SAXSdb — 1ytz

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Troponin T

Gallus gallus

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain T； UniProt 156–262	Not recorded	Troponin I × 1 （P68246） Troponin C × 1 （P02588） DR6 ALPHA-[4-(1,1,3,3 - TETRAMETHYLBUTYL)PHENYL]-OMEGA-HYDROXY-POLY(OXY-1,2-ETHANEDIYL) × 3 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；0.4 M NaH2PO4/1.6 M K2HPO4, 200 mM NaCl, 0.1 M immidazole, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.00 Å R-free 0.338
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain T； UniProt 156–262	Not recorded	Troponin I × 2 （P68246） Troponin C × 2 （P02588） DR6 ALPHA-[4-(1,1,3,3 - TETRAMETHYLBUTYL)PHENYL]-OMEGA-HYDROXY-POLY(OXY-1,2-ETHANEDIYL) × 6 CA CALCIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；0.4 M NaH2PO4/1.6 M K2HPO4, 200 mM NaCl, 0.1 M immidazole, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.00 Å R-free 0.338

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1YTZ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1YV0 Crystal structure of skeletal muscle troponin in the Ca2+-free state Deposited 2005-02-14	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain T 156–262（107 aa）	Not recorded	MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；1.6 M tri-Sodium Citrate dihydrate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 7.00 Å R-free 0.359
1YV0 Crystal structure of skeletal muscle troponin in the Ca2+-free state Deposited 2005-02-14	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain T 156–262（107 aa）	Not recorded	MG MAGNESIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；1.6 M tri-Sodium Citrate dihydrate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 7.00 Å R-free 0.359
2W49 ISOMETRICALLY CONTRACTING INSECT ASYNCHRONOUS FLIGHT MUSCLE Deposited 2008-11-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 1 148–237（90 aa） Fragment：RESIDUES 148-237 Chain 4 148–237（90 aa） Fragment：RESIDUES 148-237 Chain 7 148–237（90 aa） Fragment：RESIDUES 148-237 Chain Y 148–237（90 aa） Fragment：RESIDUES 148-237	Not recorded	CA CALCIUM ION × 16	ELECTRON MICROSCOPY cryo-EM buffer 20 MM MOPS BUFFER, 5 MM NAN3, AND MGCL2, ATP, CACL2, AND EGTA IN VARYING MILLIMOLAR CONCENTRATIONS；20 MM MOPS BUFFER, 5 MM NAN3, AND MGCL2, ATP, CACL2, AND EGTA IN VARYING MILLIMOLAR CONCENTRATIONS cryo-EM vitrification conditions Cryogen HELIUM；SMASH AGAINST A LIQUID HELIUM COOLED GOLD COATED COPPER MIRROR	Resolution 35.00 Å
2W4U Isometrically contracting insect asynchronous flight muscle quick frozen after a length step Deposited 2008-12-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 1 148–237（90 aa） Fragment：RESIDUES 148-237 Chain 4 148–237（90 aa） Fragment：RESIDUES 148-237 Chain 7 148–237（90 aa） Fragment：RESIDUES 148-237 Chain Y 148–237（90 aa） Fragment：RESIDUES 148-237	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 MM MOPS BUFFER, 5 MM NAN3, AND MGCL2, ATP, CACL2, AND EGTA IN VARYING MILLIMOLAR CONCENTRATIONS；20 MM MOPS BUFFER, 5 MM NAN3, AND MGCL2, ATP, CACL2, AND EGTA IN VARYING MILLIMOLAR CONCENTRATIONS cryo-EM vitrification conditions Cryogen HELIUM；SMASH AGAINST A LIQUID HELIUM COOLED GOLD COATED COPPER MIRROR	Resolution 35.00 Å
2Z5H Crystal structure of the head-to-tail junction of tropomyosin complexed with a fragment of TnT Deposited 2007-07-12	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain T 58–112（55 aa） Fragment：Residues 58-112	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.89 Å R-free 0.247

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TNNT3_CHICK
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain T； PDBConstruct 1–107； UniProt 156–262

