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Database: PDB
Entry: 3E6E
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Original site: 3E6E 
HEADER    ISOMERASE                               15-AUG-08   3E6E              
TITLE     CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM E.FAECALIS                 
TITLE    2 COMPLEX WITH CYCLOSERINE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE;                                          
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS;                          
SOURCE   3 ORGANISM_COMMON: STREPTOCOCCUS FAECALIS;                             
SOURCE   4 ORGANISM_TAXID: 1351;                                                
SOURCE   5 STRAIN: V583;                                                        
SOURCE   6 GENE: ALR, EF_0849;                                                  
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ALR, SCP, ISOMERASE, PYRIDOXAL PHOSPHATE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.Y.HWANG,A.PRIYADARSHI,E.H.LEE,M.W.SUNG                              
REVDAT   2   01-SEP-09 3E6E    1       JRNL                                     
REVDAT   1   18-AUG-09 3E6E    0                                                
JRNL        AUTH   A.PRIYADARSHI,E.H.LEE,M.W.SUNG,K.H.NAM,W.H.LEE,              
JRNL        AUTH 2 E.E.KIM,K.Y.HWANG                                            
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE ALANINE RACEMASE FROM           
JRNL        TITL 2 ENTEROCOCCUS FAECALIS.                                       
JRNL        REF    BIOCHIM.BIOPHYS.ACTA          V.1794  1030 2009              
JRNL        REFN                   ISSN 0006-3002                               
JRNL        PMID   19328247                                                     
JRNL        DOI    10.1016/J.BBAPAP.2009.03.006                                 
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 35274                          
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) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 5                               
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 50.00                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200                       
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 2141                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8637                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 10.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3E6E COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-AUG-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB048932.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 4                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 4A                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35274                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : 0.10200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.31400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.840                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 3E5P                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8K, CA(OAC)2, HEPES, SCP,             
REMARK 280  CYCLOHEXYL-METHYL-BETA-D-MALTOSIDE, PH 8.0, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 295K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.46500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.46500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       47.29850            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       78.09300            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       47.29850            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       78.09300            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       73.46500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       47.29850            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       78.09300            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       73.46500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       47.29850            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       78.09300            
