HEADER LYSOZYME 14-MAR-02 1GWD
TITLE TRI-IODIDE DERIVATIVE OF HEN EGG-WHITE LYSOZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE, ALLERGEN GAL D 4, GAL D IV;
COMPND 5 EC: 3.2.1.17
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031
KEYWDS LYSOZYME, HYDROLASE, GLYCOSIDASE, BACTERIOLYTIC ENZYME, ALLER
EXPDTA X-RAY DIFFRACTION
AUTHOR G.EVANS,G.BRICOGNE
REVDAT 4 28-JUN-17 1GWD 1 REMARK
REVDAT 3 24-FEB-09 1GWD 1 VERSN
REVDAT 2 03-JUL-02 1GWD 1 COMPND
REVDAT 1 06-JUN-02 1GWD 0
JRNL AUTH G.EVANS,G.BRICOGNE
JRNL TITL TRIIODIDE DERIVATIZATION AND COMBINATORIAL COUNTER-ION
JRNL TITL 2 REPLACEMENT: TWO METHODS FOR ENHANCING PHASING SIGNAL USING
JRNL TITL 3 LABORATORY CU KALPHA X-RAY EQUIPMENT
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 58 976 2002
JRNL REFN ISSN 0907-4449
JRNL PMID 12037300
JRNL DOI 10.1107/S0907444902005486
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 11832
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 589
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1001
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 103
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : NULL ; NULL ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT CORRECTION APPLIED
REMARK 4
REMARK 4 1GWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1290009563.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.70
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ELLIOTT GX-13
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : SUPPER MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 180 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 143946
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 15.091
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 12.10
REMARK 200 R MERGE (I) : 0.02100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 11.70
REMARK 200 R MERGE FOR SHELL (I) : 0.04600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 15.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M NACL, 0.025M SODIUM ACETATE AT
REMARK 280 PH4.7,0.1% SODIUM AZIDE, 25% ETHYLENE GLYCOL AND THEN SOAKED IN
REMARK 280 AN EQUIVALENT SOLUTION WITH 50MM KI/50MM I2., PH 4.70
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 18.41000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.52500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.52500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.61500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.52500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.52500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.20500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.52500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.52500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.61500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.52500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.52500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.20500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 18.41000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 I IOD A1147 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2016 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2060 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 C CMO A 1135 C CMO A 1135 8555 1.37
REMARK 500 O HOH A 2040 O HOH A 2040 7556 1.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 18 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 21 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1144 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 73 O
