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1ba4

;THE SOLUTION STRUCTURE OF AMYLOID BETA-PEPTIDE (1-40) IN A WATER-MICELLE ENVIRONMENT. IS THE MEMBRANE-SPANNING DOMAIN WHERE WE THINK IT IS? NMR, 10 STRUCTURES ;

Method: SOLUTION NMR Dmax: 43.6 Å Quality: REASONABLE

SAXS Profile

SAXS profile for 1ba4

P(r) Distribution

P(r) distribution for 1ba4

1. Structure Basics

entry_id1ba4
deposition_date1998-04-07
title;THE SOLUTION STRUCTURE OF AMYLOID BETA-PEPTIDE (1-40) IN A WATER-MICELLE ENVIRONMENT. IS THE MEMBRANE-SPANNING DOMAIN WHERE WE THINK IT IS? NMR, 10 STRUCTURES ;
keywords;GLYCOPROTEIN, AMYLOID BETA-PEPTIDE, ALZHEIMER'S DISEASE, SDS-MICELLES ;; GLYCOPROTEIN
methodSOLUTION NMR

Download Data

2. SAXS Parameters (CRYSOL)

rg_guinier17.08
rg_electron16.52
i030201100.00
molecular_weight43268.0 kDa
excluded_volume53811 ų
envelope_volume30869 ų
shell_volume13879 ų
envelope_diameter73.8
shell_rg24.99
envelope_rg20.56
shape_rg16.50
total_rg17.36
total_atoms5980
n_residues400
n_harmonics20
q_range— – 0.5000 −1
n_points101
shell_typedirectional
solvent_density0.3340 e/ų
contrast_shell0.0300 e/ų
crysol_version4.1.3

3. P(r) Analysis (GNOM)

dmax43.6
rg_real15.86
rg_real_error0.08
i0_real2.8670e+07
i0_real_error2.7680e+05
rg_reciprocal17.31
i0_reciprocal30200000.0000
total_estimate0.6698
solution_quality REASONABLE a REASONABLE solution
n_peaks1
r_peak_primary18.9
skewness0.174
kurtosis-0.770
angular_range— – 0.4650 −1
current_alpha4.2410
highest_alpha25890.0000
n_real_points77
gnom_version4.1.3
quality_criteria AN1: 0.009; Oscil: 1.000; Stabil: 0.978; Sysdev: 0.000; Positv: 1.000; Valcen: 0.777; Smooth: 0.000

4. Crystallography & Experiment

5. Entities & Polymer Info (1)

6. Citations (1)

7. Files & Curves (10)