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 16675

Title: The NMR structure of protein-glutaminase from Chryseobacterium proteolyticum   PubMed: 20195702

Deposition date: 2010-01-14 Original release date: 2010-05-05

Authors: Kumeta, Hiroyuki; Miwa, Noriko; Ogura, Kenji; Kai, Yuko; Mizukoshi, Toshimi; Shimba, Nobuhisa; Suzuki, Ei-ichiro; Inagaki, Fuyuhiko

Citation: Kumeta, Hiroyuki; Miwa, Noriko; Ogura, Kenji; Kai, Yuko; Mizukoshi, Toshimi; Shimba, Nobuhisa; Suzuki, Ei-ichiro; Inagaki, Fuyuhiko. "The NMR structure of protein-glutaminase from Chryseobacterium proteolyticum."  J. Biomol. NMR 46, 251-255 (2010).

Assembly members:
protein-glutaminase, polymer, 185 residues, 19875.396 Da.

Natural source:   Common Name: Chryseobacterium proteolyticum   Taxonomy ID: 118127   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Chryseobacterium proteolyticum

Experimental source:   Production method: recombinant technology   Host organism: Corynebacterium glutamicum

Entity Sequences (FASTA):
protein-glutaminase: LASVIPDVATLNSLFNQIKN QSCGTSTASSPCITFRYPVD GCYARAHKMRQILMNNGYDC EKQFVYGNLKASTGTCCVAW SYHVAILVSYKNASGVTEKR IIDPSLFSSGPVTDTAWRNA CVNTSCGSASVSSYANTAGN VYYRSPSNSYLYDNNLINTN CVLTKFSLLSGCSPSPAPDV SSCGF

Data sets:
Data typeCount
13C chemical shifts797
15N chemical shifts205
1H chemical shifts1247

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein-glutaminase1

Entities:

Entity 1, protein-glutaminase 185 residues - 19875.396 Da.

1   LEUALASERVALILEPROASPVALALATHR
2   LEUASNSERLEUPHEASNGLNILELYSASN
3   GLNSERCYSGLYTHRSERTHRALASERSER
4   PROCYSILETHRPHEARGTYRPROVALASP
5   GLYCYSTYRALAARGALAHISLYSMETARG
6   GLNILELEUMETASNASNGLYTYRASPCYS
7   GLULYSGLNPHEVALTYRGLYASNLEULYS
8   ALASERTHRGLYTHRCYSCYSVALALATRP
9   SERTYRHISVALALAILELEUVALSERTYR
10   LYSASNALASERGLYVALTHRGLULYSARG
11   ILEILEASPPROSERLEUPHESERSERGLY
12   PROVALTHRASPTHRALATRPARGASNALA
13   CYSVALASNTHRSERCYSGLYSERALASER
14   VALSERSERTYRALAASNTHRALAGLYASN
15   VALTYRTYRARGSERPROSERASNSERTYR
16   LEUTYRASPASNASNLEUILEASNTHRASN
17   CYSVALLEUTHRLYSPHESERLEULEUSER
18   GLYCYSSERPROSERPROALAPROASPVAL
19   SERSERCYSGLYPHE

Samples:

CN-label: protein glutaminase, [U-13C; U-15N], 1.15 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCCN-labelisotropicsample_conditions_1
2D 1H-13C HSQCCN-labelisotropicsample_conditions_1
3D 1H-15N NOESYCN-labelisotropicsample_conditions_1
3D HCCH-TOCSYCN-labelisotropicsample_conditions_1
3D HNCOCN-labelisotropicsample_conditions_1
3D HN(CO)CACN-labelisotropicsample_conditions_1
3D HNCACN-labelisotropicsample_conditions_1
3D HBHA(CO)NHCN-labelisotropicsample_conditions_1
3D HN(CA)HACN-labelisotropicsample_conditions_1
3D CBCA(CO)NHCN-labelisotropicsample_conditions_1
3D HNCACBCN-labelisotropicsample_conditions_1
3D CCH-TOCSYCN-labelisotropicsample_conditions_1
3D 1H-13C NOESYCN-labelisotropicsample_conditions_1
2D HbCbCgCdHdCN-labelisotropicsample_conditions_1
2D HbCbCgCdCeHeCN-labelisotropicsample_conditions_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v5.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.111, Goddard - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAB21508 BAF76799

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