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1g1c

I1 DOMAIN FROM TITIN

Method: X-RAY DIFFRACTION Dmax: 90.2 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

IMMUNOGLOBULIN-LIKE DOMAIN I1 FROM 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 2027–2125 Fragment：MOST N-TERMINAL IG DOMAIN, RESIDUES 2027-2125 No other associated polymer 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
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 2027–2125 Fragment：MOST N-TERMINAL IG DOMAIN, RESIDUES 2027-2125 No other associated polymer 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

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 1G1C Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BPV TITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES Deposited 1998-08-11 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 14859–14961（103 aa） Fragment：71 TH DOMAIN FROM THE A-BAND
Mutation：I9V No recorded non-water small molecule 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
1NCT TITIN MODULE M5, N-TERMINALLY EXTENDED, NMR Deposited 1996-08-13 Different construct Different experimental method Different experimental conditions Different structure-quality metrics 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 experimental method Different experimental conditions Different structure-quality metrics 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 experimental method Different experimental conditions Different structure-quality metrics 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 experimental method Different experimental conditions Different structure-quality metrics 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 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 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 7 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 1–99； UniProt 2027–2125 Author chain B； PDBConstruct 1–99； UniProt 2027–2125

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 1g1c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1g1c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1g1c
Deposition date deposition_date2000-10-11
Structure title titleI1 DOMAIN FROM TITIN
Keywords keywordsimmunoglobulin domain, Beta-sandwhich, I-set, structural protein; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier25.59 Å
Radius of gyration Rg (electron density) rg_electron25.20 Å
Forward intensity I(0) i08721760.00
Molecular weight molecular_weight22217.0 kDa
Excluded volume excluded_volume27655 ų
Envelope volume envelope_volume36126 ų
Hydration-shell volume shell_volume12716 ų
Envelope diameter envelope_diameter91.7 Å
Shell Rg shell_rg30.58 Å
Envelope Rg envelope_rg24.74 Å
Shape Rg shape_rg25.17 Å
Total Rg total_rg25.96 Å
Total atoms total_atoms1564
Residues n_residues196
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 dmax90.2 Å
Rg (real space) rg_real25.89 Å
Rg uncertainty (real space) rg_real_error1.11 Å
I(0) (real space) i0_real8.7220e+06
I(0) uncertainty (real space) i0_real_error1.4300e+05
Rg (reciprocal space) rg_reciprocal25.80 Å
I(0) (reciprocal space) i0_reciprocal8721000.0000
Solution quality estimate total_estimate0.7261
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.4 Å
Skewness Skewness skewness0.426
Kurtosis Kurtosis kurtosis-0.680
Angular range angular_range— – 0.3100 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1278000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.408; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.220; Smooth: 0.994
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1g1ca_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.4 — I set domains
Domain ID domain_idd1g1cb_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.4 — I set domains

CATH v4.4 (2 domains)

Domain ID domain_id1g1cA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1g1cB00
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)