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Database: PDB
Entry: 1P5F
LinkDB: 1P5F
Original site: 1P5F 
HEADER    UNKNOWN FUNCTION                        26-APR-03   1P5F              
TITLE     CRYSTAL STRUCTURE OF HUMAN DJ-1                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RNA-BINDING PROTEIN REGULATORY SUBUNIT;                    
COMPND   3 CHAIN: A;                                                            
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 BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-15B                                   
KEYWDS    UNKNOWN FUNCTION                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.WILSON,J.L.COLLINS,Y.HOD,D.RINGE,G.A.PETSKO                       
REVDAT   3   13-JUL-11 1P5F    1       VERSN                                    
REVDAT   2   24-FEB-09 1P5F    1       VERSN                                    
REVDAT   1   12-AUG-03 1P5F    0                                                
JRNL        AUTH   M.A.WILSON,J.L.COLLINS,Y.HOD,D.RINGE,G.A.PETSKO              
JRNL        TITL   THE 1.1 A RESOLUTION CRYSTAL STRUCTURE OF DJ-1, THE PROTEIN  
JRNL        TITL 2 MUTATED IN AUTOSOMAL RECESSIVE EARLY ONSET PARKINSON'S       
JRNL        TITL 3 DISEASE                                                      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 100  9256 2003              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   12855764                                                     
JRNL        DOI    10.1073/PNAS.1133288100                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.139                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.139                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.161                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.700                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 4714                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 99689                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.129                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.129                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.155                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.100                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 3998                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 78833                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1370                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 0                                             
REMARK   3   SOLVENT ATOMS      : 252                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1551.60                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1392.60                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 18                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 15913                   
REMARK   3   NUMBER OF RESTRAINTS                     : 21047                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.014                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.032                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.031                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.084                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.100                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.075                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.006                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.047                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.103                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1P5F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019029.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-AUG-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : BENT GE(111)                       
REMARK 200  OPTICS                         : CONICAL SI MIRROR                  
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   : 99689                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 36.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO PHASING            
REMARK 200 SOFTWARE USED: SOLVE/RESOLVE                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, TRIS-HCL, SODIUM CITRATE, PH    
REMARK 280  8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 23K                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       25.14067            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       50.28133            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       50.28133            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       25.14067            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER GENERATED FROM THE        
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS: Y, X, -Z+1         
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: 14800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       75.42200            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 398  LIES ON A SPECIAL POSITION.                          
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     ALA A     2                                                      
REMARK 465     ASP A   189                                                      
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    SER A   3   N   -  CA  -  CB  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    SER A   3   CA  -  C   -  O   ANGL. DEV. = -21.5 DEGREES          
REMARK 500    SER A   3   CA  -  C   -  N   ANGL. DEV. =  16.7 DEGREES          
REMARK 500    ARG A   5   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A  98   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    CYS A 106   CA  -  C   -  N   ANGL. DEV. =  13.6 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    CYS A 106     -101.02     77.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 357        DISTANCE =  5.80 ANGSTROMS                       
REMARK 525    HOH A 438        DISTANCE =  5.13 ANGSTROMS                       
DBREF  1P5F A    1   189  UNP    Q99497   PARK7_HUMAN      1    189             
SEQRES   1 A  189  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 A  189  ALA GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET          
SEQRES   3 A  189  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 A  189  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 A  189  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 A  189  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 A  189  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 A  189  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 A  189  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 A  189  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS          
SEQRES  11 A  189  ASP LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 A  189  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 A  189  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 A  189  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 A  189  ALA PRO LEU VAL LEU LYS ASP                                  
FORMUL   2  HOH   *252(H2 O)                                                    
HELIX    1   1 GLU A   15  ALA A   29  1                                  15    
HELIX    2   2 LEU A   58  GLU A   64  1                                   7    
HELIX    3   3 GLY A   75  SER A   85  1                                  11    
HELIX    4   4 SER A   85  ARG A   98  1                                  14    
HELIX    5   5 GLY A  108  HIS A  115  1                                   8    
HELIX    6   6 HIS A  126  LEU A  128  5                                   3    
HELIX    7   7 ALA A  129  MET 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 PRO A  184  VAL A  186  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  VAL A  70           
SHEET    6   A 7 ILE A 152  SER A 155  1  O  LEU A 153   N  ALA A 104           
SHEET    7   A 7 VAL A 146  ASP A 149 -1  N  GLU A 147   O  THR A 154           
SHEET    1   B 2 VAL A  44  GLN A  45  0                                        
SHEET    2   B 2 VAL A  51  ILE A  52 -1  O  ILE A  52   N  VAL A  44           
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           
CISPEP   1 GLY A   65    PRO A   66          0         6.06                     
CRYST1   75.306   75.306   75.422  90.00  90.00 120.00 P 31 2 1      6          
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      0.013279  0.007667  0.000000        0.00000                         
SCALE2      0.000000  0.015333  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013259        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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