REMARK 290   SMTRY3   8  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET C     1                                                      
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   O3P  DCS C   372     O    HOH C   374              2.15            
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    GLU A  31   CB  -  CA  -  C   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    GLY A  32   N   -  CA  -  C   ANGL. DEV. = -17.5 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    PRO A   8       -1.74    -57.85                                   
REMARK 500    PRO A  30       -3.16    -47.96                                   
REMARK 500    GLU A  31        5.41     54.15                                   
REMARK 500    LEU A  91      -31.90    -36.70                                   
REMARK 500    ASP A 101       60.25     37.00                                   
REMARK 500    PRO A 121      -58.24    -29.50                                   
REMARK 500    GLU A 122       52.36   -118.55                                   
REMARK 500    SER A 123        1.19    -65.21                                   
REMARK 500    ASN A 124        0.36     49.65                                   
REMARK 500    MET A 137      -29.15    107.30                                   
REMARK 500    ARG A 139      -53.83   -126.69                                   
REMARK 500    LYS A 159        1.04     81.12                                   
REMARK 500    LEU A 162      -40.29   -139.98                                   
REMARK 500    TRP A 163       75.49     64.07                                   
REMARK 500    GLU A 197      155.21    157.61                                   
REMARK 500    ASN A 231      106.01    -53.39                                   
REMARK 500    PRO A 232        3.74    -56.64                                   
REMARK 500    ASN A 235       18.92   -151.41                                   
REMARK 500    ALA A 242      109.77    -58.59                                   
REMARK 500    SER A 251     -160.10   -164.43                                   
REMARK 500    ALA A 261      140.21    -39.19                                   
REMARK 500    GLU A 269       38.54     78.81                                   
REMARK 500    ALA A 275     -166.15   -166.83                                   
REMARK 500    GLU A 323     -150.89   -177.23                                   
REMARK 500    ASP A 337      111.56   -167.83                                   
REMARK 500    GLU A 352       31.43     70.28                                   
REMARK 500    THR A 353     -153.42   -139.61                                   
REMARK 500    GLU B  31       72.43    -69.35                                   
REMARK 500    ALA B  48      -70.42    -42.82                                   
REMARK 500    ASP B 101       77.67     42.60                                   
REMARK 500    LEU B 119       55.81   -115.32                                   
REMARK 500    GLU B 122     -136.16     49.39                                   
REMARK 500    ARG B 139      -77.32    -95.01                                   
REMARK 500    TRP B 163       85.41    -66.37                                   
REMARK 500    ALA B 193       -9.65    -56.57                                   
REMARK 500    GLU B 196      -61.32    -97.39                                   
REMARK 500    PRO B 199     -167.23    -78.51                                   
REMARK 500    VAL B 204       15.32   -144.55                                   
REMARK 500    HIS B 213       50.33   -152.77                                   
REMARK 500    ASN B 235        2.23   -152.15                                   
REMARK 500    THR B 353     -152.06   -123.02                                   
REMARK 500    PHE B 362      109.09    -53.75                                   
REMARK 500    HIS C   6       46.34    -96.05                                   
