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Database: PDB
Entry: 5VDV
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Original site: 5VDV 
HEADER    TRANSFERASE                             03-APR-17   5VDV              
TITLE     HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS) IN COMPLEX WITH COMPOUND F3      
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 5VDV    1       JRNL                                     
REVDAT   2   04-OCT-17 5VDV    1       JRNL                                     
REVDAT   1   27-SEP-17 5VDV    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.    3.00 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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.27                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 17350                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 887                             
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 55.2772 -  5.4462    1.00     2843   158  0.2005 0.2296        
REMARK   3     2  5.4462 -  4.3233    1.00     2732   154  0.1836 0.2347        
REMARK   3     3  4.3233 -  3.7770    1.00     2759   140  0.1894 0.2697        
REMARK   3     4  3.7770 -  3.4317    1.00     2709   161  0.2093 0.2645        
REMARK   3     5  3.4317 -  3.1857    1.00     2708   139  0.2471 0.3279        
REMARK   3     6  3.1857 -  2.9979    1.00     2712   135  0.2749 0.3478        
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)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.720           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 72.49                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 89.60                          
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      :  0.002           5518                                  
REMARK   3   ANGLE     :  0.468           7487                                  
REMARK   3   CHIRALITY :  0.024            843                                  
REMARK   3   PLANARITY :  0.001           1051                                  
REMARK   3   DIHEDRAL  : 11.984           1958                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -28.5782  -3.3167 -23.9259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7354 T22:   0.8401                                     
REMARK   3      T33:   0.7223 T12:  -0.0579                                     
REMARK   3      T13:  -0.1322 T23:   0.1958                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8204 L22:   3.1062                                     
REMARK   3      L33:   1.5041 L12:   0.1458                                     
REMARK   3      L13:   2.3845 L23:   0.8607                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8210 S12:  -0.4698 S13:  -2.1335                       
REMARK   3      S21:   0.2699 S22:  -0.3948 S23:  -0.3524                       
REMARK   3      S31:   0.6474 S32:   0.4491 S33:  -0.4119                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 200 THROUGH 307 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.4249  12.9135 -21.1279              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4993 T22:   0.9567                                     
REMARK   3      T33:   0.7070 T12:  -0.2311                                     
REMARK   3      T13:  -0.0449 T23:   0.0578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5864 L22:   4.8272                                     
REMARK   3      L33:   3.9949 L12:  -1.6598                                     
REMARK   3      L13:   0.2189 L23:   1.1044                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4082 S12:  -0.3892 S13:  -0.1283                       
REMARK   3      S21:   0.3745 S22:  -0.2620 S23:  -0.7880                       
REMARK   3      S31:   0.2506 S32:   0.5767 S33:  -0.1917                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 308 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -37.4343  14.2350 -20.9383              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5683 T22:   0.3040                                     
REMARK   3      T33:   0.3974 T12:  -0.1485                                     
REMARK   3      T13:   0.0524 T23:  -0.0480                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2507 L22:   1.6661                                     
REMARK   3      L33:   3.4677 L12:   0.0822                                     
REMARK   3      L13:   0.6153 L23:   0.0750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0714 S12:  -0.0019 S13:   0.0769                       
REMARK   3      S21:  -0.1538 S22:   0.0091 S23:  -0.0864                       
REMARK   3      S31:  -0.0768 S32:   0.3542 S33:   0.0527                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 161 THROUGH 195 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -32.3803  18.5103  24.3991              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6473 T22:   0.6852                                     
REMARK   3      T33:   0.7313 T12:  -0.1073                                     
REMARK   3      T13:   0.2204 T23:   0.0176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4232 L22:   3.7909                                     
REMARK   3      L33:   3.6989 L12:  -2.4175                                     
REMARK   3      L13:  -3.2240 L23:   1.3184                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9230 S12:   0.2264 S13:   1.7949                       
REMARK   3      S21:  -0.2649 S22:  -0.3862 S23:  -0.8362                       
REMARK   3      S31:  -0.8766 S32:   0.8311 S33:  -0.4886                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 196 THROUGH 307 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.1790   1.2533  20.5453              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5701 T22:   1.3739                                     
REMARK   3      T33:   1.1211 T12:   0.2307                                     
REMARK   3      T13:   0.0750 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6657 L22:   4.4943                                     
REMARK   3      L33:   2.2853 L12:   0.8875                                     
REMARK   3      L13:  -0.1520 L23:   0.1129                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0859 S12:   0.0366 S13:  -0.1869                       
REMARK   3      S21:  -0.0704 S22:   0.1859 S23:  -0.9803                       
REMARK   3      S31:  -0.0434 S32:   1.0057 S33:  -0.2284                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 308 THROUGH 434 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -32.2321   2.1018  18.0469              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5373 T22:   0.4640                                     
REMARK   3      T33:   0.5317 T12:   0.0871                                     
REMARK   3      T13:   0.0258 T23:   0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6150 L22:   1.0794                                     
REMARK   3      L33:   4.6517 L12:   0.3004                                     
REMARK   3      L13:  -0.4814 L23:   0.8635                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0096 S12:   0.1450 S13:  -0.0382                       
REMARK   3      S21:  -0.0717 S22:   0.1283 S23:  -0.3745                       
REMARK   3      S31:  -0.1656 S32:   0.6935 S33:  -0.1000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 435 THROUGH 520 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -44.7039  -2.0602  24.3219              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5909 T22:   0.3584                                     
REMARK   3      T33:   0.4463 T12:   0.1727                                     
REMARK   3      T13:   0.0399 T23:   0.0578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3783 L22:   1.4595                                     
REMARK   3      L33:   4.7401 L12:   0.9658                                     
REMARK   3      L13:  -1.5849 L23:   1.1654                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0116 S12:  -0.1086 S13:  -0.4501                       
REMARK   3      S21:   0.1280 S22:   0.0475 S23:   0.1721                       
REMARK   3      S31:   0.2754 S32:   0.4676 S33:  -0.0638                       
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  : 3062                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VDV 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_1000227276.                                   
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   : 17370                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.998                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.268                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.900                              
REMARK 200  R MERGE                    (I) : 0.17900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35100                            
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      108.72400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.47650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      108.72400            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.47650            
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     GLY A   303                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     SER A   305                                                      
REMARK 465     PRO A   306                                                      
REMARK 465     PHE A   522                                                      
REMARK 465     MET B   160                                                      
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     LYS A 173    CG   CD   CE   NZ                                   
REMARK 470     ARG A 176    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 179    CG1  CG2  CD1                                       
REMARK 470     LYS A 187    CG   CD   CE   NZ                                   
REMARK 470     LEU A 195    CG   CD1  CD2                                       
REMARK 470     ARG A 204    CG   CD   NE   CZ   NH1  NH2                        
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     ASN A 244    CG   OD1  ND2                                       
REMARK 470     LYS A 252    CG   CD   CE   NZ                                   
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     ARG A 255    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 256    CG   OD1  ND2                                       
REMARK 470     LYS A 258    CG   CD   CE   NZ                                   
REMARK 470     GLU A 259    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 266    CG   CD1  CD2                                       
REMARK 470     GLU A 267    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 269    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 275    CG   CD   CE   NZ                                   
REMARK 470     LEU A 277    CG   CD1  CD2                                       
REMARK 470     LYS A 279    CG   CD   CE   NZ                                   
REMARK 470     ARG A 281    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 282    CG   CD   CE   NZ                                   
REMARK 470     ILE A 284    CG1  CG2  CD1                                       
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     ASN A 368    CG   OD1  ND2                                       
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     GLU A 385    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 400    CG   CD   CE   NZ                                   
REMARK 470     GLU A 401    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 407    CG   CD   CE   NZ                                   
REMARK 470     LYS A 411    CG   CD   CE   NZ                                   
REMARK 470     ASP A 426    CG   OD1  OD2                                       
REMARK 470     LYS A 428    CG   CD   CE   NZ                                   
REMARK 470     ASP A 431    CG   OD1  OD2                                       
REMARK 470     LYS B 164    CG   CD   CE   NZ                                   
REMARK 470     GLU B 170    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 171    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     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     ASP B 191    CG   OD1  OD2                                       
