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Biological Magnetic Resonance Data Bank


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BMRB Entry 16585

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16585
MolProbity Validation Chart

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Title: Solution structure of SNase140   PubMed: 20415411

Deposition date: 2009-10-26 Original release date: 2010-05-19

Authors: Wang, Min; Feng, Yingang; Yao, Hongwei; Wang, Jinfeng

Citation: Wang, Min; Feng, Yingang; Yao, Hongwei; Wang, Jinfeng. "Importance of the C-terminal loop l137-s141 for the folding and folding stability of staphylococcal nuclease"  Biochemistry 49, 4318-4326 (2010).

Assembly members:
SNase140, polymer, 140 residues, 15914.683 Da.

Natural source:   Common Name: Staphylococcus aureus   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):
SNase140: ATSTKKLHKEPATLIKAIDG DTVKLMYKGQPMTFRLLLVD TPETKHPKKGVEKYGPEASA FTKKMVENAKKIEVEFDKGQ RTDKYGRGLAYIYADGKMVN EALVRQGLAKVAYVYKPNNT HEQLLRKSEAQAKKEKLNIW

Data sets:
Data typeCount
13C chemical shifts579
15N chemical shifts135
1H chemical shifts964

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SNase1401

Entities:

Entity 1, SNase140 140 residues - 15914.683 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   HISGLUGLNLEULEUARGLYSSERGLUALA
14   GLNALALYSLYSGLULYSLEUASNILETRP

Samples:

sample_1: sodium acetate, [U-2H], 50 mM; potassium chloride 250 mM; EDTA 1 mM; sodium azide 0.02%; DSS 0.2 mM; H20 90%; D20 10%

sample_conditions_1: ionic strength: 250 mM; pH: 5.0; pressure: 1.0 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

FELIX, Accelrys Software Inc. - chemical shift assignment, data analysis, peak picking, processing

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

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

BMRB 136 1581 1582 1704 17718 18013 1874 1875 1876 1877 1878 18788 188 189 2784 2785 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

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