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Database: PDB
Entry: 1EPV
LinkDB: 1EPV
Original site: 1EPV 
HEADER    ISOMERASE                               29-MAR-00   1EPV              
TITLE     ALANINE RACEMASE WITH BOUND INHIBITOR DERIVED FROM D-                 
TITLE    2 CYCLOSERINE                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;                 
SOURCE   3 ORGANISM_TAXID: 1422;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PMALR3                                    
KEYWDS    ALPHA-BETA BARREL, ISOMERASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.D.FENN,G.F.STAMPER,A.A.MOROLLO,D.RINGE                              
REVDAT   3   24-FEB-09 1EPV    1       VERSN                                    
REVDAT   2   16-SEP-03 1EPV    1       AUTHOR JRNL   REMARK MASTER              
REVDAT   2 2                   1       SOURCE                                   
REVDAT   1   14-JAN-03 1EPV    0                                                
JRNL        AUTH   T.D.FENN,G.F.STAMPER,A.A.MOROLLO,D.RINGE                     
JRNL        TITL   A SIDE REACTION OF ALANINE RACEMASE:                         
JRNL        TITL 2 TRANSAMINATION OF CYCLOSERINE.                               
JRNL        REF    BIOCHEMISTRY                  V.  42  5775 2003              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   12741835                                                     
JRNL        DOI    10.1021/BI027022D                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 259525.850                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 34234                          
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) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2398                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4980                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2890                       
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 383                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6057                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 255                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.27                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.31                            
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) : 0.31                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.37                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.020                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.69                            
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        : 0.31                                                 
REMARK   3   BSOL        : 50.99                                                
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  : CSX.PAR                                        
REMARK   3  PARAMETER FILE  4  : KCX.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : CSX.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : KCX.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1EPV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB010799.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35816                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.790                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33900                            
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: NULL                         
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM ACETATE,  TRIS, PH      
REMARK 280  8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       49.57850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.63050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.12150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.63050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.57850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.12150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 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     GLY A   384                                                      
REMARK 465     GLU A   385                                                      
REMARK 465     SER A   386                                                      
