HEADER OXIDOREDUCTASE 15-MAY-09 3HHP
TITLE MALATE DEHYDROGENASE OPEN CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.1.1.37;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 GENE: MDH, B3236, JW3205;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS MALATE DEHYDROGENASE, MDH, CITRIC ACID CYCLE, TCA CYCLE, NAD,
KEYWDS 2 OXIDOREDUCTASE, TRICARBOXYLIC ACID CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZAITSEVA,K.M.MENEELY,A.L.LAMB
REVDAT 2 21-FEB-24 3HHP 1 REMARK
REVDAT 1 22-SEP-09 3HHP 0
JRNL AUTH J.ZAITSEVA,K.M.MENEELY,A.L.LAMB
JRNL TITL STRUCTURE OF ESCHERICHIA COLI MALATE DEHYDROGENASE AT 1.45 A
JRNL TITL 2 RESOLUTION.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 65 866 2009
JRNL REFN ESSN 1744-3091
JRNL PMID 19724119
JRNL DOI 10.1107/S1744309109032217
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 215852
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 21468
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13842
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.3390
REMARK 3 BIN FREE R VALUE SET COUNT : 1512
REMARK 3 BIN FREE R VALUE : 0.3630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8978
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 525
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.65
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): 0.071
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.073
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.253
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9654 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13198 ; 2.065 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1379 ; 5.290 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 363 ;36.441 ;26.336
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1711 ;12.961 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;21.454 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1594 ; 0.144 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7225 ; 0.012 ; 0.021
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): 6391 ; 1.315 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10333 ; 2.077 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3263 ; 3.433 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2811 ; 5.613 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3HHP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000053147.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.25
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 215865
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 60.971
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.05600
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) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.41700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM ADA, 0.2 M SODIUM ACETATE, 30%
REMARK 280 PEG MME 5000, 5% GLYCEROL, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 73.01300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.98600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 73.01300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.98600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 3070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 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 ALA B 80
REMARK 465 ARG B 81
REMARK 465 LYS B 82
REMARK 465 PRO B 83
REMARK 465 GLY B 84
REMARK 465 MET B 85
REMARK 465 ASP B 86
REMARK 465 LYS B 312
REMARK 465 ALA D 80
REMARK 465 ARG D 81
REMARK 465 LYS D 82
REMARK 465 PRO D 83
REMARK 465 GLY D 84
REMARK 465 LYS D 312
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP B 297 O HOH B 378 1.65
REMARK 500 OD1 ASN B 119 O HOH B 525 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 212 CB GLU A 212 CG -0.125
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 MET A 1 CG - SD - CE ANGL. DEV. = 10.7 DEGREES
REMARK 500 ARG A 153 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ASP A 257 CB - CG - OD1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 ARG A 262 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 153 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 233 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP C 34 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP C 150 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG C 233 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG C 262 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LEU C 292 CB - CG - CD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 ASP D 139 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP D 257 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG D 262 NE - CZ - NH2 ANGL. DEV. = -4.2 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 59 -159.25 -130.82
REMARK 500 SER B 59 -158.38 -128.40
REMARK 500 SER B 59 -154.72 -129.53
REMARK 500 SER B 222 -169.19 -120.73
REMARK 500 SER C 59 -162.80 -123.91
REMARK 500 SER D 59 -163.76 -126.26
REMARK 500 SER D 59 -164.22 -126.04
REMARK 500 THR D 224 -55.36 -125.43
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3HHP A 1 312 UNP P61889 MDH_ECOLI 1 312
DBREF 3HHP B 1 312 UNP P61889 MDH_ECOLI 1 312
DBREF 3HHP C 1 312 UNP P61889 MDH_ECOLI 1 312
DBREF 3HHP D 1 312 UNP P61889 MDH_ECOLI 1 312
SEQRES 1 A 312 MET LYS VAL ALA VAL LEU GLY ALA ALA GLY GLY ILE GLY
SEQRES 2 A 312 GLN ALA LEU ALA LEU LEU LEU LYS THR GLN LEU PRO SER
SEQRES 3 A 312 GLY SER GLU LEU SER LEU TYR ASP ILE ALA PRO VAL THR
