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 17446

Title: 1H 15N 13C Backbone Assignment of Sap97 N terminal region and PDZ1 domain   PubMed: 22242544

Deposition date: 2011-02-07 Original release date: 2012-08-14

Authors: Phelan, Marie; Tully, Mark; Leyland, Mark; Lian, Lu-Yun

Citation: Tully, Mark; Grossmann, J.; Phelan, Marie; Pandelaneni, Sravan; Leyland, Mark; Lian, Lu-Yun. "Conformational characterization of synapse-associated protein 97 by nuclear magnetic resonance and small-angle X-ray scattering shows compact and elongated forms"  Biochemistry 51, 899-908 (2012).

Assembly members:
SAP97NPDZ1, polymer, 214 residues, Formula weight is not available

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

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

Entity Sequences (FASTA):
SAP97NPDZ1: SMSKQCEPVQPGNPWESGSL SSAAVTSESLPGGLSPPVEK YRYQDEEVLPSERISPQVPN EVLGPELVHVSEKSLSEIEN VHGFVSHSHISPIKANPPPV LVNTDSLETPTYVNGTDADY EYEEITLERGNSGLGFSIAG GTDNPHIGDDSSIFITKIIT GGAAAQDGRLRVNDCILRVN EADVRDVTHSKAVEALKEAG SIVRLYVKRRKPAS

Data sets:
Data typeCount
13C chemical shifts567
15N chemical shifts181
1H chemical shifts630

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SAP97NPDZ11

Entities:

Entity 1, SAP97NPDZ1 214 residues - Formula weight is not available

1   SERMETSERLYSGLNCYSGLUPROVALGLN
2   PROGLYASNPROTRPGLUSERGLYSERLEU
3   SERSERALAALAVALTHRSERGLUSERLEU
4   PROGLYGLYLEUSERPROPROVALGLULYS
5   TYRARGTYRGLNASPGLUGLUVALLEUPRO
6   SERGLUARGILESERPROGLNVALPROASN
7   GLUVALLEUGLYPROGLULEUVALHISVAL
8   SERGLULYSSERLEUSERGLUILEGLUASN
9   VALHISGLYPHEVALSERHISSERHISILE
10   SERPROILELYSALAASNPROPROPROVAL
11   LEUVALASNTHRASPSERLEUGLUTHRPRO
12   THRTYRVALASNGLYTHRASPALAASPTYR
13   GLUTYRGLUGLUILETHRLEUGLUARGGLY
14   ASNSERGLYLEUGLYPHESERILEALAGLY
15   GLYTHRASPASNPROHISILEGLYASPASP
16   SERSERILEPHEILETHRLYSILEILETHR
17   GLYGLYALAALAALAGLNASPGLYARGLEU
18   ARGVALASNASPCYSILELEUARGVALASN
19   GLUALAASPVALARGASPVALTHRHISSER
20   LYSALAVALGLUALALEULYSGLUALAGLY
21   SERILEVALARGLEUTYRVALLYSARGARG
22   LYSPROALASER

Samples:

sample_1: SAP97NPDZ1, [U-98% 13C; U-98% 15N], 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

Analysis v2.1.3, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP Q62696

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts