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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 18825

Title: Complex structure of C-terminal CFTR peptide and extended PDZ1 domain from NHERF1.   PubMed: 23583913

Authors: Bhattacharya, Shibani; Ju, Jeong; Cowburn, David; Bu, Zimei

Citation: Bhattacharya, Shibani; Ju, Jeong Ho; Orlova, Natalia; Khajeh, Jahan Ali; Cowburn, David; Bu, Zimei. "Ligand-Induced Dynamic Changes in Extended PDZ Domains from NHERF1."  J. Mol. Biol. 425, 2509-2528 (2013).

Assembly members:
PDZ1, polymer, 117 residues, 12822.731 Da.
CFTR, polymer, 5 residues, 632.693 Da.

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

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

Entity Sequences (FASTA):
PDZ1: GIDPFTMLPRLCCLEKGPNG YGFHLHGEKGKLGQYIRLVE PGSPAEKAGLLAGDRLVEVN GENVEKETHQQVVSRIRAAL NAVRLLVVDPETDEQLQKLG VQVREELLRAQEAPGQA
CFTR: QDTRL

Data sets:
Data typeCount
13C chemical shifts481
15N chemical shifts116
1H chemical shifts832

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1extended PDZ1 domain from NHERF11
2C-terminal CFTR peptide2

Entities:

Entity 1, extended PDZ1 domain from NHERF1 117 residues - 12822.731 Da.

1   GLYILEASPPROPHETHRMETLEUPROARG
2   LEUCYSCYSLEUGLULYSGLYPROASNGLY
3   TYRGLYPHEHISLEUHISGLYGLULYSGLY
4   LYSLEUGLYGLNTYRILEARGLEUVALGLU
5   PROGLYSERPROALAGLULYSALAGLYLEU
6   LEUALAGLYASPARGLEUVALGLUVALASN
7   GLYGLUASNVALGLULYSGLUTHRHISGLN
8   GLNVALVALSERARGILEARGALAALALEU
9   ASNALAVALARGLEULEUVALVALASPPRO
10   GLUTHRASPGLUGLNLEUGLNLYSLEUGLY
11   VALGLNVALARGGLUGLULEULEUARGALA
12   GLNGLUALAPROGLYGLNALA

Entity 2, C-terminal CFTR peptide 5 residues - 632.693 Da.

1   GLNASPTHRARGLEU

Samples:

sample_1: PDZ1, [U-99% 13C; U-99% 15N], 286 uM; TRIS 20 mM; sodium chloride 150 mM; DTT 0.5 mM; EDTA 0.5 mM; CFTR 275 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
4D 13C,15N NOESYsample_1isotropicsample_conditions_1
4D 13C,13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 13C,15N f1,f2-filtered NOESYsample_1isotropicsample_conditions_1
2D 13C,15N f2-filtered NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.5, Keller and Wuthrich - data analysis, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

ARIA v2.2, Linge, O, . - refinement

TALOS v1.01, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 18824
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