HEADER HYDROLASE 03-FEB-16 5HZX
TITLE CRYSTAL STRUCTURE OF ZEBRAFISH MTH1 IN COMPLEX WITH TH588
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUDIX (NUCLEOSIDE DIPHOSPHATE LINKED MOIETY X)-TYPE MOTIF
COMPND 3 1;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: UNCHARACTERIZED PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DANIO RERIO;
SOURCE 3 ORGANISM_COMMON: ZEBRAFISH;
SOURCE 4 ORGANISM_TAXID: 7955;
SOURCE 5 GENE: NUDT1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS INHIBITOR, COMPLEX, MTH1, TH588, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.NARWAL,R.GUSTAFSSON,L.BRAUTIGAM,L.PUDELKO,A.-S.JEMTH,H.GAD,
AUTHOR 2 S.KARSTEN,J.CARRERAS-PUIGVERT,E.HOMAN,C.BERNDT,U.W.BERGLUND,
AUTHOR 3 T.HELLEDAY,P.STENMARK
REVDAT 5 10-JAN-24 5HZX 1 REMARK
REVDAT 4 06-SEP-17 5HZX 1 REMARK
REVDAT 3 01-JUN-16 5HZX 1 JRNL
REVDAT 2 24-FEB-16 5HZX 1 AUTHOR
REVDAT 1 10-FEB-16 5HZX 0
JRNL AUTH L.BRAUTIGAM,L.PUDELKO,A.S.JEMTH,H.GAD,M.NARWAL,R.GUSTAFSSON,
JRNL AUTH 2 S.KARSTEN,J.CARRERAS PUIGVERT,E.HOMAN,C.BERNDT,U.W.BERGLUND,
JRNL AUTH 3 P.STENMARK,T.HELLEDAY
JRNL TITL HYPOXIC SIGNALING AND THE CELLULAR REDOX TUMOR ENVIRONMENT
JRNL TITL 2 DETERMINE SENSITIVITY TO MTH1 INHIBITION.
JRNL REF CANCER RES. V. 76 2366 2016
JRNL REFN ESSN 1538-7445
JRNL PMID 26862114
JRNL DOI 10.1158/0008-5472.CAN-15-2380
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 25407
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1377
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1840
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.3010
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.3640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2506
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 298
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.91000
REMARK 3 B22 (A**2) : -0.54000
REMARK 3 B33 (A**2) : -0.37000
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): 0.165
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.412
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2702 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2563 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3653 ; 1.311 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5908 ; 0.914 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 320 ; 5.981 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 130 ;32.176 ;24.462
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 482 ;13.372 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;18.846 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 384 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3030 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 629 ; 0.003 ; 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): 1266 ; 1.042 ; 1.629
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1264 ; 1.041 ; 1.628
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1589 ; 1.793 ; 2.437
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1590 ; 1.792 ; 2.437
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1436 ; 1.406 ; 1.846
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1436 ; 1.406 ; 1.846
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2058 ; 2.349 ; 2.707
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3011 ; 5.337 ;13.813
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3012 ; 5.337 ;13.825
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 156 B 3 156 9430 0.09 0.05
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 5HZX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218017.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91991
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26840
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 47.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.21000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 1.00000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: 3ZR1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG 10K, 0.1 M SODIUM ACETATE, PH
