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Database: PDB
Entry: 1PDW
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HEADER    PROTEIN BINDING                         20-MAY-03   1PDW              
TITLE     CRYSTAL STRUCTURE OF HUMAN DJ-1, P 1 21 1 SPACE GROUP                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DJ-1;                                                      
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DJ-1, PROTEIN BINDING                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.TAO,L.TONG                                                          
REVDAT   3   24-FEB-09 1PDW    1       VERSN                                    
REVDAT   2   19-AUG-03 1PDW    1       JRNL                                     
REVDAT   1   24-JUN-03 1PDW    0                                                
JRNL        AUTH   X.TAO,L.TONG                                                 
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN DJ-1, A PROTEIN                   
JRNL        TITL 2 ASSOCIATED WITH EARLY ONSET PARKINSON'S DISEASE.             
JRNL        REF    J.BIOL.CHEM.                  V. 278 31372 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12761214                                                     
JRNL        DOI    10.1074/JBC.M304221200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.91                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 61031                          
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 SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4695                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.28                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5067                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1930                       
REMARK   3   BIN FREE R VALUE                    : 0.2750                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 438                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11051                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 970                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 7.10                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.24000                                              
REMARK   3    B22 (A**2) : 0.92000                                              
REMARK   3    B33 (A**2) : -5.17000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.29000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.31                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.24                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.86                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.310 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.050 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.810 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 47.19                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1PDW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019260.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-APR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9724                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67190                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : 0.09400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23100                            
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: COMO                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG3350, 100 MM TRIS, PH 8.0,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       41.83200            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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     MET A     1                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     LEU A   190                                                      
REMARK 465     GLU A   191                                                      
REMARK 465     HIS A   192                                                      
REMARK 465     HIS A   193                                                      
REMARK 465     HIS A   194                                                      
REMARK 465     HIS A   195                                                      
REMARK 465     HIS A   196                                                      
REMARK 465     HIS A   197                                                      
REMARK 465     MET B   201                                                      
REMARK 465     ASP B   389                                                      
REMARK 465     LEU B   390                                                      
REMARK 465     GLU B   391                                                      
REMARK 465     HIS B   392                                                      
REMARK 465     HIS B   393                                                      
REMARK 465     HIS B   394                                                      
REMARK 465     HIS B   395                                                      
REMARK 465     HIS B   396                                                      
REMARK 465     HIS B   397                                                      
REMARK 465     MET C  1001                                                      
REMARK 465     ASP C  1189                                                      
REMARK 465     LEU C  1190                                                      
REMARK 465     GLU C  1191                                                      
REMARK 465     HIS C  1192                                                      
REMARK 465     HIS C  1193                                                      
REMARK 465     HIS C  1194                                                      
REMARK 465     HIS C  1195                                                      
REMARK 465     HIS C  1196                                                      
REMARK 465     HIS C  1197                                                      
REMARK 465     MET D  1201                                                      
REMARK 465     ASP D  1389                                                      
REMARK 465     LEU D  1390                                                      
REMARK 465     GLU D  1391                                                      
