BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 25138

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25138
MolProbity Validation Chart

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Title: Chemical shift assignments of DRB4(1-153), a dsRNA binding protein in A. thaliana RNAi pathway   PubMed: 25281003

Deposition date: 2014-08-09 Original release date: 2014-10-14

Authors: Deshmukh, Mandar V.; Chiliveri, Sai Chaitanya

Citation: Chiliveri, Sai Chaitanya; Deshmukh, Mandar. "Chemical shift assignments of DRB4 (1-153), a dsRNA binding protein in A. thaliana RNAi pathway."  Biomol NMR Assign 9, 253-256 (2015).

Assembly members:
DRB4(1-153), polymer, 153 residues, Formula weight is not available

Natural source:   Common Name: Thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

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

Entity Sequences (FASTA):
DRB4(1-153): MDHVYKGQLQAYALQHNLEL PVYANEREGPPHAPRFRCNV TFCGQTFQSSEFFPTLKSAE HAAAKIAVASLTPQSPEGID VAYKNLLQEIAQKESSLLPF YATATSGPSHAPTFTSTVEF AGKVFSGEEAKTKKLAEMSA AKVAFMSIKNGNS

Data sets:
Data typeCount
13C chemical shifts559
15N chemical shifts148
1H chemical shifts951

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1DRB4(1-153)1

Entities:

Entity 1, DRB4(1-153) 153 residues - Formula weight is not available

1   METASPHISVALTYRLYSGLYGLNLEUGLN
2   ALATYRALALEUGLNHISASNLEUGLULEU
3   PROVALTYRALAASNGLUARGGLUGLYPRO
4   PROHISALAPROARGPHEARGCYSASNVAL
5   THRPHECYSGLYGLNTHRPHEGLNSERSER
6   GLUPHEPHEPROTHRLEULYSSERALAGLU
7   HISALAALAALALYSILEALAVALALASER
8   LEUTHRPROGLNSERPROGLUGLYILEASP
9   VALALATYRLYSASNLEULEUGLNGLUILE
10   ALAGLNLYSGLUSERSERLEULEUPROPHE
11   TYRALATHRALATHRSERGLYPROSERHIS
12   ALAPROTHRPHETHRSERTHRVALGLUPHE
13   ALAGLYLYSVALPHESERGLYGLUGLUALA
14   LYSTHRLYSLYSLEUALAGLUMETSERALA
15   ALALYSVALALAPHEMETSERILELYSASN
16   GLYASNSER

Samples:

15N: DRB4(1-153), [U-100% 15N], 0.5 mM; Potassium phosphate buffer 50 mM; Na2SO4 100 mM; DTT 4 mM

13C_15N: DRB4(1-153), [U-100% 13C; U-100% 15N], 0.5 mM; Potassium phosphate buffer 50 mM; Na2SO4 100 mM; DTT 4 mM

10_13C: DRB4(1-153), [U-10% 13C; U-100% 15N], 0.5 mM; Potassium phosphate buffer 50 mM; Na2SO4 100 mM; DTT 4 mM

15N_D2O: DRB4(1-153), [U-100% 15N], 0.5 mM; Potassium phosphate buffer 50 mM; Na2SO4 100 mM; DTT 4 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15Nisotropicsample_conditions_1
3D HNCO13C_15Nisotropicsample_conditions_1
3D HN(CA)CO13C_15Nisotropicsample_conditions_1
3D HNCA13C_15Nisotropicsample_conditions_1
3D HN(CO)CA13C_15Nisotropicsample_conditions_1
3D HNCACB13C_15Nisotropicsample_conditions_1
3D HN(CO)CACB13C_15Nisotropicsample_conditions_1
2D 1H-13C HSQC13C_15Nisotropicsample_conditions_1
3D H(CCO)NH-TOCSY13C_15Nisotropicsample_conditions_1
3D (H)C(CO)NH-TOCSY13C_15Nisotropicsample_conditions_1
3D HCCH-TOCSY13C_15Nisotropicsample_conditions_1
3D HNHA13C_15Nisotropicsample_conditions_1
3D HNHB13C_15Nisotropicsample_conditions_1
2D 1H-15N HSQC15N_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC10_13Cisotropicsample_conditions_1
2D 1H-1H TOCSY15N_D2Oisotropicsample_conditions_1
2D 1H-1H NOESY15N_D2Oisotropicsample_conditions_1
3D 1H-15N NOESY15Nisotropicsample_conditions_1
3D 1H-13C NOESY13C_15Nisotropicsample_conditions_1

Software:

TOPSPIN v2.1.6, Bruker Biospin - collection, processing

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

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

DBJ BAG69145
GB AAL67059 AAN13025 AEE80393 AEE80394 AEE80395
REF NP_001154686 NP_191839 NP_974480
SP Q8H1D4

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