BMRB Entry 18013

Title:
Staphylococcal Nuclease PHS variant
Deposition date:
2011-10-21
Original release date:
2012-06-05
Authors:
Matzapetakis, Manolis; Pais, Tiago; Lamosa, Pedro; Turner, David; Santos, Helena
Citation:

Citation: Pais, Tiago; Lamosa, Pedro; Matzapetakis, Manolis; Turner, David; Santos, Helena. "Mannosylglycerate stabilizes staphylococcal nuclease with restriction of slow -sheet motions."  Protein Sci. 21, 1126-1137 (2012).
PubMed: 22619184

Assembly members:

Assembly members:
SNase_PHS, polymer, 149 residues, 16742.2689 Da.

Natural source:

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

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts642
15N chemical shifts159
1H chemical shifts1046

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SNase PHS1

Entities:

Entity 1, SNase PHS 149 residues - 16742.2689 Da.

1   ALATHRSERTHRLYSLYSLEUHISLYSGLU
2   PROALATHRLEUILELYSALAILEASPGLY
3   ASPTHRVALLYSLEUMETTYRLYSGLYGLN
4   PROMETTHRPHEARGLEULEULEUVALASP
5   THRPROGLUTHRLYSHISPROLYSLYSGLY
6   VALGLULYSTYRGLYPROGLUALASERALA
7   PHETHRLYSLYSMETVALGLUASNALALYS
8   LYSILEGLUVALGLUPHEASPLYSGLYGLN
9   ARGTHRASPLYSTYRGLYARGGLYLEUALA
10   TYRILETYRALAASPGLYLYSMETVALASN
11   GLUALALEUVALARGGLNGLYLEUALALYS
12   VALALATYRVALTYRLYSGLYASNASNTHR
13   HISGLUGLNLEULEUARGLYSALAGLUALA
14   GLNALALYSLYSGLULYSLEUASNILETRP
15   SERGLUASPASNALAASPSERGLYGLN

Samples:

13C15N: SNase PHS, [U-13C; U-15N], 1.0 mM

310K: ionic strength: 0.060 M; pH: 5.500; pressure: 1.000 atm; temperature: 310.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQC/HMQC13C15Nisotropic310K
3D 1H-13C NOESY13C15Nisotropic310K
2D 1H-15N HSQC/HMQC13C15Nisotropic310K
3D 1H-15N NOESY13C15Nisotropic310K
3D CBCA(CO)NH13C15Nisotropic310K
CBcgcgHD (hbCBcgcdHD)13C15Nisotropic310K
hCCH TOCSY (hC_CH.TOCSY)13C15Nisotropic310K
3D HNCACB13C15Nisotropic310K
3D HBHA(CO)NH13C15Nisotropic310K
2D 1H-1H NOESY13C15Nisotropic310K

Software:

CARA v1.8.4, Keller and Wuthrich - Assignment

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - Explicit water refinement

ANALYSIS v2.1, CCPN - data analysis, NOESY assignment

CcpNmr_Entry_Completion_Interface v2.1, PDBe & CCPN - data deposition

TOPSPIN v2.1, Bruker Biospin - Data collection and processing

UNIO v2.0, Herrmann, Guntert and Wuthrich - Structure determination

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Bruker Avance III 800 MHz

Related Database Links:

BMRB 16585 1704 17718 1874 1875 1876 1877 1878 18788 4010 4052 4053
PDB
DBJ BAB41979 BAB56977 BAB94634 BAF67032 BAF77694
EMBL CAA24594 CAG39855 CAG42530 CAI80436 CAQ49298
GB AAC14660 AAW36415 ABD22328 ABD29945 ABE02272
PRF 1109959A 710414A
REF WP_000141556 WP_000141557 WP_001548082 WP_001566557 WP_001574556
SP P00644 Q5HHM4 Q6GB41 Q6GIK1 Q7A6P2
AlphaFold P00644 Q7A6P2 Q6GIK1 Q6GB41 Q5HHM4

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