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Database: PDB
Entry: 4E2I
LinkDB: 4E2I
Original site: 4E2I 
HEADER    HYDROLASE/DNA BINDING PROTEIN           08-MAR-12   4E2I              
TITLE     THE COMPLEX STRUCTURE OF THE SV40 HELICASE LARGE T ANTIGEN AND P68    
TITLE    2 SUBUNIT OF DNA POLYMERASE ALPHA-PRIMASE                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LARGE T ANTIGEN;                                           
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 FRAGMENT: UNP RESIDUES 266-627;                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA POLYMERASE ALPHA SUBUNIT B;                            
COMPND   8 CHAIN: 2, 3, 6, U, W, 5, 7, 9, 1, 4, 8;                              
COMPND   9 FRAGMENT: UNP RESIDUES 1-78;                                         
COMPND  10 SYNONYM: DNA POLYMERASE ALPHA 70 KDA SUBUNIT;                        
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SIMIAN VIRUS 40;                                
SOURCE   3 ORGANISM_COMMON: SV40;                                               
SOURCE   4 ORGANISM_TAXID: 10633;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 GENE: POLA2;                                                         
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    REPLICATION INITIATION, HYDROLASE-DNA BINDING COMPLEX, HYDROLASE-DNA  
KEYWDS   2 BINDING PROTEIN COMPLEX                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.ZHOU,D.R.ARNETT,X.YU,A.BREWSTER,G.A.SOWD,C.L.XIE,S.VILA,D.GAI,      
AUTHOR   2 E.FANNING,X.S.CHEN                                                   
REVDAT   2   28-AUG-13 4E2I    1       JRNL                                     
REVDAT   1   13-JUN-12 4E2I    0                                                
JRNL        AUTH   B.ZHOU,D.R.ARNETT,X.YU,A.BREWSTER,G.A.SOWD,C.L.XIE,S.VILA,   
JRNL        AUTH 2 D.GAI,E.FANNING,X.S.CHEN                                     
JRNL        TITL   STRUCTURAL BASIS FOR THE INTERACTION OF A HEXAMERIC          
JRNL        TITL 2 REPLICATIVE HELICASE WITH THE REGULATORY SUBUNIT OF HUMAN    
JRNL        TITL 3 DNA POLYMERASE ALPHA-PRIMASE.                                
JRNL        REF    J.BIOL.CHEM.                  V. 287 26854 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22700977                                                     
JRNL        DOI    10.1074/JBC.M112.363655                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    5.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 5.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
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)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 35234                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.305                           
REMARK   3   FREE R VALUE                     : 0.314                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3538                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 41862                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.003                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4E2I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071086.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.11587                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39723                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 5.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 74.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
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) : 5.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 5.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.96 M SODIUM MALONATE, PH 6.0, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      193.51600            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000      124.54900            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000      124.54900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       96.75800            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000      124.54900            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000      124.54900            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      290.27400            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000      124.54900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      124.54900            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       96.75800            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000      124.54900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      124.54900            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      290.27400            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      193.51600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, 2, 3, 6,            
REMARK 350                    AND CHAINS: 5, 1, 4                               
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: UNDECAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L, U, W, 7,            
REMARK 350                    AND CHAINS: 9, 8                                  
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG C 583   CD  -  NE  -  CZ  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ARG C 583   NE  -  CZ  -  NH1 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    ARG C 583   NE  -  CZ  -  NH2 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG I 583   CD  -  NE  -  CZ  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ARG I 583   NE  -  CZ  -  NH1 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    ARG I 583   NE  -  CZ  -  NH2 ANGL. DEV. =   9.7 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    TYR A 297      -94.16   -115.70                                   
REMARK 500    SER A 298      125.62   -173.47                                   
REMARK 500    HIS A 313      -71.05   -122.78                                   
REMARK 500    ASN A 415       78.73     53.74                                   
REMARK 500    LYS A 419       59.62   -152.71                                   
REMARK 500    ARG A 420      -56.34   -130.82                                   
REMARK 500    PHE A 424       65.09   -106.74                                   
REMARK 500    PRO A 427      175.18    -56.00                                   
REMARK 500    ASP A 429       91.21     56.11                                   
REMARK 500    SER A 430      -34.00   -152.00                                   
REMARK 500    PRO A 453      157.46    -48.32                                   
REMARK 500    ASP A 466       16.17     56.44                                   
REMARK 500    ASP A 474       93.13     41.96                                   
REMARK 500    LYS A 512       84.02     56.48                                   
REMARK 500    HIS A 513      -90.96     54.83                                   
REMARK 500    GLN A 519     -165.94   -116.40                                   
REMARK 500    PRO A 523     -163.09    -68.93                                   
REMARK 500    ASN A 529       73.95   -115.03                                   
REMARK 500    VAL A 542      -57.00   -125.00                                   
REMARK 500    PRO A 549       89.50    -66.96                                   
REMARK 500    SER A 560       59.79   -144.10                                   
REMARK 500    ARG A 567       79.00     52.28                                   
REMARK 500    TYR A 582      -64.84    -91.35                                   
REMARK 500    ALA A 586        1.92    -68.74                                   
REMARK 500    SER A 608     -159.92    -85.65                                   
REMARK 500    LEU A 626       61.97   -103.82                                   
REMARK 500    GLN B 267      145.15   -175.55                                   
REMARK 500    TYR B 297      -94.25   -116.13                                   
REMARK 500    SER B 298      125.85   -172.78                                   
REMARK 500    HIS B 313      -71.45   -122.44                                   
REMARK 500    ASN B 415       78.62     53.49                                   
REMARK 500    LYS B 419       59.41   -152.66                                   
REMARK 500    ARG B 420      -57.05   -130.57                                   
REMARK 500    PHE B 424       65.25   -106.99                                   
REMARK 500    PRO B 427      175.56    -55.99                                   
REMARK 500    ASP B 429       91.39     56.45                                   
REMARK 500    SER B 430      -34.71   -152.11                                   
REMARK 500    PRO B 453      157.45    -48.39                                   
REMARK 500    ASP B 466       16.76     56.54                                   
REMARK 500    ASP B 474       93.08     42.08                                   
REMARK 500    LYS B 512       84.11     56.23                                   
REMARK 500    HIS B 513      -91.24     54.85                                   
REMARK 500    GLN B 519     -165.70   -116.37                                   
REMARK 500    PRO B 523     -162.93    -69.03                                   
REMARK 500    ASN B 529       73.91   -115.22                                   
REMARK 500    VAL B 542      -56.67   -124.97                                   
REMARK 500    PRO B 549       89.50    -67.03                                   
REMARK 500    SER B 560       59.86   -144.10                                   
REMARK 500    ARG B 567       79.06     52.26                                   
REMARK 500    TYR B 582      -64.76    -91.40                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     387 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 700  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G 317   ND1                                                    
REMARK 620 2 HIS G 313   NE2 116.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 700  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 317   ND1                                                    
REMARK 620 2 HIS B 313   NE2 111.0                                              
REMARK 620 3 CYS B 302   SG   98.6  93.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 700  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 313   NE2                                                    
REMARK 620 2 HIS A 317   ND1 106.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 700  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I 317   ND1                                                    
REMARK 620 2 HIS I 313   NE2 107.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K 700  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K 317   ND1                                                    
REMARK 620 2 HIS K 313   NE2 103.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 700                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 700                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 700                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 700                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 700                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 700                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 700                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 700                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 700                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 700                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 700                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 700                  
DBREF  4E2I A  266   627  UNP    Q9DH70   Q9DH70_SV40    266    627             
DBREF  4E2I B  266   627  UNP    Q9DH70   Q9DH70_SV40    266    627             
DBREF  4E2I C  266   627  UNP    Q9DH70   Q9DH70_SV40    266    627             
DBREF  4E2I D  266   627  UNP    Q9DH70   Q9DH70_SV40    266    627             
DBREF  4E2I E  266   627  UNP    Q9DH70   Q9DH70_SV40    266    627             
DBREF  4E2I F  266   627  UNP    Q9DH70   Q9DH70_SV40    266    627             
DBREF  4E2I G  266   627  UNP    Q9DH70   Q9DH70_SV40    266    627             
DBREF  4E2I H  266   627  UNP    Q9DH70   Q9DH70_SV40    266    627             
DBREF  4E2I I  266   627  UNP    Q9DH70   Q9DH70_SV40    266    627             
DBREF  4E2I J  266   627  UNP    Q9DH70   Q9DH70_SV40    266    627             
DBREF  4E2I K  266   627  UNP    Q9DH70   Q9DH70_SV40    266    627             
DBREF  4E2I L  266   627  UNP    Q9DH70   Q9DH70_SV40    266    627             
DBREF  4E2I 2    1    78  UNP    Q14181   DPOA2_HUMAN      1     78             
DBREF  4E2I 3    1    78  UNP    Q14181   DPOA2_HUMAN      1     78             
DBREF  4E2I 6    1    78  UNP    Q14181   DPOA2_HUMAN      1     78             
DBREF  4E2I U    1    78  UNP    Q14181   DPOA2_HUMAN      1     78             
DBREF  4E2I W    1    78  UNP    Q14181   DPOA2_HUMAN      1     78             
DBREF  4E2I 5    1    78  UNP    Q14181   DPOA2_HUMAN      1     78             
DBREF  4E2I 7    1    78  UNP    Q14181   DPOA2_HUMAN      1     78             
DBREF  4E2I 9    1    78  UNP    Q14181   DPOA2_HUMAN      1     78             
DBREF  4E2I 1    1    78  UNP    Q14181   DPOA2_HUMAN      1     78             
DBREF  4E2I 4    1    78  UNP    Q14181   DPOA2_HUMAN      1     78             
DBREF  4E2I 8    1    78  UNP    Q14181   DPOA2_HUMAN      1     78             
SEQRES   1 A  362  LYS GLN VAL SER TRP LYS LEU VAL THR GLU TYR ALA MET          
SEQRES   2 A  362  GLU THR LYS CYS ASP ASP VAL LEU LEU LEU LEU GLY MET          
SEQRES   3 A  362  TYR LEU GLU PHE GLN TYR SER PHE GLU MET CYS LEU LYS          
SEQRES   4 A  362  CYS ILE LYS LYS GLU GLN PRO SER HIS TYR LYS TYR HIS          
SEQRES   5 A  362  GLU LYS HIS TYR ALA ASN ALA ALA ILE PHE ALA ASP SER          
SEQRES   6 A  362  LYS ASN GLN LYS THR ILE CYS GLN GLN ALA VAL ASP THR          
SEQRES   7 A  362  VAL LEU ALA LYS LYS ARG VAL ASP SER LEU GLN LEU THR          
SEQRES   8 A  362  ARG GLU GLN MET LEU THR ASN ARG PHE ASN ASP LEU LEU          
SEQRES   9 A  362  ASP ARG MET ASP ILE MET PHE GLY SER THR GLY SER ALA          
SEQRES  10 A  362  ASP ILE GLU GLU TRP MET ALA GLY VAL ALA TRP LEU HIS          
SEQRES  11 A  362  CYS LEU LEU PRO LYS MET ASP SER VAL VAL TYR ASP PHE          
SEQRES  12 A  362  LEU LYS CYS MET VAL TYR ASN ILE PRO LYS LYS ARG TYR          
SEQRES  13 A  362  TRP LEU PHE LYS GLY PRO ILE ASP SER GLY LYS THR THR          
SEQRES  14 A  362  LEU ALA ALA ALA LEU LEU GLU LEU CYS GLY GLY LYS ALA          
SEQRES  15 A  362  LEU ASN VAL ASN LEU PRO LEU ASP ARG LEU ASN PHE GLU          
SEQRES  16 A  362  LEU GLY VAL ALA ILE ASP GLN PHE LEU VAL VAL PHE GLU          
SEQRES  17 A  362  ASP VAL LYS GLY THR GLY GLY GLU SER ARG ASP LEU PRO          
SEQRES  18 A  362  SER GLY GLN GLY ILE ASN ASN LEU ASP ASN LEU ARG ASP          
SEQRES  19 A  362  TYR LEU ASP GLY SER VAL LYS VAL ASN LEU GLU LYS LYS          
SEQRES  20 A  362  HIS LEU ASN LYS ARG THR GLN ILE PHE PRO PRO GLY ILE          
SEQRES  21 A  362  VAL THR MET ASN GLU TYR SER VAL PRO LYS THR LEU GLN          
SEQRES  22 A  362  ALA ARG PHE VAL LYS GLN ILE ASP PHE ARG PRO LYS ASP          
SEQRES  23 A  362  TYR LEU LYS HIS CYS LEU GLU ARG SER GLU PHE LEU LEU          
SEQRES  24 A  362  GLU LYS ARG ILE ILE GLN SER GLY ILE ALA LEU LEU LEU          
SEQRES  25 A  362  MET LEU ILE TRP TYR ARG PRO VAL ALA GLU PHE ALA GLN          
SEQRES  26 A  362  SER ILE GLN SER ARG ILE VAL GLU TRP LYS GLU ARG LEU          
SEQRES  27 A  362  ASP LYS GLU PHE SER LEU SER VAL TYR GLN LYS MET LYS          
SEQRES  28 A  362  PHE ASN VAL ALA MET GLY ILE GLY VAL LEU ASP                  
SEQRES   1 B  362  LYS GLN VAL SER TRP LYS LEU VAL THR GLU TYR ALA MET          
SEQRES   2 B  362  GLU THR LYS CYS ASP ASP VAL LEU LEU LEU LEU GLY MET          
SEQRES   3 B  362  TYR LEU GLU PHE GLN TYR SER PHE GLU MET CYS LEU LYS          
SEQRES   4 B  362  CYS ILE LYS LYS GLU GLN PRO SER HIS TYR LYS TYR HIS          
SEQRES   5 B  362  GLU LYS HIS TYR ALA ASN ALA ALA ILE PHE ALA ASP SER          
SEQRES   6 B  362  LYS ASN GLN LYS THR ILE CYS GLN GLN ALA VAL ASP THR          
SEQRES   7 B  362  VAL LEU ALA LYS LYS ARG VAL ASP SER LEU GLN LEU THR          
SEQRES   8 B  362  ARG GLU GLN MET LEU THR ASN ARG PHE ASN ASP LEU LEU          
SEQRES   9 B  362  ASP ARG MET ASP ILE MET PHE GLY SER THR GLY SER ALA          
SEQRES  10 B  362  ASP ILE GLU GLU TRP MET ALA GLY VAL ALA TRP LEU HIS          
SEQRES  11 B  362  CYS LEU LEU PRO LYS MET ASP SER VAL VAL TYR ASP PHE          
SEQRES  12 B  362  LEU LYS CYS MET VAL TYR ASN ILE PRO LYS LYS ARG TYR          
SEQRES  13 B  362  TRP LEU PHE LYS GLY PRO ILE ASP SER GLY LYS THR THR          
SEQRES  14 B  362  LEU ALA ALA ALA LEU LEU GLU LEU CYS GLY GLY LYS ALA          
SEQRES  15 B  362  LEU ASN VAL ASN LEU PRO LEU ASP ARG LEU ASN PHE GLU          
SEQRES  16 B  362  LEU GLY VAL ALA ILE ASP GLN PHE LEU VAL VAL PHE GLU          
SEQRES  17 B  362  ASP VAL LYS GLY THR GLY GLY GLU SER ARG ASP LEU PRO          
SEQRES  18 B  362  SER GLY GLN GLY ILE ASN ASN LEU ASP ASN LEU ARG ASP          
SEQRES  19 B  362  TYR LEU ASP GLY SER VAL LYS VAL ASN LEU GLU LYS LYS          
SEQRES  20 B  362  HIS LEU ASN LYS ARG THR GLN ILE PHE PRO PRO GLY ILE          
SEQRES  21 B  362  VAL THR MET ASN GLU TYR SER VAL PRO LYS THR LEU GLN          
SEQRES  22 B  362  ALA ARG PHE VAL LYS GLN ILE ASP PHE ARG PRO LYS ASP          
SEQRES  23 B  362  TYR LEU LYS HIS CYS LEU GLU ARG SER GLU PHE LEU LEU          
SEQRES  24 B  362  GLU LYS ARG ILE ILE GLN SER GLY ILE ALA LEU LEU LEU          
SEQRES  25 B  362  MET LEU ILE TRP TYR ARG PRO VAL ALA GLU PHE ALA GLN          
SEQRES  26 B  362  SER ILE GLN SER ARG ILE VAL GLU TRP LYS GLU ARG LEU          
SEQRES  27 B  362  ASP LYS GLU PHE SER LEU SER VAL TYR GLN LYS MET LYS          
SEQRES  28 B  362  PHE ASN VAL ALA MET GLY ILE GLY VAL LEU ASP                  
SEQRES   1 C  362  LYS GLN VAL SER TRP LYS LEU VAL THR GLU TYR ALA MET          
SEQRES   2 C  362  GLU THR LYS CYS ASP ASP VAL LEU LEU LEU LEU GLY MET          
SEQRES   3 C  362  TYR LEU GLU PHE GLN TYR SER PHE GLU MET CYS LEU LYS          
SEQRES   4 C  362  CYS ILE LYS LYS GLU GLN PRO SER HIS TYR LYS TYR HIS          
SEQRES   5 C  362  GLU LYS HIS TYR ALA ASN ALA ALA ILE PHE ALA ASP SER          
SEQRES   6 C  362  LYS ASN GLN LYS THR ILE CYS GLN GLN ALA VAL ASP THR          
SEQRES   7 C  362  VAL LEU ALA LYS LYS ARG VAL ASP SER LEU GLN LEU THR          
SEQRES   8 C  362  ARG GLU GLN MET LEU THR ASN ARG PHE ASN ASP LEU LEU          
SEQRES   9 C  362  ASP ARG MET ASP ILE MET PHE GLY SER THR GLY SER ALA          
SEQRES  10 C  362  ASP ILE GLU GLU TRP MET ALA GLY VAL ALA TRP LEU HIS          
SEQRES  11 C  362  CYS LEU LEU PRO LYS MET ASP SER VAL VAL TYR ASP PHE          
SEQRES  12 C  362  LEU LYS CYS MET VAL TYR ASN ILE PRO LYS LYS ARG TYR          
SEQRES  13 C  362  TRP LEU PHE LYS GLY PRO ILE ASP SER GLY LYS THR THR          
SEQRES  14 C  362  LEU ALA ALA ALA LEU LEU GLU LEU CYS GLY GLY LYS ALA          
SEQRES  15 C  362  LEU ASN VAL ASN LEU PRO LEU ASP ARG LEU ASN PHE GLU          
SEQRES  16 C  362  LEU GLY VAL ALA ILE ASP GLN PHE LEU VAL VAL PHE GLU          
SEQRES  17 C  362  ASP VAL LYS GLY THR GLY GLY GLU SER ARG ASP LEU PRO          
SEQRES  18 C  362  SER GLY GLN GLY ILE ASN ASN LEU ASP ASN LEU ARG ASP          
SEQRES  19 C  362  TYR LEU ASP GLY SER VAL LYS VAL ASN LEU GLU LYS LYS          
SEQRES  20 C  362  HIS LEU ASN LYS ARG THR GLN ILE PHE PRO PRO GLY ILE          
