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Database: PDB
Entry: 3LXG
LinkDB: 3LXG
Original site: 3LXG 
HEADER    HYDROLASE                               25-FEB-10   3LXG              
TITLE     CRYSTAL STRUCTURE OF RAT PHOSPHODIESTERASE 10A IN COMPLEX WITH LIGAND 
TITLE    2 WEB-3                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP AND CAMP-INHIBITED CGMP 3',5'-CYCLIC PHOSPHODIESTERASE
COMPND   3 10A;                                                                 
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: RESIDUES 463-770;                                          
COMPND   6 EC: 3.1.4.17, 3.1.4.35;                                              
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: PDE10A;                                                        
SOURCE   6 EXPRESSION_SYSTEM: BACULOVIRUS;                                      
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL: SF9 INSECT CELLS                             
KEYWDS    PHOSPHODIESTERASE 10A; CATALYTIC DOMAIN, ALLOSTERIC ENZYME, CAMP,     
KEYWDS   2 CAMP-BINDING, CGMP, CGMP-BINDING, HYDROLASE, METAL-BINDING,          
KEYWDS   3 NUCLEOTIDE-BINDING                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.MOSBACHER,A.JESTEL,S.STEINBACHER                                    
REVDAT   2   16-JUN-10 3LXG    1       JRNL                                     
REVDAT   1   19-MAY-10 3LXG    0                                                
JRNL        AUTH   N.HOFGEN,H.STANGE,R.SCHINDLER,H.J.LANKAU,C.GRUNWALD,         
JRNL        AUTH 2 B.LANGEN,U.EGERLAND,P.TREMMEL,M.N.PANGALOS,K.L.MARQUIS,      
JRNL        AUTH 3 T.HAGE,B.L.HARRISON,M.S.MALAMAS,N.J.BRANDON,T.KRONBACH       
JRNL        TITL   DISCOVERY OF IMIDAZO[1,5-A]PYRIDO[3,2-E]PYRAZINES AS A NEW   
JRNL        TITL 2 CLASS OF PHOSPHODIESTERASE 10A INHIBITIORS.                  
JRNL        REF    J.MED.CHEM.                   V.  53  4399 2010              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   20450197                                                     
JRNL        DOI    10.1021/JM1002793                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 64.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 17793                          
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 969                             
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 964                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 47                           
REMARK   3   BIN FREE R VALUE                    : 0.3660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2499                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 118                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.87000                                             
REMARK   3    B22 (A**2) : -1.87000                                             
REMARK   3    B33 (A**2) : 2.80000                                              
REMARK   3    B12 (A**2) : -0.93000                                             
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): 0.256         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.211         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.160         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.927         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
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):  2603 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1754 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3532 ; 1.056 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4261 ; 0.853 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   309 ; 5.017 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   124 ;35.042 ;23.871       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   446 ;15.645 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;16.488 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   379 ; 0.057 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2868 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   533 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   649 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1847 ; 0.174 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1307 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1259 ; 0.085 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   123 ; 0.126 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.093 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    11 ; 0.196 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    36 ; 0.183 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.113 ; 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):  2035 ; 1.982 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   619 ; 0.357 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2500 ; 2.448 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1349 ; 3.605 ; 4.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1032 ; 5.080 ; 6.000       