REMARK 465     HIS D  1392                                                      
REMARK 465     HIS D  1393                                                      
REMARK 465     HIS D  1394                                                      
REMARK 465     HIS D  1395                                                      
REMARK 465     HIS D  1396                                                      
REMARK 465     HIS D  1397                                                      
REMARK 465     MET E  2001                                                      
REMARK 465     GLU E  2191                                                      
REMARK 465     HIS E  2192                                                      
REMARK 465     HIS E  2193                                                      
REMARK 465     HIS E  2194                                                      
REMARK 465     HIS E  2195                                                      
REMARK 465     HIS E  2196                                                      
REMARK 465     HIS E  2197                                                      
REMARK 465     MET F  2201                                                      
REMARK 465     ASP F  2389                                                      
REMARK 465     LEU F  2390                                                      
REMARK 465     GLU F  2391                                                      
REMARK 465     HIS F  2392                                                      
REMARK 465     HIS F  2393                                                      
REMARK 465     HIS F  2394                                                      
REMARK 465     HIS F  2395                                                      
REMARK 465     HIS F  2396                                                      
REMARK 465     HIS F  2397                                                      
REMARK 465     MET G  3001                                                      
REMARK 465     HIS G  3193                                                      
REMARK 465     HIS G  3194                                                      
REMARK 465     HIS G  3195                                                      
REMARK 465     HIS G  3196                                                      
REMARK 465     HIS G  3197                                                      
REMARK 465     MET H  3201                                                      
REMARK 465     ASP H  3389                                                      
REMARK 465     LEU H  3390                                                      
REMARK 465     GLU H  3391                                                      
REMARK 465     HIS H  3392                                                      
REMARK 465     HIS H  3393                                                      
REMARK 465     HIS H  3394                                                      
REMARK 465     HIS H  3395                                                      
REMARK 465     HIS H  3396                                                      
REMARK 465     HIS H  3397                                                      
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    ASP A  49       11.53     54.67                                   
REMARK 500    GLU A  64       53.28   -103.58                                   
REMARK 500    CYS A 106     -104.06     65.50                                   
REMARK 500    PRO A 127      -39.76    -33.02                                   
REMARK 500    LEU A 128       31.04    -81.94                                   
REMARK 500    ALA A 129       13.74   -151.94                                   
REMARK 500    GLU B 264       72.52    -67.71                                   
REMARK 500    CYS B 306     -108.41     63.10                                   
REMARK 500    ALA C1039       39.96    -98.86                                   
REMARK 500    CYS C1106     -104.79     64.05                                   
REMARK 500    SER D1203     -150.08    164.60                                   
REMARK 500    LYS D1263        2.98    -67.85                                   
REMARK 500    CYS D1306     -109.07     60.15                                   
REMARK 500    GLU E2064       72.50    -60.08                                   
REMARK 500    ASN E2076      -71.88    -47.14                                   
REMARK 500    CYS E2106      -95.92     69.31                                   
REMARK 500    ASP E2189        0.49    -67.57                                   
REMARK 500    CYS F2306     -111.57     60.62                                   
REMARK 500    ALA G3039       40.22   -100.19                                   
REMARK 500    ASP G3049        8.10     59.38                                   
REMARK 500    CYS G3106     -106.77     57.90                                   
REMARK 500    VAL G3186       41.15     71.70                                   
REMARK 500    SER H3203     -134.17    -86.29                                   
REMARK 500    GLU H3264       28.78    -79.88                                   
REMARK 500    CYS H3306     -108.52     68.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C4913        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH G4848        DISTANCE =  6.09 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PDV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DJ-1, P 31 2 1 SPACE GROUP                
REMARK 900 RELATED ID: 1PE0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE K130R MUTANT OF HUMAN DJ-1                  
DBREF  1PDW A    1   189  UNP    Q99497   PARK7_HUMAN      1    189             
DBREF  1PDW B  201   389  UNP    Q99497   PARK7_HUMAN      1    189             
DBREF  1PDW C 1001  1189  UNP    Q99497   PARK7_HUMAN      1    189             
DBREF  1PDW D 1201  1389  UNP    Q99497   PARK7_HUMAN      1    189             
DBREF  1PDW E 2001  2189  UNP    Q99497   PARK7_HUMAN      1    189             
DBREF  1PDW F 2201  2389  UNP    Q99497   PARK7_HUMAN      1    189             
DBREF  1PDW G 3001  3189  UNP    Q99497   PARK7_HUMAN      1    189             
DBREF  1PDW H 3201  3389  UNP    Q99497   PARK7_HUMAN      1    189             
SEQADV 1PDW MSE A   17  UNP  Q99497    MET    17 MODIFIED RESIDUE               
SEQADV 1PDW MSE A   26  UNP  Q99497    MET    26 MODIFIED RESIDUE               