REMARK 500    PRO C   8       -9.96    -57.17                                   
REMARK 500    LYS C  57       -9.86    -52.20                                   
REMARK 500    GLN C 118       33.14     35.62                                   
REMARK 500    GLU C 160        2.59    -67.95                                   
REMARK 500    PRO C 199     -177.42    -68.34                                   
REMARK 500    VAL C 204      -18.71   -144.65                                   
REMARK 500    HIS C 213       65.63   -154.04                                   
REMARK 500    PRO C 217      173.71    -51.62                                   
REMARK 500    ASN C 235       -9.93   -146.23                                   
REMARK 500    SER C 251     -154.71   -154.10                                   
REMARK 500    GLU C 269       56.63     33.50                                   
REMARK 500    ALA C 275     -165.43   -173.69                                   
REMARK 500    HIS C 293        2.07    -67.64                                   
REMARK 500    GLU C 324      147.57    -38.52                                   
REMARK 500    ASP C 337       97.01   -167.11                                   
REMARK 500    THR C 353     -153.18   -137.42                                   
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 LYS A  159     GLU A  160                  147.69                    
REMARK 500 LEU B   29     PRO B   30                  -64.33                    
REMARK 500 SER B  123     ASN B  124                  147.08                    
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 372                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCS B 372                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCS C 372                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3E5P   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN COMPLEX WITH CYCLOSERINE                                
DBREF  3E6E A    1   371  UNP    Q837J0   Q837J0_ENTFA     1    371             
DBREF  3E6E B    1   371  UNP    Q837J0   Q837J0_ENTFA     1    371             
DBREF  3E6E C    1   371  UNP    Q837J0   Q837J0_ENTFA     1    371             
SEQADV 3E6E PRO A  329  UNP  Q837J0    SER   329 ENGINEERED                     
SEQADV 3E6E PRO B  329  UNP  Q837J0    SER   329 ENGINEERED                     
SEQADV 3E6E PRO C  329  UNP  Q837J0    SER   329 ENGINEERED                     
SEQRES   1 A  371  MET VAL VAL GLY TRP HIS ARG PRO THR ARG LEU HIS ILE          
SEQRES   2 A  371  ASP THR GLN ALA ILE THR GLU ASN VAL GLN LYS GLU CYS          
SEQRES   3 A  371  GLN ARG LEU PRO GLU GLY THR ALA LEU PHE ALA VAL VAL          
SEQRES   4 A  371  LYS ALA ASN GLY TYR GLY HIS GLY ALA VAL GLU SER ALA          
SEQRES   5 A  371  LYS ALA ALA LYS LYS GLY GLY ALA THR GLY PHE CYS VAL          
SEQRES   6 A  371  ALA LEU LEU ASP GLU ALA ILE GLU LEU ARG GLU ALA GLY          
SEQRES   7 A  371  VAL GLN ASP PRO ILE LEU ILE LEU SER VAL VAL ASP LEU          
SEQRES   8 A  371  ALA TYR VAL PRO LEU LEU ILE GLN TYR ASP LEU SER VAL          
SEQRES   9 A  371  THR VAL ALA THR GLN GLU TRP LEU GLU ALA ALA LEU GLN          
SEQRES  10 A  371  GLN LEU THR PRO GLU SER ASN THR PRO LEU ARG VAL HIS          
SEQRES  11 A  371  LEU LYS VAL ASP THR GLY MET GLY ARG ILE GLY PHE LEU          
SEQRES  12 A  371  THR PRO GLU GLU THR LYS GLN ALA VAL ARG PHE VAL GLN          
SEQRES  13 A  371  SER HIS LYS GLU PHE LEU TRP GLU GLY ILE PHE THR HIS          
SEQRES  14 A  371  PHE SER THR ALA ASP GLU ILE ASP THR SER TYR PHE GLU          
SEQRES  15 A  371  LYS GLN ALA GLY ARG PHE LYS ALA VAL LEU ALA VAL LEU          
SEQRES  16 A  371  GLU GLU LEU PRO ARG TYR VAL HIS VAL SER ASN SER ALA          
SEQRES  17 A  371  THR ALA LEU TRP HIS PRO ASP VAL PRO GLY ASN MET ILE          
SEQRES  18 A  371  ARG TYR GLY VAL ALA MET TYR GLY LEU ASN PRO SER GLY          
SEQRES  19 A  371  ASN LYS LEU ALA PRO SER TYR ALA LEU LYS PRO ALA LEU          
SEQRES  20 A  371  ARG LEU THR SER GLU LEU ILE HIS VAL LYS ARG LEU ALA          
