HEADER HYDROLASE 31-JAN-17 5MZG
TITLE CRYSTAL STRUCTURE OF MOUSE MTH1 IN COMPLEX WITH TH588
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 7,8-DIHYDRO-8-OXOGUANINE TRIPHOSPHATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 2-HYDROXY-DATP DIPHOSPHATASE,8-OXO-DGTPASE,NUCLEOSIDE
COMPND 5 DIPHOSPHATE-LINKED MOIETY X MOTIF 1,NUDIX MOTIF 1;
COMPND 6 EC: 3.6.1.55,3.6.1.56;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: NUDT1, MTH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INHIBITOR, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.NARWAL,A.-S.JEMTH,T.HELLEDAY,P.STENMARK
REVDAT 4 17-JAN-24 5MZG 1 REMARK
REVDAT 3 14-FEB-18 5MZG 1 JRNL
REVDAT 2 24-JAN-18 5MZG 1 JRNL
REVDAT 1 10-JAN-18 5MZG 0
JRNL AUTH M.NARWAL,A.S.JEMTH,R.GUSTAFSSON,I.ALMLOF,U.WARPMAN BERGLUND,
JRNL AUTH 2 T.HELLEDAY,P.STENMARK
JRNL TITL CRYSTAL STRUCTURES AND INHIBITOR INTERACTIONS OF MOUSE AND
JRNL TITL 2 DOG MTH1 REVEAL SPECIES-SPECIFIC DIFFERENCES IN AFFINITY.
JRNL REF BIOCHEMISTRY V. 57 593 2018
JRNL REFN ISSN 1520-4995
JRNL PMID 29281266
JRNL DOI 10.1021/ACS.BIOCHEM.7B01163
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 27865
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1492
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2030
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 110
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2498
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.34000
REMARK 3 B22 (A**2) : -0.10000
REMARK 3 B33 (A**2) : -2.24000
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): 0.136
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.129
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.093
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.153
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2644 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2429 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3572 ; 1.503 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5606 ; 0.741 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 310 ; 6.999 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 129 ;30.785 ;24.031
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 447 ;13.422 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;18.326 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 367 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2959 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 641 ; 0.001 ; 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): 1241 ; 2.096 ; 2.686
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1236 ; 2.012 ; 2.678
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1545 ; 2.996 ; 4.002
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1546 ; 2.996 ; 4.003
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1403 ; 3.146 ; 3.080
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1387 ; 3.032 ; 3.056
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1999 ; 4.846 ; 4.445
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2887 ; 6.798 ;21.558
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2845 ; 6.757 ;21.332
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 : NULL
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 5MZG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1200003290.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96770
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29434
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 61.570
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.61700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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: 3ZR1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM THIOCYANATE AND 20%
REMARK 280 PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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