SEQADV 1PDW MSE A  133  UNP  Q99497    MET   133 MODIFIED RESIDUE               
SEQADV 1PDW MSE A  134  UNP  Q99497    MET   134 MODIFIED RESIDUE               
SEQADV 1PDW LEU A  190  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW GLU A  191  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS A  192  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS A  193  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS A  194  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS A  195  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS A  196  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS A  197  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW MSE B  217  UNP  Q99497    MET    17 MODIFIED RESIDUE               
SEQADV 1PDW MSE B  226  UNP  Q99497    MET    26 MODIFIED RESIDUE               
SEQADV 1PDW MSE B  333  UNP  Q99497    MET   133 MODIFIED RESIDUE               
SEQADV 1PDW MSE B  334  UNP  Q99497    MET   134 MODIFIED RESIDUE               
SEQADV 1PDW LEU B  390  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW GLU B  391  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS B  392  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS B  393  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS B  394  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS B  395  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS B  396  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS B  397  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW MSE C 1017  UNP  Q99497    MET    17 MODIFIED RESIDUE               
SEQADV 1PDW MSE C 1026  UNP  Q99497    MET    26 MODIFIED RESIDUE               
SEQADV 1PDW MSE C 1133  UNP  Q99497    MET   133 MODIFIED RESIDUE               
SEQADV 1PDW MSE C 1134  UNP  Q99497    MET   134 MODIFIED RESIDUE               
SEQADV 1PDW LEU C 1190  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW GLU C 1191  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS C 1192  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS C 1193  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS C 1194  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS C 1195  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS C 1196  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS C 1197  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW MSE D 1217  UNP  Q99497    MET    17 MODIFIED RESIDUE               
SEQADV 1PDW MSE D 1226  UNP  Q99497    MET    26 MODIFIED RESIDUE               
SEQADV 1PDW MSE D 1333  UNP  Q99497    MET   133 MODIFIED RESIDUE               
SEQADV 1PDW MSE D 1334  UNP  Q99497    MET   134 MODIFIED RESIDUE               
SEQADV 1PDW LEU D 1390  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW GLU D 1391  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS D 1392  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS D 1393  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS D 1394  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS D 1395  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS D 1396  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS D 1397  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW MSE E 2017  UNP  Q99497    MET    17 MODIFIED RESIDUE               
SEQADV 1PDW MSE E 2026  UNP  Q99497    MET    26 MODIFIED RESIDUE               
SEQADV 1PDW MSE E 2133  UNP  Q99497    MET   133 MODIFIED RESIDUE               
SEQADV 1PDW MSE E 2134  UNP  Q99497    MET   134 MODIFIED RESIDUE               
SEQADV 1PDW LEU E 2190  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW GLU E 2191  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS E 2192  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS E 2193  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS E 2194  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS E 2195  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS E 2196  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS E 2197  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW MSE F 2217  UNP  Q99497    MET    17 MODIFIED RESIDUE               
SEQADV 1PDW MSE F 2226  UNP  Q99497    MET    26 MODIFIED RESIDUE               
SEQADV 1PDW MSE F 2333  UNP  Q99497    MET   133 MODIFIED RESIDUE               
SEQADV 1PDW MSE F 2334  UNP  Q99497    MET   134 MODIFIED RESIDUE               
SEQADV 1PDW LEU F 2390  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW GLU F 2391  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS F 2392  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS F 2393  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS F 2394  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS F 2395  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS F 2396  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS F 2397  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW MSE G 3017  UNP  Q99497    MET    17 MODIFIED RESIDUE               
SEQADV 1PDW MSE G 3026  UNP  Q99497    MET    26 MODIFIED RESIDUE               
SEQADV 1PDW MSE G 3133  UNP  Q99497    MET   133 MODIFIED RESIDUE               
SEQADV 1PDW MSE G 3134  UNP  Q99497    MET   134 MODIFIED RESIDUE               
SEQADV 1PDW LEU G 3190  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW GLU G 3191  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS G 3192  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS G 3193  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS G 3194  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS G 3195  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS G 3196  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS G 3197  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW MSE H 3217  UNP  Q99497    MET    17 MODIFIED RESIDUE               
SEQADV 1PDW MSE H 3226  UNP  Q99497    MET    26 MODIFIED RESIDUE               
SEQADV 1PDW MSE H 3333  UNP  Q99497    MET   133 MODIFIED RESIDUE               
SEQADV 1PDW MSE H 3334  UNP  Q99497    MET   134 MODIFIED RESIDUE               
SEQADV 1PDW LEU H 3390  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW GLU H 3391  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS H 3392  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS H 3393  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS H 3394  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS H 3395  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS H 3396  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PDW HIS H 3397  UNP  Q99497              EXPRESSION TAG                 
SEQRES   1 A  197  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 A  197  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE          
SEQRES   3 A  197  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 A  197  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 A  197  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 A  197  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 A  197  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 A  197  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 A  197  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 A  197  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS          
SEQRES  11 A  197  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 A  197  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 A  197  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 A  197  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 A  197  ALA PRO LEU VAL LEU LYS ASP LEU GLU HIS HIS HIS HIS          
SEQRES  16 A  197  HIS HIS                                                      
SEQRES   1 B  197  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 B  197  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE          
SEQRES   3 B  197  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 B  197  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 B  197  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 B  197  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 B  197  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 B  197  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 B  197  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 B  197  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS          
SEQRES  11 B  197  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 B  197  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 B  197  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 B  197  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 B  197  ALA PRO LEU VAL LEU LYS ASP LEU GLU HIS HIS HIS HIS          
SEQRES  16 B  197  HIS HIS                                                      
SEQRES   1 C  197  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 C  197  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE          
SEQRES   3 C  197  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 C  197  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 C  197  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 C  197  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 C  197  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 C  197  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 C  197  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 C  197  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS          
SEQRES  11 C  197  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 C  197  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 C  197  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 C  197  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 C  197  ALA PRO LEU VAL LEU LYS ASP LEU GLU HIS HIS HIS HIS          
SEQRES  16 C  197  HIS HIS                                                      
SEQRES   1 D  197  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 D  197  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE          
SEQRES   3 D  197  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 D  197  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 D  197  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 D  197  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 D  197  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 D  197  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 D  197  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 D  197  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS          
SEQRES  11 D  197  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 D  197  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 D  197  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 D  197  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 D  197  ALA PRO LEU VAL LEU LYS ASP LEU GLU HIS HIS HIS HIS          
SEQRES  16 D  197  HIS HIS                                                      
SEQRES   1 E  197  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 E  197  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE          
SEQRES   3 E  197  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 E  197  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 E  197  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 E  197  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 E  197  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 E  197  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 E  197  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 E  197  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS          
SEQRES  11 E  197  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 E  197  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 E  197  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 E  197  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 E  197  ALA PRO LEU VAL LEU LYS ASP LEU GLU HIS HIS HIS HIS          
SEQRES  16 E  197  HIS HIS                                                      
SEQRES   1 F  197  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 F  197  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE          
SEQRES   3 F  197  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 F  197  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 F  197  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 F  197  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 F  197  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 F  197  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 F  197  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 F  197  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS          
SEQRES  11 F  197  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 F  197  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 F  197  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 F  197  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 F  197  ALA PRO LEU VAL LEU LYS ASP LEU GLU HIS HIS HIS HIS          
SEQRES  16 F  197  HIS HIS                                                      
SEQRES   1 G  197  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 G  197  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE          
SEQRES   3 G  197  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 G  197  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 G  197  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 G  197  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 G  197  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 G  197  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 G  197  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 G  197  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS          
SEQRES  11 G  197  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 G  197  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 G  197  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 G  197  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 G  197  ALA PRO LEU VAL LEU LYS ASP LEU GLU HIS HIS HIS HIS          
SEQRES  16 G  197  HIS HIS                                                      
SEQRES   1 H  197  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 H  197  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE          
SEQRES   3 H  197  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 H  197  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 H  197  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 H  197  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 H  197  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 H  197  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 H  197  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 H  197  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS          
SEQRES  11 H  197  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 H  197  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 H  197  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 H  197  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 H  197  ALA PRO LEU VAL LEU LYS ASP LEU GLU HIS HIS HIS HIS          
SEQRES  16 H  197  HIS HIS                                                      
MODRES 1PDW MSE A   17  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE A   26  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE A  133  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE A  134  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE B  217  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE B  226  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE B  333  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE B  334  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE C 1017  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE C 1026  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE C 1133  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE C 1134  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE D 1217  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE D 1226  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE D 1333  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE D 1334  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE E 2017  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE E 2026  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE E 2133  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE E 2134  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE F 2217  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE F 2226  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE F 2333  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE F 2334  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE G 3017  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE G 3026  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE G 3133  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE G 3134  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE H 3217  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE H 3226  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE H 3333  MET  SELENOMETHIONINE                                   
MODRES 1PDW MSE H 3334  MET  SELENOMETHIONINE                                   
HET    MSE  A  17       8                                                       
HET    MSE  A  26       8                                                       
HET    MSE  A 133       8                                                       
HET    MSE  A 134       8                                                       
HET    MSE  B 217       8                                                       
HET    MSE  B 226       8                                                       
HET    MSE  B 333       8                                                       
HET    MSE  B 334       8                                                       
HET    MSE  C1017       8                                                       
HET    MSE  C1026       8                                                       
HET    MSE  C1133       8                                                       
HET    MSE  C1134       8                                                       
HET    MSE  D1217       8                                                       
HET    MSE  D1226       8                                                       
HET    MSE  D1333       8                                                       
HET    MSE  D1334       8                                                       
HET    MSE  E2017       8                                                       
HET    MSE  E2026       8                                                       
HET    MSE  E2133       8                                                       
HET    MSE  E2134       8                                                       
HET    MSE  F2217       8                                                       
HET    MSE  F2226       8                                                       
HET    MSE  F2333       8                                                       
HET    MSE  F2334       8                                                       
HET    MSE  G3017       8                                                       
HET    MSE  G3026       8                                                       
HET    MSE  G3133       8                                                       
HET    MSE  G3134       8                                                       
HET    MSE  H3217       8                                                       
HET    MSE  H3226       8                                                       
HET    MSE  H3333       8                                                       
HET    MSE  H3334       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    32(C5 H11 N O2 SE)                                           
FORMUL   9  HOH   *970(H2 O)                                                    
HELIX    1   1 GLU A   15  ALA A   29  1                                  15    
HELIX    2   2 LEU A   58  LYS A   63  1                                   6    
HELIX    3   3 GLY A   75  GLU A   84  1                                  10    
HELIX    4   4 SER A   85  ARG A   98  1                                  14    
HELIX    5   5 PRO A  109  HIS A  115  1                                   7    
HELIX    6   6 HIS A  126  LEU A  128  5                                   3    
HELIX    7   7 ALA A  129  MSE A  134  1                                   6    
HELIX    8   8 GLY A  157  GLY A  159  5                                   3    
HELIX    9   9 THR A  160  GLY A  174  1                                  15    
HELIX   10  10 GLY A  174  ALA A  183  1                                  10    
HELIX   11  11 GLU B  215  ALA B  229  1                                  15    
HELIX   12  12 LEU B  258  LYS B  262  1                                   5    
HELIX   13  13 GLY B  275  GLU B  284  1                                  10    
HELIX   14  14 SER B  285  ARG B  298  1                                  14    
HELIX   15  15 GLY B  308  HIS B  315  1                                   8    
HELIX   16  16 HIS B  326  LEU B  328  5                                   3    
HELIX   17  17 ALA B  329  ASN B  335  1                                   7    
HELIX   18  18 GLY B  357  GLY B  359  5                                   3    
HELIX   19  19 THR B  360  ALA B  383  1                                  24    
HELIX   20  20 PRO B  384  VAL B  386  5                                   3    
HELIX   21  21 GLU C 1015  ALA C 1029  1                                  15    
HELIX   22  22 LEU C 1058  LYS C 1062  1                                   5    
HELIX   23  23 GLY C 1075  SER C 1085  1                                  11    
HELIX   24  24 SER C 1085  ARG C 1098  1                                  14    
HELIX   25  25 PRO C 1109  HIS C 1115  1                                   7    
HELIX   26  26 HIS C 1126  LEU C 1128  5                                   3    
HELIX   27  27 ALA C 1129  ASN C 1135  1                                   7    
HELIX   28  28 GLY C 1157  GLY C 1159  5                                   3    
HELIX   29  29 THR C 1160  GLY C 1174  1                                  15    
HELIX   30  30 GLY C 1174  ALA C 1183  1                                  10    
HELIX   31  31 PRO C 1184  VAL C 1186  5                                   3    
HELIX   32  32 GLU D 1215  ALA D 1229  1                                  15    
HELIX   33  33 LEU D 1258  LYS D 1263  1                                   6    
HELIX   34  34 GLY D 1275  SER D 1285  1                                  11    
HELIX   35  35 SER D 1285  ARG D 1298  1                                  14    
HELIX   36  36 PRO D 1309  HIS D 1315  1                                   7    
HELIX   37  37 HIS D 1326  LEU D 1328  5                                   3    
HELIX   38  38 ALA D 1329  MSE D 1334  1                                   6    
HELIX   39  39 GLY D 1357  GLY D 1359  5                                   3    
HELIX   40  40 THR D 1360  GLY D 1374  1                                  15    
HELIX   41  41 GLY D 1374  ALA D 1383  1                                  10    
HELIX   42  42 PRO D 1384  VAL D 1386  5                                   3    
HELIX   43  43 GLU E 2015  ALA E 2029  1                                  15    
HELIX   44  44 LEU E 2058  GLU E 2064  1                                   7    
HELIX   45  45 GLY E 2075  SER E 2083  1                                   9    
HELIX   46  46 SER E 2085  ARG E 2098  1                                  14    
HELIX   47  47 PRO E 2109  HIS E 2115  1                                   7    
HELIX   48  48 HIS E 2126  LEU E 2128  5                                   3    
HELIX   49  49 ALA E 2129  ASN E 2135  1                                   7    
HELIX   50  50 GLY E 2157  GLY E 2159  5                                   3    
HELIX   51  51 THR E 2160  GLY E 2174  1                                  15    
HELIX   52  52 GLY E 2174  ALA E 2183  1                                  10    
HELIX   53  53 PRO E 2184  VAL E 2186  5                                   3    
HELIX   54  54 GLU F 2215  ALA F 2229  1                                  15    
HELIX   55  55 LEU F 2258  GLU F 2264  1                                   7    
HELIX   56  56 GLY F 2275  SER F 2285  1                                  11    
HELIX   57  57 SER F 2285  ARG F 2298  1                                  14    
HELIX   58  58 PRO F 2309  HIS F 2315  1                                   7    
HELIX   59  59 HIS F 2326  LEU F 2328  5                                   3    
HELIX   60  60 ALA F 2329  MSE F 2334  1                                   6    
HELIX   61  61 GLY F 2357  GLY F 2359  5                                   3    
HELIX   62  62 THR F 2360  GLY F 2374  1                                  15    
HELIX   63  63 GLY F 2374  ALA F 2383  1                                  10    
HELIX   64  64 PRO F 2384  VAL F 2386  5                                   3    
HELIX   65  65 GLU G 3015  ALA G 3029  1                                  15    
HELIX   66  66 LEU G 3058  LYS G 3062  1                                   5    
HELIX   67  67 GLY G 3075  SER G 3085  1                                  11    
HELIX   68  68 SER G 3085  ARG G 3098  1                                  14    
HELIX   69  69 PRO G 3109  HIS G 3115  1                                   7    
HELIX   70  70 HIS G 3126  LEU G 3128  5                                   3    
HELIX   71  71 ALA G 3129  ASN G 3135  1                                   7    
HELIX   72  72 GLY G 3157  GLY G 3159  5                                   3    
HELIX   73  73 THR G 3160  VAL G 3186  1                                  27    
