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HEADER HYDROLASE 14-MAR-03 1HL7
TITLE GAMMA LACTAMASE FROM AN AUREOBACTERIUM SPECIES IN COMPLEX
TITLE 2 WITH 3A,4,7,7A-TETRAHYDRO-BENZO [1,3] DIOXOL-2-ONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAMMA LACTAMASE;
COMPND 3 SYNONYM: CO-FACTOR FREE HALOPEROXIDASE (BY IDENTITY);
COMPND 4 CHAIN: A, B;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AUREOBACTERIUM;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 4 EXPRESSION_SYSTEM_STRAIN: DH5;
SOURCE 5 EXPRESSION_SYSTEM_PLASMID: PTRC99;
SOURCE 6 OTHER_DETAILS: CHIROTECH CULTURE COLLECTION
KEYWDS ALPHA/BETA HYDROLASE, CO-FACTOR FREE HALOPEROXIDASE,
KEYWDS 2 TETRAHEDRAL INTERMEDIATE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.LINE,M.N.ISUPOV,J.A.LITTLECHILD
REVDAT 1 30-MAR-04 1HL7 0
JRNL AUTH K.LINE,M.N.ISUPOV,J.A.LITTLECHILD
JRNL TITL THE CRYSTAL STRUCTURE OF GAMMA LACTAMASE FROM
JRNL TITL 2 AUREOBACTERIUM SPECIOES REVEALS A TETRAHEDRAL
JRNL TITL 3 INTERMEDIATE IN THE ACTIVE SITE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 11.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 100
REMARK 3 NUMBER OF REFLECTIONS : 118797
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) : NONE
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2388
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.73
REMARK 3 BIN RESOLUTION RANGE LOW : 1.774
REMARK 3 REFLECTION IN BIN (WORKING SET) : 0.185
REMARK 3 BIN R VALUE (WORKING SET) : 181
REMARK 3 BIN FREE R VALUE SET COUNT : 0.200
REMARK 3 BIN FREE R VALUE : NONE
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4444
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 681
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.9
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.6
REMARK 3 B11 (A**2) : NONE
REMARK 3 B22 (A**2) : NONE
REMARK 3 B33 (A**2) : NONE
REMARK 3 B12 (A**2) : NONE
REMARK 3 B13 (A**2) : NONE
REMARK 3 B23 (A**2) : NONE
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.061
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.060
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.033
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.981
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 4444 ; 0.014 ; 0.021
REMARK 3 BOND ANGLES REFINED (DEGREES): 6044 ; 1.380 ; 1.941
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 555 ; 5.495 ; 5.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 647 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 3512 ; 0.007 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED (A): 2405 ; 0.244 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED (A): 509 ; 0.143 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 82 ; 0.151 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED (A): 54 ; 0.138 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 2748 ; 1.445 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 4373 ; 2.336 ; 6.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 1696 ; 3.530 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 1671 ; 5.180 ;10.000
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 : NONE
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NONE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MAS
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NONE
REMARK 4
REMARK 4 1HL7 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 14-MAR-2003.
REMARK 100 THE EBI ID CODE IS EBI-12338.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-2001
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG BEAMLINE X11
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8482
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 118797
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.73
REMARK 200 RESOLUTION RANGE LOW (A) : 11
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100
REMARK 200 DATA REDUNDANCY : 7.5
REMARK 200 R MERGE (I) : 0.079
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 28.18
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 100
REMARK 200 DATA REDUNDANCY IN SHELL : 7.2
REMARK 200 R MERGE FOR SHELL (I) : 0.345
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.5
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1BRO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X,1/2+Y,1/2+Z
REMARK 290 14555 -X,1/2-Y,1/2+Z
REMARK 290 15555 -X,1/2+Y,1/2-Z
REMARK 290 16555 X,1/2-Y,1/2-Z
REMARK 290 17555 Z,1/2+X,1/2+Y
REMARK 290 18555 Z,1/2-X,1/2-Y
REMARK 290 19555 -Z,1/2-X,1/2+Y
REMARK 290 20555 -Z,1/2+X,1/2-Y
REMARK 290 21555 Y,1/2+Z,1/2+X
REMARK 290 22555 -Y,1/2+Z,1/2-X
REMARK 290 23555 Y,1/2-Z,1/2-X
REMARK 290 24555 -Y,1/2-Z,1/2+X
REMARK 290 25555 1/2+X,Y,1/2+Z
REMARK 290 26555 1/2-X,-Y,1/2+Z
REMARK 290 27555 1/2-X,Y,1/2-Z
REMARK 290 28555 1/2+X,-Y,1/2-Z
REMARK 290 29555 1/2+Z,X,1/2+Y
REMARK 290 30555 1/2+Z,-X,1/2-Y
REMARK 290 31555 1/2-Z,-X,1/2+Y
REMARK 290 32555 1/2-Z,X,1/2-Y
REMARK 290 33555 1/2+Y,Z,1/2+X
REMARK 290 34555 1/2-Y,Z,1/2-X
REMARK 290 35555 1/2+Y,-Z,1/2-X
REMARK 290 36555 1/2-Y,-Z,1/2+X
REMARK 290 37555 1/2+X,1/2+Y,Z
REMARK 290 38555 1/2-X,1/2-Y,Z
REMARK 290 39555 1/2-X,1/2+Y,-Z
REMARK 290 40555 1/2+X,1/2-Y,-Z
REMARK 290 41555 1/2+Z,1/2+X,Y
REMARK 290 42555 1/2+Z,1/2-X,-Y
REMARK 290 43555 1/2-Z,1/2-X,Y
REMARK 290 44555 1/2-Z,1/2+X,-Y
REMARK 290 45555 1/2+Y,1/2+Z,X
REMARK 290 46555 1/2-Y,1/2+Z,-X
REMARK 290 47555 1/2+Y,1/2-Z,-X
REMARK 290 48555 1/2-Y,1/2-Z,X
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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 120.29600
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 120.29600
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 120.29600
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 120.29600
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 120.29600
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 120.29600
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 120.29600
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 120.29600
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 120.29600
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 120.29600
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 120.29600
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 120.29600
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 120.29600
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 120.29600
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 120.29600
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 120.29600
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 120.29600
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 120.29600
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 120.29600
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 120.29600
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 120.29600
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 120.29600
