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Database: PDB
Entry: 5C9V
LinkDB: 5C9V
Original site: 5C9V 
HEADER    SIGNALING PROTEIN                       29-JUN-15   5C9V              
TITLE     STRUCTURE OF HUMAN PARKIN G319A                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE PARKIN;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 137-465;                                      
COMPND   5 SYNONYM: PARKIN,PARKINSON JUVENILE DISEASE PROTEIN 2,PARKINSON       
COMPND   6 DISEASE PROTEIN 2;                                                   
COMPND   7 EC: 6.3.2.-;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 OTHER_DETAILS: ENGINEERED MUTATION AT POSITION G319A                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PARK2, PRKN;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: POPINK                                    
KEYWDS    PARKIN, UBIQUITIN, E3 LIGASE, RBR, PARKINSON'S DISEASE, MITOPHAGY,    
KEYWDS   2 CELL SIGNALLING, SIGNALING PROTEIN                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.WAUER,D.KOMANDER                                                    
REVDAT   4   13-SEP-17 5C9V    1       REMARK                                   
REVDAT   3   26-AUG-15 5C9V    1       JRNL                                     
REVDAT   2   29-JUL-15 5C9V    1       JRNL                                     
REVDAT   1   22-JUL-15 5C9V    0                                                
JRNL        AUTH   T.WAUER,M.SIMICEK,A.SCHUBERT,D.KOMANDER                      
JRNL        TITL   MECHANISM OF PHOSPHO-UBIQUITIN-INDUCED PARKIN ACTIVATION.    
JRNL        REF    NATURE                        V. 524   370 2015              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   26161729                                                     
JRNL        DOI    10.1038/NATURE14879                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.WAUER,D.KOMANDER                                           
REMARK   1  TITL   STRUCTURE OF THE HUMAN PARKIN LIGASE DOMAIN IN AN            
REMARK   1  TITL 2 AUTOINHIBITED STATE.                                         
REMARK   1  REF    EMBO J.                       V.  32  2099 2013              
REMARK   1  REFN                   ESSN 1460-2075                               
REMARK   1  PMID   23727886                                                     
REMARK   1  DOI    10.1038/EMBOJ.2013.125                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 84.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 22270                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.150                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1148                            
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 84.7350 -  4.6998    1.00     2724   143  0.1701 0.1904        
REMARK   3     2  4.6998 -  3.7304    1.00     2681   131  0.1585 0.2267        
REMARK   3     3  3.7304 -  3.2588    1.00     2616   147  0.1981 0.2167        
REMARK   3     4  3.2588 -  2.9608    1.00     2634   148  0.2282 0.2211        
REMARK   3     5  2.9608 -  2.7486    1.00     2641   132  0.2522 0.2630        
REMARK   3     6  2.7486 -  2.5865    1.00     2638   137  0.2528 0.2808        
REMARK   3     7  2.5865 -  2.4570    1.00     2590   158  0.2624 0.3119        
REMARK   3     8  2.4570 -  2.3500    1.00     2598   152  0.2722 0.2852        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.800           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           2450                                  
REMARK   3   ANGLE     :  0.691           3324                                  
REMARK   3   CHIRALITY :  0.029            346                                  
REMARK   3   PLANARITY :  0.003            432                                  
REMARK   3   DIHEDRAL  : 13.913            872                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   7.8845  31.4194  36.9402              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3663 T22:   0.3066                                     
REMARK   3      T33:   0.2457 T12:  -0.0140                                     
REMARK   3      T13:   0.0139 T23:   0.0305                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1353 L22:   1.2053                                     
REMARK   3      L33:   0.6839 L12:   1.1426                                     
REMARK   3      L13:   0.0605 L23:  -0.1762                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0275 S12:   0.2777 S13:  -0.0836                       
REMARK   3      S21:   0.0212 S22:   0.0596 S23:  -0.0111                       
REMARK   3      S31:  -0.0069 S32:   0.0155 S33:  -0.0337                       
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 5C9V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211277.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91730                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22270                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 86.680                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 4BM9                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M LITHIUM SULPHATE, 0.01 M MGCL2,    
REMARK 280  0.05 M MES PH 5.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  291K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-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        0.00000            
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        0.00000            
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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       84.68000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       48.89002            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       32.33000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       84.68000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       48.89002            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       32.33000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       84.68000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       48.89002            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       32.33000            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       84.68000            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       48.89002            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       32.33000            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       84.68000            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       48.89002            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       32.33000            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       84.68000            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       48.89002            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       32.33000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       97.78004            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       64.66000            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       97.78004            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       64.66000            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       97.78004            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       64.66000            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       97.78004            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       64.66000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       97.78004            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       64.66000            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       97.78004            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       64.66000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL                        
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 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 S    SO4 A 510  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 601  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 632  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 680  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   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     GLY A   354                                                      
REMARK 465     GLY A   355                                                      
REMARK 465     ASN A   356                                                      
REMARK 465     GLY A   385                                                      
REMARK 465     THR A   386                                                      
REMARK 465     THR A   387                                                      
REMARK 465     THR A   388                                                      
REMARK 465     GLN A   389                                                      
REMARK 465     ALA A   390                                                      
REMARK 465     ALA A   405                                                      
REMARK 465     ALA A   406                                                      
REMARK 465     SER A   407                                                      
REMARK 465     LYS A   408                                                      
REMARK 465     GLU A   409                                                      
REMARK 465     THR A   410                                                      
REMARK 465     ILE A   411                                                      
REMARK 465     LYS A   412                                                      
REMARK 465     LYS A   413                                                      
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     ILE A 142    CG1  CG2  CD1                                       
REMARK 470     GLU A 195    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 234    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 282    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 283    CG   CD1  CD2                                       
REMARK 470     GLU A 310    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 344    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 346    CG   OD1  OD2                                       
REMARK 470     GLN A 347    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 358    CG   CD1  CD2                                       
REMARK 470     GLU A 374    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 392    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 399    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 426    CG   CD   OE1  OE2                                  
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    CYS A 337      -78.17   -103.63                                   
REMARK 500    ALA A 401       36.22    -82.42                                   
REMARK 500    CYS A 441      -74.22   -111.20                                   
REMARK 500    HIS A 461       59.53   -161.77                                   
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 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 150   SG                                                     
REMARK 620 2 CYS A 154   SG  110.8                                              
REMARK 620 3 CYS A 212   SG  113.7 113.2                                        
REMARK 620 4 HIS A 215   NE2 109.1  99.7 109.5                                  
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 166   SG                                                     
REMARK 620 2 CYS A 169   SG  110.0                                              
REMARK 620 3 CYS A 196   SG  107.4 112.1                                        
REMARK 620 4 CYS A 201   SG  106.0 108.1 113.0                                  
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 238   SG                                                     
REMARK 620 2 CYS A 241   SG  110.2                                              
REMARK 620 3 CYS A 260   SG  114.4 117.1                                        
REMARK 620 4 CYS A 263   SG  109.3 105.6  99.0                                  
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 253   SG                                                     
REMARK 620 2 HIS A 257   ND1 100.7                                              
REMARK 620 3 CYS A 289   SG  111.7  97.1                                        
REMARK 620 4 CYS A 293   SG  120.9 109.6 113.3                                  
REMARK 620 N                    1     2     3                                   
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 332   SG                                                     
REMARK 620 2 CYS A 337   SG  119.8                                              
REMARK 620 3 CYS A 352   SG  108.0 104.0                                        
REMARK 620 4 CYS A 360   SG  108.0 114.2 100.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 507  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 365   SG                                                     
REMARK 620 2 CYS A 368   SG  110.6                                              
REMARK 620 3 HIS A 373   NE2 105.3 106.5                                        
REMARK 620 4 CYS A 377   SG  105.1 121.7 106.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 508  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 418   SG                                                     
REMARK 620 2 CYS A 421   SG  114.5                                              
REMARK 620 3 CYS A 436   SG  111.8 101.3                                        
REMARK 620 4 CYS A 441   SG  104.0 115.8 109.7                                  
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 446   SG                                                     
REMARK 620 2 CYS A 449   SG  115.0                                              
REMARK 620 3 CYS A 457   SG  113.5 112.3                                        
REMARK 620 4 HIS A 461   NE2 106.0  99.3 109.5                                  
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 ZN A 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 517                 
DBREF  5C9V A  137   465  UNP    O60260   PRKN2_HUMAN    137    465             
SEQADV 5C9V GLY A  136  UNP  O60260              EXPRESSION TAG                 
SEQADV 5C9V ALA A  319  UNP  O60260    GLY   319 ENGINEERED MUTATION            
SEQRES   1 A  330  GLY PRO ALA GLY ARG SER ILE TYR ASN SER PHE TYR VAL          
SEQRES   2 A  330  TYR CYS LYS GLY PRO CYS GLN ARG VAL GLN PRO GLY LYS          
SEQRES   3 A  330  LEU ARG VAL GLN CYS SER THR CYS ARG GLN ALA THR LEU          
SEQRES   4 A  330  THR LEU THR GLN GLY PRO SER CYS TRP ASP ASP VAL LEU          
SEQRES   5 A  330  ILE PRO ASN ARG MET SER GLY GLU CYS GLN SER PRO HIS          
SEQRES   6 A  330  CYS PRO GLY THR SER ALA GLU PHE PHE PHE LYS CYS GLY          
SEQRES   7 A  330  ALA HIS PRO THR SER ASP LYS GLU THR SER VAL ALA LEU          
SEQRES   8 A  330  HIS LEU ILE ALA THR ASN SER ARG ASN ILE THR CYS ILE          
SEQRES   9 A  330  THR CYS THR ASP VAL ARG SER PRO VAL LEU VAL PHE GLN          
SEQRES  10 A  330  CYS ASN SER ARG HIS VAL ILE CYS LEU ASP CYS PHE HIS          
SEQRES  11 A  330  LEU TYR CYS VAL THR ARG LEU ASN ASP ARG GLN PHE VAL          
SEQRES  12 A  330  HIS ASP PRO GLN LEU GLY TYR SER LEU PRO CYS VAL ALA          
SEQRES  13 A  330  GLY CYS PRO ASN SER LEU ILE LYS GLU LEU HIS HIS PHE          
SEQRES  14 A  330  ARG ILE LEU GLY GLU GLU GLN TYR ASN ARG TYR GLN GLN          
SEQRES  15 A  330  TYR ALA ALA GLU GLU CYS VAL LEU GLN MET GLY GLY VAL          
SEQRES  16 A  330  LEU CYS PRO ARG PRO GLY CYS GLY ALA GLY LEU LEU PRO          
SEQRES  17 A  330  GLU PRO ASP GLN ARG LYS VAL THR CYS GLU GLY GLY ASN          
SEQRES  18 A  330  GLY LEU GLY CYS GLY PHE ALA PHE CYS ARG GLU CYS LYS          
SEQRES  19 A  330  GLU ALA TYR HIS GLU GLY GLU CYS SER ALA VAL PHE GLU          
SEQRES  20 A  330  ALA SER GLY THR THR THR GLN ALA TYR ARG VAL ASP GLU          
SEQRES  21 A  330  ARG ALA ALA GLU GLN ALA ARG TRP GLU ALA ALA SER LYS          
SEQRES  22 A  330  GLU THR ILE LYS LYS THR THR LYS PRO CYS PRO ARG CYS          
SEQRES  23 A  330  HIS VAL PRO VAL GLU LYS ASN GLY GLY CYS MET HIS MET          
SEQRES  24 A  330  LYS CYS PRO GLN PRO GLN CYS ARG LEU GLU TRP CYS TRP          
SEQRES  25 A  330  ASN CYS GLY CYS GLU TRP ASN ARG VAL CYS MET GLY ASP          
SEQRES  26 A  330  HIS TRP PHE ASP VAL                                          
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     ZN  A 507       1                                                       
HET     ZN  A 508       1                                                       
HET    SO4  A 509       5                                                       
HET    SO4  A 510       5                                                       
HET    SO4  A 511       5                                                       
HET    SO4  A 512       5                                                       
HET    SO4  A 513       5                                                       
HET    SO4  A 514       5                                                       
HET    GOL  A 515       6                                                       
HET    GOL  A 516       6                                                       
HET    GOL  A 517       6                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   ZN    8(ZN 2+)                                                     
FORMUL  10  SO4    6(O4 S 2-)                                                   
FORMUL  16  GOL    3(C3 H8 O3)                                                  
FORMUL  19  HOH   *81(H2 O)                                                     
HELIX    1 AA1 CYS A  182  ILE A  188  1                                   7    
HELIX    2 AA2 LEU A  261  ASP A  274  1                                  14    
HELIX    3 AA3 GLU A  300  LEU A  307  5                                   8    
HELIX    4 AA4 GLY A  308  GLN A  317  1                                  10    
HELIX    5 AA5 GLN A  317  GLN A  326  1                                  10    
HELIX    6 AA6 SER A  378  ALA A  383  1                                   6    
HELIX    7 AA7 ASP A  394  ALA A  401  1                                   8    
HELIX    8 AA8 ASN A  454  TRP A  462  1                                   9    
SHEET    1 AA1 4 ALA A 206  CYS A 212  0                                        
SHEET    2 AA1 4 ARG A 156  CYS A 166 -1  N  LYS A 161   O  LYS A 211           
SHEET    3 AA1 4 TYR A 147  CYS A 150 -1  N  VAL A 148   O  GLN A 158           
SHEET    4 AA1 4 VAL A 224  ALA A 225 -1  O  VAL A 224   N  TYR A 149           
SHEET    1 AA2 2 LEU A 174  LEU A 176  0                                        
SHEET    2 AA2 2 GLY A 194  CYS A 196 -1  O  GLU A 195   N  THR A 175           
SHEET    1 AA3 3 ILE A 229  ALA A 230  0                                        
SHEET    2 AA3 3 VAL A 248  VAL A 250 -1  O  VAL A 248   N  ALA A 230           
SHEET    3 AA3 3 VAL A 258  CYS A 260 -1  O  ILE A 259   N  LEU A 249           
SHEET    1 AA4 2 VAL A 278  ASP A 280  0                                        
SHEET    2 AA4 2 GLY A 284  SER A 286 -1  O  SER A 286   N  VAL A 278           
SHEET    1 AA5 2 VAL A 330  LEU A 331  0                                        
SHEET    2 AA5 2 GLY A 340  LEU A 341 -1  O  LEU A 341   N  VAL A 330           
SHEET    1 AA6 2 LYS A 349  THR A 351  0                                        
SHEET    2 AA6 2 ALA A 363  CYS A 365 -1  O  PHE A 364   N  VAL A 350           
SHEET    1 AA7 2 THR A 415  PRO A 417  0                                        
SHEET    2 AA7 2 PRO A 424  GLU A 426 -1  O  VAL A 425   N  LYS A 416           
