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Database: PDB
Entry: 6NFG
LinkDB: 6NFG
Original site: 6NFG 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       20-DEC-18   6NFG              
TITLE     CYCLIC GMP-AMP SYNTHASE IN COMPLEX WITH COMPOUND 16 INHIBITOR: 7-     
TITLE    2 HYDROXY-N-METHYL-5-PHENYLPYRAZOLO[1,5-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 6NFG    0                                                
SPRSDE     23-JAN-19 6NFG      5V8H                                             
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.    2.76 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) : 2.76                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 104.53                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 21446                          
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)  : 0.185                          
REMARK   3   R VALUE            (WORKING SET)  : 0.182                          
REMARK   3   FREE R VALUE                      : 0.244                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.020                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1076                           
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               : 11                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.76                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.90                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 96.51                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2752                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2280                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2619                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2230                   
REMARK   3   BIN FREE R VALUE                        : 0.3400                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.83                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 133                      
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            : 5379                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 177                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.36                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.92                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.42940                                             
REMARK   3    B22 (A**2) : 6.85930                                              
REMARK   3    B33 (A**2) : -18.28870                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -11.77780                                            
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.330               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.340               
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      : 0.903                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.876                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5555   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7518   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1886   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 116    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 807    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5555   ; 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   : 731    ; 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   : 6352   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.14                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.74                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.57                    
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):  -31.7475   12.1145  -21.9944           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0556 T22:   -0.1132                                    
REMARK   3     T33:   -0.0505 T12:   -0.0057                                    
REMARK   3     T13:    0.0189 T23:    0.0230                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9569 L22:    1.0325                                    
REMARK   3     L33:    0.8340 L12:   -0.0977                                    
REMARK   3     L13:   -0.0612 L23:   -0.1548                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0608 S12:   -0.0068 S13:   -0.0178                     
REMARK   3     S21:    0.0331 S22:   -0.0553 S23:   -0.1363                     
REMARK   3     S31:    0.0296 S32:    0.0493 S33:   -0.0055                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -29.8844    2.8783   20.3139           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1054 T22:   -0.1173                                    
REMARK   3     T33:   -0.0167 T12:    0.0241                                    
REMARK   3     T13:    0.0001 T23:   -0.0497                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1445 L22:    1.3700                                    
REMARK   3     L33:    0.9032 L12:    0.0636                                    
REMARK   3     L13:   -0.1032 L23:    0.1157                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0011 S12:   -0.0834 S13:    0.0929                     
REMARK   3     S21:    0.0308 S22:    0.1257 S23:   -0.3049                     
REMARK   3     S31:   -0.0032 S32:    0.1177 S33:   -0.1268                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6NFG 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_1000238690.                                   
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                             : 7                                  
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          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21449                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.760                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 104.530                            
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  : 7.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.76                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
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: RODS                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
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 280  TEMPERATURE 277K, TEMPERATURE 277.15K                               
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      108.57400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.80100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      108.57400            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.80100            
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     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     ASN A   260                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     SER A   305                                                      
REMARK 465     PRO A   306                                                      
REMARK 465     GLY A   367                                                      
REMARK 465     ASN A   368                                                      
REMARK 465     GLY A   369                                                      
REMARK 465     PHE A   522                                                      
REMARK 465     ARG B   255                                                      
REMARK 465     ASN B   256                                                      
REMARK 465     PRO B   257                                                      
REMARK 465     ILE B   291                                                      
REMARK 465     LYS B   292                                                      
REMARK 465     ASP B   293                                                      
REMARK 465     ARG B   302                                                      
REMARK 465     GLY B   303                                                      
REMARK 465     GLY B   304                                                      
REMARK 465     SER B   305                                                      
REMARK 465     PRO B   306                                                      
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     LYS A 171    CG   CD   CE   NZ                                   
REMARK 470     ARG A 176    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 187    CG   CD   CE   NZ                                   
REMARK 470     LEU A 195    CG   CD1  CD2                                       
REMARK 470     GLU A 216    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 220    CG1  CG2  CD1                                       
REMARK 470     ARG A 236    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 240    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 252    CG   CD   CE   NZ                                   
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
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     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     GLU A 287    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 290    CG   OD1  OD2                                       
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     ASP A 295    CG   OD1  OD2                                       
REMARK 470     ARG A 300    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 301    CG   CD   CE   NZ                                   
REMARK 470     ARG A 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 314    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 319    CG   OD1  OD2                                       
REMARK 470     LYS A 350    CG   CD   CE   NZ                                   
REMARK 470     LYS A 365    CG   CD   CE   NZ                                   
REMARK 470     GLU A 366    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 370    CG   CD1  CD2  CE1  CE2  CZ                         
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 401    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 426    CG   OD1  OD2                                       
REMARK 470     LYS A 428    CG   CD   CE   NZ                                   
REMARK 470     LYS B 164    CG   CD   CE   NZ                                   
REMARK 470     LYS B 173    CG   CD   CE   NZ                                   
REMARK 470     LEU B 174    CG   CD1  CD2                                       
REMARK 470     ARG B 176    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 177    CG   OD1  OD2                                       
REMARK 470     ASP B 178    CG   OD1  OD2                                       
REMARK 470     ILE B 179    CG1  CG2  CD1                                       
REMARK 470     LEU B 195    CG   CD1  CD2                                       
REMARK 470     ARG B 196    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 198    CG   CD   CE   NZ                                   
REMARK 470     ARG B 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 208    CG   CD1  CD2                                       
REMARK 470     SER B 213    OG                                                  
REMARK 470     ASN B 224    CG   OD1  ND2                                       
REMARK 470     GLU B 225    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 236    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 240    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 254    CG   CD   CE   NZ                                   
REMARK 470     LYS B 258    CG   CD   CE   NZ                                   
REMARK 470     GLU B 259    CG   CD   OE1  OE2                                  
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     LYS B 282    CG   CD   CE   NZ                                   
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     ILE B 288    CG1  CG2  CD1                                       
REMARK 470     ASP B 290    CG   OD1  OD2                                       
REMARK 470     THR B 294    OG1  CG2                                            
REMARK 470     ASP B 295    CG   OD1  OD2                                       
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     GLU B 314    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 315    CG   CD   CE   NZ                                   
REMARK 470     LEU B 322    CG   CD1  CD2                                       
REMARK 470     LYS B 350    CG   CD   CE   NZ                                   
REMARK 470     GLN B 351    CG   CD   OE1  NE2                                  
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 384    CG   CD   CE   NZ                                   
REMARK 470     GLU B 401    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 426    CG   OD1  OD2                                       
REMARK 470     LYS B 427    CG   CD   CE   NZ                                   
REMARK 470     LYS B 428    CG   CD   CE   NZ                                   
REMARK 470     LYS B 432    CG   CD   CE   NZ                                   
REMARK 470     LYS B 458    CG   CD   CE   NZ                                   
REMARK 470     ARG B 499    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 515    CG   CD   OE1  OE2                                  
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    SER A 313   N   -  CA  -  C   ANGL. DEV. = -18.1 DEGREES          
REMARK 500    SER B 313   N   -  CA  -  C   ANGL. DEV. = -16.7 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       34.68    -96.17                                   
REMARK 500    ALA A 222       73.59     52.37                                   
REMARK 500    ARG A 246       -4.14     70.24                                   
REMARK 500    GLU A 267       68.89   -108.63                                   
REMARK 500    SER A 313     -125.58     54.55                                   
REMARK 500    LYS A 315      -51.85   -129.83                                   
REMARK 500    SER A 345      157.13     94.03                                   
REMARK 500    PRO A 356     -176.32    -68.88                                   
REMARK 500    GLU A 372       39.76    -81.29                                   
REMARK 500    LYS A 428        4.88     82.88                                   
REMARK 500    LEU A 430        5.04    -67.31                                   
REMARK 500    PHE B 203       34.86    -96.98                                   
REMARK 500    ASN B 210       48.01     72.58                                   
REMARK 500    ALA B 222       74.40     52.90                                   
REMARK 500    PRO B 235      -70.06    -50.81                                   
REMARK 500    ARG B 246       -3.07     69.59                                   
REMARK 500    GLU B 267       68.22   -107.86                                   
REMARK 500    SER B 313     -121.42     51.79                                   
REMARK 500    GLU B 314       42.29   -142.30                                   
REMARK 500    LYS B 315      -44.41   -142.50                                   
REMARK 500    TRP B 343      -63.16   -108.82                                   
REMARK 500    SER B 345      155.84     92.48                                   
REMARK 500    PRO B 356     -175.35    -69.16                                   
REMARK 500    GLU B 372       40.94    -77.38                                   
REMARK 500    PHE B 516       70.26     53.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 792        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH A 793        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH A 794        DISTANCE =  6.47 ANGSTROMS                       
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  118.7                                              
REMARK 620 3 CYS A 397   SG  104.3 119.5                                        
REMARK 620 4 CYS A 404   SG   99.6 106.9 105.4                                  
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  118.7                                              
REMARK 620 3 CYS B 397   SG  105.7 118.5                                        
REMARK 620 4 CYS B 404   SG  100.0 105.6 106.0                                  
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 KKP 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 KKP B 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5V8J   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5V8N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5V8O   RELATED DB: PDB                                   
DBREF  6NFG A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
DBREF  6NFG 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    KKP  A 602      32                                                       
HET     ZN  B 601       1                                                       
HET    KKP  B 602      32                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     KKP 7-HYDROXY-N-METHYL-5-PHENYLPYRAZOLO[1,5-A]PYRIMIDINE-3-          
HETNAM   2 KKP  CARBOXAMIDE                                                     
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  KKP    2(C14 H12 N4 O2)                                             
FORMUL   7  HOH   *177(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 LYS A  428  PHE A  433  5                                   6    
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 PHE A  516  GLU A  521  1                                   6    
HELIX   16 AB7 ALA B  162  LEU B  174  1                                  13    
HELIX   17 AB8 SER B  175  LYS B  198  1                                  24    
HELIX   18 AB9 LEU B  262  LEU B  266  5                                   5    
HELIX   19 AC1 SER B  272  ASP B  290  1                                  19    
HELIX   20 AC2 PRO B  331  GLN B  335  5                                   5    
HELIX   21 AC3 SER B  345  LEU B  354  1                                  10    
HELIX   22 AC4 PHE B  379  ASN B  389  1                                  11    
HELIX   23 AC5 ASN B  399  LYS B  403  5                                   5    
HELIX   24 AC6 CYS B  405  PHE B  424  1                                  20    
HELIX   25 AC7 HIS B  429  PHE B  433  5                                   5    
HELIX   26 AC8 SER B  434  ASN B  449  1                                  16    
HELIX   27 AC9 GLN B  451  LYS B  458  5                                   8    
HELIX   28 AD1 ASP B  459  THR B  477  1                                  19    
HELIX   29 AD2 ASP B  497  ASN B  514  1                                  18    
SHEET    1 AA1 7 VAL A 206  LEU A 209  0                                        
SHEET    2 AA1 7 GLU A 225  GLU A 233 -1  O  MET A 229   N  LEU A 209           
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 209  0                                        
SHEET    2 AA2 5 GLU A 225  GLU A 233 -1  O  MET A 229   N  LEU A 209           
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  2.16  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.44  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.28  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.32  
LINK         NE2 HIS B 390                ZN    ZN B 601     1555   1555  2.12  
LINK         SG  CYS B 396                ZN    ZN B 601     1555   1555  2.46  
LINK         SG  CYS B 397                ZN    ZN B 601     1555   1555  2.25  
LINK         SG  CYS B 404                ZN    ZN B 601     1555   1555  2.35  
CISPEP   1 PHE A  253    LYS A  254          0         7.32                     
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2  8 ARG A 376  SER A 378  SER A 434  TYR A 436                    
SITE     2 AC2  8 ASN A 482  PHE A 488  HOH A 701  HOH A 755                    
SITE     1 AC3  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
SITE     1 AC4  7 ARG B 376  SER B 434  TYR B 436  ASN B 482                    
SITE     2 AC4  7 PHE B 488  HOH B 701  HOH B 736                               
CRYST1  217.148   45.602   86.820  90.00 105.69  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      0.004605  0.000000  0.001294        0.00000                         
SCALE2      0.000000  0.021929  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011964        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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