GenomeNet

Database: PDB
Entry: 3S46
LinkDB: 3S46
Original site: 3S46 
HEADER    ISOMERASE                               18-MAY-11   3S46              
TITLE     THE CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM STREPTOCOCCUS          
TITLE    2 PNEUMONIAE                                                           
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: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   3 ORGANISM_TAXID: 1313;                                                
SOURCE   4 STRAIN: R800;                                                        
SOURCE   5 GENE: ALAR, ALR, SP_1698;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET17                                     
KEYWDS    ALPHA/BETA BARREL, EXTENDED BETA-STRAND DOMAIN, PYRIDOXAL PHOSPHATE   
KEYWDS   2 COFACTOR, ALANINE RACEMASE, CARBAMYLATED LYSINE, ISOMERASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.IM,M.L.SHARPE,U.STRYCH,M.DAVLIEVA,K.L.KRAUSE                        
REVDAT   1   22-JUN-11 3S46    0                                                
SPRSDE     22-JUN-11 3S46      3MUB                                             
JRNL        AUTH   H.IM,M.L.SHARPE,U.STRYCH,M.DAVLIEVA,K.L.KRAUSE               
JRNL        TITL   THE CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM STREPTOCOCCUS 
JRNL        TITL 2 PNEUMONIAE, A TARGET FOR STRUCTURE-BASED DRUG DESIGN.        
JRNL        REF    BMC MICROBIOL.                V.  11   116 2011              
JRNL        REFN                   ESSN 1471-2180                               
JRNL        PMID   21612658                                                     
JRNL        DOI    10.1186/1471-2180-11-116                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 63336                          
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 + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3379                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4412                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3220                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 236                          
REMARK   3   BIN FREE R VALUE                    : 0.3550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5638                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 507                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.18000                                              
REMARK   3    B22 (A**2) : 0.18000                                              
REMARK   3    B33 (A**2) : -0.27000                                             
REMARK   3    B12 (A**2) : 0.09000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.127         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.099         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.274         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.959                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5758 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7837 ; 1.448 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   732 ; 5.731 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   243 ;38.010 ;24.938       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   953 ;13.905 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;16.374 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   917 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4311 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3646 ; 0.668 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5874 ; 1.186 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2112 ; 2.035 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1962 ; 3.082 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   367                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.7980  64.3680 -19.1930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1384 T22:   0.2189                                     
REMARK   3      T33:   0.3094 T12:   0.0561                                     
REMARK   3      T13:  -0.0476 T23:   0.0420                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4797 L22:   0.3420                                     
REMARK   3      L33:   1.2513 L12:   0.1629                                     
REMARK   3      L13:   0.4969 L23:  -0.0940                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1776 S12:   0.1654 S13:   0.1991                       
REMARK   3      S21:  -0.0308 S22:  -0.0144 S23:  -0.0338                       
REMARK   3      S31:  -0.2291 S32:   0.1903 S33:   0.1920                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   367                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.2140  64.6770  -1.3690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1384 T22:   0.4070                                     
REMARK   3      T33:   0.2788 T12:   0.2197                                     
REMARK   3      T13:  -0.0577 T23:  -0.1185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7892 L22:   0.4369                                     
REMARK   3      L33:   1.3413 L12:   0.1244                                     
REMARK   3      L13:   0.6816 L23:  -0.0277                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2014 S12:  -0.5622 S13:   0.2217                       
REMARK   3      S21:   0.0233 S22:  -0.0116 S23:   0.0513                       
REMARK   3      S31:  -0.2549 S32:  -0.4431 S33:   0.2130                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES: WITH TLS ADDED                                  
REMARK   4                                                                      
REMARK   4 3S46 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065738.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.2                                
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                             
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                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66748                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 23.030                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.700                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1SFT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M NA CITRATE, 0.1M MES, 10%           
REMARK 280  GLYCEROL, PH 7.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.36633            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       78.73267            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       78.73267            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       39.36633            
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: 6060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  19   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG A 347   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 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    LLP A  40      152.19    -39.14                                   
REMARK 500    GLU A 118       49.78    -92.61                                   
REMARK 500    ARG A 136      -77.77   -101.86                                   
REMARK 500    THR A 168       31.42   -141.49                                   
REMARK 500    ALA A 200      -16.31   -153.64                                   
REMARK 500    PHE A 214     -122.68    -94.75                                   
REMARK 500    SER A 247     -156.29   -151.61                                   
REMARK 500    ASN A 292       -3.14     76.54                                   
REMARK 500    THR A 349     -159.41   -136.74                                   
REMARK 500    GLU B  91       28.45    -73.09                                   
REMARK 500    ASP B 100       65.69     74.04                                   
REMARK 500    ARG B 136      -78.84    -98.60                                   
REMARK 500    ALA B 200      -10.61   -146.01                                   
REMARK 500    PHE B 214     -118.80    -94.36                                   
REMARK 500    SER B 247     -159.96   -150.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 418        DISTANCE =  5.24 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ A 369                 
DBREF  3S46 A    1   367  UNP    P0A2W8   ALR_STRPN        1    367             
DBREF  3S46 B    1   367  UNP    P0A2W8   ALR_STRPN        1    367             
SEQRES   1 A  367  MET LYS ALA SER PRO HIS ARG PRO THR LYS ALA LEU ILE          
SEQRES   2 A  367  HIS LEU GLY ALA ILE ARG GLN ASN ILE GLN GLN MET GLY          
SEQRES   3 A  367  ALA HIS ILE PRO GLN GLY THR LEU LYS LEU ALA VAL VAL          
SEQRES   4 A  367  LLP ALA ASN ALA TYR GLY HIS GLY ALA VAL ALA VAL ALA          
SEQRES   5 A  367  LYS ALA ILE GLN ASP ASP VAL ASP GLY PHE CYS VAL SER          
SEQRES   6 A  367  ASN ILE ASP GLU ALA ILE GLU LEU ARG GLN ALA GLY LEU          
SEQRES   7 A  367  SER LYS PRO ILE LEU ILE LEU GLY VAL SER GLU ILE GLU          
SEQRES   8 A  367  ALA VAL ALA LEU ALA LYS GLU TYR ASP PHE THR LEU THR          
SEQRES   9 A  367  VAL ALA GLY LEU GLU TRP ILE GLN ALA LEU LEU ASP LYS          
SEQRES  10 A  367  GLU VAL ASP LEU THR GLY LEU THR VAL HIS LEU KCX ILE          
SEQRES  11 A  367  ASP SER GLY MET GLY ARG ILE GLY PHE ARG GLU ALA SER          
SEQRES  12 A  367  GLU VAL GLU GLN ALA GLN ASP LEU LEU GLN GLN HIS GLY          
SEQRES  13 A  367  VAL CYS VAL GLU GLY ILE PHE THR HIS PHE ALA THR ALA          
SEQRES  14 A  367  ASP GLU GLU SER ASP ASP TYR PHE ASN ALA GLN LEU GLU          
SEQRES  15 A  367  ARG PHE LYS THR ILE LEU ALA SER MET LYS GLU VAL PRO          
SEQRES  16 A  367  GLU LEU VAL HIS ALA SER ASN SER ALA THR THR LEU TRP          
SEQRES  17 A  367  HIS VAL GLU THR ILE PHE ASN ALA VAL ARG MET GLY ASP          
SEQRES  18 A  367  ALA MET TYR GLY LEU ASN PRO SER GLY ALA VAL LEU ASP          
SEQRES  19 A  367  LEU PRO TYR ASP LEU ILE PRO ALA LEU THR LEU GLU SER          
SEQRES  20 A  367  ALA LEU VAL HIS VAL LYS THR VAL PRO ALA GLY ALA CYS          
SEQRES  21 A  367  MET GLY TYR GLY ALA THR TYR GLN ALA ASP SER GLU GLN          
SEQRES  22 A  367  VAL ILE ALA THR VAL PRO ILE GLY TYR ALA ASP GLY TRP          
SEQRES  23 A  367  THR ARG ASP MET GLN ASN PHE SER VAL LEU VAL ASP GLY          
SEQRES  24 A  367  GLN ALA CYS PRO ILE VAL GLY ARG VAL SER MET ASP GLN          
SEQRES  25 A  367  ILE THR ILE ARG LEU PRO LYS LEU TYR PRO LEU GLY THR          
SEQRES  26 A  367  LYS VAL THR LEU ILE GLY SER ASN GLY ASP LYS GLU ILE          
SEQRES  27 A  367  THR ALA THR GLN VAL ALA THR TYR ARG VAL THR ILE ASN          
SEQRES  28 A  367  TYR GLU VAL VAL CYS LEU LEU SER ASP ARG ILE PRO ARG          
SEQRES  29 A  367  GLU TYR TYR                                                  
SEQRES   1 B  367  MET LYS ALA SER PRO HIS ARG PRO THR LYS ALA LEU ILE          
SEQRES   2 B  367  HIS LEU GLY ALA ILE ARG GLN ASN ILE GLN GLN MET GLY          
SEQRES   3 B  367  ALA HIS ILE PRO GLN GLY THR LEU LYS LEU ALA VAL VAL          
SEQRES   4 B  367  LLP ALA ASN ALA TYR GLY HIS GLY ALA VAL ALA VAL ALA          
SEQRES   5 B  367  LYS ALA ILE GLN ASP ASP VAL ASP GLY PHE CYS VAL SER          
SEQRES   6 B  367  ASN ILE ASP GLU ALA ILE GLU LEU ARG GLN ALA GLY LEU          
SEQRES   7 B  367  SER LYS PRO ILE LEU ILE LEU GLY VAL SER GLU ILE GLU          
SEQRES   8 B  367  ALA VAL ALA LEU ALA LYS GLU TYR ASP PHE THR LEU THR          
SEQRES   9 B  367  VAL ALA GLY LEU GLU TRP ILE GLN ALA LEU LEU ASP LYS          
SEQRES  10 B  367  GLU VAL ASP LEU THR GLY LEU THR VAL HIS LEU KCX ILE          
SEQRES  11 B  367  ASP SER GLY MET GLY ARG ILE GLY PHE ARG GLU ALA SER          
SEQRES  12 B  367  GLU VAL GLU GLN ALA GLN ASP LEU LEU GLN GLN HIS GLY          
SEQRES  13 B  367  VAL CYS VAL GLU GLY ILE PHE THR HIS PHE ALA THR ALA          
SEQRES  14 B  367  ASP GLU GLU SER ASP ASP TYR PHE ASN ALA GLN LEU GLU          
SEQRES  15 B  367  ARG PHE LYS THR ILE LEU ALA SER MET LYS GLU VAL PRO          
SEQRES  16 B  367  GLU LEU VAL HIS ALA SER ASN SER ALA THR THR LEU TRP          
SEQRES  17 B  367  HIS VAL GLU THR ILE PHE ASN ALA VAL ARG MET GLY ASP          
SEQRES  18 B  367  ALA MET TYR GLY LEU ASN PRO SER GLY ALA VAL LEU ASP          
SEQRES  19 B  367  LEU PRO TYR ASP LEU ILE PRO ALA LEU THR LEU GLU SER          
SEQRES  20 B  367  ALA LEU VAL HIS VAL LYS THR VAL PRO ALA GLY ALA CYS          
SEQRES  21 B  367  MET GLY TYR GLY ALA THR TYR GLN ALA ASP SER GLU GLN          
SEQRES  22 B  367  VAL ILE ALA THR VAL PRO ILE GLY TYR ALA ASP GLY TRP          
SEQRES  23 B  367  THR ARG ASP MET GLN ASN PHE SER VAL LEU VAL ASP GLY          
SEQRES  24 B  367  GLN ALA CYS PRO ILE VAL GLY ARG VAL SER MET ASP GLN          
SEQRES  25 B  367  ILE THR ILE ARG LEU PRO LYS LEU TYR PRO LEU GLY THR          
SEQRES  26 B  367  LYS VAL THR LEU ILE GLY SER ASN GLY ASP LYS GLU ILE          
SEQRES  27 B  367  THR ALA THR GLN VAL ALA THR TYR ARG VAL THR ILE ASN          
SEQRES  28 B  367  TYR GLU VAL VAL CYS LEU LEU SER ASP ARG ILE PRO ARG          
SEQRES  29 B  367  GLU TYR TYR                                                  
