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Database: PDB
Entry: 3HQW
LinkDB: 3HQW
Original site: 3HQW 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           08-JUN-09   3HQW              
TITLE     DISCOVERY OF NOVEL INHIBITORS OF PDE10A                               
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 EC: 3.1.4.17, 3.1.4.35;                                              
COMPND   6 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: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    PHOSPHODIESTERASE 10A PDE10A PDE INHIBITORS, ALLOSTERIC ENZYME,       
KEYWDS   2 ALTERNATIVE SPLICING, CAMP, CAMP-BINDING, CGMP, CGMP-BINDING,        
KEYWDS   3 CYTOPLASM, HYDROLASE, MAGNESIUM, METAL-BINDING, NUCLEOTIDE-BINDING,  
KEYWDS   4 ZINC, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PANDIT,E.S.MARR                                                     
REVDAT   4   04-APR-18 3HQW    1       REMARK                                   
REVDAT   3   01-NOV-17 3HQW    1       REMARK                                   
REVDAT   2   22-SEP-09 3HQW    1       JRNL                                     
REVDAT   1   04-AUG-09 3HQW    0                                                
JRNL        AUTH   P.R.VERHOEST,D.S.CHAPIN,M.CORMAN,K.FONSECA,J.F.HARMS,X.HOU,  
JRNL        AUTH 2 E.S.MARR,F.S.MENNITI,F.NELSON,R.O'CONNOR,J.PANDIT,           
JRNL        AUTH 3 C.PROULX-LAFRANCE,A.W.SCHMIDT,C.J.SCHMIDT,J.A.SUICIAK,       
JRNL        AUTH 4 S.LIRAS                                                      
JRNL        TITL   DISCOVERY OF A NOVEL CLASS OF PHOSPHODIESTERASE 10A          
JRNL        TITL 2 INHIBITORS AND IDENTIFICATION OF CLINICAL CANDIDATE          
JRNL        TITL 3 2-[4-(1-METHYL-4-PYRIDIN-4-YL-1H-PYRAZOL-3-YL)               
JRNL        TITL 4 -PHENOXYMETHYL]-QUINOLINE (PF-2545920) FOR THE TREATMENT OF  
JRNL        TITL 5 SCHIZOPHRENIA                                                
JRNL        REF    J.MED.CHEM.                   V.  52  5188 2009              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   19630403                                                     
JRNL        DOI    10.1021/JM900521K                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 49409                          
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) : 0.159                           
REMARK   3   R VALUE            (WORKING SET) : 0.157                           
REMARK   3   FREE R VALUE                     : 0.185                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3803                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3037                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3250                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 243                          
REMARK   3   BIN FREE R VALUE                    : 0.3410                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2461                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 576                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.81000                                             
REMARK   3    B22 (A**2) : -0.81000                                             
REMARK   3    B33 (A**2) : 1.22000                                              
REMARK   3    B12 (A**2) : -0.41000                                             
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): 0.083         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.084         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.056         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.741         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2551 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2276 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3454 ; 1.186 ; 1.951       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5295 ; 0.802 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   302 ; 4.785 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   373 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2806 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   535 ; 0.007 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   653 ; 0.225 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2710 ; 0.237 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1264 ; 0.080 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   403 ; 0.167 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.151 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     9 ; 0.149 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    42 ; 0.259 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    40 ; 0.211 ; 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):  1513 ; 0.646 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2451 ; 1.309 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1038 ; 2.111 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1003 ; 3.510 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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   : 1.40                                          
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 3HQW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000053472.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, D*TREK                      
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, D*TREK                  
