GenomeNet

Database: PDB
Entry: 6HUE
LinkDB: 6HUE
Original site: 6HUE 
HEADER    LIGASE                                  07-OCT-18   6HUE              
TITLE     PARKINS65N                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE PARKIN;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PARKIN,PARKIN RBR E3 UBIQUITIN-PROTEIN LIGASE,PARKINSON     
COMPND   5 JUVENILE DISEASE PROTEIN 2,PARKINSON DISEASE PROTEIN 2;              
COMPND   6 EC: 2.3.2.31;                                                        
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: PRKN, PARK2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    E3 LIGASE, LIGASE                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.G.MCWILLIAMS,E.BARINI,R.POHJOLAN-PIRHONEN,S.P.BROOKS,F.SINGH,       
AUTHOR   2 S.BUREL,K.BALK,A.KUMAR,L.MONTAVA-GARRIGA,A.R.PRESCOTT,S.M.HASSOUN,   
AUTHOR   3 F.MOUTON-LIGER,G.BALL,R.HILLS,A.KNEBEL,A.ULUSOY,D.A.DI MONTE,        
AUTHOR   4 J.TAMJAR,O.ANTICO,K.FEARS,L.SMITH,R.BRAMBILLA,E.PALIN,M.VALORI,      
AUTHOR   5 J.EEROLA-RAUTIO,P.TIENARI,O.CORTI,S.B.DUNNETT,I.G.GANLEY,            
AUTHOR   6 A.SUOMALAINEN,M.M.K.MUQIT                                            
REVDAT   3   30-SEP-20 6HUE    1       JRNL                                     
REVDAT   2   21-NOV-18 6HUE    1       JRNL                                     
REVDAT   1   17-OCT-18 6HUE    0                                                
JRNL        AUTH   T.G.MCWILLIAMS,E.BARINI,R.POHJOLAN-PIRHONEN,S.P.BROOKS,      
JRNL        AUTH 2 F.SINGH,S.BUREL,K.BALK,A.KUMAR,L.MONTAVA-GARRIGA,            
JRNL        AUTH 3 A.R.PRESCOTT,S.M.HASSOUN,F.MOUTON-LIGER,G.BALL,R.HILLS,      
JRNL        AUTH 4 A.KNEBEL,A.ULUSOY,D.A.DI MONTE,J.TAMJAR,O.ANTICO,K.FEARS,    
JRNL        AUTH 5 L.SMITH,R.BRAMBILLA,E.PALIN,M.VALORI,J.EEROLA-RAUTIO,        
JRNL        AUTH 6 P.TIENARI,O.CORTI,S.B.DUNNETT,I.G.GANLEY,A.SUOMALAINEN,      
JRNL        AUTH 7 M.M.K.MUQIT                                                  
JRNL        TITL   PHOSPHORYLATION OF PARKIN AT SERINE 65 IS ESSENTIAL FOR ITS  
JRNL        TITL 2 ACTIVATION IN VIVO .                                         
JRNL        REF    OPEN BIOLOGY                  V.   8       2018              
JRNL        REFN                   ESSN 2046-2441                               
JRNL        PMID   30404819                                                     
JRNL        DOI    10.1098/RSOB.180108                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 20094                          
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) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1095                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.92                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1425                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3690                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.3990                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5992                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 157                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.58000                                              
REMARK   3    B22 (A**2) : 4.08000                                              
REMARK   3    B33 (A**2) : -5.66000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.422         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.407         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.598        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6380 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5847 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8645 ; 1.579 ; 1.944       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13399 ; 1.037 ; 3.008       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   792 ; 6.838 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   316 ;36.863 ;23.481       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1040 ;17.971 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    56 ;18.531 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   913 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7257 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1551 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3084 ; 3.907 ; 6.463       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3083 ; 3.907 ; 6.463       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3847 ; 6.273 ; 9.667       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3848 ; 6.272 ; 9.667       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3296 ; 3.683 ; 6.668       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3296 ; 3.683 ; 6.668       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4780 ; 6.031 ; 9.898       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 25053 ;11.337 ;59.669       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 25028 ;11.332 ;59.683       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6HUE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-OCT-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200012335.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-NOV-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-1                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.966                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21291                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.980                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.12500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: PHASER                                                
REMARK 200 STARTING MODEL: 5C1Z                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BIS-TRIS PH 5.5, 200MM LISO4 AND   
REMARK 280  20% PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.0K      
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       33.21550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      103.34500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.43500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      103.34500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.21550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.43500            
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    77                                                      
REMARK 465     GLN A    78                                                      
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   379                                                      
REMARK 465     VAL A   380                                                      
REMARK 465     PHE A   381                                                      
REMARK 465     GLU A   382                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     SER A   384                                                      
REMARK 465     GLY A   385                                                      
REMARK 465     THR A   386                                                      
REMARK 465     THR A   387                                                      
REMARK 465     THR A   388                                                      
REMARK 465     GLN A   389                                                      
REMARK 465     ALA A   390                                                      
REMARK 465     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    77                                                      
REMARK 465     GLN B    78                                                      
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     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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    TYR B   285     OH   TYR B   315              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A   9      149.13   -178.09                                   
REMARK 500    CYS A 154      -37.36    -39.39                                   
REMARK 500    GLN A 155       43.70     39.46                                   
REMARK 500    THR A 168      -68.84   -104.61                                   
REMARK 500    ARG A 170       28.26     80.68                                   
REMARK 500    ASN A 190       27.38     48.89                                   
REMARK 500    SER A 198      128.31    -39.82                                   
REMARK 500    GLN A 252       49.96    -88.88                                   
REMARK 500    GLN A 282       49.36   -106.58                                   
REMARK 500    LEU A 283      -34.25   -173.57                                   
REMARK 500    ARG A 334      132.44    -36.50                                   
REMARK 500    GLU A 367      -77.19    -74.87                                   
REMARK 500    CYS A 441      -64.03   -133.59                                   
REMARK 500    HIS A 461       55.77   -150.75                                   
REMARK 500    SER B   9      146.40   -172.39                                   
REMARK 500    ASN B  52      -50.73    -26.57                                   
REMARK 500    VAL B  56      -38.64    -38.57                                   
REMARK 500    GLN B  64      -11.91     89.99                                   
REMARK 500    THR B 168      -67.61   -101.04                                   
REMARK 500    HIS B 200       -3.46     77.28                                   
REMARK 500    HIS B 227      -58.27    -29.33                                   
REMARK 500    THR B 242        8.87     57.76                                   
REMARK 500    GLN B 282       38.85    -92.65                                   
REMARK 500    LEU B 283      -62.48   -159.94                                   
REMARK 500    MET B 327       51.88    -99.77                                   
REMARK 500    CYS B 352       77.85   -103.27                                   
REMARK 500    GLU B 367      -73.26    -66.78                                   
REMARK 500    ARG B 420      -70.53    -92.90                                   
REMARK 500    HIS B 422       -4.94     73.18                                   
REMARK 500    CYS B 441      -59.75   -131.68                                   
REMARK 500    HIS B 461       47.04   -154.45                                   
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  107.1                                              
REMARK 620 3 CYS A 212   SG  115.7 101.9                                        
REMARK 620 4 HIS A 215   NE2 134.0  98.3  95.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 166   SG                                                     
REMARK 620 2 CYS A 169   SG   98.6                                              
REMARK 620 3 CYS A 196   SG  128.4 108.4                                        
REMARK 620 4 CYS A 201   SG  107.2 101.7 109.0                                  
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  102.0                                              
REMARK 620 3 CYS A 260   SG  122.3 116.3                                        
REMARK 620 4 CYS A 263   SG  103.1 107.7 104.1                                  
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 112.3                                              
REMARK 620 3 CYS A 289   SG  108.7 116.8                                        
REMARK 620 4 CYS A 293   SG  111.5  99.4 107.9                                  
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   88.6                                              
REMARK 620 3 CYS A 352   SG   83.8 105.5                                        
REMARK 620 4 GLY A 361   N   151.8 118.6  81.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 506  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 365   SG                                                     
REMARK 620 2 CYS A 368   SG  107.4                                              
REMARK 620 3 HIS A 373   NE2 122.5 102.0                                        
REMARK 620 4 CYS A 377   SG  105.6 110.7 108.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 507  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 418   SG                                                     
REMARK 620 2 CYS A 421   SG   97.9                                              
REMARK 620 3 CYS A 436   SG  100.8  91.8                                        
REMARK 620 4 CYS A 441   SG   99.9 113.7 144.3                                  
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  107.2                                              
REMARK 620 3 CYS A 457   SG  114.7 110.6                                        
REMARK 620 4 HIS A 461   NE2 109.6 114.4 100.4                                  
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  102.8                                              
REMARK 620 3 CYS B 212   SG  117.4 103.8                                        
REMARK 620 4 HIS B 215   NE2 125.2  99.3 104.7                                  
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  108.8                                              
REMARK 620 3 CYS B 196   SG  114.6 117.5                                        
REMARK 620 4 CYS B 201   SG  105.9 102.6 105.9                                  
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  100.2                                              
REMARK 620 3 CYS B 260   SG  124.7 121.4                                        
REMARK 620 4 CYS B 263   SG  110.0 101.7  96.3                                  
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 110.9                                              
REMARK 620 3 CYS B 289   SG  110.7 117.1                                        
REMARK 620 4 CYS B 293   SG  109.4  99.7 108.4                                  
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  144.9                                              
REMARK 620 3 CYS B 352   SG   95.2 102.2                                        
REMARK 620 4 GLY B 361   N   140.6  73.7  77.0                                  
REMARK 620 5 HOH B 602   O   108.1  83.2 130.6  57.2                            
REMARK 620 N                    1     2     3     4                             
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   98.8                                              
REMARK 620 3 HIS B 373   NE2 116.3 106.7                                        
REMARK 620 4 CYS B 377   SG  106.7 111.3 115.7                                  
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   93.8                                              
REMARK 620 3 CYS B 436   SG  102.4  98.8                                        
REMARK 620 4 CYS B 441   SG   99.3 120.2 133.6                                  
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   93.7                                              
REMARK 620 3 CYS B 457   SG  116.1 116.0                                        
REMARK 620 4 HIS B 461   NE2 102.3  96.4 126.2                                  
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  6HUE A    1   465  UNP    O60260   PRKN_HUMAN       1    465             
DBREF  6HUE B    1   465  UNP    O60260   PRKN_HUMAN       1    465             
SEQADV 6HUE ASN A   65  UNP  O60260    SER    65 ENGINEERED MUTATION            
SEQADV 6HUE     A       UNP  O60260    GLY    84 DELETION                       
SEQADV 6HUE     A       UNP  O60260    GLY    85 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ASP    86 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ASP    87 DELETION                       
SEQADV 6HUE     A       UNP  O60260    PRO    88 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ARG    89 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ASN    90 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ALA    91 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ALA    92 DELETION                       
SEQADV 6HUE     A       UNP  O60260    GLY    93 DELETION                       
SEQADV 6HUE     A       UNP  O60260    GLY    94 DELETION                       
SEQADV 6HUE     A       UNP  O60260    CYS    95 DELETION                       
SEQADV 6HUE     A       UNP  O60260    GLU    96 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ARG    97 DELETION                       
SEQADV 6HUE     A       UNP  O60260    GLU    98 DELETION                       
SEQADV 6HUE     A       UNP  O60260    PRO    99 DELETION                       
SEQADV 6HUE     A       UNP  O60260    GLN   100 DELETION                       
SEQADV 6HUE     A       UNP  O60260    SER   101 DELETION                       
SEQADV 6HUE     A       UNP  O60260    LEU   102 DELETION                       
SEQADV 6HUE     A       UNP  O60260    THR   103 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ARG   104 DELETION                       
SEQADV 6HUE     A       UNP  O60260    VAL   105 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ASP   106 DELETION                       
SEQADV 6HUE     A       UNP  O60260    LEU   107 DELETION                       
SEQADV 6HUE     A       UNP  O60260    SER   108 DELETION                       
SEQADV 6HUE     A       UNP  O60260    SER   109 DELETION                       
SEQADV 6HUE     A       UNP  O60260    SER   110 DELETION                       
SEQADV 6HUE     A       UNP  O60260    VAL   111 DELETION                       
SEQADV 6HUE     A       UNP  O60260    LEU   112 DELETION                       
SEQADV 6HUE     A       UNP  O60260    PRO   113 DELETION                       
SEQADV 6HUE     A       UNP  O60260    GLY   114 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ASP   115 DELETION                       
SEQADV 6HUE     A       UNP  O60260    SER   116 DELETION                       
SEQADV 6HUE     A       UNP  O60260    VAL   117 DELETION                       
SEQADV 6HUE     A       UNP  O60260    GLY   118 DELETION                       
SEQADV 6HUE     A       UNP  O60260    LEU   119 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ALA   120 DELETION                       
SEQADV 6HUE     A       UNP  O60260    VAL   121 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ILE   122 DELETION                       
SEQADV 6HUE     A       UNP  O60260    LEU   123 DELETION                       
SEQADV 6HUE     A       UNP  O60260    HIS   124 DELETION                       
SEQADV 6HUE     A       UNP  O60260    THR   125 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ASP   126 DELETION                       
SEQADV 6HUE     A       UNP  O60260    SER   127 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ARG   128 DELETION                       
SEQADV 6HUE     A       UNP  O60260    LYS   129 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ASP   130 DELETION                       
SEQADV 6HUE     A       UNP  O60260    SER   131 DELETION                       
SEQADV 6HUE     A       UNP  O60260    PRO   132 DELETION                       
SEQADV 6HUE     A       UNP  O60260    PRO   133 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ALA   134 DELETION                       
SEQADV 6HUE     A       UNP  O60260    GLY   135 DELETION                       
SEQADV 6HUE     A       UNP  O60260    SER   136 DELETION                       
SEQADV 6HUE     A       UNP  O60260    PRO   137 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ALA   138 DELETION                       
SEQADV 6HUE     A       UNP  O60260    GLY   139 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ARG   140 DELETION                       
SEQADV 6HUE     A       UNP  O60260    SER   141 DELETION                       
SEQADV 6HUE     A       UNP  O60260    ILE   142 DELETION                       
SEQADV 6HUE     A       UNP  O60260    TYR   143 DELETION                       
SEQADV 6HUE ASN B   65  UNP  O60260    SER    65 ENGINEERED MUTATION            
SEQADV 6HUE     B       UNP  O60260    GLY    84 DELETION                       
SEQADV 6HUE     B       UNP  O60260    GLY    85 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ASP    86 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ASP    87 DELETION                       
SEQADV 6HUE     B       UNP  O60260    PRO    88 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ARG    89 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ASN    90 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ALA    91 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ALA    92 DELETION                       
SEQADV 6HUE     B       UNP  O60260    GLY    93 DELETION                       
SEQADV 6HUE     B       UNP  O60260    GLY    94 DELETION                       
SEQADV 6HUE     B       UNP  O60260    CYS    95 DELETION                       
SEQADV 6HUE     B       UNP  O60260    GLU    96 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ARG    97 DELETION                       
SEQADV 6HUE     B       UNP  O60260    GLU    98 DELETION                       
SEQADV 6HUE     B       UNP  O60260    PRO    99 DELETION                       
SEQADV 6HUE     B       UNP  O60260    GLN   100 DELETION                       
SEQADV 6HUE     B       UNP  O60260    SER   101 DELETION                       
SEQADV 6HUE     B       UNP  O60260    LEU   102 DELETION                       
SEQADV 6HUE     B       UNP  O60260    THR   103 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ARG   104 DELETION                       
SEQADV 6HUE     B       UNP  O60260    VAL   105 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ASP   106 DELETION                       
SEQADV 6HUE     B       UNP  O60260    LEU   107 DELETION                       
SEQADV 6HUE     B       UNP  O60260    SER   108 DELETION                       
SEQADV 6HUE     B       UNP  O60260    SER   109 DELETION                       
SEQADV 6HUE     B       UNP  O60260    SER   110 DELETION                       
SEQADV 6HUE     B       UNP  O60260    VAL   111 DELETION                       
SEQADV 6HUE     B       UNP  O60260    LEU   112 DELETION                       
SEQADV 6HUE     B       UNP  O60260    PRO   113 DELETION                       
SEQADV 6HUE     B       UNP  O60260    GLY   114 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ASP   115 DELETION                       
SEQADV 6HUE     B       UNP  O60260    SER   116 DELETION                       
SEQADV 6HUE     B       UNP  O60260    VAL   117 DELETION                       
SEQADV 6HUE     B       UNP  O60260    GLY   118 DELETION                       
SEQADV 6HUE     B       UNP  O60260    LEU   119 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ALA   120 DELETION                       
SEQADV 6HUE     B       UNP  O60260    VAL   121 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ILE   122 DELETION                       
SEQADV 6HUE     B       UNP  O60260    LEU   123 DELETION                       
SEQADV 6HUE     B       UNP  O60260    HIS   124 DELETION                       
SEQADV 6HUE     B       UNP  O60260    THR   125 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ASP   126 DELETION                       
SEQADV 6HUE     B       UNP  O60260    SER   127 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ARG   128 DELETION                       
SEQADV 6HUE     B       UNP  O60260    LYS   129 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ASP   130 DELETION                       
SEQADV 6HUE     B       UNP  O60260    SER   131 DELETION                       
SEQADV 6HUE     B       UNP  O60260    PRO   132 DELETION                       
SEQADV 6HUE     B       UNP  O60260    PRO   133 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ALA   134 DELETION                       
SEQADV 6HUE     B       UNP  O60260    GLY   135 DELETION                       
SEQADV 6HUE     B       UNP  O60260    SER   136 DELETION                       
SEQADV 6HUE     B       UNP  O60260    PRO   137 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ALA   138 DELETION                       
SEQADV 6HUE     B       UNP  O60260    GLY   139 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ARG   140 DELETION                       
SEQADV 6HUE     B       UNP  O60260    SER   141 DELETION                       
SEQADV 6HUE     B       UNP  O60260    ILE   142 DELETION                       
SEQADV 6HUE     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 ASN          
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 ASN          
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   *157(H2 O)                                                    
HELIX    1 AA1 SER A   22  GLY A   35  1                                  14    
HELIX    2 AA2 PRO A   37  ASP A   39  5                                   3    
HELIX    3 AA3 CYS A  182  ILE A  188  1                                   7    
HELIX    4 AA4 LEU A  261  ARG A  275  1                                  15    
HELIX    5 AA5 GLU A  300  ILE A  306  5                                   7    
HELIX    6 AA6 LEU A  307  GLN A  317  1                                  11    
HELIX    7 AA7 GLN A  317  GLY A  328  1                                  12    
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  GLN B  317  1                                  10    
HELIX   16 AB7 GLN B  317  MET B  327  1                                  11    
HELIX   17 AB8 ASP B  394  ALA B  401  1                                   8    
HELIX   18 AB9 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  PHE A   7 -1  N  VAL A   5   O  PHE A  13           
SHEET    3 AA1 5 ILE A  66  GLN A  71  1  O  ILE A  69   N  ARG A   6           
SHEET    4 AA1 5 LEU A  41  PHE A  45 -1  N  ILE A  44   O  HIS A  68           
SHEET    5 AA1 5 LYS A  48  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  GLN A 165   O  GLU A 207           
SHEET    3 AA2 4 TYR A 147  CYS A 150 -1  N  VAL A 148   O  GLN A 158           
SHEET    4 AA2 4 VAL A 224  ALA A 225 -1  O  VAL A 224   N  TYR A 149           
SHEET    1 AA3 2 LEU A 174  LEU A 176  0                                        
SHEET    2 AA3 2 GLY A 194  CYS A 196 -1  O  GLU A 195   N  THR A 175           
SHEET    1 AA4 3 ILE A 229  ALA A 230  0                                        
SHEET    2 AA4 3 VAL A 248  VAL A 250 -1  O  VAL A 248   N  ALA A 230           
SHEET    3 AA4 3 VAL A 258  CYS A 260 -1  O  ILE A 259   N  LEU A 249           
SHEET    1 AA5 2 VAL A 278  ASP A 280  0                                        
SHEET    2 AA5 2 GLY A 284  SER A 286 -1  O  GLY A 284   N  ASP A 280           
SHEET    1 AA6 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  ILE B  69   N  ARG B   6           
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  LYS B 161   O  LYS B 211           
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  VAL B 350  0                                        
SHEET    2 AB7 2 PHE B 364  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  2.31  
LINK         SG  CYS A 154                ZN    ZN A 501     1555   1555  2.29  
LINK         SG  CYS A 166                ZN    ZN A 502     1555   1555  2.33  
LINK         SG  CYS A 169                ZN    ZN A 502     1555   1555  2.33  
LINK         SG  CYS A 196                ZN    ZN A 502     1555   1555  2.32  
LINK         SG  CYS A 201                ZN    ZN A 502     1555   1555  2.37  
LINK         SG  CYS A 212                ZN    ZN A 501     1555   1555  2.32  
LINK         NE2 HIS A 215                ZN    ZN A 501     1555   1555  1.87  
LINK         SG  CYS A 238                ZN    ZN A 503     1555   1555  2.34  
LINK         SG  CYS A 241                ZN    ZN A 503     1555   1555  2.29  
LINK         SG  CYS A 253                ZN    ZN A 504     1555   1555  2.35  
LINK         ND1 HIS A 257                ZN    ZN A 504     1555   1555  1.93  
LINK         SG  CYS A 260                ZN    ZN A 503     1555   1555  2.32  
LINK         SG  CYS A 263                ZN    ZN A 503     1555   1555  2.33  
LINK         SG  CYS A 289                ZN    ZN A 504     1555   1555  2.31  
LINK         SG  CYS A 293                ZN    ZN A 504     1555   1555  2.32  
LINK         SG  CYS A 332                ZN    ZN A 505     1555   1555  2.37  
LINK         SG  CYS A 337                ZN    ZN A 505     1555   1555  2.59  
LINK         SG  CYS A 352                ZN    ZN A 505     1555   1555  2.38  
LINK         N   GLY A 361                ZN    ZN A 505     1555   1555  2.65  
LINK         SG  CYS A 365                ZN    ZN A 506     1555   1555  2.33  
LINK         SG  CYS A 368                ZN    ZN A 506     1555   1555  2.36  
LINK         NE2 HIS A 373                ZN    ZN A 506     1555   1555  1.96  
LINK         SG  CYS A 377                ZN    ZN A 506     1555   1555  2.36  
LINK         SG  CYS A 418                ZN    ZN A 507     1555   1555  2.32  
LINK         SG  CYS A 421                ZN    ZN A 507     1555   1555  2.32  
LINK         SG  CYS A 436                ZN    ZN A 507     1555   1555  2.30  
LINK         SG  CYS A 441                ZN    ZN A 507     1555   1555  2.34  
LINK         SG  CYS A 446                ZN    ZN A 508     1555   1555  2.29  
LINK         SG  CYS A 449                ZN    ZN A 508     1555   1555  2.33  
LINK         SG  CYS A 457                ZN    ZN A 508     1555   1555  2.29  
LINK         NE2 HIS A 461                ZN    ZN A 508     1555   1555  1.91  
LINK         SG  CYS B 150                ZN    ZN B 501     1555   1555  2.28  
LINK         SG  CYS B 154                ZN    ZN B 501     1555   1555  2.32  
LINK         SG  CYS B 166                ZN    ZN B 502     1555   1555  2.31  
LINK         SG  CYS B 169                ZN    ZN B 502     1555   1555  2.34  
LINK         SG  CYS B 196                ZN    ZN B 502     1555   1555  2.31  
LINK         SG  CYS B 201                ZN    ZN B 502     1555   1555  2.32  
LINK         SG  CYS B 212                ZN    ZN B 501     1555   1555  2.33  
LINK         NE2 HIS B 215                ZN    ZN B 501     1555   1555  1.89  
LINK         SG  CYS B 238                ZN    ZN B 503     1555   1555  2.37  
LINK         SG  CYS B 241                ZN    ZN B 503     1555   1555  2.30  
LINK         SG  CYS B 253                ZN    ZN B 504     1555   1555  2.36  
LINK         ND1 HIS B 257                ZN    ZN B 504     1555   1555  1.93  
LINK         SG  CYS B 260                ZN    ZN B 503     1555   1555  2.32  
LINK         SG  CYS B 263                ZN    ZN B 503     1555   1555  2.29  
LINK         SG  CYS B 289                ZN    ZN B 504     1555   1555  2.35  
LINK         SG  CYS B 293                ZN    ZN B 504     1555   1555  2.32  
LINK         SG  CYS B 332                ZN    ZN B 505     1555   1555  2.34  
LINK         SG  CYS B 337                ZN    ZN B 505     1555   1555  2.34  
LINK         SG  CYS B 352                ZN    ZN B 505     1555   1555  2.37  
LINK         N   GLY B 361                ZN    ZN B 505     1555   1555  2.64  
LINK         SG  CYS B 365                ZN    ZN B 506     1555   1555  2.32  
LINK         SG  CYS B 368                ZN    ZN B 506     1555   1555  2.34  
LINK         NE2 HIS B 373                ZN    ZN B 506     1555   1555  1.93  
LINK         SG  CYS B 377                ZN    ZN B 506     1555   1555  2.34  
LINK         SG  CYS B 418                ZN    ZN B 507     1555   1555  2.31  
LINK         SG  CYS B 421                ZN    ZN B 507     1555   1555  2.33  
LINK         SG  CYS B 436                ZN    ZN B 507     1555   1555  2.32  
LINK         SG  CYS B 441                ZN    ZN B 507     1555   1555  2.33  
LINK         SG  CYS B 446                ZN    ZN B 508     1555   1555  2.29  
LINK         SG  CYS B 449                ZN    ZN B 508     1555   1555  2.34  
LINK         SG  CYS B 457                ZN    ZN B 508     1555   1555  2.30  
LINK         NE2 HIS B 461                ZN    ZN B 508     1555   1555  1.94  
LINK        ZN    ZN B 505                 O   HOH B 602     1555   1555  2.59  
CISPEP   1 GLY A  152    PRO A  153          0       -11.77                     
CISPEP   2 SER A  246    PRO A  247          0         0.85                     
CISPEP   3 GLY B  152    PRO B  153          0        -5.97                     
CISPEP   4 SER B  246    PRO B  247          0         5.71                     
CISPEP   5 GLY B  336    CYS B  337          0         6.20                     
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  5 ARG A 348  CYS A 365  CYS A 368  HIS A 373                    
SITE     2 AC6  5 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  8 GLN A  57  ASN A  58  LYS A 161  ARG A 163                    
SITE     2 AC9  8 LYS A 211  THR A 217  ARG A 455  HOH A 605                    
SITE     1 AD1  6 VAL A 186  LEU A 187  ILE A 188  PRO A 189                    
SITE     2 AD1  6 GLU A 207  PHE A 208                                          
SITE     1 AD2  6 HIS A 227  VAL A 250  GLN A 252  ARG A 256                    
SITE     2 AD2  6 VAL A 465  HOH A 603                                          
SITE     1 AD3  5 PHE A 146  TYR A 147  TRP A 183  LEU A 226                    
SITE     2 AD3  5 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  5 CYS B 238  THR B 240  CYS B 241  CYS B 260                    
SITE     2 AD6  5 CYS B 263                                                     
SITE     1 AD7  4 CYS B 253  HIS B 257  CYS B 289  CYS B 293                    
SITE     1 AD8  5 CYS B 332  CYS B 337  CYS B 352  GLY B 361                    
SITE     2 AD8  5 HOH B 602                                                     
SITE     1 AD9  5 ARG B 348  CYS B 365  CYS B 368  HIS B 373                    
SITE     2 AD9  5 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  7 ASN B  58  LYS B 161  ARG B 163  LYS B 211                    
SITE     2 AE3  7 THR B 217  ARG B 455  HOH B 603                               
SITE     1 AE4  6 TRP B 183  HIS B 227  LEU B 228  VAL B 250                    
SITE     2 AE4  6 GLN B 252  TRP B 403                                          
SITE     1 AE5  4 VAL B 186  LEU B 187  PRO B 189  PHE B 208                    
SITE     1 AE6  5 PHE B 146  TYR B 147  TRP B 183  LEU B 226                    
SITE     2 AE6  5 ILE B 229                                                     
CRYST1   66.431   66.870  206.690  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      0.015053  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014954  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004838        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system