HEADER HYDROLASE/HYDROLASE INHIBITOR 23-JUN-17 5XUJ
TITLE CRYSTAL STRUCTURE OF PDE10A IN COMPLEX WITH 7-(4-CHLOROPHENYL)-2-
TITLE 2 METHYLPYRAZOLO[1,5-A]PYRIMIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP AND CAMP-INHIBITED CGMP 3',5'-CYCLIC PHOSPHODIESTERASE
COMPND 3 10A;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: UNP RESIDUES 449-789;
COMPND 6 EC: 3.1.4.17,3.1.4.35;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PDE10A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PDE10A INHIBITOR, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.AMANO,K.HONBOU
REVDAT 2 27-MAR-24 5XUJ 1 LINK
REVDAT 1 14-MAR-18 5XUJ 0
JRNL AUTH A.CHINO,R.SEO,Y.AMANO,I.NAMATAME,W.HAMAGUCHI,K.HONBOU,
JRNL AUTH 2 T.MIHARA,M.YAMAZAKI,M.TOMISHIMA,N.MASUDA
JRNL TITL FRAGMENT-BASED DISCOVERY OF PYRIMIDO[1,2-B]INDAZOLE PDE10A
JRNL TITL 2 INHIBITORS.
JRNL REF CHEM. PHARM. BULL. V. 66 286 2018
JRNL REFN ISSN 1347-5223
JRNL PMID 29491261
JRNL DOI 10.1248/CPB.C17-00836
REMARK 2
REMARK 2 RESOLUTION. 2.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 78.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 21730
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1156
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) : 2.44
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.50
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1567
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.44
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5102
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 95
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.02000
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): 1.248
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.350
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.253
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.199
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5243 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7096 ; 1.569 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 627 ; 5.832 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 246 ;37.314 ;24.146
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 936 ;18.804 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;19.698 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 779 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3967 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2517 ; 3.735 ; 5.125
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3141 ; 5.567 ; 7.670
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2726 ; 4.289 ; 5.308
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8466 ; 9.253 ;42.892
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: NULL
REMARK 4
REMARK 4 5XUJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1300004193.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NE3A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23115
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.440
REMARK 200 RESOLUTION RANGE LOW (A) : 78.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.44
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.35600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM BIS-TRIS PROPANE PH6.0, 50MM
REMARK 280 MAGNESIUM SULFATE, 15% PEG 3350, VAPOR DIFFUSION, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 296K
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 25.16950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.79850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.64950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.79850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.16950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.64950
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
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 GLY A 445
REMARK 465 SER A 446
REMARK 465 HIS A 447
REMARK 465 TYR A 574
REMARK 465 LEU A 575
REMARK 465 GLN A 576
REMARK 465 LYS A 577
REMARK 465 PHE A 578
REMARK 465 ASP A 579
REMARK 465 HIS A 580
REMARK 465 PRO A 581
REMARK 465 LEU A 582
REMARK 465 ALA A 583
REMARK 465 ALA A 584
REMARK 465 LEU A 585
REMARK 465 TYR A 586
REMARK 465 SER A 587
REMARK 465 GLU A 770
REMARK 465 THR A 771
REMARK 465 ALA A 772
REMARK 465 THR A 773
REMARK 465 TRP A 774
REMARK 465 ILE A 775
REMARK 465 SER A 776
REMARK 465 SER A 777
REMARK 465 PRO A 778
REMARK 465 SER A 779
REMARK 465 VAL A 780
REMARK 465 ALA A 781
REMARK 465 GLN A 782
REMARK 465 LYS A 783
REMARK 465 ALA A 784
REMARK 465 ALA A 785
REMARK 465 ALA A 786
REMARK 465 SER A 787
REMARK 465 GLU A 788
REMARK 465 ASP A 789
REMARK 465 GLY B 445
REMARK 465 SER B 446
REMARK 465 HIS B 447
REMARK 465 GLU B 770
REMARK 465 THR B 771
REMARK 465 ALA B 772
REMARK 465 THR B 773
REMARK 465 TRP B 774
REMARK 465 ILE B 775
REMARK 465 SER B 776
REMARK 465 SER B 777
REMARK 465 PRO B 778
REMARK 465 SER B 779
REMARK 465 VAL B 780
REMARK 465 ALA B 781
REMARK 465 GLN B 782
REMARK 465 LYS B 783
REMARK 465 ALA B 784
REMARK 465 ALA B 785
REMARK 465 ALA B 786
REMARK 465 SER B 787
REMARK 465 GLU B 788
REMARK 465 ASP B 789
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 902 O HOH A 931 1.74
REMARK 500 O HOH A 902 O HOH A 927 1.94
REMARK 500 O HOH A 927 O HOH A 931 1.98
REMARK 500 CB SER A 612 O HOH A 909 2.08
REMARK 500 O ILE B 630 OG1 THR B 633 2.13
REMARK 500 OG SER A 573 O HOH A 901 2.17
REMARK 500 O PHE A 548 NH1 ARG A 553 2.18
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 HIS A 525 47.13 -71.91
REMARK 500 LEU A 605 154.84 -42.50
REMARK 500 SER A 615 -178.30 -68.38
REMARK 500 TYR A 619 -72.23 -54.11
REMARK 500 GLU A 620 71.12 -59.80
REMARK 500 GLN A 621 -43.88 171.11
REMARK 500 LYS A 718 53.43 -90.94
REMARK 500 VAL A 733 -58.08 -125.22
REMARK 500 LEU B 505 2.69 -68.96
REMARK 500 ARG B 521 52.49 -107.13
REMARK 500 TYR B 524 -55.95 -125.56
REMARK 500 ASP B 579 55.22 39.85
REMARK 500 SER B 589 58.34 31.87
REMARK 500 GLN B 604 -7.86 -53.16
REMARK 500 ASN B 609 91.93 -59.77
