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1u0p

Stable A-state hairpin of T4 fibritin foldon

Method: SOLUTION NMR Dmax: 50.2 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

fibritin

Enterobacteria phage Ox2

UniProt Q38650

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 458–484 Fragment：C-terminal domain No other associated polymer SOLUTION NMR NMR measurement conditions：pH 2；298 K；Ionic strength (raw mmCIF value) 20 mM；Pressure ambient NMR sample composition：250 uM foldon U/15N,13C, pH 2, 90% H2O, 10% D2O | 90% H2O/10% D2O 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 1U0P Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2IBL Crystal structure of a helper molecule (HT-mf-thromb) based on mini-fibritin (mf) crystal structure (pdb:1OX3). Deposited 2006-09-11 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 456–484（29 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10.5；293 K；30% PEG 400, 0.1 M TrisHCl, 0.2 M magnesium chloride, pH 10.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K
Resolution 1.32 Å R-free 0.170
5C69 Crystal Structure of Prefusion-stabilized RSV F variant PR-DM Deposited 2015-06-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 459–484（26 aa） Fragment：F2 subunit, F1 subunit ectodomain
Mutation：N67I, S215P, I379V, M447V SO4 SULFATE ION × 42 NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID × 12 CL CHLORIDE ION × 30 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 9.5；293 K；1.24M K/Na tartrate, 0.2M LiSO4, 0.1M CHES pH 9.5
Resolution 2.30 Å R-free 0.217
5C6B Crystal Structure of Prefusion-stabilized RSV F variant SC-TM Deposited 2015-06-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 6 PDB declaration: hexameric
Chain F 458–484（27 aa） Fragment：ectodomain
Mutation：N67I, S215P, E487Q, I379V, M447V,N67I, S215P, E487Q, I379V, M447V NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID × 6 SO4 SULFATE ION × 24 CL CHLORIDE ION × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 9.5；293 K；1.34M K/Na tartrate, 0.2M LiSO4, 0.1M CHES pH 9.5
Resolution 2.40 Å R-free 0.211
5TPN Crystal structure of RSV F in complex with human antibody hRSV90 Deposited 2016-10-20 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 458–484（27 aa）
Mutation：N67I, S215P, I379V, M447V No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；30% PEG, 400/200 mM MgCl2, 6H2O/100 mM HEPES pH 7.5
Resolution 3.14 Å R-free 0.262

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q38650_BPOX2
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–27； UniProt 458–484

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 1u0p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1u0p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1u0p
Deposition date deposition_date2004-07-14
Structure title titleStable A-state hairpin of T4 fibritin foldon
Keywords keywordsbeta-hairpin, hairpin, folding nucleus, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier12.42 Å
Radius of gyration Rg (electron density) rg_electron12.42 Å
Forward intensity I(0) i013795700.00
Molecular weight molecular_weight30805.0 kDa
Excluded volume excluded_volume38986 ų
Envelope volume envelope_volume15974 ų
Hydration-shell volume shell_volume9418 ų
Envelope diameter envelope_diameter49.1 Å
Shell Rg shell_rg19.96 Å
Envelope Rg envelope_rg16.12 Å
Shape Rg shape_rg12.42 Å
Total Rg total_rg13.19 Å
Total atoms total_atoms4290
Residues n_residues270
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 dmax50.2 Å
Rg (real space) rg_real12.60 Å
Rg uncertainty (real space) rg_real_error0.63 Å
I(0) (real space) i0_real1.3800e+07
I(0) uncertainty (real space) i0_real_error1.5280e+05
Rg (reciprocal space) rg_reciprocal12.59 Å
I(0) (reciprocal space) i0_reciprocal13800000.0000
Solution quality estimate total_estimate0.7047
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.1 Å
Skewness Skewness skewness0.424
Kurtosis Kurtosis kurtosis-0.273
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12020.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.333; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.161; Smooth: 0.997
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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_idd1u0pa1
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.17 — Fibritin
Family Family familyh.1.17.1 — Fibritin
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8. Citations (1)

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9. Files and Curves (10)