REMARK 470     HIS B 192    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU B 195    CG   CD1  CD2                                       
REMARK 470     ARG B 196    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 197    CG   CD1  CD2                                       
REMARK 470     LYS B 198    CG   CD   CE   NZ                                   
REMARK 470     ARG B 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 208    CG   CD1  CD2                                       
REMARK 470     SER B 213    OG                                                  
REMARK 470     VAL B 218    CG1  CG2                                            
REMARK 470     ILE B 220    CG1  CG2  CD1                                       
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     ASN B 244    CG   OD1  ND2                                       
REMARK 470     LYS B 252    CG   CD   CE   NZ                                   
REMARK 470     LYS B 254    CG   CD   CE   NZ                                   
REMARK 470     ARG B 255    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 256    CG   OD1  ND2                                       
REMARK 470     LYS B 258    CG   CD   CE   NZ                                   
REMARK 470     GLU B 259    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 262    CG   CD1  CD2                                       
REMARK 470     LEU B 266    CG   CD1  CD2                                       
REMARK 470     GLU B 267    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 269    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 275    CG   CD   CE   NZ                                   
REMARK 470     LEU B 277    CG   CD1  CD2                                       
REMARK 470     LYS B 279    CG   CD   CE   NZ                                   
REMARK 470     ARG B 281    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 282    CG   CD   CE   NZ                                   
REMARK 470     ILE B 284    CG1  CG2  CD1                                       
REMARK 470     LYS B 285    CG   CD   CE   NZ                                   
REMARK 470     GLU B 286    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 287    CG   CD   OE1  OE2                                  
REMARK 470     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 362    CG   CD   CE   NZ                                   
REMARK 470     LYS B 365    CG   CD   CE   NZ                                   
REMARK 470     GLU B 372    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 373    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 384    CG   CD   CE   NZ                                   
REMARK 470     LYS B 400    CG   CD   CE   NZ                                   
REMARK 470     GLU B 401    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 411    CG   CD   CE   NZ                                   
REMARK 470     GLU B 418    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 422    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 426    CG   OD1  OD2                                       
REMARK 470     LYS B 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    SER A   313     O    HOH A   701              2.10            
REMARK 500   N    GLN B   238     O    LYS B   252              2.12            
REMARK 500   N    GLN A   238     O    LYS A   252              2.17            
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       47.96    -96.79                                   
REMARK 500    ASN A 210       49.73    -83.32                                   
REMARK 500    ARG A 246       -9.32     82.11                                   
REMARK 500    LYS A 254       20.79   -142.74                                   
REMARK 500    SER A 328     -179.20    -69.10                                   
REMARK 500    SER A 345      161.90     88.25                                   
REMARK 500    LYS A 428       51.86     72.49                                   
REMARK 500    ASN A 449       77.00   -113.60                                   
REMARK 500    PHE A 516       73.99     46.58                                   
REMARK 500    PHE B 203       47.63    -96.85                                   
REMARK 500    ARG B 246       -9.19     82.33                                   
REMARK 500    LYS B 254       21.04   -141.94                                   
REMARK 500    SER B 328     -178.96    -69.04                                   
REMARK 500    SER B 345      161.12     89.00                                   
REMARK 500    LYS B 428       51.88    -90.73                                   
REMARK 500    ASN B 449       76.85   -113.73                                   
REMARK 500    PHE B 516       74.52     46.56                                   
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  117.7                                              
REMARK 620 3 CYS A 397   SG   90.0 116.8                                        
REMARK 620 4 CYS A 404   SG  111.6 111.5 107.2                                  
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  120.2                                              
REMARK 620 3 CYS B 397   SG   93.7 117.8                                        
REMARK 620 4 CYS B 404   SG  106.3 112.1 104.4                                  
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 9BV 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 SO4 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9BV B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9BV B 604                 
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: 5VDW   RELATED DB: PDB                                   
DBREF  5VDV A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
DBREF  5VDV B  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
SEQADV 5VDV MET A  160  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 5VDV 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    9BV  A 602      38                                                       
HET     ZN  B 601       1                                                       
HET    SO4  B 602       5                                                       
HET    9BV  B 603      38                                                       
HET    9BV  B 604      19                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     9BV TETRAZOLO[5,1-B]QUINAZOLIN-9-OL                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  9BV    3(C8 H5 N5 O)                                                
FORMUL   6  SO4    O4 S 2-                                                      
FORMUL   9  HOH   *66(H2 O)                                                     
HELIX    1 AA1 GLY A  161  LEU A  174  1                                  14    
HELIX    2 AA2 SER A  175  ALA A  182  1                                   8    
HELIX    3 AA3 ALA A  182  ASP A  200  1                                  19    
HELIX    4 AA4 GLY A  212  HIS A  217  1                                   6    
HELIX    5 AA5 ASN A  260  LEU A  266  5                                   7    
HELIX    6 AA6 SER A  272  ASN A  289  1                                  18    
HELIX    7 AA7 ILE A  340  SER A  345  1                                   6    
HELIX    8 AA8 SER A  345  LYS A  355  1                                  11    
HELIX    9 AA9 PHE A  379  ASN A  388  1                                  10    
HELIX   10 AB1 ASN A  399  LYS A  403  5                                   5    
HELIX   11 AB2 CYS A  405  PHE A  424  1                                  20    
HELIX   12 AB3 HIS A  429  PHE A  433  5                                   5    
HELIX   13 AB4 SER A  434  ASN A  449  1                                  16    
HELIX   14 AB5 GLN A  451  LYS A  458  5                                   8    
HELIX   15 AB6 ASP A  459  GLU A  478  1                                  20    
HELIX   16 AB7 ASP A  497  ASN A  514  1                                  18    
HELIX   17 AB8 ALA B  162  LEU B  174  1                                  13    
HELIX   18 AB9 SER B  175  ALA B  182  1                                   8    
HELIX   19 AC1 ALA B  182  ASP B  200  1                                  19    
HELIX   20 AC2 ASN B  260  LEU B  266  5                                   7    
HELIX   21 AC3 SER B  272  ASN B  289  1                                  18    
HELIX   22 AC4 ILE B  340  SER B  345  1                                   6    
HELIX   23 AC5 SER B  345  LYS B  355  1                                  11    
HELIX   24 AC6 PHE B  379  ASN B  388  1                                  10    
HELIX   25 AC7 ASN B  399  LYS B  403  5                                   5    
HELIX   26 AC8 CYS B  405  PHE B  424  1                                  20    
HELIX   27 AC9 HIS B  429  PHE B  433  5                                   5    
HELIX   28 AD1 SER B  434  ASN B  449  1                                  16    
HELIX   29 AD2 GLN B  451  LYS B  458  5                                   8    
HELIX   30 AD3 ASP B  459  GLU B  478  1                                  20    
HELIX   31 AD4 ASP B  497  ASN B  514  1                                  18    
SHEET    1 AA1 7 VAL A 206  LEU A 208  0                                        
SHEET    2 AA1 7 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3 AA1 7 ILE A 316  SER A 326  1  O  THR A 321   N  PHE A 230           
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  GLN A 238   O  LYS A 252           
SHEET    1 AA2 5 VAL A 206  LEU A 208  0                                        
SHEET    2 AA2 5 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3 AA2 5 ILE A 316  SER A 326  1  O  THR A 321   N  PHE A 230           
SHEET    4 AA2 5 VAL A 308  ILE A 312 -1  N  ILE A 312   O  ILE A 316           
SHEET    5 AA2 5 VAL A 296  MET A 298 -1  N  ILE A 297   O  LEU A 311           
SHEET    1 AA3 2 ALA A 364  GLU A 366  0                                        
SHEET    2 AA3 2 GLY A 369  GLN A 371 -1  O  GLN A 371   N  ALA A 364           
SHEET    1 AA4 7 VAL B 206  LEU B 208  0                                        
SHEET    2 AA4 7 GLU B 225  GLU B 233 -1  O  LYS B 231   N  GLY B 207           
SHEET    3 AA4 7 ILE B 316  SER B 326  1  O  THR B 321   N  PHE B 230           
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 VAL B 206  LEU B 208  0                                        
SHEET    2 AA5 5 GLU B 225  GLU B 233 -1  O  LYS B 231   N  GLY B 207           
SHEET    3 AA5 5 ILE B 316  SER B 326  1  O  THR B 321   N  PHE B 230           
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           
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.10  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.37  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.17  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.25  
LINK         NE2 HIS B 390                ZN    ZN B 601     1555   1555  2.09  
LINK         SG  CYS B 396                ZN    ZN B 601     1555   1555  2.28  
LINK         SG  CYS B 397                ZN    ZN B 601     1555   1555  2.20  
LINK         SG  CYS B 404                ZN    ZN B 601     1555   1555  2.30  
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2  8 ARG A 376  LEU A 377  TYR A 436  HIS A 437                    
SITE     2 AC2  8 ASN A 482  LEU A 490  HOH A 721  HOH A 728                    
SITE     1 AC3  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
SITE     1 AC4  5 ARG A 300  ARG B 423  GLU B 511  PRO B 517                    
SITE     2 AC4  5 VAL B 518                                                     
SITE     1 AC5  6 ARG B 376  SER B 434  TYR B 436  ASN B 482                    
SITE     2 AC5  6 HOH B 717  HOH B 722                                          
SITE     1 AC6  5 LYS A 299  LEU A 311  ARG B 423  GLN B 507                    
SITE     2 AC6  5 TYR B 510                                                     
CRYST1  217.448   46.953   89.733  90.00 111.43  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      0.004599  0.000000  0.001805        0.00000                         
SCALE2      0.000000  0.021298  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011972        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system