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Database: PDB
Entry: 6CYC
LinkDB: 6CYC
Original site: 6CYC 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           05-APR-18   6CYC              
TITLE     PDE2 IN COMPLEX WITH COMPOUND 5                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CGMP-DEPENDENT 3',5'-CYCLIC PHOSPHODIESTERASE;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CYCLIC GMP-STIMULATED PHOSPHODIESTERASE,CGSPDE;             
COMPND   5 EC: 3.1.4.17;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PDE2A;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    PDE2, INHIBITION, STRUCTURE-GUIDED DESIGN, HYDROLASE-HYDROLASE        
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LU                                                                  
REVDAT   1   19-SEP-18 6CYC    0                                                
JRNL        AUTH   S.J.STACHEL,R.BERGER,A.B.NOMLAND,A.T.GINNETTI,D.V.PAONE,     
JRNL        AUTH 2 D.WANG,V.PURI,H.LANGE,J.DROTT,J.LU,J.MARCUS,M.P.DWYER,       
JRNL        AUTH 3 S.SUON,J.M.USLANER,S.M.SMITH                                 
JRNL        TITL   STRUCTURE-GUIDED DESIGN AND PROCOGNITIVE ASSESSMENT OF A     
JRNL        TITL 2 POTENT AND SELECTIVE PHOSPHODIESTERASE 2A INHIBITOR.         
JRNL        REF    ACS MED CHEM LETT             V.   9   815 2018              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   30128073                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.8B00214                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.54 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.17                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 105149                         
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)  : 0.185                          
REMARK   3   FREE R VALUE                      : 0.205                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 5255                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.54                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.58                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.52                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 7468                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1997                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 7053                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1985                   
REMARK   3   BIN FREE R VALUE                        : 0.2200                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.56                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 415                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5540                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 98                                      
REMARK   3   SOLVENT ATOMS            : 400                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.78                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.60230                                              
REMARK   3    B22 (A**2) : -1.27420                                             
REMARK   3    B33 (A**2) : -3.32800                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.200               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.080               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.077               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.078               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.076               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5838   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7893   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2022   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 135    ; 8.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 898    ; 8.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5838   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 751    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7454   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.96                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.58                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.25                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6CYC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000233719.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
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          : AUTOPROC                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 105238                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.540                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.170                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.68000                            
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: NULL                         
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG8000, 0.1M HEPES PH7.5, 1MM       
REMARK 280  TCEP, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
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 -1.000000  0.000000  0.000000       36.12500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.82500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.20500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.82500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.12500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.20500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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   547                                                      
REMARK 465     HIS A   548                                                      
REMARK 465     HIS A   549                                                      
REMARK 465     HIS A   550                                                      
REMARK 465     HIS A   551                                                      
REMARK 465     HIS A   552                                                      
REMARK 465     HIS A   553                                                      
REMARK 465     GLU A   554                                                      
REMARK 465     ASN A   555                                                      
REMARK 465     LEU A   556                                                      
REMARK 465     TYR A   557                                                      
REMARK 465     PHE A   558                                                      
REMARK 465     GLN A   559                                                      
REMARK 465     GLY A   560                                                      
REMARK 465     GLU A   561                                                      
REMARK 465     LEU A   562                                                      
REMARK 465     SER A   563                                                      
REMARK 465     THR A   564                                                      
REMARK 465     ASP A   573                                                      
REMARK 465     ASP A   574                                                      
REMARK 465     ASP A   575                                                      
REMARK 465     ASP A   576                                                      
REMARK 465     LYS A   577                                                      
REMARK 465     SER A   578                                                      
REMARK 465     ASP A   579                                                      
REMARK 465     ASP A   580                                                      
REMARK 465     GLU A   581                                                      
REMARK 465     ASP A   917                                                      
REMARK 465     GLU A   918                                                      
REMARK 465     GLU A   919                                                      
REMARK 465     MET B   547                                                      
REMARK 465     HIS B   548                                                      
REMARK 465     HIS B   549                                                      
REMARK 465     HIS B   550                                                      
REMARK 465     HIS B   551                                                      
REMARK 465     HIS B   552                                                      
REMARK 465     HIS B   553                                                      
REMARK 465     GLU B   554                                                      
REMARK 465     ASN B   555                                                      
REMARK 465     LEU B   556                                                      
REMARK 465     TYR B   557                                                      
REMARK 465     PHE B   558                                                      
REMARK 465     GLN B   559                                                      
REMARK 465     GLY B   560                                                      
REMARK 465     GLU B   561                                                      
REMARK 465     ASP B   574                                                      
REMARK 465     ASP B   575                                                      
REMARK 465     ASP B   576                                                      
REMARK 465     LYS B   577                                                      
REMARK 465     SER B   578                                                      
REMARK 465     ASP B   579                                                      
REMARK 465     ASP B   580                                                      
REMARK 465     ASP B   917                                                      
REMARK 465     GLU B   918                                                      
REMARK 465     GLU B   919                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 568    CG   CD   CE   NZ                                   
REMARK 470     LYS A 584    CG   CD   CE   NZ                                   
REMARK 470     LEU A 586    CG   CD1  CD2                                       
REMARK 470     HIS A 587    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP A 588    CG   OD1  OD2                                       
REMARK 470     LYS A 648    CG   CD   CE   NZ                                   
REMARK 470     HIS A 741    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 751    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 752    CG   CD   CE   NZ                                   
REMARK 470     LYS A 778    CG   CD   CE   NZ                                   
REMARK 470     LYS A 782    CG   CD   CE   NZ                                   
REMARK 470     ARG A 790    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 793    CG   CD   CE   NZ                                   
REMARK 470     LYS A 897    CG   CD   CE   NZ                                   
REMARK 470     HIS A 900    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 901    CG   CD   CE   NZ                                   
REMARK 470     LEU B 562    CG   CD1  CD2                                       
REMARK 470     GLU B 581    CG   CD   OE1  OE2                                  
REMARK 470     THR B 583    OG1  CG2                                            
REMARK 470     LYS B 584    CG   CD   CE   NZ                                   
REMARK 470     LYS B 778    CG   CD   CE   NZ                                   
REMARK 470     LYS B 782    CG   CD   CE   NZ                                   
REMARK 470     LYS B 793    CG   CD   CE   NZ                                   
REMARK 470     ARG B 820    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 843    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 857    CG   CD   OE1  OE2                                  
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    GLU A 676       65.71   -100.38                                   
REMARK 500    ILE A 866      -63.61   -105.42                                   
REMARK 500    ASN A 911       14.93     57.65                                   
REMARK 500    ILE B 866      -59.81   -123.14                                   
REMARK 500    LYS B 901       41.26   -153.91                                   
REMARK 500    THR B 903       41.29   -109.00                                   
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 HIS A 660   NE2                                                    
REMARK 620 2 HIS A 696   NE2 101.6                                              
REMARK 620 3 ASP A 697   OD2  91.2  87.1                                        
REMARK 620 4 ASP A 808   OD1  97.9  91.1 170.9                                  
REMARK 620 5 HOH A1101   O   161.7  95.8  84.3  87.0                            
REMARK 620 6 HOH A1192   O    93.3 164.9  94.9  84.6  69.5                      
REMARK 620 N                    1     2     3     4     5                       
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 ASP A 697   OD1                                                    
REMARK 620 2 HOH A1104   O    82.0                                              
REMARK 620 3 HOH A1142   O   169.9  89.5                                        
REMARK 620 4 HOH A1156   O    89.2  93.0  85.8                                  
REMARK 620 5 HOH A1218   O    97.5 178.6  91.1  88.3                            
REMARK 620 6 HOH A1101   O    95.4  94.9  90.7 171.3  83.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 660   NE2                                                    
REMARK 620 2 HIS B 696   NE2 102.8                                              
REMARK 620 3 ASP B 697   OD2  91.8  86.8                                        
REMARK 620 4 ASP B 808   OD1  97.6  92.3 170.5                                  
REMARK 620 5 HOH B1110   O   162.2  94.5  85.1  85.6                            
REMARK 620 6 HOH B1206   O    94.4 162.8  93.1  85.0  68.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1002  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 697   OD1                                                    
REMARK 620 2 HOH B1110   O    97.7                                              
REMARK 620 3 HOH B1133   O   168.9  90.0                                        
REMARK 620 4 HOH B1269   O    99.6  84.3  89.0                                  
REMARK 620 5 HOH B1134   O    88.6 169.3  85.0  86.1                            
REMARK 620 6 HOH B1104   O    84.3  95.4  87.1 176.0  93.8                      
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 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 FKJ A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FKJ B 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1008                
DBREF  6CYC A  578   919  UNP    O00408   PDE2A_HUMAN    322    663             
DBREF  6CYC B  578   919  UNP    O00408   PDE2A_HUMAN    322    663             
SEQADV 6CYC MET A  547  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC HIS A  548  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC HIS A  549  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC HIS A  550  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC HIS A  551  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC HIS A  552  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC HIS A  553  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC GLU A  554  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC ASN A  555  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC LEU A  556  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC TYR A  557  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC PHE A  558  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC GLN A  559  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC GLY A  560  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC GLU A  561  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC LEU A  562  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC SER A  563  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC THR A  564  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC SER A  565  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC LEU A  566  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC TYR A  567  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC LYS A  568  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC LYS A  569  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC ALA A  570  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC GLY A  571  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC PHE A  572  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC ASP A  573  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC ASP A  574  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC ASP A  575  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC ASP A  576  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC LYS A  577  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC MET B  547  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC HIS B  548  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC HIS B  549  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC HIS B  550  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC HIS B  551  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC HIS B  552  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC HIS B  553  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC GLU B  554  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC ASN B  555  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC LEU B  556  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC TYR B  557  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC PHE B  558  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC GLN B  559  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC GLY B  560  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC GLU B  561  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC LEU B  562  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC SER B  563  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC THR B  564  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC SER B  565  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC LEU B  566  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC TYR B  567  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC LYS B  568  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC LYS B  569  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC ALA B  570  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC GLY B  571  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC PHE B  572  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC ASP B  573  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC ASP B  574  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC ASP B  575  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC ASP B  576  UNP  O00408              EXPRESSION TAG                 
SEQADV 6CYC LYS B  577  UNP  O00408              EXPRESSION TAG                 
SEQRES   1 A  373  MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN          
SEQRES   2 A  373  GLY GLU LEU SER THR SER LEU TYR LYS LYS ALA GLY PHE          
SEQRES   3 A  373  ASP ASP ASP ASP LYS SER ASP ASP GLU TYR THR LYS LEU          
SEQRES   4 A  373  LEU HIS ASP GLY ILE GLN PRO VAL ALA ALA ILE ASP SER          
SEQRES   5 A  373  ASN PHE ALA SER PHE THR TYR THR PRO ARG SER LEU PRO          
SEQRES   6 A  373  GLU ASP ASP THR SER MET ALA ILE LEU SER MET LEU GLN          
SEQRES   7 A  373  ASP MET ASN PHE ILE ASN ASN TYR LYS ILE ASP CYS PRO          
SEQRES   8 A  373  THR LEU ALA ARG PHE CYS LEU MET VAL LYS LYS GLY TYR          
SEQRES   9 A  373  ARG ASP PRO PRO TYR HIS ASN TRP MET HIS ALA PHE SER          
SEQRES  10 A  373  VAL SER HIS PHE CYS TYR LEU LEU TYR LYS ASN LEU GLU          
SEQRES  11 A  373  LEU THR ASN TYR LEU GLU ASP ILE GLU ILE PHE ALA LEU          
SEQRES  12 A  373  PHE ILE SER CYS MET CYS HIS ASP LEU ASP HIS ARG GLY          
SEQRES  13 A  373  THR ASN ASN SER PHE GLN VAL ALA SER LYS SER VAL LEU          
SEQRES  14 A  373  ALA ALA LEU TYR SER SER GLU GLY SER VAL MET GLU ARG          
SEQRES  15 A  373  HIS HIS PHE ALA GLN ALA ILE ALA ILE LEU ASN THR HIS          
SEQRES  16 A  373  GLY CYS ASN ILE PHE ASP HIS PHE SER ARG LYS ASP TYR          
SEQRES  17 A  373  GLN ARG MET LEU ASP LEU MET ARG ASP ILE ILE LEU ALA          
SEQRES  18 A  373  THR ASP LEU ALA HIS HIS LEU ARG ILE PHE LYS ASP LEU          
SEQRES  19 A  373  GLN LYS MET ALA GLU VAL GLY TYR ASP ARG ASN ASN LYS          
SEQRES  20 A  373  GLN HIS HIS ARG LEU LEU LEU CYS LEU LEU MET THR SER          
SEQRES  21 A  373  CYS ASP LEU SER ASP GLN THR LYS GLY TRP LYS THR THR          
SEQRES  22 A  373  ARG LYS ILE ALA GLU LEU ILE TYR LYS GLU PHE PHE SER          
SEQRES  23 A  373  GLN GLY ASP LEU GLU LYS ALA MET GLY ASN ARG PRO MET          
SEQRES  24 A  373  GLU MET MET ASP ARG GLU LYS ALA TYR ILE PRO GLU LEU          
SEQRES  25 A  373  GLN ILE SER PHE MET GLU HIS ILE ALA MET PRO ILE TYR          
SEQRES  26 A  373  LYS LEU LEU GLN ASP LEU PHE PRO LYS ALA ALA GLU LEU          
SEQRES  27 A  373  TYR GLU ARG VAL ALA SER ASN ARG GLU HIS TRP THR LYS          
SEQRES  28 A  373  VAL SER HIS LYS PHE THR ILE ARG GLY LEU PRO SER ASN          
SEQRES  29 A  373  ASN SER LEU ASP PHE LEU ASP GLU GLU                          
SEQRES   1 B  373  MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN          
SEQRES   2 B  373  GLY GLU LEU SER THR SER LEU TYR LYS LYS ALA GLY PHE          
SEQRES   3 B  373  ASP ASP ASP ASP LYS SER ASP ASP GLU TYR THR LYS LEU          
SEQRES   4 B  373  LEU HIS ASP GLY ILE GLN PRO VAL ALA ALA ILE ASP SER          
SEQRES   5 B  373  ASN PHE ALA SER PHE THR TYR THR PRO ARG SER LEU PRO          
SEQRES   6 B  373  GLU ASP ASP THR SER MET ALA ILE LEU SER MET LEU GLN          
SEQRES   7 B  373  ASP MET ASN PHE ILE ASN ASN TYR LYS ILE ASP CYS PRO          
SEQRES   8 B  373  THR LEU ALA ARG PHE CYS LEU MET VAL LYS LYS GLY TYR          
SEQRES   9 B  373  ARG ASP PRO PRO TYR HIS ASN TRP MET HIS ALA PHE SER          
SEQRES  10 B  373  VAL SER HIS PHE CYS TYR LEU LEU TYR LYS ASN LEU GLU          
SEQRES  11 B  373  LEU THR ASN TYR LEU GLU ASP ILE GLU ILE PHE ALA LEU          
SEQRES  12 B  373  PHE ILE SER CYS MET CYS HIS ASP LEU ASP HIS ARG GLY          
SEQRES  13 B  373  THR ASN ASN SER PHE GLN VAL ALA SER LYS SER VAL LEU          
SEQRES  14 B  373  ALA ALA LEU TYR SER SER GLU GLY SER VAL MET GLU ARG          
SEQRES  15 B  373  HIS HIS PHE ALA GLN ALA ILE ALA ILE LEU ASN THR HIS          
SEQRES  16 B  373  GLY CYS ASN ILE PHE ASP HIS PHE SER ARG LYS ASP TYR          
SEQRES  17 B  373  GLN ARG MET LEU ASP LEU MET ARG ASP ILE ILE LEU ALA          
SEQRES  18 B  373  THR ASP LEU ALA HIS HIS LEU ARG ILE PHE LYS ASP LEU          
SEQRES  19 B  373  GLN LYS MET ALA GLU VAL GLY TYR ASP ARG ASN ASN LYS          
SEQRES  20 B  373  GLN HIS HIS ARG LEU LEU LEU CYS LEU LEU MET THR SER          
SEQRES  21 B  373  CYS ASP LEU SER ASP GLN THR LYS GLY TRP LYS THR THR          
SEQRES  22 B  373  ARG LYS ILE ALA GLU LEU ILE TYR LYS GLU PHE PHE SER          
SEQRES  23 B  373  GLN GLY ASP LEU GLU LYS ALA MET GLY ASN ARG PRO MET          
SEQRES  24 B  373  GLU MET MET ASP ARG GLU LYS ALA TYR ILE PRO GLU LEU          
SEQRES  25 B  373  GLN ILE SER PHE MET GLU HIS ILE ALA MET PRO ILE TYR          
SEQRES  26 B  373  LYS LEU LEU GLN ASP LEU PHE PRO LYS ALA ALA GLU LEU          
SEQRES  27 B  373  TYR GLU ARG VAL ALA SER ASN ARG GLU HIS TRP THR LYS          
SEQRES  28 B  373  VAL SER HIS LYS PHE THR ILE ARG GLY LEU PRO SER ASN          
SEQRES  29 B  373  ASN SER LEU ASP PHE LEU ASP GLU GLU                          
HET     ZN  A1001       1                                                       
HET     MG  A1002       1                                                       
HET    FKJ  A1003      25                                                       
HET    EDO  A1004       4                                                       
HET    EDO  A1005       4                                                       
HET    EDO  A1006       4                                                       
HET    EDO  A1007       4                                                       
HET    EDO  A1008       4                                                       
HET    EDO  A1009       4                                                       
HET     ZN  B1001       1                                                       
HET     MG  B1002       1                                                       
