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Database: PDB
Entry: 2O8H
LinkDB: 2O8H
Original site: 2O8H 
HEADER    HYDROLASE                               12-DEC-06   2O8H              
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF RAT PHOSPHODIESTERASE 10A
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHODIESTERASE-10A;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND   5 SYNONYM: PDE10A2;                                                    
COMPND   6 EC: 3.1.4.17;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: PDE10A, PDE10A;                                                
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    PHOSPHODIESTERASE 10A; ZN-BINDING SITE, HYDROLASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PANDIT,E.S.MARR                                                     
REVDAT   5   18-OCT-17 2O8H    1       REMARK                                   
REVDAT   4   24-FEB-09 2O8H    1       VERSN                                    
REVDAT   3   27-FEB-07 2O8H    1       JRNL                                     
REVDAT   2   13-FEB-07 2O8H    1       JRNL                                     
REVDAT   1   09-JAN-07 2O8H    0                                                
JRNL        AUTH   T.A.CHAPPIE,J.M.HUMPHREY,M.P.ALLEN,K.G.ESTEP,C.B.FOX,        
JRNL        AUTH 2 L.A.LEBEL,S.LIRAS,E.S.MARR,F.S.MENNITI,J.PANDIT,C.J.SCHMIDT, 
JRNL        AUTH 3 M.TU,R.D.WILLIAMS,F.V.YANG                                   
JRNL        TITL   DISCOVERY OF A SERIES OF                                     
JRNL        TITL 2 6,7-DIMETHOXY-4-PYRROLIDYLQUINAZOLINE PDE10A INHIBITORS      
JRNL        REF    J.MED.CHEM.                   V.  50   182 2007              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   17228859                                                     
JRNL        DOI    10.1021/JM060653B                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 37822                          
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2905                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1437                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 133                          
REMARK   3   BIN FREE R VALUE                    : 0.4290                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2491                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 312                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.27000                                             
REMARK   3    B22 (A**2) : -2.27000                                             
REMARK   3    B33 (A**2) : 3.40000                                              
REMARK   3    B12 (A**2) : -1.13000                                             
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): 0.148         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.148         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.152         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.541         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2590 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2312 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3511 ; 1.476 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5384 ; 0.896 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   306 ; 5.391 ; 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):   380 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2834 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   532 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   765 ; 0.231 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2802 ; 0.245 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1393 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   194 ; 0.233 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     4 ; 0.162 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    10 ; 0.129 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    50 ; 0.210 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.254 ; 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):  1532 ; 0.742 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2481 ; 1.312 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1058 ; 2.071 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1030 ; 3.245 ; 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 2O8H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-DEC-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000040819.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-02                          
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37865                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 53.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67500                            
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: AMORE                                                 
REMARK 200 STARTING MODEL: HOMOLOGY MODEL OF PDE10A                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
