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Database: PDB
Entry: 5C1Z
LinkDB: 5C1Z
Original site: 5C1Z 
HEADER    LIGASE                                  15-JUN-15   5C1Z              
TITLE     PARKIN (UBLR0RBR)                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE PARKIN;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PARKIN,PARKINSON JUVENILE DISEASE PROTEIN 2,PARKINSON       
COMPND   5 DISEASE PROTEIN 2;                                                   
COMPND   6 EC: 6.3.2.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PARK2, PRKN;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    LIGASE                                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.KUMAR,J.D.AGUIRRE,T.E.C.CONDOS,R.J.MARTINEZ-TORRES,V.K.CHAUGULE,    
AUTHOR   2 R.TOTH,R.SUNDARAMOORTHY,P.MERCIER,A.KNEBEL,D.E.SPRATT,K.R.BARBER,    
AUTHOR   3 G.S.SHAW,H.WALDEN                                                    
REVDAT   3   28-OCT-15 5C1Z    1       JRNL                                     
REVDAT   2   19-AUG-15 5C1Z    1       JRNL                                     
REVDAT   1   29-JUL-15 5C1Z    0                                                
JRNL        AUTH   A.KUMAR,J.D.AGUIRRE,T.E.CONDOS,R.J.MARTINEZ-TORRES,          
JRNL        AUTH 2 V.K.CHAUGULE,R.TOTH,R.SUNDARAMOORTHY,P.MERCIER,A.KNEBEL,     
JRNL        AUTH 3 D.E.SPRATT,K.R.BARBER,G.S.SHAW,H.WALDEN                      
JRNL        TITL   DISRUPTION OF THE AUTOINHIBITED STATE PRIMES THE E3 LIGASE   
JRNL        TITL 2 PARKIN FOR ACTIVATION AND CATALYSIS.                         
JRNL        REF    EMBO J.                       V.  34  2506 2015              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   26254304                                                     
JRNL        DOI    10.15252/EMBJ.201592337                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 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) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.36                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 87826                          
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)  : 0.193                          
REMARK   3   R VALUE            (WORKING SET)  : 0.192                          
REMARK   3   FREE R VALUE                      : 0.212                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.860                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 4270                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.79                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.84                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.42                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 6364                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2245                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 6072                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2243                   
REMARK   3   BIN FREE R VALUE                        : 0.2270                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.59                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 292                      
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            : 6036                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 711                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.89210                                             
REMARK   3    B22 (A**2) : -3.93230                                             
REMARK   3    B33 (A**2) : 8.82450                                              
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) : 0.255               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.124               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.111               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.116               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.107               
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      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6381   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8677   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2239   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 170    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 958    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6381   ; 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   : 805    ; 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   : 7754   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.94                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.78                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.86                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.2105   10.3842    8.1537           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0044 T22:   -0.0353                                    
REMARK   3     T33:   -0.0640 T12:   -0.0067                                    
REMARK   3     T13:   -0.0038 T23:   -0.0096                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9566 L22:    0.6094                                    
REMARK   3     L33:    1.9418 L12:   -0.4301                                    
REMARK   3     L13:   -1.2837 L23:    0.5867                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1624 S12:   -0.0006 S13:   -0.0999                     
REMARK   3     S21:   -0.0386 S22:   -0.0062 S23:    0.0528                     
REMARK   3     S31:    0.2089 S32:   -0.0454 S33:    0.1686                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -27.2312   -3.6225   43.3544           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0317 T22:    0.0150                                    
REMARK   3     T33:   -0.0630 T12:   -0.0069                                    
REMARK   3     T13:   -0.0096 T23:   -0.0022                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5887 L22:    0.9742                                    
REMARK   3     L33:    1.8729 L12:   -0.4257                                    
REMARK   3     L13:    0.5771 L23:   -1.2822                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0094 S12:   -0.0416 S13:    0.0489                     
REMARK   3     S21:   -0.0016 S22:   -0.1606 S23:   -0.0994                     
REMARK   3     S31:   -0.0517 S32:    0.2069 S33:    0.1700                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5C1Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210875.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : .9174                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87891                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.360                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: 4K95                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: LISO4, PEG3350, PH 5.5, VAPOR            
REMARK 280  DIFFUSION, TEMPERATURE 277K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       33.65500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      103.11500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.66000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      103.11500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.65500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.66000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   354                                                      
REMARK 465     GLY A   357                                                      
REMARK 465     LEU A   358                                                      
REMARK 465     GLY A   359                                                      
REMARK 465     CYS A   360                                                      
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     ALA A   406                                                      
REMARK 465     SER A   407                                                      
REMARK 465     LYS A   408                                                      
REMARK 465     GLU A   409                                                      
REMARK 465     THR A   410                                                      
REMARK 465     ILE A   411                                                      
REMARK 465     LYS A   412                                                      
REMARK 465     LYS A   413                                                      
REMARK 465     GLY B   354                                                      
REMARK 465     GLY B   357                                                      
REMARK 465     LEU B   358                                                      
REMARK 465     GLY B   359                                                      
REMARK 465     CYS B   360                                                      
REMARK 465     ALA B   383                                                      
REMARK 465     SER B   384                                                      
REMARK 465     GLY B   385                                                      
REMARK 465     THR B   386                                                      
REMARK 465     THR B   387                                                      
REMARK 465     THR B   388                                                      
REMARK 465     GLN B   389                                                      
REMARK 465     ALA B   390                                                      
REMARK 465     ALA B   406                                                      
REMARK 465     SER B   407                                                      
REMARK 465     LYS B   408                                                      
REMARK 465     GLU B   409                                                      
REMARK 465     THR B   410                                                      
REMARK 465     ILE B   411                                                      
REMARK 465     LYS B   412                                                      
REMARK 465     LYS B   413                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A 282    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 353    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 356    CB   CG   OD1  ND2                                  
REMARK 470     PHE A 381    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 382    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 282    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 353    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 356    CB   CG   OD1  ND2                                  
REMARK 470     PHE B 381    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 382    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  81       31.47    -97.70                                   
REMARK 500    GLN A 252       30.76    -94.33                                   
REMARK 500    LEU A 283      -49.08   -137.45                                   
REMARK 500    ALA A 401       36.46    -83.58                                   
REMARK 500    ARG A 420      -62.84    -94.93                                   
REMARK 500    CYS A 441      -74.27   -103.19                                   
REMARK 500    HIS A 461       57.23   -150.60                                   
REMARK 500    ASN B  81       32.06    -94.24                                   
REMARK 500    GLN B 252       30.40    -94.49                                   
REMARK 500    LEU B 283      -49.29   -133.27                                   
REMARK 500    PRO B 335       83.11    -69.55                                   
REMARK 500    ALA B 401       34.28    -84.62                                   
REMARK 500    ARG B 420      -64.20    -94.60                                   
REMARK 500    CYS B 441      -72.04   -101.88                                   
REMARK 500    HIS B 461       57.50   -151.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 953        DISTANCE =  6.39 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 150   SG                                                     
REMARK 620 2 CYS A 154   SG  110.3                                              
REMARK 620 3 CYS A 212   SG  113.6 113.9                                        
REMARK 620 4 HIS A 215   NE2 113.9 101.1 103.2                                  
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 166   SG                                                     
REMARK 620 2 CYS A 169   SG  105.5                                              
REMARK 620 3 CYS A 196   SG  110.2 106.2                                        
REMARK 620 4 CYS A 201   SG  109.2 115.4 110.1                                  
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 238   SG                                                     
REMARK 620 2 CYS A 241   SG  107.3                                              
REMARK 620 3 CYS A 260   SG  114.8 115.1                                        
REMARK 620 4 CYS A 263   SG  109.6 108.3 101.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 253   SG                                                     
REMARK 620 2 HIS A 257   ND1 105.7                                              
REMARK 620 3 CYS A 289   SG  116.0 105.0                                        
REMARK 620 4 CYS A 293   SG  114.1  99.9 114.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 505  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 332   SG                                                     
REMARK 620 2 CYS A 352   SG  106.9                                              
REMARK 620 3 GLY A 361   N   120.7 101.7                                        
REMARK 620 N                    1     2                                         
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 365   SG                                                     
REMARK 620 2 CYS A 368   SG  107.6                                              
REMARK 620 3 HIS A 373   NE2 107.2 104.7                                        
REMARK 620 4 CYS A 377   SG  111.8 116.2 108.8                                  
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  117.6                                              
REMARK 620 3 CYS A 436   SG  110.2 102.0                                        
REMARK 620 4 CYS A 441   SG  103.6 114.6 108.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 508  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 446   SG                                                     
REMARK 620 2 CYS A 449   SG  116.7                                              
REMARK 620 3 CYS A 457   SG  112.0 109.5                                        
REMARK 620 4 HIS A 461   NE2 102.2 105.7 110.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 150   SG                                                     
REMARK 620 2 CYS B 154   SG  110.6                                              
REMARK 620 3 CYS B 212   SG  112.9 113.9                                        
REMARK 620 4 HIS B 215   NE2 114.2 100.9 103.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 166   SG                                                     
REMARK 620 2 CYS B 169   SG  105.6                                              
REMARK 620 3 CYS B 196   SG  110.3 105.9                                        
REMARK 620 4 CYS B 201   SG  108.5 116.5 110.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 238   SG                                                     
REMARK 620 2 CYS B 241   SG  107.3                                              
REMARK 620 3 CYS B 260   SG  114.9 114.4                                        
REMARK 620 4 CYS B 263   SG  108.4 108.3 103.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 253   SG                                                     
REMARK 620 2 HIS B 257   ND1 106.0                                              
REMARK 620 3 CYS B 289   SG  116.0 105.7                                        
REMARK 620 4 CYS B 293   SG  114.3  99.2 113.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 505  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 332   SG                                                     
REMARK 620 2 CYS B 337   SG  134.1                                              
REMARK 620 3 CYS B 352   SG  104.8  93.9                                        
REMARK 620 4 GLY B 361   N   121.4  95.2  99.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 506  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 365   SG                                                     
REMARK 620 2 CYS B 368   SG  107.1                                              
REMARK 620 3 HIS B 373   NE2 106.9 104.6                                        
REMARK 620 4 CYS B 377   SG  110.6 117.7 109.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 507  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 418   SG                                                     
REMARK 620 2 CYS B 421   SG  116.5                                              
REMARK 620 3 CYS B 436   SG  111.1 103.3                                        
REMARK 620 4 CYS B 441   SG  103.4 113.0 109.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 508  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 446   SG                                                     
REMARK 620 2 CYS B 449   SG  115.0                                              
REMARK 620 3 CYS B 457   SG  112.0 110.6                                        
REMARK 620 4 HIS B 461   NE2 101.2 105.5 112.0                                  
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 SO4 A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 512                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 512                  
DBREF  5C1Z A    1   465  UNP    O60260   PRKN2_HUMAN      1    465             
DBREF  5C1Z B    1   465  UNP    O60260   PRKN2_HUMAN      1    465             
SEQADV 5C1Z     A       UNP  O60260    GLY    84 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    GLY    85 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ASP    86 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ASP    87 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    PRO    88 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ARG    89 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ASN    90 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ALA    91 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ALA    92 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    GLY    93 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    GLY    94 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    CYS    95 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    GLU    96 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ARG    97 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    GLU    98 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    PRO    99 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    GLN   100 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    SER   101 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    LEU   102 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    THR   103 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ARG   104 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    VAL   105 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ASP   106 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    LEU   107 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    SER   108 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    SER   109 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    SER   110 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    VAL   111 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    LEU   112 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    PRO   113 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    GLY   114 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ASP   115 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    SER   116 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    VAL   117 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    GLY   118 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    LEU   119 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ALA   120 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    VAL   121 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ILE   122 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    LEU   123 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    HIS   124 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    THR   125 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ASP   126 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    SER   127 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ARG   128 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    LYS   129 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ASP   130 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    SER   131 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    PRO   132 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    PRO   133 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ALA   134 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    GLY   135 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    SER   136 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    PRO   137 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ALA   138 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    GLY   139 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ARG   140 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    SER   141 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    ILE   142 DELETION                       
SEQADV 5C1Z     A       UNP  O60260    TYR   143 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    GLY    84 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    GLY    85 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ASP    86 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ASP    87 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    PRO    88 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ARG    89 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ASN    90 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ALA    91 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ALA    92 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    GLY    93 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    GLY    94 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    CYS    95 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    GLU    96 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ARG    97 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    GLU    98 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    PRO    99 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    GLN   100 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    SER   101 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    LEU   102 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    THR   103 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ARG   104 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    VAL   105 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ASP   106 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    LEU   107 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    SER   108 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    SER   109 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    SER   110 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    VAL   111 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    LEU   112 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    PRO   113 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    GLY   114 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ASP   115 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    SER   116 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    VAL   117 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    GLY   118 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    LEU   119 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ALA   120 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    VAL   121 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ILE   122 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    LEU   123 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    HIS   124 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    THR   125 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ASP   126 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    SER   127 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ARG   128 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    LYS   129 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ASP   130 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    SER   131 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    PRO   132 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    PRO   133 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ALA   134 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    GLY   135 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    SER   136 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    PRO   137 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ALA   138 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    GLY   139 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ARG   140 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    SER   141 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    ILE   142 DELETION                       
SEQADV 5C1Z     B       UNP  O60260    TYR   143 DELETION                       
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  GLN 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  405  MET ILE VAL PHE VAL ARG PHE ASN SER SER HIS GLY PHE          
SEQRES   2 B  405  PRO VAL GLU VAL ASP SER ASP THR SER ILE PHE GLN LEU          
SEQRES   3 B  405  LYS GLU VAL VAL ALA LYS ARG GLN GLY VAL PRO ALA ASP          
SEQRES   4 B  405  GLN LEU ARG VAL ILE PHE ALA GLY LYS GLU LEU ARG ASN          
SEQRES   5 B  405  ASP TRP THR VAL GLN ASN CYS ASP LEU ASP GLN GLN SER          
SEQRES   6 B  405  ILE VAL HIS ILE VAL GLN ARG PRO TRP ARG LYS GLY GLN          
SEQRES   7 B  405  GLU MET ASN ALA THR ASN SER PHE TYR VAL TYR CYS LYS          
SEQRES   8 B  405  GLY PRO CYS GLN ARG VAL GLN PRO GLY LYS LEU ARG VAL          
SEQRES   9 B  405  GLN CYS SER THR CYS ARG GLN ALA THR LEU THR LEU THR          
SEQRES  10 B  405  GLN GLY PRO SER CYS TRP ASP ASP VAL LEU ILE PRO ASN          
SEQRES  11 B  405  ARG MET SER GLY GLU CYS GLN SER PRO HIS CYS PRO GLY          
SEQRES  12 B  405  THR SER ALA GLU PHE PHE PHE LYS CYS GLY ALA HIS PRO          
SEQRES  13 B  405  THR SER ASP LYS GLU THR SER VAL ALA LEU HIS LEU ILE          
SEQRES  14 B  405  ALA THR ASN SER ARG ASN ILE THR CYS ILE THR CYS THR          
SEQRES  15 B  405  ASP VAL ARG SER PRO VAL LEU VAL PHE GLN CYS ASN SER          
SEQRES  16 B  405  ARG HIS VAL ILE CYS LEU ASP CYS PHE HIS LEU TYR CYS          
SEQRES  17 B  405  VAL THR ARG LEU ASN ASP ARG GLN PHE VAL HIS ASP PRO          
SEQRES  18 B  405  GLN LEU GLY TYR SER LEU PRO CYS VAL ALA GLY CYS PRO          
SEQRES  19 B  405  ASN SER LEU ILE LYS GLU LEU HIS HIS PHE ARG ILE LEU          
SEQRES  20 B  405  GLY GLU GLU GLN TYR ASN ARG TYR GLN GLN TYR GLY ALA          
SEQRES  21 B  405  GLU GLU CYS VAL LEU GLN MET GLY GLY VAL LEU CYS PRO          
SEQRES  22 B  405  ARG PRO GLY CYS GLY ALA GLY LEU LEU PRO GLU PRO ASP          
SEQRES  23 B  405  GLN ARG LYS VAL THR CYS GLU GLY GLY ASN GLY LEU GLY          
SEQRES  24 B  405  CYS GLY PHE ALA PHE CYS ARG GLU CYS LYS GLU ALA TYR          
SEQRES  25 B  405  HIS GLU GLY GLU CYS SER ALA VAL PHE GLU ALA SER GLY          
SEQRES  26 B  405  THR THR THR GLN ALA TYR ARG VAL ASP GLU ARG ALA ALA          
SEQRES  27 B  405  GLU GLN ALA ARG TRP GLU ALA ALA SER LYS GLU THR ILE          
SEQRES  28 B  405  LYS LYS THR THR LYS PRO CYS PRO ARG CYS HIS VAL PRO          
SEQRES  29 B  405  VAL GLU LYS ASN GLY GLY CYS MET HIS MET LYS CYS PRO          
SEQRES  30 B  405  GLN PRO GLN CYS ARG LEU GLU TRP CYS TRP ASN CYS GLY          
SEQRES  31 B  405  CYS GLU TRP ASN ARG VAL CYS MET GLY ASP HIS TRP PHE          
SEQRES  32 B  405  ASP VAL                                                      
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET     ZN  A 504       1                                                       
HET     ZN  A 505       1                                                       
HET     ZN  A 506       1                                                       
HET     ZN  A 507       1                                                       
HET     ZN  A 508       1                                                       
HET    SO4  A 509       5                                                       
HET    GOL  A 510       6                                                       
HET    GOL  A 511       6                                                       
HET     CL  A 512       1                                                       
HET     ZN  B 501       1                                                       
HET     ZN  B 502       1                                                       
HET     ZN  B 503       1                                                       
HET     ZN  B 504       1                                                       
HET     ZN  B 505       1                                                       
HET     ZN  B 506       1                                                       
HET     ZN  B 507       1                                                       
HET     ZN  B 508       1                                                       
HET    SO4  B 509       5                                                       
HET    GOL  B 510       6                                                       
HET    GOL  B 511       6                                                       
HET     CL  B 512       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   ZN    16(ZN 2+)                                                    
FORMUL  11  SO4    2(O4 S 2-)                                                   
FORMUL  12  GOL    4(C3 H8 O3)                                                  
FORMUL  14   CL    2(CL 1-)                                                     
FORMUL  27  HOH   *711(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 THR A   55  ASP A   60  1                                   6    
HELIX    4 AA4 CYS A  182  ILE A  188  1                                   7    
HELIX    5 AA5 LEU A  261  ASP A  274  1                                  14    
HELIX    6 AA6 GLU A  300  LEU A  307  5                                   8    
HELIX    7 AA7 GLY A  308  GLN A  317  1                                  10    
HELIX    8 AA8 GLN A  317  MET A  327  1                                  11    
HELIX    9 AA9 ASP A  394  ALA A  401  1                                   8    
HELIX   10 AB1 ASN A  454  TRP A  462  1                                   9    
HELIX   11 AB2 SER B   22  GLY B   35  1                                  14    
HELIX   12 AB3 PRO B   37  ASP B   39  5                                   3    
HELIX   13 AB4 THR B   55  ASP B   60  1                                   6    
HELIX   14 AB5 CYS B  182  ILE B  188  1                                   7    
HELIX   15 AB6 LEU B  261  ASP B  274  1                                  14    
HELIX   16 AB7 GLU B  300  LEU B  307  5                                   8    
HELIX   17 AB8 GLY B  308  GLN B  317  1                                  10    
HELIX   18 AB9 GLN B  317  MET B  327  1                                  11    
HELIX   19 AC1 ASP B  394  ALA B  401  1                                   8    
HELIX   20 AC2 ASN B  454  TRP B  462  1                                   9    
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 4 ALA A 206  CYS A 212  0                                        
SHEET    2 AA2 4 ARG A 156  CYS A 166 -1  N  ARG A 163   O  PHE A 209           
SHEET    3 AA2 4 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  SER A 286   N  VAL A 278           
SHEET    1 AA6 2 VAL A 330  LEU A 331  0                                        
SHEET    2 AA6 2 GLY A 340  LEU A 341 -1  O  LEU A 341   N  VAL A 330           
SHEET    1 AA7 2 LYS A 349  THR A 351  0                                        
SHEET    2 AA7 2 ALA A 363  CYS A 365 -1  O  PHE A 364   N  VAL A 350           
SHEET    1 AA8 2 THR A 415  PRO A 417  0                                        
SHEET    2 AA8 2 PRO A 424  GLU A 426 -1  O  VAL A 425   N  LYS A 416           
SHEET    1 AA9 2 HIS A 433  LYS A 435  0                                        
SHEET    2 AA9 2 GLU A 444  CYS A 446 -1  O  TRP A 445   N  MET A 434           
SHEET    1 AB1 5 PHE B  13  GLU B  16  0                                        
SHEET    2 AB1 5 ILE B   2  ARG B   6 -1  N  VAL B   5   O  PHE B  13           
SHEET    3 AB1 5 ILE B  66  GLN B  71  1  O  VAL B  67   N  PHE B   4           
SHEET    4 AB1 5 LEU B  41  PHE B  45 -1  N  ILE B  44   O  HIS B  68           
SHEET    5 AB1 5 LYS B  48  LEU B  50 -1  O  LYS B  48   N  PHE B  45           
SHEET    1 AB2 4 ALA B 206  CYS B 212  0                                        
SHEET    2 AB2 4 ARG B 156  CYS B 166 -1  N  ARG B 163   O  PHE B 209           
SHEET    3 AB2 4 TYR B 147  CYS B 150 -1  N  VAL B 148   O  GLN B 158           
SHEET    4 AB2 4 VAL B 224  ALA B 225 -1  O  VAL B 224   N  TYR B 149           
SHEET    1 AB3 2 LEU B 174  LEU B 176  0                                        
SHEET    2 AB3 2 GLY B 194  CYS B 196 -1  O  GLU B 195   N  THR B 175           
SHEET    1 AB4 3 ILE B 229  ALA B 230  0                                        
SHEET    2 AB4 3 VAL B 248  VAL B 250 -1  O  VAL B 248   N  ALA B 230           
SHEET    3 AB4 3 VAL B 258  CYS B 260 -1  O  ILE B 259   N  LEU B 249           
SHEET    1 AB5 2 VAL B 278  ASP B 280  0                                        
SHEET    2 AB5 2 GLY B 284  SER B 286 -1  O  SER B 286   N  VAL B 278           
SHEET    1 AB6 2 VAL B 330  LEU B 331  0                                        
SHEET    2 AB6 2 GLY B 340  LEU B 341 -1  O  LEU B 341   N  VAL B 330           
SHEET    1 AB7 2 LYS B 349  THR B 351  0                                        
SHEET    2 AB7 2 ALA B 363  CYS B 365 -1  O  PHE B 364   N  VAL B 350           
SHEET    1 AB8 2 THR B 415  PRO B 417  0                                        
SHEET    2 AB8 2 PRO B 424  GLU B 426 -1  O  VAL B 425   N  LYS B 416           
SHEET    1 AB9 2 HIS B 433  LYS B 435  0                                        
SHEET    2 AB9 2 GLU B 444  CYS B 446 -1  O  TRP B 445   N  MET B 434           
LINK         SG  CYS A 150                ZN    ZN A 501     1555   1555  2.30  
LINK         SG  CYS A 154                ZN    ZN A 501     1555   1555  2.39  
LINK         SG  CYS A 166                ZN    ZN A 502     1555   1555  2.39  
LINK         SG  CYS A 169                ZN    ZN A 502     1555   1555  2.36  
LINK         SG  CYS A 196                ZN    ZN A 502     1555   1555  2.26  
LINK         SG  CYS A 201                ZN    ZN A 502     1555   1555  2.31  
LINK         SG  CYS A 212                ZN    ZN A 501     1555   1555  2.31  
LINK         NE2 HIS A 215                ZN    ZN A 501     1555   1555  2.03  
LINK         SG  CYS A 238                ZN    ZN A 503     1555   1555  2.32  
LINK         SG  CYS A 241                ZN    ZN A 503     1555   1555  2.35  
LINK         SG  CYS A 253                ZN    ZN A 504     1555   1555  2.32  
LINK         ND1 HIS A 257                ZN    ZN A 504     1555   1555  2.07  
LINK         SG  CYS A 260                ZN    ZN A 503     1555   1555  2.35  
LINK         SG  CYS A 263                ZN    ZN A 503     1555   1555  2.31  
LINK         SG  CYS A 289                ZN    ZN A 504     1555   1555  2.29  
LINK         SG  CYS A 293                ZN    ZN A 504     1555   1555  2.40  
LINK         SG  CYS A 332                ZN    ZN A 505     1555   1555  2.72  
LINK         SG  CYS A 352                ZN    ZN A 505     1555   1555  2.40  
LINK         N   GLY A 361                ZN    ZN A 505     1555   1555  2.63  
LINK         SG  CYS A 365                ZN    ZN A 506     1555   1555  2.28  
LINK         SG  CYS A 368                ZN    ZN A 506     1555   1555  2.26  
LINK         NE2 HIS A 373                ZN    ZN A 506     1555   1555  2.13  
LINK         SG  CYS A 377                ZN    ZN A 506     1555   1555  2.45  
LINK         SG  CYS A 418                ZN    ZN A 507     1555   1555  2.31  
LINK         SG  CYS A 421                ZN    ZN A 507     1555   1555  2.38  
LINK         SG  CYS A 436                ZN    ZN A 507     1555   1555  2.28  
LINK         SG  CYS A 441                ZN    ZN A 507     1555   1555  2.37  
LINK         SG  CYS A 446                ZN    ZN A 508     1555   1555  2.28  
LINK         SG  CYS A 449                ZN    ZN A 508     1555   1555  2.34  
LINK         SG  CYS A 457                ZN    ZN A 508     1555   1555  2.22  
LINK         NE2 HIS A 461                ZN    ZN A 508     1555   1555  2.07  
LINK         SG  CYS B 150                ZN    ZN B 501     1555   1555  2.29  
LINK         SG  CYS B 154                ZN    ZN B 501     1555   1555  2.37  
LINK         SG  CYS B 166                ZN    ZN B 502     1555   1555  2.39  
LINK         SG  CYS B 169                ZN    ZN B 502     1555   1555  2.36  
