HEADER HYDROLASE 23-SEP-11 3TXB
TITLE HEWL CO-CRYSTALLIZATION WITH CISPLATIN IN AQUEOUS MEDIA WITH GLYCEROL
TITLE 2 AS THE CRYOPROTECTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 19-147;
COMPND 5 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C, ALLERGEN GAL D IV;
COMPND 6 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;
SOURCE 5 TISSUE: EGG WHITE
KEYWDS HEN EGG WHITE LYSOZYME (HEWL), BACTERIAL CELL WALL LYSIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.W.M.TANLEY,A.M.M.SCHREURS,J.R.HELLIWELL,L.M.J.KROON-BATENBURG
REVDAT 3 13-SEP-23 3TXB 1 REMARK LINK
REVDAT 2 27-MAR-13 3TXB 1 JRNL
REVDAT 1 30-JAN-13 3TXB 0
JRNL AUTH S.W.TANLEY,A.M.SCHREURS,J.R.HELLIWELL,L.M.KROON-BATENBURG
JRNL TITL EXPERIENCE WITH EXCHANGE AND ARCHIVING OF RAW DATA:
JRNL TITL 2 COMPARISON OF DATA FROM TWO DIFFRACTOMETERS AND FOUR
JRNL TITL 3 SOFTWARE PACKAGES ON A SERIES OF LYSOZYME CRYSTALS.
JRNL REF J.APPL.CRYSTALLOGR. V. 46 108 2013
JRNL REFN ISSN 0021-8898
JRNL PMID 23396873
JRNL DOI 10.1107/S0021889812044172
REMARK 2
REMARK 2 RESOLUTION. 1.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 15220
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 810
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.63
REMARK 3 REFLECTION IN BIN (WORKING SET) : 411
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 34.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.4220
REMARK 3 BIN FREE R VALUE SET COUNT : 23
REMARK 3 BIN FREE R VALUE : 0.4650
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 : 189
REMARK 3 SOLVENT ATOMS : 73
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.123
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.123
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.018
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1175 ; 0.026 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1539 ; 1.950 ; 2.010
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 128 ; 6.809 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 50 ;38.199 ;23.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 166 ;14.228 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;14.984 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 144 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 794 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 635 ; 0.800 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1008 ; 1.343 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 540 ; 2.351 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 531 ; 3.670 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 129
REMARK 3 ORIGIN FOR THE GROUP (A): -20.3111 -0.5783 -9.5338
REMARK 3 T TENSOR
REMARK 3 T11: 0.0130 T22: 0.0189
REMARK 3 T33: 0.0295 T12: -0.0047
REMARK 3 T13: 0.0059 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.2467 L22: 1.2334
REMARK 3 L33: 0.8139 L12: 0.5080
REMARK 3 L13: 0.0883 L23: 0.0115
REMARK 3 S TENSOR
REMARK 3 S11: 0.0159 S12: -0.0449 S13: -0.0683
REMARK 3 S21: -0.0159 S22: -0.0074 S23: -0.0470
REMARK 3 S31: -0.0338 S32: 0.0056 S33: -0.0085
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3TXB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1000068036.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.7
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 : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NONE
REMARK 200 OPTICS : OSMIC CONFOCAL MAX-FLUX, BLUE
REMARK 200 CONFIGURATION
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15220
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.590
REMARK 200 RESOLUTION RANGE LOW (A) : 55.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.9
REMARK 200 DATA REDUNDANCY : 25.77
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : 0.10600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 18.93
REMARK 200 R MERGE FOR SHELL (I) : 0.37700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER MOLECULAR REPLACEMENT
REMARK 200 STARTING MODEL: PDB ENTRY 2W1Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 49 MG HEWL + 3 MG CISPLATIN IN 1 ML
REMARK 280 0.04 M SODIUM ACETATE + 1 ML 10% SODIUM CHLORIDE, WITH GLYCEROL
REMARK 280 AS CRYOPROTECTANT, PH 4.7, BATCH, TEMPERATURE 295K
