BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25381

Title: Structure of the E. coli threonylcarbamoyl-AMP synthase TsaC   PubMed: 26060251

Deposition date: 2014-12-06 Original release date: 2015-06-15

Authors: Harris, Kimberly; Bobay, Benjamin; Sarachan, Kathryn; Sims, Alexis; Bilbille, Yann; Deutsch, Christopher; Iwata-Reuyl, Dirk; Agris, Paul

Citation: Harris, Kimberly; Bobay, Benjamin; Sarachan, Kathryn; Sims, Alexis; Bilbille, Yann; Deutsch, Christopher; Iwata-Reuyl, Dirk; Agris, Paul. "NMR-based Structural Analysis of Threonylcarbamoyl-AMP Synthase and Its Substrate Interactions"  J. Biol. Chem. 290, 20032-20043 (2015).

Assembly members:
entity, polymer, 189 residues, 20655.629 Da.

Natural source:   Common Name: E.coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: NNNLQRDAIAAAIDVLNEER VIAYPTEAVFGVGCDPDSET AVMRLLELKQRPVDKGLILI AANYEQLKPYIDDTMLTDVQ RETIFSRWPGPVTFVFPAPA TTPRWLTGRFDSLAVRVTDH PLVVALCQAYGKPLVSTSAN LSGLPPCRTVDEVRAQFGAA FPVVPGETGGRLNPSEIRDA LTGELFRQG

Data sets:
Data typeCount
13C chemical shifts723
15N chemical shifts168
1H chemical shifts1102

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 189 residues - 20655.629 Da.

1   ASNASNASNLEUGLNARGASPALAILEALA
2   ALAALAILEASPVALLEUASNGLUGLUARG
3   VALILEALATYRPROTHRGLUALAVALPHE
4   GLYVALGLYCYSASPPROASPSERGLUTHR
5   ALAVALMETARGLEULEUGLULEULYSGLN
6   ARGPROVALASPLYSGLYLEUILELEUILE
7   ALAALAASNTYRGLUGLNLEULYSPROTYR
8   ILEASPASPTHRMETLEUTHRASPVALGLN
9   ARGGLUTHRILEPHESERARGTRPPROGLY
10   PROVALTHRPHEVALPHEPROALAPROALA
11   THRTHRPROARGTRPLEUTHRGLYARGPHE
12   ASPSERLEUALAVALARGVALTHRASPHIS
13   PROLEUVALVALALALEUCYSGLNALATYR
14   GLYLYSPROLEUVALSERTHRSERALAASN
15   LEUSERGLYLEUPROPROCYSARGTHRVAL
16   ASPGLUVALARGALAGLNPHEGLYALAALA
17   PHEPROVALVALPROGLYGLUTHRGLYGLY
18   ARGLEUASNPROSERGLUILEARGASPALA
19   LEUTHRGLYGLULEUPHEARGGLNGLY

Samples:

sample_1: Recombinant TsaC protein, [U-100% 13C; U-100% 15N], 1 mM; D2O, [U-100% 2H], 10%; potassium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: Recombinant TsaC protein, [U-100% 13C; U-100% 15N], 1 mM; D2O, [U-100% 2H], 10%; potassium phosphate 20 mM; sodium chloride 100 mM; Pf1 bacteriophage 12 mg/mL; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 15N TOCSY-HSQCsample_1isotropicsample_conditions_1
1H-15N HSQC-IPAPsample_2isotropicsample_conditions_1
1H-15N TROSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Varian Inova 600 MHz
  • Bruker Avance II 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts