BMRB Entry 19618

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19618
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
1H, 15N and 13C resonance assignment of a transport protein
Deposition date:
2013-11-18
Original release date:
2014-04-28
Authors:
Zhang, Yi; Wang, Lei; Hu, Yunfei; Jin, Changwen
Citation:

Citation: Zhang, Yi; Wang, Lei; Hu, Yunfei; Jin, Changwen. "Solution structure of the TatB component of the twin-arginine translocation system."  Biochim. Biophys. Acta 1838, 1881-1888 (2014).
PubMed: 24699374

Assembly members:

Assembly members:
protein, polymer, 109 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
protein: MFDIGFSELLLVFIIGLVVL GPQRLPVAVKTVAGWIRALR SLATTVQNELTQELKLQEFQ DSLKKVEKASLTNLTPELKA SMDELRQAAESMKRSYVAND PLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts469
15N chemical shifts116
1H chemical shifts753

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1transport protein1

Entities:

Entity 1, transport protein 109 residues - Formula weight is not available

1   METPHEASPILEGLYPHESERGLULEULEU
2   LEUVALPHEILEILEGLYLEUVALVALLEU
3   GLYPROGLNARGLEUPROVALALAVALLYS
4   THRVALALAGLYTRPILEARGALALEUARG
5   SERLEUALATHRTHRVALGLNASNGLULEU
6   THRGLNGLULEULYSLEUGLNGLUPHEGLN
7   ASPSERLEULYSLYSVALGLULYSALASER
8   LEUTHRASNLEUTHRPROGLULEULYSALA
9   SERMETASPGLULEUARGGLNALAALAGLU
10   SERMETLYSARGSERTYRVALALAASNASP
11   PROLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: transport protein, [U-100% 13C; U-100% 15N], 1 mM; sodium acetate 20 mM; DPC 40 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.02 M; pH: 5.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB EIQ59273 EYV46754
REF WP_053263795

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks