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 18018

Title: NMR structure of the putative ATPase regulatory protein YP_916642.1 from Paracoccus denitrificans

Deposition date: 2011-10-24 Original release date: 2011-11-29

Authors: Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; Morales-Rios, Edga; Zarco-Zavala, Mariel; Garcia-Trejo, Jose; Dutta, Samit; JCSG, JCSG

Citation: Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; Dutta, Samit; Morales-Rios, Edga; Garcia-Trejo, Jose; Zarco-Zavala, Mariel. "NMR structure of the putative ATPase regulatory protein YP_916642.1 from Paracoccus denitrificans"  Not known ., .-..

Assembly members:
entity, polymer, 104 residues, 11687.060 Da.

Natural source:   Common Name: Paracoccus denitrificans   Taxonomy ID: 266   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Paracoccus denitrificans

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

Entity Sequences (FASTA):
entity: MTTFDDRERAHEAKFAHDAE LNFKAEARRNRLLGEWAAGL LGKTGDDARAYALTVVTSDF DEPGDEDVFRKLAADLEGKA DEETIRAKMVELRATAREQI ISEI

Data sets:
Data typeCount
13C chemical shifts360
15N chemical shifts98
1H chemical shifts593

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YP_916642.11

Entities:

Entity 1, YP_916642.1 104 residues - 11687.060 Da.

1   METTHRTHRPHEASPASPARGGLUARGALA
2   HISGLUALALYSPHEALAHISASPALAGLU
3   LEUASNPHELYSALAGLUALAARGARGASN
4   ARGLEULEUGLYGLUTRPALAALAGLYLEU
5   LEUGLYLYSTHRGLYASPASPALAARGALA
6   TYRALALEUTHRVALVALTHRSERASPPHE
7   ASPGLUPROGLYASPGLUASPVALPHEARG
8   LYSLEUALAALAASPLEUGLUGLYLYSALA
9   ASPGLUGLUTHRILEARGALALYSMETVAL
10   GLULEUARGALATHRALAARGGLUGLNILE
11   ILESERGLUILE

Samples:

sample_1: YP_916642.1, [U-98% 13C; U-98% 15N], 1.5 mM; sodium chloride 50 mM; sodium phosphate 25 mM; sodium azide 5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.083 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
5D APSY CBCACONHsample_1isotropicsample_conditions_1
4D APSY HACANHsample_1isotropicsample_conditions_1
5D APSY HACACONHsample_1isotropicsample_conditions_1

Software:

CYANA, G ntert P. - refinement

UNIO, Unio Herrmann Wuthrich - chemical shift assignment, structure solution

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 19510
PDB
GB ABL70946
REF WP_011749137

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