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Biological Magnetic Resonance Data Bank


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BMRB Entry 17935

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17935
MolProbity Validation Chart

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Title: 1H, 13C, 15N assignment and secondary structure determination of GATase subunit of GMP Synthetase from Methanococcus jannaschii   PubMed: 22203461

Deposition date: 2011-09-13 Original release date: 2011-12-20

Authors: Ali, Rustam; Sarma, Siddhartha

Citation: Ali, Rustam; Kumar, Sanjeev; Balaram, Hemalatha; Sarma, Siddhartha. "1H, 13C, 15N assignment and secondary structure determination of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii."  Biomol. NMR Assignments 6, 193-196 (2012).

Assembly members:
GATase_subunit, polymer, 188 residues, 21020.2 Da.

Natural source:   Common Name: Methanococcus jannaschii   Taxonomy ID: 2190   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanococcus jannaschii

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

Entity Sequences (FASTA):
GATase_subunit: MIVILDNGGQYVHRIHRSLK YIGVSSKIVPNTTPLEEIES NKEVKGIILSGGPDIEKAKN CIDIALNAKLPILGICLGHQ LIALAYGGEVGRAEAEEYAL TKVYVDKENDLFKNVPREFN AWASHKDEVKKVPEGFEILA HSDICQVEAMKHKTKPIYGV QFHPEVAHTEYGNEILKNFC KVCGYKFE

Data sets:
Data typeCount
13C chemical shifts395
15N chemical shifts185
1H chemical shifts857

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GATase subunit1

Entities:

Entity 1, GATase subunit 188 residues - 21020.2 Da.

1   METILEVALILELEUASPASNGLYGLYGLN
2   TYRVALHISARGILEHISARGSERLEULYS
3   TYRILEGLYVALSERSERLYSILEVALPRO
4   ASNTHRTHRPROLEUGLUGLUILEGLUSER
5   ASNLYSGLUVALLYSGLYILEILELEUSER
6   GLYGLYPROASPILEGLULYSALALYSASN
7   CYSILEASPILEALALEUASNALALYSLEU
8   PROILELEUGLYILECYSLEUGLYHISGLN
9   LEUILEALALEUALATYRGLYGLYGLUVAL
10   GLYARGALAGLUALAGLUGLUTYRALALEU
11   THRLYSVALTYRVALASPLYSGLUASNASP
12   LEUPHELYSASNVALPROARGGLUPHEASN
13   ALATRPALASERHISLYSASPGLUVALLYS
14   LYSVALPROGLUGLYPHEGLUILELEUALA
15   HISSERASPILECYSGLNVALGLUALAMET
16   LYSHISLYSTHRLYSPROILETYRGLYVAL
17   GLNPHEHISPROGLUVALALAHISTHRGLU
18   TYRGLYASNGLUILELEULYSASNPHECYS
19   LYSVALCYSGLYTYRLYSPHEGLU

Samples:

sample_1: GATase subunit, [U-99% 15N], 0.7 mM; D2O 10%; H2O 90%; PMSF 1 mM; potassium phosphate 20 mM; EDTA 0.1 mM; DTT 2 mM; sodium azide 0.01%

sample_2: GATase subunit, [U-99% 13C; U-99% 15N], 0.6 mM; H2O 90%; D2O 10%; potassium phosphate 20 mM; EDTA 0.1 mM; DTT 2 mM; PMSF 1 mM; sodium azide 0.01%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_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-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

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

CCPN, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
GB AAB99597
SP Q58970

Download simulated HSQC data in one of the following formats:
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