BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 5053

Title: Solution Structure of the Orphan PABC Domain from Saccharomyces cerevisiae Poly(A)-binding Protein

Authors: Kozlov, Guennadi; Siddiqui, Nadeem; Coillet-Matillon, Stephane; Trempe, Jean-Francois; Ekiel, Irena; Sprules, Tara; Gehring, Kalle

Citation: Kozlov, Guennadi; Siddiqui, Nadeem; Coillet-Matillon, Stephane; Trempe, Jean-Francois; Ekiel, Irena; Sprules, Tara; Gehring, Kalle. "Solution Structure of the Orphan PABC Domain from Saccharomyces cerevisiae Poly(A)-binding Protein"  J. Biol. Chem. 277, 22822-22828 (2002).

Assembly members:
C-terminal domain of Pab1p, polymer, 92 residues, 10434 Da.

Natural source:   Common Name: Yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
C-terminal domain of Pab1p: GPLGSPRNANDNNQFYQQKQ RQALGEQLYKKVSAKTSNEE AAGKITGMILDLPPQEVFPL LESDELFEQHYKEASAAYES FKKEQEQQTEQA

Data sets:
Data typeCount
1H chemical shifts504
13C chemical shifts174
15N chemical shifts85
coupling constants68

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PABC domain1

Entities:

Entity 1, PABC domain 92 residues - 10434 Da.

1   GLYPROLEUGLYSERPROARGASNALAASN
2   ASPASNASNGLNPHETYRGLNGLNLYSGLN
3   ARGGLNALALEUGLYGLUGLNLEUTYRLYS
4   LYSVALSERALALYSTHRSERASNGLUGLU
5   ALAALAGLYLYSILETHRGLYMETILELEU
6   ASPLEUPROPROGLNGLUVALPHEPROLEU
7   LEUGLUSERASPGLULEUPHEGLUGLNHIS
8   TYRLYSGLUALASERALAALATYRGLUSER
9   PHELYSLYSGLUGLNGLUGLNGLNTHRGLU
10   GLNALA

Samples:

sample_1: C-terminal domain of Pab1p, [U-15N], 3.0 mM; NaCl 150 mM

sample_2: C-terminal domain of Pab1p 3.0 mM; NaCl 150 mM

sample_3: C-terminal domain of Pab1p, [U-13C; U-15N], 3.0 mM; NaCl 150 mM

conditions_1: pH: 6.3; temperature: 303 K; ionic strength: 0.15 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYnot availablenot availablenot available
3D 1H-1H-15N NOESYnot availablenot availablenot available
3D 1H-1H-15N TOCSYnot availablenot availablenot available
3D CBCA(CO)NHnot availablenot availablenot available
3D HNCACBnot availablenot availablenot available

Software:

XWINNMR v2.1 - data collection

GIFA v4.31 - data processing

XEASY v1.3.13 - data analysis

ARIA v0.9 - automated NOE assignment

CNS v0.9 - refinement

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Varian UnityPlus 750 MHz

Related Database Links:

PDB
DBJ BAA00017 GAA22994
EMBL CAY79353
GB AAA34787 AAA34838 AAB64692 AAT92873 AHY75721
REF NP_011092 XP_011103263
SP P04147
TPG DAA07827