SEQRES  21 A  371  ALA GLY GLU GLY ILE GLY TYR GLY GLU THR TYR VAL THR          
SEQRES  22 A  371  GLU ALA GLU GLU TRP ILE GLY THR VAL PRO ILE GLY TYR          
SEQRES  23 A  371  ALA ASP GLY TRP LEU ARG HIS LEU GLN GLY PHE THR VAL          
SEQRES  24 A  371  LEU VAL ASN GLY LYS ARG CYS GLU ILE VAL GLY ARG VAL          
SEQRES  25 A  371  CYS MET ASP GLN CYS MET ILE ARG LEU ALA GLU GLU VAL          
SEQRES  26 A  371  PRO VAL GLY PRO VAL VAL THR LEU VAL GLY LYS ASP GLY          
SEQRES  27 A  371  ASN GLU GLU ASN THR LEU GLN MET VAL ALA GLU LYS LEU          
SEQRES  28 A  371  GLU THR ILE HIS TYR GLU VAL ALA CYS THR PHE SER GLN          
SEQRES  29 A  371  ARG ILE PRO ARG GLU TYR ASN                                  
SEQRES   1 B  371  MET VAL VAL GLY TRP HIS ARG PRO THR ARG LEU HIS ILE          
SEQRES   2 B  371  ASP THR GLN ALA ILE THR GLU ASN VAL GLN LYS GLU CYS          
SEQRES   3 B  371  GLN ARG LEU PRO GLU GLY THR ALA LEU PHE ALA VAL VAL          
SEQRES   4 B  371  LYS ALA ASN GLY TYR GLY HIS GLY ALA VAL GLU SER ALA          
SEQRES   5 B  371  LYS ALA ALA LYS LYS GLY GLY ALA THR GLY PHE CYS VAL          
SEQRES   6 B  371  ALA LEU LEU ASP GLU ALA ILE GLU LEU ARG GLU ALA GLY          
SEQRES   7 B  371  VAL GLN ASP PRO ILE LEU ILE LEU SER VAL VAL ASP LEU          
SEQRES   8 B  371  ALA TYR VAL PRO LEU LEU ILE GLN TYR ASP LEU SER VAL          
SEQRES   9 B  371  THR VAL ALA THR GLN GLU TRP LEU GLU ALA ALA LEU GLN          
SEQRES  10 B  371  GLN LEU THR PRO GLU SER ASN THR PRO LEU ARG VAL HIS          
SEQRES  11 B  371  LEU LYS VAL ASP THR GLY MET GLY ARG ILE GLY PHE LEU          
SEQRES  12 B  371  THR PRO GLU GLU THR LYS GLN ALA VAL ARG PHE VAL GLN          
SEQRES  13 B  371  SER HIS LYS GLU PHE LEU TRP GLU GLY ILE PHE THR HIS          
SEQRES  14 B  371  PHE SER THR ALA ASP GLU ILE ASP THR SER TYR PHE GLU          
SEQRES  15 B  371  LYS GLN ALA GLY ARG PHE LYS ALA VAL LEU ALA VAL LEU          
SEQRES  16 B  371  GLU GLU LEU PRO ARG TYR VAL HIS VAL SER ASN SER ALA          
SEQRES  17 B  371  THR ALA LEU TRP HIS PRO ASP VAL PRO GLY ASN MET ILE          
SEQRES  18 B  371  ARG TYR GLY VAL ALA MET TYR GLY LEU ASN PRO SER GLY          
SEQRES  19 B  371  ASN LYS LEU ALA PRO SER TYR ALA LEU LYS PRO ALA LEU          
SEQRES  20 B  371  ARG LEU THR SER GLU LEU ILE HIS VAL LYS ARG LEU ALA          
SEQRES  21 B  371  ALA GLY GLU GLY ILE GLY TYR GLY GLU THR TYR VAL THR          
SEQRES  22 B  371  GLU ALA GLU GLU TRP ILE GLY THR VAL PRO ILE GLY TYR          
SEQRES  23 B  371  ALA ASP GLY TRP LEU ARG HIS LEU GLN GLY PHE THR VAL          
SEQRES  24 B  371  LEU VAL ASN GLY LYS ARG CYS GLU ILE VAL GLY ARG VAL          
SEQRES  25 B  371  CYS MET ASP GLN CYS MET ILE ARG LEU ALA GLU GLU VAL          
SEQRES  26 B  371  PRO VAL GLY PRO VAL VAL THR LEU VAL GLY LYS ASP GLY          
SEQRES  27 B  371  ASN GLU GLU ASN THR LEU GLN MET VAL ALA GLU LYS LEU          
SEQRES  28 B  371  GLU THR ILE HIS TYR GLU VAL ALA CYS THR PHE SER GLN          
SEQRES  29 B  371  ARG ILE PRO ARG GLU TYR ASN                                  
SEQRES   1 C  371  MET VAL VAL GLY TRP HIS ARG PRO THR ARG LEU HIS ILE          
SEQRES   2 C  371  ASP THR GLN ALA ILE THR GLU ASN VAL GLN LYS GLU CYS          
SEQRES   3 C  371  GLN ARG LEU PRO GLU GLY THR ALA LEU PHE ALA VAL VAL          
SEQRES   4 C  371  LYS ALA ASN GLY TYR GLY HIS GLY ALA VAL GLU SER ALA          
SEQRES   5 C  371  LYS ALA ALA LYS LYS GLY GLY ALA THR GLY PHE CYS VAL          
SEQRES   6 C  371  ALA LEU LEU ASP GLU ALA ILE GLU LEU ARG GLU ALA GLY          
SEQRES   7 C  371  VAL GLN ASP PRO ILE LEU ILE LEU SER VAL VAL ASP LEU          
SEQRES   8 C  371  ALA TYR VAL PRO LEU LEU ILE GLN TYR ASP LEU SER VAL          
SEQRES   9 C  371  THR VAL ALA THR GLN GLU TRP LEU GLU ALA ALA LEU GLN          
SEQRES  10 C  371  GLN LEU THR PRO GLU SER ASN THR PRO LEU ARG VAL HIS          
SEQRES  11 C  371  LEU LYS VAL ASP THR GLY MET GLY ARG ILE GLY PHE LEU          
SEQRES  12 C  371  THR PRO GLU GLU THR LYS GLN ALA VAL ARG PHE VAL GLN          
SEQRES  13 C  371  SER HIS LYS GLU PHE LEU TRP GLU GLY ILE PHE THR HIS          
SEQRES  14 C  371  PHE SER THR ALA ASP GLU ILE ASP THR SER TYR PHE GLU          
SEQRES  15 C  371  LYS GLN ALA GLY ARG PHE LYS ALA VAL LEU ALA VAL LEU          
SEQRES  16 C  371  GLU GLU LEU PRO ARG TYR VAL HIS VAL SER ASN SER ALA          
SEQRES  17 C  371  THR ALA LEU TRP HIS PRO ASP VAL PRO GLY ASN MET ILE          
SEQRES  18 C  371  ARG TYR GLY VAL ALA MET TYR GLY LEU ASN PRO SER GLY          
SEQRES  19 C  371  ASN LYS LEU ALA PRO SER TYR ALA LEU LYS PRO ALA LEU          
SEQRES  20 C  371  ARG LEU THR SER GLU LEU ILE HIS VAL LYS ARG LEU ALA          
SEQRES  21 C  371  ALA GLY GLU GLY ILE GLY TYR GLY GLU THR TYR VAL THR          
SEQRES  22 C  371  GLU ALA GLU GLU TRP ILE GLY THR VAL PRO ILE GLY TYR          
SEQRES  23 C  371  ALA ASP GLY TRP LEU ARG HIS LEU GLN GLY PHE THR VAL          
SEQRES  24 C  371  LEU VAL ASN GLY LYS ARG CYS GLU ILE VAL GLY ARG VAL          
SEQRES  25 C  371  CYS MET ASP GLN CYS MET ILE ARG LEU ALA GLU GLU VAL          
SEQRES  26 C  371  PRO VAL GLY PRO VAL VAL THR LEU VAL GLY LYS ASP GLY          
SEQRES  27 C  371  ASN GLU GLU ASN THR LEU GLN MET VAL ALA GLU LYS LEU          
SEQRES  28 C  371  GLU THR ILE HIS TYR GLU VAL ALA CYS THR PHE SER GLN          
SEQRES  29 C  371  ARG ILE PRO ARG GLU TYR ASN                                  
HET    DCS  A 372      22                                                       
HET    DCS  B 372      22                                                       
HET    DCS  C 372      22                                                       
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   4  DCS    3(C11 H16 N3 O7 P)                                           
FORMUL   7  HOH   *130(H2 O)                                                    
HELIX    1   1 ASP A   14  LEU A   29  1                                  16    
HELIX    2   2 VAL A   39  GLY A   45  1                                   7    
HELIX    3   3 GLY A   47  LYS A   57  1                                  11    
HELIX    4   4 LEU A   67  ALA A   77  1                                  11    
HELIX    5   5 ASP A   90  ALA A   92  5                                   3    
HELIX    6   6 TYR A   93  TYR A  100  1                                   8    
HELIX    7   7 THR A  108  GLN A  118  1                                  11    
HELIX    8   8 THR A  144  LYS A  159  1                                  16    
HELIX    9   9 THR A  178  VAL A  194  1                                  17    
HELIX   10  10 ASN A  206  HIS A  213  1                                   8    
HELIX   11  11 GLY A  224  GLY A  229  5                                   6    
HELIX   12  12 GLY A  266  THR A  270  5                                   5    
HELIX   13  13 LEU A  291  GLN A  295  5                                   5    
HELIX   14  14 THR A  343  GLU A  352  1                                  10    
HELIX   15  15 ILE A  354  PHE A  362  1                                   9    
HELIX   16  16 ASP B   14  LEU B   29  1                                  16    
HELIX   17  17 VAL B   39  GLY B   45  1                                   7    
HELIX   18  18 GLY B   47  GLY B   59  1                                  13    
HELIX   19  19 LEU B   67  ALA B   77  1                                  11    
HELIX   20  20 ASP B   90  VAL B   94  5                                   5    
HELIX   21  21 PRO B   95  TYR B  100  1                                   6    
HELIX   22  22 THR B  108  LEU B  116  1                                   9    
HELIX   23  23 THR B  144  SER B  157  1                                  14    
HELIX   24  24 THR B  178  ALA B  193  1                                  16    
HELIX   25  25 ASN B  206  HIS B  213  1                                   8    
HELIX   26  26 GLY B  224  GLY B  229  5                                   6    
HELIX   27  27 GLY B  266  THR B  270  5                                   5    
HELIX   28  28 LEU B  291  GLN B  295  5                                   5    
HELIX   29  29 THR B  343  LEU B  351  1                                   9    
HELIX   30  30 ILE B  354  PHE B  362  1                                   9    
HELIX   31  31 ASP C   14  GLN C   27  1                                  14    
HELIX   32  32 VAL C   39  HIS C   46  1                                   8    
HELIX   33  33 GLY C   47  LYS C   57  1                                  11    
HELIX   34  34 LEU C   67  ALA C   77  1                                  11    
HELIX   35  35 ASP C   90  ALA C   92  5                                   3    
HELIX   36  36 TYR C   93  TYR C  100  1                                   8    
HELIX   37  37 THR C  108  GLN C  117  1                                  10    
HELIX   38  38 THR C  144  SER C  157  1                                  14    
HELIX   39  39 THR C  178  ALA C  193  1                                  16    
HELIX   40  40 ASN C  206  HIS C  213  1                                   8    
HELIX   41  41 GLY C  224  GLY C  229  5                                   6    
HELIX   42  42 GLY C  266  THR C  270  5                                   5    
HELIX   43  43 LEU C  291  GLN C  295  5                                   5    
HELIX   44  44 THR C  343  GLU C  352  1                                  10    
HELIX   45  45 ILE C  354  PHE C  362  1                                   9    
SHEET    1   A 7 HIS A 255  LEU A 259  0                                        
SHEET    2   A 7 GLU A 277  VAL A 282 -1  O  GLU A 277   N  LEU A 259           
SHEET    3   A 7 CYS A 317  LEU A 321 -1  O  ILE A 319   N  GLY A 280           
SHEET    4   A 7 LYS A 304  VAL A 309 -1  N  GLU A 307   O  ARG A 320           
SHEET    5   A 7 THR A 298  VAL A 301 -1  N  VAL A 299   O  CYS A 306           
SHEET    6   A 7 VAL A 330  ASP A 337 -1  O  THR A 332   N  LEU A 300           
SHEET    7   A 7 GLU A 340  ASN A 342 -1  O  ASN A 342   N  GLY A 335           
SHEET    1   B 9 HIS A 255  LEU A 259  0                                        
SHEET    2   B 9 GLU A 277  VAL A 282 -1  O  GLU A 277   N  LEU A 259           
SHEET    3   B 9 CYS A 317  LEU A 321 -1  O  ILE A 319   N  GLY A 280           
SHEET    4   B 9 LYS A 304  VAL A 309 -1  N  GLU A 307   O  ARG A 320           
SHEET    5   B 9 THR A 298  VAL A 301 -1  N  VAL A 299   O  CYS A 306           
SHEET    6   B 9 VAL A 330  ASP A 337 -1  O  THR A 332   N  LEU A 300           
SHEET    7   B 9 LEU A 249  GLU A 252 -1  N  SER A 251   O  VAL A 331           
SHEET    8   B 9 ARG A  10  HIS A  12 -1  N  ARG A  10   O  THR A 250           
SHEET    9   B 9 ARG A 368  GLU A 369  1  O  GLU A 369   N  LEU A  11           
SHEET    1   C 8 TYR A 201  HIS A 203  0                                        
SHEET    2   C 8 GLY A 165  PHE A 167  1  N  ILE A 166   O  HIS A 203           
SHEET    3   C 8 VAL A 129  LYS A 132  1  N  LEU A 131   O  GLY A 165           
SHEET    4   C 8 SER A 103  VAL A 106  1  N  VAL A 104   O  HIS A 130           
SHEET    5   C 8 ILE A  83  ILE A  85  1  N  ILE A  85   O  SER A 103           
SHEET    6   C 8 GLY A  62  VAL A  65  1  N  PHE A  63   O  LEU A  84           
SHEET    7   C 8 ALA A  34  VAL A  38  1  N  ALA A  37   O  GLY A  62           
SHEET    8   C 8 MET A 220  TYR A 223  1  O  ILE A 221   N  PHE A  36           
SHEET    1   D 2 GLY A 264  ILE A 265  0                                        
SHEET    2   D 2 TYR A 271  VAL A 272 -1  O  TYR A 271   N  ILE A 265           
SHEET    1   E 5 GLU B 340  ASN B 342  0                                        
SHEET    2   E 5 VAL B 330  ASP B 337 -1  N  ASP B 337   O  GLU B 340           
SHEET    3   E 5 LEU B 247  GLU B 252 -1  N  SER B 251   O  VAL B 331           
SHEET    4   E 5 ARG B  10  ILE B  13 -1  N  ARG B  10   O  THR B 250           
SHEET    5   E 5 ARG B 368  TYR B 370  1  O  GLU B 369   N  LEU B  11           
SHEET    1   F 9 ALA B  34  VAL B  38  0                                        
SHEET    2   F 9 ALA B  60  VAL B  65  1  O  THR B  61   N  LEU B  35           
SHEET    3   F 9 ILE B  83  ILE B  85  1  O  LEU B  84   N  PHE B  63           
