BMRB Entry 16590

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16590
MolProbity Validation Chart

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Title:
protein x
Deposition date:
2009-10-28
Original release date:
2010-05-06
Authors:
Petri, Edward; Celic, Andjelka; Kennedy, Scott; Ehrlich, Barbara; Boggon, Titus; Hodsdon, Michael
Citation:

Citation: Petri, Edward; Celic, Andjelka; Kennedy, Scott; Ehrlich, Barbara; Boggon, Titus; Hodsdon, Michael. "Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity."  Proc. Natl. Acad. Sci. U.S.A. 107, 9176-9181 (2010).
PubMed: 20439752

Assembly members:

Assembly members:
EF-hand domain of polycystin-2, polymer, 78 residues, 9009.663 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: pET-28a+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EF-hand domain of polycystin-2: NTVDDISESLRQGGGKLNFD ELRQDLKGKGHTDAEIEAIF TKYDQDGDQELTEHEHQQMR DDLEKEREDLDLDHSSLP

Data sets:
Data typeCount
13C chemical shifts157
15N chemical shifts76
1H chemical shifts461

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1EF-hand domain of polycystin-21

Entities:

Entity 1, EF-hand domain of polycystin-2 78 residues - 9009.663 Da.

1   ASNTHRVALASPASPILESERGLUSERLEU
2   ARGGLNGLYGLYGLYLYSLEUASNPHEASP
3   GLULEUARGGLNASPLEULYSGLYLYSGLY
4   HISTHRASPALAGLUILEGLUALAILEPHE
5   THRLYSTYRASPGLNASPGLYASPGLNGLU
6   LEUTHRGLUHISGLUHISGLNGLNMETARG
7   ASPASPLEUGLULYSGLUARGGLUASPLEU
8   ASPLEUASPHISSERSERLEUPRO

Samples:

sample_1: EF-hand domain of polycystin-2, [U-13C; U-15N], 1 mM; D2O 5%; sodium azide 0.05%; PMSF 10 uM; TRIS pH7.4 2 mM; sodium chloride 150 mM; Ca2+ 20 mM; D2O 95%

sample_2: EF-hand domain of polycystin-2, [U-15N], 1 mM; TRIS pH7.4 2 mM; Ca2+ 20 mM; sodium chloride 150 mM; D2O 5%; PMSF 10 uM; H2O 95%

sample_conditions_1: ionic strength: 0.150 M; pH: 7.4; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

SPARKY, Goddard - peak picking

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

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

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

PSVS, Bhattacharya and Montelione - geometry optimization

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16191 17621 18268
PDB
DBJ BAG56956 BAG57494
EMBL CAG31243 CAI38797
GB AAC16004 AAC50520 AAC50933 AAI11455 AAI12262
REF NP_000288 NP_001026311 NP_001039777 NP_001232908 XP_001099242
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