REMARK 500 VAL B 733 -72.11 -124.64
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 ZN A 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 529 NE2
REMARK 620 2 HIS A 563 NE2 95.1
REMARK 620 3 ASP A 564 OD2 87.4 82.1
REMARK 620 4 ASP A 674 OD1 92.0 89.7 171.7
REMARK 620 5 HOH A 908 O 170.3 79.7 83.8 96.1
REMARK 620 6 HOH A 931 O 108.1 156.5 95.0 93.1 76.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 564 OD1
REMARK 620 2 HOH A 905 O 88.5
REMARK 620 3 HOH A 906 O 171.0 85.7
REMARK 620 4 HOH A 908 O 95.0 159.7 88.2
REMARK 620 5 HOH A 925 O 96.3 89.6 76.8 70.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 529 NE2
REMARK 620 2 HIS B 563 NE2 94.2
REMARK 620 3 ASP B 564 OD2 82.5 85.7
REMARK 620 4 ASP B 674 OD1 85.4 87.8 165.8
REMARK 620 5 HOH B 906 O 173.2 92.6 97.3 95.5
REMARK 620 6 HOH B 941 O 91.6 168.3 105.1 82.6 81.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 564 OD1
REMARK 620 2 HOH B 901 O 75.1
REMARK 620 3 HOH B 906 O 96.4 92.1
REMARK 620 4 HOH B 927 O 106.0 169.3 77.2
REMARK 620 5 HOH B 933 O 158.8 84.0 81.1 94.0
REMARK 620 6 HOH B 934 O 102.5 90.6 161.0 99.5 80.5
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 ZN A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8G6 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 802
DBREF 5XUJ A 449 789 UNP Q9Y233 PDE10_HUMAN 449 789
DBREF 5XUJ B 449 789 UNP Q9Y233 PDE10_HUMAN 449 789
SEQADV 5XUJ GLY A 445 UNP Q9Y233 EXPRESSION TAG
SEQADV 5XUJ SER A 446 UNP Q9Y233 EXPRESSION TAG
SEQADV 5XUJ HIS A 447 UNP Q9Y233 EXPRESSION TAG
SEQADV 5XUJ MET A 448 UNP Q9Y233 EXPRESSION TAG
SEQADV 5XUJ GLY B 445 UNP Q9Y233 EXPRESSION TAG
SEQADV 5XUJ SER B 446 UNP Q9Y233 EXPRESSION TAG
SEQADV 5XUJ HIS B 447 UNP Q9Y233 EXPRESSION TAG
SEQADV 5XUJ MET B 448 UNP Q9Y233 EXPRESSION TAG
SEQRES 1 A 345 GLY SER HIS MET SER ILE CYS THR SER GLU GLU TRP GLN
SEQRES 2 A 345 GLY LEU MET GLN PHE THR LEU PRO VAL ARG LEU CYS LYS
SEQRES 3 A 345 GLU ILE GLU LEU PHE HIS PHE ASP ILE GLY PRO PHE GLU
SEQRES 4 A 345 ASN MET TRP PRO GLY ILE PHE VAL TYR MET VAL HIS ARG
SEQRES 5 A 345 SER CYS GLY THR SER CYS PHE GLU LEU GLU LYS LEU CYS
SEQRES 6 A 345 ARG PHE ILE MET SER VAL LYS LYS ASN TYR ARG ARG VAL
SEQRES 7 A 345 PRO TYR HIS ASN TRP LYS HIS ALA VAL THR VAL ALA HIS
SEQRES 8 A 345 CYS MET TYR ALA ILE LEU GLN ASN ASN HIS THR LEU PHE
SEQRES 9 A 345 THR ASP LEU GLU ARG LYS GLY LEU LEU ILE ALA CYS LEU
SEQRES 10 A 345 CYS HIS ASP LEU ASP HIS ARG GLY PHE SER ASN SER TYR
SEQRES 11 A 345 LEU GLN LYS PHE ASP HIS PRO LEU ALA ALA LEU TYR SER
SEQRES 12 A 345 THR SER THR MET GLU GLN HIS HIS PHE SER GLN THR VAL
SEQRES 13 A 345 SER ILE LEU GLN LEU GLU GLY HIS ASN ILE PHE SER THR
SEQRES 14 A 345 LEU SER SER SER GLU TYR GLU GLN VAL LEU GLU ILE ILE
SEQRES 15 A 345 ARG LYS ALA ILE ILE ALA THR ASP LEU ALA LEU TYR PHE
SEQRES 16 A 345 GLY ASN ARG LYS GLN LEU GLU GLU MET TYR GLN THR GLY
SEQRES 17 A 345 SER LEU ASN LEU ASN ASN GLN SER HIS ARG ASP ARG VAL
SEQRES 18 A 345 ILE GLY LEU MET MET THR ALA CYS ASP LEU CYS SER VAL
SEQRES 19 A 345 THR LYS LEU TRP PRO VAL THR LYS LEU THR ALA ASN ASP
SEQRES 20 A 345 ILE TYR ALA GLU PHE TRP ALA GLU GLY ASP GLU MET LYS
SEQRES 21 A 345 LYS LEU GLY ILE GLN PRO ILE PRO MET MET ASP ARG ASP
SEQRES 22 A 345 LYS LYS ASP GLU VAL PRO GLN GLY GLN LEU GLY PHE TYR
SEQRES 23 A 345 ASN ALA VAL ALA ILE PRO CYS TYR THR THR LEU THR GLN
SEQRES 24 A 345 ILE LEU PRO PRO THR GLU PRO LEU LEU LYS ALA CYS ARG
SEQRES 25 A 345 ASP ASN LEU SER GLN TRP GLU LYS VAL ILE ARG GLY GLU
SEQRES 26 A 345 GLU THR ALA THR TRP ILE SER SER PRO SER VAL ALA GLN
SEQRES 27 A 345 LYS ALA ALA ALA SER GLU ASP
SEQRES 1 B 345 GLY SER HIS MET SER ILE CYS THR SER GLU GLU TRP GLN
SEQRES 2 B 345 GLY LEU MET GLN PHE THR LEU PRO VAL ARG LEU CYS LYS
SEQRES 3 B 345 GLU ILE GLU LEU PHE HIS PHE ASP ILE GLY PRO PHE GLU
SEQRES 4 B 345 ASN MET TRP PRO GLY ILE PHE VAL TYR MET VAL HIS ARG
SEQRES 5 B 345 SER CYS GLY THR SER CYS PHE GLU LEU GLU LYS LEU CYS
SEQRES 6 B 345 ARG PHE ILE MET SER VAL LYS LYS ASN TYR ARG ARG VAL
SEQRES 7 B 345 PRO TYR HIS ASN TRP LYS HIS ALA VAL THR VAL ALA HIS
SEQRES 8 B 345 CYS MET TYR ALA ILE LEU GLN ASN ASN HIS THR LEU PHE
SEQRES 9 B 345 THR ASP LEU GLU ARG LYS GLY LEU LEU ILE ALA CYS LEU
SEQRES 10 B 345 CYS HIS ASP LEU ASP HIS ARG GLY PHE SER ASN SER TYR
SEQRES 11 B 345 LEU GLN LYS PHE ASP HIS PRO LEU ALA ALA LEU TYR SER
SEQRES 12 B 345 THR SER THR MET GLU GLN HIS HIS PHE SER GLN THR VAL
SEQRES 13 B 345 SER ILE LEU GLN LEU GLU GLY HIS ASN ILE PHE SER THR
SEQRES 14 B 345 LEU SER SER SER GLU TYR GLU GLN VAL LEU GLU ILE ILE
SEQRES 15 B 345 ARG LYS ALA ILE ILE ALA THR ASP LEU ALA LEU TYR PHE
SEQRES 16 B 345 GLY ASN ARG LYS GLN LEU GLU GLU MET TYR GLN THR GLY
SEQRES 17 B 345 SER LEU ASN LEU ASN ASN GLN SER HIS ARG ASP ARG VAL
SEQRES 18 B 345 ILE GLY LEU MET MET THR ALA CYS ASP LEU CYS SER VAL
SEQRES 19 B 345 THR LYS LEU TRP PRO VAL THR LYS LEU THR ALA ASN ASP
SEQRES 20 B 345 ILE TYR ALA GLU PHE TRP ALA GLU GLY ASP GLU MET LYS
SEQRES 21 B 345 LYS LEU GLY ILE GLN PRO ILE PRO MET MET ASP ARG ASP
SEQRES 22 B 345 LYS LYS ASP GLU VAL PRO GLN GLY GLN LEU GLY PHE TYR
SEQRES 23 B 345 ASN ALA VAL ALA ILE PRO CYS TYR THR THR LEU THR GLN
SEQRES 24 B 345 ILE LEU PRO PRO THR GLU PRO LEU LEU LYS ALA CYS ARG
SEQRES 25 B 345 ASP ASN LEU SER GLN TRP GLU LYS VAL ILE ARG GLY GLU
SEQRES 26 B 345 GLU THR ALA THR TRP ILE SER SER PRO SER VAL ALA GLN
SEQRES 27 B 345 LYS ALA ALA ALA SER GLU ASP
HET ZN A 801 1
HET MG A 802 1
HET 8G6 A 803 17
HET ZN B 801 1
HET MG B 802 1
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM 8G6 7-(4-CHLOROPHENYL)-2-METHYL-PYRAZOLO[1,5-A]PYRIMIDINE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 8G6 C13 H10 CL N3
FORMUL 8 HOH *95(H2 O)
HELIX 1 AA1 THR A 452 GLN A 461 1 10
HELIX 2 AA2 PRO A 465 CYS A 469 5 5
HELIX 3 AA3 LYS A 470 LEU A 474 5 5
HELIX 4 AA4 PHE A 482 ASN A 484 5 3
HELIX 5 AA5 MET A 485 GLY A 499 1 15
HELIX 6 AA6 GLU A 504 ASN A 518 1 15