SEQRES 4 A 312 PRO GLY VAL ALA VAL ASP LEU SER HIS ILE PRO THR ALA
SEQRES 5 A 312 VAL LYS ILE LYS GLY PHE SER GLY GLU ASP ALA THR PRO
SEQRES 6 A 312 ALA LEU GLU GLY ALA ASP VAL VAL LEU ILE SER ALA GLY
SEQRES 7 A 312 VAL ALA ARG LYS PRO GLY MET ASP ARG SER ASP LEU PHE
SEQRES 8 A 312 ASN VAL ASN ALA GLY ILE VAL LYS ASN LEU VAL GLN GLN
SEQRES 9 A 312 VAL ALA LYS THR CYS PRO LYS ALA CYS ILE GLY ILE ILE
SEQRES 10 A 312 THR ASN PRO VAL ASN THR THR VAL ALA ILE ALA ALA GLU
SEQRES 11 A 312 VAL LEU LYS LYS ALA GLY VAL TYR ASP LYS ASN LYS LEU
SEQRES 12 A 312 PHE GLY VAL THR THR LEU ASP ILE ILE ARG SER ASN THR
SEQRES 13 A 312 PHE VAL ALA GLU LEU LYS GLY LYS GLN PRO GLY GLU VAL
SEQRES 14 A 312 GLU VAL PRO VAL ILE GLY GLY HIS SER GLY VAL THR ILE
SEQRES 15 A 312 LEU PRO LEU LEU SER GLN VAL PRO GLY VAL SER PHE THR
SEQRES 16 A 312 GLU GLN GLU VAL ALA ASP LEU THR LYS ARG ILE GLN ASN
SEQRES 17 A 312 ALA GLY THR GLU VAL VAL GLU ALA LYS ALA GLY GLY GLY
SEQRES 18 A 312 SER ALA THR LEU SER MET GLY GLN ALA ALA ALA ARG PHE
SEQRES 19 A 312 GLY LEU SER LEU VAL ARG ALA LEU GLN GLY GLU GLN GLY
SEQRES 20 A 312 VAL VAL GLU CYS ALA TYR VAL GLU GLY ASP GLY GLN TYR
SEQRES 21 A 312 ALA ARG PHE PHE SER GLN PRO LEU LEU LEU GLY LYS ASN
SEQRES 22 A 312 GLY VAL GLU GLU ARG LYS SER ILE GLY THR LEU SER ALA
SEQRES 23 A 312 PHE GLU GLN ASN ALA LEU GLU GLY MET LEU ASP THR LEU
SEQRES 24 A 312 LYS LYS ASP ILE ALA LEU GLY GLU GLU PHE VAL ASN LYS
SEQRES 1 B 312 MET LYS VAL ALA VAL LEU GLY ALA ALA GLY GLY ILE GLY
SEQRES 2 B 312 GLN ALA LEU ALA LEU LEU LEU LYS THR GLN LEU PRO SER
SEQRES 3 B 312 GLY SER GLU LEU SER LEU TYR ASP ILE ALA PRO VAL THR
SEQRES 4 B 312 PRO GLY VAL ALA VAL ASP LEU SER HIS ILE PRO THR ALA
SEQRES 5 B 312 VAL LYS ILE LYS GLY PHE SER GLY GLU ASP ALA THR PRO
SEQRES 6 B 312 ALA LEU GLU GLY ALA ASP VAL VAL LEU ILE SER ALA GLY
SEQRES 7 B 312 VAL ALA ARG LYS PRO GLY MET ASP ARG SER ASP LEU PHE
SEQRES 8 B 312 ASN VAL ASN ALA GLY ILE VAL LYS ASN LEU VAL GLN GLN
SEQRES 9 B 312 VAL ALA LYS THR CYS PRO LYS ALA CYS ILE GLY ILE ILE
SEQRES 10 B 312 THR ASN PRO VAL ASN THR THR VAL ALA ILE ALA ALA GLU
SEQRES 11 B 312 VAL LEU LYS LYS ALA GLY VAL TYR ASP LYS ASN LYS LEU
SEQRES 12 B 312 PHE GLY VAL THR THR LEU ASP ILE ILE ARG SER ASN THR
SEQRES 13 B 312 PHE VAL ALA GLU LEU LYS GLY LYS GLN PRO GLY GLU VAL
SEQRES 14 B 312 GLU VAL PRO VAL ILE GLY GLY HIS SER GLY VAL THR ILE
SEQRES 15 B 312 LEU PRO LEU LEU SER GLN VAL PRO GLY VAL SER PHE THR
SEQRES 16 B 312 GLU GLN GLU VAL ALA ASP LEU THR LYS ARG ILE GLN ASN
SEQRES 17 B 312 ALA GLY THR GLU VAL VAL GLU ALA LYS ALA GLY GLY GLY
SEQRES 18 B 312 SER ALA THR LEU SER MET GLY GLN ALA ALA ALA ARG PHE
SEQRES 19 B 312 GLY LEU SER LEU VAL ARG ALA LEU GLN GLY GLU GLN GLY
