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1bpv

TITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES

Method: SOLUTION NMR Dmax: 46.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

TITIN

Homo sapiens

UniProt Q10466

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 14859–14961 Fragment：71 TH DOMAIN FROM THE A-BAND Mutation：I9V No other associated polymer SOLUTION NMR NMR measurement conditions：pH 5.6；310 K；Ionic strength (raw mmCIF value) 50 mM NACL NMR sample composition：10 MM ACETATE BUFFER Resolution not provided

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 1BPV Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1G1C I1 DOMAIN FROM TITIN Deposited 2000-10-11 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2027–2125（99 aa） Fragment：MOST N-TERMINAL IG DOMAIN, RESIDUES 2027-2125
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；294 K；3.25 M NaCl, 0.1 M Tris-HCL pH 8.0, 1mM EDTA, 1mM DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP at 294K
Resolution 2.10 Å R-free 0.248
1G1C I1 DOMAIN FROM TITIN Deposited 2000-10-11 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2027–2125（99 aa） Fragment：MOST N-TERMINAL IG DOMAIN, RESIDUES 2027-2125
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；294 K；3.25 M NaCl, 0.1 M Tris-HCL pH 8.0, 1mM EDTA, 1mM DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP at 294K
Resolution 2.10 Å R-free 0.248
1NCT TITIN MODULE M5, N-TERMINALLY EXTENDED, NMR Deposited 1996-08-13 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 26059–26155（97 aa） Fragment：N-TERMINALLY EXTENDED MODULE M5
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.8；300 K
Resolution not provided
1NCU Titin Module M5, N-terminally Extended, NMR Deposited 1996-08-13 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 26059–26155（97 aa） Fragment：N-TERMINALLY EXTENDED MODULE M5
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.8；300 K
Resolution not provided
1TIT TITIN, IG REPEAT 27, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1996-02-02 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 5253–5341（89 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1TIU TITIN, IG REPEAT 27, NMR, 24 STRUCTURES Deposited 1996-02-02 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 5253–5341（89 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1TKI AUTOINHIBITED SERINE KINASE DOMAIN OF THE GIANT MUSCLE PROTEIN TITIN Deposited 1998-05-29 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 24748–25068（321 aa） Fragment：KINASE
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å R-free 0.248
1TKI AUTOINHIBITED SERINE KINASE DOMAIN OF THE GIANT MUSCLE PROTEIN TITIN Deposited 1998-05-29 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 24748–25068（321 aa） Fragment：KINASE
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å R-free 0.248

6 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q10466_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 10–112； UniProt 14859–14961

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1bpv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bpv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bpv
Deposition date deposition_date1998-08-11
Structure title titleTITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES
Keywords keywordsTITIN, CONNECTIN, FIBRONECTIN TYPE III; CONNECTIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.00 Å
Radius of gyration Rg (electron density) rg_electron13.92 Å
Forward intensity I(0) i04321530000.00
Molecular weight molecular_weight570740.0 kDa
Excluded volume excluded_volume717200 ų
Envelope volume envelope_volume22545 ų
Hydration-shell volume shell_volume12820 ų
Envelope diameter envelope_diameter56.3 Å
Shell Rg shell_rg20.86 Å
Envelope Rg envelope_rg15.88 Å
Shape Rg shape_rg13.90 Å
Total Rg total_rg14.03 Å
Total atoms total_atoms80150
Residues n_residues5200
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax46.2 Å
Rg (real space) rg_real14.10 Å
Rg uncertainty (real space) rg_real_error0.28 Å
I(0) (real space) i0_real4.3220e+09
I(0) uncertainty (real space) i0_real_error4.4050e+07
Rg (reciprocal space) rg_reciprocal14.10 Å
I(0) (reciprocal space) i0_reciprocal4322000000.0000
Solution quality estimate total_estimate0.8715
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.6 Å
Skewness Skewness skewness0.537
Kurtosis Kurtosis kurtosis-0.041
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha232200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.806; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.926; Smooth: 0.983
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1bpva1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.1 — Fibronectin type III
Domain ID domain_idd1bpva2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1bpvA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
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8. Citations (1)

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9. Files and Curves (10)