BMRB Entry 17254

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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/BMR17254
MolProbity Validation Chart

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Title:
Promiscuous Binding at the Crossroads of Numerous Cancer Pathways: Insight from the Binding of GIP with Glutaminase L
Deposition date:
2010-10-13
Original release date:
2011-03-24
Authors:
Zoetewey, David; Ovee, Mohiuddin; Banerjee, Monimoy; Bhaskaran, Rajagopalan; Mohanty, Smita
Citation:

Citation: Zoetewey, David; Ovee, Mohiuddin; Banerjee, Monimoy; Bhaskaran, Rajagopalan; Mohanty, Smita. "Promiscuous binding at the crossroads of numerous cancer pathways: insight from the binding of glutaminase interacting protein with glutaminase L."  Biochemistry 50, 3528-3539 (2011).
PubMed: 21417405

Assembly members:

Assembly members:
Glutaminase_Interacting_Protein_3, polymer, 124 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-3c/GIP

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Glutaminase_Interacting_Protein_3: MSYIPGQPVTAVVQRVEIHK LRQGENLILGFSIGGGIDQD PSQNPFSEDKTDKGIYVTRV SEGGPAEIAGLQIGDKIMQV NGWDMTMVTHDQARKRLTKR SEEVVRLLVTRQSLQKAVQQ SMLS

Data sets:
Data typeCount
13C chemical shifts502
15N chemical shifts131
1H chemical shifts877

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1GIP1

Entities:

Entity 1, GIP 124 residues - Formula weight is not available

1   METSERTYRILEPROGLYGLNPROVALTHR
2   ALAVALVALGLNARGVALGLUILEHISLYS
3   LEUARGGLNGLYGLUASNLEUILELEUGLY
4   PHESERILEGLYGLYGLYILEASPGLNASP
5   PROSERGLNASNPROPHESERGLUASPLYS
6   THRASPLYSGLYILETYRVALTHRARGVAL
7   SERGLUGLYGLYPROALAGLUILEALAGLY
8   LEUGLNILEGLYASPLYSILEMETGLNVAL
9   ASNGLYTRPASPMETTHRMETVALTHRHIS
10   ASPGLNALAARGLYSARGLEUTHRLYSARG
11   SERGLUGLUVALVALARGLEULEUVALTHR
12   ARGGLNSERLEUGLNLYSALAVALGLNGLN
13   SERMETLEUSER

Samples:

sample_1: Glutaminase Interacting Protein 3, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; sodium phosphate 50 mM; sodium azide 0.1 % w/v; EDTA 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 273 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

ARIA v1.1, Dr. Michael Nilges, Institut Pasteur - Automated NOE assignment, NMR structure calculation

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

UNP O14907-1
AlphaFold Q7LCQ4

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