Troponin I

Gallus gallus

UniProt P68246

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain I； UniProt 1–182	Not recorded	Troponin T × 1 （P12620） Troponin C × 1 （P02588） DR6 ALPHA-[4-(1,1,3,3 - TETRAMETHYLBUTYL)PHENYL]-OMEGA-HYDROXY-POLY(OXY-1,2-ETHANEDIYL) × 3 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；0.4 M NaH2PO4/1.6 M K2HPO4, 200 mM NaCl, 0.1 M immidazole, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.00 Å R-free 0.338
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain I； UniProt 1–182	Not recorded	Troponin T × 2 （P12620） Troponin C × 2 （P02588） DR6 ALPHA-[4-(1,1,3,3 - TETRAMETHYLBUTYL)PHENYL]-OMEGA-HYDROXY-POLY(OXY-1,2-ETHANEDIYL) × 6 CA CALCIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；0.4 M NaH2PO4/1.6 M K2HPO4, 200 mM NaCl, 0.1 M immidazole, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.00 Å R-free 0.338

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1YTZ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1VDI Solution structure of actin-binding domain of troponin in Ca2+-free state Deposited 2004-03-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 131–182（52 aa） Fragment：residues 131-182	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1VDJ Solution structure of actin-binding domain of troponin in Ca2+-bound state Deposited 2004-03-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 131–182（52 aa） Fragment：residues 131-182	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1YV0 Crystal structure of skeletal muscle troponin in the Ca2+-free state Deposited 2005-02-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 1–137（137 aa）	Not recorded	MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；1.6 M tri-Sodium Citrate dihydrate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 7.00 Å R-free 0.359
1YV0 Crystal structure of skeletal muscle troponin in the Ca2+-free state Deposited 2005-02-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain I 1–137（137 aa）	Not recorded	MG MAGNESIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；1.6 M tri-Sodium Citrate dihydrate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 7.00 Å R-free 0.359
2W49 ISOMETRICALLY CONTRACTING INSECT ASYNCHRONOUS FLIGHT MUSCLE Deposited 2008-11-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 2 4–144（141 aa） Fragment：RESIDUES 4-144 Chain 5 4–144（141 aa） Fragment：RESIDUES 4-144 Chain 8 4–144（141 aa） Fragment：RESIDUES 4-144 Chain Z 4–144（141 aa） Fragment：RESIDUES 4-144	Not recorded	CA CALCIUM ION × 16	ELECTRON MICROSCOPY cryo-EM buffer 20 MM MOPS BUFFER, 5 MM NAN3, AND MGCL2, ATP, CACL2, AND EGTA IN VARYING MILLIMOLAR CONCENTRATIONS；20 MM MOPS BUFFER, 5 MM NAN3, AND MGCL2, ATP, CACL2, AND EGTA IN VARYING MILLIMOLAR CONCENTRATIONS cryo-EM vitrification conditions Cryogen HELIUM；SMASH AGAINST A LIQUID HELIUM COOLED GOLD COATED COPPER MIRROR	Resolution 35.00 Å
2W4U Isometrically contracting insect asynchronous flight muscle quick frozen after a length step Deposited 2008-12-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 2 4–144（141 aa） Fragment：RESIDUES 4-144 Chain 5 4–144（141 aa） Fragment：RESIDUES 4-144 Chain 8 4–144（141 aa） Fragment：RESIDUES 4-144 Chain Z 4–144（141 aa） Fragment：RESIDUES 4-144	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 MM MOPS BUFFER, 5 MM NAN3, AND MGCL2, ATP, CACL2, AND EGTA IN VARYING MILLIMOLAR CONCENTRATIONS；20 MM MOPS BUFFER, 5 MM NAN3, AND MGCL2, ATP, CACL2, AND EGTA IN VARYING MILLIMOLAR CONCENTRATIONS cryo-EM vitrification conditions Cryogen HELIUM；SMASH AGAINST A LIQUID HELIUM COOLED GOLD COATED COPPER MIRROR	Resolution 35.00 Å

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TNNI2_CHICK
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain I； PDBConstruct 1–182； UniProt 1–182

Troponin C

Gallus gallus

UniProt P02588

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain C； UniProt 1–162	Not recorded	Troponin T × 1 （P12620） Troponin I × 1 （P68246） DR6 ALPHA-[4-(1,1,3,3 - TETRAMETHYLBUTYL)PHENYL]-OMEGA-HYDROXY-POLY(OXY-1,2-ETHANEDIYL) × 3 CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；0.4 M NaH2PO4/1.6 M K2HPO4, 200 mM NaCl, 0.1 M immidazole, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.00 Å R-free 0.338
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain C； UniProt 1–162	Not recorded	Troponin T × 2 （P12620） Troponin I × 2 （P68246） DR6 ALPHA-[4-(1,1,3,3 - TETRAMETHYLBUTYL)PHENYL]-OMEGA-HYDROXY-POLY(OXY-1,2-ETHANEDIYL) × 6 CA CALCIUM ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；0.4 M NaH2PO4/1.6 M K2HPO4, 200 mM NaCl, 0.1 M immidazole, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.00 Å R-free 0.338

