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Database: PDB
Entry: 5C23
LinkDB: 5C23
Original site: 5C23 
HEADER    LIGASE                                  15-JUN-15   5C23              
TITLE     PARKIN (S65DUBLR0RBR)                                                 
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    E3 LIGASE2, 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 5C23    1       JRNL                                     
REVDAT   2   19-AUG-15 5C23    1       JRNL                                     
REVDAT   1   29-JUL-15 5C23    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.    2.37 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) : 2.37                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.16                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 37544                          
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)  : 0.221                          
REMARK   3   R VALUE            (WORKING SET)  : 0.220                          
REMARK   3   FREE R VALUE                      : 0.241                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.940                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1854                           
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               : 19                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.37                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.44                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.79                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2770                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2419                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2625                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2406                   
REMARK   3   BIN FREE R VALUE                        : 0.2672                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.23                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 145                      
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            : 6042                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 313                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.97                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.20130                                             
REMARK   3    B22 (A**2) : -6.84960                                             
REMARK   3    B33 (A**2) : 12.05100                                             
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) : 0.376               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.413               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.238               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.381               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.234               
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      : 0.912                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6236   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8450   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2138   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 162    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 910    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6236   ; 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   : 782    ; 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   : 6857   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.007                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.87                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.74                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.01                    
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):   -6.3596    2.9978   43.1001           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1016 T22:   -0.1311                                    
REMARK   3     T33:   -0.2264 T12:   -0.0187                                    
REMARK   3     T13:   -0.0068 T23:    0.0064                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9860 L22:    1.1665                                    
REMARK   3     L33:    1.8479 L12:   -0.4733                                    
REMARK   3     L13:   -1.0038 L23:    0.9370                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0361 S12:    0.0512 S13:   -0.0020                     
REMARK   3     S21:   -0.0124 S22:   -0.0207 S23:    0.0400                     
REMARK   3     S31:    0.0714 S32:   -0.1633 S33:    0.0568                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -19.5775  -10.2134    8.3176           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1036 T22:   -0.1427                                    
REMARK   3     T33:   -0.2200 T12:   -0.0179                                    
REMARK   3     T13:    0.0018 T23:   -0.0057                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1729 L22:    1.0031                                    
REMARK   3     L33:    1.9459 L12:   -0.5052                                    
REMARK   3     L13:    0.9811 L23:   -0.9779                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0445 S12:   -0.0148 S13:    0.0572                     
REMARK   3     S21:    0.0753 S22:   -0.0234 S23:   -0.0187                     
REMARK   3     S31:   -0.1940 S32:    0.0520 S33:    0.0679                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5C23 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_1000210897.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-FEB-15                          
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                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : .9172                              
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 : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35690                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.370                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 23.160                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.17000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.17000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 5C1Z                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, LISO4, 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       33.13950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      102.81950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.14500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      102.81950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.13950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.14500            
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    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    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    ARG A  72      110.09   -160.11                                   
REMARK 500    ASN A  81       42.10    -94.29                                   
REMARK 500    THR A 168      -62.63    -90.18                                   
REMARK 500    GLU A 221       76.93    -66.45                                   
REMARK 500    GLN A 252       32.70    -85.65                                   
REMARK 500    LEU A 283      -44.97   -148.06                                   
REMARK 500    ARG A 442       26.49     48.73                                   
REMARK 500    ARG B  72      109.81   -160.75                                   
REMARK 500    ASN B  81       42.41    -93.70                                   
REMARK 500    LYS B 151       39.20    -89.61                                   
REMARK 500    THR B 168      -62.01    -98.21                                   
REMARK 500    GLU B 221       77.05    -66.40                                   
REMARK 500    GLN B 252       34.35    -84.85                                   
REMARK 500    LEU B 283      -44.51   -149.74                                   
REMARK 500    PHE B 381      111.15   -167.09                                   
REMARK 500    CYS B 441      -65.08    -93.30                                   
REMARK 500    ARG B 442       23.87     48.77                                   
REMARK 500    HIS B 461       69.68   -151.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 150   SG                                                     
REMARK 620 2 CYS A 154   SG  111.1                                              
REMARK 620 3 CYS A 212   SG  116.1 110.2                                        
REMARK 620 4 HIS A 215   NE2 105.8 106.4 106.6                                  
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  110.7                                              
REMARK 620 3 CYS A 196   SG  114.5 104.2                                        
REMARK 620 4 CYS A 201   SG  111.9 110.8 104.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 238   SG                                                     
REMARK 620 2 CYS A 241   SG  108.2                                              
REMARK 620 3 CYS A 260   SG  110.6 114.4                                        
REMARK 620 4 CYS A 263   SG  111.6 110.0 101.9                                  
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 103.7                                              
REMARK 620 3 CYS A 289   SG  109.1 100.4                                        
REMARK 620 4 CYS A 293   SG  121.7 107.3 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 505  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 332   SG                                                     
REMARK 620 2 CYS A 337   SG   99.0                                              
REMARK 620 3 CYS A 352   SG  117.9  87.8                                        
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  110.9                                              
REMARK 620 3 HIS A 373   NE2 120.8  93.5                                        
REMARK 620 4 CYS A 377   SG  101.0 116.9 114.7                                  
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 436   SG  114.7                                              
REMARK 620 3 CYS A 441   SG   98.8 120.4                                        
REMARK 620 N                    1     2                                         
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  127.0                                              
REMARK 620 3 CYS A 457   SG  111.2 101.3                                        
REMARK 620 4 HIS A 461   NE2 111.0  97.1 107.1                                  
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  112.8                                              
REMARK 620 3 CYS B 212   SG  113.8 110.3                                        
REMARK 620 4 HIS B 215   NE2 106.1 105.3 108.0                                  
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  110.1                                              
REMARK 620 3 CYS B 196   SG  109.3 104.5                                        
REMARK 620 4 CYS B 201   SG  113.3 112.3 106.9                                  
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  106.6                                              
REMARK 620 3 CYS B 260   SG  113.2 115.8                                        
REMARK 620 4 CYS B 263   SG  112.4 106.7 101.9                                  
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 104.5                                              
REMARK 620 3 CYS B 289   SG  112.9 100.7                                        
REMARK 620 4 CYS B 293   SG  118.8 104.3 113.0                                  
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   93.4                                              
REMARK 620 3 CYS B 352   SG  119.2  92.0                                        
REMARK 620 N                    1     2                                         
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  111.3                                              
REMARK 620 3 HIS B 373   NE2 121.2  92.9                                        
REMARK 620 4 CYS B 377   SG  103.5 116.4 112.2                                  
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  109.6                                              
REMARK 620 3 CYS B 436   SG  116.2 100.0                                        
REMARK 620 4 CYS B 441   SG  105.2 106.9 118.3                                  
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  127.2                                              
REMARK 620 3 CYS B 457   SG  115.4  99.8                                        
REMARK 620 4 HIS B 461   NE2 106.6  98.2 107.3                                  
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 GOL 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 SO4 A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 513                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 511                 
DBREF  5C23 A    1   465  UNP    O60260   PRKN2_HUMAN      1    465             
DBREF  5C23 B    1   465  UNP    O60260   PRKN2_HUMAN      1    465             
SEQADV 5C23 ASP A   65  UNP  O60260    SER    65 CONFLICT                       
SEQADV 5C23     A       UNP  O60260    GLY    84 DELETION                       
SEQADV 5C23     A       UNP  O60260    GLY    85 DELETION                       
SEQADV 5C23     A       UNP  O60260    ASP    86 DELETION                       
SEQADV 5C23     A       UNP  O60260    ASP    87 DELETION                       
SEQADV 5C23     A       UNP  O60260    PRO    88 DELETION                       
SEQADV 5C23     A       UNP  O60260    ARG    89 DELETION                       
SEQADV 5C23     A       UNP  O60260    ASN    90 DELETION                       
SEQADV 5C23     A       UNP  O60260    ALA    91 DELETION                       
SEQADV 5C23     A       UNP  O60260    ALA    92 DELETION                       
SEQADV 5C23     A       UNP  O60260    GLY    93 DELETION                       
SEQADV 5C23     A       UNP  O60260    GLY    94 DELETION                       
SEQADV 5C23     A       UNP  O60260    CYS    95 DELETION                       
SEQADV 5C23     A       UNP  O60260    GLU    96 DELETION                       
SEQADV 5C23     A       UNP  O60260    ARG    97 DELETION                       
SEQADV 5C23     A       UNP  O60260    GLU    98 DELETION                       
SEQADV 5C23     A       UNP  O60260    PRO    99 DELETION                       
SEQADV 5C23     A       UNP  O60260    GLN   100 DELETION                       
SEQADV 5C23     A       UNP  O60260    SER   101 DELETION                       
SEQADV 5C23     A       UNP  O60260    LEU   102 DELETION                       
SEQADV 5C23     A       UNP  O60260    THR   103 DELETION                       
SEQADV 5C23     A       UNP  O60260    ARG   104 DELETION                       
SEQADV 5C23     A       UNP  O60260    VAL   105 DELETION                       
SEQADV 5C23     A       UNP  O60260    ASP   106 DELETION                       
SEQADV 5C23     A       UNP  O60260    LEU   107 DELETION                       
SEQADV 5C23     A       UNP  O60260    SER   108 DELETION                       
SEQADV 5C23     A       UNP  O60260    SER   109 DELETION                       
SEQADV 5C23     A       UNP  O60260    SER   110 DELETION                       
SEQADV 5C23     A       UNP  O60260    VAL   111 DELETION                       
SEQADV 5C23     A       UNP  O60260    LEU   112 DELETION                       
SEQADV 5C23     A       UNP  O60260    PRO   113 DELETION                       
SEQADV 5C23     A       UNP  O60260    GLY   114 DELETION                       
SEQADV 5C23     A       UNP  O60260    ASP   115 DELETION                       
SEQADV 5C23     A       UNP  O60260    SER   116 DELETION                       
SEQADV 5C23     A       UNP  O60260    VAL   117 DELETION                       
SEQADV 5C23     A       UNP  O60260    GLY   118 DELETION                       
SEQADV 5C23     A       UNP  O60260    LEU   119 DELETION                       
SEQADV 5C23     A       UNP  O60260    ALA   120 DELETION                       
SEQADV 5C23     A       UNP  O60260    VAL   121 DELETION                       
SEQADV 5C23     A       UNP  O60260    ILE   122 DELETION                       
SEQADV 5C23     A       UNP  O60260    LEU   123 DELETION                       
SEQADV 5C23     A       UNP  O60260    HIS   124 DELETION                       
SEQADV 5C23     A       UNP  O60260    THR   125 DELETION                       
SEQADV 5C23     A       UNP  O60260    ASP   126 DELETION                       
SEQADV 5C23     A       UNP  O60260    SER   127 DELETION                       
SEQADV 5C23     A       UNP  O60260    ARG   128 DELETION                       
SEQADV 5C23     A       UNP  O60260    LYS   129 DELETION                       
SEQADV 5C23     A       UNP  O60260    ASP   130 DELETION                       
SEQADV 5C23     A       UNP  O60260    SER   131 DELETION                       
SEQADV 5C23     A       UNP  O60260    PRO   132 DELETION                       
SEQADV 5C23     A       UNP  O60260    PRO   133 DELETION                       
SEQADV 5C23     A       UNP  O60260    ALA   134 DELETION                       
SEQADV 5C23     A       UNP  O60260    GLY   135 DELETION                       
SEQADV 5C23     A       UNP  O60260    SER   136 DELETION                       
SEQADV 5C23     A       UNP  O60260    PRO   137 DELETION                       
SEQADV 5C23     A       UNP  O60260    ALA   138 DELETION                       
SEQADV 5C23     A       UNP  O60260    GLY   139 DELETION                       
SEQADV 5C23     A       UNP  O60260    ARG   140 DELETION                       
SEQADV 5C23     A       UNP  O60260    SER   141 DELETION                       
SEQADV 5C23     A       UNP  O60260    ILE   142 DELETION                       
SEQADV 5C23     A       UNP  O60260    TYR   143 DELETION                       
SEQADV 5C23 ASP B   65  UNP  O60260    SER    65 CONFLICT                       
SEQADV 5C23     B       UNP  O60260    GLY    84 DELETION                       
SEQADV 5C23     B       UNP  O60260    GLY    85 DELETION                       
SEQADV 5C23     B       UNP  O60260    ASP    86 DELETION                       
SEQADV 5C23     B       UNP  O60260    ASP    87 DELETION                       
SEQADV 5C23     B       UNP  O60260    PRO    88 DELETION                       
SEQADV 5C23     B       UNP  O60260    ARG    89 DELETION                       
SEQADV 5C23     B       UNP  O60260    ASN    90 DELETION                       
SEQADV 5C23     B       UNP  O60260    ALA    91 DELETION                       
SEQADV 5C23     B       UNP  O60260    ALA    92 DELETION                       
SEQADV 5C23     B       UNP  O60260    GLY    93 DELETION                       
SEQADV 5C23     B       UNP  O60260    GLY    94 DELETION                       
SEQADV 5C23     B       UNP  O60260    CYS    95 DELETION                       
SEQADV 5C23     B       UNP  O60260    GLU    96 DELETION                       
SEQADV 5C23     B       UNP  O60260    ARG    97 DELETION                       
SEQADV 5C23     B       UNP  O60260    GLU    98 DELETION                       
SEQADV 5C23     B       UNP  O60260    PRO    99 DELETION                       
SEQADV 5C23     B       UNP  O60260    GLN   100 DELETION                       
SEQADV 5C23     B       UNP  O60260    SER   101 DELETION                       
SEQADV 5C23     B       UNP  O60260    LEU   102 DELETION                       
SEQADV 5C23     B       UNP  O60260    THR   103 DELETION                       
SEQADV 5C23     B       UNP  O60260    ARG   104 DELETION                       
SEQADV 5C23     B       UNP  O60260    VAL   105 DELETION                       
SEQADV 5C23     B       UNP  O60260    ASP   106 DELETION                       
SEQADV 5C23     B       UNP  O60260    LEU   107 DELETION                       
SEQADV 5C23     B       UNP  O60260    SER   108 DELETION                       
SEQADV 5C23     B       UNP  O60260    SER   109 DELETION                       
SEQADV 5C23     B       UNP  O60260    SER   110 DELETION                       
SEQADV 5C23     B       UNP  O60260    VAL   111 DELETION                       
SEQADV 5C23     B       UNP  O60260    LEU   112 DELETION                       
SEQADV 5C23     B       UNP  O60260    PRO   113 DELETION                       
SEQADV 5C23     B       UNP  O60260    GLY   114 DELETION                       
SEQADV 5C23     B       UNP  O60260    ASP   115 DELETION                       
SEQADV 5C23     B       UNP  O60260    SER   116 DELETION                       
SEQADV 5C23     B       UNP  O60260    VAL   117 DELETION                       
SEQADV 5C23     B       UNP  O60260    GLY   118 DELETION                       
SEQADV 5C23     B       UNP  O60260    LEU   119 DELETION                       
SEQADV 5C23     B       UNP  O60260    ALA   120 DELETION                       
SEQADV 5C23     B       UNP  O60260    VAL   121 DELETION                       
SEQADV 5C23     B       UNP  O60260    ILE   122 DELETION                       
SEQADV 5C23     B       UNP  O60260    LEU   123 DELETION                       
SEQADV 5C23     B       UNP  O60260    HIS   124 DELETION                       
SEQADV 5C23     B       UNP  O60260    THR   125 DELETION                       
SEQADV 5C23     B       UNP  O60260    ASP   126 DELETION                       
SEQADV 5C23     B       UNP  O60260    SER   127 DELETION                       
SEQADV 5C23     B       UNP  O60260    ARG   128 DELETION                       
SEQADV 5C23     B       UNP  O60260    LYS   129 DELETION                       
SEQADV 5C23     B       UNP  O60260    ASP   130 DELETION                       
SEQADV 5C23     B       UNP  O60260    SER   131 DELETION                       
SEQADV 5C23     B       UNP  O60260    PRO   132 DELETION                       
SEQADV 5C23     B       UNP  O60260    PRO   133 DELETION                       
SEQADV 5C23     B       UNP  O60260    ALA   134 DELETION                       
SEQADV 5C23     B       UNP  O60260    GLY   135 DELETION                       
SEQADV 5C23     B       UNP  O60260    SER   136 DELETION                       
SEQADV 5C23     B       UNP  O60260    PRO   137 DELETION                       
SEQADV 5C23     B       UNP  O60260    ALA   138 DELETION                       
SEQADV 5C23     B       UNP  O60260    GLY   139 DELETION                       
SEQADV 5C23     B       UNP  O60260    ARG   140 DELETION                       
SEQADV 5C23     B       UNP  O60260    SER   141 DELETION                       
SEQADV 5C23     B       UNP  O60260    ILE   142 DELETION                       
SEQADV 5C23     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 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  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 ASP          
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    GOL  A 509       6                                                       
HET    GOL  A 510       6                                                       
HET    SO4  A 511       5                                                       
HET    SO4  A 512       5                                                       
HET     CL  A 513       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    GOL  B 509       6                                                       
HET    GOL  B 510       6                                                       
HET    SO4  B 511       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   ZN    16(ZN 2+)                                                    
FORMUL  11  GOL    4(C3 H8 O3)                                                  
FORMUL  13  SO4    3(O4 S 2-)                                                   
FORMUL  15   CL    CL 1-                                                        
FORMUL  27  HOH   *313(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  ARG A  275  1                                  15    
HELIX    6 AA6 GLU A  300  LEU A  307  5                                   8    
HELIX    7 AA7 GLY A  308  GLY A  328  1                                  21    
HELIX    8 AA8 ASP A  394  ALA A  401  1                                   8    
HELIX    9 AA9 ASN A  454  TRP A  462  1                                   9    
HELIX   10 AB1 SER B   22  GLY B   35  1                                  14    
HELIX   11 AB2 PRO B   37  ASP B   39  5                                   3    
HELIX   12 AB3 CYS B  182  ILE B  188  1                                   7    
HELIX   13 AB4 LEU B  261  ARG B  275  1                                  15    
HELIX   14 AB5 GLU B  300  LEU B  307  5                                   8    
HELIX   15 AB6 GLY B  308  GLY B  328  1                                  21    
HELIX   16 AB7 ASP B  394  ALA B  401  1                                   8    
HELIX   17 AB8 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  GLY A 284   N  ASP A 280           
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 LYS A 416  PRO A 417  0                                        
SHEET    2 AA8 2 PRO A 424  VAL A 425 -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  GLN B 165   O  GLU B 207           
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  GLY B 284   N  ASP B 280           
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  2.44  
LINK         SG  CYS A 166                ZN    ZN A 502     1555   1555  2.35  
LINK         SG  CYS A 169                ZN    ZN A 502     1555   1555  2.27  
LINK         SG  CYS A 196                ZN    ZN A 502     1555   1555  2.34  
LINK         SG  CYS A 201                ZN    ZN A 502     1555   1555  2.29  
LINK         SG  CYS A 212                ZN    ZN A 501     1555   1555  2.34  
LINK         NE2 HIS A 215                ZN    ZN A 501     1555   1555  1.97  
LINK         SG  CYS A 238                ZN    ZN A 503     1555   1555  2.31  
LINK         SG  CYS A 241                ZN    ZN A 503     1555   1555  2.26  
LINK         SG  CYS A 253                ZN    ZN A 504     1555   1555  2.46  
LINK         ND1 HIS A 257                ZN    ZN A 504     1555   1555  1.95  
LINK         SG  CYS A 260                ZN    ZN A 503     1555   1555  2.31  
LINK         SG  CYS A 263                ZN    ZN A 503     1555   1555  2.33  
LINK         SG  CYS A 289                ZN    ZN A 504     1555   1555  2.32  
LINK         SG  CYS A 293                ZN    ZN A 504     1555   1555  2.47  
LINK         SG  CYS A 332                ZN    ZN A 505     1555   1555  2.24  
LINK         SG  CYS A 337                ZN    ZN A 505     1555   1555  2.63  
LINK         SG  CYS A 352                ZN    ZN A 505     1555   1555  2.72  
LINK         SG  CYS A 365                ZN    ZN A 506     1555   1555  2.50  
LINK         SG  CYS A 368                ZN    ZN A 506     1555   1555  2.28  
LINK         NE2 HIS A 373                ZN    ZN A 506     1555   1555  2.46  
LINK         SG  CYS A 377                ZN    ZN A 506     1555   1555  2.48  
LINK         SG  CYS A 418                ZN    ZN A 507     1555   1555  2.40  
LINK         SG  CYS A 436                ZN    ZN A 507     1555   1555  2.18  
LINK         SG  CYS A 441                ZN    ZN A 507     1555   1555  2.50  
LINK         SG  CYS A 446                ZN    ZN A 508     1555   1555  2.20  
LINK         SG  CYS A 449                ZN    ZN A 508     1555   1555  2.37  
LINK         SG  CYS A 457                ZN    ZN A 508     1555   1555  2.41  
LINK         NE2 HIS A 461                ZN    ZN A 508     1555   1555  2.12  
LINK         SG  CYS B 150                ZN    ZN B 501     1555   1555  2.23  
LINK         SG  CYS B 154                ZN    ZN B 501     1555   1555  2.40  
LINK         SG  CYS B 166                ZN    ZN B 502     1555   1555  2.38  
LINK         SG  CYS B 169                ZN    ZN B 502     1555   1555  2.25  
LINK         SG  CYS B 196                ZN    ZN B 502     1555   1555  2.30  
LINK         SG  CYS B 201                ZN    ZN B 502     1555   1555  2.28  
LINK         SG  CYS B 212                ZN    ZN B 501     1555   1555  2.36  
