BMRBj - BMREntryMaster

Found 1 Document (1.345 seconds)

BMRB: 2049

1HB6

The Secondary Structure in Solution of Acyl-Coenzyme A Binding Protein from Bovine Liver Using 1H Nuclear Magnetic Resonance Spectroscopy

Authors

Andersen, K.V., Ludvigsen, S., Mandrup, S., Knudsen, J., Poulsen, F.M.

Assembly

acyl-coenzyme A binding protein

Entity

1. acyl-coenzyme A binding protein (polymer), 86 monomers, 9913.139 Da Detail

SQAEFDKAAE EVKHLKTKPA DEEMLFIYSH YKQATVGDIN TERPGMLDFK GKAKWDAWNE LKGTSKEDAM KAYIDKVEEL KKKYGI

Formula weight

9913.139 Da

Source organism

Bos primigenius

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.8 %, Completeness: 83.1 %, Completeness (bb): 97.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	83.1 % (456 of 549)	83.1 % (456 of 549)
Backbone	97.1 % (170 of 175)	97.1 % (170 of 175)
Sidechain	76.5 % (286 of 374)	76.5 % (286 of 374)
Aromatic	97.9 % (46 of 47)	97.9 % (46 of 47)
Methyl	97.3 % (36 of 37)	97.3 % (36 of 37)

1. acyl-coenzyme A binding protein

SQAEFDKAAE EVKHLKTKPA DEEMLFIYSH YKQATVGDIN TERPGMLDFK GKAKWDAWNE LKGTSKEDAM KAYIDKVEEL KKKYGI

Show sample condition

Sample

Temperature 298 K, pH 7

Release date

1995-07-30

Citation

The secondary structure in solution of acyl-coenzyme A binding protein from bovine liver using 1H nuclear magnetic resonance spectroscopy
Andersen, K.V., Ludvigsen, S., Mandrup, S., Knudsen, J., Poulsen, F.M.
Biochemistry (1991), 30, 10654-10663, PubMed 1931985 , DOI 10.1021/bi00108a008 , Abstract

Related entities 1. acyl-coenzyme A binding protein, : 1 : 6 : 2 : 133 entities Detail

Interaction partners 1. acyl-coenzyme A binding protein, : 14 interactors Detail

More details for 14 interactors identified by 3 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr2049_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr2049_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_assignment_data_set_one	Warning	531		100.0 (chain: 1, length: 86)

Assigned chemical shifts

Saveframe: chemical_shift_assignment_data_set_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 86, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 531
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
29	SER	HG	5.011
35	THR	HG1	4.459
64	THR	HG1	5.896

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Found 1 Document (1.345 seconds)

BMRB: 2049

Sample

Related entities 1. acyl-coenzyme A binding protein, : 1 : 6 : 2 : 133 entities Detail

Interaction partners 1. acyl-coenzyme A binding protein, : 14 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail