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 15577

Title: C Repressor   PubMed: 19636908

Deposition date: 2007-12-03 Original release date: 2008-10-14

Authors: Massad, Tariq; Papadopoulos, Evangelos; Damberg, Peter

Citation: Massad, Tariq; Papadopoulos, Evangelos; Henriksson-Peltola, Petri; Haggard-Ljungquist, Elisabeth; Damberg, Peter. "Assignment of 1H, 13C, and 15N chemical shift resonances of P2 C-repressor protein"  Biomol. NMR Assignments 2, 215-217 (2008).

Assembly members:
Crepressor, polymer, 99 residues, Formula weight is not available

Natural source:   Common Name: Enterobacteria phage P2   Taxonomy ID: 10679   Superkingdom: Viruses   Kingdom: not available   Genus/species: P2-like viruses Enterobacteria phage P2

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

Entity Sequences (FASTA):
Crepressor: MSNTISEKIVLMRKSEYLSR QQLADLTGVPYGTLSYYESG RSTPPTDVMMNILQTPQFTK YTLWFMTNQIAPESGQIAPA LAHFGQNETTSPHSGQKTG

Data sets:
Data typeCount
13C chemical shifts422
15N chemical shifts106
1H chemical shifts670

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Crepressor1

Entities:

Entity 1, Crepressor 99 residues - Formula weight is not available

1   METSERASNTHRILESERGLULYSILEVAL
2   LEUMETARGLYSSERGLUTYRLEUSERARG
3   GLNGLNLEUALAASPLEUTHRGLYVALPRO
4   TYRGLYTHRLEUSERTYRTYRGLUSERGLY
5   ARGSERTHRPROPROTHRASPVALMETMET
6   ASNILELEUGLNTHRPROGLNPHETHRLYS
7   TYRTHRLEUTRPPHEMETTHRASNGLNILE
8   ALAPROGLUSERGLYGLNILEALAPROALA
9   LEUALAHISPHEGLYGLNASNGLUTHRTHR
10   SERPROHISSERGLYGLNLYSTHRGLY

Samples:

sample_1: Crepressor, [U-100% 13C; U-100% 15N], 0.6 mM; sodium phosphate 5 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.005 M; pH: 6; pressure: 0.7 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 900 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
EMBL CAJ43636 CAJ43638 CAJ43640 CAJ43642 CAJ43644
GB AAD03298 AAO64734 ABJ01492 AHM44333 AHM48945
REF NP_046787 WP_001306384 WP_001350698
SP P04132

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