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Database: PDB
Entry: 5N2W
LinkDB: 5N2W
Original site: 5N2W 
HEADER    LIGASE                                  08-FEB-17   5N2W              
TITLE     WT-PARKIN AND PUB COMPLEX                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE PARKIN,E3 UBIQUITIN-PROTEIN    
COMPND   3 LIGASE PARKIN;                                                       
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PARKIN,PARKINSON JUVENILE DISEASE PROTEIN 2,PARKINSON       
COMPND   6 DISEASE PROTEIN 2,PARKIN,PARKINSON JUVENILE DISEASE PROTEIN 2,       
COMPND   7 PARKINSON DISEASE PROTEIN 2;                                         
COMPND   8 EC: 2.3.2.-,2.3.2.-;                                                 
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: POLYUBIQUITIN-B;                                           
COMPND  12 CHAIN: B;                                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: SER65 IS PHOSPHORYLATED TO GIVE SEP65                 
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;                                 
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    COMPLEX STRUCTURE OF PARKIN AND PUB, TRANSFERASE, LIGASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.KUMAR,V.K.CHAUGULE,C.JOHNSON,R.TOTH,R.SUNDARAMOORTHY,A.KNEBEL,      
AUTHOR   2 H.WALDEN                                                             
REVDAT   5   31-JAN-18 5N2W    1       REMARK                                   
REVDAT   4   13-SEP-17 5N2W    1       REMARK                                   
REVDAT   3   17-MAY-17 5N2W    1       JRNL                                     
REVDAT   2   26-APR-17 5N2W    1       JRNL                                     
REVDAT   1   19-APR-17 5N2W    0                                                
JRNL        AUTH   A.KUMAR,V.K.CHAUGULE,T.E.C.CONDOS,K.R.BARBER,C.JOHNSON,      
JRNL        AUTH 2 R.TOTH,R.SUNDARAMOORTHY,A.KNEBEL,G.S.SHAW,H.WALDEN           
JRNL        TITL   PARKIN-PHOSPHOUBIQUITIN COMPLEX REVEALS CRYPTIC              
JRNL        TITL 2 UBIQUITIN-BINDING SITE REQUIRED FOR RBR LIGASE ACTIVITY.     
JRNL        REF    NAT. STRUCT. MOL. BIOL.       V.  24   475 2017              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   28414322                                                     
JRNL        DOI    10.1038/NSMB.3400                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.68 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.68                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 15007                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.201                          
REMARK   3   R VALUE            (WORKING SET)  : 0.198                          
REMARK   3   FREE R VALUE                      : 0.243                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 758                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 8                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.68                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.87                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 92.54                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2665                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2319                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2538                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2275                   
REMARK   3   BIN FREE R VALUE                        : 0.3238                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.77                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 127                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3609                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 19                                      
REMARK   3   SOLVENT ATOMS            : 29                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 70.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.35660                                              
REMARK   3    B22 (A**2) : 3.35660                                              
REMARK   3    B33 (A**2) : -6.71320                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.364               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.329               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 1.966               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.329               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.879                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3720   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5026   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1290   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 101    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 532    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3720   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 474    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4105   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.14                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.00                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 20.48                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|1 - A|74 }                                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -26.8020  -28.6790   27.8360           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2725 T22:    0.2964                                    
REMARK   3     T33:    0.2506 T12:   -0.0245                                    
REMARK   3     T13:   -0.0016 T23:   -0.0034                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.7513 L22:    3.7468                                    
REMARK   3     L33:    7.7154 L12:   -1.4739                                    
REMARK   3     L13:    1.6781 L23:   -1.1797                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0771 S12:    0.0299 S13:   -0.0683                     
REMARK   3     S21:    0.1152 S22:   -0.0654 S23:   -0.3332                     
REMARK   3     S31:   -0.0081 S32:    0.4421 S33:    0.1425                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|82 - A|228 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -16.1410  -71.2120    0.2500           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.5054 T22:    0.3501                                    
REMARK   3     T33:    0.3428 T12:    0.0264                                    
REMARK   3     T13:   -0.0275 T23:    0.0254                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.0042 L22:    4.4759                                    
REMARK   3     L33:    2.7081 L12:    2.0071                                    
REMARK   3     L13:   -0.5022 L23:   -0.8491                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1110 S12:   -0.5459 S13:   -0.7350                     
REMARK   3     S21:    0.4476 S22:   -0.1680 S23:   -0.5726                     
REMARK   3     S31:    0.4431 S32:    0.3314 S33:    0.0570                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|229 - A|328 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -33.9370  -40.7990   10.0280           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1601 T22:    0.1314                                    
REMARK   3     T33:    0.0100 T12:    0.0241                                    
REMARK   3     T13:    0.0536 T23:    0.0115                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1473 L22:    2.7995                                    
REMARK   3     L33:    1.2394 L12:   -0.2026                                    
REMARK   3     L13:    0.4084 L23:    0.2089                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0262 S12:    0.0391 S13:   -0.0298                     
REMARK   3     S21:   -0.0239 S22:    0.0115 S23:   -0.0598                     
REMARK   3     S31:    0.2375 S32:    0.0182 S33:    0.0148                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { A|329 - A|377 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -26.2530  -12.5850   -5.0130           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.4852 T22:    0.4705                                    
REMARK   3     T33:    0.4068 T12:   -0.0253                                    
REMARK   3     T13:    0.1732 T23:    0.1074                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.8594 L22:    9.3295                                    
REMARK   3     L33:    8.1863 L12:    0.4905                                    
REMARK   3     L13:   -0.3911 L23:   -0.1548                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0263 S12:    0.6458 S13:    0.1488                     
REMARK   3     S21:   -0.5219 S22:    0.0561 S23:   -0.6261                     
REMARK   3     S31:   -0.3145 S32:    0.5922 S33:   -0.0824                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { A|387 - A|405 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -24.8490  -49.1040   17.1900           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.7079 T22:    0.6975                                    
REMARK   3     T33:    0.3606 T12:    0.0070                                    
REMARK   3     T13:    0.0650 T23:   -0.0339                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    9.3238 L22:   12.8586                                    
REMARK   3     L33:    0.8718 L12:    1.5695                                    
REMARK   3     L13:   -0.0129 L23:   -3.2029                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.7647 S12:    0.1976 S13:   -0.5513                     
REMARK   3     S21:   -0.0176 S22:    0.5211 S23:   -1.3288                     
REMARK   3     S31:   -0.0067 S32:    0.6445 S33:    0.2436                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { A|413 - A|465 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -52.9770  -69.8520    5.4120           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.3227 T22:    0.4149                                    
REMARK   3     T33:    0.2538 T12:   -0.0597                                    
REMARK   3     T13:   -0.0050 T23:    0.0212                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.8058 L22:   11.0295                                    
REMARK   3     L33:    3.1797 L12:    1.7843                                    
REMARK   3     L13:   -0.4756 L23:   -1.2141                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0848 S12:    0.2959 S13:   -0.2725                     
REMARK   3     S21:    0.0293 S22:   -0.1053 S23:   -0.0676                     
REMARK   3     S31:    0.2174 S32:    0.1587 S33:    0.0205                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { B|1 - B|76 }                                         
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.5680  -51.1860    7.0180           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.3743 T22:    0.5243                                    
REMARK   3     T33:    0.1926 T12:   -0.0518                                    
REMARK   3     T13:   -0.0997 T23:    0.0551                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.1109 L22:    6.6365                                    
REMARK   3     L33:    3.4294 L12:   -0.0903                                    
REMARK   3     L13:   -0.8229 L23:    0.0368                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1143 S12:   -0.7349 S13:   -0.1352                     
REMARK   3     S21:    0.8127 S22:   -0.2747 S23:   -0.6602                     
REMARK   3     S31:    0.1285 S32:    0.1192 S33:    0.1604                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5N2W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003417.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15028                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.680                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.340                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.10700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.68                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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: 5C1Z, 5CAW                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS PH 8.5, 200MM TMAO, PEG MME   
REMARK 280  2000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 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   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       43.74500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       43.74500            
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       43.74500            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       43.74500            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       43.74500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       43.74500            
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: 3130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A    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     SER A   378                                                      
REMARK 465     ALA A   379                                                      
REMARK 465     VAL A   380                                                      
REMARK 465     PHE A   381                                                      
REMARK 465     GLU A   382                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     SER A   384                                                      
REMARK 465     GLY A   385                                                      
REMARK 465     THR A   386                                                      
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 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    HOH A   606     O    HOH A   607              0.00            
REMARK 500   O    HOH A   616     O    HOH A   617              0.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 353   CD    GLU A 353   OE2     0.076                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    THR A 177   CB  -  CA  -  C   ANGL. DEV. =  19.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  62     -118.35     26.16                                   
REMARK 500    ASP A  62     -117.56     26.16                                   
REMARK 500    GLN A  64       18.90     58.15                                   
REMARK 500    PRO A  73     -138.06    -71.85                                   
REMARK 500    PRO A 202       30.61    -97.78                                   
REMARK 500    THR A 240      -74.06    -87.31                                   
REMARK 500    THR A 242       47.29    -97.47                                   
REMARK 500    LEU A 283      -51.50   -121.25                                   
REMARK 500    PRO A 288     -163.41    -79.89                                   
REMARK 500    CYS A 337      -85.36    -91.86                                   
REMARK 500    LEU A 358       47.04    -80.74                                   
REMARK 500    GLU A 367      -67.51    -92.19                                   
REMARK 500    ALA A 401       49.78    -88.45                                   
REMARK 500    CYS A 441      -73.54   -107.86                                   
REMARK 500    HIS A 461       59.13   -152.24                                   
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 508  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 150   SG                                                     
REMARK 620 2 CYS A 154   SG  113.6                                              
REMARK 620 3 CYS A 212   SG  107.2 112.3                                        
REMARK 620 4 HIS A 215   NE2 104.1 116.1 102.4                                  
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  109.8                                              
REMARK 620 3 CYS A 196   SG  112.4 108.1                                        
REMARK 620 4 CYS A 201   SG  107.2 105.7 113.4                                  
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  109.1                                              
REMARK 620 3 CYS A 260   SG  117.2 117.5                                        
REMARK 620 4 CYS A 263   SG  112.3 100.2  98.7                                  
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 102.5                                              
REMARK 620 3 CYS A 289   SG  116.9 105.1                                        
REMARK 620 4 CYS A 293   SG  110.2 101.4 118.0                                  
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  105.6                                              
REMARK 620 3 CYS A 352   SG   99.0 101.6                                        
REMARK 620 4 CYS A 360   SG  107.0 124.4 116.0                                  
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 365   SG                                                     
REMARK 620 2 CYS A 368   SG  110.8                                              
REMARK 620 3 HIS A 373   NE2 125.4  88.5                                        
REMARK 620 4 CYS A 377   SG  117.6 102.1 106.4                                  
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 418   SG                                                     
REMARK 620 2 CYS A 421   SG  110.6                                              
REMARK 620 3 CYS A 436   SG  110.7 107.8                                        
REMARK 620 4 CYS A 441   SG  105.6 105.6 116.4                                  
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  114.0                                              
REMARK 620 3 CYS A 457   SG  104.5 118.4                                        
REMARK 620 4 HIS A 461   NE2 103.0 108.6 107.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 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 CL A 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TMO A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TMO A 511                 
DBREF  5N2W A    1    83  UNP    O60260   PRKN2_HUMAN      1     83             
DBREF  5N2W A  144   465  UNP    O60260   PRKN2_HUMAN    144    465             
DBREF  5N2W B    1    76  UNP    P0CG47   UBB_HUMAN        1     76             
SEQADV 5N2W CYS A  347  UNP  O60260    GLN   347 CONFLICT                       
SEQRES   1 A  405  MET ILE VAL PHE VAL ARG PHE ASN SER SER HIS GLY PHE          
SEQRES   2 A  405  PRO VAL GLU VAL ASP SER ASP THR SER ILE PHE GLN LEU          
SEQRES   3 A  405  LYS GLU VAL VAL ALA LYS ARG GLN GLY VAL PRO ALA ASP          
SEQRES   4 A  405  GLN LEU ARG VAL ILE PHE ALA GLY LYS GLU LEU ARG ASN          
SEQRES   5 A  405  ASP TRP THR VAL GLN ASN CYS ASP LEU ASP GLN GLN SER          
SEQRES   6 A  405  ILE VAL HIS ILE VAL GLN ARG PRO TRP ARG LYS GLY GLN          
SEQRES   7 A  405  GLU MET ASN ALA THR ASN SER PHE TYR VAL TYR CYS LYS          
SEQRES   8 A  405  GLY PRO CYS GLN ARG VAL GLN PRO GLY LYS LEU ARG VAL          
SEQRES   9 A  405  GLN CYS SER THR CYS ARG GLN ALA THR LEU THR LEU THR          
SEQRES  10 A  405  GLN GLY PRO SER CYS TRP ASP ASP VAL LEU ILE PRO ASN          
SEQRES  11 A  405  ARG MET SER GLY GLU CYS GLN SER PRO HIS CYS PRO GLY          
SEQRES  12 A  405  THR SER ALA GLU PHE PHE PHE LYS CYS GLY ALA HIS PRO          
SEQRES  13 A  405  THR SER ASP LYS GLU THR SER VAL ALA LEU HIS LEU ILE          
SEQRES  14 A  405  ALA THR ASN SER ARG ASN ILE THR CYS ILE THR CYS THR          
SEQRES  15 A  405  ASP VAL ARG SER PRO VAL LEU VAL PHE GLN CYS ASN SER          
SEQRES  16 A  405  ARG HIS VAL ILE CYS LEU ASP CYS PHE HIS LEU TYR CYS          
SEQRES  17 A  405  VAL THR ARG LEU ASN ASP ARG GLN PHE VAL HIS ASP PRO          
SEQRES  18 A  405  GLN LEU GLY TYR SER LEU PRO CYS VAL ALA GLY CYS PRO          
SEQRES  19 A  405  ASN SER LEU ILE LYS GLU LEU HIS HIS PHE ARG ILE LEU          
SEQRES  20 A  405  GLY GLU GLU GLN TYR ASN ARG TYR GLN GLN TYR GLY ALA          
SEQRES  21 A  405  GLU GLU CYS VAL LEU GLN MET GLY GLY VAL LEU CYS PRO          
SEQRES  22 A  405  ARG PRO GLY CYS GLY ALA GLY LEU LEU PRO GLU PRO ASP          
SEQRES  23 A  405  CYS ARG LYS VAL THR CYS GLU GLY GLY ASN GLY LEU GLY          
SEQRES  24 A  405  CYS GLY PHE ALA PHE CYS ARG GLU CYS LYS GLU ALA TYR          
SEQRES  25 A  405  HIS GLU GLY GLU CYS SER ALA VAL PHE GLU ALA SER GLY          
SEQRES  26 A  405  THR THR THR GLN ALA TYR ARG VAL ASP GLU ARG ALA ALA          
SEQRES  27 A  405  GLU GLN ALA ARG TRP GLU ALA ALA SER LYS GLU THR ILE          
SEQRES  28 A  405  LYS LYS THR THR LYS PRO CYS PRO ARG CYS HIS VAL PRO          
SEQRES  29 A  405  VAL GLU LYS ASN GLY GLY CYS MET HIS MET LYS CYS PRO          
SEQRES  30 A  405  GLN PRO GLN CYS ARG LEU GLU TRP CYS TRP ASN CYS GLY          
SEQRES  31 A  405  CYS GLU TRP ASN ARG VAL CYS MET GLY ASP HIS TRP PHE          
SEQRES  32 A  405  ASP VAL                                                      
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 5N2W SEP B   65  SER  MODIFIED RESIDUE                                   
MODRES 5N2W 3CN B   76  GLY  MODIFIED RESIDUE                                   
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     ZN  A 507       1                                                       
HET     ZN  A 508       1                                                       
HET     CL  A 509       1                                                       
HET    TMO  A 510       5                                                       
HET    TMO  A 511       5                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     3CN 3-AMINOPROPANE                                                   
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     TMO TRIMETHYLAMINE OXIDE                                             
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   2  SEP    C3 H8 N O6 P                                                 
FORMUL   2  3CN    C3 H9 N                                                      
FORMUL   3   ZN    8(ZN 2+)                                                     
FORMUL  11   CL    CL 1-                                                        
FORMUL  12  TMO    2(C3 H9 N O)                                                 
FORMUL  14  HOH   *29(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 CYS A  182  ILE A  188  1                                   7    
HELIX    4 AA4 LEU A  261  ASP A  274  1                                  14    
HELIX    5 AA5 GLU A  300  LEU A  307  5                                   8    
HELIX    6 AA6 GLY A  308  MET A  327  1                                  20    
HELIX    7 AA7 ASP A  394  ALA A  401  1                                   8    
HELIX    8 AA8 ASN A  454  TRP A  462  1                                   9    
HELIX    9 AA9 THR B   22  GLY B   35  1                                  14    
HELIX   10 AB1 LEU B   56  ASN B   60  5                                   5    
SHEET    1 AA1 5 PHE A  13  GLU A  16  0                                        
SHEET    2 AA1 5 ILE A   2  ARG A   6 -1  N  VAL A   5   O  PHE A  13           
SHEET    3 AA1 5 ILE A  66  GLN A  71  1  O  VAL A  67   N  ARG A   6           
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  GLU A  49 -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  GLN A 165   O  GLU A 207           
SHEET    3 AA2 4 TYR A 147  CYS A 150 -1  N  VAL A 148   O  GLN A 158           
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  GLY A 284   N  ASP A 280           
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  LYS B   6   O  LEU B  67           
SHEET    5 AA6 5 THR B  12  GLU B  16 -1  O  LEU B  15   N  ILE B   3           
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           
SHEET    1 AA9 2 THR A 415  PRO A 417  0                                        
SHEET    2 AA9 2 PRO A 424  GLU A 426 -1  O  VAL A 425   N  LYS A 416           
SHEET    1 AB1 2 HIS A 433  LYS A 435  0                                        
SHEET    2 AB1 2 GLU A 444  CYS A 446 -1  O  TRP A 445   N  MET A 434           
LINK         SG  CYS A 150                ZN    ZN A 508     1555   1555  2.32  
LINK         SG  CYS A 154                ZN    ZN A 508     1555   1555  2.43  
LINK         SG  CYS A 166                ZN    ZN A 504     1555   1555  2.28  
LINK         SG  CYS A 169                ZN    ZN A 504     1555   1555  2.31  
LINK         SG  CYS A 196                ZN    ZN A 504     1555   1555  2.19  
LINK         SG  CYS A 201                ZN    ZN A 504     1555   1555  2.36  
LINK         SG  CYS A 212                ZN    ZN A 508     1555   1555  2.26  
LINK         NE2 HIS A 215                ZN    ZN A 508     1555   1555  2.11  
LINK         SG  CYS A 238                ZN    ZN A 505     1555   1555  2.34  
LINK         SG  CYS A 241                ZN    ZN A 505     1555   1555  2.38  
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 505     1555   1555  2.35  
LINK         SG  CYS A 263                ZN    ZN A 505     1555   1555  2.33  
LINK         SG  CYS A 289                ZN    ZN A 501     1555   1555  2.33  
LINK         SG  CYS A 293                ZN    ZN A 501     1555   1555  2.30  
LINK         SG  CYS A 332                ZN    ZN A 506     1555   1555  2.32  
LINK         SG  CYS A 337                ZN    ZN A 506     1555   1555  2.22  
LINK         SG  CYS A 347                 CA  3CN B  76     1555   1555  1.95  
LINK         SG  CYS A 352                ZN    ZN A 506     1555   1555  2.40  
LINK         SG  CYS A 360                ZN    ZN A 506     1555   1555  2.34  
LINK         SG  CYS A 365                ZN    ZN A 502     1555   1555  2.38  
LINK         SG  CYS A 368                ZN    ZN A 502     1555   1555  2.28  
LINK         NE2 HIS A 373                ZN    ZN A 502     1555   1555  2.28  
LINK         SG  CYS A 377                ZN    ZN A 502     1555   1555  2.76  
LINK         SG  CYS A 418                ZN    ZN A 507     1555   1555  2.33  
LINK         SG  CYS A 421                ZN    ZN A 507     1555   1555  2.34  
LINK         SG  CYS A 436                ZN    ZN A 507     1555   1555  2.26  
LINK         SG  CYS A 441                ZN    ZN A 507     1555   1555  2.37  
LINK         SG  CYS A 446                ZN    ZN A 503     1555   1555  2.27  
LINK         SG  CYS A 449                ZN    ZN A 503     1555   1555  2.23  
LINK         SG  CYS A 457                ZN    ZN A 503     1555   1555  2.34  
LINK         NE2 HIS A 461                ZN    ZN A 503     1555   1555  2.11  
LINK         C   GLU B  64                 N   SEP B  65     1555   1555  1.34  
LINK         C   SEP B  65                 N   THR B  66     1555   1555  1.35  
LINK         C   GLY B  75                 ND  3CN B  76     1555   1555  1.41  
CISPEP   1 GLY A  152    PRO A  153          0         2.40                     
CISPEP   2 SER A  246    PRO A  247          0        -3.86                     
CISPEP   3 GLY A  357    LEU A  358          0         5.32                     
CISPEP   4 CYS A  360    GLY A  361          0        -8.93                     
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 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 418  CYS A 421  CYS A 436  CYS A 441                    
SITE     1 AC8  4 CYS A 150  CYS A 154  CYS A 212  HIS A 215                    
SITE     1 AC9  5 THR A 237  CYS A 238  ALA A 397  GLN A 400                    
SITE     2 AC9  5 ALA A 401                                                     
SITE     1 AD1  3 VAL A 186  LEU A 187  PHE A 208                               
SITE     1 AD2  8 GLY A  47  HIS A  68  THR A 270  ARG A 271                    
SITE     2 AD2  8 ASP A 274  GLN A 389  ALA A 390  TYR A 391                    
CRYST1  147.290  147.290   87.490  90.00  90.00 120.00 P 63 2 2     12          
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      0.006789  0.003920  0.000000        0.00000                         
SCALE2      0.000000  0.007840  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011430        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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