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1b5z

;CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS ;

Method: X-RAY DIFFRACTION D_max: 63.5 Å Quality: REASONABLE

SAXS Profile

P(r) Distribution

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1. Structure Basics

entry_id	1b5z
deposition_date	1999-01-11
title	;CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS ;
keywords	HYDROLASE, HYDROGEN BOND, STABILITY; 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	20.14 Å
rg_electron	19.12 Å
i0	17410100.00
molecular_weight	29386.0 kDa
excluded_volume	35910 Å³
envelope_volume	41608 Å³
shell_volume	18524 Å³
envelope_diameter	64.6 Å
shell_rg	24.82 Å
envelope_rg	19.22 Å
shape_rg	19.11 Å
total_rg	19.91 Å
total_atoms	2056
n_residues	260
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	63.5 Å
rg_real	20.08 Å
rg_real_error	0.32 Å
i0_real	1.7410e+07
i0_real_error	2.2110e+05
rg_reciprocal	20.10 Å
i0_reciprocal	17410000.0000
total_estimate	0.7342
solution_quality	REASONABLE a REASONABLE solution
n_peaks	2
r_peak_primary	23.6 Å
skewness	0.252
kurtosis	-0.403
angular_range	— – 0.3950 Å⁻¹
current_alpha	0.0000
highest_alpha	2179000.0000
n_real_points	71
gnom_version	4.1.3
quality_criteria	AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 0.260; Positv: 1.000; Valcen: 0.999; Smooth: 0.994

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4. Crystallography & Experiment

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5. Entities & Polymer Info (2)

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6. Citations (7)

;Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. ;

Biochemistry (1999)

PMID: 10350481 · DOI: 10.1021/bi9901228 PRIMARY

;A General Rule for the Relationship between Hydrophobic Effect and Conformational Stability of a Protein: Stability and Structure of a Series of Hydrophobic Mutants of Human Lysozyme ;

J.Mol.Biol. (1998)

;Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Tyrosine--> Phenylalanine Mutants ;

Biochemistry (1998)

;Contribution of the Hydrophobic Effect to the Stability of Human Lysozyme: Calorimetric Studies and X-Ray Structural Analyses of the Nine Valine to Alanine Mutants ;

Biochemistry (1997)

Contribution of Water Molecules in the Interior of a Protein to the Conformational Stability

J.Mol.Biol. (1997)

The Structure, Stability, and Folding Process of Amyloidogenic Mutant Human Lysozyme

J.Biochem.(Tokyo) (1996)

;Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: Calorimetric Studies and X-Ray Structural Analysis of the Five Isoleucine to Valine Mutants ;

J.Mol.Biol. (1995)

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length_a	64.670 Å
length_b	110.300 Å
length_c	43.640 Å
angle_alpha	90.00 °
angle_beta	90.00 °
angle_gamma	90.00 °
z_pdb	8

space_group	P 21 21 21
int_tables_number	19
crystal_system	—

resolution	2.200 Å
resolution_low	8.000 Å
r_factor	0.1480
r_work	0.1480
r_free	—

description	LYSOZYME
formula_weight	14704.7 kDa
ec_number	3.2.1.17
mutation	S82A
src_method	man
entity_count	2

type	polypeptide(L)
strand_id	A,B
atom_count	2193

;CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS ;

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 (7)

7. Files & Curves (10)

Files (7)

Curves (3)

organism	Homo sapiens
common_name	human
ncbi_taxonomy_id	9606
host_organism	Saccharomyces cerevisiae

description	water
formula_weight	18.0 kDa
src_method	nat
entity_count	137

fit	/app/data/saxs_computation/b5/1b5z/1b5z.fit
pddf	/app/data/pr_computation/b5/1b5z/1b5z.pr.out
profile	/app/data/saxs_computation/b5/1b5z/1b5z.dat