SEQRES  21 C  362  VAL THR MET ASN GLU TYR SER VAL PRO LYS THR LEU GLN          
SEQRES  22 C  362  ALA ARG PHE VAL LYS GLN ILE ASP PHE ARG PRO LYS ASP          
SEQRES  23 C  362  TYR LEU LYS HIS CYS LEU GLU ARG SER GLU PHE LEU LEU          
SEQRES  24 C  362  GLU LYS ARG ILE ILE GLN SER GLY ILE ALA LEU LEU LEU          
SEQRES  25 C  362  MET LEU ILE TRP TYR ARG PRO VAL ALA GLU PHE ALA GLN          
SEQRES  26 C  362  SER ILE GLN SER ARG ILE VAL GLU TRP LYS GLU ARG LEU          
SEQRES  27 C  362  ASP LYS GLU PHE SER LEU SER VAL TYR GLN LYS MET LYS          
SEQRES  28 C  362  PHE ASN VAL ALA MET GLY ILE GLY VAL LEU ASP                  
SEQRES   1 D  362  LYS GLN VAL SER TRP LYS LEU VAL THR GLU TYR ALA MET          
SEQRES   2 D  362  GLU THR LYS CYS ASP ASP VAL LEU LEU LEU LEU GLY MET          
SEQRES   3 D  362  TYR LEU GLU PHE GLN TYR SER PHE GLU MET CYS LEU LYS          
SEQRES   4 D  362  CYS ILE LYS LYS GLU GLN PRO SER HIS TYR LYS TYR HIS          
SEQRES   5 D  362  GLU LYS HIS TYR ALA ASN ALA ALA ILE PHE ALA ASP SER          
SEQRES   6 D  362  LYS ASN GLN LYS THR ILE CYS GLN GLN ALA VAL ASP THR          
SEQRES   7 D  362  VAL LEU ALA LYS LYS ARG VAL ASP SER LEU GLN LEU THR          
SEQRES   8 D  362  ARG GLU GLN MET LEU THR ASN ARG PHE ASN ASP LEU LEU          
SEQRES   9 D  362  ASP ARG MET ASP ILE MET PHE GLY SER THR GLY SER ALA          
SEQRES  10 D  362  ASP ILE GLU GLU TRP MET ALA GLY VAL ALA TRP LEU HIS          
SEQRES  11 D  362  CYS LEU LEU PRO LYS MET ASP SER VAL VAL TYR ASP PHE          
SEQRES  12 D  362  LEU LYS CYS MET VAL TYR ASN ILE PRO LYS LYS ARG TYR          
SEQRES  13 D  362  TRP LEU PHE LYS GLY PRO ILE ASP SER GLY LYS THR THR          
SEQRES  14 D  362  LEU ALA ALA ALA LEU LEU GLU LEU CYS GLY GLY LYS ALA          
SEQRES  15 D  362  LEU ASN VAL ASN LEU PRO LEU ASP ARG LEU ASN PHE GLU          
SEQRES  16 D  362  LEU GLY VAL ALA ILE ASP GLN PHE LEU VAL VAL PHE GLU          
SEQRES  17 D  362  ASP VAL LYS GLY THR GLY GLY GLU SER ARG ASP LEU PRO          
SEQRES  18 D  362  SER GLY GLN GLY ILE ASN ASN LEU ASP ASN LEU ARG ASP          
SEQRES  19 D  362  TYR LEU ASP GLY SER VAL LYS VAL ASN LEU GLU LYS LYS          
SEQRES  20 D  362  HIS LEU ASN LYS ARG THR GLN ILE PHE PRO PRO GLY ILE          
SEQRES  21 D  362  VAL THR MET ASN GLU TYR SER VAL PRO LYS THR LEU GLN          
SEQRES  22 D  362  ALA ARG PHE VAL LYS GLN ILE ASP PHE ARG PRO LYS ASP          
SEQRES  23 D  362  TYR LEU LYS HIS CYS LEU GLU ARG SER GLU PHE LEU LEU          
SEQRES  24 D  362  GLU LYS ARG ILE ILE GLN SER GLY ILE ALA LEU LEU LEU          
SEQRES  25 D  362  MET LEU ILE TRP TYR ARG PRO VAL ALA GLU PHE ALA GLN          
SEQRES  26 D  362  SER ILE GLN SER ARG ILE VAL GLU TRP LYS GLU ARG LEU          
SEQRES  27 D  362  ASP LYS GLU PHE SER LEU SER VAL TYR GLN LYS MET LYS          
SEQRES  28 D  362  PHE ASN VAL ALA MET GLY ILE GLY VAL LEU ASP                  
SEQRES   1 E  362  LYS GLN VAL SER TRP LYS LEU VAL THR GLU TYR ALA MET          
SEQRES   2 E  362  GLU THR LYS CYS ASP ASP VAL LEU LEU LEU LEU GLY MET          
SEQRES   3 E  362  TYR LEU GLU PHE GLN TYR SER PHE GLU MET CYS LEU LYS          
SEQRES   4 E  362  CYS ILE LYS LYS GLU GLN PRO SER HIS TYR LYS TYR HIS          
SEQRES   5 E  362  GLU LYS HIS TYR ALA ASN ALA ALA ILE PHE ALA ASP SER          
SEQRES   6 E  362  LYS ASN GLN LYS THR ILE CYS GLN GLN ALA VAL ASP THR          
SEQRES   7 E  362  VAL LEU ALA LYS LYS ARG VAL ASP SER LEU GLN LEU THR          
SEQRES   8 E  362  ARG GLU GLN MET LEU THR ASN ARG PHE ASN ASP LEU LEU          
SEQRES   9 E  362  ASP ARG MET ASP ILE MET PHE GLY SER THR GLY SER ALA          
SEQRES  10 E  362  ASP ILE GLU GLU TRP MET ALA GLY VAL ALA TRP LEU HIS          
SEQRES  11 E  362  CYS LEU LEU PRO LYS MET ASP SER VAL VAL TYR ASP PHE          
SEQRES  12 E  362  LEU LYS CYS MET VAL TYR ASN ILE PRO LYS LYS ARG TYR          
SEQRES  13 E  362  TRP LEU PHE LYS GLY PRO ILE ASP SER GLY LYS THR THR          
SEQRES  14 E  362  LEU ALA ALA ALA LEU LEU GLU LEU CYS GLY GLY LYS ALA          
SEQRES  15 E  362  LEU ASN VAL ASN LEU PRO LEU ASP ARG LEU ASN PHE GLU          
SEQRES  16 E  362  LEU GLY VAL ALA ILE ASP GLN PHE LEU VAL VAL PHE GLU          
SEQRES  17 E  362  ASP VAL LYS GLY THR GLY GLY GLU SER ARG ASP LEU PRO          
SEQRES  18 E  362  SER GLY GLN GLY ILE ASN ASN LEU ASP ASN LEU ARG ASP          
SEQRES  19 E  362  TYR LEU ASP GLY SER VAL LYS VAL ASN LEU GLU LYS LYS          
SEQRES  20 E  362  HIS LEU ASN LYS ARG THR GLN ILE PHE PRO PRO GLY ILE          
SEQRES  21 E  362  VAL THR MET ASN GLU TYR SER VAL PRO LYS THR LEU GLN          
SEQRES  22 E  362  ALA ARG PHE VAL LYS GLN ILE ASP PHE ARG PRO LYS ASP          
SEQRES  23 E  362  TYR LEU LYS HIS CYS LEU GLU ARG SER GLU PHE LEU LEU          
SEQRES  24 E  362  GLU LYS ARG ILE ILE GLN SER GLY ILE ALA LEU LEU LEU          
SEQRES  25 E  362  MET LEU ILE TRP TYR ARG PRO VAL ALA GLU PHE ALA GLN          
SEQRES  26 E  362  SER ILE GLN SER ARG ILE VAL GLU TRP LYS GLU ARG LEU          
SEQRES  27 E  362  ASP LYS GLU PHE SER LEU SER VAL TYR GLN LYS MET LYS          
SEQRES  28 E  362  PHE ASN VAL ALA MET GLY ILE GLY VAL LEU ASP                  
SEQRES   1 F  362  LYS GLN VAL SER TRP LYS LEU VAL THR GLU TYR ALA MET          
SEQRES   2 F  362  GLU THR LYS CYS ASP ASP VAL LEU LEU LEU LEU GLY MET          
SEQRES   3 F  362  TYR LEU GLU PHE GLN TYR SER PHE GLU MET CYS LEU LYS          
SEQRES   4 F  362  CYS ILE LYS LYS GLU GLN PRO SER HIS TYR LYS TYR HIS          
SEQRES   5 F  362  GLU LYS HIS TYR ALA ASN ALA ALA ILE PHE ALA ASP SER          
SEQRES   6 F  362  LYS ASN GLN LYS THR ILE CYS GLN GLN ALA VAL ASP THR          
SEQRES   7 F  362  VAL LEU ALA LYS LYS ARG VAL ASP SER LEU GLN LEU THR          
SEQRES   8 F  362  ARG GLU GLN MET LEU THR ASN ARG PHE ASN ASP LEU LEU          
SEQRES   9 F  362  ASP ARG MET ASP ILE MET PHE GLY SER THR GLY SER ALA          
SEQRES  10 F  362  ASP ILE GLU GLU TRP MET ALA GLY VAL ALA TRP LEU HIS          
SEQRES  11 F  362  CYS LEU LEU PRO LYS MET ASP SER VAL VAL TYR ASP PHE          
SEQRES  12 F  362  LEU LYS CYS MET VAL TYR ASN ILE PRO LYS LYS ARG TYR          
SEQRES  13 F  362  TRP LEU PHE LYS GLY PRO ILE ASP SER GLY LYS THR THR          
SEQRES  14 F  362  LEU ALA ALA ALA LEU LEU GLU LEU CYS GLY GLY LYS ALA          
SEQRES  15 F  362  LEU ASN VAL ASN LEU PRO LEU ASP ARG LEU ASN PHE GLU          
SEQRES  16 F  362  LEU GLY VAL ALA ILE ASP GLN PHE LEU VAL VAL PHE GLU          
SEQRES  17 F  362  ASP VAL LYS GLY THR GLY GLY GLU SER ARG ASP LEU PRO          
SEQRES  18 F  362  SER GLY GLN GLY ILE ASN ASN LEU ASP ASN LEU ARG ASP          
SEQRES  19 F  362  TYR LEU ASP GLY SER VAL LYS VAL ASN LEU GLU LYS LYS          
SEQRES  20 F  362  HIS LEU ASN LYS ARG THR GLN ILE PHE PRO PRO GLY ILE          
SEQRES  21 F  362  VAL THR MET ASN GLU TYR SER VAL PRO LYS THR LEU GLN          
SEQRES  22 F  362  ALA ARG PHE VAL LYS GLN ILE ASP PHE ARG PRO LYS ASP          
SEQRES  23 F  362  TYR LEU LYS HIS CYS LEU GLU ARG SER GLU PHE LEU LEU          
SEQRES  24 F  362  GLU LYS ARG ILE ILE GLN SER GLY ILE ALA LEU LEU LEU          
SEQRES  25 F  362  MET LEU ILE TRP TYR ARG PRO VAL ALA GLU PHE ALA GLN          
SEQRES  26 F  362  SER ILE GLN SER ARG ILE VAL GLU TRP LYS GLU ARG LEU          
SEQRES  27 F  362  ASP LYS GLU PHE SER LEU SER VAL TYR GLN LYS MET LYS          
SEQRES  28 F  362  PHE ASN VAL ALA MET GLY ILE GLY VAL LEU ASP                  
SEQRES   1 G  362  LYS GLN VAL SER TRP LYS LEU VAL THR GLU TYR ALA MET          
SEQRES   2 G  362  GLU THR LYS CYS ASP ASP VAL LEU LEU LEU LEU GLY MET          
SEQRES   3 G  362  TYR LEU GLU PHE GLN TYR SER PHE GLU MET CYS LEU LYS          
SEQRES   4 G  362  CYS ILE LYS LYS GLU GLN PRO SER HIS TYR LYS TYR HIS          
SEQRES   5 G  362  GLU LYS HIS TYR ALA ASN ALA ALA ILE PHE ALA ASP SER          
SEQRES   6 G  362  LYS ASN GLN LYS THR ILE CYS GLN GLN ALA VAL ASP THR          
SEQRES   7 G  362  VAL LEU ALA LYS LYS ARG VAL ASP SER LEU GLN LEU THR          
SEQRES   8 G  362  ARG GLU GLN MET LEU THR ASN ARG PHE ASN ASP LEU LEU          
SEQRES   9 G  362  ASP ARG MET ASP ILE MET PHE GLY SER THR GLY SER ALA          
SEQRES  10 G  362  ASP ILE GLU GLU TRP MET ALA GLY VAL ALA TRP LEU HIS          
SEQRES  11 G  362  CYS LEU LEU PRO LYS MET ASP SER VAL VAL TYR ASP PHE          
SEQRES  12 G  362  LEU LYS CYS MET VAL TYR ASN ILE PRO LYS LYS ARG TYR          
SEQRES  13 G  362  TRP LEU PHE LYS GLY PRO ILE ASP SER GLY LYS THR THR          
SEQRES  14 G  362  LEU ALA ALA ALA LEU LEU GLU LEU CYS GLY GLY LYS ALA          
SEQRES  15 G  362  LEU ASN VAL ASN LEU PRO LEU ASP ARG LEU ASN PHE GLU          
SEQRES  16 G  362  LEU GLY VAL ALA ILE ASP GLN PHE LEU VAL VAL PHE GLU          
SEQRES  17 G  362  ASP VAL LYS GLY THR GLY GLY GLU SER ARG ASP LEU PRO          
SEQRES  18 G  362  SER GLY GLN GLY ILE ASN ASN LEU ASP ASN LEU ARG ASP          
SEQRES  19 G  362  TYR LEU ASP GLY SER VAL LYS VAL ASN LEU GLU LYS LYS          
SEQRES  20 G  362  HIS LEU ASN LYS ARG THR GLN ILE PHE PRO PRO GLY ILE          
SEQRES  21 G  362  VAL THR MET ASN GLU TYR SER VAL PRO LYS THR LEU GLN          
SEQRES  22 G  362  ALA ARG PHE VAL LYS GLN ILE ASP PHE ARG PRO LYS ASP          
SEQRES  23 G  362  TYR LEU LYS HIS CYS LEU GLU ARG SER GLU PHE LEU LEU          
SEQRES  24 G  362  GLU LYS ARG ILE ILE GLN SER GLY ILE ALA LEU LEU LEU          
SEQRES  25 G  362  MET LEU ILE TRP TYR ARG PRO VAL ALA GLU PHE ALA GLN          
SEQRES  26 G  362  SER ILE GLN SER ARG ILE VAL GLU TRP LYS GLU ARG LEU          
SEQRES  27 G  362  ASP LYS GLU PHE SER LEU SER VAL TYR GLN LYS MET LYS          
SEQRES  28 G  362  PHE ASN VAL ALA MET GLY ILE GLY VAL LEU ASP                  
SEQRES   1 H  362  LYS GLN VAL SER TRP LYS LEU VAL THR GLU TYR ALA MET          
SEQRES   2 H  362  GLU THR LYS CYS ASP ASP VAL LEU LEU LEU LEU GLY MET          
SEQRES   3 H  362  TYR LEU GLU PHE GLN TYR SER PHE GLU MET CYS LEU LYS          
SEQRES   4 H  362  CYS ILE LYS LYS GLU GLN PRO SER HIS TYR LYS TYR HIS          
SEQRES   5 H  362  GLU LYS HIS TYR ALA ASN ALA ALA ILE PHE ALA ASP SER          
SEQRES   6 H  362  LYS ASN GLN LYS THR ILE CYS GLN GLN ALA VAL ASP THR          
SEQRES   7 H  362  VAL LEU ALA LYS LYS ARG VAL ASP SER LEU GLN LEU THR          
SEQRES   8 H  362  ARG GLU GLN MET LEU THR ASN ARG PHE ASN ASP LEU LEU          
SEQRES   9 H  362  ASP ARG MET ASP ILE MET PHE GLY SER THR GLY SER ALA          
SEQRES  10 H  362  ASP ILE GLU GLU TRP MET ALA GLY VAL ALA TRP LEU HIS          
SEQRES  11 H  362  CYS LEU LEU PRO LYS MET ASP SER VAL VAL TYR ASP PHE          
SEQRES  12 H  362  LEU LYS CYS MET VAL TYR ASN ILE PRO LYS LYS ARG TYR          
SEQRES  13 H  362  TRP LEU PHE LYS GLY PRO ILE ASP SER GLY LYS THR THR          
SEQRES  14 H  362  LEU ALA ALA ALA LEU LEU GLU LEU CYS GLY GLY LYS ALA          
SEQRES  15 H  362  LEU ASN VAL ASN LEU PRO LEU ASP ARG LEU ASN PHE GLU          
SEQRES  16 H  362  LEU GLY VAL ALA ILE ASP GLN PHE LEU VAL VAL PHE GLU          
SEQRES  17 H  362  ASP VAL LYS GLY THR GLY GLY GLU SER ARG ASP LEU PRO          
SEQRES  18 H  362  SER GLY GLN GLY ILE ASN ASN LEU ASP ASN LEU ARG ASP          
SEQRES  19 H  362  TYR LEU ASP GLY SER VAL LYS VAL ASN LEU GLU LYS LYS          
SEQRES  20 H  362  HIS LEU ASN LYS ARG THR GLN ILE PHE PRO PRO GLY ILE          
SEQRES  21 H  362  VAL THR MET ASN GLU TYR SER VAL PRO LYS THR LEU GLN          
SEQRES  22 H  362  ALA ARG PHE VAL LYS GLN ILE ASP PHE ARG PRO LYS ASP          
SEQRES  23 H  362  TYR LEU LYS HIS CYS LEU GLU ARG SER GLU PHE LEU LEU          
SEQRES  24 H  362  GLU LYS ARG ILE ILE GLN SER GLY ILE ALA LEU LEU LEU          
SEQRES  25 H  362  MET LEU ILE TRP TYR ARG PRO VAL ALA GLU PHE ALA GLN          
SEQRES  26 H  362  SER ILE GLN SER ARG ILE VAL GLU TRP LYS GLU ARG LEU          
SEQRES  27 H  362  ASP LYS GLU PHE SER LEU SER VAL TYR GLN LYS MET LYS          
SEQRES  28 H  362  PHE ASN VAL ALA MET GLY ILE GLY VAL LEU ASP                  
SEQRES   1 I  362  LYS GLN VAL SER TRP LYS LEU VAL THR GLU TYR ALA MET          
SEQRES   2 I  362  GLU THR LYS CYS ASP ASP VAL LEU LEU LEU LEU GLY MET          
SEQRES   3 I  362  TYR LEU GLU PHE GLN TYR SER PHE GLU MET CYS LEU LYS          
SEQRES   4 I  362  CYS ILE LYS LYS GLU GLN PRO SER HIS TYR LYS TYR HIS          
SEQRES   5 I  362  GLU LYS HIS TYR ALA ASN ALA ALA ILE PHE ALA ASP SER          
SEQRES   6 I  362  LYS ASN GLN LYS THR ILE CYS GLN GLN ALA VAL ASP THR          
SEQRES   7 I  362  VAL LEU ALA LYS LYS ARG VAL ASP SER LEU GLN LEU THR          
SEQRES   8 I  362  ARG GLU GLN MET LEU THR ASN ARG PHE ASN ASP LEU LEU          
SEQRES   9 I  362  ASP ARG MET ASP ILE MET PHE GLY SER THR GLY SER ALA          
SEQRES  10 I  362  ASP ILE GLU GLU TRP MET ALA GLY VAL ALA TRP LEU HIS          
SEQRES  11 I  362  CYS LEU LEU PRO LYS MET ASP SER VAL VAL TYR ASP PHE          
SEQRES  12 I  362  LEU LYS CYS MET VAL TYR ASN ILE PRO LYS LYS ARG TYR          
SEQRES  13 I  362  TRP LEU PHE LYS GLY PRO ILE ASP SER GLY LYS THR THR          
SEQRES  14 I  362  LEU ALA ALA ALA LEU LEU GLU LEU CYS GLY GLY LYS ALA          
SEQRES  15 I  362  LEU ASN VAL ASN LEU PRO LEU ASP ARG LEU ASN PHE GLU          
SEQRES  16 I  362  LEU GLY VAL ALA ILE ASP GLN PHE LEU VAL VAL PHE GLU          
SEQRES  17 I  362  ASP VAL LYS GLY THR GLY GLY GLU SER ARG ASP LEU PRO          
SEQRES  18 I  362  SER GLY GLN GLY ILE ASN ASN LEU ASP ASN LEU ARG ASP          
SEQRES  19 I  362  TYR LEU ASP GLY SER VAL LYS VAL ASN LEU GLU LYS LYS          
SEQRES  20 I  362  HIS LEU ASN LYS ARG THR GLN ILE PHE PRO PRO GLY ILE          
SEQRES  21 I  362  VAL THR MET ASN GLU TYR SER VAL PRO LYS THR LEU GLN          
SEQRES  22 I  362  ALA ARG PHE VAL LYS GLN ILE ASP PHE ARG PRO LYS ASP          
SEQRES  23 I  362  TYR LEU LYS HIS CYS LEU GLU ARG SER GLU PHE LEU LEU          
SEQRES  24 I  362  GLU LYS ARG ILE ILE GLN SER GLY ILE ALA LEU LEU LEU          
SEQRES  25 I  362  MET LEU ILE TRP TYR ARG PRO VAL ALA GLU PHE ALA GLN          
SEQRES  26 I  362  SER ILE GLN SER ARG ILE VAL GLU TRP LYS GLU ARG LEU          
SEQRES  27 I  362  ASP LYS GLU PHE SER LEU SER VAL TYR GLN LYS MET LYS          
SEQRES  28 I  362  PHE ASN VAL ALA MET GLY ILE GLY VAL LEU ASP                  
SEQRES   1 J  362  LYS GLN VAL SER TRP LYS LEU VAL THR GLU TYR ALA MET          
SEQRES   2 J  362  GLU THR LYS CYS ASP ASP VAL LEU LEU LEU LEU GLY MET          
SEQRES   3 J  362  TYR LEU GLU PHE GLN TYR SER PHE GLU MET CYS LEU LYS          
SEQRES   4 J  362  CYS ILE LYS LYS GLU GLN PRO SER HIS TYR LYS TYR HIS          
SEQRES   5 J  362  GLU LYS HIS TYR ALA ASN ALA ALA ILE PHE ALA ASP SER          
SEQRES   6 J  362  LYS ASN GLN LYS THR ILE CYS GLN GLN ALA VAL ASP THR          
SEQRES   7 J  362  VAL LEU ALA LYS LYS ARG VAL ASP SER LEU GLN LEU THR          
SEQRES   8 J  362  ARG GLU GLN MET LEU THR ASN ARG PHE ASN ASP LEU LEU          
SEQRES   9 J  362  ASP ARG MET ASP ILE MET PHE GLY SER THR GLY SER ALA          
SEQRES  10 J  362  ASP ILE GLU GLU TRP MET ALA GLY VAL ALA TRP LEU HIS          
SEQRES  11 J  362  CYS LEU LEU PRO LYS MET ASP SER VAL VAL TYR ASP PHE          
SEQRES  12 J  362  LEU LYS CYS MET VAL TYR ASN ILE PRO LYS LYS ARG TYR          
SEQRES  13 J  362  TRP LEU PHE LYS GLY PRO ILE ASP SER GLY LYS THR THR          
SEQRES  14 J  362  LEU ALA ALA ALA LEU LEU GLU LEU CYS GLY GLY LYS ALA          
SEQRES  15 J  362  LEU ASN VAL ASN LEU PRO LEU ASP ARG LEU ASN PHE GLU          
SEQRES  16 J  362  LEU GLY VAL ALA ILE ASP GLN PHE LEU VAL VAL PHE GLU          
SEQRES  17 J  362  ASP VAL LYS GLY THR GLY GLY GLU SER ARG ASP LEU PRO          
SEQRES  18 J  362  SER GLY GLN GLY ILE ASN ASN LEU ASP ASN LEU ARG ASP          
SEQRES  19 J  362  TYR LEU ASP GLY SER VAL LYS VAL ASN LEU GLU LYS LYS          
SEQRES  20 J  362  HIS LEU ASN LYS ARG THR GLN ILE PHE PRO PRO GLY ILE          
SEQRES  21 J  362  VAL THR MET ASN GLU TYR SER VAL PRO LYS THR LEU GLN          
SEQRES  22 J  362  ALA ARG PHE VAL LYS GLN ILE ASP PHE ARG PRO LYS ASP          
SEQRES  23 J  362  TYR LEU LYS HIS CYS LEU GLU ARG SER GLU PHE LEU LEU          
SEQRES  24 J  362  GLU LYS ARG ILE ILE GLN SER GLY ILE ALA LEU LEU LEU          
SEQRES  25 J  362  MET LEU ILE TRP TYR ARG PRO VAL ALA GLU PHE ALA GLN          
SEQRES  26 J  362  SER ILE GLN SER ARG ILE VAL GLU TRP LYS GLU ARG LEU          
SEQRES  27 J  362  ASP LYS GLU PHE SER LEU SER VAL TYR GLN LYS MET LYS          
SEQRES  28 J  362  PHE ASN VAL ALA MET GLY ILE GLY VAL LEU ASP                  
SEQRES   1 K  362  LYS GLN VAL SER TRP LYS LEU VAL THR GLU TYR ALA MET          
SEQRES   2 K  362  GLU THR LYS CYS ASP ASP VAL LEU LEU LEU LEU GLY MET          
SEQRES   3 K  362  TYR LEU GLU PHE GLN TYR SER PHE GLU MET CYS LEU LYS          
SEQRES   4 K  362  CYS ILE LYS LYS GLU GLN PRO SER HIS TYR LYS TYR HIS          
SEQRES   5 K  362  GLU LYS HIS TYR ALA ASN ALA ALA ILE PHE ALA ASP SER          
SEQRES   6 K  362  LYS ASN GLN LYS THR ILE CYS GLN GLN ALA VAL ASP THR          
SEQRES   7 K  362  VAL LEU ALA LYS LYS ARG VAL ASP SER LEU GLN LEU THR          
SEQRES   8 K  362  ARG GLU GLN MET LEU THR ASN ARG PHE ASN ASP LEU LEU          
SEQRES   9 K  362  ASP ARG MET ASP ILE MET PHE GLY SER THR GLY SER ALA          
SEQRES  10 K  362  ASP ILE GLU GLU TRP MET ALA GLY VAL ALA TRP LEU HIS          
SEQRES  11 K  362  CYS LEU LEU PRO LYS MET ASP SER VAL VAL TYR ASP PHE          
SEQRES  12 K  362  LEU LYS CYS MET VAL TYR ASN ILE PRO LYS LYS ARG TYR          
SEQRES  13 K  362  TRP LEU PHE LYS GLY PRO ILE ASP SER GLY LYS THR THR          
SEQRES  14 K  362  LEU ALA ALA ALA LEU LEU GLU LEU CYS GLY GLY LYS ALA          
SEQRES  15 K  362  LEU ASN VAL ASN LEU PRO LEU ASP ARG LEU ASN PHE GLU          
SEQRES  16 K  362  LEU GLY VAL ALA ILE ASP GLN PHE LEU VAL VAL PHE GLU          
SEQRES  17 K  362  ASP VAL LYS GLY THR GLY GLY GLU SER ARG ASP LEU PRO          
SEQRES  18 K  362  SER GLY GLN GLY ILE ASN ASN LEU ASP ASN LEU ARG ASP          
SEQRES  19 K  362  TYR LEU ASP GLY SER VAL LYS VAL ASN LEU GLU LYS LYS          
SEQRES  20 K  362  HIS LEU ASN LYS ARG THR GLN ILE PHE PRO PRO GLY ILE          
SEQRES  21 K  362  VAL THR MET ASN GLU TYR SER VAL PRO LYS THR LEU GLN          
SEQRES  22 K  362  ALA ARG PHE VAL LYS GLN ILE ASP PHE ARG PRO LYS ASP          
SEQRES  23 K  362  TYR LEU LYS HIS CYS LEU GLU ARG SER GLU PHE LEU LEU          
SEQRES  24 K  362  GLU LYS ARG ILE ILE GLN SER GLY ILE ALA LEU LEU LEU          
SEQRES  25 K  362  MET LEU ILE TRP TYR ARG PRO VAL ALA GLU PHE ALA GLN          
SEQRES  26 K  362  SER ILE GLN SER ARG ILE VAL GLU TRP LYS GLU ARG LEU          
SEQRES  27 K  362  ASP LYS GLU PHE SER LEU SER VAL TYR GLN LYS MET LYS          
SEQRES  28 K  362  PHE ASN VAL ALA MET GLY ILE GLY VAL LEU ASP                  
SEQRES   1 L  362  LYS GLN VAL SER TRP LYS LEU VAL THR GLU TYR ALA MET          
SEQRES   2 L  362  GLU THR LYS CYS ASP ASP VAL LEU LEU LEU LEU GLY MET          
SEQRES   3 L  362  TYR LEU GLU PHE GLN TYR SER PHE GLU MET CYS LEU LYS          
SEQRES   4 L  362  CYS ILE LYS LYS GLU GLN PRO SER HIS TYR LYS TYR HIS          
SEQRES   5 L  362  GLU LYS HIS TYR ALA ASN ALA ALA ILE PHE ALA ASP SER          
SEQRES   6 L  362  LYS ASN GLN LYS THR ILE CYS GLN GLN ALA VAL ASP THR          
SEQRES   7 L  362  VAL LEU ALA LYS LYS ARG VAL ASP SER LEU GLN LEU THR          
SEQRES   8 L  362  ARG GLU GLN MET LEU THR ASN ARG PHE ASN ASP LEU LEU          
SEQRES   9 L  362  ASP ARG MET ASP ILE MET PHE GLY SER THR GLY SER ALA          
SEQRES  10 L  362  ASP ILE GLU GLU TRP MET ALA GLY VAL ALA TRP LEU HIS          
SEQRES  11 L  362  CYS LEU LEU PRO LYS MET ASP SER VAL VAL TYR ASP PHE          
SEQRES  12 L  362  LEU LYS CYS MET VAL TYR ASN ILE PRO LYS LYS ARG TYR          
SEQRES  13 L  362  TRP LEU PHE LYS GLY PRO ILE ASP SER GLY LYS THR THR          
SEQRES  14 L  362  LEU ALA ALA ALA LEU LEU GLU LEU CYS GLY GLY LYS ALA          
SEQRES  15 L  362  LEU ASN VAL ASN LEU PRO LEU ASP ARG LEU ASN PHE GLU          
SEQRES  16 L  362  LEU GLY VAL ALA ILE ASP GLN PHE LEU VAL VAL PHE GLU          
SEQRES  17 L  362  ASP VAL LYS GLY THR GLY GLY GLU SER ARG ASP LEU PRO          
SEQRES  18 L  362  SER GLY GLN GLY ILE ASN ASN LEU ASP ASN LEU ARG ASP          
SEQRES  19 L  362  TYR LEU ASP GLY SER VAL LYS VAL ASN LEU GLU LYS LYS          
SEQRES  20 L  362  HIS LEU ASN LYS ARG THR GLN ILE PHE PRO PRO GLY ILE          
SEQRES  21 L  362  VAL THR MET ASN GLU TYR SER VAL PRO LYS THR LEU GLN          
SEQRES  22 L  362  ALA ARG PHE VAL LYS GLN ILE ASP PHE ARG PRO LYS ASP          
SEQRES  23 L  362  TYR LEU LYS HIS CYS LEU GLU ARG SER GLU PHE LEU LEU          
SEQRES  24 L  362  GLU LYS ARG ILE ILE GLN SER GLY ILE ALA LEU LEU LEU          
SEQRES  25 L  362  MET LEU ILE TRP TYR ARG PRO VAL ALA GLU PHE ALA GLN          
SEQRES  26 L  362  SER ILE GLN SER ARG ILE VAL GLU TRP LYS GLU ARG LEU          
SEQRES  27 L  362  ASP LYS GLU PHE SER LEU SER VAL TYR GLN LYS MET LYS          
SEQRES  28 L  362  PHE ASN VAL ALA MET GLY ILE GLY VAL LEU ASP                  
SEQRES   1 2   78  MET SER ALA SER ALA GLN GLN LEU ALA GLU GLU LEU GLN          
SEQRES   2 2   78  ILE PHE GLY LEU ASP CYS GLU GLU ALA LEU ILE GLU LYS          
SEQRES   3 2   78  LEU VAL GLU LEU CYS VAL GLN TYR GLY GLN ASN GLU GLU          
SEQRES   4 2   78  GLY MET VAL GLY GLU LEU ILE ALA PHE CYS THR SER THR          
SEQRES   5 2   78  HIS LYS VAL GLY LEU THR SER GLU ILE LEU ASN SER PHE          
SEQRES   6 2   78  GLU HIS GLU PHE LEU SER LYS ARG LEU SER LYS ALA ARG          
SEQRES   1 3   78  MET SER ALA SER ALA GLN GLN LEU ALA GLU GLU LEU GLN          
SEQRES   2 3   78  ILE PHE GLY LEU ASP CYS GLU GLU ALA LEU ILE GLU LYS          
SEQRES   3 3   78  LEU VAL GLU LEU CYS VAL GLN TYR GLY GLN ASN GLU GLU          
SEQRES   4 3   78  GLY MET VAL GLY GLU LEU ILE ALA PHE CYS THR SER THR          
SEQRES   5 3   78  HIS LYS VAL GLY LEU THR SER GLU ILE LEU ASN SER PHE          
SEQRES   6 3   78  GLU HIS GLU PHE LEU SER LYS ARG LEU SER LYS ALA ARG          
SEQRES   1 6   78  MET SER ALA SER ALA GLN GLN LEU ALA GLU GLU LEU GLN          
SEQRES   2 6   78  ILE PHE GLY LEU ASP CYS GLU GLU ALA LEU ILE GLU LYS          
SEQRES   3 6   78  LEU VAL GLU LEU CYS VAL GLN TYR GLY GLN ASN GLU GLU          
SEQRES   4 6   78  GLY MET VAL GLY GLU LEU ILE ALA PHE CYS THR SER THR          
SEQRES   5 6   78  HIS LYS VAL GLY LEU THR SER GLU ILE LEU ASN SER PHE          
SEQRES   6 6   78  GLU HIS GLU PHE LEU SER LYS ARG LEU SER LYS ALA ARG          
SEQRES   1 U   78  MET SER ALA SER ALA GLN GLN LEU ALA GLU GLU LEU GLN          
SEQRES   2 U   78  ILE PHE GLY LEU ASP CYS GLU GLU ALA LEU ILE GLU LYS          
SEQRES   3 U   78  LEU VAL GLU LEU CYS VAL GLN TYR GLY GLN ASN GLU GLU          
SEQRES   4 U   78  GLY MET VAL GLY GLU LEU ILE ALA PHE CYS THR SER THR          
SEQRES   5 U   78  HIS LYS VAL GLY LEU THR SER GLU ILE LEU ASN SER PHE          
SEQRES   6 U   78  GLU HIS GLU PHE LEU SER LYS ARG LEU SER LYS ALA ARG          
SEQRES   1 W   78  MET SER ALA SER ALA GLN GLN LEU ALA GLU GLU LEU GLN          
SEQRES   2 W   78  ILE PHE GLY LEU ASP CYS GLU GLU ALA LEU ILE GLU LYS          
SEQRES   3 W   78  LEU VAL GLU LEU CYS VAL GLN TYR GLY GLN ASN GLU GLU          
SEQRES   4 W   78  GLY MET VAL GLY GLU LEU ILE ALA PHE CYS THR SER THR          
SEQRES   5 W   78  HIS LYS VAL GLY LEU THR SER GLU ILE LEU ASN SER PHE          
SEQRES   6 W   78  GLU HIS GLU PHE LEU SER LYS ARG LEU SER LYS ALA ARG          
SEQRES   1 5   78  MET SER ALA SER ALA GLN GLN LEU ALA GLU GLU LEU GLN          
SEQRES   2 5   78  ILE PHE GLY LEU ASP CYS GLU GLU ALA LEU ILE GLU LYS          
SEQRES   3 5   78  LEU VAL GLU LEU CYS VAL GLN TYR GLY GLN ASN GLU GLU          
SEQRES   4 5   78  GLY MET VAL GLY GLU LEU ILE ALA PHE CYS THR SER THR          
SEQRES   5 5   78  HIS LYS VAL GLY LEU THR SER GLU ILE LEU ASN SER PHE          
SEQRES   6 5   78  GLU HIS GLU PHE LEU SER LYS ARG LEU SER LYS ALA ARG          
SEQRES   1 7   78  MET SER ALA SER ALA GLN GLN LEU ALA GLU GLU LEU GLN          
SEQRES   2 7   78  ILE PHE GLY LEU ASP CYS GLU GLU ALA LEU ILE GLU LYS          
SEQRES   3 7   78  LEU VAL GLU LEU CYS VAL GLN TYR GLY GLN ASN GLU GLU          
SEQRES   4 7   78  GLY MET VAL GLY GLU LEU ILE ALA PHE CYS THR SER THR          
SEQRES   5 7   78  HIS LYS VAL GLY LEU THR SER GLU ILE LEU ASN SER PHE          
SEQRES   6 7   78  GLU HIS GLU PHE LEU SER LYS ARG LEU SER LYS ALA ARG          
SEQRES   1 9   78  MET SER ALA SER ALA GLN GLN LEU ALA GLU GLU LEU GLN          
SEQRES   2 9   78  ILE PHE GLY LEU ASP CYS GLU GLU ALA LEU ILE GLU LYS          
SEQRES   3 9   78  LEU VAL GLU LEU CYS VAL GLN TYR GLY GLN ASN GLU GLU          
SEQRES   4 9   78  GLY MET VAL GLY GLU LEU ILE ALA PHE CYS THR SER THR          
SEQRES   5 9   78  HIS LYS VAL GLY LEU THR SER GLU ILE LEU ASN SER PHE          
SEQRES   6 9   78  GLU HIS GLU PHE LEU SER LYS ARG LEU SER LYS ALA ARG          
SEQRES   1 1   78  MET SER ALA SER ALA GLN GLN LEU ALA GLU GLU LEU GLN          
SEQRES   2 1   78  ILE PHE GLY LEU ASP CYS GLU GLU ALA LEU ILE GLU LYS          
SEQRES   3 1   78  LEU VAL GLU LEU CYS VAL GLN TYR GLY GLN ASN GLU GLU          
SEQRES   4 1   78  GLY MET VAL GLY GLU LEU ILE ALA PHE CYS THR SER THR          
SEQRES   5 1   78  HIS LYS VAL GLY LEU THR SER GLU ILE LEU ASN SER PHE          
SEQRES   6 1   78  GLU HIS GLU PHE LEU SER LYS ARG LEU SER LYS ALA ARG          
SEQRES   1 4   78  MET SER ALA SER ALA GLN GLN LEU ALA GLU GLU LEU GLN          
SEQRES   2 4   78  ILE PHE GLY LEU ASP CYS GLU GLU ALA LEU ILE GLU LYS          
SEQRES   3 4   78  LEU VAL GLU LEU CYS VAL GLN TYR GLY GLN ASN GLU GLU          
SEQRES   4 4   78  GLY MET VAL GLY GLU LEU ILE ALA PHE CYS THR SER THR          
SEQRES   5 4   78  HIS LYS VAL GLY LEU THR SER GLU ILE LEU ASN SER PHE          
SEQRES   6 4   78  GLU HIS GLU PHE LEU SER LYS ARG LEU SER LYS ALA ARG          
SEQRES   1 8   78  MET SER ALA SER ALA GLN GLN LEU ALA GLU GLU LEU GLN          
SEQRES   2 8   78  ILE PHE GLY LEU ASP CYS GLU GLU ALA LEU ILE GLU LYS          
SEQRES   3 8   78  LEU VAL GLU LEU CYS VAL GLN TYR GLY GLN ASN GLU GLU          
SEQRES   4 8   78  GLY MET VAL GLY GLU LEU ILE ALA PHE CYS THR SER THR          
SEQRES   5 8   78  HIS LYS VAL GLY LEU THR SER GLU ILE LEU ASN SER PHE          
SEQRES   6 8   78  GLU HIS GLU PHE LEU SER LYS ARG LEU SER LYS ALA ARG          
HET     ZN  A 700       1                                                       
HET     ZN  B 700       1                                                       
HET     ZN  C 700       1                                                       
HET     ZN  D 700       1                                                       
HET     ZN  E 700       1                                                       
HET     ZN  F 700       1                                                       
HET     ZN  G 700       1                                                       
HET     ZN  H 700       1                                                       
HET     ZN  I 700       1                                                       
HET     ZN  J 700       1                                                       
HET     ZN  K 700       1                                                       
HET     ZN  L 700       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL  24   ZN    12(ZN 2+)                                                    
HELIX    1   1 SER A  269  LYS A  281  1                                  13    
HELIX    2   2 ASP A  284  LEU A  293  1                                  10    
HELIX    3   3 CYS A  302  LYS A  307  1                                   6    
HELIX    4   4 TYR A  316  ALA A  328  1                                  13    
HELIX    5   5 ASN A  332  LEU A  355  1                                  24    
HELIX    6   6 THR A  356  PHE A  376  1                                  21    
HELIX    7   7 ASP A  383  CYS A  396  1                                  14    
HELIX    8   8 LYS A  400  ASN A  415  1                                  16    
HELIX    9   9 GLY A  431  GLY A  444  1                                  14    
HELIX   10  10 ARG A  456  GLY A  462  1                                   7    
HELIX   11  11 GLN A  489  ASN A  496  1                                   8    
HELIX   12  12 LEU A  497  GLY A  503  1                                   7    
HELIX   13  13 PRO A  534  ALA A  539  1                                   6    
HELIX   14  14 LYS A  550  GLU A  558  1                                   9    
HELIX   15  15 SER A  560  LYS A  566  1                                   7    
HELIX   16  16 SER A  571  TYR A  582  1                                  12    
HELIX   17  17 PRO A  584  PHE A  588  5                                   5    
HELIX   18  18 ILE A  592  PHE A  607  1                                  16    
HELIX   19  19 SER A  608  GLY A  622  1                                  15    
HELIX   20  20 SER B  269  LYS B  281  1                                  13    
HELIX   21  21 ASP B  284  LEU B  293  1                                  10    
HELIX   22  22 CYS B  302  LYS B  307  1                                   6    
HELIX   23  23 TYR B  316  ALA B  328  1                                  13    
HELIX   24  24 ASN B  332  LEU B  355  1                                  24    
HELIX   25  25 THR B  356  PHE B  376  1                                  21    
HELIX   26  26 ASP B  383  CYS B  396  1                                  14    
HELIX   27  27 LYS B  400  ASN B  415  1                                  16    
HELIX   28  28 GLY B  431  GLY B  444  1                                  14    
HELIX   29  29 ARG B  456  GLY B  462  1                                   7    
HELIX   30  30 GLN B  489  ASN B  496  1                                   8    
HELIX   31  31 LEU B  497  GLY B  503  1                                   7    
HELIX   32  32 PRO B  534  ALA B  539  1                                   6    
HELIX   33  33 LYS B  550  GLU B  558  1                                   9    
HELIX   34  34 SER B  560  LYS B  566  1                                   7    
HELIX   35  35 SER B  571  TYR B  582  1                                  12    
HELIX   36  36 PRO B  584  PHE B  588  5                                   5    
HELIX   37  37 ILE B  592  PHE B  607  1                                  16    
HELIX   38  38 SER B  608  GLY B  622  1                                  15    
HELIX   39  39 SER C  269  LYS C  281  1                                  13    
HELIX   40  40 ASP C  284  LEU C  293  1                                  10    
HELIX   41  41 CYS C  302  LYS C  307  1                                   6    
HELIX   42  42 TYR C  316  ALA C  328  1                                  13    
HELIX   43  43 ASN C  332  LEU C  355  1                                  24    
HELIX   44  44 THR C  356  PHE C  376  1                                  21    
HELIX   45  45 ASP C  383  CYS C  396  1                                  14    
HELIX   46  46 LYS C  400  ASN C  415  1                                  16    
HELIX   47  47 GLY C  431  GLY C  444  1                                  14    
HELIX   48  48 ARG C  456  GLY C  462  1                                   7    
HELIX   49  49 GLN C  489  ASN C  496  1                                   8    
HELIX   50  50 LEU C  497  GLY C  503  1                                   7    
HELIX   51  51 PRO C  534  ALA C  539  1                                   6    
HELIX   52  52 LYS C  550  GLU C  558  1                                   9    
HELIX   53  53 SER C  560  LYS C  566  1                                   7    
HELIX   54  54 SER C  571  TYR C  582  1                                  12    
HELIX   55  55 PRO C  584  PHE C  588  5                                   5    
HELIX   56  56 ILE C  592  PHE C  607  1                                  16    
HELIX   57  57 SER C  608  GLY C  622  1                                  15    
HELIX   58  58 SER D  269  LYS D  281  1                                  13    
HELIX   59  59 ASP D  284  LEU D  293  1                                  10    
HELIX   60  60 CYS D  302  LYS D  307  1                                   6    
HELIX   61  61 TYR D  316  ALA D  328  1                                  13    
HELIX   62  62 ASN D  332  LEU D  355  1                                  24    
HELIX   63  63 THR D  356  PHE D  376  1                                  21    
HELIX   64  64 ASP D  383  CYS D  396  1                                  14    
HELIX   65  65 LYS D  400  ASN D  415  1                                  16    
HELIX   66  66 GLY D  431  GLY D  444  1                                  14    
HELIX   67  67 ARG D  456  GLY D  462  1                                   7    
HELIX   68  68 GLN D  489  ASN D  496  1                                   8    
HELIX   69  69 LEU D  497  GLY D  503  1                                   7    
HELIX   70  70 PRO D  534  ALA D  539  1                                   6    
HELIX   71  71 LYS D  550  GLU D  558  1                                   9    
HELIX   72  72 SER D  560  LYS D  566  1                                   7    
HELIX   73  73 SER D  571  TYR D  582  1                                  12    
HELIX   74  74 PRO D  584  PHE D  588  5                                   5    
HELIX   75  75 ILE D  592  PHE D  607  1                                  16    
HELIX   76  76 SER D  608  GLY D  622  1                                  15    
HELIX   77  77 SER E  269  LYS E  281  1                                  13    
HELIX   78  78 ASP E  284  LEU E  293  1                                  10    
HELIX   79  79 CYS E  302  LYS E  307  1                                   6    
HELIX   80  80 TYR E  316  ALA E  328  1                                  13    
HELIX   81  81 ASN E  332  LEU E  355  1                                  24    
HELIX   82  82 THR E  356  PHE E  376  1                                  21    
HELIX   83  83 ASP E  383  CYS E  396  1                                  14    
HELIX   84  84 LYS E  400  ASN E  415  1                                  16    
HELIX   85  85 GLY E  431  GLY E  444  1                                  14    
HELIX   86  86 ARG E  456  GLY E  462  1                                   7    
HELIX   87  87 GLN E  489  ASN E  496  1                                   8    
HELIX   88  88 LEU E  497  GLY E  503  1                                   7    
HELIX   89  89 PRO E  534  ALA E  539  1                                   6    
HELIX   90  90 LYS E  550  GLU E  558  1                                   9    
HELIX   91  91 SER E  560  LYS E  566  1                                   7    
HELIX   92  92 SER E  571  TYR E  582  1                                  12    
HELIX   93  93 PRO E  584  PHE E  588  5                                   5    
HELIX   94  94 ILE E  592  PHE E  607  1                                  16    
HELIX   95  95 SER E  608  GLY E  622  1                                  15    
HELIX   96  96 SER F  269  LYS F  281  1                                  13    
HELIX   97  97 ASP F  284  LEU F  293  1                                  10    
HELIX   98  98 CYS F  302  LYS F  307  1                                   6    
HELIX   99  99 TYR F  316  ALA F  328  1                                  13    
HELIX  100 100 ASN F  332  LEU F  355  1                                  24    
HELIX  101 101 THR F  356  PHE F  376  1                                  21    
HELIX  102 102 ASP F  383  CYS F  396  1                                  14    
HELIX  103 103 LYS F  400  ASN F  415  1                                  16    
HELIX  104 104 GLY F  431  GLY F  444  1                                  14    
HELIX  105 105 ARG F  456  GLY F  462  1                                   7    
HELIX  106 106 GLN F  489  ASN F  496  1                                   8    
HELIX  107 107 LEU F  497  GLY F  503  1                                   7    
HELIX  108 108 PRO F  534  ALA F  539  1                                   6    
HELIX  109 109 LYS F  550  GLU F  558  1                                   9    
HELIX  110 110 SER F  560  LYS F  566  1                                   7    
HELIX  111 111 SER F  571  TYR F  582  1                                  12    
HELIX  112 112 PRO F  584  PHE F  588  5                                   5    
HELIX  113 113 ILE F  592  PHE F  607  1                                  16    
HELIX  114 114 SER F  608  GLY F  622  1                                  15    
HELIX  115 115 SER G  269  LYS G  281  1                                  13    
HELIX  116 116 ASP G  284  LEU G  293  1                                  10    
HELIX  117 117 CYS G  302  LYS G  307  1                                   6    
HELIX  118 118 TYR G  316  ALA G  328  1                                  13    
HELIX  119 119 ASN G  332  LEU G  355  1                                  24    
HELIX  120 120 THR G  356  PHE G  376  1                                  21    
HELIX  121 121 ASP G  383  CYS G  396  1                                  14    
HELIX  122 122 LYS G  400  ASN G  415  1                                  16    
HELIX  123 123 GLY G  431  GLY G  444  1                                  14    
HELIX  124 124 ARG G  456  GLY G  462  1                                   7    
HELIX  125 125 GLN G  489  ASN G  496  1                                   8    
HELIX  126 126 LEU G  497  GLY G  503  1                                   7    
HELIX  127 127 PRO G  534  ALA G  539  1                                   6    
HELIX  128 128 LYS G  550  GLU G  558  1                                   9    
HELIX  129 129 SER G  560  LYS G  566  1                                   7    
HELIX  130 130 SER G  571  TYR G  582  1                                  12    
HELIX  131 131 PRO G  584  PHE G  588  5                                   5    
HELIX  132 132 ILE G  592  PHE G  607  1                                  16    
HELIX  133 133 SER G  608  GLY G  622  1                                  15    
HELIX  134 134 SER H  269  LYS H  281  1                                  13    
HELIX  135 135 ASP H  284  LEU H  293  1                                  10    
HELIX  136 136 CYS H  302  LYS H  307  1                                   6    
HELIX  137 137 TYR H  316  ALA H  328  1                                  13    
HELIX  138 138 ASN H  332  LEU H  355  1                                  24    
HELIX  139 139 THR H  356  PHE H  376  1                                  21    
HELIX  140 140 ASP H  383  CYS H  396  1                                  14    
HELIX  141 141 LYS H  400  ASN H  415  1                                  16    
HELIX  142 142 GLY H  431  GLY H  444  1                                  14    
HELIX  143 143 ARG H  456  GLY H  462  1                                   7    
HELIX  144 144 GLN H  489  ASN H  496  1                                   8    
HELIX  145 145 LEU H  497  GLY H  503  1                                   7    
HELIX  146 146 PRO H  534  ALA H  539  1                                   6    
HELIX  147 147 LYS H  550  GLU H  558  1                                   9    
HELIX  148 148 SER H  560  LYS H  566  1                                   7    
HELIX  149 149 SER H  571  TYR H  582  1                                  12    
HELIX  150 150 PRO H  584  PHE H  588  5                                   5    
HELIX  151 151 ILE H  592  PHE H  607  1                                  16    
HELIX  152 152 SER H  608  GLY H  622  1                                  15    
HELIX  153 153 SER I  269  LYS I  281  1                                  13    
HELIX  154 154 ASP I  284  LEU I  293  1                                  10    
HELIX  155 155 CYS I  302  LYS I  307  1                                   6    
HELIX  156 156 TYR I  316  ALA I  328  1                                  13    
HELIX  157 157 ASN I  332  LEU I  355  1                                  24    
HELIX  158 158 THR I  356  PHE I  376  1                                  21    
HELIX  159 159 ASP I  383  CYS I  396  1                                  14    
HELIX  160 160 LYS I  400  ASN I  415  1                                  16    
HELIX  161 161 GLY I  431  GLY I  444  1                                  14    
HELIX  162 162 ARG I  456  GLY I  462  1                                   7    
HELIX  163 163 GLN I  489  ASN I  496  1                                   8    
HELIX  164 164 LEU I  497  GLY I  503  1                                   7    
HELIX  165 165 PRO I  534  ALA I  539  1                                   6    
HELIX  166 166 LYS I  550  GLU I  558  1                                   9    
HELIX  167 167 SER I  560  LYS I  566  1                                   7    
HELIX  168 168 SER I  571  TYR I  582  1                                  12    
HELIX  169 169 PRO I  584  PHE I  588  5                                   5    
HELIX  170 170 ILE I  592  PHE I  607  1                                  16    
HELIX  171 171 SER I  608  GLY I  622  1                                  15    
HELIX  172 172 SER J  269  LYS J  281  1                                  13    
HELIX  173 173 ASP J  284  LEU J  293  1                                  10    
HELIX  174 174 CYS J  302  LYS J  307  1                                   6    
HELIX  175 175 TYR J  316  ALA J  328  1                                  13    
HELIX  176 176 ASN J  332  LEU J  355  1                                  24    
HELIX  177 177 THR J  356  PHE J  376  1                                  21    
HELIX  178 178 ASP J  383  CYS J  396  1                                  14    
HELIX  179 179 LYS J  400  ASN J  415  1                                  16    
HELIX  180 180 GLY J  431  GLY J  444  1                                  14    
HELIX  181 181 ARG J  456  GLY J  462  1                                   7    
HELIX  182 182 GLN J  489  ASN J  496  1                                   8    
HELIX  183 183 LEU J  497  GLY J  503  1                                   7    
HELIX  184 184 PRO J  534  ALA J  539  1                                   6    
HELIX  185 185 LYS J  550  GLU J  558  1                                   9    
HELIX  186 186 SER J  560  LYS J  566  1                                   7    
HELIX  187 187 SER J  571  TYR J  582  1                                  12    
HELIX  188 188 PRO J  584  PHE J  588  5                                   5    
HELIX  189 189 ILE J  592  PHE J  607  1                                  16    
HELIX  190 190 SER J  608  GLY J  622  1                                  15    
HELIX  191 191 SER K  269  LYS K  281  1                                  13    
HELIX  192 192 ASP K  284  LEU K  293  1                                  10    
HELIX  193 193 CYS K  302  LYS K  307  1                                   6    
HELIX  194 194 TYR K  316  ALA K  328  1                                  13    
HELIX  195 195 ASN K  332  LEU K  355  1                                  24    
HELIX  196 196 THR K  356  PHE K  376  1                                  21    
HELIX  197 197 ASP K  383  CYS K  396  1                                  14    
HELIX  198 198 LYS K  400  ASN K  415  1                                  16    
HELIX  199 199 GLY K  431  GLY K  444  1                                  14    
HELIX  200 200 ARG K  456  GLY K  462  1                                   7    
HELIX  201 201 GLN K  489  ASN K  496  1                                   8    
HELIX  202 202 LEU K  497  GLY K  503  1                                   7    
HELIX  203 203 PRO K  534  ALA K  539  1                                   6    
HELIX  204 204 LYS K  550  GLU K  558  1                                   9    
HELIX  205 205 SER K  560  LYS K  566  1                                   7    
HELIX  206 206 SER K  571  TYR K  582  1                                  12    
HELIX  207 207 PRO K  584  PHE K  588  5                                   5    
HELIX  208 208 ILE K  592  PHE K  607  1                                  16    
HELIX  209 209 SER K  608  GLY K  622  1                                  15    
HELIX  210 210 SER L  269  LYS L  281  1                                  13    
HELIX  211 211 ASP L  284  LEU L  293  1                                  10    
HELIX  212 212 CYS L  302  LYS L  307  1                                   6    
HELIX  213 213 TYR L  316  ALA L  328  1                                  13    
HELIX  214 214 ASN L  332  LEU L  355  1                                  24    
HELIX  215 215 THR L  356  PHE L  376  1                                  21    
HELIX  216 216 ASP L  383  CYS L  396  1                                  14    
HELIX  217 217 LYS L  400  ASN L  415  1                                  16    
HELIX  218 218 GLY L  431  GLY L  444  1                                  14    
HELIX  219 219 ARG L  456  GLY L  462  1                                   7    
HELIX  220 220 GLN L  489  ASN L  496  1                                   8    
HELIX  221 221 LEU L  497  GLY L  503  1                                   7    
HELIX  222 222 PRO L  534  ALA L  539  1                                   6    
HELIX  223 223 LYS L  550  GLU L  558  1                                   9    
HELIX  224 224 SER L  560  LYS L  566  1                                   7    
HELIX  225 225 SER L  571  TYR L  582  1                                  12    
HELIX  226 226 PRO L  584  PHE L  588  5                                   5    
HELIX  227 227 ILE L  592  PHE L  607  1                                  16    
HELIX  228 228 SER L  608  GLY L  622  1                                  15    
HELIX  229 229 SER 2    4  PHE 2   15  1                                  12    
HELIX  230 230 GLU 2   20  GLU 2   29  1                                  10    
HELIX  231 231 GLU 2   29  TYR 2   34  1                                   6    
HELIX  232 232 ASN 2   37  ILE 2   46  1                                  10    
HELIX  233 233 ALA 2   47  THR 2   52  1                                   6    
HELIX  234 234 ASN 2   63  HIS 2   67  5                                   5    
HELIX  235 235 LEU 2   70  LEU 2   74  5                                   5    
HELIX  236 236 SER 3    4  PHE 3   15  1                                  12    
HELIX  237 237 GLU 3   20  TYR 3   34  1                                  15    
HELIX  238 238 ASN 3   37  ILE 3   46  1                                  10    
HELIX  239 239 ALA 3   47  THR 3   52  1                                   6    
HELIX  240 240 ASN 3   63  HIS 3   67  5                                   5    
HELIX  241 241 LEU 3   70  LEU 3   74  5                                   5    
HELIX  242 242 SER 6    4  PHE 6   15  1                                  12    
HELIX  243 243 GLU 6   20  GLU 6   29  1                                  10    
HELIX  244 244 GLU 6   29  TYR 6   34  1                                   6    
HELIX  245 245 ASN 6   37  ILE 6   46  1                                  10    
HELIX  246 246 ALA 6   47  THR 6   52  1                                   6    
HELIX  247 247 ASN 6   63  HIS 6   67  5                                   5    
HELIX  248 248 LEU 6   70  LEU 6   74  5                                   5    
HELIX  249 249 SER U    4  PHE U   15  1                                  12    
HELIX  250 250 GLU U   20  GLU U   29  1                                  10    
HELIX  251 251 GLU U   29  TYR U   34  1                                   6    
HELIX  252 252 ASN U   37  ILE U   46  1                                  10    
HELIX  253 253 ALA U   47  THR U   52  1                                   6    
HELIX  254 254 ASN U   63  HIS U   67  5                                   5    
HELIX  255 255 LEU U   70  LEU U   74  5                                   5    
HELIX  256 256 SER W    4  PHE W   15  1                                  12    
HELIX  257 257 GLU W   20  GLU W   29  1                                  10    
HELIX  258 258 GLU W   29  TYR W   34  1                                   6    
HELIX  259 259 ASN W   37  ILE W   46  1                                  10    
HELIX  260 260 ALA W   47  THR W   52  1                                   6    
HELIX  261 261 ASN W   63  HIS W   67  5                                   5    
HELIX  262 262 LEU W   70  LEU W   74  5                                   5    
HELIX  263 263 SER 5    4  PHE 5   15  1                                  12    
HELIX  264 264 GLU 5   20  TYR 5   34  1                                  15    
HELIX  265 265 ASN 5   37  ILE 5   46  1                                  10    
HELIX  266 266 ALA 5   47  THR 5   52  1                                   6    
HELIX  267 267 ASN 5   63  HIS 5   67  5                                   5    
HELIX  268 268 LEU 5   70  LEU 5   74  5                                   5    
HELIX  269 269 SER 7    4  PHE 7   15  1                                  12    
HELIX  270 270 GLU 7   20  TYR 7   34  1                                  15    
HELIX  271 271 ASN 7   37  ILE 7   46  1                                  10    
HELIX  272 272 ALA 7   47  THR 7   52  1                                   6    
HELIX  273 273 ASN 7   63  HIS 7   67  5                                   5    
HELIX  274 274 LEU 7   70  LEU 7   74  5                                   5    
HELIX  275 275 SER 9    4  PHE 9   15  1                                  12    
HELIX  276 276 GLU 9   20  TYR 9   34  1                                  15    
HELIX  277 277 ASN 9   37  ILE 9   46  1                                  10    
HELIX  278 278 ALA 9   47  THR 9   52  1                                   6    
HELIX  279 279 ASN 9   63  HIS 9   67  5                                   5    
HELIX  280 280 LEU 9   70  LEU 9   74  5                                   5    
HELIX  281 281 SER 1    4  PHE 1   15  1                                  12    
HELIX  282 282 GLU 1   20  GLU 1   29  1                                  10    
HELIX  283 283 GLU 1   29  TYR 1   34  1                                   6    
HELIX  284 284 ASN 1   37  ILE 1   46  1                                  10    
HELIX  285 285 ALA 1   47  THR 1   52  1                                   6    
HELIX  286 286 ASN 1   63  HIS 1   67  5                                   5    
HELIX  287 287 LEU 1   70  LEU 1   74  5                                   5    
HELIX  288 288 SER 4    4  PHE 4   15  1                                  12    
HELIX  289 289 GLU 4   20  GLU 4   29  1                                  10    
HELIX  290 290 GLU 4   29  TYR 4   34  1                                   6    
HELIX  291 291 ASN 4   37  ILE 4   46  1                                  10    
HELIX  292 292 ALA 4   47  THR 4   52  1                                   6    
HELIX  293 293 ASN 4   63  HIS 4   67  5                                   5    
HELIX  294 294 LEU 4   70  LEU 4   74  5                                   5    
HELIX  295 295 SER 8    4  PHE 8   15  1                                  12    
HELIX  296 296 GLU 8   20  GLU 8   29  1                                  10    
HELIX  297 297 GLU 8   29  TYR 8   34  1                                   6    
HELIX  298 298 ASN 8   37  ILE 8   46  1                                  10    
HELIX  299 299 ALA 8   47  THR 8   52  1                                   6    
HELIX  300 300 ASN 8   63  HIS 8   67  5                                   5    
HELIX  301 301 LEU 8   70  LEU 8   74  5                                   5    
SHEET    1   A 5 GLY A 445  LYS A 446  0                                        
SHEET    2   A 5 LEU A 469  PHE A 472  1  O  LEU A 469   N  LYS A 446           
SHEET    3   A 5 GLY A 524  MET A 528  1  O  THR A 527   N  PHE A 472           
SHEET    4   A 5 TYR A 421  LYS A 425  1  N  TRP A 422   O  VAL A 526           
SHEET    5   A 5 PHE A 541  GLN A 544  1  O  LYS A 543   N  LEU A 423           
SHEET    1   B 5 GLY B 445  LYS B 446  0                                        
SHEET    2   B 5 LEU B 469  PHE B 472  1  O  LEU B 469   N  LYS B 446           
SHEET    3   B 5 GLY B 524  MET B 528  1  O  THR B 527   N  PHE B 472           
SHEET    4   B 5 TYR B 421  LYS B 425  1  N  TRP B 422   O  VAL B 526           
SHEET    5   B 5 PHE B 541  GLN B 544  1  O  LYS B 543   N  LEU B 423           
SHEET    1   C 5 GLY C 445  LYS C 446  0                                        
SHEET    2   C 5 LEU C 469  PHE C 472  1  O  LEU C 469   N  LYS C 446           
SHEET    3   C 5 GLY C 524  MET C 528  1  O  THR C 527   N  PHE C 472           
SHEET    4   C 5 TYR C 421  LYS C 425  1  N  TRP C 422   O  VAL C 526           
SHEET    5   C 5 PHE C 541  GLN C 544  1  O  LYS C 543   N  LEU C 423           
SHEET    1   D 5 GLY D 445  LYS D 446  0                                        
SHEET    2   D 5 LEU D 469  PHE D 472  1  O  LEU D 469   N  LYS D 446           
SHEET    3   D 5 GLY D 524  MET D 528  1  O  THR D 527   N  PHE D 472           
SHEET    4   D 5 TYR D 421  LYS D 425  1  N  TRP D 422   O  VAL D 526           
SHEET    5   D 5 PHE D 541  GLN D 544  1  O  LYS D 543   N  LEU D 423           
SHEET    1   E 5 GLY E 445  LYS E 446  0                                        
SHEET    2   E 5 LEU E 469  PHE E 472  1  O  LEU E 469   N  LYS E 446           
SHEET    3   E 5 GLY E 524  MET E 528  1  O  THR E 527   N  PHE E 472           
SHEET    4   E 5 TYR E 421  LYS E 425  1  N  TRP E 422   O  VAL E 526           
SHEET    5   E 5 PHE E 541  GLN E 544  1  O  LYS E 543   N  LEU E 423           
SHEET    1   F 2 LEU E 509  GLU E 510  0                                        
SHEET    2   F 2 ASN E 515  ARG E 517 -1  O  ARG E 517   N  LEU E 509           
SHEET    1   G 5 GLY F 445  LYS F 446  0                                        
SHEET    2   G 5 LEU F 469  PHE F 472  1  O  LEU F 469   N  LYS F 446           
SHEET    3   G 5 GLY F 524  MET F 528  1  O  THR F 527   N  PHE F 472           
SHEET    4   G 5 TYR F 421  LYS F 425  1  N  TRP F 422   O  VAL F 526           
SHEET    5   G 5 PHE F 541  GLN F 544  1  O  LYS F 543   N  LEU F 423           
SHEET    1   H 5 GLY G 445  LYS G 446  0                                        
SHEET    2   H 5 LEU G 469  PHE G 472  1  O  LEU G 469   N  LYS G 446           
SHEET    3   H 5 GLY G 524  MET G 528  1  O  THR G 527   N  PHE G 472           
SHEET    4   H 5 TYR G 421  LYS G 425  1  N  TRP G 422   O  VAL G 526           
SHEET    5   H 5 PHE G 541  GLN G 544  1  O  LYS G 543   N  LEU G 423           
SHEET    1   I 5 GLY H 445  LYS H 446  0                                        
SHEET    2   I 5 LEU H 469  PHE H 472  1  O  LEU H 469   N  LYS H 446           
SHEET    3   I 5 GLY H 524  MET H 528  1  O  THR H 527   N  PHE H 472           
SHEET    4   I 5 TYR H 421  LYS H 425  1  N  TRP H 422   O  VAL H 526           
SHEET    5   I 5 PHE H 541  GLN H 544  1  O  LYS H 543   N  LEU H 423           
SHEET    1   J 5 GLY I 445  LYS I 446  0                                        
SHEET    2   J 5 LEU I 469  PHE I 472  1  O  LEU I 469   N  LYS I 446           
SHEET    3   J 5 GLY I 524  MET I 528  1  O  THR I 527   N  PHE I 472           
SHEET    4   J 5 TYR I 421  LYS I 425  1  N  TRP I 422   O  VAL I 526           
SHEET    5   J 5 PHE I 541  GLN I 544  1  O  LYS I 543   N  LEU I 423           
SHEET    1   K 5 GLY J 445  LYS J 446  0                                        
SHEET    2   K 5 LEU J 469  PHE J 472  1  O  LEU J 469   N  LYS J 446           
SHEET    3   K 5 GLY J 524  MET J 528  1  O  THR J 527   N  PHE J 472           
SHEET    4   K 5 TYR J 421  LYS J 425  1  N  TRP J 422   O  VAL J 526           
SHEET    5   K 5 PHE J 541  GLN J 544  1  O  LYS J 543   N  LEU J 423           
SHEET    1   L 5 GLY K 445  LYS K 446  0                                        
SHEET    2   L 5 LEU K 469  PHE K 472  1  O  LEU K 469   N  LYS K 446           
SHEET    3   L 5 GLY K 524  MET K 528  1  O  THR K 527   N  PHE K 472           
SHEET    4   L 5 TYR K 421  LYS K 425  1  N  TRP K 422   O  VAL K 526           
SHEET    5   L 5 PHE K 541  GLN K 544  1  O  LYS K 543   N  LEU K 423           
SHEET    1   M 5 GLY L 445  LYS L 446  0                                        
SHEET    2   M 5 LEU L 469  PHE L 472  1  O  LEU L 469   N  LYS L 446           
SHEET    3   M 5 GLY L 524  MET L 528  1  O  THR L 527   N  PHE L 472           
SHEET    4   M 5 TYR L 421  LYS L 425  1  N  TRP L 422   O  VAL L 526           
SHEET    5   M 5 PHE L 541  GLN L 544  1  O  LYS L 543   N  LEU L 423           
SHEET    1   N 2 LEU L 509  GLU L 510  0                                        
SHEET    2   N 2 ASN L 515  ARG L 517 -1  O  ARG L 517   N  LEU L 509           
LINK         ND1 HIS G 317                ZN    ZN G 700     1555   1555  2.34  
LINK         ND1 HIS C 317                ZN    ZN C 700     1555   1555  2.40  
LINK         ND1 HIS B 317                ZN    ZN B 700     1555   1555  2.50  
LINK         NE2 HIS A 313                ZN    ZN A 700     1555   1555  2.51  
LINK         NE2 HIS B 313                ZN    ZN B 700     1555   1555  2.53  
LINK         NE2 HIS G 313                ZN    ZN G 700     1555   1555  2.53  
LINK         ND1 HIS I 317                ZN    ZN I 700     1555   1555  2.53  
LINK         ND1 HIS E 317                ZN    ZN E 700     1555   1555  2.53  
LINK         ND1 HIS D 317                ZN    ZN D 700     1555   1555  2.54  
LINK         NE2 HIS I 313                ZN    ZN I 700     1555   1555  2.60  
LINK         ND1 HIS K 317                ZN    ZN K 700     1555   1555  2.61  
LINK         NE2 HIS J 313                ZN    ZN J 700     1555   1555  2.63  
LINK         NE2 HIS L 313                ZN    ZN L 700     1555   1555  2.63  
LINK         NE2 HIS F 313                ZN    ZN F 700     1555   1555  2.65  
LINK         ND1 HIS A 317                ZN    ZN A 700     1555   1555  2.67  
LINK         NE2 HIS K 313                ZN    ZN K 700     1555   1555  2.69  
LINK         NE2 HIS H 313                ZN    ZN H 700     1555   1555  2.69  
LINK         SG  CYS B 302                ZN    ZN B 700     1555   1555  2.87  
SITE     1 AC1  4 CYS A 302  CYS A 305  HIS A 313  HIS A 317                    
SITE     1 AC2  4 CYS B 302  CYS B 305  HIS B 313  HIS B 317                    
SITE     1 AC3  4 CYS C 302  CYS C 305  HIS C 313  HIS C 317                    
SITE     1 AC4  4 CYS D 302  CYS D 305  HIS D 313  HIS D 317                    
SITE     1 AC5  4 CYS E 302  CYS E 305  HIS E 313  HIS E 317                    
SITE     1 AC6  4 CYS F 302  CYS F 305  HIS F 313  HIS F 317                    
SITE     1 AC7  4 CYS G 302  CYS G 305  HIS G 313  HIS G 317                    
SITE     1 AC8  4 CYS H 302  CYS H 305  HIS H 313  HIS H 317                    
SITE     1 AC9  4 CYS I 302  CYS I 305  HIS I 313  HIS I 317                    
SITE     1 BC1  4 CYS J 302  CYS J 305  HIS J 313  HIS J 317                    
SITE     1 BC2  4 CYS K 302  CYS K 305  HIS K 313  HIS K 317                    
SITE     1 BC3  4 CYS L 302  CYS L 305  HIS L 313  HIS L 317                    
CRYST1  249.098  249.098  387.032  90.00  90.00  90.00 P 41 21 2    96          
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      0.004014  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004014  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002584        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system