BMRB Entry 4648

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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/BMR4648
MolProbity Validation Chart

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Title:
Solution Structure and Dynamics of an Open B-sheet, Glycolytic Enzyme-monomeric 23.7 kDa Phosphoglycerate Mutase from Schizosaccharomyces pombe
Deposition date:
2000-10-04
Original release date:
2001-05-09
Authors:
Uhrinova, S.; Uhrin, D.; Nairn, J.; Price, N.; Fothergill-Gilmore, L.
Citation:

Citation: Uhrinova, S.; Uhrin, D.; Nairn, J.; Price, N.; Fothergill-Gilmore, L.. "Solution Structure and Dynamics of an Open B-sheet, Glycolytic Enzyme-monomeric 23.7 kDa Phosphoglycerate Mutase from Schizosaccharomyces pombe "  J. Mol. Biol. 306, 275-290 (2001).

Assembly members:

Assembly members:
Phosphoglycerate Mutase, polymer, 211 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Schizosaccharomyces pombe

Experimental source:

Experimental source:   Production method: .

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Phosphoglycerate Mutase: MTTEAAPNLLVLTRHGESEW NKLNLFTGWKDPALSETGIK EAKLGGERLKSRGYKFDIAF TSALQRAQKTCQIILEEVGE PNLETIKSEKLNERYYGDLQ GLNKDDARKKWGAEQVQIWR RSYDIAPPNGESLKDTAERV LPYYKSTIVPHILKGEKVLI AAHGNSLRALIMDLEGLTGD QIVKRELATGVPIVYHLDKD GKYVSKELIDN

Data sets:
Data typeCount
15N chemical shifts188
1H chemical shifts1215
13C chemical shifts615
coupling constants203

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Phosphoglycerate Mutase1

Entities:

Entity 1, Phosphoglycerate Mutase 211 residues - Formula weight is not available

1   METTHRTHRGLUALAALAPROASNLEULEU
2   VALLEUTHRARGHISGLYGLUSERGLUTRP
3   ASNLYSLEUASNLEUPHETHRGLYTRPLYS
4   ASPPROALALEUSERGLUTHRGLYILELYS
5   GLUALALYSLEUGLYGLYGLUARGLEULYS
6   SERARGGLYTYRLYSPHEASPILEALAPHE
7   THRSERALALEUGLNARGALAGLNLYSTHR
8   CYSGLNILEILELEUGLUGLUVALGLYGLU
9   PROASNLEUGLUTHRILELYSSERGLULYS
10   LEUASNGLUARGTYRTYRGLYASPLEUGLN
11   GLYLEUASNLYSASPASPALAARGLYSLYS
12   TRPGLYALAGLUGLNVALGLNILETRPARG
13   ARGSERTYRASPILEALAPROPROASNGLY
14   GLUSERLEULYSASPTHRALAGLUARGVAL
15   LEUPROTYRTYRLYSSERTHRILEVALPRO
16   HISILELEULYSGLYGLULYSVALLEUILE
17   ALAALAHISGLYASNSERLEUARGALALEU
18   ILEMETASPLEUGLUGLYLEUTHRGLYASP
19   GLNILEVALLYSARGGLULEUALATHRGLY
20   VALPROILEVALTYRHISLEUASPLYSASP
21   GLYLYSTYRVALSERLYSGLULEUILEASP
22   ASN

Samples:

sample_1: Phosphoglycerate Mutase 1 mM; sodium acetate 200 mM; ammonium sulphate 200 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 6.4; temperature: 310 K; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1not availablesample_cond_1
3D 13C-separated NOESYsample_1not availablesample_cond_1
HNHAsample_1not availablesample_cond_1

Software:

FELIX vFelix95 - processing

XEASY vXEASY(1995) - data analysis

X-PLOR v3.851 - refinement

model-free vextended model, 1995 - data analysis

NMR spectrometers:

  • Bruker DMX 800 MHz

Related Database Links:

PDB
EMBL CAA53154 CAA97363
REF NP_594889
SP P36623
AlphaFold P36623

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