REMARK 620 2 CYS A 64 O 90.4
REMARK 620 3 HOH A2053 O 165.2 90.5
REMARK 620 4 HOH A2051 O 86.3 94.7 78.9
REMARK 620 5 SER A 60 O 93.9 93.3 100.8 172.0
REMARK 620 6 SER A 72 OG 100.9 168.5 78.1 84.1 88.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1131
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1132
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1133
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1137
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1138
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1139
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1140
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1143
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1144
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1145
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1146
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1147
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1134
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A1135
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1136
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 132L RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 193L RELATED DB: PDB
REMARK 900 THE 1.33 A STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 194L RELATED DB: PDB
REMARK 900 THE 1.40 A STRUCTURE OF SPACEHAB-01 HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1A2Y RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME, D18A MUTANT, IN COMPLEX WITH MOUSE
REMARK 900 MONOCLONAL ANTIBODY D1.3
REMARK 900 RELATED ID: 1AKI RELATED DB: PDB
REMARK 900 THE STRUCTURE OF THE ORTHORHOMBIC FORM OF HEN EGG-WHITE LYSOZYME AT
REMARK 900 1.5 ANGSTROMS RESOLUTION
REMARK 900 RELATED ID: 1AT5 RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME WITH A SUCCINIMIDE RESIDUE
REMARK 900 RELATED ID: 1AT6 RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE
REMARK 900 RELATED ID: 1AZF RELATED DB: PDB
REMARK 900 CHICKEN EGG WHITE LYSOZYME CRYSTAL GROWN IN BROMIDE SOLUTION
REMARK 900 RELATED ID: 1B0D RELATED DB: PDB
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME
REMARK 900 CRYSTALS
REMARK 900 RELATED ID: 1B2K RELATED DB: PDB
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME
REMARK 900 CRYSTALS
REMARK 900 RELATED ID: 1BGI RELATED DB: PDB
REMARK 900 ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)
REMARK 900 RELATED ID: 1BHZ RELATED DB: PDB
REMARK 900 LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF HEN EGG WHITE
REMARK 900 LYSOZYME FROM MASC DATA
REMARK 900 RELATED ID: 1BVK RELATED DB: PDB
REMARK 900 HUMANIZED ANTI-LYSOZYME FV COMPLEXED WITH LYSOZYME
REMARK 900 RELATED ID: 1BVX RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF GEL GROWN TETRAGONAL HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1BWH RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF GROUND CONTROL GROWN TETRAGONAL HEN EGG
REMARK 900 WHITE LYSOZYME
REMARK 900 RELATED ID: 1BWI RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF MICROBATCH OIL DROP GROWN TETRAGONAL HEN EGG
REMARK 900 WHITE LYSOZYME
REMARK 900 RELATED ID: 1BWJ RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF MICROGRAVITY GROWN TETRAGONAL HEN EGG WHITE
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1C08 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV-HEN LYSOZYME COMPLEX
REMARK 900 RELATED ID: 1C10 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER PRESSURE OF XENON (8 BAR)
REMARK 900 RELATED ID: 1DPW RELATED DB: PDB
REMARK 900 STRUCTURE OF HEN EGG-WHITE LYSOZYME IN COMPLEX WITH MPD
REMARK 900 RELATED ID: 1DPX RELATED DB: PDB
REMARK 900 STRUCTURE OF HEN EGG-WHITE LYSOZYME
REMARK 900 RELATED ID: 1DQJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ANTI-LYSOZYME ANTIBODY HYHEL-63 COMPLEXED
REMARK 900 WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1E8L RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF HEN LYSOZYME
REMARK 900 RELATED ID: 1F0W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME GROWN AT PH 6.5
REMARK 900 RELATED ID: 1F10 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME GROWN AT PH 6.5 AT 88%
REMARK 900 RELATIVE HUMIDITY
REMARK 900 RELATED ID: 1F3J RELATED DB: PDB
REMARK 900 HISTOCOMPATIBILITY ANTIGEN I-AG7
REMARK 900 RELATED ID: 1FDL RELATED DB: PDB
REMARK 900 IGG1 FAB FRAGMENT (ANTI-LYSOZYME ANTIBODY D1 .3, KAPPA) - LYSOZYME
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1FLQ RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1FLU RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1FLW RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1FLY RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1FN5 RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE
REMARK 900 RELATED ID: 1G7H RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1.3(VLW92A)
REMARK 900 RELATED ID: 1G7I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1.3 (VLW92F)
REMARK 900 RELATED ID: 1G7J RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1.3 (VLW92H)
REMARK 900 RELATED ID: 1G7L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1.3 (VLW92S)
REMARK 900 RELATED ID: 1G7M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1.3 (VLW92V)
REMARK 900 RELATED ID: 1GPQ RELATED DB: PDB
REMARK 900 STRUCTURE OF IVY COMPLEXED WITH ITS TARGET , HEWL
REMARK 900 RELATED ID: 1H6M RELATED DB: PDB
REMARK 900 COVALENT GLYCOSYL-ENZYME INTERMEDIATE OF HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1H87 RELATED DB: PDB
REMARK 900 GADOLINIUM DERIVATIVE OF TETRAGONAL HEN EGG- WHITE LYSOZYME AT 1.7
REMARK 900 A RESOLUTION
REMARK 900 RELATED ID: 1HC0 RELATED DB: PDB
REMARK 900 STRUCTURE OF LYSOZYME WITH PERIODATE
REMARK 900 RELATED ID: 1HEL RELATED DB: PDB
REMARK 900 HEN EGG-WHITE LYSOZYME WILD TYPE
REMARK 900 RELATED ID: 1HEM RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH SER 91 REPLACED BY THR (S91T)
REMARK 900 RELATED ID: 1HEN RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY VAL AND SER 91 REPLACED BY
REMARK 900 THR (I55V, S91T)
REMARK 900 RELATED ID: 1HEO RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY VAL (I55V)
REMARK 900 RELATED ID: 1HEP RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY SER, ILE 55 REPLACED BY VAL,
REMARK 900 AND SER 91 REPLACED BY THR (T40S,I55V,S91T)
REMARK 900 RELATED ID: 1HEQ RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY SER AND SER 91 REPLACED BY
REMARK 900 THR (T40S, S91T)
REMARK 900 RELATED ID: 1HER RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY SER (T40S)
REMARK 900 RELATED ID: 1HEW RELATED DB: PDB
REMARK 900 LYSOZYME COMPLEXED WITH THE INHIBITOR TRI-N -ACETYLCHITOTRIOSE
REMARK 900 RELATED ID: 1HF4 RELATED DB: PDB
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME
REMARK 900 CRYSTALS
REMARK 900 RELATED ID: 1HSW RELATED DB: PDB
REMARK 900 LYSOZYME (MUCOPEPTIDE N-ACETYLMURAMYL HYDROLASE )
REMARK 900 RELATED ID: 1HSX RELATED DB: PDB
REMARK 900 LYSOZYME GROWN AT BASIC PH AND ITS LOW HUMIDITY VARIANT
