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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

Method: SOLUTION NMR Dmax: 32.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

TRYPSIN INHIBITOR

Cucurbita maxima

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–29 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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.

Other PDB Difference from Current Entry 2CTI 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 Parsed fields agree 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 method 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 oligomeric state Different experimental method 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
2STA ANIONIC SALMON TRYPSIN IN COMPLEX WITH SQUASH SEED INHIBITOR (CUCURBITA MAXIMA TRYPSIN INHIBITOR I) Deposited 1998-12-10 Different oligomeric state Different ligand/ion Different experimental method 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 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；pH 6.0
Resolution 1.80 Å R-free 0.233
2V1V 3D STRUCTURE OF THE M8L MUTANT OF SQUASH TRYPSIN INHIBITOR CMTI-I Deposited 2007-05-30 Different mutation/modification Different experimental conditions 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 Parsed fields agree 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 1
Chains and sequence ranges Author chain A； 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 2cti

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2cti
Deposition date deposition_date1990-08-28
Structure title titleDETERMINATION 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
Keywords keywordsPROTEINASE INHIBITOR (TRYPSIN); PROTEINASE INHIBITOR (TRYPSIN)
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier8.70 Å
Radius of gyration Rg (electron density) rg_electron8.63 Å
Forward intensity I(0) i05458020.00
Molecular weight molecular_weight16369.0 kDa
Excluded volume excluded_volume19776 ų
Envelope volume envelope_volume7375 ų
Hydration-shell volume shell_volume6702 ų
Envelope diameter envelope_diameter32.4 Å
Shell Rg shell_rg14.98 Å
Envelope Rg envelope_rg10.28 Å
Shape Rg shape_rg8.68 Å
Total Rg total_rg9.27 Å
Total atoms total_atoms2180
Residues n_residues145
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 dmax32.8 Å
Rg (real space) rg_real8.75 Å
Rg uncertainty (real space) rg_real_error0.41 Å
I(0) (real space) i0_real5.4580e+06
I(0) uncertainty (real space) i0_real_error5.6890e+04
Rg (reciprocal space) rg_reciprocal8.75 Å
I(0) (reciprocal space) i0_reciprocal5458000.0000
Solution quality estimate total_estimate0.8064
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary9.5 Å
Skewness Skewness skewness0.512
Kurtosis Kurtosis kurtosis0.042
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17790.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.626; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.669; Smooth: 0.933
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2ctia_
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
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8. Citations (2)

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9. Files and Curves (10)