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 19.97850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.33100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.33100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.96775
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.33100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.33100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.98925
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.33100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.33100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 29.96775
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.33100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.33100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.98925
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 19.97850
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ALA A 31 CA ALA A 31 CB 0.128
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 52 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 87 CB - CG - OD1 ANGL. DEV. = 6.4 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 A1138 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 60 O
REMARK 620 2 CYS A 64 O 84.9
REMARK 620 3 SER A 72 OG 91.4 168.9
REMARK 620 4 ARG A 73 O 97.0 95.6 95.2
REMARK 620 5 HOH A2077 O 96.2 87.2 82.9 166.7
REMARK 620 6 HOH A2082 O 174.2 100.9 83.1 81.5 85.1
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 CL A 1130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1131
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1132
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1133
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1134
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1135
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1136
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1137
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1138
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 131
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 132
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 133
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 134
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 135
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 136
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 137
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 138
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 139
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 140
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 141
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 143
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 144
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 145
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 146
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 148
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 149
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 153
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 156
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 157
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 158
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2I6Z RELATED DB: PDB
REMARK 900 X-RAY DIFFRACTION STUDIES OF ADDUCTS BETWEEN ANTICANCER PLATINUM
REMARK 900 DRUGS AND HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 3TXC RELATED DB: PDB
REMARK 900 RELATED ID: 3TXD RELATED DB: PDB
REMARK 900 RELATED ID: 3TXE RELATED DB: PDB
REMARK 900 RELATED ID: 3TXF RELATED DB: PDB
REMARK 900 RELATED ID: 3TXG RELATED DB: PDB
REMARK 900 RELATED ID: 3TXH RELATED DB: PDB
REMARK 900 RELATED ID: 3TXI RELATED DB: PDB
REMARK 900 RELATED ID: 3TXJ RELATED DB: PDB
REMARK 900 RELATED ID: 3TXK RELATED DB: PDB
REMARK 900 RELATED ID: 3TXL RELATED DB: PDB
DBREF 3TXB A 1 129 UNP P00698 LYSC_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 CL A1130 1
HET CL A1131 1
HET CL A1132 1
HET CL A1133 1
HET CL A1134 1
HET CL A1135 1
HET CL A1136 1
HET CL A1137 1
HET NA A1138 1
HET GOL A 801 6
HET GOL A 130 6
HET GOL A 131 6
HET GOL A 132 6
HET GOL A 133 6
HET GOL A 134 6
HET GOL A 135 6
HET GOL A 136 6
HET GOL A 137 6
