BMRB: 5551

Homonuclear chemical shift assignment for LEKTI domain 6 (HF7665)

Authors

Lauber, T., Roesch, P., Marx, U.C.

Assembly

LEKTI domain 6 (HF7665) monomer

Entity

1. LEKTI domain 6 (HF7665) monomer (polymer, Thiol state: all disulfide bound), 68 monomers, 7669.426 Da Detail

ESGKATSYAE LCNEYRKLVR NGKLACTREN DPIQGPDGKV HGNTCSMCEV FFQAEEEEKK KKEGESRN

Formula weight

7669.426 Da

Entity Connection

disulfide 2 Detail

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ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS12:SG	1:CYS48:SG
2	disulfide	sing	1:CYS26:SG	1:CYS45:SG

Source organism

Homo sapiens

Exptl. method

NMR

Refine. method

SIMULATED ANNEALING

Data set

assigned_chemical_shifts, coupling_constants

Chem. Shift Complete

Sequence coverage: 98.5 %, Completeness: 96.9 %, Completeness (bb): 96.4 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	96.9 % (401 of 414)	96.9 % (401 of 414)
Backbone	96.4 % (135 of 140)	96.4 % (135 of 140)
Sidechain	97.1 % (266 of 274)	97.1 % (266 of 274)
Aromatic	100.0 % (20 of 20)	100.0 % (20 of 20)
Methyl	95.2 % (20 of 21)	95.2 % (20 of 21)

1. LEKTI domain 6

ESGKATSYAE LCNEYRKLVR NGKLACTREN DPIQGPDGKV HGNTCSMCEV FFQAEEEEKK KKEGESRN

Show sample condition

Sample

Temperature 298 (±1) K, pH 4.0 (±0.2)

#	Name	Isotope labeling	Type	Concentration
1	LEKTI domain 6			2.0 mM

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Protein Blocks Logo

Calculated from 21 models in PDB: 1H0Z, Strand ID: A Detail

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Coupling constant

24 J values in 1 lists
Temperature 298 (±1) K, pH 4.0 (±0.2) Detail

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Temperature 298 (±1) K, pH 4.0 (±0.2)

Experiment name DQF-COSY, 2D-1H clean-TOCSY, NOESY

List #1 j-couplings

Release date

2002-10-07

Citation

Homologous proteins with different folds: the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI
Lauber, T., Schulz, A., Schweimer, K., Adermann, K., Marx, U.C.
J. Mol. Biol. (2003), 328, 205-219, PubMed 12684009 , DOI 10.1016/s0022-2836(03)00245-6 , Abstract

Related entities 1. LEKTI domain 6 (HF7665) monomer, : 1 : 2 : 47 entities Detail

Experiments performed 3 experiments Detail