BMRB Entry 17398

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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/BMR17398
MolProbity Validation Chart

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Title:
A protein from yeast
Deposition date:
2011-01-07
Original release date:
2011-12-20
Authors:
Qiu, Yu; Zhang, Jiahai; Zhang, Wen
Citation:

Citation: Qiu, Yu; Zhang, Wen; Zhao, Chen; Wang, Yan; Wang, Weiwei; Zhang, Jiahai; Zhang, Zhiyong; Li, Guohong; Shi, Yunyu; Tu, Xiaoming; Wu, Jihui. "Solution structure of the Pdp1 PWWP domain reveals its unique binding sites for methylated H4K20 and DNA."  Biochem. J. 442, 527-538 (2012).
PubMed: 22150589

Assembly members:

Assembly members:
A protein from fission yeast, polymer, 216 residues, 24872.488 Da.

Natural source:

Natural source:   Common Name: fission yeast   Taxonomy ID: 4896   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Schizosaccharomyces pombe

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
A protein from fission yeast: SADDRLNFGDRILVKAPGYP WWPALLLRRKETKDSLNTNS SFNVLYKVLFFPDFNFAWVK RNSVKPLLDSEIAKFLGSSK RKSKELIEAYEASKTPPDLK EESSTDLESADDRLNFGDRI LVKAPGYPWWPALLLRRKET KDSLNTNSSFNVLYKVLFFP DFNFAWVKRNSVKPLLDSEI AKFLGSSKRKSKELIEAYEA SKTPPDLKEESSTDLE

Data sets:
Data typeCount
13C chemical shifts379
15N chemical shifts105
1H chemical shifts661

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1A protein from fission yeast1

Entities:

Entity 1, A protein from fission yeast 216 residues - 24872.488 Da.

1   SERALAASPASPARGLEUASNPHEGLYASP
2   ARGILELEUVALLYSALAPROGLYTYRPRO
3   TRPTRPPROALALEULEULEUARGARGLYS
4   GLUTHRLYSASPSERLEUASNTHRASNSER
5   SERPHEASNVALLEUTYRLYSVALLEUPHE
6   PHEPROASPPHEASNPHEALATRPVALLYS
7   ARGASNSERVALLYSPROLEULEUASPSER
8   GLUILEALALYSPHELEUGLYSERSERLYS
9   ARGLYSSERLYSGLULEUILEGLUALATYR
10   GLUALASERLYSTHRPROPROASPLEULYS
11   GLUGLUSERSERTHRASPLEUGLUSERALA
12   ASPASPARGLEUASNPHEGLYASPARGILE
13   LEUVALLYSALAPROGLYTYRPROTRPTRP
14   PROALALEULEULEUARGARGLYSGLUTHR
15   LYSASPSERLEUASNTHRASNSERSERPHE
16   ASNVALLEUTYRLYSVALLEUPHEPHEPRO
17   ASPPHEASNPHEALATRPVALLYSARGASN
18   SERVALLYSPROLEULEUASPSERGLUILE
19   ALALYSPHELEUGLYSERSERLYSARGLYS
20   SERLYSGLULEUILEGLUALATYRGLUALA
21   SERLYSTHRPROPROASPLEULYSGLUGLU
22   SERSERTHRASPLEUGLU

Samples:

sample_1: a protein from fission yeast 0.6 mM; sodium phosphate 20 mM; sodium chloride 100 mM; EDTA 2 mM; H2O 90%; D2O 10%

sample_2: a protein from fission yeast 0.6 mM; sodium phosphate 20 mM; sodium chloride 100 mM; EDTA 2 mM; D2O 100%

sample_conditions_1: ionic strength: 0.140 M; pH: 4.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB

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