BMRB Entry 15567

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15567
MolProbity Validation Chart

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Title:
Structure of the second PDZ domain of NHERF-1
Deposition date:
2007-11-27
Original release date:
2009-05-28
Authors:
Cheng, Hong; Li, Jianquan; Dai, Zhongping; Bu, Zimei; Roder, Heinrich
Citation:

Citation: Cheng, Hong; Li, Jianquan; Ruzaliya, Fazlieva; Dai, Zhongping; Bu, Zimei; Roder, Heinrich. "Autoinhibitory interactions between the PDZ2 and C-terminal domains in the scaffolding protein NHERF-1"  Structure 17, 660-669 (2009).
PubMed: 19446522

Assembly members:

Assembly members:
PDZ2, polymer, 98 residues, 10731 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 151/D-TOPO/PDZ2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PDZ2: GIDPFTMLRPRLCTMKKGPS GYGFNLHSDKSKPGQFIRSV DPDSPAEASGLRAQDRIVEV NGVCMEGKQHGDVVSAIRAG GDETKLLVVDRETDEFFK

Data sets:
Data typeCount
13C chemical shifts340
15N chemical shifts90
1H chemical shifts569

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 98 residues - 10731 Da.

1   GLYILEASPPROPHETHRMETLEUARGPRO
2   ARGLEUCYSTHRMETLYSLYSGLYPROSER
3   GLYTYRGLYPHEASNLEUHISSERASPLYS
4   SERLYSPROGLYGLNPHEILEARGSERVAL
5   ASPPROASPSERPROALAGLUALASERGLY
6   LEUARGALAGLNASPARGILEVALGLUVAL
7   ASNGLYVALCYSMETGLUGLYLYSGLNHIS
8   GLYASPVALVALSERALAILEARGALAGLY
9   GLYASPGLUTHRLYSLEULEUVALVALASP
10   ARGGLUTHRASPGLUPHEPHELYS

Samples:

sample_1: PDZ2 1 mM; NaCl 150 mM; HEPES 20 mM; DTT 0.5 mM; D2O, [U-100% 2H], 5%; H2O 95%

sample_2: PDZ2, [U-100% 15N], 1 mM; NaCl 150 mM; HEPES 20 mM; DTT 0.5 mM; D2O, [U-100% 2H], 5%; H2O 95%

sample_3: PDZ2, [U-100% 13C; U-100% 15N], 1 mM; NaCl 150 mM; HEPES 20 mM; DTT 0.5 mM; D2O, [U-100% 2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.5; pressure: 1 atm; temperature: 288.1 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1anisotropicsample_conditions_1
2D 1H-1H NOESYsample_1anisotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HN(COCA)CBsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

FELIX v2000, Accelrys Software Inc. - chemical shift calculation, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

xwinnmr, Bruker Biospin - chemical shift calculation, collection

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

BMRB 16637 16638 18826
PDB
DBJ BAG54683
GB EAW89189 EHH58322

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