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 : 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 3LXG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057851.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.947                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : LN2 COOLED FIXED-EXIT              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19899                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 64.960                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLPREP                      
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, PH 6.5, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 298K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
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+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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       60.07450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.68403            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       27.70633            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       60.07450            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       34.68403            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       27.70633            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       60.07450            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       34.68403            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       27.70633            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.36806            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       55.41267            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       69.36806            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       55.41267            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       69.36806            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       55.41267            
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: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A  507   CD   CE   NZ                                        
REMARK 480     GLU A  596   CD   OE1  OE2                                       
REMARK 480     LYS A  633   CE   NZ                                             
REMARK 480     GLN A  699   OE1  NE2                                            
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    TYR A 514      -58.17   -131.99                                   
REMARK 500    VAL A 723      -58.07   -124.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A  71        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH A  84        DISTANCE =  5.44 ANGSTROMS                       
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 761  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 111   O                                                      
REMARK 620 2 HIS A 553   NE2 105.1                                              
REMARK 620 3 HIS A 519   NE2 144.6 110.3                                        
REMARK 620 4 ASP A 664   OD1  96.0  91.2  84.8                                  
REMARK 620 5 ASP A 554   OD2  79.8  94.1  96.1 173.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A   2  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 554   OD1                                                    
REMARK 620 2 HOH A 109   O    75.1                                              
REMARK 620 3 HOH A 110   O    97.9  84.9                                        
REMARK 620 4 HOH A 108   O   161.0  86.9  86.3                                  
REMARK 620 5 HOH A 111   O    81.6  95.6 179.2  94.4                            
REMARK 620 6 HOH A 104   O   116.5 164.4  83.2  82.3  96.4                      
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 Z73 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 761                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2                    
DBREF  3LXG A  453   760  UNP    Q9QYJ6   PDE10_RAT      463    770             
SEQRES   1 A  308  ASN LEU PRO ALA ARG ILE CYS ARG ASP ILE GLU LEU PHE          
SEQRES   2 A  308  HIS PHE ASP ILE GLY PRO PHE GLU ASN MET TRP PRO GLY          
SEQRES   3 A  308  ILE PHE VAL TYR MET ILE HIS ARG SER CYS GLY THR SER          
SEQRES   4 A  308  CYS PHE GLU LEU GLU LYS LEU CYS ARG PHE ILE MET SER          
SEQRES   5 A  308  VAL LYS LYS ASN TYR ARG ARG VAL PRO TYR HIS ASN TRP          
SEQRES   6 A  308  LYS HIS ALA VAL THR VAL ALA HIS CYS MET TYR ALA ILE          
SEQRES   7 A  308  LEU GLN ASN ASN ASN GLY LEU PHE THR ASP LEU GLU ARG          
SEQRES   8 A  308  LYS GLY LEU LEU ILE ALA CYS LEU CYS HIS ASP LEU ASP          
SEQRES   9 A  308  HIS ARG GLY PHE SER ASN SER TYR LEU GLN LYS PHE ASP          
SEQRES  10 A  308  HIS PRO LEU ALA ALA LEU TYR SER THR SER THR MET GLU          
SEQRES  11 A  308  GLN HIS HIS PHE SER GLN THR VAL SER ILE LEU GLN LEU          
