BMRB Entry 18732

Title:
NMR structure of the protein NP_390345.1 from Bacilus subtilis
Deposition date:
2012-09-21
Original release date:
2012-10-22
Authors:
Proudfoot, Andrew; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation:

Citation: Proudfoot, Andrew; Wuthrich, Kurt. "NMR structure of the protein NP_390345.1 from Bacilus subtilis"  .

Assembly members:

Assembly members:
NP_390345.1, polymer, 87 residues, 10333.016 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts324
15N chemical shifts90
1H chemical shifts615

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NP_390345.11

Entities:

Entity 1, NP_390345.1 87 residues - 10333.016 Da.

1   GLYGLUGLUTHRPROLEUVALTHRALAARG
2   HISMETSERLYSTRPGLUGLUILEALAVAL
3   LYSGLUALALYSLYSARGTYRPROLEUALA
4   GLNVALLEUPHELYSGLNLYSVALTRPASP
5   ARGLYSARGLYSASPGLUALAVALLYSGLN
6   TYRHISLEUTHRLEUARGGLUGLYSERLYS
7   GLUPHEGLYVALPHEVALTHRILESERPHE
8   ASPPROTYRSERGLNLYSVALASNLYSILE
9   ALAILELEUGLUGLUTYRGLN

Samples:

sample_1: NP_390345.1, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM; calcium chloride 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.220 M; pH: 6.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_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
APSY 4D-HACANHsample_1isotropicsample_conditions_1
APSY 5D-CBCACONHsample_1isotropicsample_conditions_1
APSY 5D-HACACONHsample_1isotropicsample_conditions_1

Software:

CYANA, G ntert P. - refinement

Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAI85984 BAM52951 BAM58525 GAK78312
EMBL CAB14396 CCU58980 CEI57685 CEJ78107 CJS87682
GB ADV93209 AEP91497 AFQ58416 AGA24194 AGE64116
REF NP_390345 WP_003246051 WP_015384086 WP_017696198 WP_021480018
SP O32019
AlphaFold O32019

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