BMRB Entry 5939

Title:
Backbone and sidechain assignment of murine Spred2 EVH1 domain
Deposition date:
2003-09-09
Original release date:
2007-05-04
Authors:
Fossi, Michele; Zimmermann, Juergen; Jarchau, Thomas; Lemak, Alexander; Walter, Ulrich; Wiegelt, Johan; Sundstrom, Michael; Arrowsmith, Cheryl; Edwards, Aled; Oschkinat, Hartmut; Ball, Linda
Citation:

Citation: Zimmermann, Juergen; Jarchau, Thomas; Walter, Ulrich; Oschkinat, Hartmut; Ball, Linda. "Letter to the Editor: 1H, 13C and 15N resonance assignment of the human Spred2 EVH1 domain"  J. Biomol. NMR 29, 435-436 (2004).
PubMed: 15213456

Assembly members:

Assembly members:
murine Spred2 EVH1 domain, polymer, 126 residues, 14193 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology

Data sets:
Data typeCount
1H chemical shifts810
13C chemical shifts353
15N chemical shifts127

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Spred2 EVH1 domain1

Entities:

Entity 1, Spred2 EVH1 domain 126 residues - 14193 Da.

1   GLYSERMETTHRGLUGLUTHRHISPROASP
2   ASPASPSERTYRILEVALARGVALLYSALA
3   VALVALMETTHRARGASPASPSERSERGLY
4   GLYTRPPHEPROGLNGLUGLYGLYGLYILE
5   SERARGVALGLYVALCYSLYSVALMETHIS
6   PROGLUGLYASNGLYARGSERGLYPHELEU
7   ILEHISGLYGLUARGGLNLYSASPLYSLEU
8   VALVALLEUGLUCYSTYRVALARGLYSASP
9   LEUVALTYRTHRLYSALAASNPROTHRPHE
10   HISHISTRPLYSVALASPASNARGLYSPHE
11   GLYLEUTHRPHEGLNSERPROALAASPALA
12   ARGALAPHEASPARGGLYVALARGLYSALA
13   ILEGLUASPLEUILEGLU

Samples:

Sample_1: murine Spred2 EVH1 domain, [U-15N], 1.0 mM; H2O 100%

Sample_2: murine Spred2 EVH1 domain, [U-15N; U-13C], 1.0 mM; H2O 100%

Sample_3: murine Spred2 EVH1 domain, [U-15N; U-13C], 1.0 mM; D2O 100%

Cond_1: pH: 6.0; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
15N-NOESY-HSQCnot availablenot availableCond_1
13C-NOESY-HSQCnot availablenot availableCond_1
13C-HMQC-NOESYnot availablenot availableCond_1
CBCACONNHnot availablenot availableCond_1
CBCANNHnot availablenot availableCond_1
15N-HSQCnot availablenot availableCond_1
CCCONNHnot availablenot availableCond_1
HCCCONNHnot availablenot availableCond_1
2D-NOESYnot availablenot availableCond_1
2D-TOCSYnot availablenot availableCond_1
2D-COSYnot availablenot availableCond_1
15N-TOCSYnot availablenot availableCond_1

Software:

XWIN-NMR v2.6, Bruker Biospin - collection

ANSIG v3.3, Kraulis - data analysis, chemical shift assignment, peak picking, integration

AZARA v2.1, Boucher - data analysis, peak picking

PSVS v1.3, Hang, Montelione, et al. - refinement, structure validation

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

ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution, refinement

NMR spectrometers:

  • Bruker DMX 750 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAB62849 BAC29425 BAE46587 BAE90243 BAG51727
EMBL CAH90125
GB AAH66013 AAI11496 AAI30293 AAI36335 AAP59415
REF NP_001040559 NP_001121682 NP_001127241 NP_001248029 NP_277058
SP Q3C2P8 Q5RDN2 Q7Z698 Q924S7
TPG DAA24561
AlphaFold Q3C2P8 Q5RDN2 Q7Z698 Q924S7

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