SEQRES  12 A  308  GLU GLY HIS ASN ILE PHE SER THR LEU SER SER SER GLU          
SEQRES  13 A  308  TYR GLU GLN VAL LEU GLU ILE ILE ARG LYS ALA ILE ILE          
SEQRES  14 A  308  ALA THR ASP LEU ALA LEU TYR PHE GLY ASN ARG LYS GLN          
SEQRES  15 A  308  LEU GLU GLU MET TYR GLN THR GLY SER LEU ASN LEU HIS          
SEQRES  16 A  308  ASN GLN SER HIS ARG ASP ARG VAL ILE GLY LEU MET MET          
SEQRES  17 A  308  THR ALA CYS ASP LEU CYS SER VAL THR LYS LEU TRP PRO          
SEQRES  18 A  308  VAL THR LYS LEU THR ALA ASN ASP ILE TYR ALA GLU PHE          
SEQRES  19 A  308  TRP ALA GLU GLY ASP GLU MET LYS LYS LEU GLY ILE GLN          
SEQRES  20 A  308  PRO ILE PRO MET MET ASP ARG ASP LYS ARG ASP GLU VAL          
SEQRES  21 A  308  PRO GLN GLY GLN LEU GLY PHE TYR ASN ALA VAL ALA ILE          
SEQRES  22 A  308  PRO CYS TYR THR THR LEU THR GLN ILE LEU PRO PRO THR          
SEQRES  23 A  308  GLU PRO LEU LEU LYS ALA CYS ARG ASP ASN LEU ASN GLN          
SEQRES  24 A  308  TRP GLU LYS VAL ILE ARG GLY GLU GLU                          
HET    Z73  A   1      20                                                       
HET     ZN  A 761       1                                                       
HET     MG  A   2       1                                                       
HETNAM     Z73 2-METHOXY-6,7-DIMETHYL-9-PROPYLIMIDAZO[1,5-A]PYRIDO[3,           
HETNAM   2 Z73  2-E]PYRAZINE                                                    
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2  Z73    C15 H18 N4 O                                                 
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  HOH   *118(H2 O)                                                    
HELIX    1   1 PRO A  455  ILE A  462  1                                   8    
HELIX    2   2 PHE A  472  ASN A  474  5                                   3    
HELIX    3   3 MET A  475  GLY A  489  1                                  15    
HELIX    4   4 GLU A  494  ASN A  508  1                                  15    
HELIX    5   5 ASN A  516  ASN A  533  1                                  18    
HELIX    6   6 THR A  539  HIS A  553  1                                  15    
HELIX    7   7 SER A  561  ASP A  569  1                                   9    
HELIX    8   8 HIS A  570  TYR A  576  1                                   7    
HELIX    9   9 SER A  579  GLN A  594  1                                  16    
HELIX   10  10 SER A  605  ALA A  622  1                                  18    
HELIX   11  11 ASP A  624  THR A  641  1                                  18    
HELIX   12  12 ASN A  648  LEU A  665  1                                  18    
HELIX   13  13 CYS A  666  LYS A  670  5                                   5    
HELIX   14  14 LEU A  671  LEU A  696  1                                  26    
HELIX   15  15 ILE A  701  ASP A  710  5                                  10    
HELIX   16  16 GLU A  711  VAL A  723  1                                  13    
HELIX   17  17 VAL A  723  LEU A  735  1                                  13    
HELIX   18  18 THR A  738  ARG A  757  1                                  20    
LINK        ZN    ZN A 761                 O   HOH A 111     1555   1555  1.89  
LINK         NE2 HIS A 553                ZN    ZN A 761     1555   1555  2.05  
LINK         NE2 HIS A 519                ZN    ZN A 761     1555   1555  2.10  
LINK         OD1 ASP A 554                MG    MG A   2     1555   1555  2.13  
LINK         OD1 ASP A 664                ZN    ZN A 761     1555   1555  2.13  
LINK        MG    MG A   2                 O   HOH A 109     1555   1555  2.14  
LINK        MG    MG A   2                 O   HOH A 110     1555   1555  2.18  
LINK         OD2 ASP A 554                ZN    ZN A 761     1555   1555  2.19  
LINK        MG    MG A   2                 O   HOH A 108     1555   1555  2.33  
LINK        MG    MG A   2                 O   HOH A 111     1555   1555  2.37  
LINK        MG    MG A   2                 O   HOH A 104     1555   1555  2.54  
SITE     1 AC1 10 HOH A  18  TYR A 514  LEU A 665  SER A 667                    
SITE     2 AC1 10 VAL A 668  ILE A 682  PHE A 686  MET A 703                    
SITE     3 AC1 10 GLN A 716  PHE A 719                                          
SITE     1 AC2  5 HOH A 111  HIS A 519  HIS A 553  ASP A 554                    
SITE     2 AC2  5 ASP A 664                                                     
SITE     1 AC3  6 HOH A 104  HOH A 108  HOH A 109  HOH A 110                    
SITE     2 AC3  6 HOH A 111  ASP A 554                                          
CRYST1  120.149  120.149   83.119  90.00  90.00 120.00 H 3           9          
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      0.008323  0.004805  0.000000        0.00000                         
SCALE2      0.000000  0.009611  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012031        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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