REMARK 900 RELATED ID: 1IC4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT( HD32A)-HEN LYSOZYMECOMPLEX
REMARK 900 RELATED ID: 1IC5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT( HD99A)-HEN LYSOZYMECOMPLEX
REMARK 900 RELATED ID: 1IC7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT( HD32A99A)-HENLYSOZYME
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1IEE RELATED DB: PDB
REMARK 900 STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME AT 0.94 AFROM
REMARK 900 CRYSTALS GROWN BY THE COUNTER-DIFFUSION METHOD
REMARK 900 RELATED ID: 1IO5 RELATED DB: PDB
REMARK 900 HYDROGEN AND HYDRATION OF HEN EGG-WHITE LYSOZYME DETERMINEDBY
REMARK 900 NEUTRON DIFFRACTION
REMARK 900 RELATED ID: 1IOQ RELATED DB: PDB
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLINGMUTATION
REMARK 900 RELATED ID: 1IOR RELATED DB: PDB
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLINGMUTATION
REMARK 900 RELATED ID: 1IOS RELATED DB: PDB
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLINGMUTATION
REMARK 900 RELATED ID: 1IOT RELATED DB: PDB
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLINGMUTATION
REMARK 900 RELATED ID: 1IR7 RELATED DB: PDB
REMARK 900 IM MUTANT OF LYSOZYME
REMARK 900 RELATED ID: 1IR8 RELATED DB: PDB
REMARK 900 IM MUTANT OF LYSOZYME
REMARK 900 RELATED ID: 1IR9 RELATED DB: PDB
REMARK 900 IM MUTANT OF LYSOZYME
REMARK 900 RELATED ID: 1JA2 RELATED DB: PDB
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: APOWDER
REMARK 900 DIFFRACTION STUDY
REMARK 900 RELATED ID: 1JA4 RELATED DB: PDB
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: APOWDER
REMARK 900 DIFFRACTION STUDY
REMARK 900 RELATED ID: 1JA6 RELATED DB: PDB
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: APOWDER
REMARK 900 DIFFRACTION STUDY
REMARK 900 RELATED ID: 1JA7 RELATED DB: PDB
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: APOWDER
REMARK 900 DIFFRACTION STUDY
REMARK 900 RELATED ID: 1JIS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN AT PH 4.6
REMARK 900 RELATED ID: 1JIT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN IN PRESENCE30%
REMARK 900 TREHALOSE
REMARK 900 RELATED ID: 1JIY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN IN PRESENCE20%
REMARK 900 SORBITOL
REMARK 900 RELATED ID: 1JJ0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN IN PRESENCEOF 30%
REMARK 900 SUCROSE
REMARK 900 RELATED ID: 1JJ1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME GROWN AT PH 4.6IN
REMARK 900 PRESENCE OF 5% SORBITOL
REMARK 900 RELATED ID: 1JJ3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN AT PH 4.6
REMARK 900 RELATED ID: 1JPO RELATED DB: PDB
REMARK 900 LOW TEMPERATURE ORTHORHOMBIC LYSOZYME
REMARK 900 RELATED ID: 1JTO RELATED DB: PDB
REMARK 900 DEGENERATE INTERFACES IN ANTIGEN-ANTIBODY COMPLEXES
REMARK 900 RELATED ID: 1KIP RELATED DB: PDB
REMARK 900 FV MUTANT Y(B 32)A (VH DOMAIN) OF MOUSE MONOCLONAL ANTIBODY D1.3
REMARK 900 COMPLEXED WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1KIQ RELATED DB: PDB
REMARK 900 FV MUTANT Y(B 101)F (VH DOMAIN) OF MOUSE MONOCLONAL ANTIBODY D1.3
REMARK 900 COMPLEXED WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1KIR RELATED DB: PDB
REMARK 900 FV MUTANT Y(A 50)S (VL DOMAIN) OF MOUSE MONOCLONAL ANTIBODY D1.3
REMARK 900 COMPLEXED WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1KXW RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1KXX RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1KXY RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1LCN RELATED DB: PDB
