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1c4w

1.9 A STRUCTURE OF A-THIOPHOSPHONATE MODIFIED CHEY D57C

Method: X-RAY DIFFRACTION D_max: 45.9 Å Quality: REASONABLE

SAXS Profile

P(r) Distribution

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1. Structure Basics

entry_id	1c4w
deposition_date	1999-09-28
title	1.9 A STRUCTURE OF A-THIOPHOSPHONATE MODIFIED CHEY D57C
keywords	Phosphono-CheY, Active Form of the Response Regulator, Chemotaxis, SIGNALING PROTEIN; SIGNALING PROTEIN
method	X-RAY DIFFRACTION

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Download Data

SAXS curve (.dat) P(r) distribution (.pr.out) Structure (CIF)

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2. SAXS Parameters (CRYSOL)

rg_guinier	14.79 Å
rg_electron	13.28 Å
i0	3851860.00
molecular_weight	14046.0 kDa
excluded_volume	17716 Å³
envelope_volume	19199 Å³
shell_volume	12124 Å³
envelope_diameter	44.0 Å
shell_rg	19.22 Å
envelope_rg	13.55 Å
shape_rg	13.28 Å
total_rg	14.56 Å
total_atoms	982
n_residues	127
n_harmonics	20
q_range	— – 0.5000 Å⁻¹
n_points	101
shell_type	directional
solvent_density	0.3340 e/Å³
contrast_shell	0.0300 e/Å³
crysol_version	4.1.3

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3. P(r) Analysis (GNOM)

dmax	45.9 Å
rg_real	14.65 Å
rg_real_error	0.20 Å
i0_real	3.8520e+06
i0_real_error	3.6620e+04
rg_reciprocal	14.67 Å
i0_reciprocal	3852000.0000
total_estimate	0.7168
solution_quality	REASONABLE a REASONABLE solution
n_peaks	2
r_peak_primary	20.3 Å
skewness	-0.008
kurtosis	-0.429
angular_range	— – 0.5000 Å⁻¹
current_alpha	0.0000
highest_alpha	747000.0000
n_real_points	80
gnom_version	4.1.3
quality_criteria	AN1: 0.000; Oscil: 0.857; Stabil: 1.000; Sysdev: 0.256; Positv: 1.000; Valcen: 0.980; Smooth: 0.996

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4. Crystallography & Experiment

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5. Entities & Polymer Info (2)

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6. Citations (6)

The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY.

Biochemistry (2000)

PMID: 10819997 · DOI: 10.1021/bi9925524 PRIMARY

Synthesis and Biochemical Characterization of an Analogue of CheY-phosphate, a Signal Transduction Protein in Bacterial Chemotaxis

Biochemistry (1998)

DOI: 10.1021/bi9806293

;Uncoupled Phosphorylation and Activation in Bacterial Chemotaxis: the 2.3 A Structure of an Aspartate to Lysine Mutant at Position 13 of CheY ;

J.Biol.Chem. (1997)

DOI: 10.1074/jbc.272.18.11850

Crystal Structures of CheY Mutants Y106W and T87I/Y106W. CheY Activation Correlates with Movement of Residue 106.

J.Biol.Chem. (1997)

DOI: 10.1074/jbc.272.8.5000

Tyrosine 106 Plays an Important Role in Chemotaxis Signal Transduction in Escherichia Coli

J.Bacteriol. (1996)

;Uncoupled Phosphorylation and Activation in Bacterial Chemotaxis. The 2.1 A Structure of a Threonine to Isoleucine Mutant at Position 87 of CheY ;

J.Biol.Chem. (1995)

DOI: 10.1074/jbc.270.29.17386

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length_a	45.620 Å
length_b	47.740 Å
length_c	53.130 Å
angle_alpha	90.00 °
angle_beta	90.00 °
angle_gamma	90.00 °
z_pdb	4

space_group	P 21 21 21
int_tables_number	19
crystal_system	—

resolution	1.840 Å
resolution_low	10.000 Å
r_factor	—
r_work	0.2080
r_free	—

description	CHEMOTAXIS PROTEIN CHEY
formula_weight	14063.2 kDa
mutation	D57(CYQ)
src_method	man
entity_count	1

type	polypeptide(L)
strand_id	A
atom_count	1131

1.9 A STRUCTURE OF A-THIOPHOSPHONATE MODIFIED CHEY D57C

SAXS Profile

P(r) Distribution

1. Structure Basics

Download Data

2. SAXS Parameters (CRYSOL)

3. P(r) Analysis (GNOM)

4. Crystallography & Experiment

Unit Cell

Symmetry

Refinement

Diffraction

5. Entities & Polymer Info (2)

Entity 1 polymer

Polymer

Source

Entity 2 water

6. Citations (6)

7. Files & Curves (10)

Files (7)

Curves (3)

organism	Escherichia coli
ncbi_taxonomy_id	562
host_organism	Escherichia coli

description	water
formula_weight	18.0 kDa
src_method	nat
entity_count	140

fit	/app/data/saxs_computation/c4/1c4w/1c4w.fit
pddf	/app/data/pr_computation/c4/1c4w/1c4w.pr.out
profile	/app/data/saxs_computation/c4/1c4w/1c4w.dat