HEADER LYASE/LYASE INHIBITOR 20-SEP-13 4MU3
TITLE THE FORM A STRUCTURE OF AN E21Q CATALYTIC MUTANT OF A. THALIANA IGPD2
TITLE 2 IN COMPLEX WITH MN2+ AND A MIXTURE OF ITS SUBSTRATE, 2R3S-IGP, AND AN
TITLE 3 INHIBITOR, 2S3S-IGP, TO 1.12 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE 2, CHLOROPLASTIC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SHORT CONSTRUCT (UNP RESIDUES 69-272);
COMPND 5 SYNONYM: IGPD 2, PROTEIN HISTIDINE BIOSYNTHESIS 5B;
COMPND 6 EC: 4.2.1.19;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: AT4G14910, DL3495C, HISN5B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS HYDRO-LYASE, HISTIDINE BIOSYNTHESIS, MANGANESE BINDING,
KEYWDS 2 CHLOROPLASTIC, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.BISSON,K.L.BRITTON,S.E.SEDELNIKOVA,P.J.BAKER,D.W.RICE
REVDAT 4 20-SEP-23 4MU3 1 SEQADV LINK
REVDAT 3 15-NOV-17 4MU3 1 REMARK
REVDAT 2 22-JUL-15 4MU3 1 JRNL
REVDAT 1 24-SEP-14 4MU3 0
JRNL AUTH C.BISSON,K.L.BRITTON,S.E.SEDELNIKOVA,H.F.RODGERS,
JRNL AUTH 2 T.C.EADSFORTH,R.C.VINER,T.R.HAWKES,P.J.BAKER,D.W.RICE
JRNL TITL CRYSTAL STRUCTURES REVEAL THAT THE REACTION MECHANISM OF
JRNL TITL 2 IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE IS CONTROLLED BY
JRNL TITL 3 SWITCHING MN(II) COORDINATION.
JRNL REF STRUCTURE V. 23 1236 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 26095028
JRNL DOI 10.1016/J.STR.2015.05.012
REMARK 2
REMARK 2 RESOLUTION. 1.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 1.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 89279
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) : 0.126
REMARK 3 R VALUE (WORKING SET) : 0.125
REMARK 3 FREE R VALUE : 0.139
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4612
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) : 1.12
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6155
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 316
REMARK 3 BIN FREE R VALUE : 0.2300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1443
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 205
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.02
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): 0.022
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.022
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.012
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.568
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.979
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.971
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1577 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1516 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2141 ; 1.715 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3489 ; 0.876 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 205 ; 6.576 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 75 ;32.133 ;23.467
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 266 ;10.447 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;12.548 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 246 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1785 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 377 ; 0.002 ; 0.020
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): 763 ; 2.318 ; 0.932
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 762 ; 2.321 ; 0.926
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 957 ; 1.725 ; 1.402
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 958 ; 1.736 ; 1.402
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 814 ;10.287 ; 1.344
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 814 ;10.247 ; 1.345
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1175 ; 8.807 ; 1.828
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1827 ; 6.338 ; 9.108
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1828 ; 6.336 ; 9.119
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3092 ;18.340 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 45 ;38.849 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3224 ;34.042 ; 5.000
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 : 1.20
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 4MU3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000082366.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-FEB-11
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 : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : KIRKPATRICK BAEZ BIMORPH MIRROR
REMARK 200 PAIR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS (XIA2)
REMARK 200 DATA SCALING SOFTWARE : XSCALE (XIA2), SCALA (XIA2)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94992
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.120
REMARK 200 RESOLUTION RANGE LOW (A) : 46.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.56800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2F1D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% ETHYLENE GLYCOL, PH 8.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 3 2
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 Y,X,-Z
REMARK 290 14555 -Y,-X,-Z
REMARK 290 15555 Y,-X,Z
REMARK 290 16555 -Y,X,Z
REMARK 290 17555 X,Z,-Y
REMARK 290 18555 -X,Z,Y
REMARK 290 19555 -X,-Z,-Y
REMARK 290 20555 X,-Z,Y
REMARK 290 21555 Z,Y,-X
REMARK 290 22555 Z,-Y,X
REMARK 290 23555 -Z,Y,X
REMARK 290 24555 -Z,-Y,-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 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 0.00000
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: 24-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 24-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 105680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 137230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 30.0 KCAL/MOL
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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 6 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 8 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 9 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 9 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 9 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 10 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 11 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 12 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 13 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 13 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 13 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 14 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 14 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 14 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 15 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 15 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 15 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 16 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 16 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 16 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 17 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 17 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 17 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 18 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 18 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 18 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 19 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 19 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 19 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 20 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 20 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 20 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 21 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 21 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 21 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 22 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 22 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 22 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 23 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 23 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 23 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 24 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 24 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 24 -1.000000 0.000000 0.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 496 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 559 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 560 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 564 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 584 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 597 LIES ON A SPECIAL POSITION.
