;9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY ;

entry_id	1dyl
deposition_date	2000-02-02
title	;9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY ;
keywords	;VIRUS/VIRAL PROTEIN, ALPHAVIRUS, SFV, CRYO-EM, IMAGE RECONSTRUCTION, ENVELOPED VIRUS, CAPSID PROTEIN, ICOSAHEDRAL VIRUS, VIRUS-VIRAL PROTEIN complex ;; VIRUS/VIRAL PROTEIN
method	ELECTRON MICROSCOPY

rg_guinier	34.99 Å
rg_electron	35.02 Å
i0	69599700.00
molecular_weight	64833.0 kDa
excluded_volume	80630 ų
envelope_volume	111940 ų
shell_volume	29546 ų
envelope_diameter	121.3 Å
shell_rg	37.49 Å
envelope_rg	34.54 Å
shape_rg	34.99 Å
total_rg	35.31 Å
total_atoms	4563
n_residues	596
n_harmonics	20
q_range	— – 0.5000 Å−1
n_points	101
shell_type	directional
solvent_density	0.3340 e/ų
contrast_shell	0.0300 e/ų
crysol_version	4.1.3

dmax	117.3 Å
rg_real	35.14 Å
rg_real_error	1.34 Å
i0_real	6.9600e+07
i0_real_error	1.2790e+06
rg_reciprocal	35.05 Å
i0_reciprocal	69590000.0000
total_estimate	0.8303
solution_quality	GOOD a GOOD solution
n_peaks	2
r_peak_primary	49.5 Å
skewness	0.319
kurtosis	-0.483
angular_range	— – 0.2250 Å−1
current_alpha	0.0000
highest_alpha	6672000.0000
n_real_points	46
gnom_version	4.1.3
quality_criteria	AN1: 0.000; Oscil: 0.777; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.793; Smooth: 0.665

Unit Cell

length_a	1.000 Å
length_b	1.000 Å
length_c	1.000 Å
angle_alpha	90.00 °
angle_beta	90.00 °
angle_gamma	90.00 °
z_pdb	1

Symmetry

space_group	P 1
int_tables_number	1
crystal_system	—

Refinement

resolution	9.000 Å
resolution_low	— Å
r_factor	—
r_work	—
r_free	—

EM 3D

resolution	9.00 Å
resolution_method	;MODEL-BASED, POLAR-FOURIER- TRANSFORMATION (FULLER ET AL. 1996, J.STRUC.BIOL. 116, 48-55; BAKER AND CHENG 1996, J.STRUC.BIOL. 116, 120- 130) MODEL-BASED CROSS COMMOM LINES SEARCH AND REFINEMENT (CROWTHER ET AL. 1970, NATURE (LONDON) 226, 421- 425; FULLER ET AL. 1996, J.STRUC.BIOL. 11 48-55;FERLENGHI ET AL. 1998, J.MOL.BIOL. 283, 71-81) ;
num_particles	5267

Files (7)

• pr_distribution /app/data/pr_computation/dy/1dyl/pr_distribution.json
• pr_output /app/data/pr_computation/dy/1dyl/1dyl.pr.out
• pr_plot /app/data/visualization/pr_computation/dy/1dyl/1dyl_pr_distribution.png
• saxs_curve_dat /app/data/saxs_computation/dy/1dyl/1dyl.dat
• saxs_fit /app/data/saxs_computation/dy/1dyl/1dyl.fit
• saxs_log /app/data/saxs_computation/dy/1dyl/1dyl.log
• saxs_plot /app/data/visualization/saxs_computation/dy/1dyl/1dyl_saxs_profile.png

Curves (3)

fit	/app/data/saxs_computation/dy/1dyl/1dyl.fit
pddf	/app/data/pr_computation/dy/1dyl/1dyl.pr.out
profile	/app/data/saxs_computation/dy/1dyl/1dyl.dat