SHEET    1 AA8 2 HIS A 433  LYS A 435  0                                        
SHEET    2 AA8 2 GLU A 444  CYS A 446 -1  O  TRP A 445   N  MET A 434           
LINK         SG  CYS A 150                ZN    ZN A 501     1555   1555  2.26  
LINK         SG  CYS A 154                ZN    ZN A 501     1555   1555  2.44  
LINK         SG  CYS A 166                ZN    ZN A 504     1555   1555  2.40  
LINK         SG  CYS A 169                ZN    ZN A 504     1555   1555  2.29  
LINK         SG  CYS A 196                ZN    ZN A 504     1555   1555  2.29  
LINK         SG  CYS A 201                ZN    ZN A 504     1555   1555  2.29  
LINK         SG  CYS A 212                ZN    ZN A 501     1555   1555  2.27  
LINK         NE2 HIS A 215                ZN    ZN A 501     1555   1555  2.00  
LINK         SG  CYS A 238                ZN    ZN A 505     1555   1555  2.38  
LINK         SG  CYS A 241                ZN    ZN A 505     1555   1555  2.35  
LINK         SG  CYS A 253                ZN    ZN A 502     1555   1555  2.34  
LINK         ND1 HIS A 257                ZN    ZN A 502     1555   1555  2.05  
LINK         SG  CYS A 260                ZN    ZN A 505     1555   1555  2.26  
LINK         SG  CYS A 263                ZN    ZN A 505     1555   1555  2.36  
LINK         SG  CYS A 289                ZN    ZN A 502     1555   1555  2.38  
LINK         SG  CYS A 293                ZN    ZN A 502     1555   1555  2.29  
LINK         SG  CYS A 332                ZN    ZN A 506     1555   1555  2.34  
LINK         SG  CYS A 337                ZN    ZN A 506     1555   1555  2.27  
LINK         SG  CYS A 352                ZN    ZN A 506     1555   1555  2.26  
LINK         SG  CYS A 360                ZN    ZN A 506     1555   1555  2.44  
LINK         SG  CYS A 365                ZN    ZN A 507     1555   1555  2.31  
LINK         SG  CYS A 368                ZN    ZN A 507     1555   1555  2.26  
LINK         NE2 HIS A 373                ZN    ZN A 507     1555   1555  2.08  
LINK         SG  CYS A 377                ZN    ZN A 507     1555   1555  2.35  
LINK         SG  CYS A 418                ZN    ZN A 508     1555   1555  2.31  
LINK         SG  CYS A 421                ZN    ZN A 508     1555   1555  2.28  
LINK         SG  CYS A 436                ZN    ZN A 508     1555   1555  2.32  
LINK         SG  CYS A 441                ZN    ZN A 508     1555   1555  2.33  
LINK         SG  CYS A 446                ZN    ZN A 503     1555   1555  2.30  
LINK         SG  CYS A 449                ZN    ZN A 503     1555   1555  2.39  
LINK         SG  CYS A 457                ZN    ZN A 503     1555   1555  2.32  
LINK         NE2 HIS A 461                ZN    ZN A 503     1555   1555  2.33  
CISPEP   1 GLY A  152    PRO A  153          0         2.87                     
CISPEP   2 SER A  246    PRO A  247          0        -1.20                     
SITE     1 AC1  4 CYS A 150  CYS A 154  CYS A 212  HIS A 215                    
SITE     1 AC2  4 CYS A 253  HIS A 257  CYS A 289  CYS A 293                    
SITE     1 AC3  4 CYS A 446  CYS A 449  CYS A 457  HIS A 461                    
SITE     1 AC4  4 CYS A 166  CYS A 169  CYS A 196  CYS A 201                    
SITE     1 AC5  4 CYS A 238  CYS A 241  CYS A 260  CYS A 263                    
SITE     1 AC6  4 CYS A 332  CYS A 337  CYS A 352  CYS A 360                    
SITE     1 AC7  4 CYS A 365  CYS A 368  HIS A 373  CYS A 377                    
SITE     1 AC8  4 CYS A 418  CYS A 421  CYS A 436  CYS A 441                    
SITE     1 AC9  5 ARG A 163  LYS A 211  THR A 217  ARG A 420                    
SITE     2 AC9  5 HOH A 624                                                     
SITE     1 AD1  2 ASN A 454  ARG A 455                                          
SITE     1 AD2  3 HIS A 279  ARG A 334  GLY A 361                               
SITE     1 AD3  2 ASN A 254  PRO A 294                                          
SITE     1 AD4  5 LYS A 151  HIS A 302  ARG A 305  TYR A 312                    
SITE     2 AD4  5 HOH A 603                                                     
SITE     1 AD5  2 ARG A 348  TYR A 372                                          
SITE     1 AD6  5 CYS A 368  HIS A 373  GLU A 376  CYS A 377                    
SITE     2 AD6  5 SER A 378                                                     
SITE     1 AD7  6 VAL A 186  LEU A 187  PRO A 189  PHE A 208                    
SITE     2 AD7  6 HOH A 604  HOH A 621                                          
SITE     1 AD8  3 ASN A 295  SER A 296  LEU A 297                               
CRYST1  169.360  169.360   96.990  90.00  90.00 120.00 H 3 2        18          
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      0.005905  0.003409  0.000000        0.00000                         
SCALE2      0.000000  0.006818  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010310        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system