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Database: PDB
Entry: 4I1F
LinkDB: 4I1F
Original site: 4I1F 
HEADER    LIGASE                                  20-NOV-12   4I1F              
TITLE     STRUCTURE OF PARKIN-S223P E3 LIGASE                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE PARKIN;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: R0RBR (UNP RESIDUES 141-465);                              
COMPND   5 SYNONYM: PARKINSON JUVENILE DISEASE PROTEIN 2, PARKINSON DISEASE     
COMPND   6 PROTEIN 2;                                                           
COMPND   7 EC: 6.3.2.-;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: 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;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    RBR E3 UBIQUITIN LIGASE, LIGASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.C.LOUGHEED,E.BRECHT,N.H.YAO                                         
REVDAT   2   03-JUL-13 4I1F    1       JRNL                                     
REVDAT   1   19-JUN-13 4I1F    0                                                
JRNL        AUTH   B.E.RILEY,J.C.LOUGHEED,K.CALLAWAY,M.VELASQUEZ,E.BRECHT,      
JRNL        AUTH 2 L.NGUYEN,T.SHALER,D.WALKER,Y.YANG,K.REGNSTROM,L.DIEP,        
JRNL        AUTH 3 Z.ZHANG,S.CHIOU,M.BOVA,D.R.ARTIS,N.YAO,J.BAKER,T.YEDNOCK,    
JRNL        AUTH 4 J.A.JOHNSTON                                                 
JRNL        TITL   STRUCTURE AND FUNCTION OF PARKIN E3 UBIQUITIN LIGASE REVEALS 
JRNL        TITL 2 ASPECTS OF RING AND HECT LIGASES.                            
JRNL        REF    NAT COMMUN                    V.   4  1982 2013              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   23770887                                                     
JRNL        DOI    10.1038/NCOMMS2982                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.58 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 72.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 52033                          
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2650                            
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) : 1.58                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.62                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3351                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.31                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 194                          
REMARK   3   BIN FREE R VALUE                    : 0.4780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2400                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 267                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.46000                                             
REMARK   3    B22 (A**2) : 0.12000                                              
REMARK   3    B33 (A**2) : 0.33000                                              
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): 0.087         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.092         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.058         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.607         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2466 ; 0.025 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3342 ; 2.260 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   304 ; 6.550 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   117 ;35.095 ;23.248       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   399 ;13.404 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;16.550 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   349 ; 0.162 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1921 ; 0.015 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : MASK                                                 
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:                                           
REMARK   3  HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT                    
REMARK   3  U VALUES      : REFINED INDIVIDUALLY                                
REMARK   4                                                                      
REMARK   4 4I1F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB076182.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2831, 1.2699                     
REMARK 200  MONOCHROMATOR                  : KHOZU DOUBLE FLAT CRYSTAL SI(111)  
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52033                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.580                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.99000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.99000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 20% PEG4000, 10%    
REMARK 280  ISOPROPANOL, 10 MM BARIUM CHLORIDE, VAPOR DIFFUSION, SITTING        
REMARK 280  DROP, TEMPERATURE 283K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       32.69250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       32.69250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       43.47750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.57750            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.47750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.57750            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       32.69250            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.47750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.57750            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       32.69250            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.47750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.57750            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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     SER A   218                                                      
REMARK 465     ASP A   219                                                      
REMARK 465     LYS A   220                                                      
REMARK 465     GLU A   221                                                      
REMARK 465     GLY A   355                                                      
REMARK 465     ASN A   356                                                      
REMARK 465     GLY A   357                                                      
REMARK 465     LEU A   358                                                      
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   609     O    HOH A   730              1.15            
REMARK 500   O    HOH A   632     O    HOH A   732              1.24            
REMARK 500   O    HOH A   654     O    HOH A   736              1.24            
REMARK 500   O    HOH A   850     O    HOH A   855              1.55            
REMARK 500   O    CYS A   201    BA     BA A   509              1.61            
REMARK 500   O    HOH A   672     O    HOH A   836              1.62            
REMARK 500   O    HOH A   628     O    HOH A   731              1.74            
REMARK 500   O    HOH A   706     O    HOH A   809              1.81            
REMARK 500   O    HOH A   652     O    HOH A   716              1.89            
REMARK 500   O    HOH A   745     O    HOH A   847              1.96            
REMARK 500   O    HOH A   649     O    HOH A   733              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER A 145   CA    SER A 145   CB      0.093                       
REMARK 500    SER A 145   CB    SER A 145   OG     -0.087                       
REMARK 500    CYS A 201   C     CYS A 201   O       0.202                       
REMARK 500    HIS A 302   CG    HIS A 302   CD2     0.054                       
REMARK 500    HIS A 303   CG    HIS A 303   CD2     0.069                       
REMARK 500    HIS A 373   CG    HIS A 373   CD2     0.055                       
REMARK 500    TRP A 453   CD1   TRP A 453   NE1     0.155                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 163   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 191   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    CYS A 196   CA  -  CB  -  SG  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    PRO A 202   C   -  N   -  CA  ANGL. DEV. =  16.2 DEGREES          
REMARK 500    PRO A 202   C   -  N   -  CD  ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ARG A 234   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 420   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 151     -104.79    -63.20                                   
REMARK 500    GLN A 155       51.18     37.14                                   
REMARK 500    THR A 168      -66.92    -91.15                                   
REMARK 500    THR A 242       13.70     55.33                                   
REMARK 500    GLN A 252       30.43    -92.69                                   
REMARK 500    LEU A 283      -48.09   -135.49                                   
REMARK 500    CYS A 337      -84.81   -112.74                                   
REMARK 500    CYS A 441      -69.47   -105.26                                   
REMARK 500    HIS A 461       50.74   -161.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    CYS A 201        23.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 508  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 461   NE2                                                    
REMARK 620 2 CYS A 446   SG  102.2                                              
REMARK 620 3 CYS A 457   SG  108.3 113.4                                        
REMARK 620 4 CYS A 449   SG  105.3 115.4 111.3                                  
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 HIS A 257   ND1                                                    
REMARK 620 2 CYS A 289   SG  105.6                                              
REMARK 620 3 CYS A 253   SG  107.5 114.0                                        
REMARK 620 4 CYS A 293   SG  101.4 115.8 111.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 CYS A 212   SG  108.8                                              
REMARK 620 3 CYS A 150   SG  110.2 108.3                                        
REMARK 620 4 CYS A 154   SG  100.7 117.5 110.9                                  
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 360   SG  106.2                                              
REMARK 620 3 CYS A 337   SG  112.3 114.5                                        
REMARK 620 4 CYS A 352   SG  110.4 108.2 105.3                                  
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 HIS A 373   NE2                                                    
REMARK 620 2 CYS A 377   SG  106.3                                              
REMARK 620 3 CYS A 368   SG  109.3 115.5                                        
REMARK 620 4 CYS A 365   SG  107.8 111.1 106.7                                  
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 441   SG                                                     
REMARK 620 2 CYS A 418   SG  111.3                                              
REMARK 620 3 CYS A 421   SG  114.1 110.1                                        
REMARK 620 4 CYS A 436   SG  112.8 103.9 104.0                                  
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 263   SG  108.4                                              
REMARK 620 3 CYS A 260   SG  114.9 101.7                                        
REMARK 620 4 CYS A 241   SG  106.8 109.0 115.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 166   SG                                                     
REMARK 620 2 CYS A 169   SG  105.8                                              
REMARK 620 3 CYS A 201   SG  111.7 112.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA A 509  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 196   O                                                      
REMARK 620 2 SER A 198   O    77.0                                              
REMARK 620 3 HOH A 816   O    73.9 145.4                                        
REMARK 620 N                    1     2                                         
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 BA A 509                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4I1H   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF PARKIN E3 LIGASE                                        
DBREF  4I1F A  141   465  UNP    O60260   PRKN2_HUMAN    141    465             
SEQADV 4I1F PRO A  223  UNP  O60260    SER   223 ENGINEERED MUTATION            
SEQRES   1 A  325  SER ILE TYR ASN SER PHE TYR VAL TYR CYS LYS GLY PRO          
SEQRES   2 A  325  CYS GLN ARG VAL GLN PRO GLY LYS LEU ARG VAL GLN CYS          
SEQRES   3 A  325  SER THR CYS ARG GLN ALA THR LEU THR LEU THR GLN GLY          
SEQRES   4 A  325  PRO SER CYS TRP ASP ASP VAL LEU ILE PRO ASN ARG MET          
SEQRES   5 A  325  SER GLY GLU CYS GLN SER PRO HIS CYS PRO GLY THR SER          
SEQRES   6 A  325  ALA GLU PHE PHE PHE LYS CYS GLY ALA HIS PRO THR SER          
SEQRES   7 A  325  ASP LYS GLU THR PRO VAL ALA LEU HIS LEU ILE ALA THR          
SEQRES   8 A  325  ASN SER ARG ASN ILE THR CYS ILE THR CYS THR ASP VAL          
SEQRES   9 A  325  ARG SER PRO VAL LEU VAL PHE GLN CYS ASN SER ARG HIS          
SEQRES  10 A  325  VAL ILE CYS LEU ASP CYS PHE HIS LEU TYR CYS VAL THR          
SEQRES  11 A  325  ARG LEU ASN ASP ARG GLN PHE VAL HIS ASP PRO GLN LEU          
SEQRES  12 A  325  GLY TYR SER LEU PRO CYS VAL ALA GLY CYS PRO ASN SER          
SEQRES  13 A  325  LEU ILE LYS GLU LEU HIS HIS PHE ARG ILE LEU GLY GLU          
SEQRES  14 A  325  GLU GLN TYR ASN ARG TYR GLN GLN TYR GLY ALA GLU GLU          
SEQRES  15 A  325  CYS VAL LEU GLN MET GLY GLY VAL LEU CYS PRO ARG PRO          
SEQRES  16 A  325  GLY CYS GLY ALA GLY LEU LEU PRO GLU PRO ASP GLN ARG          
SEQRES  17 A  325  LYS VAL THR CYS GLU GLY GLY ASN GLY LEU GLY CYS GLY          
SEQRES  18 A  325  PHE ALA PHE CYS ARG GLU CYS LYS GLU ALA TYR HIS GLU          
SEQRES  19 A  325  GLY GLU CYS SER ALA VAL PHE GLU ALA SER GLY THR THR          
SEQRES  20 A  325  THR GLN ALA TYR ARG VAL ASP GLU ARG ALA ALA GLU GLN          
SEQRES  21 A  325  ALA ARG TRP GLU ALA ALA SER LYS GLU THR ILE LYS LYS          
SEQRES  22 A  325  THR THR LYS PRO CYS PRO ARG CYS HIS VAL PRO VAL GLU          
SEQRES  23 A  325  LYS ASN GLY GLY CYS MET HIS MET LYS CYS PRO GLN PRO          
SEQRES  24 A  325  GLN CYS ARG LEU GLU TRP CYS TRP ASN CYS GLY CYS GLU          
SEQRES  25 A  325  TRP ASN ARG VAL CYS MET GLY ASP HIS TRP PHE 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     BA  A 509       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      BA BARIUM ION                                                       
FORMUL   2   ZN    8(ZN 2+)                                                     
FORMUL  10   BA    BA 2+                                                        
FORMUL  11  HOH   *267(H2 O)                                                    
HELIX    1   1 CYS A  182  ILE A  188  1                                   7    
HELIX    2   2 LEU A  261  ASP A  274  1                                  14    
HELIX    3   3 GLU A  300  LEU A  307  5                                   8    
HELIX    4   4 GLY A  308  MET A  327  1                                  20    
HELIX    5   5 ASP A  394  ALA A  401  1                                   8    
HELIX    6   6 ASN A  454  TRP A  462  1                                   9    
SHEET    1   A 4 ALA A 206  CYS A 212  0                                        
SHEET    2   A 4 ARG A 156  CYS A 166 -1  N  ARG A 163   O  PHE A 209           
SHEET    3   A 4 TYR A 147  CYS A 150 -1  N  CYS A 150   O  ARG A 156           
SHEET    4   A 4 VAL A 224  ALA A 225 -1  O  VAL A 224   N  TYR A 149           
SHEET    1   B 2 LEU A 174  LEU A 176  0                                        
SHEET    2   B 2 GLY A 194  CYS A 196 -1  O  GLU A 195   N  THR A 175           
SHEET    1   C 3 ILE A 229  ALA A 230  0                                        
SHEET    2   C 3 VAL A 248  VAL A 250 -1  O  VAL A 248   N  ALA A 230           
SHEET    3   C 3 VAL A 258  CYS A 260 -1  O  ILE A 259   N  LEU A 249           
SHEET    1   D 2 VAL A 278  ASP A 280  0                                        
SHEET    2   D 2 GLY A 284  SER A 286 -1  O  GLY A 284   N  ASP A 280           
SHEET    1   E 2 VAL A 330  LEU A 331  0                                        
SHEET    2   E 2 GLY A 340  LEU A 341 -1  O  LEU A 341   N  VAL A 330           
SHEET    1   F 2 LYS A 349  THR A 351  0                                        
SHEET    2   F 2 ALA A 363  CYS A 365 -1  O  PHE A 364   N  VAL A 350           
SHEET    1   G 2 THR A 415  PRO A 417  0                                        
SHEET    2   G 2 PRO A 424  GLU A 426 -1  O  VAL A 425   N  LYS A 416           
SHEET    1   H 2 HIS A 433  LYS A 435  0                                        
SHEET    2   H 2 GLU A 444  CYS A 446 -1  O  TRP A 445   N  MET A 434           
SSBOND   1 CYS A  323    CYS A  323                          1555   4555  2.93  
LINK         NE2 HIS A 461                ZN    ZN A 508     1555   1555  1.99  
LINK         ND1 HIS A 257                ZN    ZN A 504     1555   1555  2.00  
LINK         NE2 HIS A 215                ZN    ZN A 501     1555   1555  2.12  
LINK         SG  CYS A 332                ZN    ZN A 505     1555   1555  2.14  
LINK         NE2 HIS A 373                ZN    ZN A 506     1555   1555  2.17  
LINK         SG  CYS A 212                ZN    ZN A 501     1555   1555  2.21  
LINK         SG  CYS A 150                ZN    ZN A 501     1555   1555  2.23  
LINK         SG  CYS A 377                ZN    ZN A 506     1555   1555  2.25  
LINK         SG  CYS A 446                ZN    ZN A 508     1555   1555  2.26  
LINK         SG  CYS A 441                ZN    ZN A 507     1555   1555  2.28  
LINK         SG  CYS A 360                ZN    ZN A 505     1555   1555  2.29  
LINK         SG  CYS A 457                ZN    ZN A 508     1555   1555  2.29  
LINK         SG  CYS A 368                ZN    ZN A 506     1555   1555  2.30  
LINK         SG  CYS A 337                ZN    ZN A 505     1555   1555  2.30  
LINK         SG  CYS A 289                ZN    ZN A 504     1555   1555  2.30  
LINK         SG  CYS A 238                ZN    ZN A 503     1555   1555  2.31  
LINK         SG  CYS A 166                ZN    ZN A 502     1555   1555  2.31  
LINK         SG  CYS A 253                ZN    ZN A 504     1555   1555  2.32  
LINK         SG  CYS A 293                ZN    ZN A 504     1555   1555  2.33  
LINK         SG  CYS A 263                ZN    ZN A 503     1555   1555  2.34  
LINK         SG  CYS A 352                ZN    ZN A 505     1555   1555  2.35  
LINK         SG  CYS A 418                ZN    ZN A 507     1555   1555  2.35  
LINK         SG  CYS A 449                ZN    ZN A 508     1555   1555  2.35  
LINK         SG  CYS A 260                ZN    ZN A 503     1555   1555  2.35  
LINK         SG  CYS A 241                ZN    ZN A 503     1555   1555  2.36  
LINK         SG  CYS A 365                ZN    ZN A 506     1555   1555  2.37  
LINK         SG  CYS A 169                ZN    ZN A 502     1555   1555  2.38  
LINK         SG  CYS A 154                ZN    ZN A 501     1555   1555  2.38  
LINK         SG  CYS A 201                ZN    ZN A 502     1555   1555  2.38  
LINK         SG  CYS A 421                ZN    ZN A 507     1555   1555  2.40  
LINK         SG  CYS A 436                ZN    ZN A 507     1555   1555  2.50  
LINK         O   CYS A 196                BA    BA A 509     1555   1555  2.67  
LINK         O   SER A 198                BA    BA A 509     1555   1555  2.68  
LINK        BA    BA A 509                 O   HOH A 816     1555   1555  2.84  
CISPEP   1 GLY A  152    PRO A  153          0         4.23                     
CISPEP   2 SER A  246    PRO A  247          0        -8.44                     
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  CYS A 360                    
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  4 CYS A 196  SER A 198  CYS A 201  HOH A 816                    
CRYST1   86.955  133.155   65.385  90.00  90.00  90.00 C 2 2 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      0.011500  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007510  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015294        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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