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1vtp

VACUOLAR TARGETING PEPTIDE FROM NA-PROPI

Method: SOLUTION NMR Dmax: 44.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

VACUOLAR TARGETING PEPTIDE

Nicotiana alata

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 256–281 Fragment：C-TERMINAL RESIDUES 29 - 54 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 1VTP 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 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 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
1QH2 CHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA ALATA Deposited 1999-05-11 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 30–47（18 aa）
Chain B 345–372（28 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.2；313 K
NMR sample composition 10% D2O/90% H2O
Resolution not provided
1TIH TRYPSIN INHIBITOR (T1) FROM NICOTIANA ALATA Deposited 1995-08-03 Different construct 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
2JYY Solution structure of C8A/C37A-T1 from Nicotiana alata Deposited 2007-12-20 Different construct Different mutation/modification 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
Chains and sequence ranges Author chain A； PDBConstruct 1–26； UniProt 256–281

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 1vtp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1vtp
Deposition date deposition_date1995-11-14
Structure title titleVACUOLAR TARGETING PEPTIDE FROM NA-PROPI
Keywords keywordsNICOTIANA ALATA PROTEINASE INHIBITORS, TARGETING PEPTIDE; TARGETING PEPTIDE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier11.45 Å
Radius of gyration Rg (electron density) rg_electron11.81 Å
Forward intensity I(0) i051211300.00
Molecular weight molecular_weight57422.0 kDa
Excluded volume excluded_volume70924 ų
Envelope volume envelope_volume11141 ų
Hydration-shell volume shell_volume7500 ų
Envelope diameter envelope_diameter48.9 Å
Shell Rg shell_rg18.20 Å
Envelope Rg envelope_rg14.69 Å
Shape Rg shape_rg11.74 Å
Total Rg total_rg12.28 Å
Total atoms total_atoms7920
Residues n_residues520
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 dmax44.8 Å
Rg (real space) rg_real11.75 Å
Rg uncertainty (real space) rg_real_error0.66 Å
I(0) (real space) i0_real5.1210e+07
I(0) uncertainty (real space) i0_real_error6.6930e+05
Rg (reciprocal space) rg_reciprocal11.73 Å
I(0) (reciprocal space) i0_reciprocal51210000.0000
Solution quality estimate total_estimate0.6762
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary7.4 Å
Skewness Skewness skewness0.582
Kurtosis Kurtosis kurtosis-0.390
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5114.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.269; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.017; Smooth: 0.964
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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_idd1vtpa_
Class classj — Peptides
Fold Fold foldj.36 — Topogenic peptides
Superfamily Superfamily superfamilyj.36.2 — Vacuolar targeting peptide from NA-PROPI (residues 29-54)
Family Family familyj.36.2.1 — Vacuolar targeting peptide from NA-PROPI (residues 29-54)
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8. Citations (3)

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9. Files and Curves (10)