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Database: PDB
Entry: 2ZVI
LinkDB: 2ZVI
Original site: 2ZVI 
HEADER    ISOMERASE                               07-NOV-08   2ZVI              
TITLE     CRYSTAL STRUCTURE OF 2,3-DIKETO-5-METHYLTHIOPENTYL-1-                 
TITLE    2 PHOSPHATE ENOLASE FROM BACILLUS SUBTILIS                             
CAVEAT     2ZVI    CHIRALITY ERRORS AT THE CA CENTER OF A 22 PRO, D 66          
CAVEAT   2 2ZVI     ARG AND D 74 LYS.                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2,3-DIKETO-5-METHYLTHIOPENTYL-1-PHOSPHATE                  
COMPND   3 ENOLASE;                                                             
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 FRAGMENT: RESIDUES 10-414;                                           
COMPND   6 SYNONYM: DK-MTP-1-P ENOLASE;                                         
COMPND   7 EC: 5.3.2.-;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-15B                                   
KEYWDS    CRYSTAL STRUCTURE, ENOLASE, METHIONINE SALVAGE PATHWAY,               
KEYWDS   2 AMINO-ACID BIOSYNTHESIS, ISOMERASE, MAGNESIUM, METAL-                
KEYWDS   3 BINDING, METHIONINE BIOSYNTHESIS                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.TAMURA,T.YADANI,Y.KAI,T.INOUE,H.MATSUMURA                           
REVDAT   1   01-SEP-09 2ZVI    0                                                
JRNL        AUTH   H.TAMURA,Y.SAITO,H.ASHIDA,Y.KAI,T.INOUE,A.YOKOTA,            
JRNL        AUTH 2 H.MATSUMURA                                                  
JRNL        TITL   STRUCTURE OF THE APO DECARBAMYLATED FORM OF                  
JRNL        TITL 2 2,3-DIKETO-5-METHYLTHIOPENTYL-1-PHOSPHATE ENOLASE            
JRNL        TITL 3 FROM BACILLUS SUBTILIS                                       
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  65   942 2009              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   19690372                                                     
JRNL        DOI    10.1107/S0907444909022422                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1983182.920                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 64711                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3267                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 10262                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400                       
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 516                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11945                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 308                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.53000                                             
REMARK   3    B22 (A**2) : 8.46000                                              
REMARK   3    B33 (A**2) : -4.92000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.45000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.23                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.32                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.33                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.88                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 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 : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 27.57                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ZVI COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-NOV-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB028477.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL44XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : BRUKER DIP-6040                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64719                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08400                            
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) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27300                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2OEK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.14M NA THIOCYANATE, 21% (W/V)          
REMARK 280  POLYETHYLENE GLYCOL 3350, PH 7.4, VAPOR DIFFUSION, HANGING          
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       45.73300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     MET A    10                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     GLY A    68                                                      
REMARK 465     THR A    69                                                      
REMARK 465     ALA A   411                                                      
REMARK 465     GLU A   412                                                      
REMARK 465     ALA A   413                                                      
REMARK 465     VAL A   414                                                      
REMARK 465     MET B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     HIS B     9                                                      
REMARK 465     MET B    10                                                      
REMARK 465     GLU B    67                                                      
REMARK 465     GLY B    68                                                      
REMARK 465     THR B    69                                                      
REMARK 465     ALA B    70                                                      
REMARK 465     ALA B    71                                                      
REMARK 465     GLU B   412                                                      
REMARK 465     ALA B   413                                                      
REMARK 465     VAL B   414                                                      
REMARK 465     MET C   -10                                                      
REMARK 465     GLY C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     SER C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     HIS C     9                                                      
REMARK 465     MET C    10                                                      
REMARK 465     GLY C    40                                                      
REMARK 465     SER C    41                                                      
REMARK 465     TRP C    42                                                      
REMARK 465     THR C    43                                                      
REMARK 465     ASP C    44                                                      
REMARK 465     LEU C    45                                                      
REMARK 465     PRO C    46                                                      
REMARK 465     LEU C    47                                                      
REMARK 465     GLU C    67                                                      
REMARK 465     GLY C    68                                                      
REMARK 465     THR C    69                                                      
REMARK 465     ALA C    70                                                      
REMARK 465     ALA C    71                                                      
REMARK 465     SER C    72                                                      
REMARK 465     LYS C   410                                                      
REMARK 465     ALA C   411                                                      
REMARK 465     GLU C   412                                                      
REMARK 465     ALA C   413                                                      
REMARK 465     VAL C   414                                                      
REMARK 465     MET D   -10                                                      
REMARK 465     GLY D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     SER D    -7                                                      
REMARK 465     HIS D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     HIS D    -3                                                      
REMARK 465     HIS D    -2                                                      
REMARK 465     HIS D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     SER D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     VAL D     4                                                      
REMARK 465     PRO D     5                                                      
REMARK 465     ARG D     6                                                      
REMARK 465     GLY D     7                                                      
REMARK 465     SER D     8                                                      
REMARK 465     HIS D     9                                                      
REMARK 465     MET D    10                                                      
REMARK 465     LEU D    37                                                      
REMARK 465     THR D    38                                                      
REMARK 465     VAL D    39                                                      
REMARK 465     GLY D    40                                                      
REMARK 465     SER D    41                                                      
REMARK 465     TRP D    42                                                      
REMARK 465     THR D    43                                                      
REMARK 465     ASP D    44                                                      
REMARK 465     LEU D    45                                                      
REMARK 465     GLY D    68                                                      
REMARK 465     THR D    69                                                      
REMARK 465     ALA D    70                                                      
REMARK 465     ALA D    71                                                      
REMARK 465     SER D    72                                                      
REMARK 465     GLU D    73                                                      
REMARK 465     VAL D   414                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PRO A  22    O                                                   
REMARK 470     ASP A  44    CG   OD1  OD2                                       
REMARK 470     ARG A  66    O    CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     GLU B  51    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  66    O                                                   
REMARK 470     SER B  72    OG                                                  
REMARK 470     LYS B 150    CG   CD   CE   NZ                                   
REMARK 470     ARG B 155    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 183    CG   CD   OE1  OE2                                  
REMARK 470     THR B 184    OG1  CG2                                            
REMARK 470     GLU C  21    CG   CD   OE1  OE2                                  
REMARK 470     VAL C  39    O                                                   
