BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19033

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

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

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"  Not known ., .-..

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts214
15N chemical shifts69
1H chemical shifts450

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH3 domain of human RAS GAP 11

Entities:

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

1   GLYARGARGARGVALARGALAILELEUPRO
2   TYRTHRLYSVALPROASPTHRASPGLUILE
3   SERPHELEULYSGLYASPMETPHEILEVAL
4   HISASNGLULEUGLUASPGLYTRPMETTRP
5   VALTHRASNLEUARGTHRASPGLUGLNGLY
6   LEUILEVALGLUASPLEUVALGLUGLUVAL
7   GLYARG

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
4D-HACANH-APSYsample_1isotropicsample_conditions_1
5D-CBCACONH-APSYsample_1isotropicsample_conditions_1
5D-HACACONH-APSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_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

Related Database Links:

PDB
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