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 120.29600
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 120.29600
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 120.29600
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 120.29600
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 120.29600
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 120.29600
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 120.29600
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 120.29600
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 120.29600
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 120.29600
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY1 37 1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY2 37 0.000000 1.000000 0.000000 120.29600
REMARK 290 SMTRY3 37 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 38 -1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY2 38 0.000000 -1.000000 0.000000 120.29600
REMARK 290 SMTRY3 38 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 39 -1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY2 39 0.000000 1.000000 0.000000 120.29600
REMARK 290 SMTRY3 39 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 40 1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY2 40 0.000000 -1.000000 0.000000 120.29600
REMARK 290 SMTRY3 40 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 41 0.000000 0.000000 1.000000 120.29600
REMARK 290 SMTRY2 41 1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY3 41 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 42 0.000000 0.000000 1.000000 120.29600
REMARK 290 SMTRY2 42 -1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY3 42 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 43 0.000000 0.000000 -1.000000 120.29600
REMARK 290 SMTRY2 43 -1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY3 43 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 44 0.000000 0.000000 -1.000000 120.29600
REMARK 290 SMTRY2 44 1.000000 0.000000 0.000000 120.29600
REMARK 290 SMTRY3 44 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 45 0.000000 1.000000 0.000000 120.29600
REMARK 290 SMTRY2 45 0.000000 0.000000 1.000000 120.29600
REMARK 290 SMTRY3 45 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 46 0.000000 -1.000000 0.000000 120.29600
REMARK 290 SMTRY2 46 0.000000 0.000000 1.000000 120.29600
REMARK 290 SMTRY3 46 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 47 0.000000 1.000000 0.000000 120.29600
REMARK 290 SMTRY2 47 0.000000 0.000000 -1.000000 120.29600
REMARK 290 SMTRY3 47 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 48 0.000000 -1.000000 0.000000 120.29600
REMARK 290 SMTRY2 48 0.000000 0.000000 -1.000000 120.29600
REMARK 290 SMTRY3 48 1.000000 0.000000 0.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 A 1 .. 279 B 1 .. 279 0.219
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: TRIMERIC
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 350 BIOMT1 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 120.29600
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 120.29600
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 120.29600
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 120.29600
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350 BIOMT1 2 0.000000 -1.000000 0.000000 120.29600
REMARK 350 BIOMT2 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 2 -1.000000 0.000000 0.000000 120.29600
REMARK 350 BIOMT1 3 0.000000 0.000000 -1.000000 120.29600
REMARK 350 BIOMT2 3 -1.000000 0.000000 0.000000 120.29600
REMARK 350 BIOMT3 3 0.000000 1.000000 0.000000 0.00000
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TYR A 2 CE1 - CZ - OH ANGL. DEV. = -8.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 525 B Y
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 FORMS TETRAHEDRAL INTERMEDIATE WITH
REMARK 600 ACTIVE SITE SERINE A98 AND B98
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: BD1 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: BD1 BINDING SITE FOR CHAIN B
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HKH RELATED DB: PDB
REMARK 900 UNLIGATED GAMMA LACTAMASE FROM AN
REMARK 900 AUREOBACTERIUM SPECIES
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 NAMED CO-FACTOR FREE HALOPEROXIDASE DUE TO HIGH SEQUENCE ID
DBREF 1HL7 A 1 279 SWS Q8GJP7 Q8GJP7 2 280
DBREF 1HL7 B 1 279 SWS Q8GJP7 Q8GJP7 2 280
SEQRES 1 A 279 GLY TYR ILE THR VAL GLY ASN GLU ASN SER THR PRO ILE
SEQRES 2 A 279 GLU LEU TYR TYR GLU ASP GLN GLY SER GLY GLN PRO VAL
SEQRES 3 A 279 VAL LEU ILE HIS GLY TYR PRO LEU ASP GLY HIS SER TRP
SEQRES 4 A 279 GLU ARG GLN THR ARG GLU LEU LEU ALA GLN GLY TYR ARG
SEQRES 5 A 279 VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLY SER SER
SEQRES 6 A 279 LYS VAL ASN THR GLY TYR ASP TYR ASP THR PHE ALA ALA
SEQRES 7 A 279 ASP LEU HIS THR VAL LEU GLU THR LEU ASP LEU ARG ASP
SEQRES 8 A 279 VAL VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU LEU
SEQRES 9 A 279 ALA ARG TYR VAL ALA ARG TYR GLY HIS GLU ARG VAL ALA
SEQRES 10 A 279 LYS LEU ALA PHE LEU ALA SER LEU GLU PRO PHE LEU VAL
SEQRES 11 A 279 GLN ARG ASP ASP ASN PRO GLU GLY VAL PRO GLN GLU VAL
SEQRES 12 A 279 PHE ASP GLY ILE GLU ALA ALA ALA LYS GLY ASP ARG PHE
SEQRES 13 A 279 ALA TRP PHE THR ASP PHE TYR LYS ASN PHE TYR ASN LEU
SEQRES 14 A 279 ASP GLU ASN LEU GLY SER ARG ILE SER GLU GLN ALA VAL
SEQRES 15 A 279 THR GLY SER TRP ASN VAL ALA ILE GLY SER ALA PRO VAL
SEQRES 16 A 279 ALA ALA TYR ALA VAL VAL PRO ALA TRP ILE GLU ASP PHE
SEQRES 17 A 279 ARG SER ASP VAL GLU ALA VAL ARG ALA ALA GLY LYS PRO
SEQRES 18 A 279 THR LEU ILE LEU HIS GLY THR LYS ASP ASN ILE LEU PRO
SEQRES 19 A 279 ILE ASP ALA THR ALA ARG ARG PHE HIS GLN ALA VAL PRO
SEQRES 20 A 279 GLU ALA ASP TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY
SEQRES 21 A 279 LEU LEU TRP THR HIS ALA ASP GLU VAL ASN ALA ALA LEU
SEQRES 22 A 279 LYS THR PHE LEU ALA LYS
SEQRES 1 B 279 GLY TYR ILE THR VAL GLY ASN GLU ASN SER THR PRO ILE
SEQRES 2 B 279 GLU LEU TYR TYR GLU ASP GLN GLY SER GLY GLN PRO VAL
SEQRES 3 B 279 VAL LEU ILE HIS GLY TYR PRO LEU ASP GLY HIS SER TRP
SEQRES 4 B 279 GLU ARG GLN THR ARG GLU LEU LEU ALA GLN GLY TYR ARG
SEQRES 5 B 279 VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLY SER SER
SEQRES 6 B 279 LYS VAL ASN THR GLY TYR ASP TYR ASP THR PHE ALA ALA
SEQRES 7 B 279 ASP LEU HIS THR VAL LEU GLU THR LEU ASP LEU ARG ASP
SEQRES 8 B 279 VAL VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU LEU
SEQRES 9 B 279 ALA ARG TYR VAL ALA ARG TYR GLY HIS GLU ARG VAL ALA
SEQRES 10 B 279 LYS LEU ALA PHE LEU ALA SER LEU GLU PRO PHE LEU VAL
SEQRES 11 B 279 GLN ARG ASP ASP ASN PRO GLU GLY VAL PRO GLN GLU VAL
SEQRES 12 B 279 PHE ASP GLY ILE GLU ALA ALA ALA LYS GLY ASP ARG PHE
SEQRES 13 B 279 ALA TRP PHE THR ASP PHE TYR LYS ASN PHE TYR ASN LEU
SEQRES 14 B 279 ASP GLU ASN LEU GLY SER ARG ILE SER GLU GLN ALA VAL
SEQRES 15 B 279 THR GLY SER TRP ASN VAL ALA ILE GLY SER ALA PRO VAL
SEQRES 16 B 279 ALA ALA TYR ALA VAL VAL PRO ALA TRP ILE GLU ASP PHE
