BMRB: 4639

NMR structure of the hRap1 Myb motif reveals a canonical three helix bundle lacking the positive surface charge typical of Myb DNA binding domains

Authors

Hanaoka, S., Nagadoi, A., Yoshimura, S., Aimoto, S., Li, B., de Lange, T., Nishimura, Y.

Assembly

human Rap1

Entity

1. human Rap1 (polymer, Thiol state: not present), 59 monomers, 6649.421 Da Detail

GRIAFTDADD VAILTYVKEN ARSPSSVTGN ALWKAMEKSS LTQHSWQSLK DRYLKHLRG

Formula weight

6649.421 Da

Source organism

Homo sapiens

Exptl. method

NMR

Refine. method

distance geometry simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.3 %, Completeness: 91.5 %, Completeness (bb): 95.8 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	91.5 % (325 of 355)	91.5 % (325 of 355)
Backbone	95.8 % (115 of 120)	95.8 % (115 of 120)
Sidechain	89.4 % (210 of 235)	89.4 % (210 of 235)
Aromatic	89.7 % (26 of 29)	89.7 % (26 of 29)
Methyl	84.4 % (27 of 32)	84.4 % (27 of 32)

1. TRF2-INTERACTING TELOMERIC RAP1 PROTEIN

GRIAFTDADD VAILTYVKEN ARSPSSVTGN ALWKAMEKSS LTQHSWQSLK DRYLKHLRG

Show sample condition

Sample

Pressure 1 atm, Temperature 300 K, pH 5.5

#	Name	Isotope labeling	Type	Concentration
1	TRF2-INTERACTING TELOMERIC RAP1 PROTEIN			1.0 mM
2	potassium phosphate			100 mM
3	NaN3			1.0 mM
4	H2O			90 %
5	D2O			10 %

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Protein Blocks Logo

Calculated from 25 models in PDB: 1FEX, Strand ID: A Detail

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Release date

2002-04-02

Citation

NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking the positive surface charge typical of Myb DNA-binding domains
Hanaoka, S., Nagadoi, A., Yoshimura, S., Aimoto, S., Li, B., de Lange, T., Nishimura, Y.
J. Mol. Biol. (2001), 312, 167-175, PubMed 11545594 , DOI 10.1006/jmbi.2001.4924 , Abstract

Related entities 1. human Rap1, : 1 : 3 : 4 : 19 entities Detail

Interaction partners 1. human Rap1, : 144 interactors Detail

Experiments performed 3 experiments Detail