REMARK 465     SER A   387                                                      
REMARK 465     ALA A   388                                                      
REMARK 465     GLY B   382                                                      
REMARK 465     ARG B   383                                                      
REMARK 465     GLY B   384                                                      
REMARK 465     GLU B   385                                                      
REMARK 465     SER B   386                                                      
REMARK 465     SER B   387                                                      
REMARK 465     ALA B   388                                                      
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     ARG A 383    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH2  ARG A   373     O    HOH A   460              1.44            
REMARK 500   O    HOH A   437     O    HOH A   629              1.53            
REMARK 500   NH2  ARG A   147     O    HOH A   419              1.64            
REMARK 500   O    HOH B   543     O    HOH B   544              1.96            
REMARK 500   O    TYR A   265     O    HOH A   546              2.05            
REMARK 500   O    HIS B   155     O    HOH B   565              2.07            
REMARK 500   NH1  ARG B   309     O    HOH B   653              2.07            
REMARK 500   O    ARG A   100     O    HOH A   427              2.09            
REMARK 500   OD2  ASP B    31     O    HOH B   447              2.12            
REMARK 500   N    ASN A     2     O    HOH A   440              2.14            
REMARK 500   OE2  GLU B   143     O    HOH B   633              2.15            
REMARK 500   O    HOH A   512     O    HOH B   554              2.18            
REMARK 500   OD1  ASP A   171     O    HOH A   449              2.19            
REMARK 500   O    ARG A   309     O    HOH A   468              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG A    26     O    PRO A   320     3546     1.72            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO A  29   C     ASP A  30   N       0.173                       
REMARK 500    ASP A  30   C     ASP A  31   N       0.222                       
REMARK 500    PRO A  81   C     ILE A  82   N       0.273                       
REMARK 500    ILE A  82   C     LEU A  83   N       0.161                       
REMARK 500    PRO A  90   C     ALA A  91   N       0.148                       
REMARK 500    ALA A  91   C     ASP A  92   N       0.206                       
REMARK 500    ALA B 205   C     ALA B 206   N       0.340                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  29   O   -  C   -  N   ANGL. DEV. =  13.0 DEGREES          
REMARK 500    ASP A  30   CA  -  C   -  N   ANGL. DEV. =  16.9 DEGREES          
REMARK 500    ASP A  30   O   -  C   -  N   ANGL. DEV. = -18.6 DEGREES          
REMARK 500    ASP A  31   C   -  N   -  CA  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    PRO A  81   O   -  C   -  N   ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ILE A  82   O   -  C   -  N   ANGL. DEV. =  12.7 DEGREES          
REMARK 500    ASP A 141   CB  -  CA  -  C   ANGL. DEV. = -12.6 DEGREES          
REMARK 500    LEU A 192   CA  -  CB  -  CG  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    GLY A 232   CA  -  C   -  N   ANGL. DEV. =  26.2 DEGREES          
REMARK 500    GLY A 232   O   -  C   -  N   ANGL. DEV. = -27.1 DEGREES          
REMARK 500    ILE A 233   C   -  N   -  CA  ANGL. DEV. =  27.1 DEGREES          
REMARK 500    ARG A 347   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 347   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG B   6   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B   6   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    LEU B  27   CA  -  CB  -  CG  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    GLN B  98   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    ASP B 109   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 171   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG B 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    VAL B 307   N   -  CA  -  CB  ANGL. DEV. = -14.9 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    PHE A 106       -1.26   -145.62                                   
