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Biological Magnetic Resonance Data Bank


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BMRB Entry 18624

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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/BMR18624
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Title: Structure of N-terminal domain of a plant Grx

Deposition date: 2012-07-28 Original release date: 2013-05-20

Authors: Feng, Yingang

Citation: Liu, Xi; Liu, Shi-an; Feng, Yingang; Liu, Jian-zhong; Avery, Cheryl; Deng, Haiteng; Hirschi, Kendal; Wang, Xinquan; Cheng, Ninghui. "Solution structure of N-terminal domain of a plant glutaredoxin"  Not known ., .-..

Assembly members:
N-terminal domain of a plant Grx, polymer, 119 residues, 12907.769 Da.

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):
N-terminal domain of a plant Grx: MASAVKSLTETELLPITEAD SIPSASGVYAVYDKSDELQF VGISRNIAASVSAHLKSVPE LCGSVKVGIVEEPDKAVLTQ AWKLWIEEHIKVTGKVPPGN KSGNNTFVKVTLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts483
15N chemical shifts111
1H chemical shifts772

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal domain of a plant Grx1

Entities:

Entity 1, N-terminal domain of a plant Grx 119 residues - 12907.769 Da.

1   METALASERALAVALLYSSERLEUTHRGLU
2   THRGLULEULEUPROILETHRGLUALAASP
3   SERILEPROSERALASERGLYVALTYRALA
4   VALTYRASPLYSSERASPGLULEUGLNPHE
5   VALGLYILESERARGASNILEALAALASER
6   VALSERALAHISLEULYSSERVALPROGLU
7   LEUCYSGLYSERVALLYSVALGLYILEVAL
8   GLUGLUPROASPLYSALAVALLEUTHRGLN
9   ALATRPLYSLEUTRPILEGLUGLUHISILE
10   LYSVALTHRGLYLYSVALPROPROGLYASN
11   LYSSERGLYASNASNTHRPHEVALLYSVAL
12   THRLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: Nterm_Grx, [U-13C; U-15N], 0.5-1.0 mM; sodium phosphate 50 mM; DTT 10 mM; DSS 0.02%; D2O, [U-2H], 0.1 v/v; H2O 90%

sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

FELIX, Accelrys Software Inc. - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAC42106
GB AAC27175 AAM64346 AAN60257 AAO19648 AAO50507
REF NP_565885
SP Q8H7F6

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