REMARK 470     GLN C  54    CG   CD   OE1  NE2                                  
REMARK 470     ARG C  66    O                                                   
REMARK 470     LYS C 150    CG   CD   CE   NZ                                   
REMARK 470     VAL C 152    CG1  CG2                                            
REMARK 470     ASP C 392    CG   OD1  OD2                                       
REMARK 470     LYS C 394    O                                                   
REMARK 470     GLU C 396    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 397    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  21    CG   CD   OE1  OE2                                  
REMARK 470     GLY D  36    O                                                   
REMARK 470     GLU D  51    CG   CD   OE1  OE2                                  
REMARK 470     MET D  53    CG   SD   CE                                        
REMARK 470     GLU D  65    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  66    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  67    O    CG   CD   OE1  OE2                             
REMARK 470     LYS D 410    CG   CD   CE   NZ                                   
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    GLU A  21      -76.01   -142.30                                   
REMARK 500    THR A  38      -34.67   -133.57                                   
REMARK 500    PHE A  99       43.54   -152.20                                   
REMARK 500    ARG A 142      144.55   -173.08                                   
REMARK 500    ALA A 187       82.91   -154.13                                   
REMARK 500    VAL A 270      -22.41     74.05                                   
REMARK 500    ALA A 328       44.69    -75.52                                   
REMARK 500    SER A 337     -127.92   -129.57                                   
REMARK 500    ALA A 338      104.84     25.21                                   
REMARK 500    THR B  38      -96.64   -129.07                                   
REMARK 500    THR B  43       12.95    -62.13                                   
REMARK 500    PRO B  46      -97.86   -108.55                                   
REMARK 500    PHE B  99       28.06   -140.60                                   
REMARK 500    ARG B 142      136.71   -179.08                                   
REMARK 500    LYS B 150      -70.34    -80.55                                   
REMARK 500    VAL B 152     -135.10   -104.30                                   
REMARK 500    PHE B 189      -62.48    -29.48                                   
REMARK 500    VAL B 270      -17.35     75.77                                   
REMARK 500    SER B 337      -61.71   -134.72                                   
REMARK 500    ALA B 338      115.86    -30.65                                   
REMARK 500    ASN B 369       33.65    -97.93                                   
REMARK 500    ALA C  24      -73.44   -101.71                                   
REMARK 500    THR C  38      -81.20   -140.50                                   
REMARK 500    LYS C  49       -6.31     97.44                                   
REMARK 500    GLU C  51       34.47    -73.84                                   
REMARK 500    PHE C  99       34.00   -154.65                                   
REMARK 500    ARG C 142      148.16   -171.41                                   
REMARK 500    THR C 207      -19.58   -144.83                                   
REMARK 500    VAL C 270      -23.00     80.34                                   
REMARK 500    PRO C 305       34.39    -88.28                                   
REMARK 500    ASN C 369     -173.53    -67.48                                   
REMARK 500    ASP D  25       64.92   -116.99                                   
REMARK 500    THR D  35     -164.72   -103.33                                   
REMARK 500    GLN D  52       21.29    -77.15                                   
REMARK 500    ARG D  66      111.98    159.06                                   
REMARK 500    ALA D  76      102.63   -178.45                                   
REMARK 500    PHE D  99       42.69   -151.35                                   
REMARK 500    LYS D 107       84.74    -69.20                                   
REMARK 500    VAL D 152      -60.34   -139.35                                   
REMARK 500    TYR D 246      -78.52   -116.33                                   
REMARK 500    VAL D 270      -20.68     73.07                                   
REMARK 500    ALA D 328       34.66    -72.20                                   
REMARK 500    SER D 337      -32.46   -139.18                                   
REMARK 500    ALA D 338      105.12    -58.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO C  336     SER C  337                 -138.60                    
REMARK 500 ALA C  338     GLY C  339                  139.49                    
REMARK 500 GLY C  339     ILE C  340                 -149.90                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2ZVI A   10   414  UNP    O31666   MTNW_BACSU      10    414             
DBREF  2ZVI B   10   414  UNP    O31666   MTNW_BACSU      10    414             
DBREF  2ZVI C   10   414  UNP    O31666   MTNW_BACSU      10    414             
DBREF  2ZVI D   10   414  UNP    O31666   MTNW_BACSU      10    414             
SEQADV 2ZVI MET A  -10  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI GLY A   -9  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER A   -8  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER A   -7  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS A   -6  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS A   -5  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS A   -4  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS A   -3  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS A   -2  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS A   -1  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER A    0  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER A    1  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI GLY A    2  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI LEU A    3  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI VAL A    4  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI PRO A    5  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI ARG A    6  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI GLY A    7  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER A    8  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS A    9  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI MET B  -10  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI GLY B   -9  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER B   -8  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER B   -7  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS B   -6  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS B   -5  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS B   -4  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS B   -3  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS B   -2  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS B   -1  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER B    0  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER B    1  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI GLY B    2  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI LEU B    3  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI VAL B    4  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI PRO B    5  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI ARG B    6  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI GLY B    7  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER B    8  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS B    9  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI MET C  -10  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI GLY C   -9  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER C   -8  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER C   -7  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS C   -6  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS C   -5  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS C   -4  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS C   -3  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS C   -2  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS C   -1  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER C    0  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER C    1  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI GLY C    2  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI LEU C    3  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI VAL C    4  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI PRO C    5  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI ARG C    6  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI GLY C    7  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER C    8  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS C    9  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI MET D  -10  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI GLY D   -9  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER D   -8  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER D   -7  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS D   -6  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS D   -5  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS D   -4  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS D   -3  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS D   -2  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS D   -1  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER D    0  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER D    1  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI GLY D    2  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI LEU D    3  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI VAL D    4  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI PRO D    5  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI ARG D    6  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI GLY D    7  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI SER D    8  UNP  O31666              EXPRESSION TAG                 
SEQADV 2ZVI HIS D    9  UNP  O31666              EXPRESSION TAG                 
SEQRES   1 A  425  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  425  LEU VAL PRO ARG GLY SER HIS MET SER GLU LEU LEU ALA          
SEQRES   3 A  425  THR TYR LEU LEU THR GLU PRO GLY ALA ASP THR GLU LYS          
SEQRES   4 A  425  LYS ALA GLU GLN ILE ALA THR GLY LEU THR VAL GLY SER          
SEQRES   5 A  425  TRP THR ASP LEU PRO LEU VAL LYS GLN GLU GLN MET GLN          
SEQRES   6 A  425  LYS HIS LYS GLY ARG VAL ILE LYS VAL GLU GLU ARG GLU          
SEQRES   7 A  425  GLY THR ALA ALA SER GLU LYS GLN ALA VAL ILE THR ILE          
