9pdc

Porcine Trypsin grown from PEG and Complexed with Crystallization Additives II

Method: X-RAY DIFFRACTION Dmax: 74.3 Å Quality: GOOD

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

Trypsin

Sus scrofa

UniProt P00761

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 1–231 Not recorded CA CALCIUM ION × 1 TLA L(+)-TARTARIC ACID × 2 PEG DI(HYDROXYETHYL)ETHER × 28 PG4 TETRAETHYLENE GLYCOL × 10 PG6 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE × 2 PG5 1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE × 1 BEN BENZAMIDINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;295 K;Sitting drop vapor diffusion in Cryschem plates. Reservoirs 30% PEG 3350 buffered with 0.1 M HEPES at pH 6.5. Drops 3 ul of reservoir, 2 ul of additive mix ( TACSIMATE, PEG 3350), 3 ul of 40 mg/ml stock protein solution buffered with 0.1 M HEPES pH 6.5. Resolution 1.27 Å R-free 0.154

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.

44 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRYP_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–231; UniProt 1–231

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 9pdc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9pdc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9pdc
Deposition date deposition_date2025-06-30
最后修订 last_revision2026-05-27
Structure title titlePorcine Trypsin grown from PEG and Complexed with Crystallization Additives II
Keywords keywordspig, trypsin, crystallization, additives, Silver Bullets, TACSIMATE, PEG, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.12
Radius of gyration Rg (electron density) rg_electron18.18
Forward intensity I(0) i015442900.00
Molecular weight molecular_weight29564.0 kDa
Excluded volume excluded_volume37249 ų
Envelope volume envelope_volume46751 ų
Hydration-shell volume shell_volume20510 ų
Envelope diameter envelope_diameter72.2
Shell Rg shell_rg25.69
Envelope Rg envelope_rg19.27
Shape Rg shape_rg18.07
Total Rg total_rg19.69
Total atoms total_atoms4183
Residues n_residues223
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 dmax74.3
Rg (real space) rg_real19.03
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real1.5440e+07
I(0) uncertainty (real space) i0_real_error2.1440e+05
Rg (reciprocal space) rg_reciprocal19.05
I(0) (reciprocal space) i0_reciprocal15440000.0000
Solution quality estimate total_estimate0.7934
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.264
Kurtosis Kurtosis kurtosis-0.223
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6953000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.474; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.888; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)