176 . 1 . 1 52 52 ALA CB C 13 20.6590 2.1390 . 1 . . . . . 52 ALA CB . 5403 1 177 . 1 . 1 52 52 ALA N N 15 121.1340 0.0578 . 1 . . . . . 52 ALA N . 5403 1 178 . 1 . 1 53 53 ILE H H 1 9.1740 0.0153 . 1 . . . . . 53 ILE H . 5403 1 179 . 1 . 1 53 53 ILE C C 13 178.7465 0.0000 . 1 . . . . . 53 ILE C . 5403 1 180 . 1 . 1 53 53 ILE CA C 13 59.5710 0.3660 . 1 . . . . . 53 ILE CA . 5403 1 181 . 1 . 1 53 53 ILE CB C 13 42.8080 2.1390 . 1 . . . . . 53 ILE CB . 5403 1 182 . 1 . 1 53 53 ILE N N 15 122.3160 0.0578 . 1 . . . . . 53 ILE N . 5403 1 183 . 1 . 1 54 54 LYS H H 1 9.3580 0.0153 . 1 . . . . . 54 LYS H . 5403 1 184 . 1 . 1 54 54 LYS C C 13 178.2740 0.0000 . 1 . . . . . 54 LYS C . 5403 1 185 . 1 . 1 54 54 LYS CA C 13 53.6020 0.3660 . 1 . . . . . 54 LYS CA . 5403 1 186 . 1 . 1 54 54 LYS CB C 13 35.8170 2.1390 . 1 . . . . . 54 LYS CB . 5403 1 187 . 1 . 1 54 54 LYS N N 15 130.3890 0.0578 . 1 . . . . . 54 LYS N . 5403 1 188 . 1 . 1 55 55 VAL H H 1 9.0600 0.0153 . 1 . . . . . 55 VAL H . 5403 1 189 . 1 . 1 55 55 VAL C C 13 178.1228 0.0000 . 1 . . . . . 55 VAL C . 5403 1 190 . 1 . 1 55 55 VAL CA C 13 61.4920 0.3660 . 1 . . . . . 55 VAL CA . 5403 1 191 . 1 . 1 55 55 VAL CB C 13 33.6540 2.1390 . 1 . . . . . 55 VAL CB . 5403 1 192 . 1 . 1 55 55 VAL N N 15 126.4260 0.0578 . 1 . . . . . 55 VAL N . 5403 1 193 . 1 . 1 56 56 ARG H H 1 8.3860 0.0153 . 1 . . . . . 56 ARG H . 5403 1 194 . 1 . 1 56 56 ARG C C 13 177.1318 0.0000 . 1 . . . . . 56 ARG C . 5403 1 195 . 1 . 1 56 56 ARG CA C 13 54.4960 0.3660 . 1 . . . . . 56 ARG CA . 5403 1 196 . 1 . 1 56 56 ARG CB C 13 33.1010 2.1390 . 1 . . . . . 56 ARG CB . 5403 1 197 . 1 . 1 56 56 ARG N N 15 125.8360 0.0578 . 1 . . . . . 56 ARG N . 5403 1 198 . 1 . 1 57 57 GLY H H 1 8.2050 0.0153 . 1 . . . . . 57 GLY H . 5403 1 199 . 1 . 1 57 57 GLY C C 13 180.1373 0.0000 . 1 . . . . . 57 GLY C . 5403 1 200 . 1 . 1 57 57 GLY CA C 13 42.9230 0.3660 . 1 . . . . . 57 GLY CA . 5403 1 201 . 1 . 1 57 57 GLY N N 15 114.2470 0.0578 . 1 . . . . . 57 GLY N . 5403 1 202 . 1 . 1 58 58 LYS H H 1 8.8540 0.0153 . 1 . . . . . 58 LYS H . 5403 1 203 . 1 . 1 58 58 LYS C C 13 178.2263 0.0000 . 1 . . . . . 58 LYS C . 5403 1 204 . 1 . 1 58 58 LYS CA C 13 56.6460 0.3660 . 1 . . . . . 58 LYS CA . 5403 1 205 . 1 . 1 58 58 LYS CB C 13 32.7320 2.1390 . 1 . . . . . 58 LYS CB . 5403 1 206 . 1 . 1 58 58 LYS N N 15 123.4940 0.0578 . 1 . . . . . 58 LYS N . 5403 1 207 . 1 . 1 59 59 ALA H H 1 7.9890 0.0153 . 