BMRB Entry 19714

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19714
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Transport protein A
Deposition date:
2014-01-02
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, 100 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):
entity: MCGMGGISIWQLLIIAVIVV LLFGTKKLGSIGSDLGASIK GFKKAMSDDEPKQDKTSQDA DFTAKTIADKQADTNQEQAK TEDAKRHDKEQVLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts378
15N chemical shifts90
1H chemical shifts628

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Transport protein A1

Entities:

Entity 1, Transport protein A 100 residues - Formula weight is not available

1   METCYSGLYMETGLYGLYILESERILETRP
2   GLNLEULEUILEILEALAVALILEVALVAL
3   LEULEUPHEGLYTHRLYSLYSLEUGLYSER
4   ILEGLYSERASPLEUGLYALASERILELYS
5   GLYPHELYSLYSALAMETSERASPASPGLU
6   PROLYSGLNASPLYSTHRSERGLNASPALA
7   ASPPHETHRALALYSTHRILEALAASPLYS
8   GLNALAASPTHRASNGLNGLUGLNALALYS
9   THRGLUASPALALYSARGHISASPLYSGLU
10   GLNVALLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: transport protein A, [U-100% 15N], 1 mM; sodium phosphate 50 mM; DPC 80 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: transport protein A, [U-100% 15N], 1 mM; sodium phosphate 50 mM; DPC 80 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_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 - structure solution

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 19881
PDB
DBJ BAB38189 BAE77465 BAG79648 BAI27909 BAI33032
EMBL CAA06724 CAP78301 CAQ34195 CAR00812 CAR05477
GB AAA67633 AAC19240 AAC76839 AAG59032 AAN45349
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