BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16403

Title: SOLUTION STRUCTURE OF GLUTAREDOXIN FROM Bartonella henselae str. Houston. Seattle Structure Genomics Center for Infectious Disease (SSGCID)

Deposition date: 2009-07-10 Original release date: 2009-07-13

Authors: Leeper, Thomas; Varani, Gabriele; Zheng, Suxin

Citation: Leeper, Thomas; Varani, Gabriele; Zheng, Suxin. "SOLUTION STRUCTURE OF GLUTAREDOXIN FROM Bartonella henselae str. Houston. Seattle Structure Genomics Center for Infectious Disease (SSGCID)"  To be Published ., .-..

Assembly members:
GLUTAREDOXIN, polymer, 89 residues, 10078.538 Da.

Natural source:   Common Name: Bartonella henselae   Taxonomy ID: 283166   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bartonella henselae

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

Entity Sequences (FASTA):
GLUTAREDOXIN: GPGSMKEIILYTRPNCPYCK RARDLLDKKGVKYTDIDAST SLRQEMVQRANGRNTFPQIF IGDYHVGGCDDLYALENKGK LDSLLQDVH

Data sets:
Data typeCount
13C chemical shifts281
15N chemical shifts90
1H chemical shifts588

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GLUTAREDOXIN1

Entities:

Entity 1, GLUTAREDOXIN 89 residues - 10078.538 Da.

1   GLYPROGLYSERMETLYSGLUILEILELEU
2   TYRTHRARGPROASNCYSPROTYRCYSLYS
3   ARGALAARGASPLEULEUASPLYSLYSGLY
4   VALLYSTYRTHRASPILEASPALASERTHR
5   SERLEUARGGLNGLUMETVALGLNARGALA
6   ASNGLYARGASNTHRPHEPROGLNILEPHE
7   ILEGLYASPTYRHISVALGLYGLYCYSASP
8   ASPLEUTYRALALEUGLUASNLYSGLYLYS
9   LEUASPSERLEULEUGLNASPVALHIS

Samples:

sample_1: entity, [U-100% 15N], 0.5 ± 0.05 mM; potassium phosphate 100 ± 0 mM; potassium chloride 10 ± 0 mM; D2O 8 ± 0 %; H2O 92 ± 0 %

sample_2: entity, [U-98% 13C; U-98% 15N], 0.8 ± 0.05 mM; potassium phosphate 100 ± 0 mM; potassium chloride 10 ± 0 mM; D2O 8 ± 0 %; H2O 92 ± 0 %

sample_conditions_1: ionic strength: 110 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

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

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

SPARKY, CCPN - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz

Related Database Links:

PDB
EMBL CAF27210 CDO39798 CDO46401 CUH90372
GB ETS07795 ETS10040 ETS10550 ETS12211 KEC58084
REF WP_011180337

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