REMARK 500    SER A 119       69.33   -160.07                                   
REMARK 500    ARG A 136      -81.40    -96.96                                   
REMARK 500    CYS A 201      -37.68   -146.74                                   
REMARK 500    ASN A 203     -163.69   -103.60                                   
REMARK 500    PHE A 215     -128.11     62.04                                   
REMARK 500    SER A 264     -174.04     59.30                                   
REMARK 500    ALA A 267       56.94     33.37                                   
REMARK 500    THR A 273     -169.80   -118.32                                   
REMARK 500    PHE B 106       -8.09   -149.81                                   
REMARK 500    ARG B 136      -86.10    -94.40                                   
REMARK 500    CYS B 201      -30.98   -138.20                                   
REMARK 500    ARG B 213       49.89    -98.49                                   
REMARK 500    PHE B 215     -130.21     58.97                                   
REMARK 500    SER B 264     -164.17     69.50                                   
REMARK 500    THR B 273     -164.31   -119.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 362         0.10    SIDE_CHAIN                              
REMARK 500    TYR B 362         0.09    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLY A 232        -17.41                                           
REMARK 500    SER B 204         10.62                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCS A 1001                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCS B 1002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SFT   RELATED DB: PDB                                   
REMARK 900 ALANINE RACEMASE NATIVE                                              
DBREF  1EPV A    2   388  UNP    P10724   ALR_BACST        2    388             
DBREF  1EPV B    2   388  UNP    P10724   ALR_BACST        2    388             
SEQADV 1EPV KCX A  129  UNP  P10724    LYS   129 MODIFIED RESIDUE               
SEQADV 1EPV KCX B  129  UNP  P10724    LYS   129 MODIFIED RESIDUE               
SEQRES   1 A  387  ASN ASP PHE HIS ARG ASP THR TRP ALA GLU VAL ASP LEU          
SEQRES   2 A  387  ASP ALA ILE TYR ASP ASN VAL GLU ASN LEU ARG ARG LEU          
SEQRES   3 A  387  LEU PRO ASP ASP THR HIS ILE MET ALA VAL VAL LYS ALA          
SEQRES   4 A  387  ASN ALA TYR GLY HIS GLY ASP VAL GLN VAL ALA ARG THR          
SEQRES   5 A  387  ALA LEU GLU ALA GLY ALA SER ARG LEU ALA VAL ALA PHE          
SEQRES   6 A  387  LEU ASP GLU ALA LEU ALA LEU ARG GLU LYS GLY ILE GLU          
SEQRES   7 A  387  ALA PRO ILE LEU VAL LEU GLY ALA SER ARG PRO ALA ASP          
SEQRES   8 A  387  ALA ALA LEU ALA ALA GLN GLN ARG ILE ALA LEU THR VAL          
SEQRES   9 A  387  PHE ARG SER ASP TRP LEU GLU GLU ALA SER ALA LEU TYR          
SEQRES  10 A  387  SER GLY PRO PHE PRO ILE HIS PHE HIS LEU KCX MET ASP          
SEQRES  11 A  387  THR GLY MET GLY ARG LEU GLY VAL LYS ASP GLU GLU GLU          
SEQRES  12 A  387  THR LYS ARG ILE VAL ALA LEU ILE GLU ARG HIS PRO HIS          
SEQRES  13 A  387  PHE VAL LEU GLU GLY LEU TYR THR HIS PHE ALA THR ALA          
SEQRES  14 A  387  ASP GLU VAL ASN THR ASP TYR PHE SER TYR GLN TYR THR          
SEQRES  15 A  387  ARG PHE LEU HIS MET LEU GLU TRP LEU PRO SER ARG PRO          
SEQRES  16 A  387  PRO LEU VAL HIS CYS ALA ASN SER ALA ALA SER LEU ARG          
SEQRES  17 A  387  PHE PRO ASP ARG THR PHE ASN MET VAL ARG PHE GLY ILE          
SEQRES  18 A  387  ALA MET TYR GLY LEU ALA PRO SER PRO GLY ILE LYS PRO          
SEQRES  19 A  387  LEU LEU PRO TYR PRO LEU LYS GLU ALA PHE SER LEU HIS          
SEQRES  20 A  387  SER ARG LEU VAL HIS VAL LYS LYS LEU GLN PRO GLY GLU          
SEQRES  21 A  387  LYS VAL SER TYR GLY ALA THR TYR THR ALA GLN THR GLU          
SEQRES  22 A  387  GLU TRP ILE GLY THR ILE PRO ILE GLY TYR ALA ASP GLY          
SEQRES  23 A  387  TRP LEU ARG ARG LEU GLN HIS PHE HIS VAL LEU VAL ASP          
SEQRES  24 A  387  GLY GLN LYS ALA PRO ILE VAL GLY ARG ILE CYS MET ASP          
SEQRES  25 A  387  GLN CYS MET ILE ARG LEU PRO GLY PRO LEU PRO VAL GLY          