SEQRES 20 B 312 VAL VAL GLU CYS ALA TYR VAL GLU GLY ASP GLY GLN TYR
SEQRES 21 B 312 ALA ARG PHE PHE SER GLN PRO LEU LEU LEU GLY LYS ASN
SEQRES 22 B 312 GLY VAL GLU GLU ARG LYS SER ILE GLY THR LEU SER ALA
SEQRES 23 B 312 PHE GLU GLN ASN ALA LEU GLU GLY MET LEU ASP THR LEU
SEQRES 24 B 312 LYS LYS ASP ILE ALA LEU GLY GLU GLU PHE VAL ASN LYS
SEQRES 1 C 312 MET LYS VAL ALA VAL LEU GLY ALA ALA GLY GLY ILE GLY
SEQRES 2 C 312 GLN ALA LEU ALA LEU LEU LEU LYS THR GLN LEU PRO SER
SEQRES 3 C 312 GLY SER GLU LEU SER LEU TYR ASP ILE ALA PRO VAL THR
SEQRES 4 C 312 PRO GLY VAL ALA VAL ASP LEU SER HIS ILE PRO THR ALA
SEQRES 5 C 312 VAL LYS ILE LYS GLY PHE SER GLY GLU ASP ALA THR PRO
SEQRES 6 C 312 ALA LEU GLU GLY ALA ASP VAL VAL LEU ILE SER ALA GLY
SEQRES 7 C 312 VAL ALA ARG LYS PRO GLY MET ASP ARG SER ASP LEU PHE
SEQRES 8 C 312 ASN VAL ASN ALA GLY ILE VAL LYS ASN LEU VAL GLN GLN
SEQRES 9 C 312 VAL ALA LYS THR CYS PRO LYS ALA CYS ILE GLY ILE ILE
SEQRES 10 C 312 THR ASN PRO VAL ASN THR THR VAL ALA ILE ALA ALA GLU
SEQRES 11 C 312 VAL LEU LYS LYS ALA GLY VAL TYR ASP LYS ASN LYS LEU
SEQRES 12 C 312 PHE GLY VAL THR THR LEU ASP ILE ILE ARG SER ASN THR
SEQRES 13 C 312 PHE VAL ALA GLU LEU LYS GLY LYS GLN PRO GLY GLU VAL
SEQRES 14 C 312 GLU VAL PRO VAL ILE GLY GLY HIS SER GLY VAL THR ILE
SEQRES 15 C 312 LEU PRO LEU LEU SER GLN VAL PRO GLY VAL SER PHE THR
SEQRES 16 C 312 GLU GLN GLU VAL ALA ASP LEU THR LYS ARG ILE GLN ASN
SEQRES 17 C 312 ALA GLY THR GLU VAL VAL GLU ALA LYS ALA GLY GLY GLY
SEQRES 18 C 312 SER ALA THR LEU SER MET GLY GLN ALA ALA ALA ARG PHE
SEQRES 19 C 312 GLY LEU SER LEU VAL ARG ALA LEU GLN GLY GLU GLN GLY
SEQRES 20 C 312 VAL VAL GLU CYS ALA TYR VAL GLU GLY ASP GLY GLN TYR
SEQRES 21 C 312 ALA ARG PHE PHE SER GLN PRO LEU LEU LEU GLY LYS ASN
SEQRES 22 C 312 GLY VAL GLU GLU ARG LYS SER ILE GLY THR LEU SER ALA
SEQRES 23 C 312 PHE GLU GLN ASN ALA LEU GLU GLY MET LEU ASP THR LEU
SEQRES 24 C 312 LYS LYS ASP ILE ALA LEU GLY GLU GLU PHE VAL ASN LYS
SEQRES 1 D 312 MET LYS VAL ALA VAL LEU GLY ALA ALA GLY GLY ILE GLY
SEQRES 2 D 312 GLN ALA LEU ALA LEU LEU LEU LYS THR GLN LEU PRO SER
SEQRES 3 D 312 GLY SER GLU LEU SER LEU TYR ASP ILE ALA PRO VAL THR
SEQRES 4 D 312 PRO GLY VAL ALA VAL ASP LEU SER HIS ILE PRO THR ALA
SEQRES 5 D 312 VAL LYS ILE LYS GLY PHE SER GLY GLU ASP ALA THR PRO
SEQRES 6 D 312 ALA LEU GLU GLY ALA ASP VAL VAL LEU ILE SER ALA GLY
SEQRES 7 D 312 VAL ALA ARG LYS PRO GLY MET ASP ARG SER ASP LEU PHE
SEQRES 8 D 312 ASN VAL ASN ALA GLY ILE VAL LYS ASN LEU VAL GLN GLN
SEQRES 9 D 312 VAL ALA LYS THR CYS PRO LYS ALA CYS ILE GLY ILE ILE
SEQRES 10 D 312 THR ASN PRO VAL ASN THR THR VAL ALA ILE ALA ALA GLU
