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- PDB-1d6p: HUMAN LYSOZYME L63 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL N,N'-DI... -

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Basic information

Entry
Database: PDB / ID: 1d6p
TitleHUMAN LYSOZYME L63 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL N,N'-DIACETYLCHITOBIOSE
ComponentsLYSOZYME
KeywordsHYDROLASE / LYSOZYME / MURAMIDASE / HYDROLASE (O-GLYCOSYL) / SITE-DIRECTED MUTAGENESIS / N / N'-DIACETYLCHITOBIOSE / AFFINITY LABELING
Function / homology
Function and homology information


Antimicrobial peptides / antimicrobial humoral response / azurophil granule lumen / specific granule lumen / retina homeostasis / tertiary granule lumen / lysozyme / lysozyme activity / killing of cells of other organism / cytolysis ...Antimicrobial peptides / antimicrobial humoral response / azurophil granule lumen / specific granule lumen / retina homeostasis / tertiary granule lumen / lysozyme / lysozyme activity / killing of cells of other organism / cytolysis / defense response to Gram-negative bacterium / inflammatory response / defense response to Gram-positive bacterium / Amyloid fiber formation / defense response to bacterium / amyloid fibril formation / Neutrophil degranulation / neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / identical protein binding
Similarity search - Function
Lysozyme C / Glycoside hydrolase, family 22, lysozyme / Lysozyme - #10 / Glycosyl hydrolases family 22 (GH22) domain signature. / Glycoside hydrolase family 22 domain / Glycosyl hydrolases family 22 (GH22) domain profile. / Glycoside hydrolase, family 22 / C-type lysozyme/alpha-lactalbumin family / Alpha-lactalbumin / lysozyme C / Lysozyme ...Lysozyme C / Glycoside hydrolase, family 22, lysozyme / Lysozyme - #10 / Glycosyl hydrolases family 22 (GH22) domain signature. / Glycoside hydrolase family 22 domain / Glycosyl hydrolases family 22 (GH22) domain profile. / Glycoside hydrolase, family 22 / C-type lysozyme/alpha-lactalbumin family / Alpha-lactalbumin / lysozyme C / Lysozyme / Lysozyme-like domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Lysozyme C / Lysozyme C
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / Resolution: 2.23 Å
AuthorsMuraki, M. / Harata, K. / Sugita, N. / Sato, K.
Citation
Journal: Biochemistry / Year: 2000
Title: Protein-carbohydrate interactions in human lysozyme probed by combining site-directed mutagenesis and affinity labeling.
Authors: Muraki, M. / Harata, K. / Sugita, N. / Sato, K.I.
#1: Journal: Biochemistry / Year: 1999
Title: Dual Affinity Labeling of the Active Site of Human Lysozyme with an N-Acetyllactosamine Derivative: First Ligand Assisted Recognition of the Second Ligand
Authors: Muraki, M. / Harata, K. / Sugita, N. / Sato, K.
#2: Journal: Acta Crystallogr.,Sect.D / Year: 1998
Title: X-ray Structure of Human Lysozyme Labelled with 2',3'-Epoxypropyl b-Glycoside of Man-b1,4-GlcNAc. Structural Change and Recognition Specificity at Subsite B
Authors: Muraki, M. / Harata, K. / Sugita, N. / Sato, K.
#3: Journal: Biochemistry / Year: 1996
Title: Origin of Carbohydrate Recognition Specificity of Human Lysozyme Revealed by Affinity Labeling
Authors: Muraki, M. / Harata, K. / Sugita, N. / Sato, K.
#4: Journal: Biochemistry / Year: 1992
Title: Dissection of the Functional Role of Structural Elements of Tyrosine-63 in the Catalytic Action of Human Lysozyme
Authors: Muraki, M. / Harata, K. / Jigami, Y.
History
DepositionOct 15, 1999Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 21, 2000Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 1.3Oct 4, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.4Apr 18, 2018Group: Data collection / Category: diffrn_detector / Item: _diffrn_detector.detector
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: LYSOZYME
hetero molecules


Theoretical massNumber of molelcules
Total (without water)15,1873
Polymers14,6711
Non-polymers5162
Water77543
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)58.20, 60.78, 32.73
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein LYSOZYME /


Mass: 14670.676 Da / Num. of mol.: 1 / Mutation: Y63L
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P00695, UniProt: P61626*PLUS, lysozyme
#2: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 43 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 1.97 Å3/Da / Density % sol: 37.65 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 4.5
Details: 5M NH4NO3 IN 10 MM NAOAC(PH 4.5), VAPOR DIFFUSION, SITTING DROP, temperature 298.0K
Crystal grow
*PLUS
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
120 mg/mlprotein1drop
225 mMsodium acetate1drop
33 Mammonium nitrate1drop
425 mMsodium acetate1reservoir
55 Mammonium nitrate1reservoir

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Data collection

DiffractionMean temperature: 288 K
Diffraction sourceSource: ROTATING ANODE / Type: ENRAF-NONIUS FR571 / Wavelength: 1.5148
DetectorType: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: May 10, 1999
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5148 Å / Relative weight: 1
ReflectionResolution: 2.23→22.27 Å / Num. all: 52931 / Num. obs: 40267 / Observed criterion σ(F): 0 / Redundancy: 3.4 % / Rmerge(I) obs: 0.1
Reflection shellResolution: 2.23→2.32 Å / Rmerge(I) obs: 0.293

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Processing

Software
NameVersionClassification
MADNESSdata collection
MERGEF(BY K.HARATA)data reduction
X-PLORmodel building
X-PLOR3.1refinement
MADNESSdata reduction
MERGEF(K.HARATA)data scaling
X-PLORphasing
RefinementResolution: 2.23→8 Å / σ(F): 2 / Details: 98.3 % COMPLETENESS OF DATA
RfactorNum. reflectionSelection details
Rfree0.216 -RANDOM
Rwork0.181 --
obs0.181 --
all-3865 -
Refinement stepCycle: LAST / Resolution: 2.23→8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1025 0 33 43 1101
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.011
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg1.87
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
Software
*PLUS
Name: X-PLOR / Version: 3.1 / Classification: refinement
Refinement
*PLUS
Solvent computation
*PLUS
Displacement parameters
*PLUS
Biso mean: 12.9 Å2
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg25.3
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.46

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