HELIX 7 AA7 ASN A 526 ASN A 543 1 18
HELIX 8 AA8 ASN A 544 PHE A 548 5 5
HELIX 9 AA9 THR A 549 HIS A 563 1 15
HELIX 10 AB1 SER A 589 LEU A 605 1 17
HELIX 11 AB2 SER A 615 THR A 633 1 19
HELIX 12 AB3 ASP A 634 GLY A 652 1 19
HELIX 13 AB4 ASN A 658 LEU A 675 1 18
HELIX 14 AB5 CYS A 676 LYS A 680 5 5
HELIX 15 AB6 LEU A 681 LYS A 705 1 25
HELIX 16 AB7 ASP A 715 ASP A 720 5 6
HELIX 17 AB8 GLU A 721 VAL A 733 1 13
HELIX 18 AB9 VAL A 733 LEU A 745 1 13
HELIX 19 AC1 THR A 748 ARG A 767 1 20
HELIX 20 AC2 THR B 452 PHE B 462 1 11
HELIX 21 AC3 PRO B 465 GLU B 473 1 9
HELIX 22 AC4 ILE B 479 ASN B 484 5 6
HELIX 23 AC5 MET B 485 GLY B 499 1 15
HELIX 24 AC6 GLU B 504 ASN B 518 1 15
HELIX 25 AC7 ASN B 526 ASN B 543 1 18
HELIX 26 AC8 ASN B 544 PHE B 548 5 5
HELIX 27 AC9 THR B 549 HIS B 563 1 15
HELIX 28 AD1 SER B 571 LYS B 577 1 7
HELIX 29 AD2 HIS B 580 TYR B 586 1 7
HELIX 30 AD3 SER B 589 GLN B 604 1 16
HELIX 31 AD4 SER B 615 THR B 633 1 19
HELIX 32 AD5 ASP B 634 THR B 651 1 18
HELIX 33 AD6 ASN B 658 CYS B 676 1 19
HELIX 34 AD7 SER B 677 LYS B 680 5 4
HELIX 35 AD8 LEU B 681 LEU B 706 1 26
HELIX 36 AD9 ILE B 711 ASP B 720 5 10
HELIX 37 AE1 GLU B 721 VAL B 733 1 13
HELIX 38 AE2 VAL B 733 LEU B 745 1 13
HELIX 39 AE3 THR B 748 ARG B 767 1 20
LINK NE2 HIS A 529 ZN ZN A 801 1555 1555 2.15
LINK NE2 HIS A 563 ZN ZN A 801 1555 1555 1.83
LINK OD2 ASP A 564 ZN ZN A 801 1555 1555 2.23
LINK OD1 ASP A 564 MG MG A 802 1555 1555 1.84
LINK OD1 ASP A 674 ZN ZN A 801 1555 1555 2.20
LINK ZN ZN A 801 O HOH A 908 1555 1555 2.20
LINK ZN ZN A 801 O HOH A 931 1555 1555 2.18
LINK MG MG A 802 O HOH A 905 1555 1555 2.21
LINK MG MG A 802 O HOH A 906 1555 1555 2.00
LINK MG MG A 802 O HOH A 908 1555 1555 2.09
LINK MG MG A 802 O HOH A 925 1555 1555 2.29
LINK NE2 HIS B 529 ZN ZN B 801 1555 1555 2.23
LINK NE2 HIS B 563 ZN ZN B 801 1555 1555 2.03
LINK OD2 ASP B 564 ZN ZN B 801 1555 1555 2.08
LINK OD1 ASP B 564 MG MG B 802 1555 1555 1.78
LINK OD1 ASP B 674 ZN ZN B 801 1555 1555 2.19
LINK ZN ZN B 801 O HOH B 906 1555 1555 2.08
LINK ZN ZN B 801 O HOH B 941 1555 1555 2.41
LINK MG MG B 802 O HOH B 901 1555 1555 2.21
LINK MG MG B 802 O HOH B 906 1555 1555 2.20
LINK MG MG B 802 O HOH B 927 1555 1555 2.28
LINK MG MG B 802 O HOH B 933 1555 1555 2.25
LINK MG MG B 802 O HOH B 934 1555 1555 2.11
SITE 1 AC1 6 HIS A 529 HIS A 563 ASP A 564 ASP A 674
SITE 2 AC1 6 HOH A 908 HOH A 931
SITE 1 AC2 5 ASP A 564 HOH A 905 HOH A 906 HOH A 908
SITE 2 AC2 5 HOH A 925
SITE 1 AC3 4 TYR A 524 LEU A 635 GLN A 726 PHE A 729
SITE 1 AC4 7 HIS B 529 HIS B 563 ASP B 564 ASP B 674
SITE 2 AC4 7 MG B 802 HOH B 906 HOH B 941
SITE 1 AC5 7 ASP B 564 ZN B 801 HOH B 901 HOH B 906
SITE 2 AC5 7 HOH B 927 HOH B 933 HOH B 934
CRYST1 50.339 81.299 157.597 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 0.019865 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012300 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006345 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
