BMRBj - BMREntryMaster

Found 1 Document (1.325 seconds)

BMRB: 2539

1PRA

Determination of the Nuclear Magnetic Resonance Solution Structure of the DNA-binding Domain (Residues 1 to 69) of the 434 Repressor and Comparison with the X-ray Crystal Structure

Authors

Neri, D., Billeter, M., Wuthrich, K.

Assembly

434 repressor

Entity

1. 434 repressor (polymer), 69 monomers, 7550.460 Da Detail

SISSRVKSKR IQLGLNQAEL AQKVGTTQQS IEQLENGKTK RPRFLPELAS ALGVSVDWLL NGTSDSNVR

Formula weight

7550.46 Da

Source organism

Phage 434

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 99.3 %, Completeness (bb): 99.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	99.3 % (417 of 420)	99.3 % (417 of 420)
Backbone	99.3 % (140 of 141)	99.3 % (140 of 141)
Sidechain	99.3 % (277 of 279)	99.3 % (277 of 279)
Aromatic	100.0 % (11 of 11)	100.0 % (11 of 11)
Methyl	100.0 % (42 of 42)	100.0 % (42 of 42)

1. 434 repressor

SISSRVKSKR IQLGLNQAEL AQKVGTTQQS IEQLENGKTK RPRFLPELAS ALGVSVDWLL NGTSDSNVR

Show sample condition

Sample

Temperature 286 K, pH 5

Protein Blocks Logo

Calculated from 20 models in PDB: 1PRA, Strand ID: A Detail

Release date

1995-07-30

Citation

Determination of the nuclear magnetic resonance solution structure of the DNA-binding domain (residues 1 to 69) of the 434 repressor and comparison with the X-ray crystal structure
Neri, D., Billeter, M., Wuthrich, K.
J. Mol. Biol. (1992), 223, 743-767, PubMed 1311771 , DOI: , Abstract

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr2539_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

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Found 1 Document (1.325 seconds)

BMRB: 2539

Sample

Related entities 1. 434 repressor, : 1 : 5 : 2 : 34 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail