Entry STF0001
Bovine acyl-coenzyme A binding protein (ACBP)
Protein information
| Name of the protein: | Acyl-CoA-binding protein |
| Organism: | Bos taurus |
| Number of residues: | 86 |
| Related UniProt entry: | P07107 (Fragment: 2 - 87) |
| Related PDB entry: | 2ABD |
Visualize the data
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Experiment sets
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
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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;
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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;
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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;
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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;
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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;
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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;
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