HEADER HYDROLASE 19-JUL-06 2HR6
TITLE CRYSTAL STRUCTURE OF DUTPASE IN COMPLEX WITH SUBSTRATE ANALOGUE DUDP
TITLE 2 AND MANGANESE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DUTPASE, DUTP PYROPHOSPHATASE;
COMPND 5 EC: 3.6.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: DUT;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS JELLY ROLL, ENZYME-LIGAND-METAL COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.BARABAS,J.KOVARI,R.TAPAI,B.G.VERTESSY
REVDAT 5 30-AUG-23 2HR6 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 2HR6 1 VERSN
REVDAT 3 24-FEB-09 2HR6 1 VERSN
REVDAT 2 11-MAR-08 2HR6 1 JRNL
REVDAT 1 31-JUL-07 2HR6 0
JRNL AUTH J.KOVARI,O.BARABAS,B.VARGA,A.BEKESI,F.TOLGYESI,J.FIDY,
JRNL AUTH 2 J.NAGY,B.G.VERTESSY
JRNL TITL METHYLENE SUBSTITUTION AT THE ALPHA-BETA BRIDGING POSITION
JRNL TITL 2 WITHIN THE PHOSPHATE CHAIN OF DUDP PROFOUNDLY PERTURBS
JRNL TITL 3 LIGAND ACCOMMODATION INTO THE DUTPASE ACTIVE SITE.
JRNL REF PROTEINS V. 71 308 2008
JRNL REFN ISSN 0887-3585
JRNL PMID 17932923
JRNL DOI 10.1002/PROT.21757
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH O.BARABAS,V.PONGRACZ,J.KOVARI,M.WILMANNS,B.G.VERTESSY
REMARK 1 TITL STRUCTURAL INSIGHTS INTO THE CATALYTIC MECHANISM OF
REMARK 1 TITL 2 PHOSPHATE ESTER HYDROLYSIS BY DUTPASE.
REMARK 1 REF J.BIOL.CHEM. V. 279 42907 2004
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 15208312
REMARK 1 DOI 10.1074/JBC.M406135200
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.GONZALEZ,G.LARSSON,R.PERSSON,E.CEDERGREN-ZEPPEZAUER
REMARK 1 TITL ATOMIC RESOLUTION STRUCTURE OF ESCHERICHIA COLI DUTPASE
REMARK 1 TITL 2 DETERMINED AB INITIO
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 57 767 2001
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 11375495
REMARK 1 DOI 10.1107/S0907444901004255
REMARK 2
REMARK 2 RESOLUTION. 1.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 13953
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) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 749
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) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 832
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.1890
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1013
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 22.35
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.09000
REMARK 3 B22 (A**2) : -0.09000
REMARK 3 B33 (A**2) : 0.13000
REMARK 3 B12 (A**2) : -0.04000
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): 0.103
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.480
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1073 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1005 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1465 ; 1.702 ; 2.010
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2326 ; 0.821 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 140 ; 5.818 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 39 ;35.320 ;24.615
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 168 ;12.121 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;16.193 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 171 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1180 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 196 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 122 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 888 ; 0.191 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 490 ; 0.164 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 626 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 88 ; 0.203 ; 0.200
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): 9 ; 0.171 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 84 ; 0.251 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.284 ; 0.200
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): 714 ; 2.230 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 282 ; 0.093 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1107 ; 3.606 ;10.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 410 ; 6.010 ;20.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 356 ; 7.993 ;50.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 137
REMARK 3 RESIDUE RANGE : A 777 A 777
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1866 31.3803 4.8255
REMARK 3 T TENSOR
REMARK 3 T11: -0.0609 T22: -0.0529
REMARK 3 T33: -0.0563 T12: -0.0048
REMARK 3 T13: 0.0184 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 0.2476 L22: 0.8080
REMARK 3 L33: 0.1993 L12: -0.0981
REMARK 3 L13: -0.0217 L23: -0.0553
REMARK 3 S TENSOR
REMARK 3 S11: -0.0404 S12: 0.0061 S13: -0.0466
REMARK 3 S21: -0.0298 S22: -0.0114 S23: -0.0463
REMARK 3 S31: 0.0264 S32: 0.0100 S33: 0.0518
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2HR6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000038665.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
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) : 0.8110
REMARK 200 MONOCHROMATOR : TRIANGULAR MONOCHROMATOR
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14703
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 24.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 12.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.55800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: 1EUW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M SODIUM ACETATE,
