BMRB Entry 5492

Title:
1H and 15N Chemical Shift Assignments for the charge reverse variant of Ribonuclease Sa "5K" (D1K, D17K, D25K, E41K, E74K)
Deposition date:
2002-08-05
Original release date:
2003-02-20
Authors:
Laurents, Douglas; Huyghues-Despointes, Beatrice; Bruix, Marta; Thurlkill, Richard; Schell, David; Newsome, Stephanie; Grimsley, Gerald; Shaw, Kevin; Trevino, Saul; Rico, Manuel; Scholtz, J. Martin; Pace, C. Nick
Citation:

Citation: Laurents, Douglas; Huyghues-Despointes, Beatrice; Bruix, Marta; Thurlkill, Richard; Schell, David; Newsom, Stephanie; Grimsley, Gerald; Shaw, Kevin; Trevino, Saul; Rico, Manuel; Briggs, James; Antosiewicz, Jan; Scholtz, J.; Pace, C.. "Charge-Charge Interactions are Key Determinants of the pK Values of Ionizable Groups in Ribonuclease Sa (pI=3.5) and a Basic Variant (pI=10.2)"  J. Mol. Biol. 325, 1077-1092 (2003).
PubMed: 12527309

Assembly members:

Assembly members:
Ribonuclease Sa, polymer, 96 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: S. aureofaciens   Taxonomy ID: 1894   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Streptomyces aureofaciens

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Data sets:
Data typeCount
1H chemical shifts489
15N chemical shifts89

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
15K RNase Sa1

Entities:

Entity 1, 5K RNase Sa 96 residues - Formula weight is not available

1   LYSVALSERGLYTHRVALCYSLEUSERALA
2   LEUPROPROGLUALATHRLYSTHRLEUASN
3   LEUILEALASERLYSGLYPROPHEPROTYR
4   SERGLNASPGLYVALVALPHEGLNASNARG
5   LYSSERVALLEUPROTHRGLNSERTYRGLY
6   TYRTYRHISGLUTYRTHRVALILETHRPRO
7   GLYALAARGTHRARGGLYTHRARGARGILE
8   ILETHRGLYLYSALATHRGLNGLUASPTYR
9   TYRTHRGLYASPHISTYRALATHRPHESER
10   LEUILEASPGLNTHRCYS

Samples:

sample_1: Ribonuclease Sa, [U-13C; U-15N], 1 – 2 mM; NaCl 0.005 M

Ex_cond_1: pH: 5.5; temperature: 303 K; ionic strength: 0.005 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYnot availablenot availablenot available
2D 1H-1H NOESYnot availablenot availablenot available
2D 1H-15N HSQCnot availablenot availablenot available

Software:

No software information available

NMR spectrometers:

  • Bruker AMX 600 MHz

Related Database Links:

PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks