2mvw

Solution structure of the TRIM19 B-box1 (B1) of human promyelocytic leukemia (PML)

Method: SOLUTION NMR Dmax: 57.6 Å Quality: REASONABLE

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

Protein PML

Homo sapiens

UniProt P29590

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 120–168 Chain B; UniProt 120–168 Fragment:UNP residues 120-168 ZN ZINC ION × 4 SOLUTION NMR NMR measurement conditions:pH 7;298 K;Pressure ambient NMR sample composition:1 mM [U-99% 13C; U-99% 15N] PML B1 box, 25 mM [U-98% 2H] TRIS, 100 mM sodium chloride, 0.2 mM TCEP, 1 mM zinc chloride, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-99% 13C; U-99% 15N] PML B1 box, 25 mM [U-98% 2H] TRIS, 100 mM sodium chloride, 0.2 mM TCEP, 1 mM zinc chloride, 100% D2O | 100% D2O NMR sample composition:0.5 mM [U-99% 13C; U-99% 15N] PML B1 box, 0.5 mM PML B1 box, 25 mM [U-98% 2H] TRIS, 100 mM sodium chloride, 0.2 mM TCEP, 1 mM zinc chloride, 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.

17 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PML_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–51; UniProt 120–168 Author chain B; PDBConstruct 3–51; UniProt 120–168

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 2mvw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2mvw
Deposition date deposition_date2014-10-17
Structure title titleSolution structure of the TRIM19 B-box1 (B1) of human promyelocytic leukemia (PML)
Keywords keywordsPML, B box, TRIM19, METAL BINDING PROTEIN, E3 ligase; METAL BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.26
Radius of gyration Rg (electron density) rg_electron15.27
Forward intensity I(0) i0964646000.00
Molecular weight molecular_weight242500.0 kDa
Excluded volume excluded_volume293850 ų
Envelope volume envelope_volume45651 ų
Hydration-shell volume shell_volume19242 ų
Envelope diameter envelope_diameter65.8
Shell Rg shell_rg26.69
Envelope Rg envelope_rg21.22
Shape Rg shape_rg15.32
Total Rg total_rg15.38
Total atoms total_atoms32040
Residues n_residues2040
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 dmax57.6
Rg (real space) rg_real15.38
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real9.6460e+08
I(0) uncertainty (real space) i0_real_error1.2600e+07
Rg (reciprocal space) rg_reciprocal15.37
I(0) (reciprocal space) i0_reciprocal964600000.0000
Solution quality estimate total_estimate0.7218
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.8
Skewness Skewness skewness0.590
Kurtosis Kurtosis kurtosis0.273
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha265200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.557; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.709; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)