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 5698

Title: Backbone and Side-chain 1H, and 15N Chemical Shift Assignments for TcPABC   PubMed: 12930992

Deposition date: 2003-02-17 Original release date: 2003-09-12

Authors: Siddiqui, Nadeem; Kozlov, Guennadi; D'Orso, Ivan; Trempe, Jean-Francois; Gehring, Kalle

Citation: Siddiqui, Nadeem; Kozlov, Guennadi; D'Orso, Ivan; Trempe, Jean-Francois; Gehring, Kalle. "Solution Structure of the C-terminal Domain from Poly(A)-binding Protein in Trypanosoma cruzi: A Vegetal PABC Domain "  Protein Sci. 12, 1925-1933 (2003).

Assembly members:
C-terminal domain of PABP, polymer, 85 residues, 9090 Da.

Natural source:   Common Name: Trypanosoma cruzi   Taxonomy ID: 5693   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma cruzi

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

Entity Sequences (FASTA):
C-terminal domain of PABP: GSSLASQGQNLSTVLANLTP EQQKNVLGERLYNHIVAINP AAAAKVTGMLLEMDNGEILN LLDTPGLLDAKVQEALEVLN RHMNV

Data sets:
Data typeCount
1H chemical shifts466
15N chemical shifts80
coupling constants74

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-term domain of PABP1

Entities:

Entity 1, C-term domain of PABP 85 residues - 9090 Da.

1   GLYSERSERLEUALASERGLNGLYGLNASN
2   LEUSERTHRVALLEUALAASNLEUTHRPRO
3   GLUGLNGLNLYSASNVALLEUGLYGLUARG
4   LEUTYRASNHISILEVALALAILEASNPRO
5   ALAALAALAALALYSVALTHRGLYMETLEU
6   LEUGLUMETASPASNGLYGLUILELEUASN
7   LEULEUASPTHRPROGLYLEULEUASPALA
8   LYSVALGLNGLUALALEUGLUVALLEUASN
9   ARGHISMETASNVAL

Samples:

sample_1: C-terminal domain of PABP, [U-15N], 2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 1 mM

Ex-cond_1: pH: 6.3; temperature: 303 K; ionic strength: 0.20 M

Ex-cond_2: pH: 6.3; temperature: 303 K; ionic strength: 0.20 M

Experiments:

NameSampleSample stateSample conditions
HNCACBnot availablenot availablenot available
CBCACONHnot availablenot availablenot available
HNHAnot availablenot availablenot available
2D NOESYnot availablenot availablenot available
3D-15N NOESYnot availablenot availablenot available
IPAP-HSQCnot availablenot availablenot available

Software:

XWINNMR v2.1 - Processing

GIFA v4.31 - Processing

CNS v1.1 - Refinement

XEASY v1.3 - data analysis

ARIA v1.1 - structure solution

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Varian UNITYplus 800 MHz
  • Bruker AVANCE 600 MHz

Related Database Links:

PDB
GB AAC02537 AAC02538 AAC46487 AAC46489 EAN99758
REF XP_821609

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts