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Database: PDB
Entry: 6NFO
LinkDB: 6NFO
Original site: 6NFO 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       20-DEC-18   6NFO              
TITLE     CYCLIC GMP-AMP SYNTHASE IN COMPLEX WITH COMPOUND 20 INHIBITOR: 7-     
TITLE    2 HYDROXY-N-[(2S)-1-HYDROXYPROPAN-2-YL]-5-PHENYLPYRAZOLO[1,5-          
TITLE    3 A]PYRIMIDINE-3-CARBOXAMIDE                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 161-522;                                      
COMPND   5 SYNONYM: H-CGAS,2'3'-CGAMP SYNTHASE,MAB-21 DOMAIN-CONTAINING PROTEIN 
COMPND   6 1;                                                                   
COMPND   7 EC: 2.7.7.86;                                                        
COMPND   8 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: CGAS, C6ORF150, MB21D1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CGAS, STING, CGAMP, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR    
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.HALL                                                                
REVDAT   1   23-JAN-19 6NFO    0                                                
SPRSDE     23-JAN-19 6NFO      5V8J                                             
JRNL        AUTH   J.HALL                                                       
JRNL        TITL   DISCOVERY OF A HIGH AFFINITY INHIBITOR OF CGAS               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.93 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) : 2.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 83.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 18429                          
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)  : 0.211                          
REMARK   3   R VALUE            (WORKING SET)  : 0.210                          
REMARK   3   FREE R VALUE                      : 0.231                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.110                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 942                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.020                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.93                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.11                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 100.0                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2949                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2630                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2803                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2630                   
REMARK   3   BIN FREE R VALUE                        : 0.2800                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.95                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 146                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5372                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 27                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 74.48                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.12690                                             
REMARK   3    B22 (A**2) : -3.32730                                             
REMARK   3    B33 (A**2) : 9.45420                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -9.94700                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.400               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.357               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.918                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5563   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7551   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1857   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 122    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 810    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5563   ; 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   : 738    ; 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   : 6077   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.15                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.50                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.55                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -30.9932   12.1787  -21.3917           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0193 T22:   -0.1117                                    
REMARK   3     T33:   -0.1553 T12:   -0.2205                                    
REMARK   3     T13:   -0.0121 T23:    0.0124                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9810 L22:    1.7381                                    
REMARK   3     L33:    1.8473 L12:   -0.3397                                    
REMARK   3     L13:   -0.0418 L23:   -0.2839                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0496 S12:   -0.0521 S13:   -0.0606                     
REMARK   3     S21:    0.0289 S22:   -0.0612 S23:   -0.3211                     
REMARK   3     S31:   -0.0594 S32:    0.3529 S33:    0.0116                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -30.8626    2.4082   21.3637           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0485 T22:   -0.1322                                    
REMARK   3     T33:   -0.1118 T12:    0.2037                                    
REMARK   3     T13:   -0.0254 T23:   -0.0170                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.3130 L22:    2.2642                                    
REMARK   3     L33:    1.7970 L12:    0.0179                                    
REMARK   3     L13:   -0.2555 L23:    0.1095                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0922 S12:   -0.0205 S13:    0.1378                     
REMARK   3     S21:    0.1553 S22:    0.1543 S23:   -0.4742                     
REMARK   3     S31:    0.0875 S32:    0.3766 S33:   -0.0621                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6NFO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-DEC-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000238691.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-16                          
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                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : AIMLESS                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18440                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.930                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 83.970                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.93                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
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   (%): 50.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CONCENTRATED TO 6 MG/ML,     
REMARK 280  AND THEN MIXED AT A 2:1 RATIO WITH PEG 3350 (18-20% V/V), 0.2 M     
REMARK 280  AMMONIUM CITRATE (PH 7) IN A SITTING DROP WELL AT 277 K.            
REMARK 280  CRYOPROTECTANT WAS MADE USING MOTHER LIQUOR AT A FINAL              
REMARK 280  CONCENTRATION OF 23% PEG 3350, VAPOR DIFFUSION, SITTING DROP        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      109.39800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.99950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      109.39800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.99950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     LYS A   254                                                      
REMARK 465     ARG A   255                                                      
REMARK 465     ASN A   256                                                      
REMARK 465     PRO A   257                                                      
REMARK 465     LYS A   258                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     ARG A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     SER A   305                                                      
REMARK 465     LYS A   365                                                      
REMARK 465     GLU A   366                                                      
REMARK 465     GLY A   367                                                      
REMARK 465     GLU A   521                                                      
REMARK 465     PHE A   522                                                      
REMARK 465     ARG B   255                                                      
REMARK 465     GLU B   366                                                      
REMARK 465     GLY B   367                                                      
REMARK 465     ASN B   368                                                      
REMARK 465     GLU B   521                                                      
REMARK 465     PHE B   522                                                      
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     ARG A 176    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 178    CG   OD1  OD2                                       
REMARK 470     ILE A 179    CG1  CG2  CD1                                       
REMARK 470     MET A 185    CG   SD   CE                                        
REMARK 470     LYS A 187    CG   CD   CE   NZ                                   
REMARK 470     HIS A 192    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 195    CG   CD1  CD2                                       
REMARK 470     ARG A 196    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 213    OG                                                  
REMARK 470     TYR A 214    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR A 215    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 216    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 217    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL A 218    CG1  CG2                                            
REMARK 470     LYS A 219    CG   CD   CE   NZ                                   
REMARK 470     ILE A 220    CG1  CG2  CD1                                       
REMARK 470     GLU A 240    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 244    CG   OD1  ND2                                       
REMARK 470     LYS A 252    CG   CD   CE   NZ                                   
REMARK 470     LEU A 266    CG   CD1  CD2                                       
REMARK 470     GLU A 267    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 269    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 275    CG   CD   CE   NZ                                   
REMARK 470     LEU A 277    CG   CD1  CD2                                       
REMARK 470     LYS A 279    CG   CD   CE   NZ                                   
REMARK 470     ARG A 281    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 282    CG   CD   CE   NZ                                   
REMARK 470     LYS A 285    CG   CD   CE   NZ                                   
REMARK 470     GLU A 286    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 292    CG   CD   CE   NZ                                   
REMARK 470     ASP A 293    CG   OD1  OD2                                       
REMARK 470     THR A 294    OG1  CG2                                            
REMARK 470     LYS A 299    CG   CD   CE   NZ                                   
REMARK 470     ARG A 300    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 301    CG   CD   CE   NZ                                   
REMARK 470     LYS A 315    CG   CD   CE   NZ                                   
REMARK 470     LYS A 350    CG   CD   CE   NZ                                   
REMARK 470     ASN A 368    CG   OD1  ND2                                       
REMARK 470     GLU A 372    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 373    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 400    CG   CD   CE   NZ                                   
REMARK 470     GLU A 422    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 426    CG   OD1  OD2                                       
REMARK 470     LYS A 428    CG   CD   CE   NZ                                   
REMARK 470     ASP A 431    CG   OD1  OD2                                       
REMARK 470     LYS A 432    CG   CD   CE   NZ                                   
REMARK 470     ARG A 499    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 176    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 185    CG   SD   CE                                        
REMARK 470     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     HIS B 192    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU B 195    CG   CD1  CD2                                       
REMARK 470     ARG B 196    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 197    CG   CD1  CD2                                       
REMARK 470     LYS B 198    CG   CD   CE   NZ                                   
REMARK 470     ARG B 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 211    OG1  CG2                                            
REMARK 470     SER B 213    OG                                                  
REMARK 470     GLU B 216    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 218    CG1  CG2                                            
REMARK 470     LYS B 219    CG   CD   CE   NZ                                   
REMARK 470     ILE B 220    CG1  CG2  CD1                                       
REMARK 470     SER B 221    OG                                                  
REMARK 470     ARG B 236    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 240    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 244    CG   OD1  ND2                                       
REMARK 470     LYS B 252    CG   CD   CE   NZ                                   
REMARK 470     LYS B 254    CG   CD   CE   NZ                                   
REMARK 470     ASN B 256    CG   OD1  ND2                                       
REMARK 470     LYS B 258    CG   CD   CE   NZ                                   
REMARK 470     LEU B 266    CG   CD1  CD2                                       
REMARK 470     GLU B 267    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 269    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 275    CG   CD   CE   NZ                                   
REMARK 470     LEU B 277    CG   CD1  CD2                                       
REMARK 470     LYS B 279    CG   CD   CE   NZ                                   
REMARK 470     ARG B 281    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 282    CG   CD   CE   NZ                                   
REMARK 470     ILE B 284    CG1  CG2  CD1                                       
REMARK 470     LYS B 285    CG   CD   CE   NZ                                   
REMARK 470     GLU B 286    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 287    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 292    CG   CD   CE   NZ                                   
REMARK 470     ASP B 293    CG   OD1  OD2                                       
REMARK 470     THR B 294    OG1  CG2                                            
REMARK 470     LYS B 299    CG   CD   CE   NZ                                   
REMARK 470     ARG B 300    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 301    CG   CD   CE   NZ                                   
REMARK 470     ARG B 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 305    OG                                                  
REMARK 470     GLU B 314    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 315    CG   CD   CE   NZ                                   
REMARK 470     ASP B 319    CG   OD1  OD2                                       
REMARK 470     LYS B 350    CG   CD   CE   NZ                                   
REMARK 470     LYS B 365    CG   CD   CE   NZ                                   
REMARK 470     GLU B 372    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 373    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 400    CG   CD   CE   NZ                                   
REMARK 470     GLU B 418    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 422    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 426    CG   OD1  OD2                                       
REMARK 470     LYS B 428    CG   CD   CE   NZ                                   
REMARK 470     ASP B 431    CG   OD1  OD2                                       
REMARK 470     LYS B 432    CG   CD   CE   NZ                                   
REMARK 470     ARG B 499    CG   CD   NE   CZ   NH1  NH2                        
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    ALA B 307   C   -  N   -  CA  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    SER B 313   N   -  CA  -  C   ANGL. DEV. = -17.1 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    PHE A 203       36.07    -97.99                                   
REMARK 500    ASN A 210       31.37     76.21                                   
REMARK 500    SER A 221       -4.34     66.89                                   
REMARK 500    PRO A 235      -75.96    -60.37                                   
REMARK 500    ARG A 246       -0.82     71.87                                   
REMARK 500    GLU A 267       71.15   -111.59                                   
REMARK 500    ARG A 300      156.38    -49.81                                   
REMARK 500    ALA A 307      -59.77    -26.73                                   
REMARK 500    SER A 313       20.43     46.23                                   
REMARK 500    LYS A 315      -50.53   -131.39                                   
REMARK 500    TRP A 343      -62.30   -108.08                                   
REMARK 500    SER A 345      155.85     94.22                                   
REMARK 500    PRO A 356     -177.88    -67.68                                   
REMARK 500    GLU A 372       41.33    -81.48                                   
REMARK 500    LYS A 428        2.95     84.95                                   
REMARK 500    PHE B 203       35.77    -97.53                                   
REMARK 500    ASN B 210       48.78     71.59                                   
REMARK 500    SER B 221       -5.48     67.13                                   
REMARK 500    ARG B 246       -6.57     74.03                                   
REMARK 500    GLU B 267       70.80   -111.30                                   
REMARK 500    ARG B 300      168.27    -49.04                                   
REMARK 500    ARG B 302      -59.86   -137.64                                   
REMARK 500    SER B 313     -129.12     48.99                                   
REMARK 500    LYS B 315      -43.62   -142.66                                   
REMARK 500    TRP B 343      -62.56   -108.12                                   
REMARK 500    SER B 345      156.35     93.97                                   
REMARK 500    PRO B 356     -177.64    -68.19                                   
REMARK 500    GLU B 372       42.94    -79.10                                   
REMARK 500    LYS B 428       -8.42     85.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 390   NE2                                                    
REMARK 620 2 CYS A 396   SG  116.1                                              
REMARK 620 3 CYS A 397   SG  107.1 119.2                                        
REMARK 620 4 CYS A 404   SG   98.5 105.1 108.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 390   NE2                                                    
REMARK 620 2 CYS B 396   SG  115.5                                              
REMARK 620 3 CYS B 397   SG  108.8 118.5                                        
REMARK 620 4 CYS B 404   SG   98.9 104.2 108.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KKM A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KKM B 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5V8H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5V8N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5V8O   RELATED DB: PDB                                   
DBREF  6NFO A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
DBREF  6NFO B  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
SEQRES   1 A  362  GLY ALA SER LYS LEU ARG ALA VAL LEU GLU LYS LEU LYS          
SEQRES   2 A  362  LEU SER ARG ASP ASP ILE SER THR ALA ALA GLY MET VAL          
SEQRES   3 A  362  LYS GLY VAL VAL ASP HIS LEU LEU LEU ARG LEU LYS CYS          
SEQRES   4 A  362  ASP SER ALA PHE ARG GLY VAL GLY LEU LEU ASN THR GLY          
SEQRES   5 A  362  SER TYR TYR GLU HIS VAL LYS ILE SER ALA PRO ASN GLU          
SEQRES   6 A  362  PHE ASP VAL MET PHE LYS LEU GLU VAL PRO ARG ILE GLN          
SEQRES   7 A  362  LEU GLU GLU TYR SER ASN THR ARG ALA TYR TYR PHE VAL          
SEQRES   8 A  362  LYS PHE LYS ARG ASN PRO LYS GLU ASN PRO LEU SER GLN          
SEQRES   9 A  362  PHE LEU GLU GLY GLU ILE LEU SER ALA SER LYS MET LEU          
SEQRES  10 A  362  SER LYS PHE ARG LYS ILE ILE LYS GLU GLU ILE ASN ASP          
SEQRES  11 A  362  ILE LYS ASP THR ASP VAL ILE MET LYS ARG LYS ARG GLY          
SEQRES  12 A  362  GLY SER PRO ALA VAL THR LEU LEU ILE SER GLU LYS ILE          
SEQRES  13 A  362  SER VAL ASP ILE THR LEU ALA LEU GLU SER LYS SER SER          
SEQRES  14 A  362  TRP PRO ALA SER THR GLN GLU GLY LEU ARG ILE GLN ASN          
SEQRES  15 A  362  TRP LEU SER ALA LYS VAL ARG LYS GLN LEU ARG LEU LYS          
SEQRES  16 A  362  PRO PHE TYR LEU VAL PRO LYS HIS ALA LYS GLU GLY ASN          
SEQRES  17 A  362  GLY PHE GLN GLU GLU THR TRP ARG LEU SER PHE SER HIS          
SEQRES  18 A  362  ILE GLU LYS GLU ILE LEU ASN ASN HIS GLY LYS SER LYS          
SEQRES  19 A  362  THR CYS CYS GLU ASN LYS GLU GLU LYS CYS CYS ARG LYS          
SEQRES  20 A  362  ASP CYS LEU LYS LEU MET LYS TYR LEU LEU GLU GLN LEU          
SEQRES  21 A  362  LYS GLU ARG PHE LYS ASP LYS LYS HIS LEU ASP LYS PHE          
SEQRES  22 A  362  SER SER TYR HIS VAL LYS THR ALA PHE PHE HIS VAL CYS          
SEQRES  23 A  362  THR GLN ASN PRO GLN ASP SER GLN TRP ASP ARG LYS ASP          
SEQRES  24 A  362  LEU GLY LEU CYS PHE ASP ASN CYS VAL THR TYR PHE LEU          
SEQRES  25 A  362  GLN CYS LEU ARG THR GLU LYS LEU GLU ASN TYR PHE ILE          
SEQRES  26 A  362  PRO GLU PHE ASN LEU PHE SER SER ASN LEU ILE ASP LYS          
SEQRES  27 A  362  ARG SER LYS GLU PHE LEU THR LYS GLN ILE GLU TYR GLU          
SEQRES  28 A  362  ARG ASN ASN GLU PHE PRO VAL PHE ASP GLU PHE                  
SEQRES   1 B  362  GLY ALA SER LYS LEU ARG ALA VAL LEU GLU LYS LEU LYS          
SEQRES   2 B  362  LEU SER ARG ASP ASP ILE SER THR ALA ALA GLY MET VAL          
SEQRES   3 B  362  LYS GLY VAL VAL ASP HIS LEU LEU LEU ARG LEU LYS CYS          
SEQRES   4 B  362  ASP SER ALA PHE ARG GLY VAL GLY LEU LEU ASN THR GLY          
SEQRES   5 B  362  SER TYR TYR GLU HIS VAL LYS ILE SER ALA PRO ASN GLU          
SEQRES   6 B  362  PHE ASP VAL MET PHE LYS LEU GLU VAL PRO ARG ILE GLN          
SEQRES   7 B  362  LEU GLU GLU TYR SER ASN THR ARG ALA TYR TYR PHE VAL          
SEQRES   8 B  362  LYS PHE LYS ARG ASN PRO LYS GLU ASN PRO LEU SER GLN          
SEQRES   9 B  362  PHE LEU GLU GLY GLU ILE LEU SER ALA SER LYS MET LEU          
SEQRES  10 B  362  SER LYS PHE ARG LYS ILE ILE LYS GLU GLU ILE ASN ASP          
SEQRES  11 B  362  ILE LYS ASP THR ASP VAL ILE MET LYS ARG LYS ARG GLY          
SEQRES  12 B  362  GLY SER PRO ALA VAL THR LEU LEU ILE SER GLU LYS ILE          
SEQRES  13 B  362  SER VAL ASP ILE THR LEU ALA LEU GLU SER LYS SER SER          
SEQRES  14 B  362  TRP PRO ALA SER THR GLN GLU GLY LEU ARG ILE GLN ASN          
SEQRES  15 B  362  TRP LEU SER ALA LYS VAL ARG LYS GLN LEU ARG LEU LYS          
SEQRES  16 B  362  PRO PHE TYR LEU VAL PRO LYS HIS ALA LYS GLU GLY ASN          
SEQRES  17 B  362  GLY PHE GLN GLU GLU THR TRP ARG LEU SER PHE SER HIS          
SEQRES  18 B  362  ILE GLU LYS GLU ILE LEU ASN ASN HIS GLY LYS SER LYS          
SEQRES  19 B  362  THR CYS CYS GLU ASN LYS GLU GLU LYS CYS CYS ARG LYS          
SEQRES  20 B  362  ASP CYS LEU LYS LEU MET LYS TYR LEU LEU GLU GLN LEU          
SEQRES  21 B  362  LYS GLU ARG PHE LYS ASP LYS LYS HIS LEU ASP LYS PHE          
SEQRES  22 B  362  SER SER TYR HIS VAL LYS THR ALA PHE PHE HIS VAL CYS          
SEQRES  23 B  362  THR GLN ASN PRO GLN ASP SER GLN TRP ASP ARG LYS ASP          
SEQRES  24 B  362  LEU GLY LEU CYS PHE ASP ASN CYS VAL THR TYR PHE LEU          
SEQRES  25 B  362  GLN CYS LEU ARG THR GLU LYS LEU GLU ASN TYR PHE ILE          
SEQRES  26 B  362  PRO GLU PHE ASN LEU PHE SER SER ASN LEU ILE ASP LYS          
SEQRES  27 B  362  ARG SER LYS GLU PHE LEU THR LYS GLN ILE GLU TYR GLU          
SEQRES  28 B  362  ARG ASN ASN GLU PHE PRO VAL PHE ASP GLU PHE                  
HET     ZN  A 601       1                                                       
HET    KKM  A 602      39                                                       
HET     ZN  B 601       1                                                       
HET    KKM  B 602      39                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     KKM 7-HYDROXY-N-[(2S)-1-HYDROXYPROPAN-2-YL]-5-                       
HETNAM   2 KKM  PHENYLPYRAZOLO[1,5-A]PYRIMIDINE-3-CARBOXAMIDE                   
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  KKM    2(C16 H16 N4 O3)                                             
FORMUL   7  HOH   *27(H2 O)                                                     
HELIX    1 AA1 ALA A  162  SER A  175  1                                  14    
HELIX    2 AA2 SER A  175  LYS A  198  1                                  24    
HELIX    3 AA3 LEU A  262  LEU A  266  5                                   5    
HELIX    4 AA4 SER A  272  ILE A  291  1                                  20    
HELIX    5 AA5 PRO A  331  GLN A  335  5                                   5    
HELIX    6 AA6 SER A  345  LEU A  354  1                                  10    
HELIX    7 AA7 PHE A  379  ASN A  389  1                                  11    
HELIX    8 AA8 ASN A  399  LYS A  403  5                                   5    
HELIX    9 AA9 CYS A  405  PHE A  424  1                                  20    
HELIX   10 AB1 HIS A  429  PHE A  433  5                                   5    
HELIX   11 AB2 SER A  434  ASN A  449  1                                  16    
HELIX   12 AB3 GLN A  451  LYS A  458  5                                   8    
HELIX   13 AB4 ASP A  459  GLU A  478  1                                  20    
HELIX   14 AB5 ASP A  497  ASN A  514  1                                  18    
HELIX   15 AB6 ALA B  162  LEU B  174  1                                  13    
HELIX   16 AB7 SER B  175  LYS B  198  1                                  24    
HELIX   17 AB8 LEU B  262  LEU B  266  5                                   5    
HELIX   18 AB9 SER B  272  ILE B  291  1                                  20    
HELIX   19 AC1 PRO B  331  GLN B  335  5                                   5    
HELIX   20 AC2 SER B  345  LEU B  354  1                                  10    
HELIX   21 AC3 PHE B  379  ASN B  389  1                                  11    
HELIX   22 AC4 ASN B  399  LYS B  403  5                                   5    
HELIX   23 AC5 CYS B  405  PHE B  424  1                                  20    
HELIX   24 AC6 LYS B  428  PHE B  433  5                                   6    
HELIX   25 AC7 SER B  434  ASN B  449  1                                  16    
HELIX   26 AC8 GLN B  451  LYS B  458  5                                   8    
HELIX   27 AC9 ASP B  459  GLU B  478  1                                  20    
HELIX   28 AD1 ASP B  497  ASN B  514  1                                  18    
SHEET    1 AA1 7 VAL A 206  LEU A 208  0                                        
SHEET    2 AA1 7 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3 AA1 7 ILE A 316  SER A 326  1  O  ASP A 319   N  VAL A 228           
SHEET    4 AA1 7 PHE A 357  PRO A 361 -1  O  LEU A 359   N  LEU A 324           
SHEET    5 AA1 7 TRP A 375  SER A 378 -1  O  ARG A 376   N  VAL A 360           
SHEET    6 AA1 7 TYR A 248  LYS A 252 -1  N  TYR A 249   O  TRP A 375           
SHEET    7 AA1 7 GLN A 238  GLU A 241 -1  N  GLN A 238   O  LYS A 252           
SHEET    1 AA2 5 VAL A 206  LEU A 208  0                                        
SHEET    2 AA2 5 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3 AA2 5 ILE A 316  SER A 326  1  O  ASP A 319   N  VAL A 228           
SHEET    4 AA2 5 VAL A 308  ILE A 312 -1  N  VAL A 308   O  ILE A 320           
SHEET    5 AA2 5 VAL A 296  LYS A 299 -1  N  LYS A 299   O  THR A 309           
SHEET    1 AA3 7 VAL B 206  LEU B 208  0                                        
SHEET    2 AA3 7 GLU B 225  GLU B 233 -1  O  LYS B 231   N  GLY B 207           
SHEET    3 AA3 7 ILE B 316  SER B 326  1  O  ASP B 319   N  VAL B 228           
SHEET    4 AA3 7 PHE B 357  PRO B 361 -1  O  LEU B 359   N  LEU B 324           
SHEET    5 AA3 7 TRP B 375  SER B 378 -1  O  ARG B 376   N  VAL B 360           
SHEET    6 AA3 7 TYR B 248  PHE B 253 -1  N  TYR B 249   O  TRP B 375           
SHEET    7 AA3 7 ILE B 237  GLU B 241 -1  N  GLN B 238   O  LYS B 252           
SHEET    1 AA4 5 VAL B 206  LEU B 208  0                                        
SHEET    2 AA4 5 GLU B 225  GLU B 233 -1  O  LYS B 231   N  GLY B 207           
SHEET    3 AA4 5 ILE B 316  SER B 326  1  O  ASP B 319   N  VAL B 228           
SHEET    4 AA4 5 VAL B 308  ILE B 312 -1  N  VAL B 308   O  ILE B 320           
SHEET    5 AA4 5 VAL B 296  LYS B 299 -1  N  LYS B 299   O  THR B 309           
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.04  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.47  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.24  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.31  
LINK         NE2 HIS B 390                ZN    ZN B 601     1555   1555  2.03  
LINK         SG  CYS B 396                ZN    ZN B 601     1555   1555  2.48  
LINK         SG  CYS B 397                ZN    ZN B 601     1555   1555  2.22  
LINK         SG  CYS B 404                ZN    ZN B 601     1555   1555  2.30  
CISPEP   1 ASN B  256    PRO B  257          0         1.80                     
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2 11 ALA A 247  ARG A 376  LEU A 377  SER A 378                    
SITE     2 AC2 11 SER A 434  TYR A 436  HIS A 437  ASN A 482                    
SITE     3 AC2 11 PHE A 488  LEU A 490  HOH A 704                               
SITE     1 AC3  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
SITE     1 AC4  9 ARG B 376  LEU B 377  SER B 378  SER B 434                    
SITE     2 AC4  9 TYR B 436  HIS B 437  ASN B 482  PHE B 488                    
SITE     3 AC4  9 LEU B 490                                                     
CRYST1  218.796   45.999   90.339  90.00 111.64  90.00 C 1 2 1       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      0.004570  0.000000  0.001813        0.00000                         
SCALE2      0.000000  0.021740  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011909        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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