BMRB Entry 15415

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15415
MolProbity Validation Chart

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Title:
Solution structure of Sso6901 from Sulfolobus solfataricus P2
Deposition date:
2007-08-03
Original release date:
2008-10-29
Authors:
Feng, Yingang; Guo, Li; Huang, Li; Wang, Jinfeng
Citation:

Citation: Guo, Li; Feng, Yingang; Zhang, Zhenfeng; Yao, Hongwei; Luo, Yuanming; Wang, Jinfeng; Huang, Li. "Biochemical and structural characterization of Cren7, a novel chromatin protein conserved among Crenarchaea"  Nucleic Acids Res. 36, 1129-1137 (2008).
PubMed: 18096617

Assembly members:

Assembly members:
Cren7, polymer, 60 residues, 6685.043 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):
Cren7: MSSGKKPVKVKTPAGKEAEL VPEKVWALAPKGRKGVKIGL FKDPETGKYFRHKLPDDYPI

Data sets:
Data typeCount
13C chemical shifts279
15N chemical shifts51
1H chemical shifts434

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Cren71

Entities:

Entity 1, Cren7 60 residues - 6685.043 Da.

1   METSERSERGLYLYSLYSPROVALLYSVAL
2   LYSTHRPROALAGLYLYSGLUALAGLULEU
3   VALPROGLULYSVALTRPALALEUALAPRO
4   LYSGLYARGLYSGLYVALLYSILEGLYLEU
5   PHELYSASPPROGLUTHRGLYLYSTYRPHE
6   ARGHISLYSLEUPROASPASPTYRPROILE

Samples:

sample_1H: entity1.0 – 2.0 mM; DSS 0.01%; potassium phosphate 50 mM

sample_15N13C: entity, [U-13C; U-15N], 1.0 – 2.0 mM; DSS 0.01%; potassium phosphate 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.0; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1Hisotropicsample_conditions_1
2D DQF-COSYsample_1Hisotropicsample_conditions_1
2D 1H-1H NOESYsample_1Hisotropicsample_conditions_1
2D 1H-15N HSQCsample_15N13Cisotropicsample_conditions_1
2D 1H-13C HSQCsample_15N13Cisotropicsample_conditions_1
3D CBCA(CO)NHsample_15N13Cisotropicsample_conditions_1
3D HNCACBsample_15N13Cisotropicsample_conditions_1
3D HBHA(CO)NHsample_15N13Cisotropicsample_conditions_1
3D HNCOsample_15N13Cisotropicsample_conditions_1
3D HN(CA)COsample_15N13Cisotropicsample_conditions_1
3D 1H-15N TOCSYsample_15N13Cisotropicsample_conditions_1
3D HCCH-COSYsample_15N13Cisotropicsample_conditions_1
3D CCH-TOCSYsample_15N13Cisotropicsample_conditions_1
3D 1H-15N NOESYsample_15N13Cisotropicsample_conditions_1
3D 1H-13C NOESYsample_15N13Cisotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

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

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

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
GB AAK41249 ACP35343 ACP38003 ACP45499 ACP48703
REF WP_009992425 WP_012711256
SP C3MPN0 C3MYM4 C3N5A6 C3NDW0 C3NHU3
AlphaFold C3MPN0 C3MYM4 C3N5A6 C3NDW0 C3NHU3

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