GenomeNet

Database: PDB
Entry: 3HR1
LinkDB: 3HR1
Original site: 3HR1 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           08-JUN-09   3HR1              
TITLE     DISCOVERY OF NOVEL INHIBITORS OF PDE10A                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP AND CAMP-INHIBITED CGMP 3',5'-CYCLIC                  
COMPND   3 PHOSPHODIESTERASE 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: BACULOVIRUS                                
KEYWDS    PHOSPHODIESTERASE 10A, PDE 10A, PDE10 INHIBITORS, ALLOSTERIC          
KEYWDS   2 ENZYME, ALTERNATIVE SPLICING, CAMP, CAMP-BINDING, CGMP,              
KEYWDS   3 CGMP-BINDING, CYTOPLASM, HYDROLASE, MAGNESIUM, METAL-                
KEYWDS   4 BINDING, NUCLEOTIDE-BINDING, ZINC, HYDROLASE/HYDROLASE               
KEYWDS   5 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PANDIT,E.S.MARR                                                     
REVDAT   2   22-SEP-09 3HR1    1       JRNL                                     
REVDAT   1   04-AUG-09 3HR1    0                                                
JRNL        AUTH   P.R.VERHOEST,D.S.CHAPIN,M.CORMAN,K.FONSECA,                  
JRNL        AUTH 2 J.F.HARMS,X.HOU,E.S.MARR,F.S.MENNITI,F.NELSON,               
JRNL        AUTH 3 R.O'CONNOR,J.PANDIT,C.PROULX-LAFRANCE,A.W.SCHMIDT,           
JRNL        AUTH 4 C.J.SCHMIDT,J.A.SUICIAK,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                
JRNL        TITL 5 TREATMENT OF SCHIZOPHRENIA                                   
JRNL        REF    J.MED.CHEM.                   V.  52  5188 2009              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   19630403                                                     
JRNL        DOI    10.1021/JM900521K                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.53 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 57989                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4479                            
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) : 1.53                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 586                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 12.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 65                           
REMARK   3   BIN FREE R VALUE                    : 0.4290                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2488                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 456                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.64000                                             
REMARK   3    B22 (A**2) : -0.64000                                             
REMARK   3    B33 (A**2) : 0.96000                                              
REMARK   3    B12 (A**2) : -0.32000                                             
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): 0.082         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.083         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.058         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.627         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2592 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3513 ; 1.179 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   306 ; 4.670 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   124 ;34.884 ;23.710       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   450 ;12.191 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;21.318 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   377 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1969 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1407 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1806 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   336 ; 0.143 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.044 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    57 ; 0.203 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    34 ; 0.185 ; 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):  1586 ; 0.736 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2479 ; 1.104 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1178 ; 1.862 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1034 ; 2.900 ; 4.500       
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 : 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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3HR1 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053477.                                      
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 FRE                         
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : DTREK                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57998                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.530                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 17.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 2O8H                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
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       60.33000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.83154            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       27.73667            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       60.33000            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       34.83154            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       27.73667            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       60.33000            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       34.83154            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       27.73667            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.66308            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       55.47333            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       69.66308            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       55.47333            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       69.66308            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       55.47333            
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   405                                                      
REMARK 465     HIS A   406                                                      
REMARK 465     HIS A   407                                                      
REMARK 465     HIS A   408                                                      
REMARK 465     HIS A   409                                                      
REMARK 465     HIS A   410                                                      
REMARK 465     HIS A   411                                                      
REMARK 465     SER A   412                                                      
REMARK 465     SER A   413                                                      
REMARK 465     GLY A   414                                                      
REMARK 465     LEU A   415                                                      
REMARK 465     VAL A   416                                                      
REMARK 465     PRO A   417                                                      
REMARK 465     ARG A   418                                                      
REMARK 465     GLY A   419                                                      
REMARK 465     SER A   420                                                      
REMARK 465     ALA A   421                                                      
REMARK 465     MET 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     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   115     O    HOH A   829              2.01            
REMARK 500   O    HOH A   312     O    HOH A   365              2.10            
REMARK 500   O    HOH A    96     O    HOH A   835              2.11            
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   ND2  ASN A   474     O2   SO4 A   998     3555     2.14            
REMARK 500   O    HOH A   801     O    HOH A   824     3555     2.19            
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    TYR A 514      -55.11   -121.92                                   
REMARK 500    VAL A 723      -63.78   -130.41                                   
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 101.9                                              
REMARK 620 3 ASP A 554   OD2  91.1  90.0                                        
REMARK 620 4 ASP A 664   OD1  85.5  94.6 174.8                                  
REMARK 620 5 HOH A   3   O   149.4 108.6  90.5  90.5                            
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   3   O   100.0                                              
REMARK 620 3 HOH A   5   O   103.7  88.5                                        
REMARK 620 4 HOH A 786   O    87.3 167.8  80.2                                  
REMARK 620 5 HOH A   4   O   164.6  93.1  84.7  81.3                            
REMARK 620 6 HOH A 785   O    85.6 104.3 162.8  85.9  83.2                      
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 SO4 A 997                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 998                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PF9 A 999                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1                    
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3HQW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HQY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HQZ   RELATED DB: PDB                                   
DBREF  3HR1 A  442   784  UNP    Q9QYJ6   PDE10_RAT      452    794             
SEQADV 3HR1 MET A  405  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 HIS A  406  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 HIS A  407  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 HIS A  408  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 HIS A  409  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 HIS A  410  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 HIS A  411  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 SER A  412  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 SER A  413  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 GLY A  414  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 LEU A  415  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 VAL A  416  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 PRO A  417  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 ARG A  418  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 GLY A  419  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 SER A  420  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 ALA A  421  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 MET A  422  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 MET A  423  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 HIS A  424  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 HIS A  425  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 HIS A  426  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 HIS A  427  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 HIS A  428  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 HIS A  429  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 SER A  430  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 SER A  431  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 GLY A  432  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 LEU A  433  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 VAL A  434  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 PRO A  435  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 ARG A  436  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 GLY A  437  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 SER A  438  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 ALA A  439  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 MET A  440  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 3HR1 GLY A  441  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQRES   1 A  380  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 A  380  ARG GLY SER ALA MET MET HIS HIS HIS HIS HIS HIS SER          
SEQRES   3 A  380  SER GLY LEU VAL PRO ARG GLY SER ALA MET GLY THR SER          
SEQRES   4 A  380  GLU GLU TRP GLN GLY LEU MET HIS PHE ASN LEU PRO ALA          
SEQRES   5 A  380  ARG ILE CYS ARG ASP ILE GLU LEU PHE HIS PHE ASP ILE          
SEQRES   6 A  380  GLY PRO PHE GLU ASN MET TRP PRO GLY ILE PHE VAL TYR          
SEQRES   7 A  380  MET ILE HIS ARG SER CYS GLY THR SER CYS PHE GLU LEU          
SEQRES   8 A  380  GLU LYS LEU CYS ARG PHE ILE MET SER VAL LYS LYS ASN          
SEQRES   9 A  380  TYR ARG ARG VAL PRO TYR HIS ASN TRP LYS HIS ALA VAL          
SEQRES  10 A  380  THR VAL ALA HIS CYS MET TYR ALA ILE LEU GLN ASN ASN          
SEQRES  11 A  380  ASN GLY LEU PHE THR ASP LEU GLU ARG LYS GLY LEU LEU          
SEQRES  12 A  380  ILE ALA CYS LEU CYS HIS ASP LEU ASP HIS ARG GLY PHE          
SEQRES  13 A  380  SER ASN SER TYR LEU GLN LYS PHE ASP HIS PRO LEU ALA          
SEQRES  14 A  380  ALA LEU TYR SER THR SER THR MET GLU GLN HIS HIS PHE          
SEQRES  15 A  380  SER GLN THR VAL SER ILE LEU GLN LEU GLU GLY HIS ASN          
SEQRES  16 A  380  ILE PHE SER THR LEU SER SER SER GLU TYR GLU GLN VAL          
SEQRES  17 A  380  LEU GLU ILE ILE ARG LYS ALA ILE ILE ALA THR ASP LEU          
SEQRES  18 A  380  ALA LEU TYR PHE GLY ASN ARG LYS GLN LEU GLU GLU MET          
SEQRES  19 A  380  TYR GLN THR GLY SER LEU ASN LEU HIS ASN GLN SER HIS          
SEQRES  20 A  380  ARG ASP ARG VAL ILE GLY LEU MET MET THR ALA CYS ASP          
SEQRES  21 A  380  LEU CYS SER VAL THR LYS LEU TRP PRO VAL THR LYS LEU          
SEQRES  22 A  380  THR ALA ASN ASP ILE TYR ALA GLU PHE TRP ALA GLU GLY          
SEQRES  23 A  380  ASP GLU MET LYS LYS LEU GLY ILE GLN PRO ILE PRO MET          
SEQRES  24 A  380  MET ASP ARG ASP LYS ARG ASP GLU VAL PRO GLN GLY GLN          
SEQRES  25 A  380  LEU GLY PHE TYR ASN ALA VAL ALA ILE PRO CYS TYR THR          
SEQRES  26 A  380  THR LEU THR GLN ILE LEU PRO PRO THR GLU PRO LEU LEU          
SEQRES  27 A  380  LYS ALA CYS ARG ASP ASN LEU ASN GLN TRP GLU LYS VAL          
SEQRES  28 A  380  ILE ARG GLY GLU GLU THR ALA MET TRP ILE SER GLY PRO          
SEQRES  29 A  380  ALA THR SER LYS SER THR SER GLU LYS PRO THR ARG LYS          
SEQRES  30 A  380  VAL ASP ASP                                                  
HET    SO4  A 997       5                                                       
HET    SO4  A 998       5                                                       
HET    PF9  A 999      30                                                       
HET     ZN  A   1       1                                                       
HET     MG  A   2       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PF9 2-{[4-(1-METHYL-4-PYRIDIN-4-YL-1H-PYRAZOL-3-YL)                  
HETNAM   2 PF9  PHENOXY]METHYL}QUINOLINE                                        
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  PF9    C25 H20 N4 O                                                 
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   6   MG    MG 2+                                                        
FORMUL   7  HOH   *456(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  THR A  623  1                                  19    
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         NE2 HIS A 519                ZN    ZN A   1     1555   1555  2.13  
LINK         NE2 HIS A 553                ZN    ZN A   1     1555   1555  2.11  
LINK         OD1 ASP A 554                MG    MG A   2     1555   1555  2.04  
LINK         OD2 ASP A 554                ZN    ZN A   1     1555   1555  2.18  
LINK         OD1 ASP A 664                ZN    ZN A   1     1555   1555  2.19  
LINK        ZN    ZN A   1                 O   HOH A   3     1555   1555  2.05  
LINK        MG    MG A   2                 O   HOH A   3     1555   1555  1.95  
LINK        MG    MG A   2                 O   HOH A   5     1555   1555  2.19  
LINK        MG    MG A   2                 O   HOH A 786     1555   1555  2.33  
LINK        MG    MG A   2                 O   HOH A   4     1555   1555  2.15  
LINK        MG    MG A   2                 O   HOH A 785     1555   1555  2.12  
SITE     1 AC1  5 HOH A 341  GLU A 473  ASN A 474  ARG A 510                    
SITE     2 AC1  5 SO4 A 998                                                     
SITE     1 AC2  8 HOH A 153  HOH A 164  PHE A 472  GLU A 473                    
SITE     2 AC2  8 ASN A 474  ARG A 510  ARG A 558  SO4 A 997                    
SITE     1 AC3 18 HOH A   8  HOH A  84  HOH A  98  TYR A 514                    
SITE     2 AC3 18 HIS A 647  LEU A 665  VAL A 668  TYR A 683                    
SITE     3 AC3 18 PHE A 686  PRO A 702  MET A 703  LYS A 708                    
SITE     4 AC3 18 GLU A 711  VAL A 712  GLY A 715  GLN A 716                    
SITE     5 AC3 18 PHE A 719  HOH A 829                                          
SITE     1 AC4  7  MG A   2  HOH A   3  HOH A 115  HIS A 519                    
SITE     2 AC4  7 HIS A 553  ASP A 554  ASP A 664                               
SITE     1 AC5  7  ZN A   1  HOH A   3  HOH A   4  HOH A   5                    
SITE     2 AC5  7 ASP A 554  HOH A 785  HOH A 786                               
CRYST1  120.660  120.660   83.210  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      0.008288  0.004785  0.000000        0.00000                         
SCALE2      0.000000  0.009570  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012018        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system