REMARK 280 4.0, 0.2 M LITHIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+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 38.13000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.60100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.13000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.60100
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 HIS A 0
REMARK 465 MET A 1
REMARK 465 PHE A 2
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 MET B 1
REMARK 465 PHE B 2
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 62 -83.45 -77.71
REMARK 500 ASP A 62 -83.45 -77.58
REMARK 500 ASP B 62 -81.95 -76.57
REMARK 500 ASP B 62 -81.95 -78.92
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 SO4 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2GE B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4N1U RELATED DB: PDB
REMARK 900 4N1U CONTAINS THE SAME INHIBITOR
DBREF 5HZX A 1 156 UNP Q7ZWC3 Q7ZWC3_DANRE 1 156
DBREF 5HZX B 1 156 UNP Q7ZWC3 Q7ZWC3_DANRE 1 156
SEQADV 5HZX MET A -19 UNP Q7ZWC3 INITIATING METHIONINE
SEQADV 5HZX GLY A -18 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX SER A -17 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX SER A -16 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS A -15 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS A -14 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS A -13 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS A -12 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS A -11 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS A -10 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX SER A -9 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX SER A -8 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX GLY A -7 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX LEU A -6 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX VAL A -5 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX PRO A -4 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX ARG A -3 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX GLY A -2 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX SER A -1 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS A 0 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX MET B -19 UNP Q7ZWC3 INITIATING METHIONINE
SEQADV 5HZX GLY B -18 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX SER B -17 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX SER B -16 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS B -15 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS B -14 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS B -13 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS B -12 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS B -11 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS B -10 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX SER B -9 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX SER B -8 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX GLY B -7 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX LEU B -6 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX VAL B -5 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX PRO B -4 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX ARG B -3 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX GLY B -2 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX SER B -1 UNP Q7ZWC3 EXPRESSION TAG
SEQADV 5HZX HIS B 0 UNP Q7ZWC3 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 PHE THR SER LYS LEU
SEQRES 3 A 176 LEU THR LEU VAL LEU VAL VAL GLN PRO GLY ARG VAL LEU
SEQRES 4 A 176 LEU GLY MET LYS LYS ARG GLY PHE GLY ALA GLY LYS TRP
SEQRES 5 A 176 ASN GLY PHE GLY GLY LYS VAL GLN THR GLY GLU THR ILE
SEQRES 6 A 176 GLU GLN ALA ALA ARG ARG GLU LEU LEU GLU GLU SER GLY
SEQRES 7 A 176 LEU THR VAL ASP THR LEU HIS LYS ILE GLY ASN ILE LYS
SEQRES 8 A 176 PHE GLU PHE ILE GLY GLU THR GLU LEU MET ASP VAL HIS
SEQRES 9 A 176 ILE PHE ARG ALA ASP ASN TYR GLU GLY GLU PRO ALA GLU
SEQRES 10 A 176 SER ASP GLU MET ARG PRO GLN TRP PHE ASP ILE ASP LYS
SEQRES 11 A 176 ILE PRO PHE SER GLN MET TRP ALA ASP ASP ILE LEU TRP