HELIX   74  74 GLU H 3215  ALA H 3229  1                                  15    
HELIX   75  75 LEU H 3258  LYS H 3262  1                                   5    
HELIX   76  76 LYS H 3263  GLY H 3265  5                                   3    
HELIX   77  77 GLY H 3275  GLU H 3284  1                                  10    
HELIX   78  78 SER H 3285  ARG H 3298  1                                  14    
HELIX   79  79 PRO H 3309  HIS H 3315  1                                   7    
HELIX   80  80 HIS H 3326  LEU H 3328  5                                   3    
HELIX   81  81 ALA H 3329  MSE H 3334  1                                   6    
HELIX   82  82 GLY H 3357  GLY H 3359  5                                   3    
HELIX   83  83 THR H 3360  ALA H 3383  1                                  24    
HELIX   84  84 PRO H 3384  VAL H 3386  5                                   3    
SHEET    1   A 7 ALA A  56  SER A  57  0                                        
SHEET    2   A 7 LYS A  32  GLY A  37  1  N  GLY A  37   O  ALA A  56           
SHEET    3   A 7 ARG A   5  LEU A  10  1  N  LEU A  10   O  ALA A  36           
SHEET    4   A 7 VAL A  69  LEU A  72  1  O  VAL A  71   N  LEU A   7           
SHEET    5   A 7 LEU A 101  ILE A 105  1  O  ALA A 103   N  LEU A  72           
SHEET    6   A 7 ILE A 152  SER A 155  1  O  LEU A 153   N  ILE A 102           
SHEET    7   A 7 VAL A 146  ASP A 149 -1  N  GLU A 147   O  THR A 154           
SHEET    1   B 4 VAL A  44  GLN A  45  0                                        
SHEET    2   B 4 VAL A  51  CYS A  53 -1  O  ILE A  52   N  VAL A  44           
SHEET    3   B 4 VAL B 251  CYS B 253 -1  O  CYS B 253   N  VAL A  51           
SHEET    4   B 4 VAL B 244  GLN B 245 -1  N  VAL B 244   O  ILE B 252           
SHEET    1   C 2 LYS A 122  VAL A 123  0                                        
SHEET    2   C 2 THR A 140  TYR A 141  1  O  THR A 140   N  VAL A 123           
SHEET    1   D 7 ALA B 256  SER B 257  0                                        
SHEET    2   D 7 LYS B 232  GLY B 237  1  N  GLY B 237   O  ALA B 256           
SHEET    3   D 7 ARG B 205  LEU B 210  1  N  ALA B 206   O  THR B 234           
SHEET    4   D 7 VAL B 269  LEU B 272  1  O  VAL B 271   N  LEU B 207           
SHEET    5   D 7 LEU B 301  ILE B 305  1  O  ALA B 303   N  LEU B 272           
SHEET    6   D 7 ILE B 352  SER B 355  1  O  LEU B 353   N  ILE B 302           
SHEET    7   D 7 VAL B 346  ASP B 349 -1  N  ASP B 349   O  ILE B 352           
SHEET    1   E 2 LYS B 322  VAL B 323  0                                        
SHEET    2   E 2 THR B 340  TYR B 341  1  O  THR B 340   N  VAL B 323           
SHEET    1   F 7 ALA C1056  SER C1057  0                                        
SHEET    2   F 7 LYS C1032  GLY C1037  1  N  GLY C1037   O  ALA C1056           
SHEET    3   F 7 ARG C1005  LEU C1010  1  N  LEU C1010   O  ALA C1036           
SHEET    4   F 7 VAL C1069  LEU C1072  1  O  VAL C1071   N  LEU C1007           
SHEET    5   F 7 LEU C1101  ILE C1105  1  O  ALA C1103   N  LEU C1072           
SHEET    6   F 7 ILE C1152  SER C1155  1  O  LEU C1153   N  ILE C1102           
SHEET    7   F 7 VAL C1146  ASP C1149 -1  N  ASP C1149   O  ILE C1152           
SHEET    1   G 4 VAL C1044  GLN C1045  0                                        
SHEET    2   G 4 VAL C1051  CYS C1053 -1  O  ILE C1052   N  VAL C1044           
SHEET    3   G 4 VAL D1251  ILE D1252 -1  O  VAL D1251   N  CYS C1053           
SHEET    4   G 4 VAL D1244  GLN D1245 -1  N  VAL D1244   O  ILE D1252           
SHEET    1   H 2 LYS C1122  VAL C1123  0                                        
SHEET    2   H 2 THR C1140  TYR C1141  1  O  THR C1140   N  VAL C1123           
SHEET    1   I 7 ALA D1256  SER D1257  0                                        
SHEET    2   I 7 LYS D1232  GLY D1237  1  N  GLY D1237   O  ALA D1256           
SHEET    3   I 7 ARG D1205  LEU D1210  1  N  ALA D1206   O  THR D1234           
SHEET    4   I 7 VAL D1269  LEU D1272  1  O  VAL D1271   N  LEU D1207           
SHEET    5   I 7 LEU D1301  ILE D1305  1  O  ALA D1303   N  LEU D1272           
SHEET    6   I 7 ILE D1352  SER D1355  1  O  LEU D1353   N  ILE D1302           
SHEET    7   I 7 VAL D1346  ASP D1349 -1  N  GLU D1347   O  THR D1354           
SHEET    1   J 2 LYS D1322  VAL D1323  0                                        
SHEET    2   J 2 THR D1340  TYR D1341  1  O  THR D1340   N  VAL D1323           
SHEET    1   K 7 ALA E2056  SER E2057  0                                        
SHEET    2   K 7 LYS E2032  GLY E2037  1  N  GLY E2037   O  ALA E2056           
SHEET    3   K 7 ARG E2005  LEU E2010  1  N  LEU E2010   O  ALA E2036           
SHEET    4   K 7 VAL E2069  LEU E2072  1  O  VAL E2071   N  LEU E2007           
SHEET    5   K 7 LEU E2101  ILE E2105  1  O  ALA E2103   N  LEU E2072           
SHEET    6   K 7 ILE E2152  SER E2155  1  O  LEU E2153   N  ILE E2102           
SHEET    7   K 7 VAL E2146  ASP E2149 -1  N  GLU E2147   O  THR E2154           
SHEET    1   L 4 VAL E2044  GLN E2045  0                                        
SHEET    2   L 4 VAL E2051  CYS E2053 -1  O  ILE E2052   N  VAL E2044           
SHEET    3   L 4 VAL F2251  CYS F2253 -1  O  VAL F2251   N  CYS E2053           
SHEET    4   L 4 VAL F2244  GLN F2245 -1  N  VAL F2244   O  ILE F2252           
SHEET    1   M 2 LYS E2122  VAL E2123  0                                        
SHEET    2   M 2 THR E2140  TYR E2141  1  O  THR E2140   N  VAL E2123           
SHEET    1   N 7 ALA F2256  SER F2257  0                                        
SHEET    2   N 7 LYS F2232  GLY F2237  1  N  GLY F2237   O  ALA F2256           
SHEET    3   N 7 ARG F2205  LEU F2210  1  N  LEU F2210   O  ALA F2236           
SHEET    4   N 7 VAL F2269  LEU F2272  1  O  VAL F2271   N  LEU F2207           
SHEET    5   N 7 LEU F2301  ILE F2305  1  O  ALA F2303   N  LEU F2272           
SHEET    6   N 7 ILE F2352  SER F2355  1  O  LEU F2353   N  ILE F2302           
SHEET    7   N 7 VAL F2346  ASP F2349 -1  N  GLU F2347   O  THR F2354           
SHEET    1   O 2 LYS F2322  VAL F2323  0                                        
SHEET    2   O 2 THR F2340  TYR F2341  1  O  THR F2340   N  VAL F2323           
SHEET    1   P 7 ALA G3056  SER G3057  0                                        
SHEET    2   P 7 LYS G3032  GLY G3037  1  N  GLY G3037   O  ALA G3056           
SHEET    3   P 7 ARG G3005  LEU G3010  1  N  ALA G3006   O  LYS G3032           