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1YTZ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AVS X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C Deposited 1997-09-19	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–90（90 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1 - 90	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；72 % AMMONIUM SULFATE 100 MM TRIS 2 % MPD, 5 MM CALCIUM CHLORIDE PH 7.5	Resolution 1.75 Å R-free 0.250
1AVS X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C Deposited 1997-09-19	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–90（90 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1 - 90	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；72 % AMMONIUM SULFATE 100 MM TRIS 2 % MPD, 5 MM CALCIUM CHLORIDE PH 7.5	Resolution 1.75 Å R-free 0.250
1BLQ STRUCTURE AND INTERACTION SITE OF THE REGULATORY DOMAIN OF TROPONIN-C WHEN COMPLEXED WITH THE 96-148 REGION OF TROPONIN-I, NMR, 29 STRUCTURES Deposited 1998-07-19	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–90（90 aa） Fragment：REGULATORY	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.85；303 K；Ionic strength (raw mmCIF value) 100 mM KCL；Pressure 1 NMR sample composition H2O	Resolution not provided
1CTA DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY Deposited 1992-11-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 93–126（34 aa） Chain B 93–126（34 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1CTD DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY Deposited 1992-11-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 93–126（34 aa） Chain B 93–126（34 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1JC2 COMPLEX OF THE C-DOMAIN OF TROPONIN C WITH RESIDUES 1-40 OF TROPONIN I Deposited 2001-06-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 89–163（75 aa） Fragment：residues 89-163 of GB entry 212778	Not recorded	CA CALCIUM ION × 2	SOLUTION NMR NMR measurement conditions pH 6.8；303 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambiant NMR sample composition ~1.3 mM C-domain of Sqeletal Troponin C, 1.9 mM of TnI peptide (residues 1-40), 100 mM KCl, 10 mM Imidazole, 1 mM DSS \| 90% H2O/10% D2O	Resolution not provided
1NCX TROPONIN C Deposited 1996-06-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–162（162 aa）	Not recorded	CD CADMIUM ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å
1NCY TROPONIN-C, COMPLEX WITH MANGANESE Deposited 1996-06-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–162（162 aa）	Not recorded	MN MANGANESE (II) ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å
1NCZ TROPONIN C Deposited 1996-06-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–162（162 aa）	Not recorded	TB TERBIUM(III) ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å
1NPQ structure of a rhodamine-labeled N-domain Troponin C mutant (Ca2+ saturated) in complex with skeletal Troponin I 115-131 Deposited 2003-01-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–90（90 aa） Fragment：TnC, residues 1-90	Mutation：E56C, E63C	CA CALCIUM ION × 2	SOLUTION NMR NMR measurement conditions pH 6.5；303 K；Ionic strength (raw mmCIF value) 320 mM KCl；Pressure ambiant NMR sample composition 320 mM KCl, 10 mM imidazole, 1.3% NaN3, pH 6.5, ~1mM sNTnC.2Ca2+.TnI115-131.BR56-63 \| 90% H2O/10% D2O	Resolution not provided
1PON SITE III-SITE IV TROPONIN C HETERODIMER, NMR Deposited 1996-04-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 93–126（34 aa） Fragment：SITE III AND IV Chain B 129–162（34 aa） Fragment：SITE III AND IV	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1SKT SOLUTION STRUCTURE OF APO N-DOMAIN OF TROPONIN C, NMR, 40 STRUCTURES Deposited 1998-04-06	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–90（90 aa） Fragment：N-DOMAIN, RESIDUES 1-90	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.7；277 K；Ionic strength (raw mmCIF value) 50mM KCL；Pressure 1 NMR sample composition WATER	Resolution not provided