REMARK 900 MONOCLINIC HEN EGG WHITE LYSOZYME, THIOCYANATE COMPLEX
REMARK 900 RELATED ID: 1LKR RELATED DB: PDB
REMARK 900 MONOCLINIC HEN EGG WHITE LYSOZYME IODIDE
REMARK 900 RELATED ID: 1LKS RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME NITRATE
REMARK 900 RELATED ID: 1LMA RELATED DB: PDB
REMARK 900 LYSOZYME (88 PERCENT HUMIDITY)
REMARK 900 RELATED ID: 1LPI RELATED DB: PDB
REMARK 900 HEW LYSOZYME: TRP...NA CATION-PI INTERACTION
REMARK 900 RELATED ID: 1LSA RELATED DB: PDB
REMARK 900 LYSOZYME (120 K)
REMARK 900 RELATED ID: 1LSB RELATED DB: PDB
REMARK 900 LYSOZYME (180 K)
REMARK 900 RELATED ID: 1LSC RELATED DB: PDB
REMARK 900 LYSOZYME (250 K)
REMARK 900 RELATED ID: 1LSD RELATED DB: PDB
REMARK 900 LYSOZYME (280 K)
REMARK 900 RELATED ID: 1LSE RELATED DB: PDB
REMARK 900 LYSOZYME (295 K)
REMARK 900 RELATED ID: 1LSF RELATED DB: PDB
REMARK 900 LYSOZYME (95 K)
REMARK 900 RELATED ID: 1LSG RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: LYSOZYME MODIFIED WITH HUMAN FIBRINOGEN GAMMA;
REMARK 900 CHAIN: NULL; ENGINEERED; THE 14-RESIDUE C-TERMINUS ( RESIDUES 398 -
REMARK 900 411) OF THE HUMAN FIBRINOGEN GAMMA CHAIN FUSED TO THE C-TERMINUS OF
REMARK 900 CHICKEN EGG WHITE LYSOZYME; MUTATION: N-TERM MET
REMARK 900 RELATED ID: 1LSM RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY LEU, SER 91 REPLACED BY THR,
REMARK 900 AND ASP 101 REPLACED BY SER (I55L,S91T,D101S)
REMARK 900 RELATED ID: 1LSN RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH SER 91 REPLACED BY ALA (S91A)
REMARK 900 RELATED ID: 1LSY RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ASP 52 REPLACED BY SER (D52S)
REMARK 900 RELATED ID: 1LSZ RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH ASP 52 REPLACED BY SER (D52S) COMPLEXED WITH
REMARK 900 GLCNAC4 (TETRA-N- ACETYL CHITOTETRAOSE)
REMARK 900 RELATED ID: 1LYO RELATED DB: PDB
REMARK 900 CROSS-LINKED LYSOZYME CRYSTAL IN NEAT WATER
REMARK 900 RELATED ID: 1LYS RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1LYZ RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1LZ8 RELATED DB: PDB
REMARK 900 LYSOZYME PHASED ON ANOMALOUS SIGNAL OF SULFURS AND CHLORINES
REMARK 900 RELATED ID: 1LZ9 RELATED DB: PDB
REMARK 900 ANOMALOUS SIGNAL OF SOLVENT BROMINES USED FOR PHASING OF LYSOZYME
REMARK 900 RELATED ID: 1LZA RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1LZB RELATED DB: PDB
REMARK 900 LYSOZYME CO-CRYSTALLIZED WITH TRI-N-ACETYL- CHITOTRIOSE (PH 4.7)
REMARK 900 RELATED ID: 1LZC RELATED DB: PDB
REMARK 900 LYSOZYME CO-CRYSTALLIZED WITH TETRA-N-ACETYL -CHITOTETRAOSE (PH 4.7)
REMARK 900 RELATED ID: 1LZD RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY TYR (W62Y)
REMARK 900 RELATED ID: 1LZE RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY TYR (W62Y) CO-CRYSTALLIZED
REMARK 900 WITH TRI-N- ACETYL-CHITOTRIOSE (PH 4.7)
REMARK 900 RELATED ID: 1LZG RELATED DB: PDB
REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY PHE (W62F) CO-CRYSTALLIZED
REMARK 900 WITH TRI-N- ACETYL-CHITOTRIOSE (PH 4.7)
REMARK 900 RELATED ID: 1LZH RELATED DB: PDB
REMARK 900 LYSOZYME (MONOCLINIC)
REMARK 900 RELATED ID: 1LZN RELATED DB: PDB
REMARK 900 NEUTRON STRUCTURE OF HEN EGG-WHITE LYSOZYME
REMARK 900 RELATED ID: 1LZT RELATED DB: PDB
REMARK 900 LYSOZYME , TRICLINIC CRYSTAL FORM
REMARK 900 RELATED ID: 1MEL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A CAMEL SINGLE-DOMAIN VH ANTIBODY FRAGMENT IN
REMARK 900 COMPLEX WITH LYSOZYME
REMARK 900 RELATED ID: 1MLC RELATED DB: PDB
