GenomeNet

Database: PDB
Entry: 6K9U
LinkDB: 6K9U
Original site: 6K9U 
HEADER    HYDROLASE                               18-JUN-19   6K9U              
TITLE     DISCOVERY OF PYRAZOLO[1,5-A]PYRIMIDINE DERIVATIVE AS A HIGHLY         
TITLE    2 SELECTIVE PDE10A INHIBITOR                                           
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_TAXID: 7108                                        
KEYWDS    ENZYME, PDE, BBB, BRAIN PENETRATION, CRYSTATL STRUCTURE, INHIBITOR,   
KEYWDS   2 SCHIZOPHRENIA, HYDROLASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TAKEDOMI,Y.KOIZUMI                                                  
REVDAT   2   07-AUG-19 6K9U    1       JRNL                                     
REVDAT   1   17-JUL-19 6K9U    0                                                
JRNL        AUTH   Y.KOIZUMI,Y.TANAKA,T.MATSUMURA,Y.KADOH,H.MIYOSHI,M.HONGU,    
JRNL        AUTH 2 K.TAKEDOMI,J.KOTERA,T.SASAKI,H.TANIGUCHI,Y.WATANABE,         
JRNL        AUTH 3 M.TAKAKUWA,K.KOJIMA,N.BABA,I.NAKAMURA,E.KAWANISHI            
JRNL        TITL   DISCOVERY OF A PYRAZOLO[1,5-A]PYRIMIDINE DERIVATIVE          
JRNL        TITL 2 (MT-3014) AS A HIGHLY SELECTIVE PDE10A INHIBITOR VIA CORE    
JRNL        TITL 3 STRUCTURE TRANSFORMATION FROM THE STILBENE MOIETY.           
JRNL        REF    BIOORG.MED.CHEM.              V.  27  3440 2019              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   31235264                                                     
JRNL        DOI    10.1016/J.BMC.2019.06.021                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 65.38                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 17980                          
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 905                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1348                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2462                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 111                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.25000                                             
REMARK   3    B22 (A**2) : -1.25000                                             
REMARK   3    B33 (A**2) : 1.88000                                              
REMARK   3    B12 (A**2) : -0.63000                                             
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): 0.243         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.195         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.921        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2536 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2265 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3445 ; 1.095 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5264 ; 0.803 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   306 ; 4.939 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   116 ;33.876 ;24.052       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   430 ;13.426 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;12.875 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   374 ; 0.059 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2794 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   518 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   598 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2205 ; 0.170 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1266 ; 0.177 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1179 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   107 ; 0.122 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.113 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     8 ; 0.142 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    31 ; 0.224 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.107 ; 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):  1993 ; 1.957 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   611 ; 0.433 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2454 ; 2.285 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1237 ; 3.780 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   989 ; 5.384 ; 6.000       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   454        A   760                          
REMARK   3    ORIGIN FOR THE GROUP (A):   17.727   16.865   27.437              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0462 T22:   0.0740                                     
REMARK   3      T33:   0.0513 T12:  -0.0408                                     
REMARK   3      T13:  -0.0330 T23:   0.0417                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2560 L22:   2.4407                                     
REMARK   3      L33:   1.4970 L12:   0.7313                                     
REMARK   3      L13:   0.2995 L23:   0.3467                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1356 S12:  -0.3369 S13:  -0.1069                       
REMARK   3      S21:   0.0995 S22:  -0.1509 S23:  -0.0318                       
REMARK   3      S31:   0.0738 S32:   0.0477 S33:   0.0153                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6K9U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300012281.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JAN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9999                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18913                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.380                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.6500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.35900                            
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: BICINE, PEG2000, PH 8.5, VAPOR           
REMARK 280  DIFFUSION, TEMPERATURE 293K                                         
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       60.22800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.77265            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       27.96633            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       60.22800            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       34.77265            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       27.96633            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       60.22800            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       34.77265            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       27.96633            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.54530            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       55.93267            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       69.54530            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       55.93267            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       69.54530            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       55.93267            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2                            
REMARK 350 SURFACE AREA OF THE COMPLEX: 14260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     PRO A   452                                                      
REMARK 465     ASN A   453                                                      
REMARK 465     CYS A   488                                                      
REMARK 465     GLY A   489                                                      
REMARK 465     THR A   490                                                      
REMARK 465     SER A   491                                                      
REMARK 465     CYS A   492                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LEU A  454   CG   CD1  CD2                                       
REMARK 480     ARG A  460   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     HIS A  485   CG   ND1  CD2  CE1  NE2                             
REMARK 480     GLU A  494   CG   CD   OE1  OE2                                  
REMARK 480     LEU A  495   CG   CD1  CD2                                       
REMARK 480     GLU A  496   CG   CD   OE1  OE2                                  
REMARK 480     ARG A  500   CZ   NH1  NH2                                       
REMARK 480     LYS A  507   CG   CD   CE   NZ                                   
REMARK 480     ASN A  535   CG   OD1  ND2                                       
REMARK 480     LYS A  544   CD   CE   NZ                                        
REMARK 480     GLU A  596   CG   CD   OE1  OE2                                  
REMARK 480     ARG A  709   NE   CZ   NH1  NH2                                  
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      -57.31   -124.21                                   
REMARK 500    VAL A 723      -58.88   -120.65                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 519   NE2                                                    
REMARK 620 2 HIS A 553   NE2 107.0                                              
REMARK 620 3 ASP A 554   OD2  90.8  89.2                                        
REMARK 620 4 ASP A 664   OD1  90.0  88.9 178.1                                  
REMARK 620 5 HOH A 906   O   131.4 121.3  94.8  85.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 802  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 554   OD1                                                    
REMARK 620 2 HOH A 906   O    97.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D4L A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 804                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AUTHORS WROTE THAT PHE452 IS THE N-TERMINAL OF PDE10 USED IN THIS    
REMARK 999 EXPERIMENT.                                                          
DBREF  6K9U A  452   760  UNP    Q9QYJ6   PDE10_RAT      462    770             
SEQADV 6K9U GLY A  450  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 6K9U SER A  451  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 6K9U PRO A  452  UNP  Q9QYJ6    PHE   462 SEE SEQUENCE DETAILS           
SEQRES   1 A  311  GLY SER PRO ASN LEU PRO ALA ARG ILE CYS ARG ASP ILE          
SEQRES   2 A  311  GLU LEU PHE HIS PHE ASP ILE GLY PRO PHE GLU ASN MET          
SEQRES   3 A  311  TRP PRO GLY ILE PHE VAL TYR MET ILE HIS ARG SER CYS          
SEQRES   4 A  311  GLY THR SER CYS PHE GLU LEU GLU LYS LEU CYS ARG PHE          
SEQRES   5 A  311  ILE MET SER VAL LYS LYS ASN TYR ARG ARG VAL PRO TYR          
