BMRB Entry 4386

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4386
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
HIGH-RESOLUTION SOLUTION STRUCTURE OF FREE RGS4 BY NMR
Deposition date:
1999-09-03
Original release date:
2001-07-27
Authors:
Moy, F.; Chanda, P.; Cockett, M.; Edris, W.; Jones, P.; Mason, K.; Semus, S.; Powers, R.
Citation:

Citation: Moy, F.; Chanda, P.; Cockett, M.; Edris, W.; Jones, P.; Mason, K.; Semus, S.; Powers, R.. "NMR Structure of Free RGS4 Reveals an Induced Conformational Change upon Binding G-alpha"  Biochemistry 39, 7063-7073 (2000).

Assembly members:

Assembly members:
REGULATOR OF G-PROTEIN SIGNALING 4, polymer, 166 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Norway rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PRGS4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
REGULATOR OF G-PROTEIN SIGNALING 4: MRGSVSQEEVKKWAESLENL INHECGLAAFKAFLKSEYSE ENIDFWISCEEYKKIKSPSK LSPKAKKIYNEFISVQATKE VNLDSCTREETSRNMLEPTI TCFDEAQKKIFNLMEKDSYR RFLKSRFYLDLTNPSSCGAE KQKGAKSSADCTSLVPQCAH HHHHHP

Data sets:
Data typeCount
13C chemical shifts666
15N chemical shifts159
1H chemical shifts1062

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1REGULATOR OF G-PROTEIN SIGNALING 41

Entities:

Entity 1, REGULATOR OF G-PROTEIN SIGNALING 4 166 residues - Formula weight is not available

1   METARGGLYSERVALSERGLNGLUGLUVAL
2   LYSLYSTRPALAGLUSERLEUGLUASNLEU
3   ILEASNHISGLUCYSGLYLEUALAALAPHE
4   LYSALAPHELEULYSSERGLUTYRSERGLU
5   GLUASNILEASPPHETRPILESERCYSGLU
6   GLUTYRLYSLYSILELYSSERPROSERLYS
7   LEUSERPROLYSALALYSLYSILETYRASN
8   GLUPHEILESERVALGLNALATHRLYSGLU
9   VALASNLEUASPSERCYSTHRARGGLUGLU
10   THRSERARGASNMETLEUGLUPROTHRILE
11   THRCYSPHEASPGLUALAGLNLYSLYSILE
12   PHEASNLEUMETGLULYSASPSERTYRARG
13   ARGPHELEULYSSERARGPHETYRLEUASP
14   LEUTHRASNPROSERSERCYSGLYALAGLU
15   LYSGLNLYSGLYALALYSSERSERALAASP
16   CYSTHRSERLEUVALPROGLNCYSALAHIS
17   HISHISHISHISHISPRO

Samples:

sample_1: REGULATOR OF G-PROTEIN SIGNALING 4, [U-15N; U-13C], 1 mM; phosphate buffer 50 mM; NaN3 2 mM; DTT, [U-2H], 5 mM; H2O 90%; D2O 10%

sample_2: REGULATOR OF G-PROTEIN SIGNALING 4, [U-15N; U-13C], 1 mM; phosphate buffer 50 mM; NaN3 2 mM; DTT, [U-2H], 5 mM; D2O 100%

sample_3: REGULATOR OF G-PROTEIN SIGNALING 4, [U-15N], 1 mM; phosphate buffer 50 mM; NaN3 2 mM; DTT, [U-2H], 5 mM; H2O 90%; D2O 10%

sample_cond_1: ionic strength: 50 mM; pH: 6.0; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYnot availablenot availablenot available
HNHAnot availablenot availablenot available

Software:

X-PLOR v3.84 - structure solution

NMRPipe v1.7 - processing

XWINNMR v2.0 - collection

PIPP v4.8.2 - data analysis

NMR spectrometers:

  • Bruker AMX 600 MHz

Related Database Links:

PDB
DBJ BAA20400 BAC27009 BAC30249 BAE01800 BAG35182
EMBL CAH92413
GB AAC50395 AAC52440 AAD12065 AAH00737 AAH03882
PRF 2206475B 2206475C
REF NP_001095915 NP_001106851 NP_005604 NP_033088 NP_058910
SP O08899 P49798 P49799 Q4R525 Q5R747
AlphaFold O08899 P49798 P49799 Q4R525 Q5R747

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