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       60.31100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.82057            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       27.38100            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       60.31100            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       34.82057            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       27.38100            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       60.31100            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       34.82057            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       27.38100            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.64114            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       54.76200            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       69.64114            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       54.76200            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       69.64114            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       54.76200            
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   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     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   307     O    HOH A   309              1.75            
REMARK 500   OE1  GLN A   588     O    HOH A   306              2.03            
REMARK 500   O    HOH A   143     O    HOH A   293              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 468   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 540   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 653   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
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    CYS A 488      -61.93   -100.31                                   
REMARK 500    TYR A 514      -53.76   -122.87                                   
REMARK 500    ASN A 516     -168.75   -118.43                                   
REMARK 500    ILE A 530       36.73    -91.05                                   
REMARK 500    LEU A 531      -48.63   -136.36                                   
REMARK 500    THR A 603        0.33    -69.00                                   
REMARK 500    VAL A 723      -61.23   -126.05                                   
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 A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 664   OD1                                                    
REMARK 620 2 HIS A 519   NE2  89.5                                              
REMARK 620 3 HIS A 553   NE2  95.9 108.4                                        
REMARK 620 4 ASP A 554   OD2 176.5  94.0  82.5                                  
REMARK 620 5 HOH A 308   O    89.9 151.8  99.7  87.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1002  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 126   O                                                      
REMARK 620 2 HOH A 159   O    81.9                                              
REMARK 620 3 HOH A 260   O    81.9  89.5                                        
REMARK 620 4 HOH A 308   O   156.8  96.6 121.3                                  
REMARK 620 5 ASP A 554   OD1  93.9 172.6  96.0  84.8                            
REMARK 620 N                    1     2     3     4                             
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 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 227 A 999                 
DBREF  2O8H A  442   784  UNP    Q9QYJ6   Q9QYJ6_RAT     452    794             
SEQADV 2O8H MET A  423  UNP  Q9QYJ6              INITIATING METHIONINE          
SEQADV 2O8H HIS A  424  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 2O8H HIS A  425  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 2O8H HIS A  426  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 2O8H HIS A  427  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 2O8H HIS A  428  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 2O8H HIS A  429  UNP  Q9QYJ6              EXPRESSION TAG                 
SEQADV 2O8H SER A  430  UNP  Q9QYJ6              CLONING ARTIFACT               
SEQADV 2O8H SER A  431  UNP  Q9QYJ6              CLONING ARTIFACT               
SEQADV 2O8H GLY A  432  UNP  Q9QYJ6              CLONING ARTIFACT               
SEQADV 2O8H LEU A  433  UNP  Q9QYJ6              CLONING ARTIFACT               
SEQADV 2O8H VAL A  434  UNP  Q9QYJ6              CLONING ARTIFACT               
SEQADV 2O8H PRO A  435  UNP  Q9QYJ6              CLONING ARTIFACT               
SEQADV 2O8H ARG A  436  UNP  Q9QYJ6              CLONING ARTIFACT               
SEQADV 2O8H GLY A  437  UNP  Q9QYJ6              CLONING ARTIFACT               
SEQADV 2O8H SER A  438  UNP  Q9QYJ6              CLONING ARTIFACT               
SEQADV 2O8H ALA A  439  UNP  Q9QYJ6              CLONING ARTIFACT               
SEQADV 2O8H MET A  440  UNP  Q9QYJ6              CLONING ARTIFACT               
SEQADV 2O8H GLY A  441  UNP  Q9QYJ6              CLONING ARTIFACT               
SEQRES   1 A  362  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 A  362  ARG GLY SER ALA MET GLY THR SER GLU GLU TRP GLN GLY          