1 . . . . . 59 ALA H . 5403 1 208 . 1 . 1 59 59 ALA C C 13 176.6476 0.0000 . 1 . . . . . 59 ALA C . 5403 1 209 . 1 . 1 59 59 ALA CA C 13 50.8820 0.3660 . 1 . . . . . 59 ALA CA . 5403 1 210 . 1 . 1 59 59 ALA CB C 13 22.7180 2.1390 . 1 . . . . . 59 ALA CB . 5403 1 211 . 1 . 1 59 59 ALA N N 15 129.8820 0.0578 . 1 . . . . . 59 ALA N . 5403 1 212 . 1 . 1 60 60 TYR H H 1 8.9600 0.0153 . 1 . . . . . 60 TYR H . 5403 1 213 . 1 . 1 60 60 TYR C C 13 178.5729 0.0000 . 1 . . . . . 60 TYR C . 5403 1 214 . 1 . 1 60 60 TYR CA C 13 57.1900 0.3660 . 1 . . . . . 60 TYR CA . 5403 1 215 . 1 . 1 60 60 TYR CB C 13 40.7810 2.1390 . 1 . . . . . 60 TYR CB . 5403 1 216 . 1 . 1 60 60 TYR N N 15 124.2830 0.0578 . 1 . . . . . 60 TYR N . 5403 1 217 . 1 . 1 61 61 ILE H H 1 8.4640 0.0153 . 1 . . . . . 61 ILE H . 5403 1 218 . 1 . 1 61 61 ILE C C 13 177.8985 0.0000 . 1 . . . . . 61 ILE C . 5403 1 219 . 1 . 1 61 61 ILE CA C 13 59.5900 0.3660 . 1 . . . . . 61 ILE CA . 5403 1 220 . 1 . 1 61 61 ILE CB C 13 39.4680 2.1390 . 1 . . . . . 61 ILE CB . 5403 1 221 . 1 . 1 61 61 ILE N N 15 129.3000 0.0578 . 1 . . . . . 61 ILE N . 5403 1 222 . 1 . 1 62 62 GLN H H 1 9.0760 0.0153 . 1 . . . . . 62 GLN H . 5403 1 223 . 1 . 1 62 62 GLN C C 13 177.0763 0.0000 . 1 . . . . . 62 GLN C . 5403 1 224 . 1 . 1 62 62 GLN CA C 13 53.7280 0.3660 . 1 . . . . . 62 GLN CA . 5403 1 225 . 1 . 1 62 62 GLN CB C 13 31.6880 2.1390 . 1 . . . . . 62 GLN CB . 5403 1 226 . 1 . 1 62 62 GLN N N 15 124.0200 0.0578 . 1 . . . . . 62 GLN N . 5403 1 227 . 1 . 1 63 63 THR H H 1 8.1780 0.0153 . 1 . . . . . 63 THR H . 5403 1 228 . 1 . 1 63 63 THR CA C 13 59.4730 0.3660 . 1 . . . . . 63 THR CA . 5403 1 229 . 1 . 1 63 63 THR CB C 13 72.0540 2.1390 . 1 . . . . . 63 THR CB . 5403 1 230 . 1 . 1 63 63 THR N N 15 113.0830 0.0578 . 1 . . . . . 63 THR N . 5403 1 231 . 1 . 1 64 64 ARG H H 1 8.5650 0.0153 . 1 . . . . . 64 ARG H . 5403 1 232 . 1 . 1 64 64 ARG CA C 13 57.6180 0.3660 . 1 . . . . . 64 ARG CA . 5403 1 233 . 1 . 1 64 64 ARG N N 15 120.0550 0.0578 . 1 . . . . . 64 ARG N . 5403 1 234 . 1 . 1 65 65 HIS H H 1 7.5180 0.0153 . 1 . . . . . 65 HIS H . 5403 1 235 . 1 . 1 65 65 HIS C C 13 177.0004 0.0000 . 1 . . . . . 65 HIS C . 5403 1 236 . 1 . 1 65 65 HIS CA C 13 54.0290 0.3660 . 1 . . . . . 65 HIS CA . 5403 1 237 . 1 . 1 65 65 HIS CB C 13 30.7050 2.1390 . 1 . . . . . 65 HIS CB . 5403 1 238 . 1 . 1 65 65 HIS N N 15 115.4660 0.0578 . 1 . . . . . 65 HIS N . 5403 1 239 . 1 . 