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 15357

Title: the solution structure of SNase complex   PubMed: 19658434

Authors: Geng, Yong; Shan, Lu; Feng, Yingang; Wang, Jinfeng

Citation: Geng, Yong; Feng, Yingang; Xie, Tao; Shan, Lu; Wang, Jinfeng. "The native-like interactions between SNase121 and SNase(111-143) fragments induce the recovery of their native-like structures and the ability to degrade DNA."  Biochemistry 48, 8692-8703 (2009).

Assembly members:
SNase complex -subdomain, polymer, 156 residues, 17686.604 Da.

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

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

Entity Sequences (FASTA):
SNase complex -subdomain: ATSTKKLHKEPATLIKAIDG DTVKLMYKGQPMTFRLLLVD TPETKHPKKGVEKYGPEASA FTKKMVENAKKIEVEFDKGQ RTDKYGRGLAYIYADGKMVN EALVRQGLAKVAYVYKPNNT HGSVAYVYKPNNTHEQLLRK SEAQAKKEKLNIWSED

Data sets:
Data typeCount
13C chemical shifts580
15N chemical shifts141
1H chemical shifts903

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1-subdomain1

Entities:

Entity 1, -subdomain 156 residues - 17686.604 Da.

1   ALATHRSERTHRLYSLYSLEUHISLYSGLU
2   PROALATHRLEUILELYSALAILEASPGLY
3   ASPTHRVALLYSLEUMETTYRLYSGLYGLN
4   PROMETTHRPHEARGLEULEULEUVALASP
5   THRPROGLUTHRLYSHISPROLYSLYSGLY
6   VALGLULYSTYRGLYPROGLUALASERALA
7   PHETHRLYSLYSMETVALGLUASNALALYS
8   LYSILEGLUVALGLUPHEASPLYSGLYGLN
9   ARGTHRASPLYSTYRGLYARGGLYLEUALA
10   TYRILETYRALAASPGLYLYSMETVALASN
11   GLUALALEUVALARGGLNGLYLEUALALYS
12   VALALATYRVALTYRLYSPROASNASNTHR
13   HISGLYSERVALALATYRVALTYRLYSPRO
14   ASNASNTHRHISGLUGLNLEULEUARGLYS
15   SERGLUALAGLNALALYSLYSGLULYSLEU
16   ASNILETRPSERGLUASP

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; deuterated acetate buffer 50 mM; KCl 100 mM; NaN3 0.01 (%w/v); H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 5.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 4010
PDB
DBJ BAT21500
GB AFR11891 AFR11892 AFR11893 AHG12631 AKU89572
REF WP_049881958