1GBS

CRYSTAL STRUCTURE OF BLACK SWAN GOOSE-TYPE LYSOZYME AT 1.8 ANGSTROMS RESOLUTION

PDB DOI: https://doi.org/10.2210/pdb1GBS/pdb

Classification: HYDROLASE (O-GLYCOSYL)
Organism(s): Cygnus atratus
Mutation(s): No

Deposited: 1995-03-15 Released: 1995-07-10
Deposition Author(s): Rao, Z., Machin, K., Isaacs, N.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.50 Å
R-Value Observed: 0.184

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

A strategy for rapid and effective refinement applied to black swan lysozyme.

Rao, Z., Esnouf, R., Isaacs, N., Stuart, D.

(1995) Acta Crystallogr D Biol Crystallogr 51: 331-336

PubMed: 15299299 Search on PubMed
DOI: https://doi.org/10.1107/S0907444994009893
Primary Citation of Related Structures:
1GBS

PubMed Abstract:
The crystal structure of a goose-type lysozyme from the egg white of black swan has been determined at 1.9 A resolution using a semi-automatic procedure based on the Calpha coordinates of the homologous goose protein.

Organizational Affiliation

Laboratory of Molecular Biophysics and Oxford Centre for Molecular Sciences, Oxford University, England.

Macromolecule Content

Total Structure Weight: 20.43 kDa
Atom Count: 1,586
Modelled Residue Count: 185
Deposited Residue Count: 185
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
AUSTRALIAN BLACK SWAN EGG WHITE LYSOZYME	A	185	Cygnus atratus	Mutation(s): 0 EC: 3.2.1.17
UniProt
Find proteins for P00717 (Cygnus atratus) Explore P00717 Go to UniProtKB: P00717
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P00717
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.50 Å
R-Value Observed: 0.184
Space Group: P 2₁ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 91.8	α = 90
b = 65.4	β = 90
c = 38.8	γ = 90

Software Package:

Software Name	Purpose
X-PLOR	model building
X-PLOR	refinement
PROTEIN	refinement
CCP4	refinement
X-PLOR	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 1995-07-10

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 1995-07-10
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

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