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 3
REMARK 465 ALA A 4
REMARK 465 SER A 5
REMARK 465 PRO A 6
REMARK 465 ILE A 7
REMARK 465 GLU A 8
REMARK 465 GLY A 195
REMARK 465 THR A 196
REMARK 465 ILE A 197
REMARK 465 PRO A 198
REMARK 465 SER A 199
REMARK 465 SER A 200
REMARK 465 LYS A 201
REMARK 465 GLY A 202
REMARK 465 VAL A 203
REMARK 465 LEU A 204
REMARK 465 SER A 205
REMARK 465 ARG A 206
REMARK 465 SER A 207
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 ARG A 134 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 161 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 161 NE - CZ - NH2 ANGL. DEV. = -3.7 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 ASP A 31 41.38 -107.42
REMARK 500 ASP A 71 -179.37 179.29
REMARK 500 ARG A 99 -45.49 81.69
REMARK 500 ASP A 108 -121.98 55.47
REMARK 500 LYS A 166 -41.16 -133.97
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 MN A 302 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 47 NE2
REMARK 620 2 HIS A 74 NE2 49.9
REMARK 620 3 HIS A 169 NE2 102.8 55.3
REMARK 620 4 GLU A 173 OE1 87.7 74.6 89.6
REMARK 620 5 IG2 A 303 N1 53.7 6.4 54.0 68.9
REMARK 620 6 IG2 A 303 O1 51.0 3.2 55.5 71.5 3.4
REMARK 620 7 IYP A 304 N2 53.2 6.5 54.6 68.5 0.7 3.4
REMARK 620 8 IYP A 304 O3 51.0 2.8 55.3 71.9 3.7 0.5 3.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 301 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 73 NE2
REMARK 620 2 GLU A 77 OE1 92.5
REMARK 620 3 HIS A 145 NE2 87.4 81.5
REMARK 620 4 HIS A 170 NE2 48.8 82.7 38.7
REMARK 620 5 IG2 A 303 N3 90.2 94.1 174.9 138.4
REMARK 620 6 HOH A 432 O 175.5 84.7 95.7 134.0 86.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 301 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 73 NE2
REMARK 620 2 GLU A 77 OE1 89.9
REMARK 620 3 HIS A 145 NE2 100.5 90.0
REMARK 620 4 HIS A 170 NE2 60.5 92.2 40.1
REMARK 620 5 HOH A 432 O 150.7 79.3 106.6 146.1
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MU0 RELATED DB: PDB
REMARK 900 RELATED ID: 4MU1 RELATED DB: PDB
REMARK 900 RELATED ID: 4MU2 RELATED DB: PDB
REMARK 900 RELATED ID: 4MU4 RELATED DB: PDB
DBREF 4MU3 A 4 207 UNP O23346 HIS5B_ARATH 69 272
SEQADV 4MU3 MET A 3 UNP O23346 INITIATING METHIONINE
SEQADV 4MU3 GLN A 21 UNP O23346 GLU 86 ENGINEERED MUTATION
SEQRES 1 A 205 MET ALA SER PRO ILE GLU SER ALA ARG ILE GLY GLU VAL
SEQRES 2 A 205 LYS ARG GLU THR LYS GLN THR ASN VAL SER VAL LYS ILE
SEQRES 3 A 205 ASN LEU ASP GLY HIS GLY VAL SER ASP SER SER THR GLY
SEQRES 4 A 205 ILE PRO PHE LEU ASP HIS MET LEU ASP GLN LEU ALA SER
SEQRES 5 A 205 HIS GLY LEU PHE ASP VAL HIS VAL ARG ALA THR GLY ASP
SEQRES 6 A 205 THR HIS ILE ASP ASP HIS HIS THR ASN GLU ASP VAL ALA
SEQRES 7 A 205 LEU ALA ILE GLY THR ALA LEU LEU LYS ALA LEU GLY GLU
SEQRES 8 A 205 ARG LYS GLY ILE ASN ARG PHE GLY ASP PHE THR ALA PRO
SEQRES 9 A 205 LEU ASP GLU ALA LEU ILE HIS VAL SER LEU ASP LEU SER
