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1b7o

VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

Method: X-RAY DIFFRACTION D_max: 50.6 Å Quality: GOOD

SAXS Profile

P(r) Distribution

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1. Structure Basics

entry_id	1b7o
deposition_date	1999-01-25
title	VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
keywords	MUTANT STABILITY, HUMAN LYSOZYME, 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	15.45 Å
rg_electron	14.13 Å
i0	4872520.00
molecular_weight	14803.0 kDa
excluded_volume	18099 Å³
envelope_volume	20351 Å³
shell_volume	12300 Å³
envelope_diameter	49.5 Å
shell_rg	19.75 Å
envelope_rg	14.45 Å
shape_rg	14.10 Å
total_rg	15.24 Å
total_atoms	1035
n_residues	130
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	50.6 Å
rg_real	15.37 Å
rg_real_error	0.28 Å
i0_real	4.8730e+06
i0_real_error	5.5370e+04
rg_reciprocal	15.38 Å
i0_reciprocal	4873000.0000
total_estimate	0.8813
solution_quality	GOOD a GOOD solution
n_peaks	2
r_peak_primary	20.5 Å
skewness	0.184
kurtosis	-0.291
angular_range	— – 0.5000 Å⁻¹
current_alpha	0.0000
highest_alpha	831600.0000
n_real_points	80
gnom_version	4.1.3
quality_criteria	AN1: 0.000; Oscil: 0.830; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.964

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4. Crystallography & Experiment

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5. Entities & Polymer Info (3)

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6. Citations (6)

;Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. ;

Protein Eng. (1999)

PMID: 10469827 · DOI: 10.1093/protein/12.8.663 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)

;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	56.470 Å
length_b	61.470 Å
length_c	32.690 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	1.800 Å
resolution_low	8.000 Å
r_factor	—
r_work	0.1740
r_free	—

description	PROTEIN (LYSOZYME)
formula_weight	14791.8 kDa
ec_number	3.2.1.17
mutation	G37Q
src_method	man
entity_count	1

type	polypeptide(L)
strand_id	A
atom_count	1301

VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

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

Source

Entity 2 non-polymer

Entity 3 water

6. Citations (6)

7. Files & Curves (10)

Files (7)

Curves (3)

organism	Homo sapiens
common_name	human
ncbi_taxonomy_id	9606
host_organism	Saccharomyces cerevisiae

description	SODIUM ION
formula_weight	23.0 kDa
src_method	syn
entity_count	1

description	water
formula_weight	18.0 kDa
src_method	nat
entity_count	266

fit	/app/data/saxs_computation/b7/1b7o/1b7o.fit
pddf	/app/data/pr_computation/b7/1b7o/1b7o.pr.out
profile	/app/data/saxs_computation/b7/1b7o/1b7o.dat