1vfc

Solution Structure Of The DNA Complex Of Human Trf2

Method: SOLUTION NMR Dmax: 55.6 Å Quality: REASONABLE

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

Telomeric repeat binding factor 2

Homo sapiens

UniProt Q15554

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–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 438–500 Fragment:DNA BINDING DOMAIN Short G-rich strand × 1 Short C-rich starnd × 1 SOLUTION NMR NMR measurement conditions:pH 6.9;303 K;Ionic strength (raw mmCIF value) 0.005M;Pressure ambient NMR sample composition:1.0-1.5mM TRF2 labeled with 15N and 13C, and DNA; 5mM potassium phosphate buffer, 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:1.0-1.5mM TRF2 labeled with 15N,and DNA; 5mM potassium phosphate buffer, 90% H2O, 10% D2O | 90% H2O/10% D2O 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.

17 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TERF2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–63; UniProt 438–500

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 1vfc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1vfc
Deposition date deposition_date2004-04-12
Structure title titleSolution Structure Of The DNA Complex Of Human Trf2
Keywords keywordsMyb, helix-turn-helix, telomere, protein-DNA complex, STRUCTURAL PROTEIN-DNA COMPLEX; STRUCTURAL PROTEIN/DNA
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.81
Radius of gyration Rg (electron density) rg_electron15.74
Forward intensity I(0) i02397460000.00
Molecular weight molecular_weight306900.0 kDa
Excluded volume excluded_volume338900 ų
Envelope volume envelope_volume41133 ų
Hydration-shell volume shell_volume18418 ų
Envelope diameter envelope_diameter63.5
Shell Rg shell_rg25.27
Envelope Rg envelope_rg19.76
Shape Rg shape_rg15.69
Total Rg total_rg15.98
Total atoms total_atoms36180
Residues n_residues1780
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax55.6
Rg (real space) rg_real15.80
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real2.3970e+09
I(0) uncertainty (real space) i0_real_error3.0410e+07
Rg (reciprocal space) rg_reciprocal15.80
I(0) (reciprocal space) i0_reciprocal2397000000.0000
Solution quality estimate total_estimate0.6374
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.3
Skewness Skewness skewness0.317
Kurtosis Kurtosis kurtosis-0.278
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha565400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.753; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.920; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1vfca1
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.1 — Homeodomain-like
Family Family familya.4.1.4 — DNA-binding domain of telomeric protein

CATH v4.4 (1 domains)

Domain ID domain_id1vfcA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily60 — Homeodomain-like

8. Citations (1)

9. Files and Curves (10)