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 4905

Title: 1H, 13C and 15N Chemical Shift Assignments for Urea-denatured G88W-110 Fragment of Staphylococcal Nuclease   PubMed: 11243822

Deposition date: 2000-11-24 Original release date: 2001-08-08

Authors: Ye, Keqiong; Wang, Jinfeng

Citation: Ye, Keqiong; Wang, Jinfeng. "Self-association Reaction of Denatured Staphylococcal Nuclease Fragments Characterized by Heteronuclear NMR"  J. Mol. Biol. 307, 309-322 (2001).

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

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET3d

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

Data sets:
Data typeCount
1H chemical shifts693
13C chemical shifts322
15N chemical shifts104

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SNase G88W110 fragment1

Entities:

Entity 1, SNase G88W110 fragment 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], 2.5 mM; acetate buffer, [U-99% 2H], 50 mM; Urea 6 M; H2O 90%; D2O 10%

Ex-cond_1: pH: 4.9; temperature: 305 K; ionic strength: 0.05 M

Experiments:

NameSampleSample stateSample conditions
HNCACBnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
HNCOnot availablenot availablenot available
HN(CA)COnot availablenot availablenot available
H(CCO)NHnot availablenot availablenot available
3D 1H-15N TOCSY-HSQCnot availablenot availablenot available
3D 1H-15N NOESY-HSQCnot availablenot availablenot available
3D 1H-15N/1H-15N HSQC-NOESY-HSQCnot availablenot availablenot available
HNHAnot availablenot availablenot available
1H-13C CT-HSQCnot availablenot availablenot available

Software:

FELIX v98 -

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 494 495 496 497 530 5536 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 Q7A6P2 Q6GB41 Q6GIK1

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