BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25037

Title: Solution structure of N terminal domain of the MuB AAA+ ATPase

Deposition date: 2014-06-23 Original release date: 2015-06-29

Authors: Lopez-Mendez, Blanca; Dramicanin, Marija; Campos-Olivas, Ramon; Ramon-Maiques, Santiago

Citation: Dramicanin, Marija; Lopez-Mendez, Blanca; Campos-Olivas, Ramon; Ramon-Maiques, Santiago. "Solution structure of N terminal domain of the MuB AAA+ ATPase"  To be Published ., .-..

Assembly members:
MuB-NTD, polymer, 65 residues, 7353.184 Da.

Natural source:   Common Name: Enterobacteria phage Mu   Taxonomy ID: 10677   Superkingdom: Viruses   Kingdom: not available   Genus/species: bacteriophage Mu

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

Entity Sequences (FASTA):
MuB-NTD: GPMNISDIRAGLRTLVENEE TTFKQIALESGLSTGTISSF INDKYNGDNERVSQTLQRWL EKYHA

Data sets:
Data typeCount
13C chemical shifts183
15N chemical shifts68
1H chemical shifts454

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MuB-NTD1

Entities:

Entity 1, MuB-NTD 65 residues - 7353.184 Da.

1   GLYPROMETASNILESERASPILEARGALA
2   GLYLEUARGTHRLEUVALGLUASNGLUGLU
3   THRTHRPHELYSGLNILEALALEUGLUSER
4   GLYLEUSERTHRGLYTHRILESERSERPHE
5   ILEASNASPLYSTYRASNGLYASPASNGLU
6   ARGVALSERGLNTHRLEUGLNARGTRPLEU
7   GLULYSTYRHISALA

Samples:

sample_1: MuB-NTD 500 uM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_2: MuB-NTD, [U-98% 15N], 500 uM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v2.2.6, Guntert, Mumenthaler and Wuthrich - structure solution

OPAL v1.4, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

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

CCPN v2.3.1, CCPN - chemical shift assignment, data analysis, peak picking

TOPSPIN v2.1, Bruker Biospin - collection, processing

TALOS+, Cornilescu, Delaglio and Bax - backbone torsion angle restraint generation

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
EMBL CAA25599 CDP68213 CDU35404 CTU52180 CTV64249
GB AAA32370 AAA32382 AAF01100 AAW58941 ACV50263
REF NP_050608 WP_001026707 WP_001026708 WP_001026709 WP_001026710
SP P03763 P13771
AlphaFold P03763 P13771

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