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1f5v

;STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A FLAVOPROTEIN FROM ESCHERICHIA COLI THAT REDUCES NITROCOMPOUNDS. ALTERATION OF PYRIDINE NUCLEOTIDE BINDING BY A SINGLE AMINO ACID SUBSTITUTION ;

Method: X-RAY DIFFRACTION Dmax: 80.7 Å Quality: GOOD

SAXS Profile

SAXS profile for 1f5v

P(r) Distribution

P(r) distribution for 1f5v

1. Structure Basics

entry_id1f5v
deposition_date2000-06-17
title;STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A FLAVOPROTEIN FROM ESCHERICHIA COLI THAT REDUCES NITROCOMPOUNDS. ALTERATION OF PYRIDINE NUCLEOTIDE BINDING BY A SINGLE AMINO ACID SUBSTITUTION ;
keywordsnitroreductase, flavoprotein, Escherichia coli, oxidoreduction, nitrocompound, OXIDOREDUCTASE; OXIDOREDUCTASE
methodX-RAY DIFFRACTION

Download Data

2. SAXS Parameters (CRYSOL)

rg_guinier22.68
rg_electron21.38
i049505400.00
molecular_weight54510.0 kDa
excluded_volume68081 ų
envelope_volume76568 ų
shell_volume28491 ų
envelope_diameter80.0
shell_rg29.52
envelope_rg21.77
shape_rg21.39
total_rg22.23
total_atoms3836
n_residues480
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)

dmax80.7
rg_real22.53
rg_real_error0.51
i0_real4.9510e+07
i0_real_error6.5530e+05
rg_reciprocal22.57
i0_reciprocal49510000.0000
total_estimate0.8361
solution_quality GOOD a GOOD solution
n_peaks2
r_peak_primary28.1
skewness0.165
kurtosis-0.279
angular_range— – 0.3500 −1
current_alpha0.0000
highest_alpha15220000.0000
n_real_points67
gnom_version4.1.3
quality_criteria AN1: 0.000; Oscil: 0.622; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.999

4. Crystallography & Experiment

5. Entities & Polymer Info (3)

6. Citations (1)

7. Files & Curves (10)