SAXSdb — 7tit

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

cardiac actin

OrganismNot specified

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 × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain A； UniProt 57–431 Chain B； UniProt 57–431 Chain C； UniProt 57–431 Chain D； UniProt 57–431 Chain E； UniProt 57–431 Chain F； UniProt 57–431	Not recorded	Myosin-binding protein C, cardiac-type × 6 （Q14896） tropomyosin model × 4	ELECTRON MICROSCOPY cryo-EM buffer：pH 7 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 8.00 Å

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 7TIT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7TIJ Cardiac F-actin decorated with regulatory M-domain of cardiac myosin binding protein C Deposited 2022-01-13	Different oligomeric state	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 57–431（375 aa） Chain B 57–431（375 aa） Chain C 57–431（375 aa） Chain D 57–431（375 aa） Chain E 57–431（375 aa） Chain F 57–431（375 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 8.00 Å
7TJ7 Cardiac thin filament decorated with C1 Ig-domain and regulatory M-domain of cardiac myosin binding protein C (cMyBP-C) Deposited 2022-01-14	Different oligomeric state	Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric	Chain A 57–431（375 aa） Chain B 57–431（375 aa） Chain C 57–431（375 aa） Chain D 57–431（375 aa） Chain E 57–431（375 aa） Chain F 57–431（375 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 8.00 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A4X1UMF3_PIG
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–375； UniProt 57–431 Author chain B； PDBConstruct 1–375； UniProt 57–431 Author chain C； PDBConstruct 1–375； UniProt 57–431 Author chain D； PDBConstruct 1–375； UniProt 57–431 Author chain E； PDBConstruct 1–375； UniProt 57–431 Author chain F； PDBConstruct 1–375； UniProt 57–431

Myosin-binding protein C, cardiac-type

Homo sapiens

UniProt Q14896

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 × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain G； UniProt 151–370 Chain H； UniProt 151–370 Chain I； UniProt 151–370 Chain J； UniProt 151–370 Chain K； UniProt 151–370 Chain L； UniProt 151–370	Not recorded	cardiac actin × 6 （A0A4X1UMF3） tropomyosin model × 4	ELECTRON MICROSCOPY cryo-EM buffer：pH 7 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 8.00 Å

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 7TIT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GXE Central domain of cardiac myosin binding protein C Deposited 2002-04-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 641–770（130 aa） Fragment：DOMAIN C5, RESIDUES 641-770	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；293 K；Ionic strength (raw mmCIF value) 100 MM NACL；Pressure 1	Resolution not provided
1PD6 The NMR structure of domain C2 of human cardiac Myosin Binding Protein C Deposited 2003-05-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 358–451（94 aa） Fragment：Domain C2	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 7.0；Pressure ambient NMR sample composition 0.75mM C2; 15N; 20mM phosphate buffer; 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition 0.75mM C2; 15N, 13C; 20mM phosphate buffer; 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition 0.75mM C2; 15N, 13C; 20mM phosphate buffer; 100% D2O \| 100% D2O	Resolution not provided
2AVG NMR structure of cC1 domain from Human Cardiac Myosin Binding Protein C Deposited 2005-08-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 151–260（110 aa） Fragment：cC1 domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0.1M；Pressure ambient NMR sample composition 0.8mM cC1 U-15N; 20mM phosphate buffer; 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition 0.8mM cC1 U-15N, 13C; 20mM phosphate buffer; 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition 0.8mM cC1 U-15N, 13C; 20mM phosphate buffer; 100% D2O \| 100% D2O	Resolution not provided
2K1M 3D NMR structure of domain cC0 of cardiac myosin binding protein C (MyBPC) Deposited 2008-03-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–96（95 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；303 K；Ionic strength (raw mmCIF value) 185；Pressure ambient NMR sample composition 1-1.5 mM [U-95% 13C; U-95% 15N] cC0_MyBPC, 55.5 M [U-2H] D2O, 40 mM sodium phosphate, 50 mM sodium chloride, 2 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1-1.5 mM [U-95% 15N] cC0_MyBPC, 55.5 M H2O, 40 mM sodium phosphate, 50 mM sodium chloride, 2 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1-1.5 mM cC0_MyBPC, 55.5 M H2O, 40 mM sodium phosphate, 50 mM sodium chloride, 2 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2MQ0 NMR structure of the c3 domain of human cardiac myosin binding protein-c Deposited 2014-06-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 453–543（91 aa） Fragment：unp residues 453-543	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.4；Pressure ambient NMR sample composition 50 mM sodium phosphate, 100 mM sodium chloride, 0.8 mM [U-100% 13C; U-100% 15N] protein, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2MQ3 NMR structure of the c3 domain of human cardiac myosin binding protein-c with a hypertrophic cardiomyopathy-related mutation R502W. Deposited 2014-06-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 453–543（91 aa） Fragment：unp residues 453-543	Mutation：R502W	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.4；Pressure ambient NMR sample composition 50 mM sodium phosphate, 100 mM sodium chloride, 0.8 mM [U-100% 13C; U-100% 15N] protein, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2V6H Crystal structure of the C1 domain of cardiac myosin binding protein-C Deposited 2007-07-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 151–258（108 aa） Fragment：C1 DOMAIN, RESIDUES 151-258	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；293 K；HANGING DROP; 20 C; 18%PEG, 0.1M BUFFER, PH 7.3	Resolution 1.55 Å R-free 0.241
3CX2 Crystal structure of the C1 domain of cardiac isoform of myosin binding protein-C at 1.3A Deposited 2008-04-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 151–258（108 aa） Fragment：Ig-like C2-type 1 domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；293 K；Crystals were grown at 20 C using the hanging drop method with a 2 microlitre drop containing a 1:1 mixture of protein solution and crystallising solution consisting of 8.5% PEG 3350 and 0.05M Hepes pH 6.8 over 500 microlitres of crystallising solution in the reservoir, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.30 Å R-free 0.209
5K6P The NMR structure of the m domain tri-helix bundle and C2 of human cardiac Myosin Binding Protein C Deposited 2016-05-25	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 319–451（133 aa） Fragment：residues 319-451	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 412 uM [U-99% 13C; U-99% 15N] human cMyBP-C (319-451), 10 mM MES, 1 mM CaCl2, 50 mM NaCl, 2 mM TCEP, 1 mM Na azide, 10 mM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 920 uM [U-99% 13C; U-99% 15N] human cMyBP-C (319-451), 10 mM MES, 1 mM CaCl2, 50 mM NaCl, 2 mM TCEP, 1 mM Na azide, 10 mM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 550 uM [U-99% 13C; U-99% 15N] human cMyBP-C (319-451), 10 mM MES, 1 mM CaCl2, 50 mM NaCl, 1 mM Na azide, 2 mM TCEP, 10 mM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 500 uM [U-99% 13C; U-99% 15N] human cMyBP-C (319-451), 10 mM MES, 1 mM CaCl2, 50 mM NaCl, 2 mM TCEP, 1 mM Na azide, 10 mM DSS, 99% D2O \| 99% D2O NMR sample composition 800 uM [U-99% 13C; U-99% 15N] human cMyBP-C (319-451), 10 mM MES, 1 mM CaCl2, 50 mM NaCl, 2 mM TCEP, 1 mM Na azide, 10 mM DSS, 99% D2O \| 99% D2O	Resolution not provided
6CXI Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C mode 1 Deposited 2018-04-03	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain G 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258) Chain H 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258) Chain I 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258) Chain J 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258) Chain K 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258) Chain L 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258) Chain M 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101) Chain N 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101) Chain O 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101) Chain P 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101) Chain Q 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 11.00 Å
6CXJ Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C mode 2 Deposited 2018-04-03	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain G 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258) Chain H 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258) Chain I 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258) Chain J 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258) Chain K 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258) Chain L 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258) Chain M 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101) Chain N 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101) Chain O 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101) Chain P 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101) Chain Q 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 11.00 Å
6G2T human cardiac myosin binding protein C C1 Ig-domain bound to native cardiac thin filament Deposited 2018-03-23	Different construct Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain G 151–258（108 aa） Chain H 151–258（108 aa） Chain I 151–258（108 aa） Chain J 151–258（108 aa） Chain K 151–258（108 aa） Chain L 151–258（108 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.00 Å
7LRG Filamentous actin decorated with human cardiac myosin binding protein C C2 domain Deposited 2021-02-16	Different construct Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain G 358–451（94 aa） Chain H 358–451（94 aa） Chain I 358–451（94 aa） Chain J 358–451（94 aa） Chain K 358–451（94 aa） Chain L 358–451（94 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.10 Å
7TIJ Cardiac F-actin decorated with regulatory M-domain of cardiac myosin binding protein C Deposited 2022-01-13	Different oligomeric state	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain G 151–370（220 aa） Chain H 151–370（220 aa） Chain I 151–370（220 aa） Chain J 151–370（220 aa） Chain K 151–370（220 aa） Chain L 151–370（220 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 8.00 Å
7TJ7 Cardiac thin filament decorated with C1 Ig-domain and regulatory M-domain of cardiac myosin binding protein C (cMyBP-C) Deposited 2022-01-14	Different construct Different mutation/modification Different oligomeric state	Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric	Chain G 151–370（220 aa） Chain H 151–370（220 aa） Chain I 151–370（220 aa） Chain J 151–370（220 aa） Chain K 151–370（220 aa） Chain L 151–370（220 aa） Chain M 151–370（220 aa） Chain N 151–370（220 aa） Chain O 151–370（220 aa） Chain P 151–370（220 aa） Chain Q 151–370（220 aa） Chain R 151–370（220 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 8.00 Å
8G4L Cryo-EM structure of the human cardiac myosin filament Deposited 2023-02-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 123 PDB declaration: 123-meric	Chain ao 1–1274（1274 aa） Chain bo 1–1274（1274 aa） Chain o 1–1274（1274 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.40 Å

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MYPC3_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain G； PDBConstruct 1–220； UniProt 151–370 Author chain H； PDBConstruct 1–220； UniProt 151–370 Author chain I； PDBConstruct 1–220； UniProt 151–370 Author chain J； PDBConstruct 1–220； UniProt 151–370 Author chain K； PDBConstruct 1–220； UniProt 151–370 Author chain L； PDBConstruct 1–220； UniProt 151–370

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	7tit
Deposition date deposition_date	2022-01-14
Structure title title	Cardiac thin filament decorated with regulatory M-domain of cardiac myosin binding protein C
Keywords keywords	cardiac contraction regulator, muscle protein, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	56.63 Å
Radius of gyration Rg (electron density) rg_electron	56.97 Å
Forward intensity I(0) i0	1512320000.00
Molecular weight molecular_weight	316640.0 kDa
Excluded volume excluded_volume	392600 Å³
Envelope volume envelope_volume	568390 Å³
Hydration-shell volume shell_volume	87186 Å³
Envelope diameter envelope_diameter	230.6 Å
Shell Rg shell_rg	54.23 Å
Envelope Rg envelope_rg	57.60 Å
Shape Rg shape_rg	57.02 Å
Total Rg total_rg	56.71 Å
Total atoms total_atoms	24141
Residues n_residues	3024
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	214.4 Å
Rg (real space) rg_real	57.21 Å
Rg uncertainty (real space) rg_real_error	2.74 Å
I(0) (real space) i0_real	1.5120e+09
I(0) uncertainty (real space) i0_real_error	3.3180e+07
Rg (reciprocal space) rg_reciprocal	56.14 Å
I(0) (reciprocal space) i0_reciprocal	1510000000.0000
Solution quality estimate total_estimate	0.7804
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	53.6 Å
Skewness Skewness skewness	0.664
Kurtosis Kurtosis kurtosis	0.018
Angular range angular_range	— – 0.1400 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	170100000.0000
Real-space data points n_real_points	29
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.483; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.834; Smooth: 0.859

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	cardiac actin
Molecular weight formula_weight	41830.6 kDa
Source method src_method	nat
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	24141

DDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF

Entity 2 Entity 2 polymer

Description description	Myosin-binding protein C, cardiac-type
Molecular weight formula_weight	24803.1 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,H,I,J,K,L

DDPIGLFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQPAFTGSYRCEVSTKDKFDCSNFNLTVHEAMGTGDLDLLSAFRRTSLAGGGRRISDSHEDTGILDFSSLLKKRDSFRTPRDSKLEAPAEEDVWEILRQAPPSEYERIAFQYGVTDLRGMLKRLKGMRRDEKKSTAFQKKLE

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	tropomyosin model
Molecular weight formula_weight	11507.2 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M,N,O,P

XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

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8. Citations (1)

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Resolution resolution	8.00 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	14282

fit	/app/data/saxs_computation/ti/7tit/7tit.fit
pddf	/app/data/pr_computation/ti/7tit/7tit.pr.out
profile	/app/data/saxs_computation/ti/7tit/7tit.dat

Cardiac thin filament decorated with regulatory M-domain of cardiac myosin binding protein C

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

cardiac actin

State in the Current Structure

Other States of the Same Protein in the Database

Myosin-binding protein C, cardiac-type

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)