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 20.00300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.56650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.85400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.56650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.00300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.85400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 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 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 SER A 155
REMARK 465 PHE A 156
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 ASP B 154
REMARK 465 SER B 155
REMARK 465 PHE B 156
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 151 NE - CZ - NH1 ANGL. DEV. = 3.1 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 89 -75.19 -124.30
REMARK 500 ASP A 141 -168.47 -160.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2GE A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2GE B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN B 205
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5MZG RELATED DB: PDB
DBREF 5MZG A 1 156 UNP P53368 8ODP_MOUSE 1 156
DBREF 5MZG B 1 156 UNP P53368 8ODP_MOUSE 1 156
SEQADV 5MZG MET A -19 UNP P53368 INITIATING METHIONINE
SEQADV 5MZG GLY A -18 UNP P53368 EXPRESSION TAG
SEQADV 5MZG SER A -17 UNP P53368 EXPRESSION TAG
SEQADV 5MZG SER A -16 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS A -15 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS A -14 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS A -13 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS A -12 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS A -11 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS A -10 UNP P53368 EXPRESSION TAG
SEQADV 5MZG SER A -9 UNP P53368 EXPRESSION TAG
SEQADV 5MZG SER A -8 UNP P53368 EXPRESSION TAG
SEQADV 5MZG GLY A -7 UNP P53368 EXPRESSION TAG
SEQADV 5MZG LEU A -6 UNP P53368 EXPRESSION TAG
SEQADV 5MZG VAL A -5 UNP P53368 EXPRESSION TAG
SEQADV 5MZG PRO A -4 UNP P53368 EXPRESSION TAG
SEQADV 5MZG ARG A -3 UNP P53368 EXPRESSION TAG
SEQADV 5MZG GLY A -2 UNP P53368 EXPRESSION TAG
SEQADV 5MZG SER A -1 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS A 0 UNP P53368 EXPRESSION TAG
SEQADV 5MZG MET B -19 UNP P53368 INITIATING METHIONINE
SEQADV 5MZG GLY B -18 UNP P53368 EXPRESSION TAG
SEQADV 5MZG SER B -17 UNP P53368 EXPRESSION TAG
SEQADV 5MZG SER B -16 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS B -15 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS B -14 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS B -13 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS B -12 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS B -11 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS B -10 UNP P53368 EXPRESSION TAG
SEQADV 5MZG SER B -9 UNP P53368 EXPRESSION TAG
SEQADV 5MZG SER B -8 UNP P53368 EXPRESSION TAG
SEQADV 5MZG GLY B -7 UNP P53368 EXPRESSION TAG
SEQADV 5MZG LEU B -6 UNP P53368 EXPRESSION TAG
SEQADV 5MZG VAL B -5 UNP P53368 EXPRESSION TAG
SEQADV 5MZG PRO B -4 UNP P53368 EXPRESSION TAG
SEQADV 5MZG ARG B -3 UNP P53368 EXPRESSION TAG
SEQADV 5MZG GLY B -2 UNP P53368 EXPRESSION TAG
SEQADV 5MZG SER B -1 UNP P53368 EXPRESSION TAG
SEQADV 5MZG HIS B 0 UNP P53368 EXPRESSION TAG
SEQRES 1 A 176 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 176 LEU VAL PRO ARG GLY SER HIS MET SER THR SER ARG LEU
SEQRES 3 A 176 TYR THR LEU VAL LEU VAL LEU GLN PRO GLN ARG VAL LEU
SEQRES 4 A 176 LEU GLY MET LYS LYS ARG GLY PHE GLY ALA GLY ARG TRP
SEQRES 5 A 176 ASN GLY PHE GLY GLY LYS VAL GLN GLU GLY GLU THR ILE
SEQRES 6 A 176 GLU ASP GLY ALA LYS ARG GLU LEU LEU GLU GLU SER GLY
SEQRES 7 A 176 LEU SER VAL ASP THR LEU HIS LYS VAL GLY HIS ILE SER
SEQRES 8 A 176 PHE GLU PHE VAL GLY SER PRO GLU LEU MET ASP VAL HIS
SEQRES 9 A 176 ILE PHE SER ALA ASP HIS VAL HIS GLY THR PRO THR GLU
SEQRES 10 A 176 SER GLU GLU MET ARG PRO GLN TRP PHE GLN LEU ASP GLN
SEQRES 11 A 176 ILE PRO PHE ALA ASP LEU TRP PRO ASP ASP SER TYR TRP
SEQRES 12 A 176 PHE PRO LEU LEU LEU GLN LYS LYS LYS PHE CYS GLY HIS
SEQRES 13 A 176 PHE LYS PHE GLN ASP GLN ASP THR ILE LEU SER TYR SER
