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Biological Magnetic Resonance Data Bank


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BMRB Entry 18346

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18346
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Title: NMR structure of the protein NP_390037.1 from Bacillus subtilis.

Deposition date: 2012-03-22 Original release date: 2012-04-30

Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; JCSG, JCSG

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the protein NP_390037.1 from Bacillus subtilis"  Not known ., .-..

Assembly members:
entity, polymer, 128 residues, 14274.345 Da.

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

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

Entity Sequences (FASTA):
entity: GAEALPLYYLQITGITSDGN DFAWDNLTSSQTKAPNVLKG NKLYVKARFMGYTKLTVITG KDGKNLLYNGTAKMFKSDAI LGQNKVVIGWDKYFEIPMDA LQDNSIQIKALSSGTTFVYS QKIDFERE

Data sets:
Data typeCount
13C chemical shifts432
15N chemical shifts141
1H chemical shifts926

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NP_390037.1 from Bacillus subtilis1

Entities:

Entity 1, NP_390037.1 from Bacillus subtilis 128 residues - 14274.345 Da.

1   GLYALAGLUALALEUPROLEUTYRTYRLEU
2   GLNILETHRGLYILETHRSERASPGLYASN
3   ASPPHEALATRPASPASNLEUTHRSERSER
4   GLNTHRLYSALAPROASNVALLEULYSGLY
5   ASNLYSLEUTYRVALLYSALAARGPHEMET
6   GLYTYRTHRLYSLEUTHRVALILETHRGLY
7   LYSASPGLYLYSASNLEULEUTYRASNGLY
8   THRALALYSMETPHELYSSERASPALAILE
9   LEUGLYGLNASNLYSVALVALILEGLYTRP
10   ASPLYSTYRPHEGLUILEPROMETASPALA
11   LEUGLNASPASNSERILEGLNILELYSALA
12   LEUSERSERGLYTHRTHRPHEVALTYRSER
13   GLNLYSILEASPPHEGLUARGGLU

Samples:

sample_1: NP_390037.1, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium azide 5 mM; sodium chloride 50 mM; D2O, [U-99% 2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 0.080 M; pH: 6.0; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
4D APSY-HACANHsample_1isotropicsample_conditions_1
5D APSY-HACACONHsample_1isotropicsample_conditions_1
5D APSY-CBCACONHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - geometry optimization, refinement

UNIO, Herrmann and Wuthrich - chemical shift assignment, data analysis, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CAB14072 CCU58559 CEI57363 CEJ77788
GB AAC12986 AFQ58101 AGG61547 AIC40597 AIC44829
REF NP_046565 NP_390037 WP_003246138 WP_019712873 WP_032725945
SP O31994

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