Complex of TM1a(1-14)Zip with TM9a(251-284): a model for the polymerization
domain ("overlap region")of tropomyosin

Four chain complex of a two-chain coiled coil model molecule containing the
N-terminal 14 residues of tropomyosin in a chimeric peptide (TM1a(1-14)Zip with
a two chain model molecule containing residues 251-284 of rat striated alpha
tropomyosin.

Solution NMR structure of the junction between tropomyosin molecules: implications for actin binding and regulation.

Huang YJ, Tejero R, Powers R, Montelione GT.
A topology-constrained distance network algorithm for protein structure determination from NOESY data.
Proteins. 2006 Mar 15;62(3):587-603.

A topology-constrained distance network algorithm for protein structure determination from NOESY data.

Guntert P, Mumenthaler C, Wuthrich K.Torsion angle dynamics for NMR structure calculation with the new program DYANA.
J Mol Biol. 1997 Oct 17;273(1):283-98.

Torsion angle dynamics for NMR structure calculation with the new program DYANA.

Guntert P. Automated NMR structure calculation with CYANA.
Methods Mol Biol. 2004;278:353-78.

Methods in molecular biology (Clifton, N.J.)
Automated NMR structure calculation with CYANA.

Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A.
NMRPipe: a multidimensional spectral processing system based on UNIX pipes.
J Biomol NMR. 1995 Nov;6(3):277-93.

NMRPipe: a multidimensional spectral processing system based on UNIX pipes.

Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL.
Crystallography & NMR system: A new software suite for macromolecular structure determination.
Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54 ( Pt 5):905-21.

Acta crystallographica. Section D, Biological crystallography
Crystallography & NMR system: A new software suite for macromolecular structure determination.

T. D. Goddard and D. G. Kneller, SPARKY 3,
University of California, San Francisco

Chimerica synthetic peptide containing the first 14 residues of rat striated
muscle alpha-tropomyosin and the last 18 residues of the yeast transcription
factor GCN4

Peptide containing gly-cys-gly followed by residues 251-284 of
alpha-tropomyosin from rat striated muscle. The peptide has the mutation N279K

Two chain coiled coil complex of peptide containing the first 14 residues of
alpha-tropomyosin from rat striated muscle and the last 18 residues of the
yeast transcription factor GCN4

Two-chain coiled coil of a molecule containing residues 251-284 of
alpha-tropomyosin from rat striated muscle. There is a gly-cys-cly at the
N-terminus. The peptides are cross-lined by a cysteine disulfide. The peptide
contains the mutation N279K

Crystal Structure Of Tropomyosin At 7 Angstroms Resolution In The Spermine-Induced Crystal Form

Tm9a251-284: A Peptide Model Of The C-Terminus Of A Rat Striated Alpha Tropomyosin

Crystal Structure Of The C-Terminal Fragment Of Rabbit Skeletal Alpha-Tropomyosin

Complex Of Tm1a(1-14)zip With Tm9a(251-284): A Model For The Polymerization Domain ("overlap Region") Of Tropomyosin, Northeast

Tropomyosin Crystal Structure And Muscle Regulation. Appendix. Construction Of An Atomic Model For Tropomyosin And Implications

Isometrically Contracting Insect Asynchronous Flight Muscle

Isometrically Contracting Insect Asynchronous Flight Muscle Quick Frozen After A Length Step

unnamed protein product [Rattus norvegicus]

unnamed protein product [Coturnix coturnix]

alpha-tropomyosin of skeletal fast muscle [Gallus gallus]

alpha-skeletal tropomyosin [Xenopus laevis]

striated-muscle alpha tropomyosin [Rattus norvegicus]

minor striated-muscle alpha tropomyosin [Rattus norvegicus]

tropomyosin alpha-1 chain isoform Tpm1.1st [Homo sapiens]

tropomyosin alpha-1 chain isoform Tpm1.13 [Rattus norvegicus]

tropomyosin alpha-1 chain [Oryctolagus cuniculus]

RecName: Full=Tropomyosin alpha-1 chain; AltName: Full=Alpha-tropomyosin; AltName: Full=Tropomyosin-1 [Gallus gallus]

RecName: Full=Tropomyosin alpha-1 chain; AltName: Full=Alpha-tropomyosin; AltName: Full=Tropomyosin-1 [Rattus norvegicus]

RecName: Full=Tropomyosin alpha-1 chain; AltName: Full=Alpha-tropomyosin; AltName: Full=Tropomyosin-1 [Homo sapiens]

RecName: Full=Tropomyosin alpha-1 chain; AltName: Full=Alpha-tropomyosin; AltName: Full=Tropomyosin-1 [Rana temporaria]

RecName: Full=Tropomyosin alpha-1 chain; AltName: Full=Alpha-tropomyosin; AltName: Full=Tropomyosin-1 [Sus scrofa]

Four chain complex of two model peptides containing the C- and N-terminal domains.

Initail structure was calculated with Torsion Angle Dynamics and refined with simulated annealing and included a term for explicit solvent in the refinement protocol.

Unbound N-terminal model molecule with Gly replaceing the N-terminal Acetyl group

NTD-CTD complex both chains labeled with 15N, in 100 mM NaCl, 10 mM NaPO4, 7.5% D2O pH*=6.5

NTD-CTD complex CTD labeled with 13C/15N NTD unlabeled

NTD-CTD NTD labeled with 13C/15N CTD unlabeled

NTD-CTD complex NTD labeled with 13C/15N CTD unlabeled

NTD-CTD complex one chain of CTD labeled with 13C/15N CTD one chain of CTD unlabeled both chains of NTD unlabeled

NTD-CTD complex one chain of NTD labeled with 13C/15N CTD one chain of NTD unlabeled both chains of CTD unlabeled

100 mM NaCl, 10 mM Sodium phoshate, 7.5% 2H2O pH* 6.5, 10 deg. C.

100 mM NaCl, 10 mM sodium phosphate, 99.9% deuterium oxide, pH* 6.5, 10 deg C.

AutoStructure v 1.1.2 modified solving a four chain complex of two homodimeric
parallel symmetric coiled coils.

Torsion angle dynamics for NMR structure calculation

Gaetano T. Montelione,
CABM, Rutgers University
679 Hoes Lane,
Piscataway, NJ 08854

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Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule-Honggerberg, CH-8093, Zurich, Switzerland

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