1 66 66 GLY H H 1 7.3100 0.0153 . 1 . . . . . 66 GLY H . 5403 1 240 . 1 . 1 66 66 GLY C C 13 179.5191 0.0000 . 1 . . . . . 66 GLY C . 5403 1 241 . 1 . 1 66 66 GLY CA C 13 43.7450 0.3660 . 1 . . . . . 66 GLY CA . 5403 1 242 . 1 . 1 66 66 GLY N N 15 107.3250 0.0578 . 1 . . . . . 66 GLY N . 5403 1 243 . 1 . 1 67 67 VAL H H 1 8.2200 0.0153 . 1 . . . . . 67 VAL H . 5403 1 244 . 1 . 1 67 67 VAL C C 13 176.8178 0.0000 . 1 . . . . . 67 VAL C . 5403 1 245 . 1 . 1 67 67 VAL CA C 13 59.7510 0.3660 . 1 . . . . . 67 VAL CA . 5403 1 246 . 1 . 1 67 67 VAL CB C 13 33.8680 2.1390 . 1 . . . . . 67 VAL CB . 5403 1 247 . 1 . 1 67 67 VAL N N 15 121.7460 0.0578 . 1 . . . . . 67 VAL N . 5403 1 248 . 1 . 1 68 68 ILE H H 1 8.9680 0.0153 . 1 . . . . . 68 ILE H . 5403 1 249 . 1 . 1 68 68 ILE C C 13 181.0301 0.0000 . 1 . . . . . 68 ILE C . 5403 1 250 . 1 . 1 68 68 ILE CA C 13 59.0220 0.3660 . 1 . . . . . 68 ILE CA . 5403 1 251 . 1 . 1 68 68 ILE CB C 13 41.7330 2.1390 . 1 . . . . . 68 ILE CB . 5403 1 252 . 1 . 1 68 68 ILE N N 15 126.9810 0.0578 . 1 . . . . . 68 ILE N . 5403 1 253 . 1 . 1 69 69 GLU H H 1 7.7110 0.0153 . 1 . . . . . 69 GLU H . 5403 1 254 . 1 . 1 69 69 GLU CA C 13 53.9410 0.3660 . 1 . . . . . 69 GLU CA . 5403 1 255 . 1 . 1 69 69 GLU CB C 13 31.9340 2.1390 . 1 . . . . . 69 GLU CB . 5403 1 256 . 1 . 1 69 69 GLU N N 15 123.4810 0.0578 . 1 . . . . . 69 GLU N . 5403 1 257 . 1 . 1 70 70 SER H H 1 8.8030 0.0153 . 1 . . . . . 70 SER H . 5403 1 258 . 1 . 1 70 70 SER CA C 13 57.1000 0.3660 . 1 . . . . . 70 SER CA . 5403 1 259 . 1 . 1 70 70 SER CB C 13 64.6200 2.1390 . 1 . . . . . 70 SER CB . 5403 1 260 . 1 . 1 70 70 SER N N 15 119.5860 0.0578 . 1 . . . . . 70 SER N . 5403 1 stop_ save_ save_shift_set_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_2 _Assigned_chem_shift_list.Entry_ID 5403 _Assigned_chem_shift_list.ID 2 _Assigned_chem_shift_list.Name . _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 TROSY 1 $sample_1 . 5403 2 2 TROSY-HNCA 1 $sample_1 . 5403 2 3 TROSY-HN(CO)CA 1 $sample_1 . 5403 2 4 TROSY-HNCACB 1 $sample_1 . 5403 2 5 TROSY-HNCO 1 $sample_1 . 5403 2 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_assembly_asym_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Ambiguity_set_ID _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 2 . 2 1 1 TRP NE1 N 15 130.017 0.0578 . 1 . . . . . . . . . 5403 2 2 . 2 . 2 1 1 TRP HE1 H 1 10.333 0.0153 . 1 . . . . . . . . . 5403 2 stop_ save_