SEQRES  26 A  387  THR LYS VAL THR LEU ILE GLY ARG GLN GLY ASP GLU VAL          
SEQRES  27 A  387  ILE SER ILE ASP ASP VAL ALA ARG HIS LEU GLU THR ILE          
SEQRES  28 A  387  ASN TYR GLU VAL PRO CYS THR ILE SER TYR ARG VAL PRO          
SEQRES  29 A  387  ARG ILE PHE PHE ARG HIS LYS ARG ILE MET GLU VAL ARG          
SEQRES  30 A  387  ASN ALA ILE GLY ARG GLY GLU SER SER ALA                      
SEQRES   1 B  387  ASN ASP PHE HIS ARG ASP THR TRP ALA GLU VAL ASP LEU          
SEQRES   2 B  387  ASP ALA ILE TYR ASP ASN VAL GLU ASN LEU ARG ARG LEU          
SEQRES   3 B  387  LEU PRO ASP ASP THR HIS ILE MET ALA VAL VAL LYS ALA          
SEQRES   4 B  387  ASN ALA TYR GLY HIS GLY ASP VAL GLN VAL ALA ARG THR          
SEQRES   5 B  387  ALA LEU GLU ALA GLY ALA SER ARG LEU ALA VAL ALA PHE          
SEQRES   6 B  387  LEU ASP GLU ALA LEU ALA LEU ARG GLU LYS GLY ILE GLU          
SEQRES   7 B  387  ALA PRO ILE LEU VAL LEU GLY ALA SER ARG PRO ALA ASP          
SEQRES   8 B  387  ALA ALA LEU ALA ALA GLN GLN ARG ILE ALA LEU THR VAL          
SEQRES   9 B  387  PHE ARG SER ASP TRP LEU GLU GLU ALA SER ALA LEU TYR          
SEQRES  10 B  387  SER GLY PRO PHE PRO ILE HIS PHE HIS LEU KCX MET ASP          
SEQRES  11 B  387  THR GLY MET GLY ARG LEU GLY VAL LYS ASP GLU GLU GLU          
SEQRES  12 B  387  THR LYS ARG ILE VAL ALA LEU ILE GLU ARG HIS PRO HIS          
SEQRES  13 B  387  PHE VAL LEU GLU GLY LEU TYR THR HIS PHE ALA THR ALA          
SEQRES  14 B  387  ASP GLU VAL ASN THR ASP TYR PHE SER TYR GLN TYR THR          
SEQRES  15 B  387  ARG PHE LEU HIS MET LEU GLU TRP LEU PRO SER ARG PRO          
SEQRES  16 B  387  PRO LEU VAL HIS CYS ALA ASN SER ALA ALA SER LEU ARG          
SEQRES  17 B  387  PHE PRO ASP ARG THR PHE ASN MET VAL ARG PHE GLY ILE          
SEQRES  18 B  387  ALA MET TYR GLY LEU ALA PRO SER PRO GLY ILE LYS PRO          
SEQRES  19 B  387  LEU LEU PRO TYR PRO LEU LYS GLU ALA PHE SER LEU HIS          
SEQRES  20 B  387  SER ARG LEU VAL HIS VAL LYS LYS LEU GLN PRO GLY GLU          
SEQRES  21 B  387  LYS VAL SER TYR GLY ALA THR TYR THR ALA GLN THR GLU          
SEQRES  22 B  387  GLU TRP ILE GLY THR ILE PRO ILE GLY TYR ALA ASP GLY          
SEQRES  23 B  387  TRP LEU ARG ARG LEU GLN HIS PHE HIS VAL LEU VAL ASP          
SEQRES  24 B  387  GLY GLN LYS ALA PRO ILE VAL GLY ARG ILE CYS MET ASP          
SEQRES  25 B  387  GLN CYS MET ILE ARG LEU PRO GLY PRO LEU PRO VAL GLY          
SEQRES  26 B  387  THR LYS VAL THR LEU ILE GLY ARG GLN GLY ASP GLU VAL          
SEQRES  27 B  387  ILE SER ILE ASP ASP VAL ALA ARG HIS LEU GLU THR ILE          
SEQRES  28 B  387  ASN TYR GLU VAL PRO CYS THR ILE SER TYR ARG VAL PRO          
SEQRES  29 B  387  ARG ILE PHE PHE ARG HIS LYS ARG ILE MET GLU VAL ARG          
SEQRES  30 B  387  ASN ALA ILE GLY ARG GLY GLU SER SER ALA                      
MODRES 1EPV KCX A  129  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1EPV KCX B  129  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    KCX  A 129      12                                                       
HET    KCX  B 129      12                                                       
HET    DCS  A1001      22                                                       
HET    DCS  B1002      22                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     DCS D-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-            
HETNAM   2 DCS  YLMETHYL]-N,O-CYCLOSERYLAMIDE                                   
HETSYN     DCS D-PYRIDOXYL-N,O-CYCLOSERYLAMIDE-5-MONOPHOSPHATE                  
FORMUL   1  KCX    2(C7 H14 N2 O4)                                              
FORMUL   3  DCS    2(C11 H16 N3 O7 P)                                           
FORMUL   5  HOH   *255(H2 O)                                                    
HELIX    1   1 LEU A   14  LEU A   28  1                                  15    
HELIX    2   2 VAL A   38  HIS A   45  1                                   8    
HELIX    3   3 GLY A   46  GLY A   58  1                                  13    
HELIX    4   4 PHE A   66  LYS A   76  1                                  11    
HELIX    5   5 ARG A   89  ALA A   91  5                                   3    
HELIX    6   6 ASP A   92  GLN A   99  1                                   8    
HELIX    7   7 ARG A  107  ALA A  116  1                                  10    
