BMRB: 532

1H NMR Studies on Bovine Cyclophilin: Preliminary Structural Characterization of Its Complex with Cyclosporin A

Authors

Heald, S.L., Harding, M.W., Handschumacher, R.E., Armitage, I.M.

Assembly

peptidylprolyl isomerase

Entity

1. peptidylprolyl isomerase (polymer), 163 monomers, 17737.95 Da Detail

VNPTVFFDIA VDGEPLGRVS FELFADKVPK TAENFRALST GEKGFGYKGS CFHRIIPGFM CQGGDFTRHN GTGGKSIYGE KFDDENFILK HTGPGILSMA NAGPNTNGSQ FFICTAKTEW LDGKHVVFGK VKEGMNIVEA MERFGSRNGK TSKKITIADC GQI

Formula weight

17737.95 Da

Source organism

Bos primigenius

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 1.8 %, Completeness: 1.5 %, Completeness (bb): 1.2 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	1.5 % (15 of 971)	1.5 % (15 of 971)
Backbone	1.2 % (4 of 343)	1.2 % (4 of 343)
Sidechain	1.8 % (11 of 628)	1.8 % (11 of 628)
Aromatic	8.2 % (8 of 97)	8.2 % (8 of 97)
Methyl	1.4 % (1 of 72)	1.4 % (1 of 72)

1. peptidylprolyl isomerase

VNPTVFFDIA VDGEPLGRVS FELFADKVPK TAENFRALST GEKGFGYKGS CFHRIIPGFM CQGGDFTRHN GTGGKSIYGE KFDDENFILK HTGPGILSMA NAGPNTNGSQ FFICTAKTEW LDGKHVVFGK VKEGMNIVEA MERFGSRNGK TSKKITIADC GQI

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Sample

Temperature 298 K, pH 6.8

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Release date

1995-07-30

Citation

1H NMR studies on bovine cyclophilin: preliminary structural characterization of its complex with cyclosporin A
Heald, S.L., Harding, M.W., Handschumacher, R.E., Armitage, I.M.
Biochemistry (1990), 29, 4466-4478, PubMed 2190633 , DOI: , Abstract

Related entities 1. peptidylprolyl isomerase, : 1 : 1 : 109 : 197 entities Detail

Interaction partners 1. peptidylprolyl isomerase, : 83 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail