BMRB Entry 15938

Name: p190-A RhoGAP FF1 domain
Published: 2009-04-29

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PDB ID: 2k85
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/BMR15938
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

p190-A RhoGAP FF1 domain

Deposition date:

2008-09-02

Original release date:

2009-04-29

Authors:

Bonet, Roman; Ruiz, Lidia; Martin-Malpartida, Pau; Macias, Maria

Citation:

Citation: Bonet, Roman; Ruiz, Lidia; Aragon, E.; Martin-Malpartida, Pau; Macias, Maria. "NMR structural studies on human p190-A RhoGAPFF1 revealed that domain phosphorylation by the PDGF-receptor alpha requires its previous unfolding" J. Mol. Biol. 389, 230-237 (2009).
PubMed: 19393245

Assembly members:

Assembly members:
p190-A_RhoGAP_FF1_domain, polymer, 69 residues, 7857.032 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: pET_trx

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p190-A_RhoGAP_FF1_domain: GAMGSQQIATAKDKYEWLVS RIVKNHNENWLSVSRKMQAS PEYQDYVYLEGTQKAKKLFL QHIHRLKHE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	233
15N chemical shifts	72
1H chemical shifts	482

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p190-A_RhoGAP_FF1_domain	1

Entities:

Entity 1, p190-A_RhoGAP_FF1_domain 69 residues - 7857.032 Da.

Residues 1-4 remain from the cloning after cleavage of the tag.

1

GLY

ALA

MET

GLY

SER

GLN

ILE

ALA

THR

2

ALA

LYS

ASP

LYS

TYR

GLU

TRP

LEU

VAL

SER

3

ARG

ILE

VAL

LYS

ASN

HIS

ASN

GLU

ASN

TRP

4

LEU

SER

VAL

SER

ARG

LYS

MET

GLN

ALA

SER

5

PRO

GLU

TYR

GLN

ASP

TYR

VAL

TYR

LEU

GLU

6

GLY

THR

GLN

LYS

ALA

LYS

LEU

PHE

LEU

7

GLN

HIS

ILE

HIS

ARG

LEU

LYS

HIS

GLU

Samples:

sample_1: p190-A RhoGAP FF1 domain 1 mM; sodium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.5 mM

sample_2: p190-A RhoGAP FF1 domain, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.5 mM

sample_3: p190-A RhoGAP FF1 domain, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.5 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.2; pressure: 1 atm; temperature: 285 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1

Software:

ARIA, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

XEASY, Bartels et al. - chemical shift assignment, peak picking

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

NMR spectrometers:

Bruker AMX 600 MHz

PDB	2K85
DBJ	BAB21813 BAD32520 BAE27848 BAE28076 BAE36578
GB	AAF80386 AAI31566 AAI39460 AAI39462 AAI50258
REF	NP_001003022 NP_001179327 NP_001258061 NP_004482 NP_766327
SP	P81128 P83509 Q91YM2 Q9NRY4
TPG	DAA19691
AlphaFold	P81128 P83509 Q91YM2 Q9NRY4