SHEET    4   F 9 SER B 103  VAL B 106  1  O  SER B 103   N  ILE B  85           
SHEET    5   F 9 LEU B 127  LYS B 132  1  O  ARG B 128   N  VAL B 104           
SHEET    6   F 9 PHE B 161  PHE B 167  1  O  GLY B 165   N  LEU B 131           
SHEET    7   F 9 TYR B 201  SER B 205  1  O  TYR B 201   N  GLU B 164           
SHEET    8   F 9 MET B 220  TYR B 223  1  O  ARG B 222   N  SER B 205           
SHEET    9   F 9 ALA B  34  VAL B  38  1  N  VAL B  38   O  TYR B 223           
SHEET    1   G 5 HIS B 255  LEU B 259  0                                        
SHEET    2   G 5 GLU B 277  VAL B 282 -1  O  THR B 281   N  HIS B 255           
SHEET    3   G 5 CYS B 317  LEU B 321 -1  O  LEU B 321   N  TRP B 278           
SHEET    4   G 5 LYS B 304  VAL B 309 -1  N  VAL B 309   O  MET B 318           
SHEET    5   G 5 THR B 298  VAL B 301 -1  N  VAL B 299   O  CYS B 306           
SHEET    1   H 2 GLY B 264  ILE B 265  0                                        
SHEET    2   H 2 TYR B 271  VAL B 272 -1  O  TYR B 271   N  ILE B 265           
SHEET    1   I 5 GLU C 340  ASN C 342  0                                        
SHEET    2   I 5 VAL C 330  ASP C 337 -1  N  ASP C 337   O  GLU C 340           
SHEET    3   I 5 LEU C 247  GLU C 252 -1  N  LEU C 249   O  LEU C 333           
SHEET    4   I 5 ARG C  10  ILE C  13 -1  N  ARG C  10   O  THR C 250           
SHEET    5   I 5 ARG C 368  TYR C 370  1  O  GLU C 369   N  LEU C  11           
SHEET    1   J 9 ALA C  34  VAL C  38  0                                        
SHEET    2   J 9 GLY C  62  VAL C  65  1  O  GLY C  62   N  ALA C  37           
SHEET    3   J 9 ILE C  83  ILE C  85  1  O  LEU C  84   N  PHE C  63           
SHEET    4   J 9 SER C 103  VAL C 106  1  O  SER C 103   N  ILE C  83           
SHEET    5   J 9 LEU C 127  LYS C 132  1  O  HIS C 130   N  VAL C 104           
SHEET    6   J 9 PHE C 161  PHE C 167  1  O  PHE C 167   N  LEU C 131           
SHEET    7   J 9 TYR C 201  SER C 205  1  O  TYR C 201   N  GLU C 164           
SHEET    8   J 9 MET C 220  TYR C 223  1  O  ARG C 222   N  SER C 205           
SHEET    9   J 9 ALA C  34  VAL C  38  1  N  PHE C  36   O  ILE C 221           
SHEET    1   K 5 VAL C 256  LEU C 259  0                                        
SHEET    2   K 5 GLU C 277  VAL C 282 -1  O  GLU C 277   N  LEU C 259           
SHEET    3   K 5 CYS C 317  LEU C 321 -1  O  LEU C 321   N  TRP C 278           
SHEET    4   K 5 LYS C 304  VAL C 309 -1  N  VAL C 309   O  MET C 318           
SHEET    5   K 5 THR C 298  VAL C 301 -1  N  VAL C 301   O  LYS C 304           
SHEET    1   L 2 GLY C 264  ILE C 265  0                                        
SHEET    2   L 2 TYR C 271  VAL C 272 -1  O  TYR C 271   N  ILE C 265           
SITE     1 AC1 16 VAL A  38  LYS A  40  TYR A  44  LEU A  86                    
SITE     2 AC1 16 ARG A 139  HIS A 169  SER A 207  ARG A 222                    
SITE     3 AC1 16 GLY A 224  VAL A 225  TYR A 356  HOH A 374                    
SITE     4 AC1 16 TYR C 267  TYR C 286  CYS C 313  MET C 314                    
SITE     1 AC2 13 VAL B  38  LYS B  40  TYR B  44  ARG B 139                    
SITE     2 AC2 13 HIS B 169  SER B 207  ARG B 222  GLY B 224                    
SITE     3 AC2 13 VAL B 225  TYR B 267  TYR B 286  MET B 314                    
SITE     4 AC2 13 TYR B 356                                                     
SITE     1 AC3 16 TYR A 267  TYR A 286  CYS A 313  MET A 314                    
SITE     2 AC3 16 LYS C  40  TYR C  44  LEU C  86  ARG C 139                    
SITE     3 AC3 16 HIS C 169  ASN C 206  SER C 207  ARG C 222                    
SITE     4 AC3 16 GLY C 224  VAL C 225  TYR C 356  HOH C 374                    
CRYST1   94.597  156.186  146.930  90.00  90.00  90.00 C 2 2 21     24          
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      0.010571  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006403  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006806        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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