1SMG CALCIUM-BOUND E41A MUTANT OF THE N-DOMAIN OF CHICKEN TROPONIN C, NMR, 40 STRUCTURES Deposited 1997-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–90（90 aa） Fragment：N-DOMAIN	Mutation：E41A	CA CALCIUM ION × 1	SOLUTION NMR NMR measurement conditions pH 6.7；303.15 K	Resolution not provided
1TNP STRUCTURES OF THE APO AND CALCIUM TROPONIN-C REGULATORY DOMAINS: THE MUSCLE CONTRACTION SWITCH Deposited 1995-07-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–90（90 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1TNQ STRUCTURES OF THE APO AND CALCIUM TROPONIN-C REGULATORY DOMAINS: THE MUSCLE CONTRACTION SWITCH Deposited 1995-07-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–90（90 aa）	Not recorded	CA CALCIUM ION × 2	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1TNW NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C Deposited 1995-08-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–163（162 aa）	Mutation：T130I	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1TNX NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C Deposited 1995-08-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–163（162 aa）	Mutation：T130I	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1TOP STRUCTURE OF CHICKEN SKELETAL MUSCLE TROPONIN-C AT 1.78 ANGSTROMS RESOLUTION Deposited 1993-08-11	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–162（162 aa）	Not recorded	CA CALCIUM ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.78 Å
1YV0 Crystal structure of skeletal muscle troponin in the Ca2+-free state Deposited 2005-02-14	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–162（162 aa）	Not recorded	MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；1.6 M tri-Sodium Citrate dihydrate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 7.00 Å R-free 0.359
1YV0 Crystal structure of skeletal muscle troponin in the Ca2+-free state Deposited 2005-02-14	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 1–162（162 aa）	Not recorded	MG MAGNESIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；1.6 M tri-Sodium Citrate dihydrate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 7.00 Å R-free 0.359
1ZAC N-DOMAIN OF TROPONIN C FROM CHICKEN SKELETAL MUSCLE, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1998-04-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–90（90 aa） Fragment：N-DOMAIN, RESIDUES 1-90	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.7；277 K；Ionic strength (raw mmCIF value) 50mM KCL；Pressure 1 NMR sample composition WATER	Resolution not provided
2W49 ISOMETRICALLY CONTRACTING INSECT ASYNCHRONOUS FLIGHT MUSCLE Deposited 2008-11-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 0 5–163（159 aa） Fragment：RESIDUES 5-163 Chain 3 5–163（159 aa） Fragment：RESIDUES 5-163 Chain 6 5–163（159 aa） Fragment：RESIDUES 5-163 Chain 9 5–163（159 aa） Fragment：RESIDUES 5-163	Not recorded	CA CALCIUM ION × 16	ELECTRON MICROSCOPY cryo-EM buffer 20 MM MOPS BUFFER, 5 MM NAN3, AND MGCL2, ATP, CACL2, AND EGTA IN VARYING MILLIMOLAR CONCENTRATIONS；20 MM MOPS BUFFER, 5 MM NAN3, AND MGCL2, ATP, CACL2, AND EGTA IN VARYING MILLIMOLAR CONCENTRATIONS cryo-EM vitrification conditions Cryogen HELIUM；SMASH AGAINST A LIQUID HELIUM COOLED GOLD COATED COPPER MIRROR	Resolution 35.00 Å
2W4U Isometrically contracting insect asynchronous flight muscle quick frozen after a length step Deposited 2008-12-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 0 5–163（159 aa） Fragment：RESIDUES 5-163 Chain 3 5–163（159 aa） Fragment：RESIDUES 5-163 Chain 6 5–163（159 aa） Fragment：RESIDUES 5-163 Chain 9 5–163（159 aa） Fragment：RESIDUES 5-163	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 MM MOPS BUFFER, 5 MM NAN3, AND MGCL2, ATP, CACL2, AND EGTA IN VARYING MILLIMOLAR CONCENTRATIONS；20 MM MOPS BUFFER, 5 MM NAN3, AND MGCL2, ATP, CACL2, AND EGTA IN VARYING MILLIMOLAR CONCENTRATIONS cryo-EM vitrification conditions Cryogen HELIUM；SMASH AGAINST A LIQUID HELIUM COOLED GOLD COATED COPPER MIRROR	Resolution 35.00 Å
4TNC REFINED STRUCTURE OF CHICKEN SKELETAL MUSCLE TROPONIN C IN THE TWO-CALCIUM STATE AT 2-ANGSTROMS RESOLUTION Deposited 1987-09-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–162（161 aa）	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å

