BMRB Entry 19881

Title:
transport protein m
Deposition date:
2014-03-31
Original release date:
2015-04-13
Authors:
Zhang, Yi; Hu, Yunfei; Jin, Changwen
Citation:

Citation: Zhang, Yi; Hu, Yunfei; Li, Hongwei; Jin, Changwen. "Structural basis for TatA oligomerization: an NMR study of Escherichia coli TatA dimeric structure"  Plos One 9, e103157-e103157 (2014).
PubMed: 25090434

Assembly members:

Assembly members:
entity, polymer, 97 residues, 5024.057 Da.

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

Data sets:
Data typeCount
13C chemical shifts370
15N chemical shifts90
1H chemical shifts628

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 97 residues - 5024.057 Da.

1   METGLYGLYILESERILETRPGLNLEULEU
2   ILEILEALAVALILEVALVALLEULEUPHE
3   GLYTHRLYSLYSLEUGLYSERILEGLYSER
4   ASPLEUGLYALASERILELYSGLYPHELYS
5   LYSALAMETSERASPASPGLUPROLYSGLN
6   ASPLYSTHRSERGLNASPALAASPPHETHR
7   ALALYSTHRILEALAASPLYSGLNALAASP
8   THRASNGLNGLUGLNALALYSTHRGLUASP
9   ALALYSARGHISASPLYSGLUGLNVALLEU
10   GLUHISHISHISHISHISHIS

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 50 mM; DPC 200 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

TOPSPIN, Bruker Biospin - collection

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19714
PDB
DBJ BAB38189 BAE77465 BAG79648 BAI27909 BAI33032
EMBL CAA06724 CAP78301 CAQ34195 CAR00812 CAR05477
GB AAC19240 AAC76839 AAG59032 AAN45349 AAN83218
PIR D86071
REF NP_312793 NP_418280 NP_709642 WP_000508967 WP_001234791
SP P69428 P69429 P69430 P69431
AlphaFold P69428 P69429 P69430 P69431

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