HET GOL A 138 6
HET GOL A 139 6
HET GOL A 140 6
HET GOL A 141 6
HET GOL A 142 6
HET GOL A 143 6
HET GOL A 144 6
HET GOL A 145 6
HET GOL A 146 6
HET GOL A 147 6
HET GOL A 148 6
HET GOL A 149 6
HET GOL A 150 6
HET GOL A 151 6
HET GOL A 152 6
HET GOL A 153 6
HET GOL A 154 6
HET GOL A 155 6
HET GOL A 156 6
HET GOL A 157 6
HET GOL A 158 6
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CL 8(CL 1-)
FORMUL 10 NA NA 1+
FORMUL 11 GOL 30(C3 H8 O3)
FORMUL 41 HOH *73(H2 O)
HELIX 1 1 GLY A 4 HIS A 15 1 12
HELIX 2 2 ASN A 19 TYR A 23 5 5
HELIX 3 3 SER A 24 ASN A 37 1 14
HELIX 4 4 PRO A 79 SER A 85 5 7
HELIX 5 5 ILE A 88 SER A 100 1 13
HELIX 6 6 ASN A 103 ALA A 107 5 5
HELIX 7 7 TRP A 108 CYS A 115 1 8
HELIX 8 8 ASP A 119 ILE A 124 5 6
SHEET 1 A 3 THR A 43 ARG A 45 0
SHEET 2 A 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44
SHEET 3 A 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 2.04
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.11
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.00
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.08
LINK O SER A 60 NA NA A1138 1555 1555 2.42
LINK O CYS A 64 NA NA A1138 1555 1555 2.56
LINK OG SER A 72 NA NA A1138 1555 1555 2.68
LINK O ARG A 73 NA NA A1138 1555 1555 2.65
LINK NA NA A1138 O HOH A2077 1555 1555 2.51
LINK NA NA A1138 O HOH A2082 1555 1555 2.66
SITE 1 AC1 3 TYR A 23 ASN A 113 GOL A 156
SITE 1 AC2 3 SER A 24 GLY A 26 GOL A 136
SITE 1 AC3 2 GLY A 67 THR A 69
SITE 1 AC4 2 ILE A 88 GOL A 138
SITE 1 AC5 2 LYS A 33 GOL A 144
SITE 1 AC6 2 ASN A 65 GOL A 155
SITE 1 AC7 3 ARG A 73 ASN A 74 GOL A 139
SITE 1 AC8 2 ALA A 42 ARG A 68
SITE 1 AC9 6 SER A 60 CYS A 64 SER A 72 ARG A 73
SITE 2 AC9 6 HOH A2077 HOH A2082
SITE 1 BC1 4 ALA A 122 TRP A 123 GOL A 134 GOL A 141
SITE 1 BC2 6 GLN A 57 ASN A 59 ALA A 107 HOH A2071
SITE 2 BC2 6 HOH A2074 HOH A2112
SITE 1 BC3 5 TYR A 20 ARG A 21 GOL A 137 GOL A 146
SITE 2 BC3 5 GOL A 148
SITE 1 BC4 5 ALA A 82 ASP A 87 THR A 89 ALA A 90
SITE 2 BC4 5 GOL A 154
SITE 1 BC5 5 TRP A 62 LEU A 75 ASP A 101 GLN A 121
SITE 2 BC5 5 GOL A 144
SITE 1 BC6 5 PHE A 34 THR A 118 TRP A 123 GOL A 141
SITE 2 BC6 5 GOL A 801
SITE 1 BC7 7 SER A 36 ASN A 37 ASN A 39 GLY A 67
SITE 2 BC7 7 ARG A 68 GOL A 142 GOL A 143
SITE 1 BC8 9 ASP A 18 SER A 24 LEU A 25 ARG A 61
SITE 2 BC8 9 ILE A 124 GOL A 142 GOL A 147 GOL A 150
SITE 3 BC8 9 CL A1131
SITE 1 BC9 4 TYR A 20 LYS A 96 GOL A 131 GOL A 149
SITE 1 CC1 5 ALA A 11 ARG A 14 CL A1133 HOH A2010
SITE 2 CC1 5 HOH A2097
SITE 1 CC2 3 SER A 72 CL A1136 HOH A2082
SITE 1 CC3 1 VAL A 109
SITE 1 CC4 3 GLY A 117 GOL A 134 GOL A 801
SITE 1 CC5 7 ASN A 19 ASN A 37 GOL A 135 GOL A 136
SITE 2 CC5 7 GOL A 143 GOL A 147 HOH A2036
SITE 1 CC6 6 PRO A 70 GLY A 71 GOL A 135 GOL A 142
SITE 2 CC6 6 GOL A 147 HOH A2029
SITE 1 CC7 4 ARG A 5 GOL A 133 GOL A 157 CL A1134
SITE 1 CC8 5 HIS A 15 ASN A 93 LYS A 96 GOL A 149
SITE 2 CC8 5 HOH A2106
SITE 1 CC9 5 ASN A 44 ARG A 45 GOL A 131 GOL A 156
SITE 2 CC9 5 HOH A2020
SITE 1 DC1 7 ARG A 61 TRP A 62 GLY A 71 ARG A 73
SITE 2 DC1 7 GOL A 136 GOL A 142 GOL A 143
SITE 1 DC2 5 TYR A 20 ARG A 21 THR A 47 SER A 100
SITE 2 DC2 5 GOL A 131
SITE 1 DC3 6 ARG A 14 GLY A 16 THR A 47 ARG A 128
SITE 2 DC3 6 GOL A 137 GOL A 145
SITE 1 DC4 8 ARG A 61 TRP A 62 GLN A 121 ILE A 124
SITE 2 DC4 8 ARG A 125 GOL A 136 GOL A 151 HOH A2062
SITE 1 DC5 7 ASN A 46 ASP A 48 SER A 50 ASN A 59
SITE 2 DC5 7 ARG A 61 GOL A 150 HOH A2062
SITE 1 DC6 4 GLY A 126 CYS A 127 ARG A 128 GOL A 157
SITE 1 DC7 2 ARG A 73 ASN A 77
SITE 1 DC8 6 ILE A 78 ALA A 82 THR A 89 ALA A 90
SITE 2 DC8 6 GOL A 132 HOH A2037
SITE 1 DC9 5 ASN A 74 ASN A 77 ILE A 78 PRO A 79
SITE 2 DC9 5 CL A1135
SITE 1 EC1 7 ARG A 21 GLU A 35 GOL A 146 CL A1130
SITE 2 EC1 7 HOH A2020 HOH A2038 HOH A2041
SITE 1 EC2 5 ARG A 5 CYS A 6 GOL A 144 GOL A 152
SITE 2 EC2 5 HOH A2012
SITE 1 EC3 6 THR A 43 ASN A 44 ARG A 45 THR A 51
SITE 2 EC3 6 ARG A 68 HOH A2053
CRYST1 78.662 78.662 39.957 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 0.012713 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012713 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025027 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
