Start2Fold

The database of hydrogen/deuterium exchange data on protein folding and stability

Entry STF0001

Bovine acyl-coenzyme A binding protein (ACBP)

 DOWNLOAD ENTRY IN XML

Protein information

Name of the protein: Acyl-CoA-binding protein
Organism: Bos taurus (Bovine)
Number of residues: 86
Related UniProt entry:   P07107 (Fragment: 2 - 87)
Related PDB entry:   2ABD

Visualize the data

 Click here or on the image on the right to visualize the residues using JSmol. Warning: JSmol is known to load slowly on certain browsers, depending on the size of the macromolecule. The applet is optimized for Chrome, other browsers have limited support.

Experiment sets

 Show  Hide

EARLY

Method: Quenched-flow HDX NMR

Conditions: pH 5.3; 5.0 Celsius; Probes: 82

Related publication:
 PMID 10966822

Experiment details: "The time dependence of hydrogen exchange protection in the refolding of ACBP has been followed in 20 mM sodium acetate, 0.54 M GuHCl at pH 5.3 and 278 K. A total of 17 samples were prepared for a set of refolding times ranging from 0 ms to 250 ms."

Protection threshold: protection rate (s-1) ~20±5

Sequence: SQAEFDKAAEEVKHLKTKPADEEMLFIYSHYKQATVGDINTERPGMLDFKGKAKWDAWNELKGTSKEDAMKAYIDKVEELKKKYGI
 CLICK TO DOWNLOAD SEQUENCE IN FASTA

EARLY residues

8: A; 9: A; 10: E; 11: E; 12: V; 28: Y; 29: S; 31: Y; 32: K; 34: A; 35: T; 36: V; 37: G; 39: I; 55: W; 56: D; 57: A; 58: W; 59: N; 60: E; 61: L; 62: K; 64: T; 69: A; 70: M; 71: K; 72: A; 73: Y; 74: I; 75: D; 76: K; 77: V; 78: E; 79: E; 80: L; 81: K; 82: K; 83: K; 84: Y;
 CLICK TO DOWNLOAD LIST OF RESIDUES

 Show  Hide

EARLY

Method: Quenched-flow HDX NMR

Conditions: pH 5.3; 5.0 Celsius; Probes: 82

Related publication:
 PMID 10966822

Experiment details: "The time dependence of hydrogen exchange protection in the refolding of ACBP has been followed in 20 mM sodium acetate, 0.54 M GuHCl at pH 5.3 and 278 K. A total of 17 samples were prepared for a set of refolding times ranging from 0 ms to 250 ms."

Protection threshold: Burst phase amplitude > 0.30

Sequence: SQAEFDKAAEEVKHLKTKPADEEMLFIYSHYKQATVGDINTERPGMLDFKGKAKWDAWNELKGTSKEDAMKAYIDKVEELKKKYGI
 CLICK TO DOWNLOAD SEQUENCE IN FASTA

EARLY residues

9: A; 11: E; 12: V; 61: L; 62: K; 71: K; 74: I; 75: D; 77: V; 81: K; 83: K;
 CLICK TO DOWNLOAD LIST OF RESIDUES

 Show  Hide

INTERMEDIATE

Method: Quenched-flow HDX NMR

Conditions: pH 5.3; 5.0 Celsius; Probes: 82

Related publication:
 PMID 10966822

Experiment details: "The time dependence of hydrogen exchange protection in the refolding of ACBP has been followed in 20 mM sodium acetate, 0.54 M GuHCl at pH 5.3 and 278 K. A total of 17 samples were prepared for a set of refolding times ranging from 0 ms to 250 ms."

Protection threshold: 0.20 < Burst phase amplitude < 0.30

Sequence: SQAEFDKAAEEVKHLKTKPADEEMLFIYSHYKQATVGDINTERPGMLDFKGKAKWDAWNELKGTSKEDAMKAYIDKVEELKKKYGI
 CLICK TO DOWNLOAD SEQUENCE IN FASTA

INTERMEDIATE residues

8: A; 10: E; 36: V; 57: A; 73: Y; 76: K; 78: E; 79: E; 80: L; 82: K;
 CLICK TO DOWNLOAD LIST OF RESIDUES

 Show  Hide

LATE

Method: Quenched-flow HDX NMR

Conditions: pH 5.3; 5.0 Celsius; Probes: 82

Related publication:
 PMID 10966822

Experiment details: "The time dependence of hydrogen exchange protection in the refolding of ACBP has been followed in 20 mM sodium acetate, 0.54 M GuHCl at pH 5.3 and 278 K. A total of 17 samples were prepared for a set of refolding times ranging from 0 ms to 250 ms."

Protection threshold: 0.10 < Burst phase amplitude < 0.20

Sequence: SQAEFDKAAEEVKHLKTKPADEEMLFIYSHYKQATVGDINTERPGMLDFKGKAKWDAWNELKGTSKEDAMKAYIDKVEELKKKYGI
 CLICK TO DOWNLOAD SEQUENCE IN FASTA

LATE residues

28: Y; 32: K; 34: A; 35: T; 37: G; 55: W; 58: W; 60: E; 70: M; 84: Y;
 CLICK TO DOWNLOAD LIST OF RESIDUES

 Show  Hide

STRONG

Method: Native exchange NMR

Conditions: pH 6.65; 25.0 Celsius; Probes: 43

Related publication:
 PMID 7623386

Experiment details: "Amide hydrogen exchange with solvent deuterium was performed in deuterium oxide at pH 6.65. A sample of 2 mM free ACBP in H2O was adjusted to the desired pH and lyophilized repeatedly. After a final lyophilization the protein was dissolved in 600 ml 99.99% D2O and transferred to a precooled NMR tube. The protein-ligand sample was dissolved in 600 ml of D2O and 0.04 M potassium phosphate (pH 6.65) to concentrations of 2 mM. Potassium phosphate was deuterated by repeated lyophilization from D2O, redissolved in 99.99% D2O and quickly transferred to the lyophilized protein-ligand complex. After transfer to a precooled NMR tube the sample was immediately placed in the spectrometer which in advance had been tuned and calibrated on a similar sample."

Protection threshold: log(P) > 4

Sequence: SQAEFDKAAEEVKHLKTKPADEEMLFIYSHYKQATVGDINTERPGMLDFKGKAKWDAWNELKGTSKEDAMKAYIDKVEELKKKYGI
 CLICK TO DOWNLOAD SEQUENCE IN FASTA

STRONG residues

29: S; 30: H; 31: Y; 32: K; 34: A; 35: T; 37: G; 39: I; 56: D; 57: A; 58: W; 59: N; 60: E; 61: L; 62: K; 64: T; 70: M; 72: A; 73: Y; 74: I; 76: K; 77: V; 78: E; 79: E; 80: L; 81: K; 82: K; 83: K;
 CLICK TO DOWNLOAD LIST OF RESIDUES

 Show  Hide

MEDIUM

Method: Native exchange NMR

Conditions: pH 6.65; 25.0 Celsius; Probes: 43

Related publication:
 PMID 7623386

Experiment details: "Amide hydrogen exchange with solvent deuterium was performed in deuterium oxide at pH 6.65. A sample of 2 mM free ACBP in H2O was adjusted to the desired pH and lyophilized repeatedly. After a final lyophilization the protein was dissolved in 600 ml 99.99% D2O and transferred to a precooled NMR tube. The protein-ligand sample was dissolved in 600 ml of D2O and 0.04 M potassium phosphate (pH 6.65) to concentrations of 2 mM. Potassium phosphate was deuterated by repeated lyophilization from D2O, redissolved in 99.99% D2O and quickly transferred to the lyophilized protein-ligand complex. After transfer to a precooled NMR tube the sample was immediately placed in the spectrometer which in advance had been tuned and calibrated on a similar sample."

Protection threshold: 2 < log(P) < 4

Sequence: SQAEFDKAAEEVKHLKTKPADEEMLFIYSHYKQATVGDINTERPGMLDFKGKAKWDAWNELKGTSKEDAMKAYIDKVEELKKKYGI
 CLICK TO DOWNLOAD SEQUENCE IN FASTA

MEDIUM residues

8: A; 9: A; 10: E; 11: E; 12: V; 13: K; 24: M; 38: D; 55: W; 63: G; 84: Y; 85: G;
 CLICK TO DOWNLOAD LIST OF RESIDUES