HELIX    8   8 ASP A  141  HIS A  155  1                                  15    
HELIX    9   9 THR A  175  GLU A  190  1                                  16    
HELIX   10  10 ASN A  203  PHE A  210  1                                   8    
HELIX   11  11 PRO A  211  THR A  214  5                                   4    
HELIX   12  12 GLY A  221  GLY A  226  5                                   6    
HELIX   13  13 ILE A  233  LEU A  237  5                                   5    
HELIX   14  14 SER A  264  THR A  268  5                                   5    
HELIX   15  15 GLY A  283  GLY A  287  5                                   5    
HELIX   16  16 LEU A  289  HIS A  294  5                                   6    
HELIX   17  17 SER A  341  GLU A  350  1                                  10    
HELIX   18  18 TYR A  354  ILE A  360  1                                   7    
HELIX   19  19 LEU B   14  LEU B   28  1                                  15    
HELIX   20  20 VAL B   38  HIS B   45  1                                   8    
HELIX   21  21 GLY B   46  GLY B   58  1                                  13    
HELIX   22  22 PHE B   66  LYS B   76  1                                  11    
HELIX   23  23 ARG B   89  ALA B   91  5                                   3    
HELIX   24  24 ASP B   92  GLN B   99  1                                   8    
HELIX   25  25 ARG B  107  TYR B  118  1                                  12    
HELIX   26  26 ASP B  141  ARG B  154  1                                  14    
HELIX   27  27 THR B  175  LEU B  189  1                                  15    
HELIX   28  28 GLU B  190  LEU B  192  5                                   3    
HELIX   29  29 ASN B  203  PHE B  210  1                                   8    
HELIX   30  30 GLY B  221  GLY B  226  5                                   6    
HELIX   31  31 ILE B  233  LEU B  237  5                                   5    
HELIX   32  32 SER B  264  THR B  268  5                                   5    
HELIX   33  33 GLY B  283  GLY B  287  5                                   5    
HELIX   34  34 LEU B  289  HIS B  294  5                                   6    
HELIX   35  35 SER B  341  GLU B  350  1                                  10    
HELIX   36  36 TYR B  354  ILE B  360  1                                   7    
SHEET    1   A10 ARG A 373  ARG A 378  0                                        
SHEET    2   A10 ARG A 366  ARG A 370 -1  N  ARG A 366   O  ARG A 378           
SHEET    3   A10 THR A   8  ASP A  13  1  O  ALA A  10   N  ILE A 367           
SHEET    4   A10 PHE A 245  ARG A 250 -1  O  SER A 246   N  GLU A  11           
SHEET    5   A10 LYS A 328  GLN A 335 -1  O  VAL A 329   N  SER A 249           
SHEET    6   A10 HIS A 296  VAL A 299 -1  N  LEU A 298   O  THR A 330           
SHEET    7   A10 GLN A 302  VAL A 307 -1  O  GLN A 302   N  VAL A 299           
SHEET    8   A10 CYS A 315  ARG A 318 -1  O  MET A 316   N  VAL A 307           
SHEET    9   A10 GLU A 275  ILE A 280 -1  N  GLY A 278   O  ILE A 317           
SHEET   10   A10 HIS A 253  LEU A 257 -1  O  HIS A 253   N  THR A 279           
SHEET    1   B 6 ARG A 373  ARG A 378  0                                        
SHEET    2   B 6 ARG A 366  ARG A 370 -1  N  ARG A 366   O  ARG A 378           
SHEET    3   B 6 THR A   8  ASP A  13  1  O  ALA A  10   N  ILE A 367           
SHEET    4   B 6 PHE A 245  ARG A 250 -1  O  SER A 246   N  GLU A  11           
SHEET    5   B 6 LYS A 328  GLN A 335 -1  O  VAL A 329   N  SER A 249           
SHEET    6   B 6 GLU A 338  ILE A 340 -1  O  GLU A 338   N  GLN A 335           
SHEET    1   C 9 HIS A  33  VAL A  37  0                                        
SHEET    2   C 9 ARG A  61  VAL A  64  1  O  ARG A  61   N  ALA A  36           
SHEET    3   C 9 ILE A  82  VAL A  84  1  O  LEU A  83   N  VAL A  64           
SHEET    4   C 9 ILE A 101  THR A 104 -1  N  ALA A 102   O  ILE A  82           
SHEET    5   C 9 ILE A 124  LEU A 128  1  O  HIS A 125   N  LEU A 103           
SHEET    6   C 9 PHE A 158  TYR A 164  1  N  VAL A 159   O  ILE A 124           
SHEET    7   C 9 LEU A 198  HIS A 200  1  N  LEU A 198   O  GLU A 161           
SHEET    8   C 9 MET A 217  PHE A 220 -1  N  MET A 217   O  VAL A 199           
