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Database: PDB
Entry: 4RJY
LinkDB: 4RJY
Original site: 4RJY 
HEADER    LYASE                                   11-OCT-14   4RJY              
TITLE     CRYSTAL STRUCTURE OF E. COLI L-THREONINE ALDOLASE IN COMPLEX WITH A   
TITLE    2 NON-COVALENTLY UNCLEAVED BOUND L-SERINE SUBSTRATE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LOW SPECIFICITY L-THREONINE ALDOLASE;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 1182686;                                             
SOURCE   4 STRAIN: KTE79;                                                       
SOURCE   5 GENE: A1UU_02790;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PYRIDOXAL-5-PHOSPHATE, THREONINE ALDOLASE, ALDIMINE, CATALYTIC        
KEYWDS   2 MECHANISM, RETRO-ALDOL CLEAVAGE, PLP-DEPENDENT ENZYMES, LYASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.K.SAFO,N.CHOWDHURY,A.K.GANDHI                                       
REVDAT   3   04-FEB-15 4RJY    1       JRNL                                     
REVDAT   2   21-JAN-15 4RJY    1       JRNL                                     
REVDAT   1   29-OCT-14 4RJY    0                                                
JRNL        AUTH   S.G.REMESH,M.S.GHATGE,M.H.AHMED,F.N.MUSAYEV,A.GANDHI,        
JRNL        AUTH 2 N.CHOWDHURY,M.L.DI SALVO,G.E.KELLOGG,R.CONTESTABILE,         
JRNL        AUTH 3 V.SCHIRCH,M.K.SAFO                                           
JRNL        TITL   MOLECULAR BASIS OF E. COLIL-THREONINE ALDOLASE CATALYTIC     
JRNL        TITL 2 INACTIVATION AT LOW PH.                                      
JRNL        REF    BIOCHIM.BIOPHYS.ACTA          V.1854   278 2015              
JRNL        REFN                   ISSN 0006-3002                               
JRNL        PMID   25560296                                                     
JRNL        DOI    10.1016/J.BBAPAP.2014.12.023                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
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)   (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 76865                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3871                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10252                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 851                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.87300                                              
REMARK   3    B22 (A**2) : -3.98700                                             
REMARK   3    B33 (A**2) : 1.11400                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.12200                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 78.76                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : LLP.PAR                                        
REMARK   3  PARAMETER FILE  4  : LLP-PATCH.PAR                                  
REMARK   3  PARAMETER FILE  5  : SEN.PAR                                        
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4RJY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB087439.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
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 MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5417                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77165                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 2.910                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.77                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: FRESHLY DIALYZED ETA (22 MG/ML IN 20     
REMARK 280  MM POTASSIUM PHOSPHATE, PH 7.0) WAS INCUBATED WITH L-SERINE (6.25   
REMARK 280  MM), PRECIPITANT SOLUTION CONTAINS 0.1 M SODIUM CITRATE TRIBASIC    
REMARK 280  DIHYDRATE, PH 5.6, 20% V/V 2-PROPOANOL, 20% V/V PEG 4000, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       52.44000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15680 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -120.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A   333                                                      
REMARK 465     ARG B   333                                                      
REMARK 465     ARG C   333                                                      
REMARK 465     ARG D   333                                                      
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   O    LYS C   222     O    HOH C   525              2.18            
REMARK 500   O    HOH B   650     O    HOH B   651              2.19            
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    THR A 138   N   -  CA  -  C   ANGL. DEV. = -19.7 DEGREES          
REMARK 500    THR B 138   N   -  CA  -  C   ANGL. DEV. = -16.5 DEGREES          
REMARK 500    THR C 138   N   -  CA  -  C   ANGL. DEV. = -19.1 DEGREES          
REMARK 500    THR D 138   N   -  CA  -  C   ANGL. DEV. = -20.6 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    ALA A  89       16.39     55.04                                   
REMARK 500    THR A 138       90.25     89.10                                   
REMARK 500    LLP A 197     -114.96   -105.76                                   
REMARK 500    ARG A 229      -91.05    -91.26                                   
REMARK 500    GLN A 230       59.71    -90.85                                   
REMARK 500    THR A 275     -111.70     45.40                                   
REMARK 500    SER A 304      170.38    175.20                                   
REMARK 500    ALA B  89       19.73     59.62                                   
REMARK 500    ILE B 125       -7.12    -59.86                                   
REMARK 500    THR B 138       63.83     93.05                                   
REMARK 500    LLP B 197     -114.96    -98.14                                   
REMARK 500    ARG B 229      -95.30    -95.82                                   
REMARK 500    THR B 275     -110.68     42.76                                   
REMARK 500    TYR B 293      -75.68    -39.74                                   
REMARK 500    TYR C  85      -56.20   -122.85                                   
REMARK 500    ALA C  89       17.41     58.15                                   
REMARK 500    ILE C 125       -9.69    -54.38                                   
REMARK 500    THR C 138       92.50     91.08                                   
REMARK 500    TYR C 187       33.77    -93.07                                   
REMARK 500    LLP C 197     -112.73   -104.80                                   
REMARK 500    ARG C 229     -103.00    -81.84                                   
REMARK 500    ARG C 248        3.71    -67.68                                   
REMARK 500    ARG C 272      158.64    170.26                                   
REMARK 500    THR C 275     -119.65     52.31                                   
REMARK 500    LYS D 131      -34.54   -133.14                                   
REMARK 500    THR D 138       94.03     92.07                                   
REMARK 500    LLP D 197     -121.38   -116.62                                   
REMARK 500    ARG D 229      -91.50    -88.07                                   
REMARK 500    GLN D 230       59.15    -91.28                                   
REMARK 500    THR D 275     -114.05     41.52                                   
REMARK 500    ASN D 276       32.27    -99.36                                   
REMARK 500    ALA D 287      -71.23    -36.24                                   
REMARK 500    SER D 304      163.18    173.20                                   
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 562        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH A 587        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH B 569        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH B 582        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH B 596        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH B 675        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH D 599        DISTANCE =  5.56 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  10   OG1                                                    
REMARK 620 2 SER A 196   O    87.3                                              
REMARK 620 3 THR A  10   O    79.0 163.1                                        
REMARK 620 4 THR A   8   O   108.0  83.9  91.1                                  
REMARK 620 5 THR A 201   O   103.3  80.2 112.3 144.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C  10   O                                                      
REMARK 620 2 SER C 196   O   155.5                                              
REMARK 620 3 THR C  10   OG1  71.7  84.4                                        
REMARK 620 4 THR C 201   O   116.1  74.6 105.9                                  
REMARK 620 5 THR C   8   O    96.9  81.0  97.4 144.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 196   O                                                      
REMARK 620 2 THR B  10   O   143.4                                              
REMARK 620 3 THR B  10   OG1  75.7  67.6                                        
REMARK 620 4 THR B 201   O    79.7 110.7 107.5                                  
REMARK 620 5 THR B   8   O    83.5  98.0  92.7 149.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER D 196   O                                                      
REMARK 620 2 THR D  10   O   143.0                                              
REMARK 620 3 THR D 201   O    88.3 108.2                                        
REMARK 620 4 THR D   8   O    82.4  89.2 160.6                                  
REMARK 620 5 THR D  10   OG1  78.4  65.7 103.9  90.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER D  97   OG                                                     
REMARK 620 2 SER A  97   OG  140.1                                              
REMARK 620 3 ALA D  93   O   113.3 106.2                                        
REMARK 620 4 ALA A  93   O    99.5 105.7  58.1                                  
REMARK 620 5 HOH C 641   O    76.7  73.7 130.5 171.3                            
REMARK 620 6 HOH A 679   O    75.4  66.5 167.7 113.1  58.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B  97   OG                                                     
REMARK 620 2 SER C  97   OG  144.4                                              
REMARK 620 3 ALA B  93   O   107.2 106.0                                        
REMARK 620 4 VAL B  94   O   128.5  60.8  60.7                                  
REMARK 620 5 ALA C  93   O   103.3 101.8  65.5 112.7                            
REMARK 620 6 HOH A 679   O    84.1  70.3 115.5  63.5 172.1                      
REMARK 620 7 HOH C 641   O    74.2  73.3 177.0 120.8 111.6  67.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SER A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SER B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SER C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SER D 403                 
DBREF  4RJY A    1   333  UNP    L4EJM2   L4EJM2_ECOLX     1    333             
DBREF  4RJY B    1   333  UNP    L4EJM2   L4EJM2_ECOLX     1    333             
DBREF  4RJY C    1   333  UNP    L4EJM2   L4EJM2_ECOLX     1    333             
DBREF  4RJY D    1   333  UNP    L4EJM2   L4EJM2_ECOLX     1    333             
SEQADV 4RJY LYS A  158  UNP  L4EJM2    GLU   158 CONFLICT                       
SEQADV 4RJY THR A  256  UNP  L4EJM2    ALA   256 CONFLICT                       
SEQADV 4RJY LYS B  158  UNP  L4EJM2    GLU   158 CONFLICT                       
SEQADV 4RJY THR B  256  UNP  L4EJM2    ALA   256 CONFLICT                       
SEQADV 4RJY LYS C  158  UNP  L4EJM2    GLU   158 CONFLICT                       
SEQADV 4RJY THR C  256  UNP  L4EJM2    ALA   256 CONFLICT                       
SEQADV 4RJY LYS D  158  UNP  L4EJM2    GLU   158 CONFLICT                       
SEQADV 4RJY THR D  256  UNP  L4EJM2    ALA   256 CONFLICT                       
SEQRES   1 A  333  MET ILE ASP LEU ARG SER ASP THR VAL THR ARG PRO SER          
SEQRES   2 A  333  ARG ALA MET LEU GLU ALA MET MET ALA ALA PRO VAL GLY          
SEQRES   3 A  333  ASP ASP VAL TYR GLY ASP ASP PRO THR VAL ASN ALA LEU          
SEQRES   4 A  333  GLN ASP TYR ALA ALA GLU LEU SER GLY LYS GLU ALA ALA          
SEQRES   5 A  333  ILE PHE LEU PRO THR GLY THR GLN ALA ASN LEU VAL ALA          
SEQRES   6 A  333  LEU LEU SER HIS CYS GLU ARG GLY GLU GLU TYR ILE VAL          
SEQRES   7 A  333  GLY GLN ALA ALA HIS ASN TYR LEU PHE GLU ALA GLY GLY          
SEQRES   8 A  333  ALA ALA VAL LEU GLY SER ILE GLN PRO GLN PRO ILE ASP          
SEQRES   9 A  333  ALA ALA ALA ASP GLY THR LEU PRO LEU ASP LYS VAL ALA          
SEQRES  10 A  333  MET LYS ILE LYS PRO ASP ASP ILE HIS PHE ALA ARG THR          
SEQRES  11 A  333  LYS LEU LEU SER LEU GLU ASN THR HIS ASN GLY LYS VAL          
SEQRES  12 A  333  LEU PRO ARG GLU TYR LEU LYS GLU ALA TRP GLU PHE THR          
SEQRES  13 A  333  ARG LYS ARG ASN LEU ALA LEU HIS VAL ASP GLY ALA ARG          
SEQRES  14 A  333  ILE PHE ASN ALA VAL VAL ALA TYR GLY CYS GLU LEU LYS          
SEQRES  15 A  333  GLU ILE THR GLN TYR CYS ASP SER PHE THR ILE CYS LEU          
SEQRES  16 A  333  SER LLP GLY LEU GLY THR PRO VAL GLY SER LEU LEU VAL          
SEQRES  17 A  333  GLY ASN ARG ASP TYR ILE LYS ARG ALA ILE ARG TRP ARG          
SEQRES  18 A  333  LYS MET THR GLY GLY GLY MET ARG GLN SER GLY ILE LEU          
SEQRES  19 A  333  ALA ALA ALA GLY MET TYR ALA LEU LYS ASN ASN VAL ALA          
SEQRES  20 A  333  ARG LEU GLN GLU ASP HIS ASP ASN THR ALA TRP MET ALA          
SEQRES  21 A  333  GLU GLN LEU ARG GLU ALA GLY ALA ASP VAL MET ARG GLN          
SEQRES  22 A  333  ASP THR ASN MET LEU PHE VAL ARG VAL GLY GLU GLU ASN          
SEQRES  23 A  333  ALA ALA ALA LEU GLY GLU TYR MET LYS ALA ARG ASN VAL          
SEQRES  24 A  333  LEU ILE ASN ALA SER PRO ILE VAL ARG LEU VAL THR HIS          
SEQRES  25 A  333  LEU ASP VAL SER ARG ALA GLN LEU ALA GLU VAL ALA ALA          
SEQRES  26 A  333  HIS TRP ARG ALA PHE LEU ALA ARG                              
SEQRES   1 B  333  MET ILE ASP LEU ARG SER ASP THR VAL THR ARG PRO SER          
SEQRES   2 B  333  ARG ALA MET LEU GLU ALA MET MET ALA ALA PRO VAL GLY          
SEQRES   3 B  333  ASP ASP VAL TYR GLY ASP ASP PRO THR VAL ASN ALA LEU          
SEQRES   4 B  333  GLN ASP TYR ALA ALA GLU LEU SER GLY LYS GLU ALA ALA          
SEQRES   5 B  333  ILE PHE LEU PRO THR GLY THR GLN ALA ASN LEU VAL ALA          
SEQRES   6 B  333  LEU LEU SER HIS CYS GLU ARG GLY GLU GLU TYR ILE VAL          
SEQRES   7 B  333  GLY GLN ALA ALA HIS ASN TYR LEU PHE GLU ALA GLY GLY          
SEQRES   8 B  333  ALA ALA VAL LEU GLY SER ILE GLN PRO GLN PRO ILE ASP          
SEQRES   9 B  333  ALA ALA ALA ASP GLY THR LEU PRO LEU ASP LYS VAL ALA          
SEQRES  10 B  333  MET LYS ILE LYS PRO ASP ASP ILE HIS PHE ALA ARG THR          
SEQRES  11 B  333  LYS LEU LEU SER LEU GLU ASN THR HIS ASN GLY LYS VAL          
SEQRES  12 B  333  LEU PRO ARG GLU TYR LEU LYS GLU ALA TRP GLU PHE THR          
SEQRES  13 B  333  ARG LYS ARG ASN LEU ALA LEU HIS VAL ASP GLY ALA ARG          
SEQRES  14 B  333  ILE PHE ASN ALA VAL VAL ALA TYR GLY CYS GLU LEU LYS          
SEQRES  15 B  333  GLU ILE THR GLN TYR CYS ASP SER PHE THR ILE CYS LEU          