REMARK 900 MONOCLONAL ANTIBODY FAB D44.1 RAISED AGAINST CHICKEN EGG-WHITE
REMARK 900 LYSOZYME COMPLEXED WITH LYSOZYME
REMARK 900 RELATED ID: 1QIO RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE CAUSED BY INTENSE
REMARK 900 SYNCHROTRON RADIATION TO HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1QTK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER PRESSURE OF KRYPTON (55 BAR)
REMARK 900 RELATED ID: 1RCM RELATED DB: PDB
REMARK 900 LYSOZYME (PARTIALLY REDUCED, CARBOXYMETHYLATED ( 6,127-RCM))
REMARK 900 RELATED ID: 1RFP RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UCO RELATED DB: PDB
REMARK 900 HEN EGG-WHITE LYSOZYME, LOW HUMIDITY FORM
REMARK 900 RELATED ID: 1UIA RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIB RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIC RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UID RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIE RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIF RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIG RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIH RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1XEI RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION
REMARK 900 RELATED ID: 1XEJ RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION
REMARK 900 RELATED ID: 1XEK RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION
REMARK 900 RELATED ID: 2HFM RELATED DB: PDB
REMARK 900 IGG1 FV FRAGMENT (HYHEL-10) AND LYSOZYME COMPLEX (THEORETICAL MODEL)
REMARK 900 RELATED ID: 2IFF RELATED DB: PDB
REMARK 900 IGG1 FAB FRAGMENT (HYHEL-5) COMPLEXED WITH LYSOZYME MUTANT WITH ARG
REMARK 900 68 REPLACED BY LYS (R68K)
REMARK 900 RELATED ID: 2LYM RELATED DB: PDB
REMARK 900 LYSOZYME (1 ATMOSPHERE, 1.4 M NACL)
REMARK 900 RELATED ID: 2LYO RELATED DB: PDB
REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN 90 % ACETONITRILE-WATER
REMARK 900 RELATED ID: 2LYZ RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 2LZH RELATED DB: PDB
REMARK 900 LYSOZYME (ORTHORHOMBIC)
REMARK 900 RELATED ID: 2LZT RELATED DB: PDB
REMARK 900 LYSOZYME , TRICLINIC CRYSTAL FORM
REMARK 900 RELATED ID: 3HFL RELATED DB: PDB
REMARK 900 IGG1 FAB FRAGMENT (HY/HEL-5) COMPLEXED WITH LYSOZYME
REMARK 900 RELATED ID: 3HFM RELATED DB: PDB
REMARK 900 IGG1 FAB FRAGMENT (HYHEL-10) AND LYSOZYME COMPLEX
REMARK 900 RELATED ID: 3LYM RELATED DB: PDB
REMARK 900 LYSOZYME (1000 ATMOSPHERES, 1.4 M NACL)
REMARK 900 RELATED ID: 3LYO RELATED DB: PDB
REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN 95 % ACETONITRILE-WATER
REMARK 900 RELATED ID: 3LYT RELATED DB: PDB
REMARK 900 LYSOZYME (100 KELVIN)
REMARK 900 RELATED ID: 3LYZ RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 3LZT RELATED DB: PDB
REMARK 900 REFINEMENT OF TRICLINIC LYSOZYME AT ATOMIC RESOLUTION
REMARK 900 RELATED ID: 4LYM RELATED DB: PDB
REMARK 900 LYSOZYME (MUCOPEPTIDE N-ACETYLMURAMYL HYDROLASE )
REMARK 900 RELATED ID: 4LYO RELATED DB: PDB
REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN NEAT ACETONITRILE, THEN
REMARK 900 BACK-SOAKED IN WATER
REMARK 900 RELATED ID: 4LYT RELATED DB: PDB
REMARK 900 LYSOZYME (298 KELVIN)
REMARK 900 RELATED ID: 4LYZ RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 4LZT RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION REFINEMENT OF TRICLINIC HEW LYSOZYME AT 295K
REMARK 900 RELATED ID: 5LYM RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: LYSOZYME; CHAIN: A, B ; EC: 3.2.1.17
REMARK 900 RELATED ID: 5LYT RELATED DB: PDB
REMARK 900 LYSOZYME (100 KELVIN)
