BMRB: 11122

The solution structure of the tetratrico peptide repeat of human Smooth muscle cell associated protein-1, isoform 2

Authors

Tochio, N., Sasagawa, A., Koshiba, S., Inoue, M., Kigawa, T., Yokoyama, S.

Assembly

Smooth muscle cell associated protein-1, isoform 2

Entity

1. Smooth muscle cell associated protein-1, isoform 2 (polymer, Thiol state: all free), 148 monomers, 15672.28 Da Detail

GSSGSSGMTV SGPGTPEPRP ATPGASSVEQ LRKEGNELFK CGDYGGALAA YTQALGLDAT PQDQAVLHRN RAACHLKLED YDKAETEASK AIEKDGGDVK ALYRRSQALE KLGRLDQAVL DLQRCVSLEP KNKVFQEALR NISGPSSG

Formula weight

15672.28 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 94.6 %, Completeness: 91.5 %, Completeness (bb): 91.9 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	91.5 % (1476 of 1613)	88.6 % (748 of 844)	94.7 % (584 of 617)	94.7 % (144 of 152)
Backbone	91.9 % (801 of 872)	89.1 % (271 of 304)	93.0 % (398 of 428)	94.3 % (132 of 140)
Sidechain	91.8 % (801 of 873)	88.3 % (477 of 540)	97.2 % (312 of 321)	100.0 % (12 of 12)
Aromatic	98.3 % (59 of 60)	100.0 % (30 of 30)	96.7 % (29 of 30)
Methyl	100.0 % (146 of 146)	100.0 % (73 of 73)	100.0 % (73 of 73)

1. TPR, Residues 8-142

GSSGSSGMTV SGPGTPEPRP ATPGASSVEQ LRKEGNELFK CGDYGGALAA YTQALGLDAT PQDQAVLHRN RAACHLKLED YDKAETEASK AIEKDGGDVK ALYRRSQALE KLGRLDQAVL DLQRCVSLEP KNKVFQEALR NISGPSSG

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 (±0.001) atm, Temperature 298 (±0.1) K, pH 7.0 (±0.05), Details 1.3mM TPRx3 domain {U-15N,13C;} 20mM {d-Tris HCl;} 100mM {NaCl;} 1mM {d-DTT;} 0.02% {NaN3;} 90% H2O, 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	TPRx3 domain	[U-13C; U-15N]	protein	1.3 mM
2	d-Tris HCl	natural abundance	buffer	20 mM
3	NaCl	natural abundance	salt	100 mM
4	d-DTT	natural abundance	salt	1 mM
5	NaN3	natural abundance	salt	0.02 %
6	H2O		solvent	90 %
7	D2O		solvent	10 %

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LACS Plot; CA

Referencing offset: -0.12 ppm, Outliers: 2 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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LACS Plot; CB

Referencing offset: -0.12 ppm, Outliers: 2 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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LACS Plot; HA

Referencing offset: 0.02 ppm, Outliers: 1 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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LACS Plot; CO

Referencing offset: -0.19 ppm, Outliers: 1 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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Protein Blocks Logo

Calculated from 20 models in PDB: 2DBA, Strand ID: A Detail

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Release date

2011-03-31

Citation

The solution structure of the tetratrico peptide repeat of human Smooth muscle cell associated protein-1, isoform 2
Tochio, N., Sasagawa, A., Koshiba, S., Inoue, M., Kigawa, T., Yokoyama, S.

Related entities 1. Smooth muscle cell associated protein-1, isoform 2, : 1 : 2 : 54 entities Detail

Interaction partners 1. Smooth muscle cell associated protein-1, isoform 2, : 79 interactors Detail

Experiments performed 2 experiments Detail