4cz4

HP24stab derived from the villin headpiece subdomain

Method: SOLUTION NMR Dmax: 25.4 Å Quality: GOOD

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

VILLIN-1

OrganismNot specified

UniProt P02640

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 803–826 Fragment:RESIDUES 803-826 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.5;288 K;Ionic strength (raw mmCIF value) 50;Pressure 1 NMR sample composition:10% D2O/90% WATER 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.

45 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VILI_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–25; UniProt 803–826

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 4cz4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4cz4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4cz4
Deposition date deposition_date2014-04-16
Structure title titleHP24stab derived from the villin headpiece subdomain
Keywords keywordsACTIN-BINDING PROTEIN, VILLIN, SUBDOMAIN, SUPERSECONDARY, CHICKEN, HYPERSTABLE; ACTIN-BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier8.08
Radius of gyration Rg (electron density) rg_electron8.24
Forward intensity I(0) i039622500.00
Molecular weight molecular_weight57090.0 kDa
Excluded volume excluded_volume73420 ų
Envelope volume envelope_volume5804 ų
Hydration-shell volume shell_volume5794 ų
Envelope diameter envelope_diameter28.8
Shell Rg shell_rg13.89
Envelope Rg envelope_rg9.47
Shape Rg shape_rg8.23
Total Rg total_rg8.53
Total atoms total_atoms8240
Residues n_residues480
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 dmax25.4
Rg (real space) rg_real8.07
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real3.9620e+07
I(0) uncertainty (real space) i0_real_error4.2850e+05
Rg (reciprocal space) rg_reciprocal8.07
I(0) (reciprocal space) i0_reciprocal39620000.0000
Solution quality estimate total_estimate0.8548
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary13.8
Skewness Skewness skewness-0.006
Kurtosis Kurtosis kurtosis-0.964
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1795.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.798; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.808; Smooth: 0.908

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)