SEQRES   8 A  425  ALA TYR PRO GLU ILE ASN PHE SER GLN ASP ILE PRO ALA          
SEQRES   9 A  425  LEU LEU THR THR VAL PHE GLY LYS LEU SER LEU ASP GLY          
SEQRES  10 A  425  LYS ILE LYS LEU ILE ASP LEU HIS PHE SER GLU ALA PHE          
SEQRES  11 A  425  LYS ARG ALA LEU PRO GLY PRO LYS PHE GLY VAL TYR GLY          
SEQRES  12 A  425  ILE ARG LYS LEU LEU GLY GLU PHE GLU ARG PRO LEU LEU          
SEQRES  13 A  425  MET SER ILE PHE LYS GLY VAL ILE GLY ARG ASP LEU SER          
SEQRES  14 A  425  ASP ILE LYS GLU GLN LEU ARG GLN GLN ALA LEU GLY GLY          
SEQRES  15 A  425  VAL ASP LEU ILE LYS ASP ASP GLU ILE PHE PHE GLU THR          
SEQRES  16 A  425  GLY LEU ALA PRO PHE GLU THR ARG ILE ALA GLU GLY LYS          
SEQRES  17 A  425  GLN ILE LEU LYS GLU THR TYR GLU GLN THR GLY HIS LYS          
SEQRES  18 A  425  THR LEU TYR ALA VAL ASN LEU THR GLY ARG THR ALA ASP          
SEQRES  19 A  425  LEU LYS ASP LYS ALA ARG ARG ALA ALA GLU LEU GLY ALA          
SEQRES  20 A  425  ASP ALA LEU LEU PHE ASN VAL PHE ALA TYR GLY LEU ASP          
SEQRES  21 A  425  VAL MET GLN GLY LEU ALA GLU ASP PRO GLU ILE PRO VAL          
SEQRES  22 A  425  PRO ILE MET ALA HIS PRO ALA VAL SER GLY ALA PHE THR          
SEQRES  23 A  425  SER SER PRO PHE TYR GLY PHE SER HIS ALA LEU LEU LEU          
SEQRES  24 A  425  GLY LYS LEU ASN ARG TYR CYS GLY ALA ASP PHE SER LEU          
SEQRES  25 A  425  PHE PRO SER PRO TYR GLY SER VAL ALA LEU PRO ARG ALA          
SEQRES  26 A  425  ASP ALA LEU ALA ILE HIS GLU GLU CYS VAL ARG GLU ASP          
SEQRES  27 A  425  ALA PHE ASN GLN THR PHE ALA VAL PRO SER ALA GLY ILE          
SEQRES  28 A  425  HIS PRO GLY MET VAL PRO LEU LEU MET ARG ASP PHE GLY          
SEQRES  29 A  425  ILE ASP HIS ILE ILE ASN ALA GLY GLY GLY VAL HIS GLY          
SEQRES  30 A  425  HIS PRO ASN GLY ALA GLN GLY GLY GLY ARG ALA PHE ARG          
SEQRES  31 A  425  ALA ILE ILE ASP ALA VAL LEU GLU ALA GLN PRO ILE ASP          
SEQRES  32 A  425  GLU LYS ALA GLU GLN CYS LYS ASP LEU LYS LEU ALA LEU          
SEQRES  33 A  425  ASP LYS TRP GLY LYS ALA GLU ALA VAL                          
SEQRES   1 B  425  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  425  LEU VAL PRO ARG GLY SER HIS MET SER GLU LEU LEU ALA          
SEQRES   3 B  425  THR TYR LEU LEU THR GLU PRO GLY ALA ASP THR GLU LYS          
SEQRES   4 B  425  LYS ALA GLU GLN ILE ALA THR GLY LEU THR VAL GLY SER          
SEQRES   5 B  425  TRP THR ASP LEU PRO LEU VAL LYS GLN GLU GLN MET GLN          
SEQRES   6 B  425  LYS HIS LYS GLY ARG VAL ILE LYS VAL GLU GLU ARG GLU          
SEQRES   7 B  425  GLY THR ALA ALA SER GLU LYS GLN ALA VAL ILE THR ILE          
SEQRES   8 B  425  ALA TYR PRO GLU ILE ASN PHE SER GLN ASP ILE PRO ALA          
SEQRES   9 B  425  LEU LEU THR THR VAL PHE GLY LYS LEU SER LEU ASP GLY          
SEQRES  10 B  425  LYS ILE LYS LEU ILE ASP LEU HIS PHE SER GLU ALA PHE          
SEQRES  11 B  425  LYS ARG ALA LEU PRO GLY PRO LYS PHE GLY VAL TYR GLY          
SEQRES  12 B  425  ILE ARG LYS LEU LEU GLY GLU PHE GLU ARG PRO LEU LEU          
SEQRES  13 B  425  MET SER ILE PHE LYS GLY VAL ILE GLY ARG ASP LEU SER          
SEQRES  14 B  425  ASP ILE LYS GLU GLN LEU ARG GLN GLN ALA LEU GLY GLY          
SEQRES  15 B  425  VAL ASP LEU ILE LYS ASP ASP GLU ILE PHE PHE GLU THR          
SEQRES  16 B  425  GLY LEU ALA PRO PHE GLU THR ARG ILE ALA GLU GLY LYS          
SEQRES  17 B  425  GLN ILE LEU LYS GLU THR TYR GLU GLN THR GLY HIS LYS          
SEQRES  18 B  425  THR LEU TYR ALA VAL ASN LEU THR GLY ARG THR ALA ASP          
SEQRES  19 B  425  LEU LYS ASP LYS ALA ARG ARG ALA ALA GLU LEU GLY ALA          
SEQRES  20 B  425  ASP ALA LEU LEU PHE ASN VAL PHE ALA TYR GLY LEU ASP          
SEQRES  21 B  425  VAL MET GLN GLY LEU ALA GLU ASP PRO GLU ILE PRO VAL          
SEQRES  22 B  425  PRO ILE MET ALA HIS PRO ALA VAL SER GLY ALA PHE THR          
SEQRES  23 B  425  SER SER PRO PHE TYR GLY PHE SER HIS ALA LEU LEU LEU          
SEQRES  24 B  425  GLY LYS LEU ASN ARG TYR CYS GLY ALA ASP PHE SER LEU          
SEQRES  25 B  425  PHE PRO SER PRO TYR GLY SER VAL ALA LEU PRO ARG ALA          
SEQRES  26 B  425  ASP ALA LEU ALA ILE HIS GLU GLU CYS VAL ARG GLU ASP          
SEQRES  27 B  425  ALA PHE ASN GLN THR PHE ALA VAL PRO SER ALA GLY ILE          
SEQRES  28 B  425  HIS PRO GLY MET VAL PRO LEU LEU MET ARG ASP PHE GLY          
SEQRES  29 B  425  ILE ASP HIS ILE ILE ASN ALA GLY GLY GLY VAL HIS GLY          
SEQRES  30 B  425  HIS PRO ASN GLY ALA GLN GLY GLY GLY ARG ALA PHE ARG          
SEQRES  31 B  425  ALA ILE ILE ASP ALA VAL LEU GLU ALA GLN PRO ILE ASP          
SEQRES  32 B  425  GLU LYS ALA GLU GLN CYS LYS ASP LEU LYS LEU ALA LEU          
SEQRES  33 B  425  ASP LYS TRP GLY LYS ALA GLU ALA VAL                          
SEQRES   1 C  425  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  425  LEU VAL PRO ARG GLY SER HIS MET SER GLU LEU LEU ALA          
SEQRES   3 C  425  THR TYR LEU LEU THR GLU PRO GLY ALA ASP THR GLU LYS          
SEQRES   4 C  425  LYS ALA GLU GLN ILE ALA THR GLY LEU THR VAL GLY SER          
SEQRES   5 C  425  TRP THR ASP LEU PRO LEU VAL LYS GLN GLU GLN MET GLN          
SEQRES   6 C  425  LYS HIS LYS GLY ARG VAL ILE LYS VAL GLU GLU ARG GLU          
SEQRES   7 C  425  GLY THR ALA ALA SER GLU LYS GLN ALA VAL ILE THR ILE          
SEQRES   8 C  425  ALA TYR PRO GLU ILE ASN PHE SER GLN ASP ILE PRO ALA          
SEQRES   9 C  425  LEU LEU THR THR VAL PHE GLY LYS LEU SER LEU ASP GLY          
SEQRES  10 C  425  LYS ILE LYS LEU ILE ASP LEU HIS PHE SER GLU ALA PHE          
SEQRES  11 C  425  LYS ARG ALA LEU PRO GLY PRO LYS PHE GLY VAL TYR GLY          
SEQRES  12 C  425  ILE ARG LYS LEU LEU GLY GLU PHE GLU ARG PRO LEU LEU          
SEQRES  13 C  425  MET SER ILE PHE LYS GLY VAL ILE GLY ARG ASP LEU SER          
SEQRES  14 C  425  ASP ILE LYS GLU GLN LEU ARG GLN GLN ALA LEU GLY GLY          
SEQRES  15 C  425  VAL ASP LEU ILE LYS ASP ASP GLU ILE PHE PHE GLU THR          
SEQRES  16 C  425  GLY LEU ALA PRO PHE GLU THR ARG ILE ALA GLU GLY LYS          
SEQRES  17 C  425  GLN ILE LEU LYS GLU THR TYR GLU GLN THR GLY HIS LYS          
SEQRES  18 C  425  THR LEU TYR ALA VAL ASN LEU THR GLY ARG THR ALA ASP          
SEQRES  19 C  425  LEU LYS ASP LYS ALA ARG ARG ALA ALA GLU LEU GLY ALA          
SEQRES  20 C  425  ASP ALA LEU LEU PHE ASN VAL PHE ALA TYR GLY LEU ASP          
SEQRES  21 C  425  VAL MET GLN GLY LEU ALA GLU ASP PRO GLU ILE PRO VAL          
SEQRES  22 C  425  PRO ILE MET ALA HIS PRO ALA VAL SER GLY ALA PHE THR          
SEQRES  23 C  425  SER SER PRO PHE TYR GLY PHE SER HIS ALA LEU LEU LEU          
SEQRES  24 C  425  GLY LYS LEU ASN ARG TYR CYS GLY ALA ASP PHE SER LEU          
SEQRES  25 C  425  PHE PRO SER PRO TYR GLY SER VAL ALA LEU PRO ARG ALA          
SEQRES  26 C  425  ASP ALA LEU ALA ILE HIS GLU GLU CYS VAL ARG GLU ASP          
SEQRES  27 C  425  ALA PHE ASN GLN THR PHE ALA VAL PRO SER ALA GLY ILE          
SEQRES  28 C  425  HIS PRO GLY MET VAL PRO LEU LEU MET ARG ASP PHE GLY          
SEQRES  29 C  425  ILE ASP HIS ILE ILE ASN ALA GLY GLY GLY VAL HIS GLY          
SEQRES  30 C  425  HIS PRO ASN GLY ALA GLN GLY GLY GLY ARG ALA PHE ARG          
SEQRES  31 C  425  ALA ILE ILE ASP ALA VAL LEU GLU ALA GLN PRO ILE ASP          
SEQRES  32 C  425  GLU LYS ALA GLU GLN CYS LYS ASP LEU LYS LEU ALA LEU          
SEQRES  33 C  425  ASP LYS TRP GLY LYS ALA GLU ALA VAL                          
SEQRES   1 D  425  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  425  LEU VAL PRO ARG GLY SER HIS MET SER GLU LEU LEU ALA          
SEQRES   3 D  425  THR TYR LEU LEU THR GLU PRO GLY ALA ASP THR GLU LYS          
SEQRES   4 D  425  LYS ALA GLU GLN ILE ALA THR GLY LEU THR VAL GLY SER          
SEQRES   5 D  425  TRP THR ASP LEU PRO LEU VAL LYS GLN GLU GLN MET GLN          
SEQRES   6 D  425  LYS HIS LYS GLY ARG VAL ILE LYS VAL GLU GLU ARG GLU          
SEQRES   7 D  425  GLY THR ALA ALA SER GLU LYS GLN ALA VAL ILE THR ILE          
SEQRES   8 D  425  ALA TYR PRO GLU ILE ASN PHE SER GLN ASP ILE PRO ALA          
SEQRES   9 D  425  LEU LEU THR THR VAL PHE GLY LYS LEU SER LEU ASP GLY          
SEQRES  10 D  425  LYS ILE LYS LEU ILE ASP LEU HIS PHE SER GLU ALA PHE          
SEQRES  11 D  425  LYS ARG ALA LEU PRO GLY PRO LYS PHE GLY VAL TYR GLY          
SEQRES  12 D  425  ILE ARG LYS LEU LEU GLY GLU PHE GLU ARG PRO LEU LEU          
SEQRES  13 D  425  MET SER ILE PHE LYS GLY VAL ILE GLY ARG ASP LEU SER          
SEQRES  14 D  425  ASP ILE LYS GLU GLN LEU ARG GLN GLN ALA LEU GLY GLY          
SEQRES  15 D  425  VAL ASP LEU ILE LYS ASP ASP GLU ILE PHE PHE GLU THR          
SEQRES  16 D  425  GLY LEU ALA PRO PHE GLU THR ARG ILE ALA GLU GLY LYS          
SEQRES  17 D  425  GLN ILE LEU LYS GLU THR TYR GLU GLN THR GLY HIS LYS          
SEQRES  18 D  425  THR LEU TYR ALA VAL ASN LEU THR GLY ARG THR ALA ASP          
SEQRES  19 D  425  LEU LYS ASP LYS ALA ARG ARG ALA ALA GLU LEU GLY ALA          
SEQRES  20 D  425  ASP ALA LEU LEU PHE ASN VAL PHE ALA TYR GLY LEU ASP          
SEQRES  21 D  425  VAL MET GLN GLY LEU ALA GLU ASP PRO GLU ILE PRO VAL          
SEQRES  22 D  425  PRO ILE MET ALA HIS PRO ALA VAL SER GLY ALA PHE THR          
SEQRES  23 D  425  SER SER PRO PHE TYR GLY PHE SER HIS ALA LEU LEU LEU          
SEQRES  24 D  425  GLY LYS LEU ASN ARG TYR CYS GLY ALA ASP PHE SER LEU          
SEQRES  25 D  425  PHE PRO SER PRO TYR GLY SER VAL ALA LEU PRO ARG ALA          
SEQRES  26 D  425  ASP ALA LEU ALA ILE HIS GLU GLU CYS VAL ARG GLU ASP          
SEQRES  27 D  425  ALA PHE ASN GLN THR PHE ALA VAL PRO SER ALA GLY ILE          
SEQRES  28 D  425  HIS PRO GLY MET VAL PRO LEU LEU MET ARG ASP PHE GLY          
SEQRES  29 D  425  ILE ASP HIS ILE ILE ASN ALA GLY GLY GLY VAL HIS GLY          
SEQRES  30 D  425  HIS PRO ASN GLY ALA GLN GLY GLY GLY ARG ALA PHE ARG          
SEQRES  31 D  425  ALA ILE ILE ASP ALA VAL LEU GLU ALA GLN PRO ILE ASP          
SEQRES  32 D  425  GLU LYS ALA GLU GLN CYS LYS ASP LEU LYS LEU ALA LEU          
SEQRES  33 D  425  ASP LYS TRP GLY LYS ALA GLU ALA VAL                          
FORMUL   5  HOH   *308(H2 O)                                                    
HELIX    1   1 ASP A   25  LEU A   37  1                                  13    
HELIX    2   2 PRO A   46  GLU A   51  1                                   6    
HELIX    3   3 GLN A   52  LYS A   57  5                                   6    
HELIX    4   4 ILE A   85  PHE A   87  5                                   3    
HELIX    5   5 ASP A   90  GLY A  100  1                                  11    
HELIX    6   6 LYS A  101  ASP A  105  5                                   5    
HELIX    7   7 SER A  116  ALA A  122  1                                   7    
HELIX    8   8 PHE A  128  GLY A  138  1                                  11    
HELIX    9   9 ASP A  156  GLY A  170  1                                  15    
HELIX   10  10 PRO A  188  GLY A  208  1                                  21    
HELIX   11  11 ARG A  220  ALA A  222  5                                   3    
HELIX   12  12 ASP A  223  LEU A  234  1                                  12    