SEQRES 11 D 312 VAL LEU LYS LYS ALA GLY VAL TYR ASP LYS ASN LYS LEU
SEQRES 12 D 312 PHE GLY VAL THR THR LEU ASP ILE ILE ARG SER ASN THR
SEQRES 13 D 312 PHE VAL ALA GLU LEU LYS GLY LYS GLN PRO GLY GLU VAL
SEQRES 14 D 312 GLU VAL PRO VAL ILE GLY GLY HIS SER GLY VAL THR ILE
SEQRES 15 D 312 LEU PRO LEU LEU SER GLN VAL PRO GLY VAL SER PHE THR
SEQRES 16 D 312 GLU GLN GLU VAL ALA ASP LEU THR LYS ARG ILE GLN ASN
SEQRES 17 D 312 ALA GLY THR GLU VAL VAL GLU ALA LYS ALA GLY GLY GLY
SEQRES 18 D 312 SER ALA THR LEU SER MET GLY GLN ALA ALA ALA ARG PHE
SEQRES 19 D 312 GLY LEU SER LEU VAL ARG ALA LEU GLN GLY GLU GLN GLY
SEQRES 20 D 312 VAL VAL GLU CYS ALA TYR VAL GLU GLY ASP GLY GLN TYR
SEQRES 21 D 312 ALA ARG PHE PHE SER GLN PRO LEU LEU LEU GLY LYS ASN
SEQRES 22 D 312 GLY VAL GLU GLU ARG LYS SER ILE GLY THR LEU SER ALA
SEQRES 23 D 312 PHE GLU GLN ASN ALA LEU GLU GLY MET LEU ASP THR LEU
SEQRES 24 D 312 LYS LYS ASP ILE ALA LEU GLY GLU GLU PHE VAL ASN LYS
FORMUL 5 HOH *525(H2 O)
HELIX 1 1 GLY A 10 LEU A 24 1 15
HELIX 2 2 VAL A 38 HIS A 48 1 11
HELIX 3 3 ALA A 63 GLU A 68 1 6
HELIX 4 4 ASP A 86 CYS A 109 1 24
HELIX 5 5 PRO A 120 ALA A 135 1 16
HELIX 6 6 THR A 147 GLY A 163 1 17
HELIX 7 7 GLN A 165 VAL A 169 5 5
HELIX 8 8 SER A 178 VAL A 180 5 3
HELIX 9 9 LEU A 186 VAL A 189 5 4
HELIX 10 10 THR A 195 ASN A 208 1 14
HELIX 11 11 ASN A 208 LYS A 217 1 10
HELIX 12 12 THR A 224 GLN A 243 1 20
HELIX 13 13 SER A 285 ASN A 311 1 27
HELIX 14 14 GLY B 10 LEU B 24 1 15
HELIX 15 15 VAL B 38 HIS B 48 1 11
HELIX 16 16 ALA B 63 GLU B 68 1 6
HELIX 17 17 ARG B 87 CYS B 109 1 23
HELIX 18 18 PRO B 120 ALA B 135 1 16
HELIX 19 19 THR B 147 GLY B 163 1 17
HELIX 20 20 GLN B 165 VAL B 169 5 5
HELIX 21 21 SER B 178 VAL B 180 5 3
HELIX 22 22 LEU B 186 VAL B 189 5 4
HELIX 23 23 THR B 195 LYS B 217 1 23
HELIX 24 24 THR B 224 GLN B 243 1 20
HELIX 25 25 SER B 285 ASN B 311 1 27
HELIX 26 26 GLY C 10 LEU C 24 1 15
HELIX 27 27 VAL C 38 HIS C 48 1 11
HELIX 28 28 ALA C 63 GLU C 68 1 6
HELIX 29 29 ASP C 86 CYS C 109 1 24
HELIX 30 30 PRO C 120 ALA C 135 1 16
HELIX 31 31 THR C 147 GLY C 163 1 17
HELIX 32 32 GLN C 165 VAL C 169 5 5
HELIX 33 33 SER C 178 VAL C 180 5 3
HELIX 34 34 LEU C 186 VAL C 189 5 4
HELIX 35 35 THR C 195 ALA C 218 1 24
HELIX 36 36 THR C 224 GLN C 243 1 20
HELIX 37 37 SER C 285 LYS C 312 1 28
HELIX 38 38 GLY D 10 LEU D 24 1 15
HELIX 39 39 VAL D 38 HIS D 48 1 11
HELIX 40 40 ALA D 63 GLU D 68 1 6
HELIX 41 41 ASP D 86 CYS D 109 1 24
HELIX 42 42 PRO D 120 ALA D 135 1 16
HELIX 43 43 THR D 147 GLY D 163 1 17
HELIX 44 44 GLN D 165 VAL D 169 5 5
HELIX 45 45 SER D 178 VAL D 180 5 3
HELIX 46 46 LEU D 186 VAL D 189 5 4
HELIX 47 47 THR D 195 ASN D 208 1 14
HELIX 48 48 ASN D 208 ALA D 218 1 11
HELIX 49 49 THR D 224 GLN D 243 1 20
