BMRB Entry 10145

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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/BMR10145
MolProbity Validation Chart

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Title:
Solution structure of the N-teruminus extended RhoGAP domain from human Rho GTPase activating protein 5 variant
Deposition date:
2007-12-04
Original release date:
2008-12-10
Authors:
Tomizawa, T.; Tochio, N.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Tomizawa, T.; Tochio, N.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the N-teruminus extended RhoGAP domain from human Rho GTPase activating protein 5 variant"  .

Assembly members:

Assembly members:
RhoGAP domain, polymer, 219 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: cell free synthesis   Vector: P060123-15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RhoGAP domain: GSSGSSGKNFNPPTRRNWES NYFGMPLQDLVTAEKPIPLF VEKCVEFIEDTGLCTEGLYR VSGNKTDQDNIQKQFDQDHN INLVSMEVTVNAVAGALKAF FADLPDPLIPYSLHPELLEA AKIPDKTERLHALKEIVKKF HPVNYDVFRYVITHLNRVSQ QHKINLMTADNLSICFWPTL MRPDFENREFLSTTKIHQSV VETFIQQCQFFFYNGEIVE

Data sets:
Data typeCount
13C chemical shifts990
15N chemical shifts222
1H chemical shifts1575

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Rho GTPase activating protein 5 variant1

Entities:

Entity 1, Rho GTPase activating protein 5 variant 219 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYLYSASNPHE
2   ASNPROPROTHRARGARGASNTRPGLUSER
3   ASNTYRPHEGLYMETPROLEUGLNASPLEU
4   VALTHRALAGLULYSPROILEPROLEUPHE
5   VALGLULYSCYSVALGLUPHEILEGLUASP
6   THRGLYLEUCYSTHRGLUGLYLEUTYRARG
7   VALSERGLYASNLYSTHRASPGLNASPASN
8   ILEGLNLYSGLNPHEASPGLNASPHISASN
9   ILEASNLEUVALSERMETGLUVALTHRVAL
10   ASNALAVALALAGLYALALEULYSALAPHE
11   PHEALAASPLEUPROASPPROLEUILEPRO
12   TYRSERLEUHISPROGLULEULEUGLUALA
13   ALALYSILEPROASPLYSTHRGLUARGLEU
14   HISALALEULYSGLUILEVALLYSLYSPHE
15   HISPROVALASNTYRASPVALPHEARGTYR
16   VALILETHRHISLEUASNARGVALSERGLN
17   GLNHISLYSILEASNLEUMETTHRALAASP
18   ASNLEUSERILECYSPHETRPPROTHRLEU
19   METARGPROASPPHEGLUASNARGGLUPHE
20   LEUSERTHRTHRLYSILEHISGLNSERVAL
21   VALGLUTHRPHEILEGLNGLNCYSGLNPHE
22   PHEPHETYRASNGLYGLUILEVALGLU

Samples:

sample_1: RhoGAP domain, [U-13C; U-15N], 1.31 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1not availablecondition_1
3D 15N-separated NOESYsample_1not availablecondition_1

Software:

xwinnmr v3.5, Bruker - collection

TOPSPIN v1.3, Bruker - collection

NMRPipe v20060524, Delaglio, F - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9823, Kobayashi, N. - data analysis

CYANA v2.0.17, Guentert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 900 MHz
  • Bruker AVANCE II 900 MHz

Related Database Links:

PDB
DBJ BAD92988
GB AAH50059 AAH75799 AAI29929 AAI29930 AAI50824
REF NP_001025226 NP_001164 NP_001185592 NP_033836 XP_001915097
SP P97393 Q13017
AlphaFold P97393 Q13017

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