BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16520

Title: Solution structure of humar Par-3b PDZ2 (residues 451-549)   PubMed: 20073081

Authors: Volkman, B.; Tyler, R.; Peterson, F.

Citation: Jensen, Davin; Woytovich, Christopher; Li, Margie; Duvnjak, Petar; Cassidy, Michael; Frederick, Ronnie; Bergeman, Lai; Peterson, Francis; Volkman, Brian. "Rapid, robotic, small-scale protein production for NMR screening and structure determination."  Protein Sci. 19, 570-578 (2010).

Assembly members:
hPar-3_PDZ2, polymer, 121 residues, 13394.356 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo Sapiens

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

Entity Sequences (FASTA):
hPar-3_PDZ2: MRGSHHHHHHHHGSENLYFQ GSYNTKKIGKRLNIQLKKGT EGLGFSITSRDVTIGGSAPI YVKNILPRGAAIQDGRLKAG DRLIEVNGVDLVGKSQEEVV SLLRSTKMEGTVSLLVFRQE D

Data sets:
Data typeCount
13C chemical shifts393
15N chemical shifts99
1H chemical shifts616

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hPar3 PDZ21

Entities:

Entity 1, hPar3 PDZ2 121 residues - 13394.356 Da.

Residues 429-450 (MRGSHHHHHHHHGSENLYFQGS) are a octa-His tag that was not removed from the protein prior to structure determination.

1   METARGGLYSERHISHISHISHISHISHIS
2   HISHISGLYSERGLUASNLEUTYRPHEGLN
3   GLYSERTYRASNTHRLYSLYSILEGLYLYS
4   ARGLEUASNILEGLNLEULYSLYSGLYTHR
5   GLUGLYLEUGLYPHESERILETHRSERARG
6   ASPVALTHRILEGLYGLYSERALAPROILE
7   TYRVALLYSASNILELEUPROARGGLYALA
8   ALAILEGLNASPGLYARGLEULYSALAGLY
9   ASPARGLEUILEGLUVALASNGLYVALASP
10   LEUVALGLYLYSSERGLNGLUGLUVALVAL
11   SERLEULEUARGSERTHRLYSMETGLUGLY
12   THRVALSERLEULEUVALPHEARGGLNGLU
13   ASP

Samples:

sample_1: hPar-3 PDZ2, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%; sodium azide 0.02%

sample_conditions_1: ionic strength: 53 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESY (AROMATIC)sample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement

TOPSPIN v2.1, Bruker - collection

NMRPipe v2007, Delagio,F. et al. - processing

XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis

GARANT v2.1, C. Bartels - data analysis

CYANA v2.1, Guntert, P. - structural calculation

NMR spectrometers:

  • Bruker Avance III 500 MHz

Related Database Links:

BMRB 16515
PDB
GB EPQ12192
REF XP_011836158