BMRB Entry 25483

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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/BMR25483
MolProbity Validation Chart

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Title:
Metal Binding of Glutaredoxins
Deposition date:
2015-02-11
Original release date:
2016-04-12
Authors:
Bilinovich, Stephanie; Caporoso, Joel; Taraboletti, Alexandra; Duangjumpa, Nilubol; Panzner, Matthew; Prokop, Jeremy; Shriver, Leah; Leeper, Thomas
Citation:

Citation: Bilinovich, Stephanie; Caporoso, Joel; Taraboletti, Alexandra; Duangjumpa, Nilubol; Panzner, Matthew; Prokop, Jeremy; Shriver, Leah; Leeper, Thomas. "Metal Binding of Glutaredoxins"  .

Assembly members:

Assembly members:
Glutaredoxin, polymer, 92 residues, 9940.369 Da.
SILVER ION, non-polymer, 107.868 Da.

Natural source:

Natural source:   Common Name: a-proteobacteria   Taxonomy ID: 29459   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Brucella melitensis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Glutaredoxin: GPGSMVDVIIYTRPGCPYCA RAKALLARKGAEFNEIDASA TPELRAEMQERSGRNTFPQI FIGSVHVGGSDDLYALEDEG KLDSLLKTGKLI

Data sets:
Data typeCount
13C chemical shifts361
15N chemical shifts88
1H chemical shifts581

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_1_11
2entity_1_21
3SILVER ION2

Entities:

Entity 1, entity_1_1 92 residues - 9940.369 Da.

1   GLYPROGLYSERMETVALASPVALILEILE
2   TYRTHRARGPROGLYCYSPROTYRCYSALA
3   ARGALALYSALALEULEUALAARGLYSGLY
4   ALAGLUPHEASNGLUILEASPALASERALA
5   THRPROGLULEUARGALAGLUMETGLNGLU
6   ARGSERGLYARGASNTHRPHEPROGLNILE
7   PHEILEGLYSERVALHISVALGLYGLYSER
8   ASPASPLEUTYRALALEUGLUASPGLUGLY
9   LYSLEUASPSERLEULEULYSTHRGLYLYS
10   LEUILE

Entity 2, SILVER ION - Ag - 107.868 Da.

1   AG

Samples:

sample_1: Glutaredoxin, [U-99% 13C; U-99% 15N], 1.0 mM; SILVER ION 0.5 mM; MES 50 mM; TCEP 0.01 mM; D2O, [U-99% 2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; 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 HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HCCH-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:

CcpNMR, CCPN - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

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

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Agilent INOVA 750 MHz

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