BMRB: 254

A Proton Nuclear Magnetic Resonance Assignment and Secondary Structure Determination of Recombinant Human Thioredoxin

Authors

Forman-Kay, J.D., Clore, G.MARIUS., Driscoll, P.C., Wingfield, P., Richards, F.M., Gronenborn, A.M.

Assembly

thioredoxin

Entity

1. thioredoxin (polymer), 104 monomers, 11576.08 Da Detail

VKQIESKTAF QEALDAAGDK LVVVDFSATW CGPCKMIKPF FHSLSEKYSN VIFLEVDVDD CQDVASECEV KCTPTFQFFK KGQKVGEFSG ANKEKLEATI NELV

Formula weight

11576.08 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 3.8 %, Completeness: 2.1 %, Completeness (bb): 2.9 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	2.1 % (13 of 631)	2.1 % (13 of 631)
Backbone	2.9 % (6 of 210)	2.9 % (6 of 210)
Sidechain	1.7 % (7 of 421)	1.7 % (7 of 421)
Aromatic	8.8 % (5 of 57)	8.8 % (5 of 57)
Methyl	0.0 % (0 of 55)	0.0 % (0 of 55)

1. thioredoxin

VKQIESKTAF QEALDAAGDK LVVVDFSATW CGPCKMIKPF FHSLSEKYSN VIFLEVDVDD CQDVASECEV KCTPTFQFFK KGQKVGEFSG ANKEKLEATI NELV

Show sample condition

Sample

Temperature 298 K, pH 5.5

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Release date

1995-07-30

Citation

A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin
Forman-Kay, J.D., Clore, G.MARIUS., Driscoll, P.C., Wingfield, P., Richards, F.M., Gronenborn, A.M.
Biochemistry (1989), 28, 7088-7097, PubMed 2684271 , DOI 10.1021/bi00443a045 , Abstract

Related entities 1. thioredoxin, : 1 : 1 : 33 : 227 entities Detail

Interaction partners 1. thioredoxin, : 70 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail