HEADER OXIDOREDUCTASE 30-SEP-03 1R31
TITLE HMG-COA REDUCTASE FROM PSEUDOMONAS MEVALONII COMPLEXED WITH HMG-COA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HMG-COA REDUCTASE;
COMPND 5 EC: 1.1.1.88;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS MEVALONII;
SOURCE 3 ORGANISM_TAXID: 32044;
SOURCE 4 GENE: MVAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21[DE3];
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHMGR (RODWELL, 1989)
KEYWDS 4-ELECTRON OXIDO-REDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.WATSON,C.N.STEUSSY,J.W.BURGNER,C.M.LAWRENCE,L.TABERNERO,
AUTHOR 2 V.W.RODWELL,C.V.STAUFFACHER
REVDAT 4 03-APR-24 1R31 1 REMARK
REVDAT 3 14-FEB-24 1R31 1 REMARK
REVDAT 2 24-FEB-09 1R31 1 VERSN
REVDAT 1 14-OCT-03 1R31 0
JRNL AUTH J.M.WATSON,C.N.STEUSSY,J.W.BURGNER,C.M.LAWRENCE,L.TABERNERO,
JRNL AUTH 2 V.W.RODWELL,C.V.STAUFFACHER
JRNL TITL STRUCTURAL INVESTIGATIONS OF THE BASIS FOR STEREOSELECTIVITY
JRNL TITL 2 FROM THE BINARY COMPLEX OF HMG-COA REDUCTASE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 53328
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 SET) : 0.220
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4332
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7748
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 708
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5573
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 319
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.09
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.25
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.28
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.240 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.530 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.650 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.320 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.53
REMARK 3 BSOL : 112.5
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R31 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020374.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JAN-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.050
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53328
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NATIVE HMGR MODEL AT 3.0A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M AMMONIUM SULFATE, 100 MM ADA
REMARK 280 BUFFER AT PH 6.7, MICROSEEDING, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+3/4,X+1/4,-Z+1/4
REMARK 290 14555 -Y+3/4,-X+3/4,-Z+3/4
REMARK 290 15555 Y+1/4,-X+1/4,Z+3/4
REMARK 290 16555 -Y+1/4,X+3/4,Z+1/4
REMARK 290 17555 X+3/4,Z+1/4,-Y+1/4
REMARK 290 18555 -X+1/4,Z+3/4,Y+1/4
REMARK 290 19555 -X+3/4,-Z+3/4,-Y+3/4
REMARK 290 20555 X+1/4,-Z+1/4,Y+3/4
REMARK 290 21555 Z+3/4,Y+1/4,-X+1/4
REMARK 290 22555 Z+1/4,-Y+1/4,X+3/4
REMARK 290 23555 -Z+1/4,Y+3/4,X+1/4
REMARK 290 24555 -Z+3/4,-Y+3/4,-X+3/4
REMARK 290 25555 X+1/2,Y+1/2,Z+1/2
REMARK 290 26555 -X,-Y+1/2,Z
REMARK 290 27555 -X+1/2,Y,-Z
REMARK 290 28555 X,-Y,-Z+1/2
REMARK 290 29555 Z+1/2,X+1/2,Y+1/2
REMARK 290 30555 Z,-X,-Y+1/2
REMARK 290 31555 -Z,-X+1/2,Y
REMARK 290 32555 -Z+1/2,X,-Y
REMARK 290 33555 Y+1/2,Z+1/2,X+1/2
REMARK 290 34555 -Y+1/2,Z,-X
REMARK 290 35555 Y,-Z,-X+1/2
REMARK 290 36555 -Y,-Z+1/2,X
REMARK 290 37555 Y+1/4,X+3/4,-Z+3/4
REMARK 290 38555 -Y+1/4,-X+1/4,-Z+1/4
REMARK 290 39555 Y+3/4,-X+3/4,Z+1/4
REMARK 290 40555 -Y+3/4,X+1/4,Z+3/4
REMARK 290 41555 X+1/4,Z+3/4,-Y+3/4
REMARK 290 42555 -X+3/4,Z+1/4,Y+3/4
REMARK 290 43555 -X+1/4,-Z+1/4,-Y+1/4
REMARK 290 44555 X+3/4,-Z+3/4,Y+1/4
REMARK 290 45555 Z+1/4,Y+3/4,-X+3/4
REMARK 290 46555 Z+3/4,-Y+3/4,X+1/4
REMARK 290 47555 -Z+3/4,Y+1/4,X+3/4
REMARK 290 48555 -Z+1/4,-Y+1/4,-X+1/4
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 113.68450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.68450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 113.68450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.68450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 113.68450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 113.68450
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 113.68450
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 113.68450
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 113.68450
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 113.68450
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 113.68450
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 113.68450
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 113.68450
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 113.68450
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 113.68450
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 113.68450
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 113.68450
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 113.68450
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 170.52675
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 56.84225
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 56.84225
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 170.52675
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 170.52675
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 170.52675
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 56.84225
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 56.84225
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 170.52675
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 56.84225
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 170.52675
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 56.84225
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 170.52675
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 56.84225
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 56.84225
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 56.84225
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 170.52675
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 56.84225
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 170.52675
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 170.52675
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 170.52675
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 56.84225
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 56.84225
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 170.52675
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 170.52675
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 56.84225
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 56.84225
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 56.84225
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 56.84225
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 170.52675
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 56.84225
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 170.52675
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 56.84225
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 170.52675
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 170.52675
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 170.52675
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 113.68450
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 113.68450
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 113.68450
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 113.68450
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 113.68450
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 113.68450
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 113.68450
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 113.68450
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 113.68450
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 113.68450
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 113.68450
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 113.68450
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 113.68450
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 113.68450
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 113.68450
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 113.68450
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 113.68450
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 113.68450
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 37 0.000000 1.000000 0.000000 56.84225
REMARK 290 SMTRY2 37 1.000000 0.000000 0.000000 170.52675
REMARK 290 SMTRY3 37 0.000000 0.000000 -1.000000 170.52675
REMARK 290 SMTRY1 38 0.000000 -1.000000 0.000000 56.84225
REMARK 290 SMTRY2 38 -1.000000 0.000000 0.000000 56.84225
REMARK 290 SMTRY3 38 0.000000 0.000000 -1.000000 56.84225
REMARK 290 SMTRY1 39 0.000000 1.000000 0.000000 170.52675
REMARK 290 SMTRY2 39 -1.000000 0.000000 0.000000 170.52675
REMARK 290 SMTRY3 39 0.000000 0.000000 1.000000 56.84225
REMARK 290 SMTRY1 40 0.000000 -1.000000 0.000000 170.52675
REMARK 290 SMTRY2 40 1.000000 0.000000 0.000000 56.84225
REMARK 290 SMTRY3 40 0.000000 0.000000 1.000000 170.52675
REMARK 290 SMTRY1 41 1.000000 0.000000 0.000000 56.84225
REMARK 290 SMTRY2 41 0.000000 0.000000 1.000000 170.52675
REMARK 290 SMTRY3 41 0.000000 -1.000000 0.000000 170.52675
REMARK 290 SMTRY1 42 -1.000000 0.000000 0.000000 170.52675
REMARK 290 SMTRY2 42 0.000000 0.000000 1.000000 56.84225
REMARK 290 SMTRY3 42 0.000000 1.000000 0.000000 170.52675
REMARK 290 SMTRY1 43 -1.000000 0.000000 0.000000 56.84225
REMARK 290 SMTRY2 43 0.000000 0.000000 -1.000000 56.84225
REMARK 290 SMTRY3 43 0.000000 -1.000000 0.000000 56.84225
REMARK 290 SMTRY1 44 1.000000 0.000000 0.000000 170.52675
REMARK 290 SMTRY2 44 0.000000 0.000000 -1.000000 170.52675
REMARK 290 SMTRY3 44 0.000000 1.000000 0.000000 56.84225
REMARK 290 SMTRY1 45 0.000000 0.000000 1.000000 56.84225
REMARK 290 SMTRY2 45 0.000000 1.000000 0.000000 170.52675
REMARK 290 SMTRY3 45 -1.000000 0.000000 0.000000 170.52675
REMARK 290 SMTRY1 46 0.000000 0.000000 1.000000 170.52675
REMARK 290 SMTRY2 46 0.000000 -1.000000 0.000000 170.52675
REMARK 290 SMTRY3 46 1.000000 0.000000 0.000000 56.84225
REMARK 290 SMTRY1 47 0.000000 0.000000 -1.000000 170.52675
REMARK 290 SMTRY2 47 0.000000 1.000000 0.000000 56.84225
REMARK 290 SMTRY3 47 1.000000 0.000000 0.000000 170.52675
REMARK 290 SMTRY1 48 0.000000 0.000000 -1.000000 56.84225
REMARK 290 SMTRY2 48 0.000000 -1.000000 0.000000 56.84225
REMARK 290 SMTRY3 48 -1.000000 0.000000 0.000000 56.84225
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 44050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 69360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -273.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 26300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -186.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 -56.84225
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 56.84225
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 284.21125
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ARG A 379
REMARK 465 GLY A 380
REMARK 465 HIS A 381
REMARK 465 MET A 382
REMARK 465 ALA A 383
REMARK 465 LEU A 384
REMARK 465 HIS A 385
REMARK 465 ALA A 386
REMARK 465 ARG A 387
REMARK 465 ASN A 388
REMARK 465 ILE A 389
REMARK 465 ALA A 390
REMARK 465 VAL A 391
REMARK 465 VAL A 392
REMARK 465 ALA A 393
REMARK 465 GLY A 394
REMARK 465 ALA A 395
REMARK 465 ARG A 396
REMARK 465 GLY A 397
REMARK 465 ASP A 398
REMARK 465 GLU A 399
REMARK 465 VAL A 400
REMARK 465 ASP A 401
REMARK 465 TRP A 402
REMARK 465 VAL A 403
REMARK 465 ALA A 404
REMARK 465 ARG A 405
REMARK 465 GLN A 406
REMARK 465 LEU A 407
REMARK 465 VAL A 408
REMARK 465 GLU A 409
REMARK 465 TYR A 410
REMARK 465 HIS A 411
REMARK 465 ASP A 412
REMARK 465 VAL A 413
REMARK 465 ARG A 414
REMARK 465 ALA A 415
REMARK 465 ASP A 416
REMARK 465 ARG A 417
REMARK 465 ALA A 418
REMARK 465 VAL A 419
REMARK 465 ALA A 420
REMARK 465 LEU A 421
REMARK 465 LEU A 422
REMARK 465 LYS A 423
REMARK 465 GLN A 424
REMARK 465 LYS A 425
REMARK 465 ARG A 426
REMARK 465 GLY A 427
REMARK 465 GLN A 428
REMARK 465 MET B 501
REMARK 465 SER B 502
REMARK 465 GLN B 878
REMARK 465 ARG B 879
REMARK 465 GLY B 880
REMARK 465 HIS B 881
REMARK 465 MET B 882
REMARK 465 ALA B 883
REMARK 465 LEU B 884
REMARK 465 HIS B 885
REMARK 465 ALA B 886
REMARK 465 ARG B 887
REMARK 465 ASN B 888
REMARK 465 ILE B 889
REMARK 465 ALA B 890
REMARK 465 VAL B 891
REMARK 465 VAL B 892
REMARK 465 ALA B 893
REMARK 465 GLY B 894
REMARK 465 ALA B 895
REMARK 465 ARG B 896
REMARK 465 GLY B 897
REMARK 465 ASP B 898
REMARK 465 GLU B 899
REMARK 465 VAL B 900
REMARK 465 ASP B 901
REMARK 465 TRP B 902
REMARK 465 VAL B 903
REMARK 465 ALA B 904
REMARK 465 ARG B 905
REMARK 465 GLN B 906
REMARK 465 LEU B 907
REMARK 465 VAL B 908
REMARK 465 GLU B 909
REMARK 465 TYR B 910
REMARK 465 HIS B 911
REMARK 465 ASP B 912
REMARK 465 VAL B 913
REMARK 465 ARG B 914
REMARK 465 ALA B 915
REMARK 465 ASP B 916
REMARK 465 ARG B 917
REMARK 465 ALA B 918
REMARK 465 VAL B 919
REMARK 465 ALA B 920
REMARK 465 LEU B 921
REMARK 465 LEU B 922
REMARK 465 LYS B 923
REMARK 465 GLN B 924
REMARK 465 LYS B 925
REMARK 465 ARG B 926
REMARK 465 GLY B 927
REMARK 465 GLN B 928
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 PRO A 84 CD PRO A 84 N -0.251
REMARK 500 PRO A 324 CD PRO A 324 N -0.257
REMARK 500 HIS B 521 C ILE B 522 N 0.158
REMARK 500 PRO B 584 CD PRO B 584 N -0.271
REMARK 500 GLU B 875 C GLY B 876 N -0.142
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 VAL B 619 CB - CA - C ANGL. DEV. = -14.5 DEGREES
REMARK 500 PRO B 671 C - N - CD ANGL. DEV. = -20.5 DEGREES
REMARK 500 PRO B 671 CA - N - CD ANGL. DEV. = -17.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 85 -6.35 75.22
REMARK 500 ASP A 158 -179.47 -175.34
REMARK 500 ARG A 182 -140.50 58.64
REMARK 500 ASP A 183 31.35 -71.22
REMARK 500 ALA A 187 -70.26 -44.57
REMARK 500 ARG A 210 -83.87 -108.19
REMARK 500 THR A 374 -97.14 -102.07
REMARK 500 ALA B 509 12.46 59.17
REMARK 500 ARG B 682 -141.13 65.33
REMARK 500 ALA B 687 -70.02 -44.20
REMARK 500 ARG B 710 -92.57 -105.48
REMARK 500 ASN B 811 -8.66 -57.71
REMARK 500 MET B 823 77.71 -150.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE HMG-COA LIGAND WAS FOUND DIVIDED INTO
REMARK 600 SEPARATE MEVALDEHYDE AND COA MOLECULES IN
REMARK 600 THE STRUCTURE.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MEV A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MEV B 1004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QAX RELATED DB: PDB
REMARK 900 RELATED ID: 1QAY RELATED DB: PDB
DBREF 1R31 A 1 428 UNP P13702 MVAA_PSEMV 1 428
DBREF 1R31 B 501 928 UNP P13702 MVAA_PSEMV 1 428
SEQRES 1 A 428 MET SER LEU ASP SER ARG LEU PRO ALA PHE ARG ASN LEU
SEQRES 2 A 428 SER PRO ALA ALA ARG LEU ASP HIS ILE GLY GLN LEU LEU
SEQRES 3 A 428 GLY LEU SER HIS ASP ASP VAL SER LEU LEU ALA ASN ALA
SEQRES 4 A 428 GLY ALA LEU PRO MET ASP ILE ALA ASN GLY MET ILE GLU
SEQRES 5 A 428 ASN VAL ILE GLY THR PHE GLU LEU PRO TYR ALA VAL ALA
SEQRES 6 A 428 SER ASN PHE GLN ILE ASN GLY ARG ASP VAL LEU VAL PRO
SEQRES 7 A 428 LEU VAL VAL GLU GLU PRO SER ILE VAL ALA ALA ALA SER
SEQRES 8 A 428 TYR MET ALA LYS LEU ALA ARG ALA ASN GLY GLY PHE THR
SEQRES 9 A 428 THR SER SER SER ALA PRO LEU MET HIS ALA GLN VAL GLN
SEQRES 10 A 428 ILE VAL GLY ILE GLN ASP PRO LEU ASN ALA ARG LEU SER
SEQRES 11 A 428 LEU LEU ARG ARG LYS ASP GLU ILE ILE GLU LEU ALA ASN
SEQRES 12 A 428 ARG LYS ASP GLN LEU LEU ASN SER LEU GLY GLY GLY CYS
SEQRES 13 A 428 ARG ASP ILE GLU VAL HIS THR PHE ALA ASP THR PRO ARG
SEQRES 14 A 428 GLY PRO MET LEU VAL ALA HIS LEU ILE VAL ASP VAL ARG
SEQRES 15 A 428 ASP ALA MET GLY ALA ASN THR VAL ASN THR MET ALA GLU
SEQRES 16 A 428 ALA VAL ALA PRO LEU MET GLU ALA ILE THR GLY GLY GLN
SEQRES 17 A 428 VAL ARG LEU ARG ILE LEU SER ASN LEU ALA ASP LEU ARG
SEQRES 18 A 428 LEU ALA ARG ALA GLN VAL ARG ILE THR PRO GLN GLN LEU
SEQRES 19 A 428 GLU THR ALA GLU PHE SER GLY GLU ALA VAL ILE GLU GLY
SEQRES 20 A 428 ILE LEU ASP ALA TYR ALA PHE ALA ALA VAL ASP PRO TYR
SEQRES 21 A 428 ARG ALA ALA THR HIS ASN LYS GLY ILE MET ASN GLY ILE
SEQRES 22 A 428 ASP PRO LEU ILE VAL ALA THR GLY ASN ASP TRP ARG ALA
SEQRES 23 A 428 VAL GLU ALA GLY ALA HIS ALA TYR ALA CYS ARG SER GLY
SEQRES 24 A 428 HIS TYR GLY SER LEU THR THR TRP GLU LYS ASP ASN ASN
SEQRES 25 A 428 GLY HIS LEU VAL GLY THR LEU GLU MET PRO MET PRO VAL
SEQRES 26 A 428 GLY LEU VAL GLY GLY ALA THR LYS THR HIS PRO LEU ALA
SEQRES 27 A 428 GLN LEU SER LEU ARG ILE LEU GLY VAL LYS THR ALA GLN
SEQRES 28 A 428 ALA LEU ALA GLU ILE ALA VAL ALA VAL GLY LEU ALA GLN
SEQRES 29 A 428 ASN LEU GLY ALA MET ARG ALA LEU ALA THR GLU GLY ILE
SEQRES 30 A 428 GLN ARG GLY HIS MET ALA LEU HIS ALA ARG ASN ILE ALA
SEQRES 31 A 428 VAL VAL ALA GLY ALA ARG GLY ASP GLU VAL ASP TRP VAL
SEQRES 32 A 428 ALA ARG GLN LEU VAL GLU TYR HIS ASP VAL ARG ALA ASP
SEQRES 33 A 428 ARG ALA VAL ALA LEU LEU LYS GLN LYS ARG GLY GLN
SEQRES 1 B 428 MET SER LEU ASP SER ARG LEU PRO ALA PHE ARG ASN LEU
SEQRES 2 B 428 SER PRO ALA ALA ARG LEU ASP HIS ILE GLY GLN LEU LEU
SEQRES 3 B 428 GLY LEU SER HIS ASP ASP VAL SER LEU LEU ALA ASN ALA
SEQRES 4 B 428 GLY ALA LEU PRO MET ASP ILE ALA ASN GLY MET ILE GLU
SEQRES 5 B 428 ASN VAL ILE GLY THR PHE GLU LEU PRO TYR ALA VAL ALA
SEQRES 6 B 428 SER ASN PHE GLN ILE ASN GLY ARG ASP VAL LEU VAL PRO
SEQRES 7 B 428 LEU VAL VAL GLU GLU PRO SER ILE VAL ALA ALA ALA SER
SEQRES 8 B 428 TYR MET ALA LYS LEU ALA ARG ALA ASN GLY GLY PHE THR
SEQRES 9 B 428 THR SER SER SER ALA PRO LEU MET HIS ALA GLN VAL GLN
SEQRES 10 B 428 ILE VAL GLY ILE GLN ASP PRO LEU ASN ALA ARG LEU SER
SEQRES 11 B 428 LEU LEU ARG ARG LYS ASP GLU ILE ILE GLU LEU ALA ASN
SEQRES 12 B 428 ARG LYS ASP GLN LEU LEU ASN SER LEU GLY GLY GLY CYS
SEQRES 13 B 428 ARG ASP ILE GLU VAL HIS THR PHE ALA ASP THR PRO ARG
SEQRES 14 B 428 GLY PRO MET LEU VAL ALA HIS LEU ILE VAL ASP VAL ARG
SEQRES 15 B 428 ASP ALA MET GLY ALA ASN THR VAL ASN THR MET ALA GLU
SEQRES 16 B 428 ALA VAL ALA PRO LEU MET GLU ALA ILE THR GLY GLY GLN
SEQRES 17 B 428 VAL ARG LEU ARG ILE LEU SER ASN LEU ALA ASP LEU ARG
SEQRES 18 B 428 LEU ALA ARG ALA GLN VAL ARG ILE THR PRO GLN GLN LEU
SEQRES 19 B 428 GLU THR ALA GLU PHE SER GLY GLU ALA VAL ILE GLU GLY
SEQRES 20 B 428 ILE LEU ASP ALA TYR ALA PHE ALA ALA VAL ASP PRO TYR
SEQRES 21 B 428 ARG ALA ALA THR HIS ASN LYS GLY ILE MET ASN GLY ILE
SEQRES 22 B 428 ASP PRO LEU ILE VAL ALA THR GLY ASN ASP TRP ARG ALA
SEQRES 23 B 428 VAL GLU ALA GLY ALA HIS ALA TYR ALA CYS ARG SER GLY
SEQRES 24 B 428 HIS TYR GLY SER LEU THR THR TRP GLU LYS ASP ASN ASN
SEQRES 25 B 428 GLY HIS LEU VAL GLY THR LEU GLU MET PRO MET PRO VAL
SEQRES 26 B 428 GLY LEU VAL GLY GLY ALA THR LYS THR HIS PRO LEU ALA
SEQRES 27 B 428 GLN LEU SER LEU ARG ILE LEU GLY VAL LYS THR ALA GLN
SEQRES 28 B 428 ALA LEU ALA GLU ILE ALA VAL ALA VAL GLY LEU ALA GLN
SEQRES 29 B 428 ASN LEU GLY ALA MET ARG ALA LEU ALA THR GLU GLY ILE
SEQRES 30 B 428 GLN ARG GLY HIS MET ALA LEU HIS ALA ARG ASN ILE ALA
SEQRES 31 B 428 VAL VAL ALA GLY ALA ARG GLY ASP GLU VAL ASP TRP VAL
SEQRES 32 B 428 ALA ARG GLN LEU VAL GLU TYR HIS ASP VAL ARG ALA ASP
SEQRES 33 B 428 ARG ALA VAL ALA LEU LEU LYS GLN LYS ARG GLY GLN
HET SO4 A1000 5
HET COA A1002 48
HET MEV A1003 10
HET SO4 B1001 5
HET MEV B1004 10
HETNAM SO4 SULFATE ION
HETNAM COA COENZYME A
HETNAM MEV (R)-MEVALONATE
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 COA C21 H36 N7 O16 P3 S
FORMUL 5 MEV 2(C6 H11 O4 1-)
FORMUL 8 HOH *319(H2 O)
HELIX 1 1 ALA A 9 LEU A 13 5 5
HELIX 2 2 SER A 14 GLY A 27 1 14
HELIX 3 3 SER A 29 ASN A 38 1 10
HELIX 4 4 PRO A 43 ILE A 51 1 9
HELIX 5 5 SER A 85 ALA A 99 1 15
HELIX 6 6 ASP A 123 ARG A 134 1 12
HELIX 7 7 ARG A 134 ARG A 144 1 11
HELIX 8 8 ASP A 146 LEU A 152 1 7
HELIX 9 9 GLY A 186 GLY A 206 1 21
HELIX 10 10 THR A 230 GLU A 235 1 6
HELIX 11 11 SER A 240 ASP A 258 1 19
HELIX 12 12 ASP A 258 THR A 280 1 23
HELIX 13 13 ASP A 283 CYS A 296 1 14
HELIX 14 14 GLY A 330 HIS A 335 1 6
HELIX 15 15 HIS A 335 GLY A 346 1 12
HELIX 16 16 THR A 349 THR A 374 1 26
HELIX 17 17 ALA B 509 LEU B 513 5 5
HELIX 18 18 SER B 514 GLY B 527 1 14
HELIX 19 19 SER B 529 ASN B 538 1 10
HELIX 20 20 PRO B 543 ILE B 551 1 9
HELIX 21 21 SER B 585 ALA B 599 1 15
HELIX 22 22 ASP B 623 ARG B 634 1 12
HELIX 23 23 ARG B 634 ASP B 646 1 13
HELIX 24 24 ASP B 646 LEU B 652 1 7
HELIX 25 25 GLY B 686 GLY B 706 1 21
HELIX 26 26 THR B 730 GLU B 735 1 6
HELIX 27 27 SER B 740 ASP B 758 1 19
HELIX 28 28 ASP B 758 THR B 780 1 23
HELIX 29 29 ASP B 783 CYS B 796 1 14
HELIX 30 30 GLY B 830 HIS B 835 1 6
HELIX 31 31 HIS B 835 GLY B 846 1 12
HELIX 32 32 THR B 849 GLU B 875 1 27
SHEET 1 A 4 VAL A 77 VAL A 80 0
SHEET 2 A 4 VAL A 54 ALA A 65 -1 N ALA A 65 O VAL A 77
SHEET 3 A 4 VAL B 554 ALA B 565 -1 O ILE B 555 N TYR A 62
SHEET 4 A 4 VAL B 577 VAL B 580 -1 O VAL B 577 N ALA B 565
SHEET 1 B 2 GLN A 69 ILE A 70 0
SHEET 2 B 2 ARG A 73 ASP A 74 -1 O ARG A 73 N ILE A 70
SHEET 1 C 4 THR A 104 SER A 107 0
SHEET 2 C 4 LEU A 222 ILE A 229 -1 O ARG A 224 N SER A 106
SHEET 3 C 4 LEU A 315 PRO A 322 -1 O LEU A 315 N ILE A 229
SHEET 4 C 4 THR A 305 LYS A 309 -1 N GLU A 308 O VAL A 316
SHEET 1 D 4 GLY A 155 PHE A 164 0
SHEET 2 D 4 MET A 172 ASP A 180 -1 O VAL A 174 N HIS A 162
SHEET 3 D 4 LEU A 111 VAL A 119 -1 N ILE A 118 O LEU A 173
SHEET 4 D 4 GLN A 208 LEU A 214 -1 O GLN A 208 N VAL A 119
SHEET 1 E 2 GLN B 569 ILE B 570 0
SHEET 2 E 2 ARG B 573 ASP B 574 -1 O ARG B 573 N ILE B 570
SHEET 1 F 4 THR B 604 SER B 607 0
SHEET 2 F 4 LEU B 722 ILE B 729 -1 O ARG B 724 N SER B 606
SHEET 3 F 4 LEU B 815 PRO B 822 -1 O LEU B 815 N ILE B 729
SHEET 4 F 4 THR B 805 LYS B 809 -1 N GLU B 808 O VAL B 816
SHEET 1 G 4 GLY B 655 PHE B 664 0
SHEET 2 G 4 MET B 672 ASP B 680 -1 O VAL B 674 N HIS B 662
SHEET 3 G 4 LEU B 611 ILE B 618 -1 N ILE B 618 O LEU B 673
SHEET 4 G 4 VAL B 709 LEU B 714 -1 O ILE B 713 N GLN B 615
SITE 1 AC1 7 ALA A 184 MET A 185 GLY A 186 ALA A 187
SITE 2 AC1 7 ASN A 188 THR A 189 HOH A1037
SITE 1 AC2 6 HOH B 21 ALA B 684 MET B 685 GLY B 686
SITE 2 AC2 6 ALA B 687 ASN B 688
SITE 1 AC3 21 ARG A 11 ASN A 67 GLU A 83 PRO A 84
SITE 2 AC3 21 SER A 85 ALA A 88 TYR A 92 LYS A 95
SITE 3 AC3 21 GLN A 364 GLY A 367 ALA A 368 ARG A 370
SITE 4 AC3 21 ALA A 371 MEV A1003 HOH A1048 HOH A1055
SITE 5 AC3 21 HOH A1057 HOH A1121 HOH A1130 GLU B 552
SITE 6 AC3 21 ASN B 553
SITE 1 AC4 12 GLU A 83 ARG A 261 THR A 264 LYS A 267
SITE 2 AC4 12 ASN A 271 ALA A 368 LEU A 372 ILE A 377
SITE 3 AC4 12 COA A1002 HOH A1014 HOH A1188 HOH B 17
SITE 1 AC5 9 HOH B 93 HOH B 333 GLU B 583 ARG B 761
SITE 2 AC5 9 THR B 764 LYS B 767 ASN B 771 ALA B 868
SITE 3 AC5 9 LEU B 872
CRYST1 227.369 227.369 227.369 90.00 90.00 90.00 I 41 3 2 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 0.004398 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004398 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004398 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