HET    FKJ  B1003      25                                                       
HET    EDO  B1004       4                                                       
HET    EDO  B1005       4                                                       
HET    EDO  B1006       4                                                       
HET    EDO  B1007       4                                                       
HET    EDO  B1008       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     FKJ 3-(HYDROXYMETHYL)-1-{(1S)-1-[4-(TRIFLUOROMETHYL)                 
HETNAM   2 FKJ  PHENYL]ETHYL}-1H-PYRAZOLO[3,4-D]PYRIMIDINE-4,6(5H,7H)-          
HETNAM   3 FKJ  DIONE                                                           
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  FKJ    2(C15 H13 F3 N4 O3)                                          
FORMUL   6  EDO    11(C2 H6 O2)                                                 
FORMUL  20  HOH   *400(H2 O)                                                    
HELIX    1 AA1 THR A  583  GLY A  589  1                                   7    
HELIX    2 AA2 PRO A  592  ASP A  597  1                                   6    
HELIX    3 AA3 THR A  606  LEU A  610  5                                   5    
HELIX    4 AA4 PRO A  611  ASP A  613  5                                   3    
HELIX    5 AA5 ASP A  614  MET A  626  1                                  13    
HELIX    6 AA6 ASN A  627  TYR A  632  1                                   6    
HELIX    7 AA7 ASP A  635  GLY A  649  1                                  15    
HELIX    8 AA8 ASN A  657  LEU A  675  1                                  19    
HELIX    9 AA9 GLU A  676  TYR A  680  5                                   5    
HELIX   10 AB1 GLU A  682  HIS A  696  1                                  15    
HELIX   11 AB2 ASN A  704  SER A  711  1                                   8    
HELIX   12 AB3 SER A  713  SER A  720  1                                   8    
HELIX   13 AB4 SER A  721  GLY A  723  5                                   3    
HELIX   14 AB5 SER A  724  ASN A  739  1                                  16    
HELIX   15 AB6 SER A  750  ALA A  767  1                                  18    
HELIX   16 AB7 ASP A  769  GLY A  787  1                                  19    
HELIX   17 AB8 ASN A  792  LEU A  809  1                                  18    
HELIX   18 AB9 SER A  810  LYS A  814  5                                   5    
HELIX   19 AC1 GLY A  815  MET A  840  1                                  26    
HELIX   20 AC2 MET A  845  ASP A  849  5                                   5    
HELIX   21 AC3 TYR A  854  ILE A  866  1                                  13    
HELIX   22 AC4 ILE A  866  PHE A  878  1                                  13    
HELIX   23 AC5 ALA A  881  SER A  899  1                                  19    
HELIX   24 AC6 LEU B  562  LEU B  566  5                                   5    
HELIX   25 AC7 TYR B  582  HIS B  587  1                                   6    
HELIX   26 AC8 PRO B  592  ASP B  597  1                                   6    
HELIX   27 AC9 THR B  606  LEU B  610  5                                   5    
HELIX   28 AD1 PRO B  611  ASP B  613  5                                   3    
HELIX   29 AD2 ASP B  614  MET B  626  1                                  13    
HELIX   30 AD3 ASN B  627  TYR B  632  1                                   6    
HELIX   31 AD4 ASP B  635  GLY B  649  1                                  15    
HELIX   32 AD5 ASN B  657  GLU B  676  1                                  20    
HELIX   33 AD6 LEU B  677  TYR B  680  5                                   4    
HELIX   34 AD7 GLU B  682  HIS B  696  1                                  15    
HELIX   35 AD8 ASN B  704  SER B  711  1                                   8    
HELIX   36 AD9 SER B  713  SER B  720  1                                   8    
HELIX   37 AE1 SER B  721  GLY B  723  5                                   3    
HELIX   38 AE2 SER B  724  ASN B  739  1                                  16    
HELIX   39 AE3 SER B  750  ALA B  767  1                                  18    
HELIX   40 AE4 ASP B  769  GLY B  787  1                                  19    
HELIX   41 AE5 ASN B  792  LEU B  809  1                                  18    
HELIX   42 AE6 SER B  810  LYS B  814  5                                   5    
HELIX   43 AE7 GLY B  815  MET B  840  1                                  26    
HELIX   44 AE8 MET B  845  ASP B  849  5                                   5    
HELIX   45 AE9 TYR B  854  ILE B  866  1                                  13    
HELIX   46 AF1 ILE B  866  PHE B  878  1                                  13    
HELIX   47 AF2 ALA B  881  SER B  899  1                                  19    
LINK         NE2 HIS A 660                ZN    ZN A1001     1555   1555  2.06  
LINK         NE2 HIS A 696                ZN    ZN A1001     1555   1555  2.08  
