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1cih

STRUCTURAL AND FUNCTIONAL EFFECTS OF MULTIPLE MUTATIONS AT DISTAL SITES IN CYTOCHROME C

Method: X-RAY DIFFRACTION D_max: 48.8 Å Quality: GOOD

SAXS Profile

P(r) Distribution

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1. Structure Basics

entry_id	1cih
deposition_date	1994-09-26
title	STRUCTURAL AND FUNCTIONAL EFFECTS OF MULTIPLE MUTATIONS AT DISTAL SITES IN CYTOCHROME C
keywords	ELECTRON TRANSPORT(HEME PROTEIN); ELECTRON TRANSPORT(HEME 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	14.22 Å
rg_electron	12.87 Å
i0	3225600.00
molecular_weight	12637.0 kDa
excluded_volume	15852 Å³
envelope_volume	17101 Å³
shell_volume	11235 Å³
envelope_diameter	45.8 Å
shell_rg	18.77 Å
envelope_rg	13.25 Å
shape_rg	12.81 Å
total_rg	14.31 Å
total_atoms	886
n_residues	107
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	48.8 Å
rg_real	14.10 Å
rg_real_error	0.27 Å
i0_real	3.2260e+06
i0_real_error	2.9690e+04
rg_reciprocal	14.11 Å
i0_reciprocal	3226000.0000
total_estimate	0.8513
solution_quality	GOOD a GOOD solution
n_peaks	2
r_peak_primary	18.5 Å
skewness	0.124
kurtosis	-0.261
angular_range	— – 0.5000 Å⁻¹
current_alpha	0.0000
highest_alpha	689700.0000
n_real_points	80
gnom_version	4.1.3
quality_criteria	AN1: 0.000; Oscil: 0.688; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.999

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4. Crystallography & Experiment

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5. Entities & Polymer Info (4)

Entity 1 polymer

description	CYTOCHROME C
formula_weight	11936.7 kDa
src_method	man
entity_count	1

Polymer

type	polypeptide(L)
strand_id	A
atom_count	953

TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGAHSGQAEGYSYTDAIIKKNVLWDENNMSEYLTNPKKYIPGTKMASGGLKKEKDRNDLITYLKKAAE

Source

organism	Saccharomyces cerevisiae
common_name	;baker's yeast ;
ncbi_taxonomy_id	4932

Entity 2 non-polymer

description	SULFATE ION
formula_weight	96.1 kDa
src_method	syn
entity_count	1

Entity 3 non-polymer

description	HEME C
formula_weight	618.5 kDa
src_method	syn
entity_count	1

Entity 4 water

description	water
formula_weight	18.0 kDa
src_method	nat
entity_count	67

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6. Citations (9)

Structural and functional effects of multiple mutations at distal sites in cytochrome c.

Biochemistry (1995)

PMID: 7711047 · DOI: 10.1021/bi00015a041 PRIMARY

The Role of a Conserved Internal Water Molecule and its Associated Hydrogen Bond Network in Cytochrome C

J.Mol.Biol. (1994)

Mutation of Tyrosine-67 to Phenylalanine in Cytochrome C Significantly Alters the Local Heme Environment

J.Mol.Biol. (1994)

Oxidation State-Dependent Conformational Changes in Cytochrome C

J.Mol.Biol. (1992)

High-Resolution Refinement of Yeast Iso-1-Cytochrome C and Comparisons with Other Eukaryotic Cytochromes C

J.Mol.Biol. (1990)

A Polypeptide Chain-Refolding Event Occurs in the Gly82 Variant of Yeast Iso-1-Cytochrome C

J.Mol.Biol. (1989)

Crystallization of Yeast Iso-2-Cytochrome C Using a Novel Hair Seeding Technique

J.Mol.Biol. (1989)

Role of Phenylalanine-82 in Yeast Iso-1-Cytochrome C and Remote Conformational Changes Induced by a Serine Residue at This Position

Biochemistry (1988)

Yeast Iso-1-Cytochrome C. A 2.8 Angstrom Resolution Three-Dimensional Structure Determination

J.Mol.Biol. (1988)

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length_a	36.480 Å
length_b	36.480 Å
length_c	137.280 Å
angle_alpha	90.00 °
angle_beta	90.00 °
angle_gamma	90.00 °
z_pdb	8

space_group	P 43 21 2
int_tables_number	96
crystal_system	—

resolution	1.800 Å
resolution_low	6.000 Å
r_factor	0.2000
r_work	—
r_free	—

fit	/app/data/saxs_computation/ci/1cih/1cih.fit
pddf	/app/data/pr_computation/ci/1cih/1cih.pr.out
profile	/app/data/saxs_computation/ci/1cih/1cih.dat