SEQRES 10 A 205 GLY ARG PRO TYR LEU GLY TYR ASN LEU GLU ILE PRO THR
SEQRES 11 A 205 GLN ARG VAL GLY THR TYR ASP THR GLN LEU VAL GLU HIS
SEQRES 12 A 205 PHE PHE GLN SER LEU VAL ASN THR SER GLY MET THR LEU
SEQRES 13 A 205 HIS ILE ARG GLN LEU ALA GLY LYS ASN SER HIS HIS ILE
SEQRES 14 A 205 ILE GLU ALA THR PHE LYS ALA PHE ALA ARG ALA LEU ARG
SEQRES 15 A 205 GLN ALA THR GLU SER ASP PRO ARG ARG GLY GLY THR ILE
SEQRES 16 A 205 PRO SER SER LYS GLY VAL LEU SER ARG SER
HET MN A 301 2
HET MN A 302 1
HET IG2 A 303 15
HET IYP A 304 15
HET EDO A 305 4
HET EDO A 306 4
HET EDO A 307 4
HET EDO A 308 4
HET EDO A 309 4
HETNAM MN MANGANESE (II) ION
HETNAM IG2 (2S,3S)-2,3-DIHYDROXY-3-(1H-IMIDAZOL-5-YL)PROPYL
HETNAM 2 IG2 DIHYDROGEN PHOSPHATE
HETNAM IYP (2R,3S)-2,3-DIHYDROXY-3-(1H-IMIDAZOL-5-YL)PROPYL
HETNAM 2 IYP DIHYDROGEN PHOSPHATE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 MN 2(MN 2+)
FORMUL 4 IG2 C6 H11 N2 O6 P
FORMUL 5 IYP C6 H11 N2 O6 P
FORMUL 6 EDO 5(C2 H6 O2)
FORMUL 11 HOH *205(H2 O)
HELIX 1 1 ILE A 42 LEU A 57 1 16
HELIX 2 2 ASP A 72 GLY A 92 1 21
HELIX 3 3 GLN A 141 GLY A 155 1 15
HELIX 4 4 ASN A 167 GLU A 188 1 22
SHEET 1 A 4 ILE A 12 GLU A 18 0
SHEET 2 A 4 THR A 22 ASN A 29 -1 O VAL A 26 N VAL A 15
SHEET 3 A 4 ASP A 59 GLY A 66 -1 O ARG A 63 N SER A 25
SHEET 4 A 4 SER A 36 SER A 39 1 N SER A 39 O VAL A 62
SHEET 1 B 4 PHE A 100 LEU A 107 0
SHEET 2 B 4 ALA A 110 ASP A 117 -1 O VAL A 114 N PHE A 103
SHEET 3 B 4 THR A 157 ALA A 164 -1 O HIS A 159 N SER A 115
SHEET 4 B 4 TYR A 123 TYR A 126 1 N TYR A 123 O LEU A 158
SHEET 1 C 2 ARG A 134 VAL A 135 0
SHEET 2 C 2 TYR A 138 ASP A 139 -1 O TYR A 138 N VAL A 135
LINK NE2 HIS A 47 MN MN A 302 1555 21555 2.26
LINK NE2 HIS A 73 MN A MN A 301 1555 1555 2.19
LINK NE2 HIS A 73 MN B MN A 301 1555 1555 2.19
LINK NE2 HIS A 74 MN MN A 302 1555 1555 2.26
LINK OE1 GLU A 77 MN A MN A 301 1555 1555 2.23
LINK OE1 GLU A 77 MN B MN A 301 1555 1555 2.33
LINK NE2 HIS A 145 MN B MN A 301 1555 1555 1.99
LINK NE2 HIS A 145 MN A MN A 301 1555 1555 2.45
LINK NE2 HIS A 169 MN MN A 302 1555 21555 2.26
LINK NE2 HIS A 170 MN A MN A 301 1555 21555 2.28
LINK NE2 HIS A 170 MN B MN A 301 1555 21555 2.16
LINK OE1 GLU A 173 MN MN A 302 1555 21555 2.15
LINK MN A MN A 301 N3 AIG2 A 303 1555 1555 2.29
LINK MN A MN A 301 O HOH A 432 1555 1555 2.06
LINK MN B MN A 301 O HOH A 432 1555 1555 2.20
LINK MN MN A 302 N1 AIG2 A 303 1555 1555 2.16
LINK MN MN A 302 O1 AIG2 A 303 1555 1555 2.46
LINK MN MN A 302 N2 BIYP A 304 1555 1555 2.35
LINK MN MN A 302 O3 BIYP A 304 1555 1555 2.42
CRYST1 113.100 113.100 113.100 90.00 90.00 90.00 P 4 3 2 24
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 0.008842 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008842 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008842 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
