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Biological Magnetic Resonance Data Bank


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BMRB Entry 16100

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16100
MolProbity Validation Chart

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Title: Solution NMR Structure of the C-Terminal Domain of Protein DR_A0006 from Deinococcus radiodurans, Northeast Structural Genomics Consortium Target DrR147D

Deposition date: 2008-12-31 Original release date: 2009-02-19

Authors: Mills, Jeffrey; Ghosh, Arindam; Garcia, Erwin; Wang, Huang; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G. V. T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas

Citation: Mills, Jeffrey; Ghosh, Arindam; Garcia, Erwin; Wang, Huang; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G. V. T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; SZYPERSKI, THOMAS. "Solution NMR Structure of the C-Terminal Domain of Protein DR_A0006 from Deinococcus radiodurans, Northeast Structural Genomics Consortium Target DrR147D"  Not known ., .-..

Assembly members:
DrR147D, polymer, 155 residues, 17378.928 Da.

Natural source:   Common Name: Deinococcus radiodurans   Taxonomy ID: 1299   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Deinococcus radiodurans

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

Entity Sequences (FASTA):
DrR147D: MGETVVRDAVTIGKPAEQLY AVWRDLPGLPLLMTHLRSVE VLDDKRSRWTVEAPAPLGAV SWEAELTADEPGKRIAWRSL PGARIENSGEVLFRPAPGAR GTEVVVRLTYRPPGGSAGAV IARMFNQEPSQQLRDDLMRF KREQELGLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts434
15N chemical shifts118
1H chemical shifts887

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DrR147D1

Entities:

Entity 1, DrR147D 155 residues - 17378.928 Da.

1   METGLYGLUTHRVALVALARGASPALAVAL
2   THRILEGLYLYSPROALAGLUGLNLEUTYR
3   ALAVALTRPARGASPLEUPROGLYLEUPRO
4   LEULEUMETTHRHISLEUARGSERVALGLU
5   VALLEUASPASPLYSARGSERARGTRPTHR
6   VALGLUALAPROALAPROLEUGLYALAVAL
7   SERTRPGLUALAGLULEUTHRALAASPGLU
8   PROGLYLYSARGILEALATRPARGSERLEU
9   PROGLYALAARGILEGLUASNSERGLYGLU
10   VALLEUPHEARGPROALAPROGLYALAARG
11   GLYTHRGLUVALVALVALARGLEUTHRTYR
12   ARGPROPROGLYGLYSERALAGLYALAVAL
13   ILEALAARGMETPHEASNGLNGLUPROSER
14   GLNGLNLEUARGASPASPLEUMETARGPHE
15   LYSARGGLUGLNGLULEUGLYLEUGLUHIS
16   HISHISHISHISHIS

Samples:

NC: DrR147D, [U-99% 13C; U-99% 15N], 0.9 mM; D2O, [U-2H], 10%; H2O 90%; DSS 50 uM; DTT 10 mM; sodium chloride 200 mM; sodium azide 0.02%; calcium chloride 5 mM; ammonium acetate 20 mM

NC5: DrR147D, [U-5% 13C; U-99% 15N], 0.9 mM; D2O, [U-2H], 10%; H2O 90%; DSS 50 uM; DTT 10 mM; sodium chloride 200 mM; sodium azide 0.02%; calcium chloride 5 mM; ammonium acetate 20 mM

sample_conditions_1: ionic strength: 435 mM; pH: 4.5; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCnot availableisotropicsample_conditions_1
2D 1H-13C HSQCnot availableisotropicsample_conditions_1
3D HNCOnot availableisotropicsample_conditions_1
3D HNCACBnot availableisotropicsample_conditions_1
3D HNCAnot availableisotropicsample_conditions_1
3D CBCA(CO)NHnot availableisotropicsample_conditions_1
3D HBHA(CO)NHnot availableisotropicsample_conditions_1
3D HCCH-COSYnot availableisotropicsample_conditions_1
3D simultaneous NCaliCaro HH NOESYnot availableisotropicsample_conditions_1
2D 1H-13C HSQCnot availableisotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

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

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

XEASY, Bartels et al. - data analysis

SPSCAN, Glaser - processing

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CSI, Wishart and Sykes - structure solution

TALOS, Cornilescu, Delaglio and Bax - structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

Molmol, Koradi, Billeter and Wuthrich - data analysis

PSVS, Bhattacharya and Montelione - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
GB AAF12292
REF NP_285330 WP_010889266 WP_034349816

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