BMRBj - BMREntryMaster

Found 1 Document (1.226 seconds)

BMRB: 1474

1H8P

Sequence-specific 1H NMR Assignments and Structural Characterization of Bovine Seminal Fluid Protein PDC-109 Domain b

Authors

Constantine, K.L., Ramesh, V., Banyai, L., Trexler, M., Patthy, L., Llinas, M.

Assembly

bovine seminal fluid protein

Entity

1. bovine seminal fluid protein (polymer), 45 monomers, 5372.181 Da Detail

DYAKCVFPFI YGGKKYETCT KIGSMWMSWC SLSPNYDKDR AWKYC

Formula weight

5372.181 Da

Source organism

Bos primigenius

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.6 %, Completeness: 87.2 %, Completeness (bb): 90.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	87.2 % (253 of 290)	87.2 % (253 of 290)
Backbone	90.1 % (82 of 91)	90.1 % (82 of 91)
Sidechain	84.9 % (169 of 199)	84.9 % (169 of 199)
Aromatic	97.9 % (47 of 48)	97.9 % (47 of 48)
Methyl	100.0 % (12 of 12)	100.0 % (12 of 12)

1. bovine seminal fluid protein

DYAKCVFPFI YGGKKYETCT KIGSMWMSWC SLSPNYDKDR AWKYC

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Sample

Temperature 300 K, pH 6.8

Release date

1995-07-30

Citation

Sequence-specific 1H NMR Assignments and Structural Characterization of Bovine Seminal Fluid Protein PDC-109 Domain b
Constantine, K.L., Ramesh, V., Banyai, L., Trexler, M., Patthy, L., Llinas, M.
Biochemistry (1991), 30, 1663-1672, PubMed , DOI:

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr1474_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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
38	LYS	HZ1	6.98
38	LYS	HZ2	6.98
38	LYS	HZ3	6.98

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Found 1 Document (1.226 seconds)

BMRB: 1474

Sample

Related entities 1. bovine seminal fluid protein, : 1 : 2 : 206 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail