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Database: PDB
Entry: 5VDW
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HEADER    TRANSFERASE                             03-APR-17   5VDW              
TITLE     HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS) IN COMPLEX WITH COMPOUND F1      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 161-521;                                      
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: MB21D1, C6ORF150;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE, STING, CGAMP                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.J.BYRNES,J.D.HALL                                                   
REVDAT   3   06-DEC-17 5VDW    1       JRNL                                     
REVDAT   2   04-OCT-17 5VDW    1       JRNL                                     
REVDAT   1   27-SEP-17 5VDW    0                                                
JRNL        AUTH   J.HALL,E.C.RALPH,S.SHANKER,H.WANG,L.J.BYRNES,R.HORST,J.WONG, 
JRNL        AUTH 2 A.BRAULT,D.DUMLAO,J.F.SMITH,L.A.DAKIN,D.C.SCHMITT,           
JRNL        AUTH 3 J.TRUJILLO,F.VINCENT,M.GRIFFOR,A.E.AULABAUGH                 
JRNL        TITL   THE CATALYTIC MECHANISM OF CYCLIC GMP-AMP SYNTHASE (CGAS)    
JRNL        TITL 2 AND IMPLICATIONS FOR INNATE IMMUNITY AND INHIBITION.         
JRNL        REF    PROTEIN SCI.                  V.  26  2367 2017              
JRNL        REFN                   ESSN 1469-896X                               
JRNL        PMID   28940468                                                     
JRNL        DOI    10.1002/PRO.3304                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.71 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_1999                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.42                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 23517                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.670                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1099                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 52.4263 -  5.4195    0.98     2918   139  0.1870 0.1896        
REMARK   3     2  5.4195 -  4.3022    0.99     2830   154  0.1750 0.2001        
REMARK   3     3  4.3022 -  3.7586    0.99     2850   124  0.1929 0.2585        
REMARK   3     4  3.7586 -  3.4150    0.97     2736   140  0.2398 0.3083        
REMARK   3     5  3.4150 -  3.1703    0.97     2764   146  0.2794 0.2971        
REMARK   3     6  3.1703 -  2.9834    0.98     2738   136  0.2920 0.3240        
REMARK   3     7  2.9834 -  2.8340    0.98     2767   136  0.2957 0.3619        
REMARK   3     8  2.8340 -  2.7106    0.98     2815   124  0.3148 0.3541        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.580           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.42                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.51                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           5633                                  
REMARK   3   ANGLE     :  0.714           7745                                  
REMARK   3   CHIRALITY :  0.032            863                                  
REMARK   3   PLANARITY :  0.003           1033                                  
REMARK   3   DIHEDRAL  : 14.568           2077                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 253 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -25.6307   7.9924 -20.8769              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4272 T22:   0.5327                                     
REMARK   3      T33:   0.3643 T12:   0.0989                                     
REMARK   3      T13:   0.0378 T23:   0.0762                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9574 L22:   1.9284                                     
REMARK   3      L33:   1.7826 L12:  -0.4783                                     
REMARK   3      L13:   0.4510 L23:   0.1739                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1265 S12:   0.1984 S13:  -0.0589                       
REMARK   3      S21:  -0.0145 S22:  -0.2339 S23:  -0.2564                       
REMARK   3      S31:   0.4669 S32:   0.5823 S33:   0.1061                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 254 THROUGH 307 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.4497  13.7085 -24.5965              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3589 T22:   0.7689                                     
REMARK   3      T33:   0.6695 T12:   0.0647                                     
REMARK   3      T13:   0.0380 T23:   0.1395                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7075 L22:   2.6694                                     
REMARK   3      L33:   6.3770 L12:   0.4375                                     
REMARK   3      L13:   0.5770 L23:   3.0894                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0308 S12:   0.3892 S13:  -0.0805                       
REMARK   3      S21:   0.1594 S22:  -0.1347 S23:  -0.7737                       
REMARK   3      S31:   0.4890 S32:   0.9233 S33:   0.1076                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 308 THROUGH 520 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -38.6535  14.8014 -21.1724              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2655 T22:   0.2060                                     
REMARK   3      T33:   0.2471 T12:  -0.0050                                     
REMARK   3      T13:   0.0465 T23:  -0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5525 L22:   1.2477                                     
REMARK   3      L33:   2.0959 L12:  -0.1614                                     
REMARK   3      L13:   0.4459 L23:  -0.3529                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0116 S12:   0.1083 S13:  -0.0078                       
REMARK   3      S21:   0.0436 S22:  -0.0562 S23:  -0.0765                       
REMARK   3      S31:  -0.0011 S32:   0.2378 S33:   0.0422                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 161 THROUGH 224 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.0789  16.3460  20.8911              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5403 T22:   0.6917                                     
REMARK   3      T33:   0.9884 T12:  -0.0890                                     
REMARK   3      T13:   0.0226 T23:   0.0930                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5762 L22:   0.0752                                     
REMARK   3      L33:   0.1997 L12:  -0.1724                                     
REMARK   3      L13:  -0.2376 L23:  -0.0919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6297 S12:   0.3053 S13:   0.4139                       
REMARK   3      S21:   0.0339 S22:   0.1193 S23:  -0.6383                       
REMARK   3      S31:  -0.0703 S32:   0.4378 S33:   0.4532                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 225 THROUGH 307 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.2704   1.1666  19.2940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3215 T22:   0.7754                                     
REMARK   3      T33:   0.8308 T12:   0.0236                                     
REMARK   3      T13:   0.0027 T23:   0.0471                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3757 L22:   4.5950                                     
REMARK   3      L33:   2.8081 L12:   1.0122                                     
REMARK   3      L13:   0.8329 L23:  -0.0473                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0469 S12:  -0.0244 S13:   0.1977                       
REMARK   3      S21:   0.0065 S22:  -0.1031 S23:  -0.8673                       
REMARK   3      S31:  -0.3309 S32:   0.8917 S33:   0.0426                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 308 THROUGH 520 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -36.4933   1.1970  20.3629              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2984 T22:   0.2698                                     
REMARK   3      T33:   0.3380 T12:  -0.0108                                     
REMARK   3      T13:  -0.0029 T23:  -0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9035 L22:   1.9009                                     
REMARK   3      L33:   2.5978 L12:  -0.2012                                     
REMARK   3      L13:  -0.5436 L23:  -0.5814                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0083 S12:  -0.1845 S13:   0.0448                       
REMARK   3      S21:   0.1040 S22:   0.0242 S23:  -0.1756                       
REMARK   3      S31:   0.0079 S32:   0.3609 S33:  -0.0045                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 3311                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VDW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227278.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 173                                
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                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : AIMLESS                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.3.11                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23537                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.710                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.417                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.15100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.71                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73600                            
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: 4O67                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20% PEG 3350, 0.2 M AMMONIUM          
REMARK 280  CITRATE PH 7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K       
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      108.68000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.99900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      108.68000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.99900            
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     MET A   160                                                      
REMARK 465     GLU A   521                                                      
REMARK 465     PHE A   522                                                      
REMARK 465     MET B   160                                                      
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     MET A 185    CG   SD   CE                                        
REMARK 470     LYS A 187    CG   CD   CE   NZ                                   
REMARK 470     LEU A 195    CG   CD1  CD2                                       
REMARK 470     ARG A 196    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 198    CG   CD   CE   NZ                                   
REMARK 470     ARG A 204    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     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 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     ILE A 284    CG1  CG2  CD1                                       
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     MET A 298    CG   SD   CE                                        
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     ARG A 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 305    OG                                                  
REMARK 470     LYS A 315    CG   CD   CE   NZ                                   
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     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     LYS A 432    CG   CD   CE   NZ                                   
REMARK 470     LEU B 174    CG   CD1  CD2                                       
REMARK 470     SER B 175    OG                                                  
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     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     LYS B 198    CG   CD   CE   NZ                                   
REMARK 470     ARG B 204    CG   CD   NE   CZ   NH1  NH2                        
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     ASN B 224    CG   OD1  ND2                                       
REMARK 470     GLU B 225    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 240    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 254    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     LYS B 285    CG   CD   CE   NZ                                   
REMARK 470     GLU B 286    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     MET B 298    CG   SD   CE                                        
REMARK 470     LYS B 299    CG   CD   CE   NZ                                   
REMARK 470     ARG B 300    CG   CD   NE   CZ   NH1  NH2                        
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     LEU B 322    CG   CD1  CD2                                       
REMARK 470     LYS B 365    CG   CD   CE   NZ                                   
REMARK 470     GLU B 366    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 368    CG   OD1  ND2                                       
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     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     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: 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       34.24    -98.40                                   
REMARK 500    ARG A 246      -10.90     69.11                                   
REMARK 500    LYS A 258       39.94    -82.24                                   
REMARK 500    ARG A 302      -48.25   -136.12                                   
REMARK 500    LYS A 315      -59.76   -137.60                                   
REMARK 500    TRP A 343      -67.17   -103.54                                   
REMARK 500    SER A 345      163.66     88.34                                   
REMARK 500    GLU A 402       58.36   -116.09                                   
REMARK 500    PHE A 516       71.71     41.87                                   
REMARK 500    PHE B 203       33.44    -99.70                                   
REMARK 500    SER B 221       -0.28     71.52                                   
REMARK 500    ARG B 246      -10.40     68.06                                   
REMARK 500    LYS B 258       39.65    -83.15                                   
REMARK 500    ARG B 302      -48.65   -137.77                                   
REMARK 500    LYS B 315      -61.03   -138.01                                   
REMARK 500    TRP B 343      -67.95   -103.37                                   
REMARK 500    SER B 345      162.96     89.23                                   
REMARK 500    LYS B 365       97.65    -64.83                                   
REMARK 500    GLU B 402       59.70   -117.47                                   
REMARK 500    PHE B 516       71.56     42.22                                   
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  125.3                                              
REMARK 620 3 CYS A 397   SG  100.3 119.1                                        
REMARK 620 4 CYS A 404   SG   96.2 111.6  99.3                                  
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  121.9                                              
REMARK 620 3 CYS B 397   SG   99.7 120.7                                        
REMARK 620 4 CYS B 404   SG   98.8 112.6  98.8                                  
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 9BY 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 9BY B 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VDO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDV   RELATED DB: PDB                                   
DBREF  5VDW A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
DBREF  5VDW B  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
SEQADV 5VDW MET A  160  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 5VDW MET B  160  UNP  Q8N884              EXPRESSION TAG                 
SEQRES   1 A  363  MET GLY ALA SER LYS LEU ARG ALA VAL LEU GLU LYS LEU          
SEQRES   2 A  363  LYS LEU SER ARG ASP ASP ILE SER THR ALA ALA GLY MET          
SEQRES   3 A  363  VAL LYS GLY VAL VAL ASP HIS LEU LEU LEU ARG LEU LYS          
SEQRES   4 A  363  CYS ASP SER ALA PHE ARG GLY VAL GLY LEU LEU ASN THR          
SEQRES   5 A  363  GLY SER TYR TYR GLU HIS VAL LYS ILE SER ALA PRO ASN          
SEQRES   6 A  363  GLU PHE ASP VAL MET PHE LYS LEU GLU VAL PRO ARG ILE          
SEQRES   7 A  363  GLN LEU GLU GLU TYR SER ASN THR ARG ALA TYR TYR PHE          
SEQRES   8 A  363  VAL LYS PHE LYS ARG ASN PRO LYS GLU ASN PRO LEU SER          
SEQRES   9 A  363  GLN PHE LEU GLU GLY GLU ILE LEU SER ALA SER LYS MET          
SEQRES  10 A  363  LEU SER LYS PHE ARG LYS ILE ILE LYS GLU GLU ILE ASN          
SEQRES  11 A  363  ASP ILE LYS ASP THR ASP VAL ILE MET LYS ARG LYS ARG          
SEQRES  12 A  363  GLY GLY SER PRO ALA VAL THR LEU LEU ILE SER GLU LYS          
SEQRES  13 A  363  ILE SER VAL ASP ILE THR LEU ALA LEU GLU SER LYS SER          
SEQRES  14 A  363  SER TRP PRO ALA SER THR GLN GLU GLY LEU ARG ILE GLN          
SEQRES  15 A  363  ASN TRP LEU SER ALA LYS VAL ARG LYS GLN LEU ARG LEU          
SEQRES  16 A  363  LYS PRO PHE TYR LEU VAL PRO LYS HIS ALA LYS GLU GLY          
SEQRES  17 A  363  ASN GLY PHE GLN GLU GLU THR TRP ARG LEU SER PHE SER          
SEQRES  18 A  363  HIS ILE GLU LYS GLU ILE LEU ASN ASN HIS GLY LYS SER          
SEQRES  19 A  363  LYS THR CYS CYS GLU ASN LYS GLU GLU LYS CYS CYS ARG          
SEQRES  20 A  363  LYS ASP CYS LEU LYS LEU MET LYS TYR LEU LEU GLU GLN          
SEQRES  21 A  363  LEU LYS GLU ARG PHE LYS ASP LYS LYS HIS LEU ASP LYS          
SEQRES  22 A  363  PHE SER SER TYR HIS VAL LYS THR ALA PHE PHE HIS VAL          
SEQRES  23 A  363  CYS THR GLN ASN PRO GLN ASP SER GLN TRP ASP ARG LYS          
SEQRES  24 A  363  ASP LEU GLY LEU CYS PHE ASP ASN CYS VAL THR TYR PHE          
SEQRES  25 A  363  LEU GLN CYS LEU ARG THR GLU LYS LEU GLU ASN TYR PHE          
SEQRES  26 A  363  ILE PRO GLU PHE ASN LEU PHE SER SER ASN LEU ILE ASP          
SEQRES  27 A  363  LYS ARG SER LYS GLU PHE LEU THR LYS GLN ILE GLU TYR          
SEQRES  28 A  363  GLU ARG ASN ASN GLU PHE PRO VAL PHE ASP GLU PHE              
SEQRES   1 B  363  MET GLY ALA SER LYS LEU ARG ALA VAL LEU GLU LYS LEU          
SEQRES   2 B  363  LYS LEU SER ARG ASP ASP ILE SER THR ALA ALA GLY MET          
SEQRES   3 B  363  VAL LYS GLY VAL VAL ASP HIS LEU LEU LEU ARG LEU LYS          
SEQRES   4 B  363  CYS ASP SER ALA PHE ARG GLY VAL GLY LEU LEU ASN THR          
SEQRES   5 B  363  GLY SER TYR TYR GLU HIS VAL LYS ILE SER ALA PRO ASN          
SEQRES   6 B  363  GLU PHE ASP VAL MET PHE LYS LEU GLU VAL PRO ARG ILE          
SEQRES   7 B  363  GLN LEU GLU GLU TYR SER ASN THR ARG ALA TYR TYR PHE          
SEQRES   8 B  363  VAL LYS PHE LYS ARG ASN PRO LYS GLU ASN PRO LEU SER          
SEQRES   9 B  363  GLN PHE LEU GLU GLY GLU ILE LEU SER ALA SER LYS MET          
SEQRES  10 B  363  LEU SER LYS PHE ARG LYS ILE ILE LYS GLU GLU ILE ASN          
SEQRES  11 B  363  ASP ILE LYS ASP THR ASP VAL ILE MET LYS ARG LYS ARG          
SEQRES  12 B  363  GLY GLY SER PRO ALA VAL THR LEU LEU ILE SER GLU LYS          
SEQRES  13 B  363  ILE SER VAL ASP ILE THR LEU ALA LEU GLU SER LYS SER          
SEQRES  14 B  363  SER TRP PRO ALA SER THR GLN GLU GLY LEU ARG ILE GLN          
SEQRES  15 B  363  ASN TRP LEU SER ALA LYS VAL ARG LYS GLN LEU ARG LEU          
SEQRES  16 B  363  LYS PRO PHE TYR LEU VAL PRO LYS HIS ALA LYS GLU GLY          
SEQRES  17 B  363  ASN GLY PHE GLN GLU GLU THR TRP ARG LEU SER PHE SER          
SEQRES  18 B  363  HIS ILE GLU LYS GLU ILE LEU ASN ASN HIS GLY LYS SER          
SEQRES  19 B  363  LYS THR CYS CYS GLU ASN LYS GLU GLU LYS CYS CYS ARG          
SEQRES  20 B  363  LYS ASP CYS LEU LYS LEU MET LYS TYR LEU LEU GLU GLN          
SEQRES  21 B  363  LEU LYS GLU ARG PHE LYS ASP LYS LYS HIS LEU ASP LYS          
SEQRES  22 B  363  PHE SER SER TYR HIS VAL LYS THR ALA PHE PHE HIS VAL          
SEQRES  23 B  363  CYS THR GLN ASN PRO GLN ASP SER GLN TRP ASP ARG LYS          
SEQRES  24 B  363  ASP LEU GLY LEU CYS PHE ASP ASN CYS VAL THR TYR PHE          
SEQRES  25 B  363  LEU GLN CYS LEU ARG THR GLU LYS LEU GLU ASN TYR PHE          
SEQRES  26 B  363  ILE PRO GLU PHE ASN LEU PHE SER SER ASN LEU ILE ASP          
SEQRES  27 B  363  LYS ARG SER LYS GLU PHE LEU THR LYS GLN ILE GLU TYR          
SEQRES  28 B  363  GLU ARG ASN ASN GLU PHE PRO VAL PHE ASP GLU PHE              
HET     ZN  A 601       1                                                       
HET    9BY  A 602      18                                                       
HET     ZN  B 601       1                                                       
HET    9BY  B 602      18                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     9BY [2-(1,3-THIAZOL-4-YL)-1H-BENZIMIDAZOL-1-YL]ACETIC ACID           
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  9BY    2(C12 H9 N3 O2 S)                                            
FORMUL   7  HOH   *36(H2 O)                                                     
HELIX    1 AA1 GLY A  161  LYS A  173  1                                  13    
HELIX    2 AA2 SER A  175  LYS A  198  1                                  24    
HELIX    3 AA3 LEU A  262  GLN A  264  5                                   3    
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  388  1                                  10    
HELIX    8 AA8 CYS A  405  PHE A  424  1                                  20    
HELIX    9 AA9 SER A  434  ASN A  449  1                                  16    
HELIX   10 AB1 GLN A  451  LYS A  458  5                                   8    
HELIX   11 AB2 ASP A  459  GLU A  478  1                                  20    
HELIX   12 AB3 ASP A  497  ASN A  514  1                                  18    
HELIX   13 AB4 GLU A  515  ASP A  520  5                                   6    
HELIX   14 AB5 ALA B  162  LYS B  173  1                                  12    
HELIX   15 AB6 SER B  175  LYS B  198  1                                  24    
HELIX   16 AB7 LEU B  262  GLN B  264  5                                   3    
HELIX   17 AB8 SER B  272  ILE B  291  1                                  20    
HELIX   18 AB9 PRO B  331  GLN B  335  5                                   5    
HELIX   19 AC1 SER B  345  LEU B  354  1                                  10    
HELIX   20 AC2 PHE B  379  ASN B  388  1                                  10    
HELIX   21 AC3 ASN B  399  LYS B  403  5                                   5    
HELIX   22 AC4 CYS B  405  PHE B  424  1                                  20    
HELIX   23 AC5 HIS B  429  PHE B  433  5                                   5    
HELIX   24 AC6 SER B  434  ASN B  449  1                                  16    
HELIX   25 AC7 GLN B  451  LYS B  458  5                                   8    
HELIX   26 AC8 ASP B  459  THR B  477  1                                  19    
HELIX   27 AC9 ASP B  497  ASN B  514  1                                  18    
HELIX   28 AD1 GLU B  515  ASP B  520  5                                   6    
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  GLU A 325   N  LEU A 232           
SHEET    4 AA1 7 PHE A 357  PRO A 361 -1  O  PHE A 357   N  SER A 326           
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  PHE A 253 -1  N  TYR A 249   O  TRP A 375           
SHEET    7 AA1 7 ILE A 237  GLU A 241 -1  N  GLU A 240   O  PHE A 250           
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  GLU A 325   N  LEU A 232           
SHEET    4 AA2 5 VAL A 308  ILE A 312 -1  N  LEU A 310   O  VAL A 318           
SHEET    5 AA2 5 VAL A 296  MET A 298 -1  N  ILE A 297   O  LEU A 311           
SHEET    1 AA3 2 LEU A 266  GLU A 267  0                                        
SHEET    2 AA3 2 ILE A 270  LEU A 271 -1  O  ILE A 270   N  GLU A 267           
SHEET    1 AA4 7 GLY B 207  LEU B 209  0                                        
SHEET    2 AA4 7 GLU B 225  GLU B 233 -1  O  MET B 229   N  LEU B 209           
SHEET    3 AA4 7 ILE B 316  SER B 326  1  O  GLU B 325   N  LEU B 232           
SHEET    4 AA4 7 PHE B 357  PRO B 361 -1  O  PHE B 357   N  SER B 326           
SHEET    5 AA4 7 TRP B 375  SER B 378 -1  O  ARG B 376   N  VAL B 360           
SHEET    6 AA4 7 TYR B 248  PHE B 253 -1  N  TYR B 249   O  TRP B 375           
SHEET    7 AA4 7 ILE B 237  GLU B 241 -1  N  GLN B 238   O  LYS B 252           
SHEET    1 AA5 5 GLY B 207  LEU B 209  0                                        
SHEET    2 AA5 5 GLU B 225  GLU B 233 -1  O  MET B 229   N  LEU B 209           
SHEET    3 AA5 5 ILE B 316  SER B 326  1  O  GLU B 325   N  LEU B 232           
SHEET    4 AA5 5 VAL B 308  ILE B 312 -1  N  ILE B 312   O  ILE B 316           
SHEET    5 AA5 5 VAL B 296  MET B 298 -1  N  ILE B 297   O  LEU B 311           
SHEET    1 AA6 2 LEU B 266  GLU B 267  0                                        
SHEET    2 AA6 2 ILE B 270  LEU B 271 -1  O  ILE B 270   N  GLU B 267           
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.22  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.43  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.34  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.33  
LINK         NE2 HIS B 390                ZN    ZN B 601     1555   1555  2.09  
LINK         SG  CYS B 396                ZN    ZN B 601     1555   1555  2.37  
LINK         SG  CYS B 397                ZN    ZN B 601     1555   1555  2.34  
LINK         SG  CYS B 404                ZN    ZN B 601     1555   1555  2.34  
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2  7 ARG A 376  LEU A 377  SER A 378  SER A 434                    
SITE     2 AC2  7 TYR A 436  ASN A 482  PHE A 488                               
SITE     1 AC3  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
SITE     1 AC4  8 ARG B 376  LEU B 377  SER B 378  SER B 434                    
SITE     2 AC4  8 TYR B 436  ASN B 482  PHE B 488  LEU B 490                    
CRYST1  217.360   47.998   86.861  90.00 105.29  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      0.004601  0.000000  0.001258        0.00000                         
SCALE2      0.000000  0.020834  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011935        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system