LINK         OD1 ASP A 697                MG    MG A1002     1555   1555  2.07  
LINK         OD2 ASP A 697                ZN    ZN A1001     1555   1555  2.07  
LINK         OD1 ASP A 808                ZN    ZN A1001     1555   1555  2.06  
LINK         NE2 HIS B 660                ZN    ZN B1001     1555   1555  2.05  
LINK         NE2 HIS B 696                ZN    ZN B1001     1555   1555  2.08  
LINK         OD1 ASP B 697                MG    MG B1002     1555   1555  2.07  
LINK         OD2 ASP B 697                ZN    ZN B1001     1555   1555  2.05  
LINK         OD1 ASP B 808                ZN    ZN B1001     1555   1555  2.13  
LINK        ZN    ZN A1001                 O   HOH A1101     1555   1555  2.52  
LINK        ZN    ZN A1001                 O   HOH A1192     1555   1555  2.20  
LINK        MG    MG A1002                 O   HOH A1104     1555   1555  2.10  
LINK        MG    MG A1002                 O   HOH A1142     1555   1555  2.06  
LINK        MG    MG A1002                 O   HOH A1156     1555   1555  2.11  
LINK        MG    MG A1002                 O   HOH A1218     1555   1555  2.11  
LINK        MG    MG A1002                 O   HOH A1101     1555   1555  2.11  
LINK        ZN    ZN B1001                 O   HOH B1110     1555   1555  2.60  
LINK        ZN    ZN B1001                 O   HOH B1206     1555   1555  2.20  
LINK        MG    MG B1002                 O   HOH B1110     1555   1555  2.07  
LINK        MG    MG B1002                 O   HOH B1133     1555   1555  2.13  
LINK        MG    MG B1002                 O   HOH B1269     1555   1555  2.08  
LINK        MG    MG B1002                 O   HOH B1134     1555   1555  2.16  
LINK        MG    MG B1002                 O   HOH B1104     1555   1555  2.04  
SITE     1 AC1  6 HIS A 660  HIS A 696  ASP A 697  ASP A 808                    
SITE     2 AC1  6 HOH A1101  HOH A1192                                          
SITE     1 AC2  6 ASP A 697  HOH A1101  HOH A1104  HOH A1142                    
SITE     2 AC2  6 HOH A1156  HOH A1218                                          
SITE     1 AC3 15 TYR A 655  HIS A 656  THR A 768  LEU A 770                    
SITE     2 AC3 15 THR A 805  ASP A 808  LEU A 809  GLN A 812                    
SITE     3 AC3 15 ILE A 826  GLN A 859  PHE A 862  EDO A1004                    
SITE     4 AC3 15 HOH A1119  HOH A1121  HOH A1181                               
SITE     1 AC4  6 PHE A 830  PHE A 862  FKJ A1003  EDO A1005                    
SITE     2 AC4  6 EDO A1006  HOH A1176                                          
SITE     1 AC5  6 ASN A 704  PHE A 830  EDO A1004  EDO A1006                    
SITE     2 AC5  6 HOH A1113  HOH A1219                                          
SITE     1 AC6  5 ASP A 769  LEU A 770  EDO A1004  EDO A1005                    
SITE     2 AC6  5 HOH A1161                                                     
SITE     1 AC7  8 SER A 721  GLU A 722  HOH A1114  HOH A1228                    
SITE     2 AC7  8 HIS B 772  ARG B 797  LEU B 798  CYS B 801                    
SITE     1 AC8  5 LYS A 569  PHE A 572  GLN A 733  HOH A1105                    
SITE     2 AC8  5 HOH A1171                                                     
SITE     1 AC9  4 ILE A 735  ASN A 739  TYR A 754  ARG B 751                    
SITE     1 AD1  6 HIS B 660  HIS B 696  ASP B 697  ASP B 808                    
SITE     2 AD1  6 HOH B1110  HOH B1206                                          
SITE     1 AD2  6 ASP B 697  HOH B1104  HOH B1110  HOH B1133                    
SITE     2 AD2  6 HOH B1134  HOH B1269                                          
SITE     1 AD3 15 TYR B 655  HIS B 656  THR B 768  LEU B 770                    
SITE     2 AD3 15 THR B 805  ASP B 808  LEU B 809  GLN B 812                    
SITE     3 AD3 15 ILE B 826  PHE B 862  EDO B1006  HOH B1105                    
SITE     4 AD3 15 HOH B1109  HOH B1122  HOH B1184                               
SITE     1 AD4  4 LEU B 770  EDO B1005  HOH B1107  HOH B1245                    
SITE     1 AD5  6 ASN B 704  PHE B 830  MET B 848  EDO B1004                    
SITE     2 AD5  6 EDO B1006  HOH B1210                                          
SITE     1 AD6  5 PHE B 830  ILE B 866  FKJ B1003  EDO B1005                    
SITE     2 AD6  5 HOH B1154                                                     
SITE     1 AD7  6 LYS A 569  ASN B 599  THR B 604  TYR B 605                    
SITE     2 AD7  6 THR B 606  HOH B1135                                          
SITE     1 AD8  3 PHE B 777  HIS B 865  HOH B1112                               
CRYST1   72.250   96.410  101.650  90.00  90.00  90.00 P 21 21 21    8          
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      0.013841  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010372  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009838        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system