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1qh2

CHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA ALATA

Method: SOLUTION NMR Dmax: 36.9 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (TRYPSIN INHIBITOR C2)

OrganismNot specified

UniProt Q40378

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 30–47 Chain B； UniProt 345–372 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 5.2；313 K NMR sample composition：10% D2O/90% H2O 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 1QH2 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CE3 PUTATIVE ANCESTRAL PROTEIN ENCODED BY A SINGLE SEQUENCE REPEAT OF THE MULTIDOMAIN PROTEINASE INHIBITOR FROM NICOTIANA ALATA Deposited 1999-03-14 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 29–82（54 aa） Fragment：FIRST SEQUENCE REPEAT
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.8；313 K；Pressure 1
NMR sample composition 1 mM peptide | 90% H2O/10% D2O
Resolution not provided
1FYB SOLUTION STRUCTURE OF C1-T1, A TWO-DOMAIN PROTEINASE INHIBITOR DERIVED FROM THE CIRCULAR PRECURSOR PROTEIN NA-PROPI FROM NICOTIANA ALATA Deposited 2000-09-28 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 54–164（111 aa） Fragment：DOMAINS 1 AND 2 (C1 AND T1) FROM THE SIX-DOMAIN PRECURSOR PROTEIN NA-PROPI
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.8；313 K；Ionic strength (raw mmCIF value) 0；Pressure 1
NMR measurement conditions pH 5.8；313 K；Ionic strength (raw mmCIF value) 0；Pressure 1
NMR measurement conditions pH 5.8；313 K；Ionic strength (raw mmCIF value) 0；Pressure 1
NMR sample composition 1mM C1-T1, unlabeled | 90% H2O/10% D2O
NMR sample composition 1mM C1-T1, unlabeled | 99% D2O
NMR sample composition 1mM C1-T1, U-15N,13C | 90% H2O/10% D2O
Resolution not provided
1TIH TRYPSIN INHIBITOR (T1) FROM NICOTIANA ALATA Deposited 1995-08-03 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 112–164（53 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1VTP VACUOLAR TARGETING PEPTIDE FROM NA-PROPI Deposited 1995-11-14 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 256–281（26 aa） Fragment：C-TERMINAL RESIDUES 29 - 54
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
2JYY Solution structure of C8A/C37A-T1 from Nicotiana alata Deposited 2007-12-20 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 112–164（53 aa） Fragment：UNP residues 112-164
Mutation：C8A, C37A No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.8；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 0.13 mM C8A/C37A-T1, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.13 mM C8A/C37A-T1, 100% D2O | 100% D2O
Resolution not provided

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q40378_NICAL
Isoform —
PDB entities 1, 2
Chains and sequence ranges Author chain A； PDBConstruct 1–18； UniProt 30–47 Author chain B； PDBConstruct 1–28； UniProt 345–372

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 1qh2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1qh2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1qh2
Deposition date deposition_date1999-05-11
Structure title titleCHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA ALATA
Keywords keywordsPROTEINASE INHIBITOR (CHYMOTRYPSIN), SERINE PROTEINASE INHIBITOR, POTATO II TRYPSIN INHIBITOR, NICOTIANA ALATA, HYDROLASE INHIBITOR; HYDROLASE INHIBITOR
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier10.61 Å
Radius of gyration Rg (electron density) rg_electron9.64 Å
Forward intensity I(0) i0717768.00
Molecular weight molecular_weight5019.0 kDa
Excluded volume excluded_volume6067 ų
Envelope volume envelope_volume6319 ų
Hydration-shell volume shell_volume5972 ų
Envelope diameter envelope_diameter36.0 Å
Shell Rg shell_rg14.62 Å
Envelope Rg envelope_rg10.30 Å
Shape Rg shape_rg9.61 Å
Total Rg total_rg11.09 Å
Total atoms total_atoms671
Residues n_residues46
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 dmax36.9 Å
Rg (real space) rg_real10.60 Å
Rg uncertainty (real space) rg_real_error0.40 Å
I(0) (real space) i0_real7.1780e+05
I(0) uncertainty (real space) i0_real_error8.5200e+03
Rg (reciprocal space) rg_reciprocal10.60 Å
I(0) (reciprocal space) i0_reciprocal717800.0000
Solution quality estimate total_estimate0.8672
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.5 Å
Skewness Skewness skewness0.301
Kurtosis Kurtosis kurtosis-0.170
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46570.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.798; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.940; Smooth: 0.947
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1qh2.1
Class classg — Small proteins
Fold Fold foldg.69 — Plant proteinase inhibitors
Superfamily Superfamily superfamilyg.69.1 — Plant proteinase inhibitors
Family Family familyg.69.1.1 — Plant proteinase inhibitors
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8. Citations (2)

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9. Files and Curves (10)