BMRB Entry 16191

Title:
NMR-Assignments of a Cytosolic Domain of the C-Terminus of Polycystin-2
Deposition date:
2009-03-02
Original release date:
2009-04-16
Authors:
Kalbitzer, Hans Robert
Citation:

Citation: Schumann, Frank; Hoffmeister, Helen; Schmidt, Maren; Bader, Reto; Besl, Elisabeth; Witzgall, Ralph; Kalbitzer, Hans Robert. "NMR-assignments of a cytosolic domain of the C-terminus of polycystin-2"  Biomol. NMR Assignments 3, 141-144 (2009).
PubMed: 19636966

Assembly members:

Assembly members:
Polycystin-2_Polypeptide, polymer, 123 residues, Formula weight is not available
CA, non-polymer, 40.078 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: pET41a

Data sets:
Data typeCount
13C chemical shifts348
15N chemical shifts100
1H chemical shifts569

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Polycystin-2 Polypeptide1
2Calcium2

Entities:

Entity 1, Polycystin-2 Polypeptide 123 residues - Formula weight is not available

1   GLYSERTHRALAILEGLYILEASNASPTHR
2   TYRSERGLUVALLYSSERASPLEUALAGLN
3   GLNLYSALAGLUMETGLULEUSERASPLEU
4   ILEARGLYSGLYTYRHISLYSALALEUVAL
5   LYSLEULYSLEULYSLYSASNTHRVALASP
6   ASPILESERGLUSERLEUARGGLNGLYGLY
7   GLYLYSLEUASNPHEASPGLULEUARGGLN
8   ASPLEULYSGLYLYSGLYHISTHRASPALA
9   GLUILEGLUALAILEPHETHRLYSTYRASP
10   GLNASPGLYASPGLNGLULEUTHRGLUHIS
11   GLUHISGLNGLNMETARGASPASPLEUGLU
12   LYSGLUARGGLUASPLEUASPLEUASPHIS
13   SERSERLEU

Entity 2, Calcium - Ca - 40.078 Da.

1   CA

Samples:

sample_1: Polycystin-2 Polypeptide, [U-100% 13C; U-100% 15N], 0.5 mM; Ca2 5 mM; DSS 0.1 mM; potassium phosphate buffer 10 mM; NaCl 500 mM; DTE 2 mM; H20 90%; D20 10%

sample_conditions_1: ionic strength: 0.51 M; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCANNHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 15N-TOCSY-HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N-NOESY-HSQCsample_1isotropicsample_conditions_1

Software:

AUREMOL, Bruker Biospin - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16590 17621 18268
PDB
DBJ BAG56956 BAG57494
EMBL CAI38797
GB AAC16004 AAC50520 AAC50933 AAI11455 AAI12262
REF NP_000288 NP_001039777 NP_001232908 XP_001099242 XP_002717056
SP Q13563 Q4GZT3
TPG DAA28806
AlphaFold Q13563 Q4GZT3

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