BMRBj - BMREntryMaster

Found 1 Document (1.244 seconds)

BMRB: 1120

1BDC

Sequential 1H NMR Assignments and Secondary Structure of the B Domain of Staphylococcal Protein A: Structural Changes between the Free B Domain in Solution and the Fc-Bound B Domain in Crystal

Authors

Torigoe, H., Shimada, I., Saito, A., Sato, M., Arata, Y.

Assembly

IgG Fc region-binding protein

Entity

1. IgG Fc region-binding protein (polymer), 60 monomers, 6770.353 Da Detail

TADNKFNKEQ QNAFYEILHL PNLNEEQRNG FIQSLKDDPS QSANLLAEAK KLNDAQAPKA

Formula weight

6770.353 Da

Source organism

Staphylococcus aureus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 99.7 %, Completeness (bb): 99.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	99.7 % (378 of 379)	99.7 % (378 of 379)
Backbone	99.2 % (117 of 118)	99.2 % (117 of 118)
Sidechain	100.0 % (261 of 261)	100.0 % (261 of 261)
Aromatic	100.0 % (21 of 21)	100.0 % (21 of 21)
Methyl	100.0 % (27 of 27)	100.0 % (27 of 27)

1. IgG Fc region-binding protein

TADNKFNKEQ QNAFYEILHL PNLNEEQRNG FIQSLKDDPS QSANLLAEAK KLNDAQAPKA

Show sample condition

Sample

Temperature 303 K, pH 5

Release date

1995-07-30

Citation

Sequential 1H NMR Assignments and Secondary Structure of the B Domain of Staphylococcal Protein A: Structural Changes between the Free B Domain in Solution and the Fc-Bound B Domain in Crystal
Torigoe, H., Shimada, I., Saito, A., Sato, M., Arata, Y.
Biochemistry (1990), 29, 8787-8793, DOI 10.1021/bi00489a040

Related entities 1. IgG Fc region-binding protein, : 1 : 1 : 1 : 101 : 73 entities Detail

Interaction partners 1. IgG Fc region-binding protein, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr1120_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: bmr1120_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_assignment_data_set_one	Warning	432		100.0 (chain: 1, length: 60)

Assigned chemical shifts

Saveframe: chemical_shift_assignment_data_set_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 60, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 432
- 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)
59	LYS	HZ1	7.47
59	LYS	HZ2	7.47
59	LYS	HZ3	7.47

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Found 1 Document (1.244 seconds)

BMRB: 1120

Sample

Related entities 1. IgG Fc region-binding protein, : 1 : 1 : 1 : 101 : 73 entities Detail

Interaction partners 1. IgG Fc region-binding protein, : 1 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail