4fc1

Ultra-high resolution neutron structure of crambin at room-temperature

Method: NEUTRON DIFFRACTION Dmax: 40.4 Å Quality: GOOD

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

Crambin

OrganismNot specified

UniProt P01542

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 1–46 Not recorded No other associated polymer NEUTRON DIFFRACTION X-ray crystallization conditions:290 K;large crystals were obtained in 1mL crystallization drops containing 20-30mg/ml protein in 80% EtOH/H2O; the well solution was 60% EtOH/H2O; no mixing with well solution was done., VAPOR DIFFUSION, SITTING DROP, temperature 290K Resolution 1.10 Å R-free 0.253

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.

26 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CRAM_CRAAB
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–46; UniProt 1–46

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 4fc1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4fc1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4fc1
Deposition date deposition_date2012-05-23
Structure title titleUltra-high resolution neutron structure of crambin at room-temperature
Keywords keywordsH/D exchange, neutron structure, UNKNOWN FUNCTION; UNKNOWN FUNCTION
Experimental Method methodNEUTRON DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier11.50
Radius of gyration Rg (electron density) rg_electron10.15
Forward intensity I(0) i0819815.00
Molecular weight molecular_weight5702.0 kDa
Excluded volume excluded_volume7019 ų
Envelope volume envelope_volume8486 ų
Hydration-shell volume shell_volume7197 ų
Envelope diameter envelope_diameter37.5
Shell Rg shell_rg15.67
Envelope Rg envelope_rg11.00
Shape Rg shape_rg10.50
Total Rg total_rg11.07
Total atoms total_atoms768
Residues n_residues46
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 dmax40.4
Rg (real space) rg_real11.50
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real8.1980e+05
I(0) uncertainty (real space) i0_real_error9.4160e+03
Rg (reciprocal space) rg_reciprocal11.50
I(0) (reciprocal space) i0_reciprocal819800.0000
Solution quality estimate total_estimate0.8606
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.3
Skewness Skewness skewness0.364
Kurtosis Kurtosis kurtosis-0.148
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha222000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.754; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.932; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4fc1a_
Class classg — Small proteins
Fold Fold foldg.13 — Crambin-like
Superfamily Superfamily superfamilyg.13.1 — Crambin-like
Family Family familyg.13.1.1 — Crambin-like

CATH v4.4 (1 domains)

Domain ID domain_id4fc1A00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1350 — Crambin
Homologous superfamily homologous superfamily10 — Thionin-like

8. Citations (1)

9. Files and Curves (10)