SEQRES   6 A  311  HIS ASN TRP LYS HIS ALA VAL THR VAL ALA HIS CYS MET          
SEQRES   7 A  311  TYR ALA ILE LEU GLN ASN ASN ASN GLY LEU PHE THR ASP          
SEQRES   8 A  311  LEU GLU ARG LYS GLY LEU LEU ILE ALA CYS LEU CYS HIS          
SEQRES   9 A  311  ASP LEU ASP HIS ARG GLY PHE SER ASN SER TYR LEU GLN          
SEQRES  10 A  311  LYS PHE ASP HIS PRO LEU ALA ALA LEU TYR SER THR SER          
SEQRES  11 A  311  THR MET GLU GLN HIS HIS PHE SER GLN THR VAL SER ILE          
SEQRES  12 A  311  LEU GLN LEU GLU GLY HIS ASN ILE PHE SER THR LEU SER          
SEQRES  13 A  311  SER SER GLU TYR GLU GLN VAL LEU GLU ILE ILE ARG LYS          
SEQRES  14 A  311  ALA ILE ILE ALA THR ASP LEU ALA LEU TYR PHE GLY ASN          
SEQRES  15 A  311  ARG LYS GLN LEU GLU GLU MET TYR GLN THR GLY SER LEU          
SEQRES  16 A  311  ASN LEU HIS ASN GLN SER HIS ARG ASP ARG VAL ILE GLY          
SEQRES  17 A  311  LEU MET MET THR ALA CYS ASP LEU CYS SER VAL THR LYS          
SEQRES  18 A  311  LEU TRP PRO VAL THR LYS LEU THR ALA ASN ASP ILE TYR          
SEQRES  19 A  311  ALA GLU PHE TRP ALA GLU GLY ASP GLU MET LYS LYS LEU          
SEQRES  20 A  311  GLY ILE GLN PRO ILE PRO MET MET ASP ARG ASP LYS ARG          
SEQRES  21 A  311  ASP GLU VAL PRO GLN GLY GLN LEU GLY PHE TYR ASN ALA          
SEQRES  22 A  311  VAL ALA ILE PRO CYS TYR THR THR LEU THR GLN ILE LEU          
SEQRES  23 A  311  PRO PRO THR GLU PRO LEU LEU LYS ALA CYS ARG ASP ASN          
SEQRES  24 A  311  LEU ASN GLN TRP GLU LYS VAL ILE ARG GLY GLU GLU              
HET     ZN  A 801       1                                                       
HET     MG  A 802       1                                                       
HET    D4L  A 803      33                                                       
HET    SO4  A 804       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     D4L 2-(3,7-DIMETHYLQUINOXALIN-2-YL)-~{N}-(OXAN-4-YL)-5-              
HETNAM   2 D4L  PYRROLIDIN-1-YL-PYRAZOLO[1,5-A]PYRIMIDIN-7-AMINE                
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  D4L    C25 H29 N7 O                                                 
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   6  HOH   *111(H2 O)                                                    
HELIX    1 AA1 PRO A  455  ILE A  462  1                                   8    
HELIX    2 AA2 PHE A  472  ASN A  474  5                                   3    
HELIX    3 AA3 MET A  475  SER A  487  1                                  13    
HELIX    4 AA4 GLU A  494  TYR A  509  1                                  16    
HELIX    5 AA5 ASN A  516  ASN A  533  1                                  18    
HELIX    6 AA6 THR A  539  HIS A  553  1                                  15    
HELIX    7 AA7 SER A  561  ASP A  569  1                                   9    
HELIX    8 AA8 HIS A  570  TYR A  576  1                                   7    
HELIX    9 AA9 SER A  579  GLN A  594  1                                  16    
HELIX   10 AB1 SER A  605  THR A  623  1                                  19    
HELIX   11 AB2 ASP A  624  THR A  641  1                                  18    
HELIX   12 AB3 ASN A  648  LEU A  665  1                                  18    
HELIX   13 AB4 CYS A  666  LYS A  670  5                                   5    
HELIX   14 AB5 LEU A  671  LEU A  696  1                                  26    
HELIX   15 AB6 ILE A  701  ASP A  710  5                                  10    
HELIX   16 AB7 GLU A  711  VAL A  723  1                                  13    
HELIX   17 AB8 VAL A  723  LEU A  735  1                                  13    
HELIX   18 AB9 THR A  738  ARG A  757  1                                  20    
LINK         NE2 HIS A 519                ZN    ZN A 801     1555   1555  2.06  
LINK         NE2 HIS A 553                ZN    ZN A 801     1555   1555  2.08  
LINK         OD1 ASP A 554                MG    MG A 802     1555   1555  2.35  
LINK         OD2 ASP A 554                ZN    ZN A 801     1555   1555  2.13  
LINK         OD1 ASP A 664                ZN    ZN A 801     1555   1555  2.13  
LINK        ZN    ZN A 801                 O   HOH A 906     1555   1555  1.91  
LINK        MG    MG A 802                 O   HOH A 906     1555   1555  2.34  
SITE     1 AC1  6 HIS A 519  HIS A 553  ASP A 554  ASP A 664                    
SITE     2 AC1  6  MG A 802  HOH A 906                                          
SITE     1 AC2  4 HIS A 515  ASP A 554   ZN A 801  HOH A 906                    
SITE     1 AC3 12 TYR A 514  HIS A 647  GLN A 649  LEU A 665                    
SITE     2 AC3 12 SER A 667  TYR A 683  PRO A 702  MET A 703                    
SITE     3 AC3 12 LYS A 708  GLY A 715  GLN A 716  PHE A 719                    
SITE     1 AC4  7 ARG A 457  ASP A 461  PHE A 467  ASP A 468                    
SITE     2 AC4  7 LYS A 695  LEU A 696  HOH A 901                               
CRYST1  120.456  120.456   83.899  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      0.008302  0.004793  0.000000        0.00000                         
SCALE2      0.000000  0.009586  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011919        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system