7p4r

Ultra High Resolution X-ray Structure of Orthorhombic Bovine Pancreatic Ribonuclease at 100K

Method: X-RAY DIFFRACTION Dmax: 52.5 Å Quality: GOOD

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

Ribonuclease pancreatic

Bos taurus

UniProt P61823

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 AAA; UniProt 27–150 Mutation:None EOH ETHANOL × 11 SO4 SULFATE ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7;277 K;100mg of powdered Ribonuclease A in 1ml of distilled water dissolved in 2ml of ice cold absolute ethanol. Resolution 0.85 Å R-free 0.129

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.

333 other PDB entries and 495 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNAS1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain AAA; PDBConstruct 1–124; UniProt 27–150

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 7p4r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7p4r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7p4r
Deposition date deposition_date2021-07-12
Structure title titleUltra High Resolution X-ray Structure of Orthorhombic Bovine Pancreatic Ribonuclease at 100K
Keywords keywordsNucleic acid, RNA, multiple conformations, water structure, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.69
Radius of gyration Rg (electron density) rg_electron14.66
Forward intensity I(0) i05201920.00
Molecular weight molecular_weight14681.0 kDa
Excluded volume excluded_volume17670 ų
Envelope volume envelope_volume20937 ų
Hydration-shell volume shell_volume12257 ų
Envelope diameter envelope_diameter52.6
Shell Rg shell_rg20.19
Envelope Rg envelope_rg15.12
Shape Rg shape_rg14.62
Total Rg total_rg15.77
Total atoms total_atoms1984
Residues n_residues124
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 dmax52.5
Rg (real space) rg_real15.64
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real5.2020e+06
I(0) uncertainty (real space) i0_real_error6.4690e+04
Rg (reciprocal space) rg_reciprocal15.64
I(0) (reciprocal space) i0_reciprocal5202000.0000
Solution quality estimate total_estimate0.7999
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.9
Skewness Skewness skewness0.253
Kurtosis Kurtosis kurtosis-0.403
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1007000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.812; Stabil: 0.991; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (2)

9. Files and Curves (10)