LINK         NE2 HIS B 215                ZN    ZN B 501     1555   1555  2.03  
LINK         SG  CYS B 238                ZN    ZN B 503     1555   1555  2.35  
LINK         SG  CYS B 241                ZN    ZN B 503     1555   1555  2.33  
LINK         SG  CYS B 253                ZN    ZN B 504     1555   1555  2.43  
LINK         ND1 HIS B 257                ZN    ZN B 504     1555   1555  1.97  
LINK         SG  CYS B 260                ZN    ZN B 503     1555   1555  2.32  
LINK         SG  CYS B 263                ZN    ZN B 503     1555   1555  2.28  
LINK         SG  CYS B 289                ZN    ZN B 504     1555   1555  2.27  
LINK         SG  CYS B 293                ZN    ZN B 504     1555   1555  2.56  
LINK         SG  CYS B 332                ZN    ZN B 505     1555   1555  2.30  
LINK         SG  CYS B 337                ZN    ZN B 505     1555   1555  2.81  
LINK         SG  CYS B 352                ZN    ZN B 505     1555   1555  2.74  
LINK         SG  CYS B 365                ZN    ZN B 506     1555   1555  2.41  
LINK         SG  CYS B 368                ZN    ZN B 506     1555   1555  2.25  
LINK         NE2 HIS B 373                ZN    ZN B 506     1555   1555  2.47  
LINK         SG  CYS B 377                ZN    ZN B 506     1555   1555  2.45  
LINK         SG  CYS B 418                ZN    ZN B 507     1555   1555  2.28  
LINK         SG  CYS B 421                ZN    ZN B 507     1555   1555  2.42  
LINK         SG  CYS B 436                ZN    ZN B 507     1555   1555  2.21  
LINK         SG  CYS B 441                ZN    ZN B 507     1555   1555  2.36  
LINK         SG  CYS B 446                ZN    ZN B 508     1555   1555  2.38  
LINK         SG  CYS B 449                ZN    ZN B 508     1555   1555  2.33  
LINK         SG  CYS B 457                ZN    ZN B 508     1555   1555  2.48  
LINK         NE2 HIS B 461                ZN    ZN B 508     1555   1555  2.17  
CISPEP   1 GLY A  152    PRO A  153          0         3.71                     
CISPEP   2 SER A  246    PRO A  247          0         1.90                     
CISPEP   3 GLY B  152    PRO B  153          0         2.46                     
CISPEP   4 SER B  246    PRO B  247          0         1.92                     
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  3 CYS A 332  CYS A 337  CYS A 352                               
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  5 VAL A 186  LEU A 187  GLU A 207  PHE A 208                    
SITE     2 AC9  5 HOH A 623                                                     
SITE     1 AD1  8 HIS A 227  ALA A 230  GLN A 252  ARG A 256                    
SITE     2 AD1  8 TRP A 403  GLU A 404  VAL A 465  HOH A 607                    
SITE     1 AD2  9 GLN A  57  ASN A  58  LYS A 161  ARG A 163                    
SITE     2 AD2  9 LYS A 211  THR A 217  ARG A 455  HOH A 614                    
SITE     3 AD2  9 HOH A 621                                                     
SITE     1 AD3  3 LYS A 416  TRP A 447  ASN A 448                               
SITE     1 AD4  5 PHE A 146  TYR A 147  TRP A 183  LEU A 226                    
SITE     2 AD4  5 ILE A 229                                                     
SITE     1 AD5  4 CYS B 150  CYS B 154  CYS B 212  HIS B 215                    
SITE     1 AD6  4 CYS B 166  CYS B 169  CYS B 196  CYS B 201                    
SITE     1 AD7  4 CYS B 238  CYS B 241  CYS B 260  CYS B 263                    
SITE     1 AD8  4 CYS B 253  HIS B 257  CYS B 289  CYS B 293                    
SITE     1 AD9  3 CYS B 332  CYS B 337  CYS B 352                               
SITE     1 AE1  4 CYS B 365  CYS B 368  HIS B 373  CYS B 377                    
SITE     1 AE2  4 CYS B 418  CYS B 421  CYS B 436  CYS B 441                    
SITE     1 AE3  4 CYS B 446  CYS B 449  CYS B 457  HIS B 461                    
SITE     1 AE4  5 VAL B 186  GLU B 207  PHE B 208  HOH B 602                    
SITE     2 AE4  5 HOH B 623                                                     
SITE     1 AE5  7 HIS B 227  ALA B 230  GLN B 252  ARG B 256                    
SITE     2 AE5  7 GLU B 404  VAL B 465  HOH B 619                               
SITE     1 AE6  9 ASN B  58  LYS B 161  ARG B 163  LYS B 211                    
SITE     2 AE6  9 THR B 217  ARG B 455  HOH B 613  HOH B 618                    
SITE     3 AE6  9 HOH B 660                                                     
CRYST1   66.279   66.290  205.639  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      0.015088  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015085  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004863        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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