BMRB Entry 19033

Name: NMR structure of the SH3 domain of human RAS p21 protein activator (GTPase activating protein) 1
Published: 2013-03-21

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PDB ID: 2m51
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19033
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of the SH3 domain of human RAS p21 protein activator (GTPase activating protein) 1

Deposition date:

2013-02-12

Original release date:

2013-03-21

Authors:

Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation:

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the SH3 domain of human RAS p21 protein activator (GTPase activating protein) 1" .

Assembly members:

Assembly members:
RAS_GAP_1, polymer, 62 residues, 7268.292 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RAS_GAP_1: GRRRVRAILPYTKVPDTDEI SFLKGDMFIVHNELEDGWMW VTNLRTDEQGLIVEDLVEEV GR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	214
15N chemical shifts	69
1H chemical shifts	450

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SH3 domain of human RAS GAP 1	1

Entities:

Entity 1, SH3 domain of human RAS GAP 1 62 residues - 7268.292 Da.

1

GLY

ARG

VAL

ARG

ALA

ILE

LEU

PRO

2

TYR

THR

LYS

VAL

PRO

ASP

THR

ASP

GLU

ILE

3

SER

PHE

LEU

LYS

GLY

ASP

MET

PHE

ILE

VAL

4

HIS

ASN

GLU

LEU

GLU

ASP

GLY

TRP

MET

TRP

5

VAL

THR

ASN

LEU

ARG

THR

ASP

GLU

GLN

GLY

6

LEU

ILE

VAL

GLU

ASP

LEU

VAL

GLU

VAL

7

GLY

ARG

Samples:

sample_1: RAS_GAP_1, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
4D-HACANH-APSY	sample_1	isotropic	sample_conditions_1
5D-CBCACONH-APSY	sample_1	isotropic	sample_conditions_1
5D-HACACONH-APSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.0, G ntert P. - structure solution

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

j-UNIO, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking, structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2J06 2GQI 4FSS 2J05 2GQI 2M51
DBJ	BAD92343 BAE21614 BAG35610 BAG62024 BAG62030
EMBL	CAA31122 CAH18488 CAH90505
GB	AAA16319 AAA35865 AAA52517 AAH13637 AAH20761
PRF	1411306A 1615347A 1615347B
REF	NP_001125265 NP_002881 NP_037267 NP_072179 NP_663427
SP	P09851 P20936 P50904
TPG	DAA27162
AlphaFold	P09851 P20936 P50904