BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 17551

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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/BMR17551
MolProbity Validation Chart

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Title: Solution structure of chicken ileal BABP in complex with glycochenodeoxycholic acid   PubMed: 21917914

Deposition date: 2011-03-28 Original release date: 2012-05-10

Authors: Zanzoni, Serena; Assfalg, Michael; Giorgetti, Alejandro; D'Onofrio, Mariapina; Molinari, Henriette

Citation: Zanzoni, Serena; Assfalg, Michael; Giorgetti, Alejandro; Molinari, Mariapina. "Structural requirements for cooperativity in ileal bile acid-binding proteins."  J. Biol. Chem. 286, 39307-39317 (2011).

Assembly members:
Protein, polymer, 127 residues, 14145.013 Da.
CHO, non-polymer, 449.623 Da.

Natural source:   Common Name: chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

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

Entity Sequences (FASTA):
Protein: AFTGKYEFESDENYDDFVKK IGLPADKIEMGRNCKIVTEV VQNGNDFTWTQHFPGGRTTT NSFTIDKEADMETMGGRKFK ATVKMEGGKIVADFPNYHHT AEISGGKLVEISTSSGVVYK RTSKKIA

Data sets:
Data typeCount
13C chemical shifts472
15N chemical shifts129
1H chemical shifts844

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1cI-BABP1
2GCDA_12
3GCDA_22

Entities:

Entity 1, cI-BABP 127 residues - 14145.013 Da.

1   ALAPHETHRGLYLYSTYRGLUPHEGLUSER
2   ASPGLUASNTYRASPASPPHEVALLYSLYS
3   ILEGLYLEUPROALAASPLYSILEGLUMET
4   GLYARGASNCYSLYSILEVALTHRGLUVAL
5   VALGLNASNGLYASNASPPHETHRTRPTHR
6   GLNHISPHEPROGLYGLYARGTHRTHRTHR
7   ASNSERPHETHRILEASPLYSGLUALAASP
8   METGLUTHRMETGLYGLYARGLYSPHELYS
9   ALATHRVALLYSMETGLUGLYGLYLYSILE
10   VALALAASPPHEPROASNTYRHISHISTHR
11   ALAGLUILESERGLYGLYLYSLEUVALGLU
12   ILESERTHRSERSERGLYVALVALTYRLYS
13   ARGTHRSERLYSLYSILEALA

Entity 2, GCDA_1 - C26 H43 N O5 - 449.623 Da.

1   CHO

Samples:

sample_3: Protein 0.4 mM; GLYCOCHENODEOXYCHOLIC ACID 1.6 mM; H2O 90%; D2O 10%; phosphate buffer 30 mM

sample_1: Protein, [U-100% 13C; U-100% 15N], 0.8 mM; GLYCOCHENODEOXYCHOLIC ACID 3.2 mM; H2O 90%; D2O 10%; phosphate buffer 30 mM

sample_2: Protein, [U-100% 13C; U-100% 15N], 0.8 mM; GLYCOCHENODEOXYCHOLIC ACID 3.2 mM; D2O 100%; phosphate buffer 30 mM

sample_conditions_1: ionic strength: 30 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_2isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 13C-edited 13C-filtered NOESYsample_2isotropicsample_conditions_1

Software:

NMRView v8.0.a.30, Johnson, One Moon Scientific - chemical shift assignment

TOPSPIN v2.1, Bruker Biospin - collection

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

HADDOCK v2.1, Bonvin - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
REF NP_001264629 NP_001264630 XP_003210329

Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone or all simulated shifts