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1boq

PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE

Method: X-RAY DIFFRACTION D_max: 51.7 Å Quality: REASONABLE

SAXS Profile

P(r) Distribution

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1. Structure Basics

entry_id	1boq
deposition_date	1998-08-05
title	PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE
keywords	SERINE PROTEASE, FOLDING MUTANT, HYDROLASE; HYDROLASE
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	16.16 Å
rg_electron	15.04 Å
i0	8697090.00
molecular_weight	20074.0 kDa
excluded_volume	24450 Å³
envelope_volume	26730 Å³
shell_volume	14768 Å³
envelope_diameter	51.7 Å
shell_rg	21.23 Å
envelope_rg	15.31 Å
shape_rg	15.02 Å
total_rg	16.09 Å
total_atoms	1402
n_residues	198
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	51.7 Å
rg_real	16.03 Å
rg_real_error	0.24 Å
i0_real	8.6970e+06
i0_real_error	9.6000e+04
rg_reciprocal	16.05 Å
i0_reciprocal	8697000.0000
total_estimate	0.7246
solution_quality	REASONABLE a REASONABLE solution
n_peaks	2
r_peak_primary	21.6 Å
skewness	0.105
kurtosis	-0.418
angular_range	— – 0.4950 Å⁻¹
current_alpha	0.0000
highest_alpha	2396000.0000
n_real_points	80
gnom_version	4.1.3
quality_criteria	AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 0.302; Positv: 1.000; Valcen: 0.995; Smooth: 0.989

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4. Crystallography & Experiment

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5. Entities & Polymer Info (3)

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6. Citations (7)

Pro region C-terminus:protease active site interactions are critical in catalyzing the folding of alpha-lytic protease.

Biochemistry (1998)

PMID: 9724517 · DOI: 10.1021/bi980883v PRIMARY

Structural Basis for Broad Specificity in Alpha-Lytic Protease

Biochemistry (1991)

Structural Plasticity Broadens the Specificity of an Engineered Protease

Nature (1989)

Structural Analysis of Specificity: Alpha-Lytic Protease Complexes with Analogues of Reaction Intermediates

Biochemistry (1989)

Serine Protease Mechanism: Structure of an Inhibitory Complex of Alpha-Lytic Protease and a Tightly Bound Peptide Boronic Acid

Biochemistry (1987)

Refined Structure of Alpha-Lytic Protease at 1.7 A Resolution. Analysis of Hydrogen Bonding and Solvent Structure

J.Mol.Biol. (1985)

Molecular Structure of the Alpha-Lytic Protease from Myxobacter 495 at 2.8 Angstroms Resolution

J.Mol.Biol. (1979)

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length_a	66.200 Å
length_b	66.200 Å
length_c	80.200 Å
angle_alpha	90.00 °
angle_beta	90.00 °
angle_gamma	120.00 °
z_pdb	6

space_group	P 32 2 1
int_tables_number	154
crystal_system	—

resolution	2.100 Å
resolution_low	6.000 Å
r_factor	0.1590
r_work	0.1590
r_free	0.2360

description	PROTEIN (ALPHA-LYTIC PROTEASE)
formula_weight	19889.2 kDa
ec_number	3.4.21.12
mutation	V119I
src_method	nat
entity_count	1

type	polypeptide(L)
strand_id	A
atom_count	1538

PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE

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 (3)

Entity 1 polymer

Polymer

Entity 2 non-polymer

Entity 3 water

6. Citations (7)

7. Files & Curves (10)

Files (7)

Curves (3)

description	SULFATE ION
formula_weight	96.1 kDa
src_method	syn
entity_count	2

description	water
formula_weight	18.0 kDa
src_method	nat
entity_count	136

fit	/app/data/saxs_computation/bo/1boq/1boq.fit
pddf	/app/data/pr_computation/bo/1boq/1boq.pr.out
profile	/app/data/saxs_computation/bo/1boq/1boq.dat