SHEET    9   C 9 HIS A  33  VAL A  37  1  O  HIS A  33   N  VAL A 218           
SHEET    1   D 2 LYS A 262  VAL A 263  0                                        
SHEET    2   D 2 TYR A 269  THR A 270 -1  O  TYR A 269   N  VAL A 263           
SHEET    1   E10 ARG B 373  ARG B 378  0                                        
SHEET    2   E10 ARG B 366  ARG B 370 -1  O  ARG B 366   N  ARG B 378           
SHEET    3   E10 THR B   8  ASP B  13  1  O  ALA B  10   N  ILE B 367           
SHEET    4   E10 PHE B 245  ARG B 250 -1  O  SER B 246   N  GLU B  11           
SHEET    5   E10 LYS B 328  GLN B 335 -1  N  VAL B 329   O  SER B 249           
SHEET    6   E10 HIS B 296  VAL B 299 -1  O  LEU B 298   N  THR B 330           
SHEET    7   E10 GLN B 302  VAL B 307 -1  O  GLN B 302   N  VAL B 299           
SHEET    8   E10 CYS B 315  ARG B 318 -1  O  MET B 316   N  VAL B 307           
SHEET    9   E10 GLU B 275  ILE B 280 -1  N  GLY B 278   O  ILE B 317           
SHEET   10   E10 HIS B 253  LEU B 257 -1  O  HIS B 253   N  THR B 279           
SHEET    1   F 6 ARG B 373  ARG B 378  0                                        
SHEET    2   F 6 ARG B 366  ARG B 370 -1  O  ARG B 366   N  ARG B 378           
SHEET    3   F 6 THR B   8  ASP B  13  1  O  ALA B  10   N  ILE B 367           
SHEET    4   F 6 PHE B 245  ARG B 250 -1  O  SER B 246   N  GLU B  11           
SHEET    5   F 6 LYS B 328  GLN B 335 -1  N  VAL B 329   O  SER B 249           
SHEET    6   F 6 GLU B 338  ILE B 340 -1  O  GLU B 338   N  GLN B 335           
SHEET    1   G 9 HIS B  33  VAL B  37  0                                        
SHEET    2   G 9 ARG B  61  VAL B  64  1  O  ARG B  61   N  ALA B  36           
SHEET    3   G 9 ILE B  82  VAL B  84  1  O  LEU B  83   N  VAL B  64           
SHEET    4   G 9 ILE B 101  THR B 104  1  N  ALA B 102   O  ILE B  82           
SHEET    5   G 9 ILE B 124  LEU B 128  1  O  HIS B 125   N  LEU B 103           
SHEET    6   G 9 PHE B 158  TYR B 164  1  O  VAL B 159   N  PHE B 126           
SHEET    7   G 9 LEU B 198  HIS B 200  1  O  LEU B 198   N  LEU B 163           
SHEET    8   G 9 MET B 217  PHE B 220  1  N  MET B 217   O  VAL B 199           
SHEET    9   G 9 HIS B  33  VAL B  37  1  O  HIS B  33   N  VAL B 218           
SHEET    1   H 2 LYS B 262  VAL B 263  0                                        
SHEET    2   H 2 TYR B 269  THR B 270 -1  O  TYR B 269   N  VAL B 263           
LINK         C   LEU A 128                 N   KCX A 129     1555   1555  1.33  
LINK         C   KCX A 129                 N   MET A 130     1555   1555  1.49  
LINK         OG  SER A 204                 O3P DCS A1001     1555   1555  1.98  
LINK         C   LEU B 128                 N   KCX B 129     1555   1555  1.31  
LINK         C   KCX B 129                 N   MET B 130     1555   1555  1.73  
LINK         NH1 ARG B 136                 O   DCS B1002     1555   1555  1.85  
LINK         OG  SER B 204                 O3P DCS B1002     1555   1555  1.99  
CISPEP   1 GLY A  120    PRO A  121          0         6.78                     
CISPEP   2 GLY B  120    PRO B  121          0        -1.49                     
SITE     1 AC1 20 LYS A  39  TYR A  43  LEU A  85  ARG A 136                    
SITE     2 AC1 20 HIS A 166  ASN A 203  SER A 204  ARG A 219                    
SITE     3 AC1 20 GLY A 221  ILE A 222  TYR A 354  HOH A 506                    
SITE     4 AC1 20 HOH A 518  HOH A 556  HOH A 589  HOH A 599                    
SITE     5 AC1 20 TYR B 265  TYR B 284  CYS B 311  MET B 312                    
SITE     1 AC2 19 TYR A 265  TYR A 284  CYS A 311  MET A 312                    
SITE     2 AC2 19 HOH A 469  LYS B  39  TYR B  43  ARG B 136                    
SITE     3 AC2 19 HIS B 166  ASN B 203  SER B 204  ARG B 219                    
SITE     4 AC2 19 GLY B 221  ILE B 222  TYR B 354  HOH B 401                    
SITE     5 AC2 19 HOH B 527  HOH B 557  HOH B 595                               
CRYST1   99.157   90.243   85.261  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010085  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011081  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011729        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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