BMRB Entry 15128

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15128
MolProbity Validation Chart

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Title:
Solution structure of the RGS domain of human RGS14
Deposition date:
2007-02-02
Original release date:
2007-08-23
Authors:
Dowler, Elizabeth; Diehl, Annette; Bray, James; Elkins, Jon; Soundararajan, Meera; Doyle, Declan; Gileadi, Carina; Phillips, Claire; Schoch, Guillaume; Yang, Xiawen; Brockmann, Christoph; Leidert, Martina; Rehbein, Kristina; Schmieder, Peter; Kuhne, Ronald; Higman, Victoria; Sundstrom, Michael; Arrowsmith, Cheryl; Weigelt, Johan; Edwards, Aled; Oschkinat, Hartmut; Ball, Linda
Citation:

Citation: Soundararajan, Meera; Willard, Francis; Kimple, Adam; Turnbull, Andrew; Ball, Linda; Schoch, Guillaume; Gileadi, Carina; Fedorov, Oleg; Dowler, Elizabeth; Higman, Victoria; Hutsell, Stephanie; Sundstrom, Michael; Doyle, Declan; Siderovski, David. "Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits"  Proc. Natl. Acad. Sci. USA 105, 6457-6462 (2008).
PubMed: 18434541

Assembly members:

Assembly members:
RGS14, polymer, 154 residues, 17728.135 Da.

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: Home-made vector pLIC-SGC1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RGS14: SMTEEQPVASWALSFERLLQ DPLGLAYFTEFLKKEFSAEN VTFWKACERFQQIPASDTQQ LAQEARNIYQEFLSSQALSP VNIDRQAWLGEEVLAEPRPD MFRAQQLQIFNLMKFDSYAR FVKSPLYRECLLAEAEGRPL REPGSSRLGSPDAT

Data sets:
Data typeCount
13C chemical shifts567
15N chemical shifts151
1H chemical shifts1011

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1RGS domain1

Entities:

Entity 1, RGS domain 154 residues - 17728.135 Da.

The two residues at the extreme N-terminus (SM) are from the vector following TEV cleavage of the N-terminus hexahistidine purification tag.

1   SERMETTHRGLUGLUGLNPROVALALASER
2   TRPALALEUSERPHEGLUARGLEULEUGLN
3   ASPPROLEUGLYLEUALATYRPHETHRGLU
4   PHELEULYSLYSGLUPHESERALAGLUASN
5   VALTHRPHETRPLYSALACYSGLUARGPHE
6   GLNGLNILEPROALASERASPTHRGLNGLN
7   LEUALAGLNGLUALAARGASNILETYRGLN
8   GLUPHELEUSERSERGLNALALEUSERPRO
9   VALASNILEASPARGGLNALATRPLEUGLY
10   GLUGLUVALLEUALAGLUPROARGPROASP
11   METPHEARGALAGLNGLNLEUGLNILEPHE
12   ASNLEUMETLYSPHEASPSERTYRALAARG
13   PHEVALLYSSERPROLEUTYRARGGLUCYS
14   LEULEUALAGLUALAGLUGLYARGPROLEU
15   ARGGLUPROGLYSERSERARGLEUGLYSER
16   PROASPALATHR

Samples:

sample_1: RGS14, [U-95% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O 10%; DTT, [U-99% 2H], 1 mM

sample_2: RGS14, [U-95% 13C; U-95% 15N], 1.7 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT, [U-99% 2H], 1 mM; D2O 10%

sample_3: RGS14, [U-95% 13C; U-95% 15N], 1.4 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT, [U-99% 2H], 1 mM; D2O 10%

sample_4: RGS14, [U-95% 13C; U-95% 15N], 1.1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT, [U-99% 2H], 1 mM; D2O, [U-100% 2H], 100%; sodium azide 0.02%

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 297 K

sample_conditions_2: pH: 6; pressure: 1 atm; temperature: 297 K

sample_conditions_3: pH: 6.2; pressure: 1 atm; temperature: 297 K

sample_conditions_4: pH: 6; pressure: 1 atm; temperature: 297 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCANHsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCOsample_3isotropicsample_conditions_3
3D HN(CA)COsample_3isotropicsample_conditions_3
3D HCCH-COSYsample_4isotropicsample_conditions_4
3D 1H-13C HMQC NOESYsample_4isotropicsample_conditions_4
2D 1H-1H NOESYsample_4isotropicsample_conditions_4
2D DQF-COSYsample_4isotropicsample_conditions_4
3D HCCH-TOCSYsample_4isotropicsample_conditions_4

Software:

xwinnmr v2.6 and 3.1, Bruker Biospin - collection, processing

SPARKY v3.100, Goddard - chemical shift assignment, data analysis, peak picking

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

X-PLOR NIH v2.14, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

CNSSOLVE v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DMX 750 MHz

Related Database Links:

PDB
DBJ BAJ20688
GB AAH14094 ADZ15921 EAW85011 EAW85012 EAW85013
REF NP_001179660 NP_006471 XP_001089197 XP_002744538 XP_003280558
SP O43566
TPG DAA27643
AlphaFold O43566

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