HELIX   13  13 ASN A  242  TYR A  246  5                                   5    
HELIX   14  14 GLY A  247  ASP A  257  1                                  11    
HELIX   15  15 VAL A  270  THR A  275  5                                   6    
HELIX   16  16 SER A  283  LEU A  288  1                                   6    
HELIX   17  17 GLY A  289  CYS A  295  1                                   7    
HELIX   18  18 PRO A  312  ARG A  325  1                                  14    
HELIX   19  19 HIS A  341  GLY A  343  5                                   3    
HELIX   20  20 MET A  344  GLY A  353  1                                  10    
HELIX   21  21 GLY A  361  HIS A  367  5                                   7    
HELIX   22  22 ASN A  369  GLU A  387  1                                  19    
HELIX   23  23 PRO A  390  CYS A  398  1                                   9    
HELIX   24  24 CYS A  398  GLY A  409  1                                  12    
HELIX   25  25 ASP B   25  LEU B   37  1                                  13    
HELIX   26  26 LYS B   49  GLN B   54  1                                   6    
HELIX   27  27 LYS B   55  LYS B   57  5                                   3    
HELIX   28  28 ILE B   85  PHE B   87  5                                   3    
HELIX   29  29 ASP B   90  GLY B  100  1                                  11    
HELIX   30  30 LYS B  101  ASP B  105  5                                   5    
HELIX   31  31 SER B  116  ALA B  122  1                                   7    
HELIX   32  32 PHE B  128  GLY B  138  1                                  11    
HELIX   33  33 ASP B  156  GLY B  170  1                                  15    
HELIX   34  34 PRO B  188  GLY B  208  1                                  21    
HELIX   35  35 ARG B  220  ALA B  222  5                                   3    
HELIX   36  36 ASP B  223  GLY B  235  1                                  13    
HELIX   37  37 ASN B  242  TYR B  246  5                                   5    
HELIX   38  38 GLY B  247  ASP B  257  1                                  11    
HELIX   39  39 SER B  271  SER B  276  1                                   6    
HELIX   40  40 SER B  283  LEU B  288  1                                   6    
HELIX   41  41 GLY B  289  CYS B  295  1                                   7    
HELIX   42  42 PRO B  312  ARG B  325  1                                  14    
HELIX   43  43 HIS B  341  GLY B  343  5                                   3    
HELIX   44  44 MET B  344  GLY B  353  1                                  10    
HELIX   45  45 ASN B  369  GLU B  387  1                                  19    
HELIX   46  46 PRO B  390  CYS B  398  1                                   9    
HELIX   47  47 CYS B  398  GLY B  409  1                                  12    
HELIX   48  48 ASP C   25  LEU C   37  1                                  13    
HELIX   49  49 MET C   53  LYS C   57  5                                   5    
HELIX   50  50 ILE C   85  PHE C   87  5                                   3    
HELIX   51  51 ASP C   90  GLY C  100  1                                  11    
HELIX   52  52 LYS C  101  ASP C  105  5                                   5    
HELIX   53  53 SER C  116  ARG C  121  1                                   6    
HELIX   54  54 PHE C  128  GLY C  138  1                                  11    
HELIX   55  55 ASP C  156  GLY C  170  1                                  15    
HELIX   56  56 PRO C  188  GLN C  206  1                                  19    
HELIX   57  57 ARG C  220  ALA C  222  5                                   3    
HELIX   58  58 ASP C  223  LEU C  234  1                                  12    
HELIX   59  59 ASN C  242  GLY C  247  1                                   6    
HELIX   60  60 GLY C  247  GLU C  256  1                                  10    
HELIX   61  61 VAL C  270  THR C  275  5                                   6    
HELIX   62  62 SER C  283  LEU C  288  1                                   6    
HELIX   63  63 GLY C  289  CYS C  295  1                                   7    
HELIX   64  64 PRO C  312  ARG C  325  1                                  14    
HELIX   65  65 HIS C  341  GLY C  343  5                                   3    
HELIX   66  66 MET C  344  GLY C  353  1                                  10    
HELIX   67  67 ALA C  360  HIS C  367  1                                   8    
HELIX   68  68 GLY C  370  GLU C  387  1                                  18    
HELIX   69  69 ASP C  392  GLN C  397  1                                   6    
HELIX   70  70 CYS C  398  GLY C  409  1                                  12    
HELIX   71  71 ASP D   25  THR D   35  1                                  11    
HELIX   72  72 LEU D   47  GLN D   52  1                                   6    
HELIX   73  73 ILE D   85  PHE D   87  5                                   3    
HELIX   74  74 ASP D   90  GLY D  100  1                                  11    
HELIX   75  75 LYS D  101  ASP D  105  5                                   5    
HELIX   76  76 SER D  116  ALA D  122  1                                   7    
HELIX   77  77 PHE D  128  GLY D  138  1                                  11    
HELIX   78  78 ASP D  156  GLY D  170  1                                  15    
HELIX   79  79 PRO D  188  GLY D  208  1                                  21    
HELIX   80  80 ARG D  220  ALA D  222  5                                   3    
HELIX   81  81 ASP D  223  GLY D  235  1                                  13    
