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 5525

Title: NMR structure of the first Zinc Binding domain of Nup475/TTP/TIS11   PubMed: 12515557

Deposition date: 2002-09-13 Original release date: 2003-09-05

Authors: Amann, B.; Guerrerio, A.; Pelo, J.; Luo, R.; Worthington, M.; Berg, J.

Citation: Amann, B.; Worthington, M.; Berg, J.. "A Cys3His Zinc-binding Domain from Nup475/Tristetraprolin: A Novel Fold with a Disklike Structure "  Biochemistry 42, 217-221 (2003).

Assembly members:
Tristetraproline, polymer, 77 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

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

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Tristetraproline: GSHMTTSSRYKTELCRTYSE SGRCRYGAKCQFAHGLGELR QANRHPKYKTELCHKFKLQG RCPYGSRCHFIHNPTED

Data sets:
Data typeCount
1H chemical shifts220
13C chemical shifts72
coupling constants15

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tristetraproline1
2ZINC ION2

Entities:

Entity 1, Tristetraproline 77 residues - Formula weight is not available

1   GLYSERHISMETTHRTHRSERSERARGTYR
2   LYSTHRGLULEUCYSARGTHRTYRSERGLU
3   SERGLYARGCYSARGTYRGLYALALYSCYS
4   GLNPHEALAHISGLYLEUGLYGLULEUARG
5   GLNALAASNARGHISPROLYSTYRLYSTHR
6   GLULEUCYSHISLYSPHELYSLEUGLNGLY
7   ARGCYSPROTYRGLYSERARGCYSHISPHE
8   ILEHISASNPROTHRGLUASP

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Tristetraproline 1.7 mM; ZnCl2 3.74 mM; Tris, [U-2H], 50 mM; H20 90%; D20 10%

sample_2: Tristetraproline 1.7 mM; ZnCl2 3.74 mM; Tris, [U-2H], 50 mM; D20 100%

sample_cond_1: pH: 5.8; temperature: 293 K; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
2D NOESYnot availablenot availablesample_cond_1
2D TOCSYnot availablenot availablesample_cond_1
DQF-COSYnot availablenot availablesample_cond_1
3D 13C-separated NOESYnot availablenot availablesample_cond_1
3D 15N-separated NOESYnot availablenot availablesample_cond_1
HNCACBnot availablenot availablesample_cond_1
15N-HSQC-TOCSYnot availablenot availablesample_cond_1
13C-HCCH-TOCSYnot availablenot availablesample_cond_1
HSQCJ WEXnot availablenot availablesample_cond_1

Software:

FELIX v98 - processing

CNS v1.0 - structure solution, refinement

VNMR v6.1b - collection

NMR spectrometers:

  • Varian UNITYplus 500 MHz

Related Database Links:

REF NP_035886
SWISS-PROT P22893
GenBank AAC37676 AAH21391 AAA40498 AAA72947 AAA39837
EMBL CAA32807
DBJ BAE32856 BAE35432 BAB23739
PDB