22 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TNNC2_CHICK
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–162； UniProt 1–162

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1ytz
Deposition date deposition_date	2005-02-11
Structure title title	Crystal structure of skeletal muscle troponin in the Ca2+-activated state
Keywords keywords	troponin, muscle, thin filament, actin binding, calcium, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	28.71 Å
Radius of gyration Rg (electron density) rg_electron	27.85 Å
Forward intensity I(0) i0	36825000.00
Molecular weight molecular_weight	46437.0 kDa
Excluded volume excluded_volume	58045 Å³
Envelope volume envelope_volume	80684 Å³
Hydration-shell volume shell_volume	25091 Å³
Envelope diameter envelope_diameter	99.7 Å
Shell Rg shell_rg	33.89 Å
Envelope Rg envelope_rg	27.58 Å
Shape Rg shape_rg	27.84 Å
Total Rg total_rg	28.57 Å
Total atoms total_atoms	3249
Residues n_residues	390
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	94.0 Å
Rg (real space) rg_real	28.65 Å
Rg uncertainty (real space) rg_real_error	0.67 Å
I(0) (real space) i0_real	3.6820e+07
I(0) uncertainty (real space) i0_real_error	5.2150e+05
Rg (reciprocal space) rg_reciprocal	28.68 Å
I(0) (reciprocal space) i0_reciprocal	36830000.0000
Solution quality estimate total_estimate	0.8957
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	41.0 Å
Skewness Skewness skewness	0.131
Kurtosis Kurtosis kurtosis	-0.581
Angular range angular_range	— – 0.2750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4428000.0000
Real-space data points n_real_points	56
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.984

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Troponin T
Molecular weight formula_weight	12694.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	T
Atom count atom_count	3282

MGASYSSYLAKADQKRGKKQTARETKKKVLAERRKPLNIDHLNEDKLRDKAKELWDWLYQLQTEKYDFAEQIKRKKYEIVTLRNRIDQAQKHSKKAGAKGKVGGRWK

来源 Source

来源生物 organism	Gallus gallus
通用名 common_name	chicken
NCBI Class编号 ncbi_taxonomy_id	9031
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Troponin I
Molecular weight formula_weight	21116.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I

SDEEKKRRAATARRQHLKSAMLQLAVTEIEKEAAAKEVEKQNYLAEHSPPLSLPGSMQELQELSKKLHAKIDSVDEERYDTEVKLQKTNKELEDLSQKLFDLRGKFKRPPLRRVRMSADAMLRALLGSKHKVNMDLRANLKQVKKEDTEKEKDLRDVGDWRKNIEEKSGMEGRKKMFEAGES

来源 Source

来源生物 organism	Gallus gallus
通用名 common_name	chicken
NCBI Class编号 ncbi_taxonomy_id	9031
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 polymer

Description description	Troponin C
Molecular weight formula_weight	18261.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

ASMTDQQAEARAFLSEEMIAEFKAAFDMFDADGGGDISTKELGTVMRMLGQNPTKEELDAIIEEVDEDGSGTIDFEEFLVMMVRQMKEDAKGKSEEELANCFRIFDKNADGFIDIEELGEILRATGEHVTEEDIEDLMKDSDKNNDGRIDFDEFLKMMEGVQ

来源 Source

来源生物 organism	Gallus gallus
通用名 common_name	chicken
NCBI Class编号 ncbi_taxonomy_id	9031
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 4 Entity 4 non-polymer

Description description	ALPHA-[4-(1,1,3,3 - TETRAMETHYLBUTYL)PHENYL]-OMEGA-HYDROXY-POLY(OXY-1,2-ETHANEDIYL)
Molecular weight formula_weight	1527.9 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 5 Entity 5 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	33

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7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1ytzc_
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.5 — Calmodulin-like

Domain ID domain_id	d1ytzi1
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.25 — Troponin coil-coiled subunits
Family Family family	h.1.25.2 — Troponin I

Domain ID domain_id	d1ytzt1
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.25 — Troponin coil-coiled subunits
Family Family family	h.1.25.1 — Troponin T

CATH v4.4 (4 domains)

Domain ID domain_id	1ytzC01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1ytzC02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1ytzI01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	350 — Troponin complex, TnI/TnT subunit

Domain ID domain_id	1ytzT00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	350 — Troponin complex, TnI/TnT subunit

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8. Citations (1)

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Unit-cell length a length_a	138.608 Å
Unit-cell length b length_b	138.608 Å
Unit-cell length c length_c	83.676 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	25.000 Å
R factor r_factor	0.2893
R_work r_work	0.2893
R_free r_free	0.3375

fit	/app/data/saxs_computation/yt/1ytz/1ytz.fit
pddf	/app/data/pr_computation/yt/1ytz/1ytz.pr.out
profile	/app/data/saxs_computation/yt/1ytz/1ytz.dat

Crystal structure of skeletal muscle troponin in the Ca2+-activated state

1. Protein Identity and Related Structures Protein Identity & Related Structures

Troponin T

State in the Current Structure

Other States of the Same Protein in the Database

Troponin I

State in the Current Structure

Other States of the Same Protein in the Database

Troponin C

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)