BMRB Entry 36048

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36048
MolProbity Validation Chart

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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:

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

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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