HELIX   82  82 ASN D  242  GLY D  247  1                                   6    
HELIX   83  83 GLY D  247  ASP D  257  1                                  11    
HELIX   84  84 SER D  271  SER D  276  1                                   6    
HELIX   85  85 SER D  283  GLY D  289  1                                   7    
HELIX   86  86 GLY D  289  CYS D  295  1                                   7    
HELIX   87  87 PRO D  312  ARG D  325  1                                  14    
HELIX   88  88 HIS D  341  GLY D  343  5                                   3    
HELIX   89  89 MET D  344  GLY D  353  1                                  10    
HELIX   90  90 GLY D  362  HIS D  367  5                                   6    
HELIX   91  91 ASN D  369  ALA D  388  1                                  20    
HELIX   92  92 PRO D  390  CYS D  398  1                                   9    
HELIX   93  93 CYS D  398  GLY D  409  1                                  12    
SHEET    1   A 5 ARG A  59  GLU A  64  0                                        
SHEET    2   A 5 ALA A  76  PRO A  83 -1  O  THR A  79   N  ILE A  61           
SHEET    3   A 5 GLU A  12  LEU A  19 -1  N  TYR A  17   O  ILE A  78           
SHEET    4   A 5 ILE A 108  HIS A 114 -1  O  ASP A 112   N  THR A  16           
SHEET    5   A 5 GLY A 281  PHE A 282  1  O  GLY A 281   N  LEU A 110           
SHEET    1   B 8 PHE A 333  PRO A 336  0                                        
SHEET    2   B 8 PHE A 299  PHE A 302  1  N  SER A 300   O  VAL A 335           
SHEET    3   B 8 ILE A 264  ALA A 266  1  N  ALA A 266   O  PHE A 299           
SHEET    4   B 8 ALA A 238  PHE A 241  1  N  PHE A 241   O  MET A 265           
SHEET    5   B 8 LEU A 212  ASN A 216  1  N  VAL A 215   O  ALA A 238           
SHEET    6   B 8 LEU A 174  LYS A 176  1  N  ILE A 175   O  ALA A 214           
SHEET    7   B 8 LEU A 144  ILE A 148  1  N  SER A 147   O  LEU A 174           
SHEET    8   B 8 ILE A 357  ASN A 359  1  O  ILE A 358   N  LEU A 144           
SHEET    1   C 4 ARG B  59  GLU B  65  0                                        
SHEET    2   C 4 GLN B  75  PRO B  83 -1  O  ALA B  81   N  ARG B  59           
SHEET    3   C 4 GLU B  12  THR B  20 -1  N  LEU B  19   O  ALA B  76           
SHEET    4   C 4 ILE B 108  HIS B 114 -1  O  HIS B 114   N  LEU B  14           
SHEET    1   D 8 PHE B 333  PRO B 336  0                                        
SHEET    2   D 8 PHE B 299  PHE B 302  1  N  SER B 300   O  VAL B 335           
SHEET    3   D 8 ILE B 264  ALA B 266  1  N  ALA B 266   O  LEU B 301           
SHEET    4   D 8 ALA B 238  PHE B 241  1  N  PHE B 241   O  MET B 265           
SHEET    5   D 8 LEU B 212  ASN B 216  1  N  VAL B 215   O  LEU B 240           
SHEET    6   D 8 LEU B 174  LYS B 176  1  N  ILE B 175   O  ALA B 214           
SHEET    7   D 8 LEU B 144  ILE B 148  1  N  SER B 147   O  LEU B 174           
SHEET    8   D 8 ILE B 357  ASN B 359  1  O  ILE B 358   N  LEU B 144           
SHEET    1   E 5 ARG C  59  GLU C  64  0                                        
SHEET    2   E 5 GLN C  75  PRO C  83 -1  O  THR C  79   N  ILE C  61           
SHEET    3   E 5 GLU C  12  THR C  20 -1  N  LEU C  19   O  ALA C  76           
SHEET    4   E 5 ILE C 108  HIS C 114 -1  O  HIS C 114   N  LEU C  14           
SHEET    5   E 5 GLY C 281  PHE C 282  1  O  GLY C 281   N  LEU C 110           
SHEET    1   F 8 PHE C 333  PRO C 336  0                                        
SHEET    2   F 8 PHE C 299  PHE C 302  1  N  SER C 300   O  PHE C 333           
SHEET    3   F 8 ILE C 264  ALA C 266  1  N  ALA C 266   O  LEU C 301           
SHEET    4   F 8 ALA C 238  PHE C 241  1  N  PHE C 241   O  MET C 265           
SHEET    5   F 8 LEU C 212  ASN C 216  1  N  VAL C 215   O  LEU C 240           
SHEET    6   F 8 LEU C 174  LYS C 176  1  N  ILE C 175   O  ALA C 214           
SHEET    7   F 8 LEU C 144  ILE C 148  1  N  SER C 147   O  LEU C 174           
SHEET    8   F 8 ILE C 357  ASN C 359  1  O  ILE C 358   N  MET C 146           
SHEET    1   G 5 ARG D  59  GLU D  64  0                                        
SHEET    2   G 5 VAL D  77  PRO D  83 -1  O  THR D  79   N  ILE D  61           
SHEET    3   G 5 GLU D  12  LEU D  19 -1  N  TYR D  17   O  ILE D  78           
SHEET    4   G 5 ILE D 108  HIS D 114 -1  O  ASP D 112   N  THR D  16           
SHEET    5   G 5 GLY D 281  PHE D 282  1  O  GLY D 281   N  LEU D 110           
SHEET    1   H 8 PHE D 333  PRO D 336  0                                        
SHEET    2   H 8 PHE D 299  PHE D 302  1  N  SER D 300   O  VAL D 335           
SHEET    3   H 8 ILE D 264  ALA D 266  1  N  ALA D 266   O  PHE D 299           
SHEET    4   H 8 ALA D 238  PHE D 241  1  N  LEU D 239   O  MET D 265           
SHEET    5   H 8 LEU D 212  ASN D 216  1  N  VAL D 215   O  LEU D 240           
SHEET    6   H 8 LEU D 174  LYS D 176  1  N  ILE D 175   O  LEU D 212           
SHEET    7   H 8 LEU D 144  ILE D 148  1  N  SER D 147   O  LYS D 176           
SHEET    8   H 8 ILE D 357  ASN D 359  1  O  ILE D 358   N  LEU D 144           
CISPEP   1 LEU B   45    PRO B   46          0        -1.13                     
CRYST1   79.334   91.466  106.967  90.00  90.82  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012605  0.000000  0.000180        0.00000                         
SCALE2      0.000000  0.010933  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009350        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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