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49482                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.9770                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2O8H                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       60.48000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.91814            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       27.70933            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       60.48000            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       34.91814            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       27.70933            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       60.48000            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       34.91814            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       27.70933            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.83629            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       55.41867            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       69.83629            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       55.41867            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       69.83629            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       55.41867            
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 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 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   409                                                      
REMARK 465     HIS A   410                                                      
REMARK 465     HIS A   411                                                      
REMARK 465     HIS A   412                                                      
REMARK 465     HIS A   413                                                      
REMARK 465     HIS A   414                                                      
REMARK 465     HIS A   415                                                      
REMARK 465     SER A   416                                                      
REMARK 465     SER A   417                                                      
REMARK 465     GLY A   418                                                      
REMARK 465     LEU A   419                                                      
REMARK 465     VAL A   420                                                      
REMARK 465     PRO A   421                                                      
REMARK 465     ARG A   422                                                      
REMARK 465     MET A   423                                                      
REMARK 465     HIS A   424                                                      
REMARK 465     HIS A   425                                                      
REMARK 465     HIS A   426                                                      
REMARK 465     HIS A   427                                                      
REMARK 465     HIS A   428                                                      
REMARK 465     HIS A   429                                                      
REMARK 465     SER A   430                                                      
REMARK 465     SER A   431                                                      
REMARK 465     GLY A   432                                                      
REMARK 465     LEU A   433                                                      
REMARK 465     VAL A   434                                                      
REMARK 465     PRO A   435                                                      
REMARK 465     ARG A   436                                                      
REMARK 465     GLY A   437                                                      
REMARK 465     SER A   438                                                      
REMARK 465     ALA A   439                                                      
REMARK 465     MET A   440                                                      
REMARK 465     GLY A   441                                                      
REMARK 465     THR A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     GLU A   444                                                      
REMARK 465     GLU A   445                                                      
REMARK 465     TRP A   446                                                      
REMARK 465     GLN A   447                                                      
REMARK 465     GLY A   448                                                      
REMARK 465     LEU A   449                                                      
REMARK 465     MET A   450                                                      
REMARK 465     HIS A   451                                                      
REMARK 465     PHE A   452                                                      
REMARK 465     ASN A   453                                                      
REMARK 465     LEU A   454                                                      
REMARK 465     GLY A   758                                                      
REMARK 465     GLU A   759                                                      
REMARK 465     GLU A   760                                                      
REMARK 465     THR A   761                                                      
REMARK 465     ALA A   762                                                      
REMARK 465     MET A   763                                                      
REMARK 465     TRP A   764                                                      
REMARK 465     ILE A   765                                                      
REMARK 465     SER A   766                                                      
REMARK 465     GLY A   767                                                      
REMARK 465     PRO A   768                                                      
REMARK 465     ALA A   769                                                      
REMARK 465     THR A   770                                                      
REMARK 465     SER A   771                                                      
REMARK 465     LYS A   772                                                      
REMARK 465     SER A   773                                                      
REMARK 465     THR A   774                                                      
REMARK 465     SER A   775                                                      
REMARK 465     GLU A   776                                                      
REMARK 465     LYS A   777                                                      
REMARK 465     PRO A   778                                                      
REMARK 465     THR A   779                                                      
REMARK 465     ARG A   780                                                      
REMARK 465     LYS A   781                                                      
REMARK 465     VAL A   782                                                      
REMARK 465     ASP A   783                                                      
REMARK 465     ASP A   784                                                      
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   933     O    HOH A   943              1.72            
REMARK 500   O    HOH A   211     O    HOH A   939              2.03            
REMARK 500   CE1  HIS A   647     O    HOH A   935              2.05            
REMARK 500   ND1  HIS A   647     O    HOH A   935              2.06            
REMARK 500   O    HOH A    92     O    HOH A   935              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   933     O    HOH A   934     2555     2.11            
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    SER A 491       31.73    -95.32                                   
REMARK 500    TYR A 514      -50.99   -125.45                                   
REMARK 500    VAL A 723      -64.54   -125.76                                   
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   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 519   NE2                                                    
REMARK 620 2 HIS A 553   NE2 110.0                                              
REMARK 620 3 ASP A 554   OD2  89.1  89.3                                        
REMARK 620 4 ASP A 664   OD1  93.3  92.2 176.5                                  
REMARK 620 5 HOH A 938   O   136.9 113.0  88.4  88.1                            
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 938   O    83.1                                              
REMARK 620 3 HOH A 805   O    96.9 158.8                                        
REMARK 620 4 HOH A 920   O    87.0 114.0  87.2                                  
REMARK 620 N                    1     2     3                                   
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 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PF4 A 999                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3HQY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HQZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HQ1   RELATED DB: PDB                                   
DBREF  3HQW A  442   784  UNP    Q9QYJ6   PDE10_RAT      452    794             
SEQADV 3HQW MET A  409  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW HIS A  410  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW HIS A  411  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW HIS A  412  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW HIS A  413  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW HIS A  414  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW HIS A  415  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW SER A  416  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW SER A  417  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW GLY A  418  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW LEU A  419  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW VAL A  420  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW PRO A  421  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW ARG A  422  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW MET A  423  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW HIS A  424  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW HIS A  425  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW HIS A  426  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW HIS A  427  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW HIS A  428  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW HIS A  429  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW SER A  430  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW SER A  431  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW GLY A  432  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW LEU A  433  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW VAL A  434  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW PRO A  435  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW ARG A  436  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW GLY A  437  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW SER A  438  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW ALA A  439  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW MET A  440  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HQW GLY A  441  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQRES   1 A  376  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 A  376  ARG MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL          
SEQRES   3 A  376  PRO ARG GLY SER ALA MET GLY THR SER GLU GLU TRP GLN          
SEQRES   4 A  376  GLY LEU MET HIS PHE ASN LEU PRO ALA ARG ILE CYS ARG          
SEQRES   5 A  376  ASP ILE GLU LEU PHE HIS PHE ASP ILE GLY PRO PHE GLU          
SEQRES   6 A  376  ASN MET TRP PRO GLY ILE PHE VAL TYR MET ILE HIS ARG          
SEQRES   7 A  376  SER CYS GLY THR SER CYS PHE GLU LEU GLU LYS LEU CYS          
SEQRES   8 A  376  ARG PHE ILE MET SER VAL LYS LYS ASN TYR ARG ARG VAL          
SEQRES   9 A  376  PRO TYR HIS ASN TRP LYS HIS ALA VAL THR VAL ALA HIS          
SEQRES  10 A  376  CYS MET TYR ALA ILE LEU GLN ASN ASN ASN GLY LEU PHE          
SEQRES  11 A  376  THR ASP LEU GLU ARG LYS GLY LEU LEU ILE ALA CYS LEU          
SEQRES  12 A  376  CYS HIS ASP LEU ASP HIS ARG GLY PHE SER ASN SER TYR          
SEQRES  13 A  376  LEU GLN LYS PHE ASP HIS PRO LEU ALA ALA LEU TYR SER          
SEQRES  14 A  376  THR SER THR MET GLU GLN HIS HIS PHE SER GLN THR VAL          
SEQRES  15 A  376  SER ILE LEU GLN LEU GLU GLY HIS ASN ILE PHE SER THR          
SEQRES  16 A  376  LEU SER SER SER GLU TYR GLU GLN VAL LEU GLU ILE ILE          
SEQRES  17 A  376  ARG LYS ALA ILE ILE ALA THR ASP LEU ALA LEU TYR PHE          
SEQRES  18 A  376  GLY ASN ARG LYS GLN LEU GLU GLU MET TYR GLN THR GLY          
SEQRES  19 A  376  SER LEU ASN LEU HIS ASN GLN SER HIS ARG ASP ARG VAL          
SEQRES  20 A  376  ILE GLY LEU MET MET THR ALA CYS ASP LEU CYS SER VAL          
SEQRES  21 A  376  THR LYS LEU TRP PRO VAL THR LYS LEU THR ALA ASN ASP          
SEQRES  22 A  376  ILE TYR ALA GLU PHE TRP ALA GLU GLY ASP GLU MET LYS          
SEQRES  23 A  376  LYS LEU GLY ILE GLN PRO ILE PRO MET MET ASP ARG ASP          
SEQRES  24 A  376  LYS ARG ASP GLU VAL PRO GLN GLY GLN LEU GLY PHE TYR          
SEQRES  25 A  376  ASN ALA VAL ALA ILE PRO CYS TYR THR THR LEU THR GLN          
SEQRES  26 A  376  ILE LEU PRO PRO THR GLU PRO LEU LEU LYS ALA CYS ARG          
SEQRES  27 A  376  ASP ASN LEU ASN GLN TRP GLU LYS VAL ILE ARG GLY GLU          
SEQRES  28 A  376  GLU THR ALA MET TRP ILE SER GLY PRO ALA THR SER LYS          
SEQRES  29 A  376  SER THR SER GLU LYS PRO THR ARG LYS VAL ASP ASP              
HET     ZN  A   1       1                                                       
HET     MG  A   2       1                                                       
HET    PF4  A 999      26                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PF4 4,5-BIS(4-METHOXYPHENYL)-2-THIOPHEN-2-YL-1H-IMIDAZOLE            
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  PF4    C21 H18 N2 O2 S                                              
FORMUL   5  HOH   *576(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 THR A  490  PHE A  493  5                                   4    
HELIX    5   5 GLU A  494  ASN A  508  1                                  15    
HELIX    6   6 ASN A  516  ASN A  533  1                                  18    
HELIX    7   7 THR A  539  HIS A  553  1                                  15    
HELIX    8   8 SER A  561  ASP A  569  1                                   9    
HELIX    9   9 HIS A  570  TYR A  576  1                                   7    
HELIX   10  10 SER A  579  GLN A  594  1                                  16    
HELIX   11  11 SER A  605  THR A  623  1                                  19    
HELIX   12  12 ASP A  624  THR A  641  1                                  18    
HELIX   13  13 ASN A  648  LEU A  665  1                                  18    
HELIX   14  14 CYS A  666  LYS A  670  5                                   5    
HELIX   15  15 LEU A  671  LEU A  696  1                                  26    
HELIX   16  16 ILE A  701  ASP A  710  5                                  10    
HELIX   17  17 GLU A  711  VAL A  723  1                                  13    
HELIX   18  18 VAL A  723  LEU A  735  1                                  13    
HELIX   19  19 THR A  738  ARG A  757  1                                  20    
LINK         NE2 HIS A 519                ZN    ZN A   1     1555   1555  2.01  
LINK         NE2 HIS A 553                ZN    ZN A   1     1555   1555  2.04  
LINK         OD1 ASP A 554                MG    MG A   2     1555   1555  2.19  
LINK         OD2 ASP A 554                ZN    ZN A   1     1555   1555  2.15  
LINK         OD1 ASP A 664                ZN    ZN A   1     1555   1555  2.10  
LINK        ZN    ZN A   1                 O   HOH A 938     1555   1555  1.77  
LINK        MG    MG A   2                 O   HOH A 938     1555   1555  2.47  
LINK        MG    MG A   2                 O   HOH A 805     1555   1555  2.35  
LINK        MG    MG A   2                 O   HOH A 920     1555   1555  1.99  
SITE     1 AC1  5 HIS A 519  HIS A 553  ASP A 554  ASP A 664                    
SITE     2 AC1  5 HOH A 938                                                     
SITE     1 AC2  4 ASP A 554  HOH A 805  HOH A 920  HOH A 938                    
SITE     1 AC3 13 HOH A  26  HIS A 647  VAL A 668  ILE A 682                    
SITE     2 AC3 13 TYR A 683  MET A 703  LYS A 708  GLY A 715                    
SITE     3 AC3 13 GLN A 716  PHE A 719  VAL A 723  HOH A 937                    
SITE     4 AC3 13 HOH A 945                                                     
CRYST1  120.960  120.960   83.128  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      0.008267  0.004773  0.000000        0.00000                         
SCALE2      0.000000  0.009546  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012030        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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