HELIX 50 50 SER D 285 ASN D 311 1 27
SHEET 1 A 6 VAL A 53 PHE A 58 0
SHEET 2 A 6 SER A 28 TYR A 33 1 N LEU A 30 O LYS A 54
SHEET 3 A 6 LYS A 2 LEU A 6 1 N VAL A 3 O GLU A 29
SHEET 4 A 6 VAL A 72 ILE A 75 1 O LEU A 74 N ALA A 4
SHEET 5 A 6 CYS A 113 ILE A 116 1 O GLY A 115 N VAL A 73
SHEET 6 A 6 LEU A 143 GLY A 145 1 O PHE A 144 N ILE A 116
SHEET 1 B 2 VAL A 173 GLY A 175 0
SHEET 2 B 2 ILE A 182 PRO A 184 -1 O LEU A 183 N ILE A 174
SHEET 1 C 3 VAL A 249 GLU A 255 0
SHEET 2 C 3 PHE A 263 GLY A 271 -1 O PHE A 264 N VAL A 254
SHEET 3 C 3 GLY A 274 ARG A 278 -1 O GLU A 276 N LEU A 269
SHEET 1 D 6 VAL B 53 PHE B 58 0
SHEET 2 D 6 SER B 28 TYR B 33 1 N LEU B 30 O LYS B 54
SHEET 3 D 6 LYS B 2 LEU B 6 1 N VAL B 5 O SER B 31
SHEET 4 D 6 VAL B 72 ILE B 75 1 O LEU B 74 N ALA B 4
SHEET 5 D 6 CYS B 113 ILE B 116 1 O GLY B 115 N VAL B 73
SHEET 6 D 6 LEU B 143 GLY B 145 1 O PHE B 144 N ILE B 116
SHEET 1 E 2 VAL B 173 GLY B 175 0
SHEET 2 E 2 ILE B 182 PRO B 184 -1 O LEU B 183 N ILE B 174
SHEET 1 F 3 VAL B 249 GLU B 255 0
SHEET 2 F 3 PHE B 263 GLY B 271 -1 O PHE B 264 N VAL B 254
SHEET 3 F 3 GLY B 274 ARG B 278 -1 O GLU B 276 N LEU B 269
SHEET 1 G 6 VAL C 53 PHE C 58 0
SHEET 2 G 6 SER C 28 TYR C 33 1 N LEU C 30 O LYS C 54
SHEET 3 G 6 LYS C 2 LEU C 6 1 N VAL C 3 O SER C 31
SHEET 4 G 6 VAL C 72 ILE C 75 1 O VAL C 72 N ALA C 4
SHEET 5 G 6 CYS C 113 ILE C 116 1 O GLY C 115 N ILE C 75
SHEET 6 G 6 LEU C 143 GLY C 145 1 O PHE C 144 N ILE C 116
SHEET 1 H 2 VAL C 173 GLY C 175 0
SHEET 2 H 2 ILE C 182 PRO C 184 -1 O LEU C 183 N ILE C 174
SHEET 1 I 3 VAL C 249 GLU C 255 0
SHEET 2 I 3 PHE C 263 GLY C 271 -1 O PHE C 264 N VAL C 254
SHEET 3 I 3 GLY C 274 ARG C 278 -1 O GLU C 276 N LEU C 269
SHEET 1 J 6 VAL D 53 PHE D 58 0
SHEET 2 J 6 SER D 28 TYR D 33 1 N LEU D 30 O LYS D 54
SHEET 3 J 6 LYS D 2 LEU D 6 1 N VAL D 5 O SER D 31
SHEET 4 J 6 VAL D 72 ILE D 75 1 O LEU D 74 N ALA D 4
SHEET 5 J 6 CYS D 113 ILE D 116 1 O GLY D 115 N VAL D 73
SHEET 6 J 6 LEU D 143 GLY D 145 1 O PHE D 144 N ILE D 116
SHEET 1 K 2 VAL D 173 GLY D 175 0
SHEET 2 K 2 ILE D 182 PRO D 184 -1 O LEU D 183 N ILE D 174
SHEET 1 L 3 VAL D 249 GLU D 255 0
SHEET 2 L 3 PHE D 263 GLY D 271 -1 O PHE D 264 N VAL D 254
SHEET 3 L 3 GLY D 274 ARG D 278 -1 O GLU D 276 N LEU D 269
CISPEP 1 ASN A 119 PRO A 120 0 3.99
CISPEP 2 ASN B 119 PRO B 120 0 0.71
CISPEP 3 ASN B 119 PRO B 120 0 -0.30
CISPEP 4 ASN C 119 PRO C 120 0 5.52
CISPEP 5 ASN D 119 PRO D 120 0 7.95
CRYST1 146.026 51.972 168.980 90.00 102.23 90.00 C 1 2 1 16
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 0.006848 0.000000 0.001484 0.00000
SCALE2 0.000000 0.019241 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006055 0.00000
(ATOM LINES ARE NOT SHOWN.)
END