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 16123

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for d+PHS/V66K SNase

Deposition date: 2009-01-16 Original release date: 2012-08-07

Authors: Chimenti, Michael

Citation: Chimenti, Michael. "Increased fluctuations and local structural reorganization triggered by the ionization of an internal lysine"  Protein Sci. ., .-..

Assembly members:
D+PHS-V66K_Nuclease, polymer, 143 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
D+PHS-V66K_Nuclease: ATSTKKLHKEPATLIKAIDG DTVKLMYKGQPMTFRLLLVD TPEFNEKYGPEASAFTKKMK ENAKKIEVEFDKGQRTDKYG RGLAYIYADGKMVNEALVRQ GLAKVAYVYKGNNTHEQLLR KAEAQAKKEKLNIWSEDNAD SGQ

Data sets:
Data typeCount
13C chemical shifts243
15N chemical shifts130
1H chemical shifts130

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1D+PHS/V66K1

Entities:

Entity 1, D+PHS/V66K 143 residues - Formula weight is not available

Residues 44-49 (an active site loop) were deleted from the protein; the original numbering scheme was kept.

1   ALATHRSERTHRLYSLYSLEUHISLYSGLU
2   PROALATHRLEUILELYSALAILEASPGLY
3   ASPTHRVALLYSLEUMETTYRLYSGLYGLN
4   PROMETTHRPHEARGLEULEULEUVALASP
5   THRPROGLUPHEASNGLULYSTYRGLYPRO
6   GLUALASERALAPHETHRLYSLYSMETLYS
7   GLUASNALALYSLYSILEGLUVALGLUPHE
8   ASPLYSGLYGLNARGTHRASPLYSTYRGLY
9   ARGGLYLEUALATYRILETYRALAASPGLY
10   LYSMETVALASNGLUALALEUVALARGGLN
11   GLYLEUALALYSVALALATYRVALTYRLYS
12   GLYASNASNTHRHISGLUGLNLEULEUARG
13   LYSALAGLUALAGLNALALYSLYSGLULYS
14   LEUASNILETRPSERGLUASPASNALAASP
15   SERGLYGLN

Samples:

sample_1: D+PHS/V66K Nuclease, [U-99% 15N], 1 mM; D2O 10%; H2O 90%; sodium chloride 100 mM; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 0.17 mM; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY v3.110, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15901
PDB

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