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Database: PDB
Entry: 5N38
LinkDB: 5N38
Original site: 5N38 
HEADER    LIGASE                                  08-FEB-17   5N38              
TITLE     S65DPARKIN 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                               
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    S65DPARKIN PUB COMPLEX, SPLICING, 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   07-FEB-18 5N38    1       REMARK                                   
REVDAT   4   13-SEP-17 5N38    1       REMARK                                   
REVDAT   3   17-MAY-17 5N38    1       JRNL                                     
REVDAT   2   26-APR-17 5N38    1       JRNL                                     
REVDAT   1   19-APR-17 5N38    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.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 72.56                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 16984                          
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)  : 0.189                          
REMARK   3   R VALUE            (WORKING SET)  : 0.187                          
REMARK   3   FREE R VALUE                      : 0.236                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.150                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 874                            
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               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.60                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.76                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 95.81                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2459                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2275                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2323                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2228                   
REMARK   3   BIN FREE R VALUE                        : 0.3082                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.53                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 136                      
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            : 3565                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 13                                      
REMARK   3   SOLVENT ATOMS            : 55                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.57                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.82560                                              
REMARK   3    B22 (A**2) : 0.82560                                              
REMARK   3    B33 (A**2) : -1.65130                                             
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) : 0.347               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.686               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.288               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.595               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.286               
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      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3645   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4929   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1258   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 98     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 524    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3645   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 466    ; 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   : 3987   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.22                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.22                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.81                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|1-74 }                                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -26.1996  -28.4538   28.1842           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0403 T22:   -0.0476                                    
REMARK   3     T33:   -0.0700 T12:    0.0166                                    
REMARK   3     T13:   -0.0135 T23:    0.0199                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1022 L22:    2.6719                                    
REMARK   3     L33:    5.5070 L12:   -0.2573                                    
REMARK   3     L13:    1.2472 L23:   -0.1148                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0846 S12:   -0.2468 S13:   -0.0241                     
REMARK   3     S21:    0.0362 S22:    0.0467 S23:   -0.2582                     
REMARK   3     S31:    0.2995 S32:    0.3226 S33:   -0.1313                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|79-228 }                                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -16.1321  -71.1289   -0.7945           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0256 T22:   -0.1315                                    
REMARK   3     T33:   -0.0311 T12:   -0.0689                                    
REMARK   3     T13:   -0.0841 T23:    0.0454                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4782 L22:    2.5890                                    
REMARK   3     L33:    1.6007 L12:    0.5296                                    
REMARK   3     L13:   -0.3227 L23:    0.9864                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2216 S12:   -0.4305 S13:   -0.3502                     
REMARK   3     S21:    0.3628 S22:   -0.0802 S23:   -0.4820                     
REMARK   3     S31:    0.4449 S32:    0.0521 S33:   -0.1414                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|229-328 }                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -33.5039  -40.1955   10.2082           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0137 T22:   -0.0406                                    
REMARK   3     T33:   -0.0623 T12:    0.0144                                    
REMARK   3     T13:    0.0433 T23:    0.0132                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8637 L22:    1.9115                                    
REMARK   3     L33:    1.0956 L12:   -0.2553                                    
REMARK   3     L13:   -0.0993 L23:   -0.4795                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0582 S12:   -0.0746 S13:   -0.0398                     
REMARK   3     S21:   -0.0437 S22:    0.0046 S23:   -0.0035                     
REMARK   3     S31:    0.1898 S32:    0.0613 S33:    0.0536                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { A|329-377 }                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -26.3489  -12.0189   -5.4347           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0404 T22:   -0.0541                                    
REMARK   3     T33:   -0.0448 T12:    0.0164                                    
REMARK   3     T13:    0.1031 T23:    0.1120                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5793 L22:    6.6209                                    
REMARK   3     L33:    5.4814 L12:    0.5887                                    
REMARK   3     L13:    1.0881 L23:   -0.0551                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0063 S12:    0.2488 S13:    0.0682                     
REMARK   3     S21:   -0.3063 S22:    0.1002 S23:   -0.1909                     
REMARK   3     S31:   -0.2406 S32:    0.0506 S33:   -0.0939                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { A|393-405 }                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -26.4093  -55.2402   17.2841           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1082 T22:   -0.0787                                    
REMARK   3     T33:   -0.0127 T12:    0.0306                                    
REMARK   3     T13:    0.1253 T23:    0.0869                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.0431 L22:   -0.1334                                    
REMARK   3     L33:    0.7507 L12:   -0.9263                                    
REMARK   3     L13:   -1.8681 L23:    0.0418                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0256 S12:    0.0234 S13:   -0.1961                     
REMARK   3     S21:    0.0596 S22:   -0.0770 S23:   -0.0265                     
REMARK   3     S31:    0.0408 S32:    0.1089 S33:    0.1026                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { A|413-465 }                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -52.5550  -69.1041    5.9718           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0277 T22:   -0.0078                                    
REMARK   3     T33:   -0.0739 T12:   -0.0571                                    
REMARK   3     T13:   -0.0086 T23:    0.0024                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0346 L22:    6.7811                                    
REMARK   3     L33:    2.3744 L12:    0.6656                                    
REMARK   3     L13:   -1.2691 L23:   -0.4388                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0096 S12:    0.0040 S13:    0.1905                     
REMARK   3     S21:   -0.0860 S22:   -0.0851 S23:    0.2888                     
REMARK   3     S31:   -0.2058 S32:    0.1901 S33:    0.0755                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.3978  -51.4629    6.7824           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0157 T22:    0.0522                                    
REMARK   3     T33:   -0.1385 T12:    0.0008                                    
REMARK   3     T13:   -0.0729 T23:    0.0550                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.7166 L22:    4.4110                                    
REMARK   3     L33:    2.1284 L12:   -0.1149                                    
REMARK   3     L13:   -0.2966 L23:    0.0100                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0344 S12:   -0.5416 S13:   -0.3388                     
REMARK   3     S21:    0.5469 S22:    0.0314 S23:   -0.2184                     
REMARK   3     S31:    0.2701 S32:    0.0258 S33:   -0.0658                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5N38 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003479.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-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                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
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   : 17000                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 72.560                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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   (%): 51.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
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       44.22000            
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       44.22000            
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       44.22000            
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       44.22000            
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       44.22000            
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       44.22000            
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: 3150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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     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     THR A   387                                                      
REMARK 465     THR A   388                                                      
REMARK 465     GLN A   389                                                      
REMARK 465     ALA A   390                                                      
REMARK 465     TYR A   391                                                      
REMARK 465     ARG A   392                                                      
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  48    CG   CD   CE   NZ                                   
REMARK 470     GLU A  79    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 195    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 353    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 413    CG   CD   CE   NZ                                   
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    GLN A  64       37.48     72.32                                   
REMARK 500    MET A  80      -70.67    -95.00                                   
REMARK 500    THR A 168      -85.34    -69.48                                   
REMARK 500    CYS A 201      118.59   -167.26                                   
REMARK 500    PRO A 202       42.92    -91.98                                   
REMARK 500    LEU A 226       75.77   -102.56                                   
REMARK 500    LEU A 283      -55.18   -127.28                                   
REMARK 500    PRO A 288     -157.29    -87.12                                   
REMARK 500    CYS A 337      -86.41    -90.56                                   
REMARK 500    ASP A 346       75.94   -112.03                                   
REMARK 500    ASN A 356      -77.73   -137.45                                   
REMARK 500    GLU A 367      -75.58    -94.77                                   
REMARK 500    ALA A 401       49.87    -84.72                                   
REMARK 500    CYS A 441      -85.44   -103.04                                   
REMARK 500    HIS A 461       56.46   -166.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PEG A 2501                                                       
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 A2510  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 150   SG                                                     
REMARK 620 2 CYS A 154   SG  110.1                                              
REMARK 620 3 CYS A 212   SG  110.2 110.2                                        
REMARK 620 4 HIS A 215   NE2  97.7 118.3 109.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2509  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 166   SG                                                     
REMARK 620 2 CYS A 169   SG  117.0                                              
REMARK 620 3 CYS A 196   SG  110.7  90.2                                        
REMARK 620 4 CYS A 201   SG  123.3 112.3  95.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 238   SG                                                     
REMARK 620 2 CYS A 241   SG  104.3                                              
REMARK 620 3 CYS A 260   SG  119.7 119.4                                        
REMARK 620 4 CYS A 263   SG  101.5 105.5 104.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 253   SG                                                     
REMARK 620 2 HIS A 257   ND1 101.7                                              
REMARK 620 3 CYS A 289   SG  118.4 105.4                                        
REMARK 620 4 CYS A 293   SG  111.4 104.8 113.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2506  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 332   SG                                                     
REMARK 620 2 CYS A 337   SG  111.5                                              
REMARK 620 3 CYS A 352   SG  113.8 104.3                                        
REMARK 620 4 CYS A 360   SG   95.5 106.9 124.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2505  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 365   SG                                                     
REMARK 620 2 CYS A 368   SG  127.8                                              
REMARK 620 3 HIS A 373   NE2 103.5  94.2                                        
REMARK 620 4 CYS A 377   SG  112.9 108.6 105.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2508  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 418   SG                                                     
REMARK 620 2 CYS A 421   SG  112.1                                              
REMARK 620 3 CYS A 436   SG  113.8 100.6                                        
REMARK 620 4 CYS A 441   SG  101.4 114.1 115.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2507  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 446   SG                                                     
REMARK 620 2 CYS A 449   SG  119.6                                              
REMARK 620 3 CYS A 457   SG  111.6 112.8                                        
REMARK 620 4 HIS A 461   NE2 105.4 100.7 104.5                                  
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 PEG A 2501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 2502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2510                 
DBREF  5N38 A    1    83  UNP    O60260   PRKN2_HUMAN      1     83             
DBREF  5N38 A  144   465  UNP    O60260   PRKN2_HUMAN    144    465             
DBREF  5N38 B    1    76  UNP    P0CG47   UBB_HUMAN        1     76             
SEQADV 5N38 ASP A   65  UNP  O60260    SER    65 CONFLICT                       
SEQADV 5N38 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 ASP          
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 5N38 SEP B   65  SER  MODIFIED RESIDUE                                   
MODRES 5N38 3CN B   76  GLY  MODIFIED RESIDUE                                   
HET    SEP  B  65      10                                                       
HET    3CN  B  76       4                                                       
HET    PEG  A2501       4                                                       
HET     CL  A2502       1                                                       
HET     ZN  A2503       1                                                       
HET     ZN  A2504       1                                                       
HET     ZN  A2505       1                                                       
HET     ZN  A2506       1                                                       
HET     ZN  A2507       1                                                       
HET     ZN  A2508       1                                                       
HET     ZN  A2509       1                                                       
HET     ZN  A2510       1                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     3CN 3-AMINOPROPANE                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      CL CHLORIDE ION                                                     
HETNAM      ZN ZINC ION                                                         
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   2  SEP    C3 H8 N O6 P                                                 
FORMUL   2  3CN    C3 H9 N                                                      
FORMUL   3  PEG    C4 H10 O3                                                    
FORMUL   4   CL    CL 1-                                                        
FORMUL   5   ZN    8(ZN 2+)                                                     
FORMUL  13  HOH   *55(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  ARG A  275  1                                  15    
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  PHE A   4           
SHEET    4 AA1 5 LEU A  41  PHE A  45 -1  N  ILE A  44   O  HIS A  68           
SHEET    5 AA1 5 LYS A  48  LEU A  50 -1  O  LYS A  48   N  PHE A  45           
SHEET    1 AA2 3 TYR A 147  CYS A 150  0                                        
SHEET    2 AA2 3 ARG A 156  CYS A 166 -1  O  GLN A 158   N  VAL A 148           
SHEET    3 AA2 3 ALA A 206  CYS A 212 -1  O  GLU A 207   N  GLN A 165           
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  PRO A 343 -1  O  LEU A 341   N  VAL A 330           
SHEET    3 AA6 5 THR B  66  LEU B  73  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  PRO A 343 -1  O  LEU A 341   N  VAL A 330           
SHEET    3 AA7 5 THR B  66  LEU B  73  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 A2510     1555   1555  2.28  
LINK         SG  CYS A 154                ZN    ZN A2510     1555   1555  2.32  
LINK         SG  CYS A 166                ZN    ZN A2509     1555   1555  2.36  
LINK         SG  CYS A 169                ZN    ZN A2509     1555   1555  2.62  
LINK         SG  CYS A 196                ZN    ZN A2509     1555   1555  2.60  
LINK         SG  CYS A 201                ZN    ZN A2509     1555   1555  2.45  
LINK         SG  CYS A 212                ZN    ZN A2510     1555   1555  2.33  
LINK         NE2 HIS A 215                ZN    ZN A2510     1555   1555  2.14  
LINK         SG  CYS A 238                ZN    ZN A2503     1555   1555  2.34  
LINK         SG  CYS A 241                ZN    ZN A2503     1555   1555  2.38  
LINK         SG  CYS A 253                ZN    ZN A2504     1555   1555  2.33  
LINK         ND1 HIS A 257                ZN    ZN A2504     1555   1555  2.14  
LINK         SG  CYS A 260                ZN    ZN A2503     1555   1555  2.29  
LINK         SG  CYS A 263                ZN    ZN A2503     1555   1555  2.32  
LINK         SG  CYS A 289                ZN    ZN A2504     1555   1555  2.33  
LINK         SG  CYS A 293                ZN    ZN A2504     1555   1555  2.39  
LINK         SG  CYS A 332                ZN    ZN A2506     1555   1555  2.23  
LINK         SG  CYS A 337                ZN    ZN A2506     1555   1555  2.28  
LINK         SG  CYS A 352                ZN    ZN A2506     1555   1555  2.31  
LINK         SG  CYS A 360                ZN    ZN A2506     1555   1555  2.67  
LINK         SG  CYS A 365                ZN    ZN A2505     1555   1555  2.22  
LINK         SG  CYS A 368                ZN    ZN A2505     1555   1555  2.23  
LINK         NE2 HIS A 373                ZN    ZN A2505     1555   1555  2.07  
LINK         SG  CYS A 377                ZN    ZN A2505     1555   1555  2.54  
LINK         SG  CYS A 418                ZN    ZN A2508     1555   1555  2.37  
LINK         SG  CYS A 421                ZN    ZN A2508     1555   1555  2.30  
LINK         SG  CYS A 436                ZN    ZN A2508     1555   1555  2.35  
LINK         SG  CYS A 441                ZN    ZN A2508     1555   1555  2.46  
LINK         SG  CYS A 446                ZN    ZN A2507     1555   1555  2.15  
LINK         SG  CYS A 449                ZN    ZN A2507     1555   1555  2.25  
LINK         SG  CYS A 457                ZN    ZN A2507     1555   1555  2.23  
LINK         NE2 HIS A 461                ZN    ZN A2507     1555   1555  2.30  
LINK         C   GLU B  64                 N   SEP B  65     1555   1555  1.35  
LINK         C   SEP B  65                 N   THR B  66     1555   1555  1.35  
LINK         C   GLY B  75                 ND  3CN B  76     1555   1555  1.36  
CISPEP   1 GLY A  152    PRO A  153          0         3.08                     
CISPEP   2 SER A  246    PRO A  247          0         0.73                     
CISPEP   3 GLY A  357    LEU A  358          0         7.00                     
CISPEP   4 CYS A  360    GLY A  361          0         0.59                     
SITE     1 AC1  2 ASN A 232  SER A 233                                          
SITE     1 AC2  4 THR A 237  CYS A 238  THR A 242  ALA A 397                    
SITE     1 AC3  4 CYS A 238  CYS A 241  CYS A 260  CYS A 263                    
SITE     1 AC4  4 CYS A 253  HIS A 257  CYS A 289  CYS A 293                    
SITE     1 AC5  4 CYS A 365  CYS A 368  HIS A 373  CYS A 377                    
SITE     1 AC6  4 CYS A 332  CYS A 337  CYS A 352  CYS A 360                    
SITE     1 AC7  4 CYS A 446  CYS A 449  CYS A 457  HIS A 461                    
SITE     1 AC8  4 CYS A 418  CYS A 421  CYS A 436  CYS A 441                    
SITE     1 AC9  4 CYS A 166  CYS A 169  CYS A 196  CYS A 201                    
SITE     1 AD1  4 CYS A 150  CYS A 154  CYS A 212  HIS A 215                    
CRYST1  146.540  146.540   88.440  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      0.006824  0.003940  0.000000        0.00000                         
SCALE2      0.000000  0.007880  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011307        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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