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2sta

ANIONIC SALMON TRYPSIN IN COMPLEX WITH SQUASH SEED INHIBITOR (CUCURBITA MAXIMA TRYPSIN INHIBITOR I)

Method: X-RAY DIFFRACTION Dmax: 54.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (TRYPSIN)

OrganismNot specified

UniProt P35031

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain E； UniProt 21–242 Not recorded PROTEIN (TRYPSIN INHIBITOR) × 1 （P01074） CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6；pH 6.0 Resolution 1.80 Å R-free 0.233

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.

Other PDB Difference from Current Entry 2STA Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BZX THE CRYSTAL STRUCTURE OF ANIONIC SALMON TRYPSIN IN COMPLEX WITH BOVINE PANCREATIC TRYPSIN INHIBITOR Deposited 1998-11-05 Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 21–242（222 aa）
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；0.1 M HEPES PH 7.5, 0.8-1.2 M POTASSIUM SODIUM TARTRATE
Resolution 2.10 Å R-free 0.238
1HJ8 1.00 AA Trypsin from Atlantic Salmon Deposited 2001-01-09 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–242（222 aa） Fragment：RESIDUES 21-242
Not recorded BEN BENZAMIDINE × 2 SO4 SULFATE ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.8；pH 5.80
Resolution 1.00 Å R-free 0.149
1UTJ Trypsin specificity as elucidated by LIE calculations, X-ray structures and association constant measurements Deposited 2003-12-09 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–242（242 aa）
Not recorded ABN BENZYLAMINE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；pH 6.00
Resolution 1.83 Å R-free 0.207
1UTK Trypsin specificity as elucidated by LIE calculations, X-ray structures and association constant measurements Deposited 2003-12-09 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–242（242 aa）
Not recorded SO4 SULFATE ION × 2 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；pH 6.00
Resolution 1.53 Å R-free 0.229
1UTL Trypsin specificity as elucidated by LIE calculations, X-ray structures and association constant measurements Deposited 2003-12-09 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain M 1–242（242 aa）
Not recorded PRA 3-PHENYLPROPYLAMINE × 1 CA CALCIUM ION × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；pH 6.00
Resolution 1.70 Å R-free 0.216
1UTM Trypsin specificity as elucidated by LIE calculations, X-ray structures and association constant measurements Deposited 2003-12-09 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–242（242 aa）
Not recorded PEA 2-PHENYLETHYLAMINE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；pH 6.00
Resolution 1.50 Å R-free 0.217
2STB ANIONIC SALMON TRYPSIN IN COMPLEX WITH SQUASH SEED INHIBITOR (CUCURBITA PEPO TRYPSIN INHIBITOR II) Deposited 1998-12-11 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 21–242（222 aa）
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；pH 6.0
Resolution 1.80 Å R-free 0.201
2TBS COLD-ADAPTION OF ENZYMES: STRUCTURAL COMPARISON BETWEEN SALMON AND BOVINE TRYPSINS Deposited 1994-01-14 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–242（222 aa）
Not recorded CA CALCIUM ION × 1 BEN BENZAMIDINE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRY1_SALSA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain E； PDBConstruct 1–222； UniProt 21–242

PROTEIN (TRYPSIN INHIBITOR)

OrganismNot specified

UniProt P01074

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain I； UniProt 1–29 Not recorded PROTEIN (TRYPSIN) × 1 （P35031） CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6；pH 6.0 Resolution 1.80 Å R-free 0.233

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.

Other PDB Difference from Current Entry 2STA Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CTI DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF THE TRYPSIN INHIBITOR FROM SQUASH SEEDS IN AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE AND A COMBINATION OF DISTANCE GEOMETRY AND DYNAMICAL SIMULATED ANNEALING Deposited 1990-08-28 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–29（29 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1LU0 Atomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal Coordination Deposited 2002-05-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–29（29 aa）
Chain B 1–29（29 aa）
Mutation：M8L Mutation：M8L ZN ZINC ION × 2 GOL GLYCEROL × 4 SO4 SULFATE ION × 2 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；PEG 8000, zinc sulfate, cacodylate, MPD, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K
Resolution 1.03 Å R-free 0.145
1PPE THE REFINED 2.0 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPSIN AND CMTI-I, A TRYPSIN INHIBITOR FROM SQUASH SEEDS (CUCURBITA MAXIMA): TOPOLOGICAL SIMILARITY OF THE SQUASH SEED INHIBITORS WITH THE CARBOXYPEPTIDASE A INHIBITOR FROM POTATOES Deposited 1991-10-24 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 1–29（29 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
2CTI DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF THE TRYPSIN INHIBITOR FROM SQUASH SEEDS IN AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE AND A COMBINATION OF DISTANCE GEOMETRY AND DYNAMICAL SIMULATED ANNEALING Deposited 1990-08-28 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–29（29 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
2V1V 3D STRUCTURE OF THE M8L MUTANT OF SQUASH TRYPSIN INHIBITOR CMTI-I Deposited 2007-05-30 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–29（29 aa）
Mutation：YES No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.6；298 K；Ionic strength (raw mmCIF value) 300
NMR sample composition 90% H2O/10% D2O
Resolution not provided
3CTI RELAXATION MATRIX REFINEMENT OF THE SOLUTION STRUCTURE OF SQUASH TRYPSIN INHIBITOR Deposited 1991-03-27 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–29（29 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITR1_CUCMA
Isoform —
PDB entities 2
Chains and sequence ranges Author chain I； PDBConstruct 1–29； UniProt 1–29

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 2sta

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2sta
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2sta
Deposition date deposition_date1998-12-10
Structure title titleANIONIC SALMON TRYPSIN IN COMPLEX WITH SQUASH SEED INHIBITOR (CUCURBITA MAXIMA TRYPSIN INHIBITOR I)
Keywords keywordsSERINE PROTEINASE, TRYPSIN INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.71 Å
Radius of gyration Rg (electron density) rg_electron16.67 Å
Forward intensity I(0) i014390300.00
Molecular weight molecular_weight27155.0 kDa
Excluded volume excluded_volume33335 ų
Envelope volume envelope_volume36906 ų
Hydration-shell volume shell_volume18074 ų
Envelope diameter envelope_diameter53.4 Å
Shell Rg shell_rg23.29 Å
Envelope Rg envelope_rg16.94 Å
Shape Rg shape_rg16.67 Å
Total Rg total_rg17.61 Å
Total atoms total_atoms1889
Residues n_residues248
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax54.4 Å
Rg (real space) rg_real17.56 Å
Rg uncertainty (real space) rg_real_error0.20 Å
I(0) (real space) i0_real1.4390e+07
I(0) uncertainty (real space) i0_real_error1.5020e+05
Rg (reciprocal space) rg_reciprocal17.57 Å
I(0) (reciprocal space) i0_reciprocal14390000.0000
Solution quality estimate total_estimate0.8994
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.5 Å
Skewness Skewness skewness0.075
Kurtosis Kurtosis kurtosis-0.483
Angular range angular_range— – 0.4500 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3212000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.902; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.999
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2stae_
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.2 — Eukaryotic proteases
Domain ID domain_idd2stai_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.2 — Plant inhibitors of proteinases and amylases
Family Family familyg.3.2.1 — Plant inhibitors of proteinases and amylases

CATH v4.4 (2 domains)

Domain ID domain_id2staE01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2staE02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
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8. Citations (1)

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9. Files and Curves (10)