BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 36048

Title: Solution NMR Structure of DNA Mismatch Repair Protein MutT (Family Nudix Hydrolase) from Methicillin Resistant Staphylococcus aureus 252

Deposition date: 2017-01-27 Original release date: 2017-04-24

Authors: Wahab, A.; Durreshahwar, S.; Schwalbe, H.; Richter, C.; Choudhary, M.

Citation: Wahab, A.. "Solution NMR Structure of DNA Mismatch Repair Protein MutT (Family Nudix Hydrolase) from Methicillin Resistant Staphylococcus aureus 252"  . ., .-..

Assembly members:
entity_1, polymer, 130 residues, 14914.342 Da.

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 548470   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus Staphylococcus aureus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: MKKVINVVGAIIFSDNKILC AQRSEKMSLPLMWEFPGGKV EKNETEKDALIREIREEMKC DLIVGDKVITTEHEYDFGIV RLTTYKCTLNKELPTLTEHK SIEWLSINELDKLNWAPADI PAVNKIMTEG

Data sets:
Data typeCount
13C chemical shifts586
15N chemical shifts134
1H chemical shifts982

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 130 residues - 14914.342 Da.

1   METLYSLYSVALILEASNVALVALGLYALA
2   ILEILEPHESERASPASNLYSILELEUCYS
3   ALAGLNARGSERGLULYSMETSERLEUPRO
4   LEUMETTRPGLUPHEPROGLYGLYLYSVAL
5   GLULYSASNGLUTHRGLULYSASPALALEU
6   ILEARGGLUILEARGGLUGLUMETLYSCYS
7   ASPLEUILEVALGLYASPLYSVALILETHR
8   THRGLUHISGLUTYRASPPHEGLYILEVAL
9   ARGLEUTHRTHRTYRLYSCYSTHRLEUASN
10   LYSGLULEUPROTHRLEUTHRGLUHISLYS
11   SERILEGLUTRPLEUSERILEASNGLULEU
12   ASPLYSLEUASNTRPALAPROALAASPILE
13   PROALAVALASNLYSILEMETTHRGLUGLY

Samples:

sample_1: DNA Mismatch Repair Protein MutT from Nudix Hydrolase Family, [U-99% 13C; U-99% 15N], 1 ± 0.1 mM; sodium phosphate 25 mM; NaCl 100 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: pH: 6.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1anisotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1

Software:

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

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

SPARKY vSPARKY 3, T. D. Goddard and D. G. Kneller - chemical shift assignment, data analysis

TOPSPIN v3.5 pl5, Bruker Biospin - processing

TOPSPIN v3.6 pl5, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Ascend 800 MHz
  • Bruker AvanceIII 600 MHz

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