2mhp

Solution structure of the major factor VIII binding region on von Willebrand factor

Method: SOLUTION NMR Dmax: 66.8 Å Quality: REASONABLE

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

von Willebrand factor

Homo sapiens

UniProt P04275

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 766–864 Fragment:;domains TIL' and E', UNP residues 766-864 ; No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.4;298 K;Pressure ambient NMR sample composition:300 mM [U-13C; U-15N] VWF TIL'E'-1, 20 mM sodium phosphate-2, 100 mM sodium chloride-3, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:300 mM [U-10% 13C] VWF TIL'E'-4, 20 mM sodium phosphate-5, 100 mM sodium chloride-6, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:300 mM [U-15N] VWF TIL'E'-7, 20 mM sodium phosphate-8, 100 mM sodium chloride-9, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:300 mM [U-13C; U-15N] VWF TIL'E'-10, 20 mM sodium phosphate-11, 100 mM sodium chloride-12, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:300 mM [U-15N] VWF TIL'E'-13, 20 mM sodium phosphate-14, 100 mM sodium chloride-15, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:300 mM [U-13C; U-15N] VWF TIL'E'-16, 20 mM sodium phosphate-17, 100 mM sodium chloride-18, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:300 mM [U-13C; U-15N] VWF TIL'E'-19, 20 mM sodium phosphate-20, 100 mM sodium chloride-21, 5 mg/mL Pf1 phage-22, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:300 mM [U-13C; U-15N] VWF TIL'E'-23, 20 mM sodium phosphate-24, 100 mM sodium chloride-25, 2 % w/v pentaethylene glycol dodecyl ether-26, 50 mM n-hexanol-27, 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.

46 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VWF_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–103; UniProt 766–864

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 2mhp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2mhp
Deposition date deposition_date2013-12-02
Structure title titleSolution structure of the major factor VIII binding region on von Willebrand factor
Keywords keywordsvon Willebrand factor, factor VIII, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.14
Radius of gyration Rg (electron density) rg_electron17.26
Forward intensity I(0) i0234285000.00
Molecular weight molecular_weight113360.0 kDa
Excluded volume excluded_volume136000 ų
Envelope volume envelope_volume27045 ų
Hydration-shell volume shell_volume13396 ų
Envelope diameter envelope_diameter71.2
Shell Rg shell_rg23.43
Envelope Rg envelope_rg19.25
Shape Rg shape_rg17.23
Total Rg total_rg17.54
Total atoms total_atoms15070
Residues n_residues1030
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 dmax66.8
Rg (real space) rg_real17.44
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real2.3430e+08
I(0) uncertainty (real space) i0_real_error3.4870e+06
Rg (reciprocal space) rg_reciprocal17.40
I(0) (reciprocal space) i0_reciprocal234300000.0000
Solution quality estimate total_estimate0.7346
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.8
Skewness Skewness skewness0.686
Kurtosis Kurtosis kurtosis-0.002
Angular range angular_range— – 0.4650 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha262600.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.455; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.182; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)