BMRB Entry 16320

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16320
MolProbity Validation Chart

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Title:
Solution structure of an archaeal protein SSO6904 from hyperthermophilic Sulfolobus solfataricus
Deposition date:
2009-05-28
Original release date:
2009-10-14
Authors:
Feng, Yingang; Yao, Hongwei; Wang, Jinfeng
Citation:

Citation: Feng, Yingang; Yao, Hongwei; Wang, Jinfeng. "Solution structure and calcium binding of protein SSO6904 from the hyperthermophilic archaeon Sulfolobus solfataricus."  Proteins 78, 474-479 (2010).
PubMed: 19768683

Assembly members:

Assembly members:
SSO6904, polymer, 99 residues, 11913.870 Da.

Natural source:

Natural source:   Common Name: Sulfolobus solfataricus   Taxonomy ID: 2287   Superkingdom: Archaea   Kingdom: not available   Genus/species: Sulfolobus solfataricus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SSO6904: MSILEDPEFVKLRQFKGKVN FNLVMQILDEIELDLRGSDN IKTSIIYVYSSHLDEIRKNK EFYDMIAEILQRYYKKIGIE NVNQLILTTIKLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts433
15N chemical shifts96
1H chemical shifts703

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1SSO69041

Entities:

Entity 1, SSO6904 99 residues - 11913.870 Da.

1   METSERILELEUGLUASPPROGLUPHEVAL
2   LYSLEUARGGLNPHELYSGLYLYSVALASN
3   PHEASNLEUVALMETGLNILELEUASPGLU
4   ILEGLULEUASPLEUARGGLYSERASPASN
5   ILELYSTHRSERILEILETYRVALTYRSER
6   SERHISLEUASPGLUILEARGLYSASNLYS
7   GLUPHETYRASPMETILEALAGLUILELEU
8   GLNARGTYRTYRLYSLYSILEGLYILEGLU
9   ASNVALASNGLNLEUILELEUTHRTHRILE
10   LYSLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: SS6904, [U-13C; U-15N], 1 – 1.5 mM; potassium phosphate 50 mM; potassium chloride 100 mM; D2O, [U-99.8% 2H], 10%; DSS 0.02 % w/v; sodium azide 0.02 % w/v; arginine 50 mM; glutamic acid 50 mM; H2O 90%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.2; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESY-HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY-HSQCsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
GB AAK41251 ACX92167 AKA75098 AKA77791 AKA80485
REF WP_009992428

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