LINK         SG  CYS B 196                ZN    ZN B 502     1555   1555  2.29  
LINK         SG  CYS B 201                ZN    ZN B 502     1555   1555  2.30  
LINK         SG  CYS B 212                ZN    ZN B 501     1555   1555  2.32  
LINK         NE2 HIS B 215                ZN    ZN B 501     1555   1555  2.02  
LINK         SG  CYS B 238                ZN    ZN B 503     1555   1555  2.35  
LINK         SG  CYS B 241                ZN    ZN B 503     1555   1555  2.37  
LINK         SG  CYS B 253                ZN    ZN B 504     1555   1555  2.26  
LINK         ND1 HIS B 257                ZN    ZN B 504     1555   1555  2.09  
LINK         SG  CYS B 260                ZN    ZN B 503     1555   1555  2.33  
LINK         SG  CYS B 263                ZN    ZN B 503     1555   1555  2.26  
LINK         SG  CYS B 289                ZN    ZN B 504     1555   1555  2.34  
LINK         SG  CYS B 293                ZN    ZN B 504     1555   1555  2.38  
LINK         SG  CYS B 332                ZN    ZN B 505     1555   1555  2.69  
LINK         SG  CYS B 337                ZN    ZN B 505     1555   1555  2.87  
LINK         SG  CYS B 352                ZN    ZN B 505     1555   1555  2.42  
LINK         N   GLY B 361                ZN    ZN B 505     1555   1555  2.62  
LINK         SG  CYS B 365                ZN    ZN B 506     1555   1555  2.32  
LINK         SG  CYS B 368                ZN    ZN B 506     1555   1555  2.27  
LINK         NE2 HIS B 373                ZN    ZN B 506     1555   1555  2.15  
LINK         SG  CYS B 377                ZN    ZN B 506     1555   1555  2.40  
LINK         SG  CYS B 418                ZN    ZN B 507     1555   1555  2.31  
LINK         SG  CYS B 421                ZN    ZN B 507     1555   1555  2.41  
LINK         SG  CYS B 436                ZN    ZN B 507     1555   1555  2.26  
LINK         SG  CYS B 441                ZN    ZN B 507     1555   1555  2.38  
LINK         SG  CYS B 446                ZN    ZN B 508     1555   1555  2.29  
LINK         SG  CYS B 449                ZN    ZN B 508     1555   1555  2.32  
LINK         SG  CYS B 457                ZN    ZN B 508     1555   1555  2.23  
LINK         NE2 HIS B 461                ZN    ZN B 508     1555   1555  2.09  
CISPEP   1 GLY A  152    PRO A  153          0         4.18                     
CISPEP   2 SER A  246    PRO A  247          0         0.78                     
CISPEP   3 GLY B  152    PRO B  153          0         3.91                     
CISPEP   4 SER B  246    PRO B  247          0        -0.54                     
CISPEP   5 GLY B  336    CYS B  337          0         7.30                     
SITE     1 AC1  4 CYS A 150  CYS A 154  CYS A 212  HIS A 215                    
SITE     1 AC2  4 CYS A 166  CYS A 169  CYS A 196  CYS A 201                    
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 332  CYS A 337  CYS A 352  GLY A 361                    
SITE     1 AC6  4 CYS A 365  CYS A 368  HIS A 373  CYS A 377                    
SITE     1 AC7  4 CYS A 418  CYS A 421  CYS A 436  CYS A 441                    
SITE     1 AC8  4 CYS A 446  CYS A 449  CYS A 457  HIS A 461                    
SITE     1 AC9 11 GLN A  57  ASN A  58  LYS A 161  ARG A 163                    
SITE     2 AC9 11 LYS A 211  THR A 217  ARG A 455  HOH A 657                    
SITE     3 AC9 11 HOH A 673  HOH A 705  HOH A 776                               
SITE     1 AD1  7 VAL A 186  LEU A 187  PRO A 189  GLU A 207                    
SITE     2 AD1  7 PHE A 208  HOH A 610  HOH A 634                               
SITE     1 AD2  6 HIS A 227  ALA A 230  GLN A 252  HOH A 621                    
SITE     2 AD2  6 HOH A 622  HOH A 659                                          
SITE     1 AD3  4 TYR A 147  TRP A 183  LEU A 226  ILE A 229                    
SITE     1 AD4  4 CYS B 150  CYS B 154  CYS B 212  HIS B 215                    
SITE     1 AD5  4 CYS B 166  CYS B 169  CYS B 196  CYS B 201                    
SITE     1 AD6  4 CYS B 238  CYS B 241  CYS B 260  CYS B 263                    
SITE     1 AD7  4 CYS B 253  HIS B 257  CYS B 289  CYS B 293                    
SITE     1 AD8  4 CYS B 332  CYS B 337  CYS B 352  GLY B 361                    
SITE     1 AD9  4 CYS B 365  CYS B 368  HIS B 373  CYS B 377                    
SITE     1 AE1  4 CYS B 418  CYS B 421  CYS B 436  CYS B 441                    
SITE     1 AE2  4 CYS B 446  CYS B 449  CYS B 457  HIS B 461                    
SITE     1 AE3 11 GLN B  57  ASN B  58  LYS B 161  ARG B 163                    
SITE     2 AE3 11 LYS B 211  THR B 217  ARG B 455  HOH B 675                    
SITE     3 AE3 11 HOH B 686  HOH B 692  HOH B 697                               
SITE     1 AE4  7 HIS B 227  ALA B 230  VAL B 250  GLN B 252                    
SITE     2 AE4  7 HOH B 620  HOH B 621  HOH B 650                               
SITE     1 AE5  7 VAL B 186  LEU B 187  PRO B 189  GLU B 207                    
SITE     2 AE5  7 PHE B 208  HOH B 608  HOH B 638                               
SITE     1 AE6  4 TYR B 147  TRP B 183  LEU B 226  ILE B 229                    
CRYST1   67.310   67.320  206.230  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014857  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014854  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004849        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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