MODRES 3S46 LLP A   40  LYS                                                     
MODRES 3S46 KCX A  129  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3S46 LLP B   40  LYS                                                     
MODRES 3S46 KCX B  129  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    LLP  A  40      24                                                       
HET    KCX  A 129      12                                                       
HET    LLP  B  40      24                                                       
HET    KCX  B 129      12                                                       
HET    BEZ  A 369       9                                                       
HETNAM     LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-                
HETNAM   2 LLP  PYRIDIN-4-YLMETHANE)                                            
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     BEZ BENZOIC ACID                                                     
HETSYN     LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE                             
FORMUL   1  LLP    2(C14 H24 N3 O7 P)                                           
FORMUL   1  KCX    2(C7 H14 N2 O4)                                              
FORMUL   3  BEZ    C7 H6 O2                                                     
FORMUL   4  HOH   *507(H2 O)                                                    
HELIX    1   1 LEU A   15  HIS A   28  1                                  14    
HELIX    2   2 VAL A   39  GLY A   45  1                                   7    
HELIX    3   3 GLY A   47  GLN A   56  1                                  10    
HELIX    4   4 ASP A   57  VAL A   59  5                                   3    
HELIX    5   5 ASN A   66  ALA A   76  1                                  11    
HELIX    6   6 GLU A   89  GLU A   91  5                                   3    
HELIX    7   7 ALA A   92  TYR A   99  1                                   8    
HELIX    8   8 GLY A  107  LYS A  117  1                                  11    
HELIX    9   9 GLU A  141  HIS A  155  1                                  15    
HELIX   10  10 ASP A  174  SER A  190  1                                  17    
HELIX   11  11 ASN A  202  HIS A  209  1                                   8    
HELIX   12  12 VAL A  210  ILE A  213  5                                   4    
HELIX   13  13 GLY A  220  GLY A  225  5                                   6    
HELIX   14  14 GLY A  262  THR A  266  5                                   5    
HELIX   15  15 GLY A  281  GLY A  285  5                                   5    
HELIX   16  16 THR A  287  GLN A  291  5                                   5    
HELIX   17  17 THR A  339  VAL A  348  1                                  10    
HELIX   18  18 ILE A  350  LEU A  357  1                                   8    
HELIX   19  19 LEU B   15  HIS B   28  1                                  14    
HELIX   20  20 VAL B   39  GLY B   45  1                                   7    
HELIX   21  21 GLY B   47  GLN B   56  1                                  10    
HELIX   22  22 ASP B   57  VAL B   59  5                                   3    
HELIX   23  23 ASN B   66  GLY B   77  1                                  12    
HELIX   24  24 GLU B   89  GLU B   91  5                                   3    
HELIX   25  25 ALA B   92  ASP B  100  1                                   9    
HELIX   26  26 GLY B  107  LYS B  117  1                                  11    
HELIX   27  27 GLU B  141  HIS B  155  1                                  15    
HELIX   28  28 ASP B  174  MET B  191  1                                  18    
HELIX   29  29 ASN B  202  HIS B  209  1                                   8    
HELIX   30  30 VAL B  210  ILE B  213  5                                   4    
HELIX   31  31 GLY B  262  THR B  266  5                                   5    
HELIX   32  32 GLY B  281  GLY B  285  5                                   5    
HELIX   33  33 THR B  287  GLN B  291  5                                   5    
HELIX   34  34 THR B  339  VAL B  348  1                                  10    
HELIX   35  35 ILE B  350  LEU B  357  1                                   8    
SHEET    1   A 5 LYS A 336  ILE A 338  0                                        
SHEET    2   A 5 LYS A 326  ASN A 333 -1  N  GLY A 331   O  ILE A 338           
SHEET    3   A 5 LEU A 243  ALA A 248 -1  N  LEU A 245   O  LEU A 329           
SHEET    4   A 5 LYS A  10  HIS A  14 -1  N  LYS A  10   O  GLU A 246           
SHEET    5   A 5 ARG A 364  TYR A 367  1  O  TYR A 367   N  ILE A  13           
SHEET    1   B 9 LEU A  34  VAL A  38  0                                        
SHEET    2   B 9 GLY A  61  VAL A  64  1  O  GLY A  61   N  ALA A  37           
SHEET    3   B 9 ILE A  82  VAL A  87  1  O  LEU A  85   N  VAL A  64           
SHEET    4   B 9 THR A 102  VAL A 105  1  O  THR A 102   N  ILE A  84           
SHEET    5   B 9 THR A 125  ILE A 130  1  O  HIS A 127   N  VAL A 105           
SHEET    6   B 9 CYS A 158  THR A 164  1  O  PHE A 163   N  ILE A 130           
SHEET    7   B 9 LEU A 197  SER A 201  1  O  LEU A 197   N  GLU A 160           
SHEET    8   B 9 ALA A 216  MET A 219  1  O  ARG A 218   N  SER A 201           
SHEET    9   B 9 LEU A  34  VAL A  38  1  N  VAL A  38   O  MET A 219           
SHEET    1   C 3 HIS A 251  VAL A 255  0                                        
SHEET    2   C 3 GLN A 273  VAL A 278 -1  O  GLN A 273   N  VAL A 255           
SHEET    3   C 3 ILE A 313  LEU A 317 -1  O  ILE A 315   N  ALA A 276           
SHEET    1   D 2 CYS A 260  MET A 261  0                                        
SHEET    2   D 2 TYR A 267  GLN A 268 -1  O  TYR A 267   N  MET A 261           
SHEET    1   E 2 SER A 294  VAL A 297  0                                        
SHEET    2   E 2 GLN A 300  PRO A 303 -1  O  CYS A 302   N  VAL A 295           
SHEET    1   F 5 LYS B 336  ILE B 338  0                                        
SHEET    2   F 5 LYS B 326  ASN B 333 -1  N  ASN B 333   O  LYS B 336           
SHEET    3   F 5 LEU B 243  ALA B 248 -1  N  SER B 247   O  VAL B 327           
SHEET    4   F 5 LYS B  10  HIS B  14 -1  N  LYS B  10   O  GLU B 246           
SHEET    5   F 5 ARG B 364  TYR B 367  1  O  GLU B 365   N  ILE B  13           
SHEET    1   G 9 LEU B  34  VAL B  38  0                                        
SHEET    2   G 9 GLY B  61  VAL B  64  1  O  CYS B  63   N  ALA B  37           
SHEET    3   G 9 ILE B  82  ILE B  84  1  O  LEU B  83   N  PHE B  62           
SHEET    4   G 9 THR B 102  VAL B 105  1  O  THR B 102   N  ILE B  82           
SHEET    5   G 9 THR B 125  KCX B 129  1  O  KCX B 129   N  VAL B 105           
SHEET    6   G 9 CYS B 158  PHE B 163  1  O  GLY B 161   N  LEU B 128           
SHEET    7   G 9 LEU B 197  SER B 201  1  O  LEU B 197   N  ILE B 162           
SHEET    8   G 9 ALA B 216  MET B 219  1  O  ARG B 218   N  SER B 201           
SHEET    9   G 9 LEU B  34  VAL B  38  1  N  LEU B  36   O  VAL B 217           
SHEET    1   H 3 HIS B 251  VAL B 255  0                                        
SHEET    2   H 3 GLN B 273  VAL B 278 -1  O  THR B 277   N  HIS B 251           
SHEET    3   H 3 ILE B 313  LEU B 317 -1  O  ILE B 315   N  ALA B 276           
SHEET    1   I 2 CYS B 260  MET B 261  0                                        
SHEET    2   I 2 TYR B 267  GLN B 268 -1  O  TYR B 267   N  MET B 261           
SHEET    1   J 2 SER B 294  VAL B 297  0                                        
SHEET    2   J 2 GLN B 300  PRO B 303 -1  O  CYS B 302   N  VAL B 295           
LINK         C   LLP A  40                 N   ALA A  41     1555   1555  1.55  
LINK         C   LEU A 128                 N   KCX A 129     1555   1555  1.34  
LINK         C   KCX A 129                 N   ILE A 130     1555   1555  1.33  
LINK         C   LLP B  40                 N   ALA B  41     1555   1555  1.34  
LINK         C   LEU B 128                 N   KCX B 129     1555   1555  1.33  
LINK         C   KCX B 129                 N   ILE B 130     1555   1555  1.33  
SITE     1 AC1  9 HIS A  28  ILE A  29  PRO A  30  GLU B 141                    
SITE     2 AC1  9 ALA B 142  ARG B 183  THR B 186  HOH B 393                    
SITE     3 AC1  9 HOH B 453                                                     
CRYST1  119.973  119.973  118.099  90.00  90.00 120.00 P 31 2 1     12          
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      0.008335  0.004812  0.000000        0.00000                         
SCALE2      0.000000  0.009625  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008467        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system