BMRB Entry 19843

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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/BMR19843
MolProbity Validation Chart

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Title:
Solution NMR structure of the ternary complex of human ileal bile acid-binding protein with glycocholate and glycochenodeoxycholate
Deposition date:
2014-03-07
Original release date:
2014-05-05
Authors:
Horvath, Gergo; Egyed, Orsolya; Bencsura, Akos; Simon, Agnes; Tochtrop, Gregory; DeKoster, Gergory; Covey, Douglas; Cistola, David; Toke, Orsolya
Citation:

Citation: Horvath, Gergo; Egyed, Orsolya; Bencsura, Akos; Simon, Agnes; Tochtrop, Gregory; DeKoster, Gergory; Covey, Douglas; Cistola, David; Toke, Orsolya. "Solution NMR structure of the ternary complex of human ileal bile acid-binding protein with glycocholate and glycochenodeoxycholate"  Biochem. Biophys. Res. Commun. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 127 residues, 14258.153 Da.
entity_GCH, non-polymer, 465.623 Da.
entity_CHO, non-polymer, 449.623 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: pMON5840

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AFTGKFEMESEKNYDEFMKL LGISSDVIEKARNFKIVTEV QQDGQDFTWSQHYSGGHTMT NKFTVGKESNIQTMGGKTFK ATVQMEGGKLVVNFPNYHQT SEIVGDKLVEVSTIGGVTYE RVSKRLA

Data sets:
Data typeCount
13C chemical shifts541
15N chemical shifts139
1H chemical shifts884

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2GLYCOCHOLIC ACID2
3GLYCOCHENODEOXYCHOLIC ACID3

Entities:

Entity 1, entity_1 127 residues - 14258.153 Da.

1   ALAPHETHRGLYLYSPHEGLUMETGLUSER
2   GLULYSASNTYRASPGLUPHEMETLYSLEU
3   LEUGLYILESERSERASPVALILEGLULYS
4   ALAARGASNPHELYSILEVALTHRGLUVAL
5   GLNGLNASPGLYGLNASPPHETHRTRPSER
6   GLNHISTYRSERGLYGLYHISTHRMETTHR
7   ASNLYSPHETHRVALGLYLYSGLUSERASN
8   ILEGLNTHRMETGLYGLYLYSTHRPHELYS
9   ALATHRVALGLNMETGLUGLYGLYLYSLEU
10   VALVALASNPHEPROASNTYRHISGLNTHR
11   SERGLUILEVALGLYASPLYSLEUVALGLU
12   VALSERTHRILEGLYGLYVALTHRTYRGLU
13   ARGVALSERLYSARGLEUALA

Entity 2, GLYCOCHOLIC ACID - C26 H43 N O6 - 465.623 Da.

1   GCH

Entity 3, GLYCOCHENODEOXYCHOLIC ACID - C26 H43 N O5 - 449.623 Da.

1   CHO

Samples:

sample_1: human ileal bile acid-binding protein, [U-13C; U-15N], 1.0 mM; GLYCOCHOLIC ACID 1.5 mM; GLYCOCHENODEOXYCHOLIC ACID 1.5 mM; potassium phosphate 20 mM; potassium chloride 50 mM; sodium azide 0.05%

sample_2: human ileal bile acid-binding protein 1.0 mM; GLYCOCHOLIC ACID, [U-15N], 1.5 mM; GLYCOCHENODEOXYCHOLIC ACID, [U-15N], 1.5 mM; potassium phosphate 20 mM; potassium chloride 50 mM; sodium azide 0.05%

sample_3: human ileal bile acid-binding protein 1.0 mM; GLYCOCHOLIC ACID, [1',2'-13C], 1.5 mM; GLYCOCHENODEOXYCHOLIC ACID, [1',2'-13C], 1.5 mM; potassium phosphate 20 mM; potassium chloride 50 mM; sodium azide 0.05%

sample_4: human ileal bile acid-binding protein 1.0 mM; GLYCOCHOLIC ACID, [3,4-13C], 1.5 mM; GLYCOCHENODEOXYCHOLIC ACID, [3,4-13C], 1.5 mM; potassium phosphate 20 mM; potassium chloride 50 mM; sodium azide 0.05%

sample_5: human ileal bile acid-binding protein 1.0 mM; GLYCOCHOLIC ACID, [23,24-13C], 1.5 mM; GLYCOCHENODEOXYCHOLIC ACID, [23,24-13C], 1.5 mM; potassium phosphate 20 mM; potassium chloride 50 mM; sodium azide 0.05%

sample_conditions_1: ionic strength: 70 mM; pH: 6.3; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
CBCACOCAHAsample_1isotropicsample_conditions_1
HN(CO)CAsample_1isotropicsample_conditions_1
3D CC-TOCSY-NNHsample_1isotropicsample_conditions_1
3D HCC-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D CG(CB)HBsample_1isotropicsample_conditions_1
2D CG(CD)HDsample_1isotropicsample_conditions_1
2D CG(CDCE)HEsample_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 NH-NH NOESYsample_1isotropicsample_conditions_1
3D MET-MET NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 15N-edited NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 13C-edited NOESYsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_4isotropicsample_conditions_1
2D 13C-edited NOESYsample_4isotropicsample_conditions_1
2D 1H-13C HSQCsample_5isotropicsample_conditions_1
2D 13C-edited NOESYsample_5isotropicsample_conditions_1

Software:

VNMRJ, Varian - data collection

Felix, Accelrys Software Inc. - chemical shift assignment, peak picking, processing

ARIA v2.1, Linge, O'Donoghue and Nilges - refinement, structure solution

NMR spectrometers:

  • Varian Varian NMR System 600 MHz

Related Database Links:

BMRB 17220
PDB
DBJ BAI46829
EMBL CAA62415
GB AAB82751 AAH22489 ABA12611 ADQ32819 AIC54371
REF NP_001035532 NP_001124430 NP_001436 XP_001083748 XP_001083965
SP P51161
AlphaFold P51161

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