SEQRES   3 A  362  LEU MET HIS PHE ASN LEU PRO ALA ARG ILE CYS ARG ASP          
SEQRES   4 A  362  ILE GLU LEU PHE HIS PHE ASP ILE GLY PRO PHE GLU ASN          
SEQRES   5 A  362  MET TRP PRO GLY ILE PHE VAL TYR MET ILE HIS ARG SER          
SEQRES   6 A  362  CYS GLY THR SER CYS PHE GLU LEU GLU LYS LEU CYS ARG          
SEQRES   7 A  362  PHE ILE MET SER VAL LYS LYS ASN TYR ARG ARG VAL PRO          
SEQRES   8 A  362  TYR HIS ASN TRP LYS HIS ALA VAL THR VAL ALA HIS CYS          
SEQRES   9 A  362  MET TYR ALA ILE LEU GLN ASN ASN ASN GLY LEU PHE THR          
SEQRES  10 A  362  ASP LEU GLU ARG LYS GLY LEU LEU ILE ALA CYS LEU CYS          
SEQRES  11 A  362  HIS ASP LEU ASP HIS ARG GLY PHE SER ASN SER TYR LEU          
SEQRES  12 A  362  GLN LYS PHE ASP HIS PRO LEU ALA ALA LEU TYR SER THR          
SEQRES  13 A  362  SER THR MET GLU GLN HIS HIS PHE SER GLN THR VAL SER          
SEQRES  14 A  362  ILE LEU GLN LEU GLU GLY HIS ASN ILE PHE SER THR LEU          
SEQRES  15 A  362  SER SER SER GLU TYR GLU GLN VAL LEU GLU ILE ILE ARG          
SEQRES  16 A  362  LYS ALA ILE ILE ALA THR ASP LEU ALA LEU TYR PHE GLY          
SEQRES  17 A  362  ASN ARG LYS GLN LEU GLU GLU MET TYR GLN THR GLY SER          
SEQRES  18 A  362  LEU ASN LEU HIS ASN GLN SER HIS ARG ASP ARG VAL ILE          
SEQRES  19 A  362  GLY LEU MET MET THR ALA CYS ASP LEU CYS SER VAL THR          
SEQRES  20 A  362  LYS LEU TRP PRO VAL THR LYS LEU THR ALA ASN ASP ILE          
SEQRES  21 A  362  TYR ALA GLU PHE TRP ALA GLU GLY ASP GLU MET LYS LYS          
SEQRES  22 A  362  LEU GLY ILE GLN PRO ILE PRO MET MET ASP ARG ASP LYS          
SEQRES  23 A  362  ARG ASP GLU VAL PRO GLN GLY GLN LEU GLY PHE TYR ASN          
SEQRES  24 A  362  ALA VAL ALA ILE PRO CYS TYR THR THR LEU THR GLN ILE          
SEQRES  25 A  362  LEU PRO PRO THR GLU PRO LEU LEU LYS ALA CYS ARG ASP          
SEQRES  26 A  362  ASN LEU ASN GLN TRP GLU LYS VAL ILE ARG GLY GLU GLU          
SEQRES  27 A  362  THR ALA MET TRP ILE SER GLY PRO ALA THR SER LYS SER          
SEQRES  28 A  362  THR SER GLU LYS PRO THR ARG LYS VAL ASP ASP                  
HET     ZN  A1001       1                                                       
HET     MG  A1002       1                                                       
HET    227  A 999      34                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     227 6,7-DIMETHOXY-4-{8-[(4-METHYLPIPERAZIN-1-YL)SULFONYL]-           
HETNAM   2 227  3,4-DIHYDROISOQUINOLIN-2(1H)-YL}QUINAZOLINE                     
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  227    C24 H29 N5 O4 S                                              
FORMUL   5  HOH   *312(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  CYS A  488  1                                  14    
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  LEU A  595  1                                  17    
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  LYS A  695  1                                  25    
HELIX   15  15 ILE A  701  ASP A  710  5                                  10    
HELIX   16  16 GLU A  711  VAL A  723  1                                  13    
HELIX   17  17 VAL A  723  LEU A  735  1                                  13    
HELIX   18  18 THR A  738  ARG A  757  1                                  20    
LINK        ZN    ZN A1001                 OD1 ASP A 664     1555   1555  2.17  
LINK        ZN    ZN A1001                 NE2 HIS A 519     1555   1555  1.96  
LINK        ZN    ZN A1001                 NE2 HIS A 553     1555   1555  2.14  
LINK        ZN    ZN A1001                 OD2 ASP A 554     1555   1555  2.05  
LINK        ZN    ZN A1001                 O   HOH A 308     1555   1555  1.72  
LINK        MG    MG A1002                 O   HOH A 126     1555   1555  2.78  
LINK        MG    MG A1002                 O   HOH A 159     1555   1555  2.36  
LINK        MG    MG A1002                 O   HOH A 260     1555   1555  1.97  
LINK        MG    MG A1002                 O   HOH A 308     1555   1555  2.42  
LINK        MG    MG A1002                 OD1 ASP A 554     1555   1555  1.93  
SITE     1 AC1  5 HOH A 308  HIS A 519  HIS A 553  ASP A 554                    
SITE     2 AC1  5 ASP A 664                                                     
SITE     1 AC2  5 HOH A 126  HOH A 159  HOH A 260  HOH A 308                    
SITE     2 AC2  5 ASP A 554                                                     
SITE     1 AC3 13 HOH A  34  HOH A  39  HOH A  78  HOH A 186                    
SITE     2 AC3 13 LEU A 625  PHE A 629  VAL A 668  TYR A 683                    
SITE     3 AC3 13 PHE A 686  MET A 703  GLN A 716  PHE A 719                    
SITE     4 AC3 13 VAL A 723                                                     
CRYST1  120.622  120.622   82.143  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      0.008290  0.004786  0.000000        0.00000                         
SCALE2      0.000000  0.009573  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012174        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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