SEQRES 17 B 279 ARG SER ASP VAL GLU ALA VAL ARG ALA ALA GLY LYS PRO
SEQRES 18 B 279 THR LEU ILE LEU HIS GLY THR LYS ASP ASN ILE LEU PRO
SEQRES 19 B 279 ILE ASP ALA THR ALA ARG ARG PHE HIS GLN ALA VAL PRO
SEQRES 20 B 279 GLU ALA ASP TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY
SEQRES 21 B 279 LEU LEU TRP THR HIS ALA ASP GLU VAL ASN ALA ALA LEU
SEQRES 22 B 279 LYS THR PHE LEU ALA LYS
HET BD1 A1280 10 SEE REMARK 600
HET BD1 B1280 10 SEE REMARK 600
HETNAM BD1 3A,4,7,7A-TETRAHYDRO-BENZO [1,3] DIOXOL-2-ONE
FORMUL 3 BD1 2(C7 H10 O3)
FORMUL 4 HOH *681(H2 O1)
HELIX 1 1 ASP A 35 SER A 38 5 4
HELIX 2 2 TRP A 39 GLN A 49 1 11
HELIX 3 3 ASP A 72 LEU A 87 1 16
HELIX 4 4 MET A 99 GLY A 112 1 14
HELIX 5 5 PRO A 140 ASP A 154 1 15
HELIX 6 6 ASP A 154 ASN A 168 1 15
HELIX 7 7 ASN A 168 LEU A 173 1 6
HELIX 8 8 SER A 178 GLY A 191 1 14
HELIX 9 9 VAL A 195 VAL A 200 1 6
HELIX 10 10 VAL A 200 ILE A 205 1 6
HELIX 11 11 PHE A 208 GLY A 219 1 12
HELIX 12 12 THR A 238 VAL A 246 1 9
HELIX 13 13 GLY A 260 HIS A 265 1 6
HELIX 14 14 HIS A 265 LYS A 279 1 15
HELIX 15 15 ASP B 35 SER B 38 5 4
HELIX 16 16 TRP B 39 GLN B 49 1 11
HELIX 17 17 ASP B 72 LEU B 87 1 16
HELIX 18 18 MET B 99 GLY B 112 1 14
HELIX 19 19 PRO B 140 ASP B 154 1 15
HELIX 20 20 ASP B 154 ASN B 168 1 15
HELIX 21 21 ASN B 168 LEU B 173 1 6
HELIX 22 22 SER B 178 GLY B 191 1 14
HELIX 23 23 VAL B 195 VAL B 200 1 6
HELIX 24 24 VAL B 200 ILE B 205 1 6
HELIX 25 25 PHE B 208 GLY B 219 1 12
HELIX 26 26 THR B 238 VAL B 246 1 9
HELIX 27 27 GLY B 260 HIS B 265 1 6
HELIX 28 28 HIS B 265 LYS B 279 1 15
SHEET 1 AA 8 TYR A 2 GLU A 8 0
SHEET 2 AA 8 THR A 11 GLY A 21 -1 O THR A 11 N GLU A 8
SHEET 3 AA 8 ARG A 52 TYR A 56 -1 O VAL A 53 N GLN A 20
SHEET 4 AA 8 PRO A 25 ILE A 29 1 O VAL A 26 N ILE A 54
SHEET 5 AA 8 VAL A 92 PHE A 97 1 O VAL A 93 N VAL A 27
SHEET 6 AA 8 VAL A 116 LEU A 122 1 N ALA A 117 O VAL A 92
SHEET 7 AA 8 THR A 222 GLY A 227 1 O LEU A 223 N PHE A 121
SHEET 8 AA 8 ASP A 250 VAL A 254 1 O ASP A 250 N ILE A 224
SHEET 1 BA 8 TYR B 2 GLU B 8 0
SHEET 2 BA 8 THR B 11 GLY B 21 -1 O THR B 11 N GLU B 8
SHEET 3 BA 8 ARG B 52 TYR B 56 -1 O VAL B 53 N GLN B 20
SHEET 4 BA 8 PRO B 25 ILE B 29 1 O VAL B 26 N ILE B 54
SHEET 5 BA 8 VAL B 92 PHE B 97 1 O VAL B 93 N VAL B 27
SHEET 6 BA 8 VAL B 116 LEU B 122 1 N ALA B 117 O VAL B 92
SHEET 7 BA 8 THR B 222 GLY B 227 1 O LEU B 223 N PHE B 121
SHEET 8 BA 8 ASP B 250 VAL B 254 1 O ASP B 250 N ILE B 224
LINK OG SER A 98 C7 BD1 A1280 1555 1555
LINK OG SER B 98 C7 BD1 B1280 1555 1555
CISPEP 1 TYR A 32 PRO A 33 0 -7.74
CISPEP 2 GLU A 126 PRO A 127 0 1.27
CISPEP 3 TYR B 32 PRO B 33 0 -7.67
CISPEP 4 GLU B 126 PRO B 127 0 2.19
SITE 1 AC1 10 GLY A 31 TYR A 32 PHE A 97 SER A 98
SITE 2 AC1 10 MET A 99 LEU A 125 PHE A 166 ILE A 232
SITE 3 AC1 10 LEU A 233 HIS A 259
SITE 1 AC2 11 GLY B 31 TYR B 32 PHE B 97 SER B 98
SITE 2 AC2 11 MET B 99 LEU B 125 PHE B 166 TRP B 204
SITE 3 AC2 11 ILE B 232 LEU B 233 HIS B 259
CRYST1 240.592 240.592 240.592 90.00 90.00 90.00 F 2 3 96
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 0.004156 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004156 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004156 0.00000
MTRIX1 1 0.327440 0.778490 -0.535480 99.54680 1
MTRIX2 1 0.539320 0.311340 0.782430 -112.77448 1
MTRIX3 1 0.775830 -0.545000 -0.317910 -8.95121 1
TER 2220 LYS A 279
TER 4446 LYS B 279
MASTER 463 0 2 28 16 0 6 9 5145 2 22 44
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