SEQRES 14 A 176 LEU ARG GLU VAL ASP SER PHE
SEQRES 1 B 176 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 176 LEU VAL PRO ARG GLY SER HIS MET SER THR SER ARG LEU
SEQRES 3 B 176 TYR THR LEU VAL LEU VAL LEU GLN PRO GLN ARG VAL LEU
SEQRES 4 B 176 LEU GLY MET LYS LYS ARG GLY PHE GLY ALA GLY ARG TRP
SEQRES 5 B 176 ASN GLY PHE GLY GLY LYS VAL GLN GLU GLY GLU THR ILE
SEQRES 6 B 176 GLU ASP GLY ALA LYS ARG GLU LEU LEU GLU GLU SER GLY
SEQRES 7 B 176 LEU SER VAL ASP THR LEU HIS LYS VAL GLY HIS ILE SER
SEQRES 8 B 176 PHE GLU PHE VAL GLY SER PRO GLU LEU MET ASP VAL HIS
SEQRES 9 B 176 ILE PHE SER ALA ASP HIS VAL HIS GLY THR PRO THR GLU
SEQRES 10 B 176 SER GLU GLU MET ARG PRO GLN TRP PHE GLN LEU ASP GLN
SEQRES 11 B 176 ILE PRO PHE ALA ASP LEU TRP PRO ASP ASP SER TYR TRP
SEQRES 12 B 176 PHE PRO LEU LEU LEU GLN LYS LYS LYS PHE CYS GLY HIS
SEQRES 13 B 176 PHE LYS PHE GLN ASP GLN ASP THR ILE LEU SER TYR SER
SEQRES 14 B 176 LEU ARG GLU VAL ASP SER PHE
HET 2GE A 201 19
HET SO4 A 202 5
HET SCN A 203 3
HET SCN A 204 3
HET 2GE B 201 19
HET SO4 B 202 5
HET SO4 B 203 5
HET SCN B 204 3
HET SCN B 205 3
HETNAM 2GE N~4~-CYCLOPROPYL-6-(2,3-DICHLOROPHENYL)PYRIMIDINE-2,4-
HETNAM 2 2GE DIAMINE
HETNAM SO4 SULFATE ION
HETNAM SCN THIOCYANATE ION
FORMUL 3 2GE 2(C13 H12 CL2 N4)
FORMUL 4 SO4 3(O4 S 2-)
FORMUL 5 SCN 4(C N S 1-)
FORMUL 12 HOH *156(H2 O)
HELIX 1 AA1 THR A 44 GLY A 58 1 15
HELIX 2 AA2 PRO A 112 LEU A 116 5 5
HELIX 3 AA3 TRP A 117 PRO A 118 5 2
HELIX 4 AA4 ASP A 119 GLN A 129 1 11
HELIX 5 AA5 THR B 44 GLY B 58 1 15
HELIX 6 AA6 PRO B 112 LEU B 116 5 5
HELIX 7 AA7 TRP B 117 PRO B 118 5 2
HELIX 8 AA8 ASP B 119 GLN B 129 1 11
SHEET 1 AA1 4 TRP A 32 ASN A 33 0
SHEET 2 AA1 4 ARG A 17 LYS A 23 -1 N GLY A 21 O ASN A 33
SHEET 3 AA1 4 SER A 4 LEU A 13 -1 N VAL A 12 O LEU A 19
SHEET 4 AA1 4 MET A 101 GLN A 107 0
SHEET 1 AA2 8 PHE A 35 LYS A 38 0
SHEET 2 AA2 8 SER A 4 LEU A 13 -1 N VAL A 10 O PHE A 35
SHEET 3 AA2 8 ARG A 17 LYS A 23 -1 O LEU A 19 N VAL A 12
SHEET 4 AA2 8 LEU A 80 ALA A 88 0
SHEET 5 AA2 8 HIS A 65 PHE A 74 -1 N ILE A 70 O VAL A 83
SHEET 6 AA2 8 LYS A 132 ASP A 141 1 O PHE A 139 N GLU A 73
SHEET 7 AA2 8 THR A 144 VAL A 153 -1 O SER A 147 N LYS A 138
SHEET 8 AA2 8 SER B 2 THR B 3 1 O SER B 2 N LEU A 146
SHEET 1 AA3 3 TRP B 32 ASN B 33 0
SHEET 2 AA3 3 ARG B 17 LYS B 23 -1 N GLY B 21 O ASN B 33
SHEET 3 AA3 3 MET B 101 GLN B 107 -1 O GLN B 104 N LEU B 20
SHEET 1 AA4 7 TRP B 32 ASN B 33 0
SHEET 2 AA4 7 ARG B 17 LYS B 23 -1 N GLY B 21 O ASN B 33
SHEET 3 AA4 7 ARG B 5 LEU B 13 -1 N VAL B 12 O LEU B 19
SHEET 4 AA4 7 MET B 81 ALA B 88 1 O ASP B 82 N ARG B 5
SHEET 5 AA4 7 HIS B 65 PHE B 74 -1 N VAL B 67 O ILE B 85
SHEET 6 AA4 7 PHE B 133 ASP B 141 1 O PHE B 139 N GLU B 73
SHEET 7 AA4 7 THR B 144 GLU B 152 -1 O SER B 147 N LYS B 138
SSBOND 1 CYS A 134 CYS B 134 1555 1555 2.05
SITE 1 AC1 11 THR A 8 PHE A 27 ASN A 33 PHE A 72
SITE 2 AC1 11 PHE A 74 TRP A 117 ASP A 119 ASP A 120
SITE 3 AC1 11 TRP A 123 PHE A 139 SO4 A 202
SITE 1 AC2 9 LEU A 9 LYS A 23 ASN A 33 GLY A 34
SITE 2 AC2 9 GLY A 36 GLU A 56 MET A 101 2GE A 201
SITE 3 AC2 9 HOH A 365
SITE 1 AC3 4 LEU A 108 ASP A 109 GLN A 110 ILE A 111
SITE 1 AC4 6 HIS A 69 SER A 71 GLY A 135 GLY B 135
SITE 2 AC4 6 HIS B 136 SCN B 205
SITE 1 AC5 13 TYR B 7 THR B 8 LEU B 9 PHE B 27
SITE 2 AC5 13 ASN B 33 PHE B 72 PHE B 74 TRP B 117
SITE 3 AC5 13 ASP B 119 ASP B 120 TRP B 123 PHE B 139
SITE 4 AC5 13 SO4 B 202
SITE 1 AC6 7 LYS B 23 ASN B 33 GLY B 34 GLY B 36
SITE 2 AC6 7 GLU B 56 2GE B 201 HOH B 314
SITE 1 AC7 3 TYR B 7 PHE B 27 GLN B 140
SITE 1 AC8 4 PRO B 103 GLN B 104 TRP B 105 HOH B 320
SITE 1 AC9 7 GLY A 135 HIS A 136 SER A 149 SCN A 204
SITE 2 AC9 7 HIS B 69 SER B 71 GLY B 135
CRYST1 40.006 67.708 123.133 90.00 90.00 90.00 P 21 21 21 8
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 0.024996 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014769 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008121 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
