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 15340

Title: 1H, 13C, and 15N Backbone Assignments and 13C Aliphatic Sidechain Assignments for PKA Phosphorylated CFTR Regulatory Region   PubMed: 17660831

Authors: Baker, Jennifer; Hudson, Rhea; Kanelis, Voula; Choy, Wing-Yiu; Thibodeau, Patrick; Thomas, Philip; Forman-Kay, Julie

Citation: Baker, Jennifer; Hudson, Rhea; Kanelis, Voula; Choy, Wing-Yiu; Thibodeau, Patrick; Thomas, Philip; Forman-Kay, Julie. "CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices."  Nat. Struct. Mol. Biol. 14, 738-745 (2007).

Assembly members:
Phosphorylated_CFTR_Regulatory_Region, polymer, 189 residues, Formula weight is not available

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):
Phosphorylated_CFTR_Regulatory_Region: GAMESAERRNSILTETLHRF SLEGDAPVSWTETKKQSFKQ TGEFGEKRKNSILNPINSIR KFSIVQKTPLQMNGIEEDSD EPLERRLSLVPDSEQGEAIL PRISVISTGPTLQARRRQSV LNLMTHSVNQGQNIHRKTTA STRKVSLAPQANLTELDIYS RRLSQETGLEISEEINEEDL KECLFDDME

Data sets:
Data typeCount
13C chemical shifts755
15N chemical shifts180
1H chemical shifts180

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1regulatory region1

Entities:

Entity 1, regulatory region 189 residues - Formula weight is not available

The first four residues are derived from the vector. The remaining residues are from human CFTR with the polymorphism L833. Shifts are reported for the major component of the sample phosphorylated at S660, S670, S700, S712, S737, S753, S768, S795, and S813.

1   GLYALAMETGLUSERALAGLUARGARGASN
2   SERILELEUTHRGLUTHRLEUHISARGPHE
3   SERLEUGLUGLYASPALAPROVALSERTRP
4   THRGLUTHRLYSLYSGLNSERPHELYSGLN
5   THRGLYGLUPHEGLYGLULYSARGLYSASN
6   SERILELEUASNPROILEASNSERILEARG
7   LYSPHESERILEVALGLNLYSTHRPROLEU
8   GLNMETASNGLYILEGLUGLUASPSERASP
9   GLUPROLEUGLUARGARGLEUSERLEUVAL
10   PROASPSERGLUGLNGLYGLUALAILELEU
11   PROARGILESERVALILESERTHRGLYPRO
12   THRLEUGLNALAARGARGARGGLNSERVAL
13   LEUASNLEUMETTHRHISSERVALASNGLN
14   GLYGLNASNILEHISARGLYSTHRTHRALA
15   SERTHRARGLYSVALSERLEUALAPROGLN
16   ALAASNLEUTHRGLULEUASPILETYRSER
17   ARGARGLEUSERGLNGLUTHRGLYLEUGLU
18   ILESERGLUGLUILEASNGLUGLUASPLEU
19   LYSGLUCYSLEUPHEASPASPMETGLU

Samples:

sample_1: Phosphorylated CFTR Regulatory Region, [U-98% 13C; U-98% 15N], 0.25 mM; potassium chloride 125 mM; potassium phosphate 125 mM; DSS 2 mM; DTT 5 mM; EDTA 5 mM; benzamidine 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.25 M; pH: 6.8; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CCC-TOCSY-NNHsample_1isotropicsample_conditions_1

Software:

NMRView, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific - chemical shift assignment, processing

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

BMRB 15336
EMBL CAE00701 CAE00702 CAE00703 CAE00704
GB AAA35680 AAB46352 AAC13657 AAC14011 AAC14012
REF NP_000483 NP_001028110 NP_001073386 NP_001106085 XP_003808695
SP P13569 Q00553 Q2IBF6 Q2QLE5 Q7JII7