SEQRES 12 A 176 PHE PRO LEU MET LEU GLN LYS LYS ARG PHE LEU GLY TYR
SEQRES 13 A 176 PHE LYS PHE GLN GLY HIS ASP VAL ILE VAL GLU HIS LYS
SEQRES 14 A 176 LEU ASP GLU VAL GLU ASP LEU
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 PHE THR SER LYS LEU
SEQRES 3 B 176 LEU THR LEU VAL LEU VAL VAL GLN PRO GLY ARG VAL LEU
SEQRES 4 B 176 LEU GLY MET LYS LYS ARG GLY PHE GLY ALA GLY LYS TRP
SEQRES 5 B 176 ASN GLY PHE GLY GLY LYS VAL GLN THR GLY GLU THR ILE
SEQRES 6 B 176 GLU GLN ALA ALA ARG ARG GLU LEU LEU GLU GLU SER GLY
SEQRES 7 B 176 LEU THR VAL ASP THR LEU HIS LYS ILE GLY ASN ILE LYS
SEQRES 8 B 176 PHE GLU PHE ILE GLY GLU THR GLU LEU MET ASP VAL HIS
SEQRES 9 B 176 ILE PHE ARG ALA ASP ASN TYR GLU GLY GLU PRO ALA GLU
SEQRES 10 B 176 SER ASP GLU MET ARG PRO GLN TRP PHE ASP ILE ASP LYS
SEQRES 11 B 176 ILE PRO PHE SER GLN MET TRP ALA ASP ASP ILE LEU TRP
SEQRES 12 B 176 PHE PRO LEU MET LEU GLN LYS LYS ARG PHE LEU GLY TYR
SEQRES 13 B 176 PHE LYS PHE GLN GLY HIS ASP VAL ILE VAL GLU HIS LYS
SEQRES 14 B 176 LEU ASP GLU VAL GLU ASP LEU
HET 2GE A 201 19
HET SO4 A 202 5
HET SO4 A 203 5
HET SO4 A 204 5
HET GOL A 205 6
HET PEG A 206 7
HET 2GE B 201 19
HET SO4 B 202 5
HET SO4 B 203 5
HET ACT B 204 4
HETNAM 2GE N~4~-CYCLOPROPYL-6-(2,3-DICHLOROPHENYL)PYRIMIDINE-2,4-
HETNAM 2 2GE DIAMINE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM ACT ACETATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 2GE 2(C13 H12 CL2 N4)
FORMUL 4 SO4 5(O4 S 2-)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 PEG C4 H10 O3
FORMUL 12 ACT C2 H3 O2 1-
FORMUL 13 HOH *298(H2 O)
HELIX 1 AA1 THR A 44 GLY A 58 1 15
HELIX 2 AA2 ASP A 109 ILE A 111 5 3
HELIX 3 AA3 PRO A 112 MET A 116 5 5
HELIX 4 AA4 ASP A 119 GLN A 129 1 11
HELIX 5 AA5 GLU A 154 LEU A 156 5 3
HELIX 6 AA6 THR B 44 GLY B 58 1 15
HELIX 7 AA7 ASP B 109 ILE B 111 5 3
HELIX 8 AA8 PRO B 112 MET B 116 5 5
HELIX 9 AA9 ASP B 119 GLN B 129 1 11
HELIX 10 AB1 GLU B 154 LEU B 156 5 3
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 GLN A 14 -1 N GLN A 14 O ARG A 17
SHEET 4 AA1 4 MET A 101 ASP A 107 0
SHEET 1 AA2 7 PHE A 35 LYS A 38 0
SHEET 2 AA2 7 SER A 4 GLN A 14 -1 N THR A 8 O GLY A 37
SHEET 3 AA2 7 ARG A 17 LYS A 23 -1 O ARG A 17 N GLN A 14
SHEET 4 AA2 7 LEU A 80 ALA A 88 0
SHEET 5 AA2 7 HIS A 65 PHE A 74 -1 N GLY A 68 O ILE A 85
SHEET 6 AA2 7 PHE A 133 GLN A 140 1 O PHE A 139 N GLU A 73
SHEET 7 AA2 7 VAL A 144 GLU A 152 -1 O VAL A 144 N GLN A 140
SHEET 1 AA3 4 TRP B 32 ASN B 33 0
SHEET 2 AA3 4 ARG B 17 LYS B 23 -1 N GLY B 21 O ASN B 33
SHEET 3 AA3 4 SER B 4 GLN B 14 -1 N GLN B 14 O ARG B 17
SHEET 4 AA3 4 MET B 101 ASP B 107 0
SHEET 1 AA4 7 PHE B 35 LYS B 38 0
SHEET 2 AA4 7 SER B 4 GLN B 14 -1 N THR B 8 O GLY B 37
SHEET 3 AA4 7 ARG B 17 LYS B 23 -1 O ARG B 17 N GLN B 14
SHEET 4 AA4 7 LEU B 80 ALA B 88 0
SHEET 5 AA4 7 HIS B 65 PHE B 74 -1 N GLY B 68 O ILE B 85
SHEET 6 AA4 7 PHE B 133 GLN B 140 1 O PHE B 139 N GLU B 73
SHEET 7 AA4 7 VAL B 144 GLU B 152 -1 O VAL B 144 N GLN B 140
SITE 1 AC1 9 THR A 8 ASN A 33 PHE A 72 PHE A 74
SITE 2 AC1 9 MET A 81 TRP A 117 ASP A 119 ASP A 120
SITE 3 AC1 9 SO4 A 202
SITE 1 AC2 10 LEU A 9 LYS A 23 ASN A 33 GLY A 34
SITE 2 AC2 10 GLY A 36 GLY A 37 GLU A 56 2GE A 201
SITE 3 AC2 10 HOH A 339 LEU B 156
SITE 1 AC3 4 ARG A 132 HOH A 311 HOH A 347 ARG B 25
SITE 1 AC4 6 ASP A 62 THR A 63 HIS A 65 ASP A 89
SITE 2 AC4 6 ASN A 90 HOH A 308
SITE 1 AC5 2 ASN A 90 TYR A 91
SITE 1 AC6 8 GLU A 46 GLN A 47 ARG A 50 GLN A 115
SITE 2 AC6 8 HOH A 310 HOH A 324 HOH A 340 HOH A 356
SITE 1 AC7 9 THR B 8 PHE B 27 ASN B 33 PHE B 72
SITE 2 AC7 9 MET B 81 TRP B 117 ASP B 119 ASP B 120
SITE 3 AC7 9 SO4 B 202
SITE 1 AC8 8 LEU A 156 LYS B 23 GLY B 34 GLY B 36
SITE 2 AC8 8 GLY B 37 GLU B 56 2GE B 201 HOH B 324
SITE 1 AC9 3 ARG A 25 ARG B 132 HOH B 334
SITE 1 AD1 4 HOH A 335 LEU B 122 HOH B 309 HOH B 347
CRYST1 76.260 71.202 60.924 90.00 90.00 90.00 P 21 21 2 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 0.013113 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014045 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016414 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
