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 5536

Title: 1H, 13C, and 15N Chemical Shift Assignments for G88W110 fragment of Staphylococcal Nuclease   PubMed: 17172296

Deposition date: 2002-09-22 Original release date: 2007-07-10

Authors: Liu, Dongsheng; Ye, Keqiong; Feng, Yingang; Wang, Jinfeng

Citation: Xie, Tao; Liu, Dongsheng; Feng, Yingang; Shan, Lu; Wang, Jinfeng. "Folding stability and cooperativity of the three forms of 1-110 residues fragment of staphylococcal nuclease"  Biophys. J. 92, 2090-2107 (2007).

Assembly members:
Staphylococcal nuclease, polymer, 110 residues, Formula weight is not available

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Staphylococcal nuclease: ATSTKKLHKEPATLIKAIDG DTVKLMYKGQPMTFRLLLVD TPETKHPKKGVEKYGPEASA FTKKMVENAKKIEVEFDKGQ RTDKYGRWLAYIYADGKMVN EALVRQGLAK

Data sets:
Data typeCount
1H chemical shifts620
13C chemical shifts463
15N chemical shifts109

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1G88W110 monomer1

Entities:

Entity 1, G88W110 monomer 110 residues - Formula weight is not available

1   ALATHRSERTHRLYSLYSLEUHISLYSGLU
2   PROALATHRLEUILELYSALAILEASPGLY
3   ASPTHRVALLYSLEUMETTYRLYSGLYGLN
4   PROMETTHRPHEARGLEULEULEUVALASP
5   THRPROGLUTHRLYSHISPROLYSLYSGLY
6   VALGLULYSTYRGLYPROGLUALASERALA
7   PHETHRLYSLYSMETVALGLUASNALALYS
8   LYSILEGLUVALGLUPHEASPLYSGLYGLN
9   ARGTHRASPLYSTYRGLYARGTRPLEUALA
10   TYRILETYRALAASPGLYLYSMETVALASN
11   GLUALALEUVALARGGLNGLYLEUALALYS

Samples:

Sample_1: Staphylococcal nuclease, [U-95% 13C; U-90% 15N], 2.0 – 2.5 mM

Ex-cond_1: pH: 4.9 na; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H DQF-COSYnot availablenot availablenot available
2D 1H-1H NOESYnot availablenot availablenot available
2D 1H-1H TOCSYnot availablenot availablenot available
2D 1H-15N HSQCnot availablenot availablenot available
3D 1H-1H-15N NOESYnot availablenot availablenot available
3D 1H-1H-15N TOCSYnot availablenot availablenot available
3D HNCACBnot availablenot availablenot available
3D CBCA(CO)NHnot availablenot availablenot available
3D HNCOnot availablenot availablenot available
3D HN(CA)COnot availablenot availablenot available
3D HCCONHnot availablenot availablenot available
3D HCCH-TOCSYnot availablenot availablenot available

Software:

FELIX v97 - data processing, peak assignments

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

BMRB 136 15357 1581 1582 16585 1704 17718 18013 1874 1875 1876 1877 1878 18788 188 189 2784 2785 4010 4052 4053 4905 494 495 496 497 530 6250 6251 644 6907 6908
PDB
DBJ BAB41979 BAB56977 BAB94634 BAF67032 BAF77694
EMBL CAA24594 CAG39855 CAG42530 CAI80436 CAQ49298
GB AAC14660 AAW36415 ABD22328 ABD29945 ABE02272
PRF 1109959A 710414A
REF NP_371339 NP_374001 NP_645586 WP_000141556 WP_000141557
SP P00644 Q5HHM4 Q6GB41 Q6GIK1 Q7A6P2
AlphaFold P00644 Q5HHM4 Q6GB41 Q6GIK1 Q7A6P2

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