1c3t

ROTAMER STRAIN AS A DETERMINANT OF PROTEIN STRUCTURAL SPECIFICITY

Method: SOLUTION NMR Dmax: 43.1 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (1D8 UBIQUITIN)

Homo sapiens

UniProt P62988

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 87–162 Mutation:I3L,I13L,L15V,V17L,I23V,V26L,I61L,L67I No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5.8;303 K;Ionic strength (raw mmCIF value) 50 mM;Pressure 1 NMR sample composition:2 MM 13C/15N 1D8 UBIQUITIN, 25 MM SODIUM PHOSPHATE, 25 MM SODIUM ACETATE (D3), 0.02% SODIUM AZIDE, PH 5.8 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.

83 other PDB entries and 138 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBIQ_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–76; UniProt 87–162

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 1c3t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c3t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c3t
Deposition date deposition_date1999-07-28
Structure title titleROTAMER STRAIN AS A DETERMINANT OF PROTEIN STRUCTURAL SPECIFICITY
Keywords keywordsPROTEIN DESIGN, HYDROPHOBIC CORE, PACKING, ROTAMERS, ROC, UBIQUITIN, DE NOVO PROTEIN; DE NOVO PROTEIN
Experimental Method methodSOLUTION NMR

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier12.26
Radius of gyration Rg (electron density) rg_electron11.72
Forward intensity I(0) i0395686000.00
Molecular weight molecular_weight171300.0 kDa
Excluded volume excluded_volume216330 ų
Envelope volume envelope_volume19233 ų
Hydration-shell volume shell_volume11929 ų
Envelope diameter envelope_diameter47.2
Shell Rg shell_rg19.59
Envelope Rg envelope_rg14.39
Shape Rg shape_rg11.70
Total Rg total_rg11.97
Total atoms total_atoms24640
Residues n_residues1520
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax43.1
Rg (real space) rg_real12.18
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real3.9570e+08
I(0) uncertainty (real space) i0_real_error4.8730e+06
Rg (reciprocal space) rg_reciprocal12.18
I(0) (reciprocal space) i0_reciprocal395700000.0000
Solution quality estimate total_estimate0.7982
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.4
Skewness Skewness skewness0.129
Kurtosis Kurtosis kurtosis0.103
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha201600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.460; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1c3ta_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related

CATH v4.4 (1 domains)

Domain ID domain_id1c3tA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (3)

9. Files and Curves (10)