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Database: PDB
Entry: 6GLC
LinkDB: 6GLC
Original site: 6GLC 
HEADER    LIGASE                                  23-MAY-18   6GLC              
TITLE     STRUCTURE OF PHOSPHO-PARKIN BOUND TO PHOSPHO-UBIQUITIN                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE PARKIN;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PARKIN,PARKIN RBR E3 UBIQUITIN-PROTEIN LIGASE,PARKINSON     
COMPND   5 JUVENILE DISEASE PROTEIN 2,PARKINSON DISEASE PROTEIN 2;              
COMPND   6 EC: 2.3.2.31;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: POLYUBIQUITIN-B;                                           
COMPND  10 CHAIN: B;                                                            
COMPND  11 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: PRKN, PARK2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: UBB;                                                           
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    UBIQUITIN, PARKIN, PHOSPHO-UBIQUITIN, PARKINSON'S DISEASE, E3 LIGASE, 
KEYWDS   2 RBR DOMAIN, MITOPHAGY, LIGASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.GLADKOVA,S.L.MASLEN,J.M.SKEHEL,D.KOMANDER                           
REVDAT   3   01-AUG-18 6GLC    1       JRNL                                     
REVDAT   2   18-JUL-18 6GLC    1       JRNL                                     
REVDAT   1   13-JUN-18 6GLC    0                                                
JRNL        AUTH   C.GLADKOVA,S.L.MASLEN,J.M.SKEHEL,D.KOMANDER                  
JRNL        TITL   MECHANISM OF PARKIN ACTIVATION BY PINK1.                     
JRNL        REF    NATURE                        V. 559   410 2018              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   29995846                                                     
JRNL        DOI    10.1038/S41586-018-0224-X                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.13_2998                                     
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 59.79                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.460                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 40229                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2020                            
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 59.8188 -  4.3379    1.00     2885   171  0.1562 0.1581        
REMARK   3     2  4.3379 -  3.4432    1.00     2790   140  0.1493 0.1733        
REMARK   3     3  3.4432 -  3.0080    1.00     2776   126  0.1816 0.1939        
REMARK   3     4  3.0080 -  2.7330    1.00     2746   128  0.1968 0.2281        
REMARK   3     5  2.7330 -  2.5371    1.00     2720   138  0.1892 0.2433        
REMARK   3     6  2.5371 -  2.3875    1.00     2693   165  0.2002 0.2615        
REMARK   3     7  2.3875 -  2.2679    1.00     2711   141  0.1890 0.2209        
REMARK   3     8  2.2679 -  2.1692    1.00     2740   132  0.1883 0.2338        
REMARK   3     9  2.1692 -  2.0857    1.00     2708   143  0.2026 0.2513        
REMARK   3    10  2.0857 -  2.0137    1.00     2658   156  0.2111 0.2750        
REMARK   3    11  2.0137 -  1.9507    1.00     2657   148  0.2132 0.2487        
REMARK   3    12  1.9507 -  1.8950    1.00     2734   141  0.2318 0.2649        
REMARK   3    13  1.8950 -  1.8451    1.00     2708   149  0.2625 0.2949        
REMARK   3    14  1.8451 -  1.8001    1.00     2683   142  0.2805 0.2958        
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)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.140           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.007           3135                                  
REMARK   3   ANGLE     :  0.863           4255                                  
REMARK   3   CHIRALITY :  0.056            483                                  
REMARK   3   PLANARITY :  0.005            550                                  
REMARK   3   DIHEDRAL  :  9.941           2600                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.6329 -26.8647 -16.2338              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1784 T22:   0.2594                                     
REMARK   3      T33:   0.2549 T12:  -0.0097                                     
REMARK   3      T13:   0.0429 T23:   0.0543                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8967 L22:   1.1407                                     
REMARK   3      L33:   2.0369 L12:  -0.1595                                     
REMARK   3      L13:   0.6828 L23:   0.2808                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0639 S12:   0.2440 S13:   0.1220                       
REMARK   3      S21:  -0.0855 S22:  -0.0894 S23:  -0.1474                       
REMARK   3      S31:  -0.2512 S32:   0.1791 S33:   0.0308                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6GLC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010172.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-APR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96859                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIALS                              
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40324                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 72.690                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.77300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5N2W, 5C1Z                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5% (W/V) PEG 1000, 12.5% (W/V) PEG    
REMARK 280  3350, 12.5% (V/V) MPD, 0.03 M OF EACH SODIUM NITRATE, DISODIUM      
REMARK 280  HYDROGEN PHOSPHATE, AMMONIUM SULPHATE, 0.1 M MOPS/HEPES-NA (PH      
REMARK 280  7.5), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.07933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       35.03967            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       35.03967            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       70.07933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 228  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 231  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 233  LIES ON A SPECIAL POSITION.                          
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     GLY A    -1                                                      
REMARK 465     PRO A    73                                                      
REMARK 465     TRP A    74                                                      
REMARK 465     ARG A    75                                                      
REMARK 465     LYS A    76                                                      
REMARK 465     GLY A    77                                                      
REMARK 465     GLN A    78                                                      
REMARK 465     GLU A    79                                                      
REMARK 465     MET A    80                                                      
REMARK 465     ASN A    81                                                      
REMARK 465     ALA A    82                                                      
REMARK 465     THR A    83                                                      
REMARK 465     GLY A    84                                                      
REMARK 465     GLY A    85                                                      
REMARK 465     ASP A    86                                                      
REMARK 465     ASP A    87                                                      
REMARK 465     PRO A    88                                                      
REMARK 465     ARG A    89                                                      
REMARK 465     ASN A    90                                                      
REMARK 465     ALA A    91                                                      
REMARK 465     ALA A    92                                                      
REMARK 465     GLY A    93                                                      
REMARK 465     GLY A    94                                                      
REMARK 465     CYS A    95                                                      
REMARK 465     GLU A    96                                                      
REMARK 465     ARG A    97                                                      
REMARK 465     GLU A    98                                                      
REMARK 465     PRO A    99                                                      
REMARK 465     SER A   109                                                      
REMARK 465     SER A   110                                                      
REMARK 465     VAL A   111                                                      
REMARK 465     LEU A   112                                                      
REMARK 465     PRO A   113                                                      
REMARK 465     GLY A   114                                                      
REMARK 465     ASP A   115                                                      
REMARK 465     SER A   116                                                      
REMARK 465     VAL A   117                                                      
REMARK 465     GLY A   118                                                      
REMARK 465     LEU A   119                                                      
REMARK 465     ALA A   120                                                      
REMARK 465     VAL A   121                                                      
REMARK 465     ILE A   122                                                      
REMARK 465     LEU A   123                                                      
REMARK 465     HIS A   124                                                      
REMARK 465     THR A   125                                                      
REMARK 465     ASP A   126                                                      
REMARK 465     SER A   127                                                      
REMARK 465     ARG A   128                                                      
REMARK 465     LYS A   129                                                      
REMARK 465     ASP A   130                                                      
REMARK 465     SER A   131                                                      
REMARK 465     PRO A   132                                                      
REMARK 465     PRO A   133                                                      
REMARK 465     ALA A   134                                                      
REMARK 465     GLY A   135                                                      
REMARK 465     SER A   136                                                      
REMARK 465     PRO A   137                                                      
REMARK 465     ALA A   138                                                      
REMARK 465     GLY A   139                                                      
REMARK 465     ARG A   140                                                      
REMARK 465     SER A   141                                                      
REMARK 465     ILE A   142                                                      
REMARK 465     GLY A   354                                                      
REMARK 465     GLY A   355                                                      
REMARK 465     ALA A   379                                                      
REMARK 465     VAL A   380                                                      
REMARK 465     PHE A   381                                                      
REMARK 465     GLU A   382                                                      
REMARK 465     ASN A   383                                                      
REMARK 465     LEU A   384                                                      
REMARK 465     TYR A   385                                                      
REMARK 465     PHE A   386                                                      
REMARK 465     GLN A   387                                                      
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     GLN A  40    CD   OE1  NE2                                       
REMARK 470     ARG A  42    CZ   NH1  NH2                                       
REMARK 470     LYS A  48    CD   CE   NZ                                        
REMARK 470     ARG A  51    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A  72    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 100    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 106    CG   OD1  OD2                                       
REMARK 470     GLN A 178    CG   CD   OE1  NE2                                  
REMARK 470     HIS A 200    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 282    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 310    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 334    CZ   NH1  NH2                                       
REMARK 470     GLU A 353    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 356    CG   OD1  ND2                                       
REMARK 470     GLU B  24    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  54    CZ   NH1  NH2                                       
REMARK 470     LYS B  63    CD   CE   NZ                                        
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    CYS A   201     O    HOH A   601              2.12            
REMARK 500   O    LEU A   358     O    HOH A   602              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    ASN A 144       78.02     57.79                                   
REMARK 500    CYS A 337      -97.79   -108.97                                   
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 506  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 150   SG                                                     
REMARK 620 2 CYS A 154   SG  110.0                                              
REMARK 620 3 CYS A 212   SG  111.6 114.7                                        
REMARK 620 4 HIS A 215   NE2 111.9 104.5 103.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 166   SG                                                     
REMARK 620 2 CYS A 169   SG  109.4                                              
REMARK 620 3 CYS A 196   SG  106.1 109.8                                        
REMARK 620 4 CYS A 201   SG  100.4 122.1 107.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 238   SG                                                     
REMARK 620 2 CYS A 241   SG  105.2                                              
REMARK 620 3 CYS A 260   SG  113.2 116.5                                        
REMARK 620 4 CYS A 263   SG  112.4 107.6 102.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 253   SG                                                     
REMARK 620 2 HIS A 257   ND1 108.9                                              
REMARK 620 3 CYS A 289   SG  116.1 100.1                                        
REMARK 620 4 CYS A 293   SG  114.0 102.4 113.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 505  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 332   SG                                                     
REMARK 620 2 CYS A 337   SG  112.0                                              
REMARK 620 3 CYS A 352   SG  111.7 104.0                                        
REMARK 620 4 CYS A 360   SG  106.8 112.8 109.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 365   SG                                                     
REMARK 620 2 CYS A 368   SG  108.1                                              
REMARK 620 3 HIS A 373   NE2 112.4 104.2                                        
REMARK 620 4 CYS A 377   SG  107.1 115.7 109.4                                  
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 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 101                 
DBREF  6GLC A    1   382  UNP    O60260   PRKN_HUMAN       1    382             
DBREF  6GLC B    1    76  UNP    P0CG47   UBB_HUMAN        1     76             
SEQADV 6GLC GLY A   -1  UNP  O60260              EXPRESSION TAG                 
SEQADV 6GLC PRO A    0  UNP  O60260              EXPRESSION TAG                 
SEQADV 6GLC CYS A  347  UNP  O60260    GLN   347 ENGINEERED MUTATION            
SEQADV 6GLC ASN A  383  UNP  O60260              EXPRESSION TAG                 
SEQADV 6GLC LEU A  384  UNP  O60260              EXPRESSION TAG                 
SEQADV 6GLC TYR A  385  UNP  O60260              EXPRESSION TAG                 
SEQADV 6GLC PHE A  386  UNP  O60260              EXPRESSION TAG                 
SEQADV 6GLC GLN A  387  UNP  O60260              EXPRESSION TAG                 
SEQADV 6GLC 3CN B   76  UNP  P0CG47    GLY    76 ENGINEERED MUTATION            
SEQRES   1 A  389  GLY PRO MET ILE VAL PHE VAL ARG PHE ASN SER SER HIS          
SEQRES   2 A  389  GLY PHE PRO VAL GLU VAL ASP SER ASP THR SER ILE PHE          
SEQRES   3 A  389  GLN LEU LYS GLU VAL VAL ALA LYS ARG GLN GLY VAL PRO          
SEQRES   4 A  389  ALA ASP GLN LEU ARG VAL ILE PHE ALA GLY LYS GLU LEU          
SEQRES   5 A  389  ARG ASN ASP TRP THR VAL GLN ASN CYS ASP LEU ASP GLN          
SEQRES   6 A  389  GLN SEP ILE VAL HIS ILE VAL GLN ARG PRO TRP ARG LYS          
SEQRES   7 A  389  GLY GLN GLU MET ASN ALA THR GLY GLY ASP ASP PRO ARG          
SEQRES   8 A  389  ASN ALA ALA GLY GLY CYS GLU ARG GLU PRO GLN SER LEU          
SEQRES   9 A  389  THR ARG VAL ASP LEU SER SER SER VAL LEU PRO GLY ASP          
SEQRES  10 A  389  SER VAL GLY LEU ALA VAL ILE LEU HIS THR ASP SER ARG          
SEQRES  11 A  389  LYS ASP SER PRO PRO ALA GLY SER PRO ALA GLY ARG SER          
SEQRES  12 A  389  ILE TYR ASN SER PHE TYR VAL TYR CYS LYS GLY PRO CYS          
SEQRES  13 A  389  GLN ARG VAL GLN PRO GLY LYS LEU ARG VAL GLN CYS SER          
SEQRES  14 A  389  THR CYS ARG GLN ALA THR LEU THR LEU THR GLN GLY PRO          
SEQRES  15 A  389  SER CYS TRP ASP ASP VAL LEU ILE PRO ASN ARG MET SER          
SEQRES  16 A  389  GLY GLU CYS GLN SER PRO HIS CYS PRO GLY THR SER ALA          
SEQRES  17 A  389  GLU PHE PHE PHE LYS CYS GLY ALA HIS PRO THR SER ASP          
SEQRES  18 A  389  LYS GLU THR SER VAL ALA LEU HIS LEU ILE ALA THR ASN          
SEQRES  19 A  389  SER ARG ASN ILE THR CYS ILE THR CYS THR ASP VAL ARG          
SEQRES  20 A  389  SER PRO VAL LEU VAL PHE GLN CYS ASN SER ARG HIS VAL          
SEQRES  21 A  389  ILE CYS LEU ASP CYS PHE HIS LEU TYR CYS VAL THR ARG          
SEQRES  22 A  389  LEU ASN ASP ARG GLN PHE VAL HIS ASP PRO GLN LEU GLY          
SEQRES  23 A  389  TYR SER LEU PRO CYS VAL ALA GLY CYS PRO ASN SER LEU          
SEQRES  24 A  389  ILE LYS GLU LEU HIS HIS PHE ARG ILE LEU GLY GLU GLU          
SEQRES  25 A  389  GLN TYR ASN ARG TYR GLN GLN TYR GLY ALA GLU GLU CYS          
SEQRES  26 A  389  VAL LEU GLN MET GLY GLY VAL LEU CYS PRO ARG PRO GLY          
SEQRES  27 A  389  CYS GLY ALA GLY LEU LEU PRO GLU PRO ASP CYS ARG LYS          
SEQRES  28 A  389  VAL THR CYS GLU GLY GLY ASN GLY LEU GLY CYS GLY PHE          
SEQRES  29 A  389  ALA PHE CYS ARG GLU CYS LYS GLU ALA TYR HIS GLU GLY          
SEQRES  30 A  389  GLU CYS SER ALA VAL PHE GLU ASN LEU TYR PHE GLN              
SEQRES   1 B   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 B   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 B   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 B   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 B   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SEP          
SEQRES   6 B   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY 3CN                  
MODRES 6GLC SEP A   65  SER  MODIFIED RESIDUE                                   
MODRES 6GLC SEP B   65  SER  MODIFIED RESIDUE                                   
HET    SEP  A  65      10                                                       
HET    SEP  B  65      10                                                       
HET    3CN  B  76       4                                                       
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET     ZN  A 504       1                                                       
HET     ZN  A 505       1                                                       
HET     ZN  A 506       1                                                       
HET    GOL  A 507       6                                                       
HET    GOL  A 508       6                                                       
HET    GOL  A 509       6                                                       
HET    MPD  A 510       8                                                       
HET    SO4  B 101       5                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     3CN 3-AMINOPROPANE                                                   
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETNAM     SO4 SULFATE ION                                                      
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   2  3CN    C3 H9 N                                                      
FORMUL   3   ZN    6(ZN 2+)                                                     
FORMUL   9  GOL    3(C3 H8 O3)                                                  
FORMUL  12  MPD    C6 H14 O2                                                    
FORMUL  13  SO4    O4 S 2-                                                      
FORMUL  14  HOH   *165(H2 O)                                                    
HELIX    1 AA1 SER A   22  GLY A   35  1                                  14    
HELIX    2 AA2 PRO A   37  ASP A   39  5                                   3    
HELIX    3 AA3 VAL A   56  ASP A   60  5                                   5    
HELIX    4 AA4 SER A  101  VAL A  105  5                                   5    
HELIX    5 AA5 CYS A  182  ILE A  188  1                                   7    
HELIX    6 AA6 LEU A  261  ASP A  274  1                                  14    
HELIX    7 AA7 GLU A  300  LEU A  307  5                                   8    
HELIX    8 AA8 GLY A  308  MET A  327  1                                  20    
HELIX    9 AA9 THR B   22  GLY B   35  1                                  14    
HELIX   10 AB1 PRO B   37  ASP B   39  5                                   3    
HELIX   11 AB2 LEU B   56  ASN B   60  5                                   5    
SHEET    1 AA1 5 PHE A  13  VAL A  17  0                                        
SHEET    2 AA1 5 MET A   1  PHE A   7 -1  N  MET A   1   O  VAL A  17           
SHEET    3 AA1 5 ILE A  66  GLN A  71  1  O  VAL A  67   N  PHE A   4           
SHEET    4 AA1 5 LEU A  41  PHE A  45 -1  N  ILE A  44   O  HIS A  68           
SHEET    5 AA1 5 LYS A  48  LEU A  50 -1  O  LYS A  48   N  PHE A  45           
SHEET    1 AA2 4 ALA A 206  CYS A 212  0                                        
SHEET    2 AA2 4 ARG A 156  CYS A 166 -1  N  ARG A 163   O  PHE A 209           
SHEET    3 AA2 4 PHE A 146  CYS A 150 -1  N  PHE A 146   O  GLY A 160           
SHEET    4 AA2 4 VAL A 224  ALA A 225 -1  O  VAL A 224   N  TYR A 149           
SHEET    1 AA3 2 LEU A 174  LEU A 176  0                                        
SHEET    2 AA3 2 GLY A 194  CYS A 196 -1  O  GLU A 195   N  THR A 175           
SHEET    1 AA4 3 ILE A 229  ALA A 230  0                                        
SHEET    2 AA4 3 VAL A 248  VAL A 250 -1  O  VAL A 248   N  ALA A 230           
SHEET    3 AA4 3 VAL A 258  CYS A 260 -1  O  ILE A 259   N  LEU A 249           
SHEET    1 AA5 2 VAL A 278  ASP A 280  0                                        
SHEET    2 AA5 2 GLY A 284  SER A 286 -1  O  SER A 286   N  VAL A 278           
SHEET    1 AA6 5 VAL A 330  LEU A 331  0                                        
SHEET    2 AA6 5 GLY A 340  LEU A 342 -1  O  LEU A 341   N  VAL A 330           
SHEET    3 AA6 5 THR B  66  ARG B  72  1  O  LEU B  71   N  LEU A 342           
SHEET    4 AA6 5 GLN B   2  THR B   7  1  N  PHE B   4   O  LEU B  67           
SHEET    5 AA6 5 THR B  12  GLU B  16 -1  O  ILE B  13   N  VAL B   5           
SHEET    1 AA7 5 VAL A 330  LEU A 331  0                                        
SHEET    2 AA7 5 GLY A 340  LEU A 342 -1  O  LEU A 341   N  VAL A 330           
SHEET    3 AA7 5 THR B  66  ARG B  72  1  O  LEU B  71   N  LEU A 342           
SHEET    4 AA7 5 GLN B  41  PHE B  45 -1  N  ILE B  44   O  HIS B  68           
SHEET    5 AA7 5 LYS B  48  GLN B  49 -1  O  LYS B  48   N  PHE B  45           
SHEET    1 AA8 2 LYS A 349  THR A 351  0                                        
SHEET    2 AA8 2 ALA A 363  CYS A 365 -1  O  PHE A 364   N  VAL A 350           
LINK         C   GLN A  64                 N   SEP A  65     1555   1555  1.33  
LINK         C   SEP A  65                 N   ILE A  66     1555   1555  1.33  
LINK         SG  CYS A 150                ZN    ZN A 506     1555   1555  2.36  
LINK         SG  CYS A 154                ZN    ZN A 506     1555   1555  2.35  
LINK         SG  CYS A 166                ZN    ZN A 503     1555   1555  2.41  
LINK         SG  CYS A 169                ZN    ZN A 503     1555   1555  2.34  
LINK         SG  CYS A 196                ZN    ZN A 503     1555   1555  2.13  
LINK         SG  CYS A 201                ZN    ZN A 503     1555   1555  2.45  
LINK         SG  CYS A 212                ZN    ZN A 506     1555   1555  2.27  
LINK         NE2 HIS A 215                ZN    ZN A 506     1555   1555  2.00  
LINK         SG  CYS A 238                ZN    ZN A 504     1555   1555  2.43  
LINK         SG  CYS A 241                ZN    ZN A 504     1555   1555  2.32  
LINK         SG  CYS A 253                ZN    ZN A 501     1555   1555  2.29  
LINK         ND1 HIS A 257                ZN    ZN A 501     1555   1555  2.19  
LINK         SG  CYS A 260                ZN    ZN A 504     1555   1555  2.36  
LINK         SG  CYS A 263                ZN    ZN A 504     1555   1555  2.36  
LINK         SG  CYS A 289                ZN    ZN A 501     1555   1555  2.31  
LINK         SG  CYS A 293                ZN    ZN A 501     1555   1555  2.27  
LINK         SG  CYS A 332                ZN    ZN A 505     1555   1555  2.33  
LINK         SG  CYS A 337                ZN    ZN A 505     1555   1555  2.29  
LINK         SG  CYS A 347                 CA  3CN B  76     1555   1555  1.66  
LINK         SG  CYS A 352                ZN    ZN A 505     1555   1555  2.37  
LINK         SG  CYS A 360                ZN    ZN A 505     1555   1555  2.28  
LINK         SG  CYS A 365                ZN    ZN A 502     1555   1555  2.35  
LINK         SG  CYS A 368                ZN    ZN A 502     1555   1555  2.25  
LINK         NE2 HIS A 373                ZN    ZN A 502     1555   1555  2.01  
LINK         SG  CYS A 377                ZN    ZN A 502     1555   1555  2.39  
LINK         C   GLU B  64                 N   SEP B  65     1555   1555  1.33  
LINK         C   SEP B  65                 N   THR B  66     1555   1555  1.33  
LINK         C   GLY B  75                 ND  3CN B  76     1555   1555  1.35  
CISPEP   1 GLY A  152    PRO A  153          0         7.41                     
CISPEP   2 SER A  246    PRO A  247          0        -6.42                     
SITE     1 AC1  4 CYS A 253  HIS A 257  CYS A 289  CYS A 293                    
SITE     1 AC2  4 CYS A 365  CYS A 368  HIS A 373  CYS A 377                    
SITE     1 AC3  4 CYS A 166  CYS A 169  CYS A 196  CYS A 201                    
SITE     1 AC4  4 CYS A 238  CYS A 241  CYS A 260  CYS A 263                    
SITE     1 AC5  4 CYS A 332  CYS A 337  CYS A 352  CYS A 360                    
SITE     1 AC6  4 CYS A 150  CYS A 154  CYS A 212  HIS A 215                    
SITE     1 AC7  3 PRO A  14  GLU A  16  CYS A 263                               
SITE     1 AC8  3 PRO A  14  ARG A 245  CYS A 263                               
SITE     1 AC9  6 PHE A   4  GLY A  12  ILE A  66  SER A 218                    
SITE     2 AC9  6 THR A 242  HOH A 649                                          
SITE     1 AD1  7 LYS A 299  GLU A 300  LEU A 301  HIS A 302                    
SITE     2 AD1  7 PHE B  45  ASP B  58  TYR B  59                               
SITE     1 AD2  3 ARG B  42  ARG B  72  ARG B  74                               
CRYST1   83.931   83.931  105.119  90.00  90.00 120.00 P 32 2 1      6          
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      0.011915  0.006879  0.000000        0.00000                         
SCALE2      0.000000  0.013758  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009513        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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