REMARK 280 0.1M TRIS, PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 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 49.96800
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 49.96800
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 49.96800
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 49.96800
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 49.96800
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 49.96800
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TRIMER GENERATED FROM THE
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS: 1-Y,1+X-Y,Z AND -
REMARK 300 X+Y,1-X,Z
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 12690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 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 -0.500000 -0.866025 0.000000 37.52450
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 64.99434
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -37.52450
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 64.99434
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 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 A1089 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 ALA A 138
REMARK 465 THR A 139
REMARK 465 ASP A 140
REMARK 465 ARG A 141
REMARK 465 GLY A 142
REMARK 465 GLU A 143
REMARK 465 GLY A 144
REMARK 465 GLY A 145
REMARK 465 PHE A 146
REMARK 465 GLY A 147
REMARK 465 HIS A 148
REMARK 465 SER A 149
REMARK 465 GLY A 150
REMARK 465 ARG A 151
REMARK 465 GLN A 152
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MET A 2 CG SD CE
REMARK 470 LYS A 4 NZ
REMARK 470 LYS A 8 CE NZ
REMARK 470 ILE A 9 CD1
REMARK 470 LYS A 16 NZ
REMARK 470 LEU A 20 CD2
REMARK 470 LYS A 77 CE NZ
REMARK 470 GLN A 106 CD OE1 NE2
REMARK 470 ILE A 117 CD1
REMARK 470 LEU A 132 CD1 CD2
REMARK 470 GLU A 134 OE1 OE2
REMARK 470 ASP A 137 CG OD1 OD2
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 O HOH A 1058 O HOH A 1072 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1093 O HOH A 1136 2665 2.05
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 LYS A 16 -98.44 -127.84
REMARK 500 ALA A 60 -36.72 73.99
REMARK 500 LEU A 85 -55.73 70.32
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 997 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DUD A 777 O1B
REMARK 620 2 DUD A 777 O1A 92.8
REMARK 620 3 HOH A1021 O 86.3 87.3
REMARK 620 4 HOH A1025 O 172.9 82.3 88.4
REMARK 620 5 HOH A1044 O 96.6 91.6 177.0 88.7
REMARK 620 6 HOH A1133 O 89.0 173.4 86.5 95.3 94.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DUD A 777
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 301
DBREF 2HR6 A 2 152 UNP P06968 DUT_ECOLI 1 151
SEQADV 2HR6 MET A 1 UNP P06968 CLONING ARTIFACT
SEQRES 1 A 152 MET MET LYS LYS ILE ASP VAL LYS ILE LEU ASP PRO ARG
SEQRES 2 A 152 VAL GLY LYS GLU PHE PRO LEU PRO THR TYR ALA THR SER
SEQRES 3 A 152 GLY SER ALA GLY LEU ASP LEU ARG ALA CYS LEU ASN ASP
SEQRES 4 A 152 ALA VAL GLU LEU ALA PRO GLY ASP THR THR LEU VAL PRO
SEQRES 5 A 152 THR GLY LEU ALA ILE HIS ILE ALA ASP PRO SER LEU ALA
SEQRES 6 A 152 ALA MET MET LEU PRO ARG SER GLY LEU GLY HIS LYS HIS
SEQRES 7 A 152 GLY ILE VAL LEU GLY ASN LEU VAL GLY LEU ILE ASP SER
SEQRES 8 A 152 ASP TYR GLN GLY GLN LEU MET ILE SER VAL TRP ASN ARG
SEQRES 9 A 152 GLY GLN ASP SER PHE THR ILE GLN PRO GLY GLU ARG ILE
SEQRES 10 A 152 ALA GLN MET ILE PHE VAL PRO VAL VAL GLN ALA GLU PHE
SEQRES 11 A 152 ASN LEU VAL GLU ASP PHE ASP ALA THR ASP ARG GLY GLU
SEQRES 12 A 152 GLY GLY PHE GLY HIS SER GLY ARG GLN
HET MN A 997 1
HET DUD A 777 24
HET EDO A 301 4
HETNAM MN MANGANESE (II) ION
HETNAM DUD DEOXYURIDINE-5'-DIPHOSPHATE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 MN MN 2+
FORMUL 3 DUD C9 H14 N2 O11 P2
FORMUL 4 EDO C2 H6 O2
FORMUL 5 HOH *156(H2 O)
HELIX 1 1 ARG A 71 GLY A 79 1 9
SHEET 1 A 4 ASP A 6 ILE A 9 0
SHEET 2 A 4 THR A 48 HIS A 58 -1 O ALA A 56 N LYS A 8
SHEET 3 A 4 GLN A 96 ASN A 103 -1 O ILE A 99 N VAL A 51
SHEET 4 A 4 ILE A 80 LEU A 82 -1 N VAL A 81 O TRP A 102
SHEET 1 B 4 LEU A 31 ARG A 34 0
SHEET 2 B 4 ARG A 116 PRO A 124 -1 O ALA A 118 N LEU A 33
SHEET 3 B 4 LEU A 64 LEU A 69 -1 N LEU A 69 O GLN A 119
SHEET 4 B 4 GLY A 87 ILE A 89 -1 O ILE A 89 N ALA A 66
SHEET 1 C 2 VAL A 41 LEU A 43 0
SHEET 2 C 2 PHE A 109 ILE A 111 -1 O ILE A 111 N VAL A 41
LINK O1B DUD A 777 MN MN A 997 1555 1555 2.06
LINK O1A DUD A 777 MN MN A 997 1555 1555 2.21
LINK MN MN A 997 O HOH A1021 1555 1555 2.27
LINK MN MN A 997 O HOH A1025 1555 1555 2.17
LINK MN MN A 997 O HOH A1044 1555 1555 2.20
LINK MN MN A 997 O HOH A1133 1555 1555 2.18
SITE 1 AC1 5 DUD A 777 HOH A1021 HOH A1025 HOH A1044
SITE 2 AC1 5 HOH A1133
SITE 1 AC2 22 MET A 68 ARG A 71 SER A 72 GLY A 73
SITE 2 AC2 22 ASN A 84 GLY A 87 LEU A 88 ASP A 90
SITE 3 AC2 22 TYR A 93 MET A 98 GLN A 119 MN A 997
SITE 4 AC2 22 HOH A 998 HOH A 999 HOH A1002 HOH A1005
SITE 5 AC2 22 HOH A1021 HOH A1025 HOH A1104 HOH A1115
SITE 6 AC2 22 HOH A1133 HOH A1150
SITE 1 AC3 2 LYS A 3 LYS A 4
CRYST1 75.049 75.049 99.936 90.00 90.00 120.00 P 63 2 2 12
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 0.013325 0.007693 0.000000 0.00000
SCALE2 0.000000 0.015386 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010006 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