SHEET    4   P 7 VAL G3069  LEU G3072  1  O  VAL G3071   N  LEU G3007           
SHEET    5   P 7 LEU G3101  ILE G3105  1  O  ALA G3103   N  LEU G3072           
SHEET    6   P 7 ILE G3152  SER G3155  1  O  LEU G3153   N  ILE G3102           
SHEET    7   P 7 VAL G3146  ASP G3149 -1  N  ASP G3149   O  ILE G3152           
SHEET    1   Q 4 VAL G3044  GLN G3045  0                                        
SHEET    2   Q 4 VAL G3051  ILE G3052 -1  O  ILE G3052   N  VAL G3044           
SHEET    3   Q 4 VAL H3251  CYS H3253 -1  O  CYS H3253   N  VAL G3051           
SHEET    4   Q 4 VAL H3244  GLN H3245 -1  N  VAL H3244   O  ILE H3252           
SHEET    1   R 2 LYS G3122  VAL G3123  0                                        
SHEET    2   R 2 THR G3140  TYR G3141  1  O  THR G3140   N  VAL G3123           
SHEET    1   S 7 ALA H3256  SER H3257  0                                        
SHEET    2   S 7 LYS H3232  GLY H3237  1  N  GLY H3237   O  ALA H3256           
SHEET    3   S 7 ARG H3205  LEU H3210  1  N  ALA H3206   O  THR H3234           
SHEET    4   S 7 VAL H3269  LEU H3272  1  O  VAL H3271   N  LEU H3207           
SHEET    5   S 7 LEU H3301  ILE H3305  1  O  ALA H3303   N  LEU H3272           
SHEET    6   S 7 ILE H3352  SER H3355  1  O  LEU H3353   N  ALA H3304           
SHEET    7   S 7 VAL H3346  ASP H3349 -1  N  GLU H3347   O  THR H3354           
SHEET    1   T 2 LYS H3322  VAL H3323  0                                        
SHEET    2   T 2 THR H3340  TYR H3341  1  O  THR H3340   N  VAL H3323           
LINK         C   GLU A  16                 N   MSE A  17     1555   1555  1.33  
LINK         C   MSE A  17                 N   GLU A  18     1555   1555  1.33  
LINK         C   VAL A  25                 N   MSE A  26     1555   1555  1.33  
LINK         C   MSE A  26                 N   ARG A  27     1555   1555  1.33  
LINK         C   LYS A 132                 N   MSE A 133     1555   1555  1.33  
LINK         C   MSE A 133                 N   MSE A 134     1555   1555  1.33  
LINK         C   MSE A 134                 N   ASN A 135     1555   1555  1.33  
LINK         C   GLU B 216                 N   MSE B 217     1555   1555  1.33  
LINK         C   MSE B 217                 N   GLU B 218     1555   1555  1.33  
LINK         C   VAL B 225                 N   MSE B 226     1555   1555  1.33  
LINK         C   MSE B 226                 N   ARG B 227     1555   1555  1.33  
LINK         C   LYS B 332                 N   MSE B 333     1555   1555  1.33  
LINK         C   MSE B 333                 N   MSE B 334     1555   1555  1.33  
LINK         C   MSE B 334                 N   ASN B 335     1555   1555  1.33  
LINK         C   GLU C1016                 N   MSE C1017     1555   1555  1.33  
LINK         C   MSE C1017                 N   GLU C1018     1555   1555  1.33  
LINK         C   VAL C1025                 N   MSE C1026     1555   1555  1.33  
LINK         C   MSE C1026                 N   ARG C1027     1555   1555  1.33  
LINK         C   LYS C1132                 N   MSE C1133     1555   1555  1.33  
LINK         C   MSE C1133                 N   MSE C1134     1555   1555  1.33  
LINK         C   MSE C1134                 N   ASN C1135     1555   1555  1.33  
LINK         C   GLU D1216                 N   MSE D1217     1555   1555  1.33  
LINK         C   MSE D1217                 N   GLU D1218     1555   1555  1.33  
LINK         C   VAL D1225                 N   MSE D1226     1555   1555  1.33  
LINK         C   MSE D1226                 N   ARG D1227     1555   1555  1.33  
LINK         C   LYS D1332                 N   MSE D1333     1555   1555  1.33  
LINK         C   MSE D1333                 N   MSE D1334     1555   1555  1.33  
LINK         C   MSE D1334                 N   ASN D1335     1555   1555  1.33  
LINK         C   GLU E2016                 N   MSE E2017     1555   1555  1.33  
LINK         C   MSE E2017                 N   GLU E2018     1555   1555  1.33  
LINK         C   VAL E2025                 N   MSE E2026     1555   1555  1.33  
LINK         C   MSE E2026                 N   ARG E2027     1555   1555  1.33  
LINK         C   LYS E2132                 N   MSE E2133     1555   1555  1.33  
LINK         C   MSE E2133                 N   MSE E2134     1555   1555  1.33  
LINK         C   MSE E2134                 N   ASN E2135     1555   1555  1.33  
LINK         C   GLU F2216                 N   MSE F2217     1555   1555  1.33  
LINK         C   MSE F2217                 N   GLU F2218     1555   1555  1.33  
LINK         C   VAL F2225                 N   MSE F2226     1555   1555  1.33  
LINK         C   MSE F2226                 N   ARG F2227     1555   1555  1.33  
LINK         C   LYS F2332                 N   MSE F2333     1555   1555  1.33  
LINK         C   MSE F2333                 N   MSE F2334     1555   1555  1.33  
LINK         C   MSE F2334                 N   ASN F2335     1555   1555  1.33  
LINK         C   GLU G3016                 N   MSE G3017     1555   1555  1.33  
LINK         C   MSE G3017                 N   GLU G3018     1555   1555  1.33  
LINK         C   VAL G3025                 N   MSE G3026     1555   1555  1.33  
LINK         C   MSE G3026                 N   ARG G3027     1555   1555  1.33  
LINK         C   LYS G3132                 N   MSE G3133     1555   1555  1.33  
LINK         C   MSE G3133                 N   MSE G3134     1555   1555  1.33  
LINK         C   MSE G3134                 N   ASN G3135     1555   1555  1.33  
LINK         C   GLU H3216                 N   MSE H3217     1555   1555  1.33  
LINK         C   MSE H3217                 N   GLU H3218     1555   1555  1.33  
LINK         C   VAL H3225                 N   MSE H3226     1555   1555  1.33  
LINK         C   MSE H3226                 N   ARG H3227     1555   1555  1.33  
LINK         C   LYS H3332                 N   MSE H3333     1555   1555  1.33  
LINK         C   MSE H3333                 N   MSE H3334     1555   1555  1.33  
LINK         C   MSE H3334                 N   ASN H3335     1555   1555  1.33  
CRYST1   71.256   83.664  114.159  90.00 100.56  90.00 P 1 21 1     16          
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      0.014034  0.000000  0.002615        0.00000                         
SCALE2      0.000000  0.011953  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008910        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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