BMRB Entry 17373

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17373

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Title:
PDZ2 from human SAP97
Deposition date:
2010-12-21
Original release date:
2011-01-14
Authors:
Chi, Celestine; Bach, Anders; Engstrom, Ake; Stromgaard, Kristian; Lundstrom, Patrik; Ferguson, Neil; Jemth, Per
Citation:

Citation: Chi, Celestine; Bach, Anders; Engstrom, Ake; Strmgaard, Kristian; Lundstrom, Patrik; Ferguson, Neil; Jemth, Per. "Biophysical Characterization of the Complex between Human Papillomavirus E6 Protein and Synapse-associated Protein 97."  J. Biol. Chem. 286, 3597-3606 (2011).
PubMed: 21113079

Assembly members:

Assembly members:
SAP97_PDZ2_polypeptide, polymer, 109 residues, 11678 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SAP97_PDZ2_polypeptide: MHHHHHLVPRGSKPVSEKIM EIKLIKGPKGLGFSIAGGVG NQHIPGDNSIYVTKIIEGGA AHKDGKLQIGDKLLAVNNVA LEEVTHEEAVTALKNTSDFV YLKVAKPTS

Data sets:
Data typeCount
13C chemical shifts277
15N chemical shifts90
1H chemical shifts90

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1pdz domain1

Entities:

Entity 1, pdz domain 109 residues - 11678 Da.

1   METHISHISHISHISHISLEUVALPROARG
2   GLYSERLYSPROVALSERGLULYSILEMET
3   GLUILELYSLEUILELYSGLYPROLYSGLY
4   LEUGLYPHESERILEALAGLYGLYVALGLY
5   ASNGLNHISILEPROGLYASPASNSERILE
6   TYRVALTHRLYSILEILEGLUGLYGLYALA
7   ALAHISLYSASPGLYLYSLEUGLNILEGLY
8   ASPLYSLEULEUALAVALASNASNVALALA
9   LEUGLUGLUVALTHRHISGLUGLUALAVAL
10   THRALALEULYSASNTHRSERASPPHEVAL
11   TYRLEULYSVALALALYSPROTHRSER

Samples:

sample_1: SAP97 PDZ2 polypeptide, [U-100% 15N], 0.7 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.9; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15209 17942
PDB
REF XP_012432549

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