REMARK 900 RELATED ID: 5LYZ RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 6LYT RELATED DB: PDB
REMARK 900 LYSOZYME (298 KELVIN)
REMARK 900 RELATED ID: 6LYZ RELATED DB: PDB
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 7LYZ RELATED DB: PDB
REMARK 900 LYSOZYME TRICLINIC CRYSTAL FORM
REMARK 900 RELATED ID: 8LYZ RELATED DB: PDB
REMARK 900 LYSOZYME IODINE-INACTIVATED
DBREF 1GWD A 1 129 UNP P00698 LYC_CHICK 19 147
SEQRES 1 A 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 A 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 A 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 A 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 A 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 A 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 A 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 A 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 A 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
HET IOD A1130 1
HET IOD A1131 1
HET IOD A1132 1
HET IOD A1133 1
HET EDO A1134 4
HET CMO A1135 2
HET EDO A1136 4
HET CL A1137 1
HET CL A1138 1
HET CL A1139 1
HET CL A1140 1
HET CL A1141 1
HET CL A1142 1
HET CL A1143 1
HET NA A1144 1
HET NA A1145 1
HET NA A1146 1
HET IOD A1147 1
HETNAM IOD IODIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CMO CARBON MONOXIDE
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 IOD 5(I 1-)
FORMUL 6 EDO 2(C2 H6 O2)
FORMUL 7 CMO C O
FORMUL 9 CL 7(CL 1-)
FORMUL 16 NA 3(NA 1+)
FORMUL 20 HOH *103(H2 O)
HELIX 1 1 GLY A 4 HIS A 15 1 12
HELIX 2 2 SER A 24 ASN A 37 1 14
HELIX 3 3 CYS A 80 SER A 85 5 6
HELIX 4 4 ILE A 88 SER A 100 1 13
HELIX 5 5 ASN A 103 ALA A 107 5 5
HELIX 6 6 TRP A 108 CYS A 115 1 8
HELIX 7 7 ASP A 119 ILE A 124 5 6
SHEET 1 AA 3 THR A 43 ARG A 45 0
SHEET 2 AA 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44
SHEET 3 AA 3 ILE A 58 ASN A 59 -1 O ILE A 58 N TYR A 53
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.02
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.04
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.03
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.04
LINK NA NA A1144 O ARG A 73 1555 1555 2.50
LINK NA NA A1144 O CYS A 64 1555 1555 2.52
LINK NA NA A1144 O HOH A2053 1555 1555 2.45
LINK NA NA A1144 O HOH A2051 1555 1555 2.52
LINK NA NA A1144 O SER A 60 1555 1555 2.32
LINK NA NA A1144 OG SER A 72 1555 1555 2.52
SITE 1 AC1 4 ARG A 14 ARG A 128 LEU A 129 IOD A1147
SITE 1 AC2 4 ASN A 65 GLY A 67 HOH A2021 HOH A2036
SITE 1 AC3 4 ASP A 18 ASN A 19 SER A 24 LEU A 25
SITE 1 AC4 1 ASN A 74
SITE 1 AC5 2 TYR A 23 ASN A 113
SITE 1 AC6 5 GLY A 67 ARG A 68 THR A 69 SER A 72
SITE 2 AC6 5 HOH A2053
SITE 1 AC7 3 SER A 24 GLY A 26 GLN A 121
SITE 1 AC8 1 ILE A 88
SITE 1 AC9 3 ASN A 65 PRO A 79 HOH A2065
SITE 1 BC1 2 ARG A 73 ASN A 74
SITE 1 BC2 6 SER A 60 CYS A 64 SER A 72 ARG A 73
SITE 2 BC2 6 HOH A2051 HOH A2053
SITE 1 BC3 7 TYR A 53 GLY A 54 ILE A 55 LEU A 56
SITE 2 BC3 7 GLN A 57 ILE A 58 SER A 91
SITE 1 BC4 7 GLY A 49 SER A 50 THR A 51 SER A 60
SITE 2 BC4 7 ASP A 66 ARG A 68 THR A 69
SITE 1 BC5 1 IOD A1130
SITE 1 BC6 6 GLN A 57 ILE A 58 ASN A 59 ALA A 107
SITE 2 BC6 6 TRP A 108 HOH A2102
SITE 1 BC7 4 ALA A 10 ALA A 11 HOH A2010 HOH A2103
SITE 1 BC8 1 ALA A 122
CRYST1 79.050 79.050 36.820 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012650 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012650 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027159 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
