BMRB Entry 5854

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5854

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Title:
1H, 13C, and 15N backbone assignments for the 60.8 kD dimer of the NAD+ synthetase from Bacillus subtilis
Deposition date:
2003-06-26
Original release date:
2004-02-10
Authors:
Markus, Michelle; Doliveira, Lisa; Malakian, Karl; Keeney, David; Severin, Anatoly; Underwood, Kathryn; Tsao, Desiree
Citation:

Citation: Markus, Michelle; Doliveira, Lisa; Malakian, Karl; Keeney, David; Severin, Anatoly; Underwood, Kathryn; Tsao, Desiree. "Letter to the Editor: 1H , 13C, and 15N backbone assignments and secondary structure for the 60.8 kD dimer of the NAD+ synthetase from Bacillus subtilis "  J. Biomol. NMR 28, 301-302 (2004).
PubMed: 14752265

Assembly members:

Assembly members:
NAD+ synthetase, polymer, 272 residues, 30395 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NAD+ synthetase: MSMQEKIMRELHVKPSIDPK QEIEDRVNFLKQYVKKTGAK GFVLGISGGQDSTLAGRLAQ LAVESIREEGGDAQFIAVRL PHGTQQDEDDAQLALKFIKP DKSWKFDIKSTVSAFSDQYQ QETGDQLTDFNKGNVKARTR MIAQYAIGGQEGLLVLGTDH AAEAVTGFFTKYGDGGADLL PLTGLTKRQGRTLLKELGAP ERLYLKEPTADLLDEKPQQS DETELGISYDEIDDYLEGKE VSAKVSEALEKRYSMTEHKR QVPASMFDDWWK

Data sets:
Data typeCount
1H chemical shifts250
13C chemical shifts759
15N chemical shifts250

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NAD+ synthetase subunit 11
2NAD+ synthetase subunit 21

Entities:

Entity 1, NAD+ synthetase subunit 1 272 residues - 30395 Da.

1   METSERMETGLNGLULYSILEMETARGGLU
2   LEUHISVALLYSPROSERILEASPPROLYS
3   GLNGLUILEGLUASPARGVALASNPHELEU
4   LYSGLNTYRVALLYSLYSTHRGLYALALYS
5   GLYPHEVALLEUGLYILESERGLYGLYGLN
6   ASPSERTHRLEUALAGLYARGLEUALAGLN
7   LEUALAVALGLUSERILEARGGLUGLUGLY
8   GLYASPALAGLNPHEILEALAVALARGLEU
9   PROHISGLYTHRGLNGLNASPGLUASPASP
10   ALAGLNLEUALALEULYSPHEILELYSPRO
11   ASPLYSSERTRPLYSPHEASPILELYSSER
12   THRVALSERALAPHESERASPGLNTYRGLN
13   GLNGLUTHRGLYASPGLNLEUTHRASPPHE
14   ASNLYSGLYASNVALLYSALAARGTHRARG
15   METILEALAGLNTYRALAILEGLYGLYGLN
16   GLUGLYLEULEUVALLEUGLYTHRASPHIS
17   ALAALAGLUALAVALTHRGLYPHEPHETHR
18   LYSTYRGLYASPGLYGLYALAASPLEULEU
19   PROLEUTHRGLYLEUTHRLYSARGGLNGLY
20   ARGTHRLEULEULYSGLULEUGLYALAPRO
21   GLUARGLEUTYRLEULYSGLUPROTHRALA
22   ASPLEULEUASPGLULYSPROGLNGLNSER
23   ASPGLUTHRGLULEUGLYILESERTYRASP
24   GLUILEASPASPTYRLEUGLUGLYLYSGLU
25   VALSERALALYSVALSERGLUALALEUGLU
26   LYSARGTYRSERMETTHRGLUHISLYSARG
27   GLNVALPROALASERMETPHEASPASPTRP
28   TRPLYS

Samples:

sample_1: NAD+ synthetase, [U-2H; U-13C; U-15N], 1.0 mM

sample_2: NAD+ synthetase, [U-2H; U-15N], 210 – 270 uM

conditions_1: pH: 7.5 na; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
The spectrometer was equipped with a triple resonance probe with x, y, and znot availablenot availableconditions_1
gradients.not availablenot availableconditions_1

Software:

nmrPipe v2.1 - processing, inital visualization with nmrDraw

PIPP v4.2.2 - analysis of spectra, specifically peak-picking

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAA08947 BAI83777 BAM49243 BAM56513 GAK81413
EMBL CAB12107 CCU56768 CEI55431 CEJ75856
GB AAA22635 ADV95243 AEP89377 AFI26860 AFQ56248
REF NP_388195 WP_003241188 WP_003246440 WP_010332951 WP_014662699
SP P08164
AlphaFold P08164

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