SEQRES  16 B  333  SER LLP GLY LEU GLY THR PRO VAL GLY SER LEU LEU VAL          
SEQRES  17 B  333  GLY ASN ARG ASP TYR ILE LYS ARG ALA ILE ARG TRP ARG          
SEQRES  18 B  333  LYS MET THR GLY GLY GLY MET ARG GLN SER GLY ILE LEU          
SEQRES  19 B  333  ALA ALA ALA GLY MET TYR ALA LEU LYS ASN ASN VAL ALA          
SEQRES  20 B  333  ARG LEU GLN GLU ASP HIS ASP ASN THR ALA TRP MET ALA          
SEQRES  21 B  333  GLU GLN LEU ARG GLU ALA GLY ALA ASP VAL MET ARG GLN          
SEQRES  22 B  333  ASP THR ASN MET LEU PHE VAL ARG VAL GLY GLU GLU ASN          
SEQRES  23 B  333  ALA ALA ALA LEU GLY GLU TYR MET LYS ALA ARG ASN VAL          
SEQRES  24 B  333  LEU ILE ASN ALA SER PRO ILE VAL ARG LEU VAL THR HIS          
SEQRES  25 B  333  LEU ASP VAL SER ARG ALA GLN LEU ALA GLU VAL ALA ALA          
SEQRES  26 B  333  HIS TRP ARG ALA PHE LEU ALA ARG                              
SEQRES   1 C  333  MET ILE ASP LEU ARG SER ASP THR VAL THR ARG PRO SER          
SEQRES   2 C  333  ARG ALA MET LEU GLU ALA MET MET ALA ALA PRO VAL GLY          
SEQRES   3 C  333  ASP ASP VAL TYR GLY ASP ASP PRO THR VAL ASN ALA LEU          
SEQRES   4 C  333  GLN ASP TYR ALA ALA GLU LEU SER GLY LYS GLU ALA ALA          
SEQRES   5 C  333  ILE PHE LEU PRO THR GLY THR GLN ALA ASN LEU VAL ALA          
SEQRES   6 C  333  LEU LEU SER HIS CYS GLU ARG GLY GLU GLU TYR ILE VAL          
SEQRES   7 C  333  GLY GLN ALA ALA HIS ASN TYR LEU PHE GLU ALA GLY GLY          
SEQRES   8 C  333  ALA ALA VAL LEU GLY SER ILE GLN PRO GLN PRO ILE ASP          
SEQRES   9 C  333  ALA ALA ALA ASP GLY THR LEU PRO LEU ASP LYS VAL ALA          
SEQRES  10 C  333  MET LYS ILE LYS PRO ASP ASP ILE HIS PHE ALA ARG THR          
SEQRES  11 C  333  LYS LEU LEU SER LEU GLU ASN THR HIS ASN GLY LYS VAL          
SEQRES  12 C  333  LEU PRO ARG GLU TYR LEU LYS GLU ALA TRP GLU PHE THR          
SEQRES  13 C  333  ARG LYS ARG ASN LEU ALA LEU HIS VAL ASP GLY ALA ARG          
SEQRES  14 C  333  ILE PHE ASN ALA VAL VAL ALA TYR GLY CYS GLU LEU LYS          
SEQRES  15 C  333  GLU ILE THR GLN TYR CYS ASP SER PHE THR ILE CYS LEU          
SEQRES  16 C  333  SER LLP GLY LEU GLY THR PRO VAL GLY SER LEU LEU VAL          
SEQRES  17 C  333  GLY ASN ARG ASP TYR ILE LYS ARG ALA ILE ARG TRP ARG          
SEQRES  18 C  333  LYS MET THR GLY GLY GLY MET ARG GLN SER GLY ILE LEU          
SEQRES  19 C  333  ALA ALA ALA GLY MET TYR ALA LEU LYS ASN ASN VAL ALA          
SEQRES  20 C  333  ARG LEU GLN GLU ASP HIS ASP ASN THR ALA TRP MET ALA          
SEQRES  21 C  333  GLU GLN LEU ARG GLU ALA GLY ALA ASP VAL MET ARG GLN          
SEQRES  22 C  333  ASP THR ASN MET LEU PHE VAL ARG VAL GLY GLU GLU ASN          
SEQRES  23 C  333  ALA ALA ALA LEU GLY GLU TYR MET LYS ALA ARG ASN VAL          
SEQRES  24 C  333  LEU ILE ASN ALA SER PRO ILE VAL ARG LEU VAL THR HIS          
SEQRES  25 C  333  LEU ASP VAL SER ARG ALA GLN LEU ALA GLU VAL ALA ALA          
SEQRES  26 C  333  HIS TRP ARG ALA PHE LEU ALA ARG                              
SEQRES   1 D  333  MET ILE ASP LEU ARG SER ASP THR VAL THR ARG PRO SER          
SEQRES   2 D  333  ARG ALA MET LEU GLU ALA MET MET ALA ALA PRO VAL GLY          
SEQRES   3 D  333  ASP ASP VAL TYR GLY ASP ASP PRO THR VAL ASN ALA LEU          
SEQRES   4 D  333  GLN ASP TYR ALA ALA GLU LEU SER GLY LYS GLU ALA ALA          
SEQRES   5 D  333  ILE PHE LEU PRO THR GLY THR GLN ALA ASN LEU VAL ALA          
SEQRES   6 D  333  LEU LEU SER HIS CYS GLU ARG GLY GLU GLU TYR ILE VAL          
SEQRES   7 D  333  GLY GLN ALA ALA HIS ASN TYR LEU PHE GLU ALA GLY GLY          
SEQRES   8 D  333  ALA ALA VAL LEU GLY SER ILE GLN PRO GLN PRO ILE ASP          
SEQRES   9 D  333  ALA ALA ALA ASP GLY THR LEU PRO LEU ASP LYS VAL ALA          
SEQRES  10 D  333  MET LYS ILE LYS PRO ASP ASP ILE HIS PHE ALA ARG THR          
SEQRES  11 D  333  LYS LEU LEU SER LEU GLU ASN THR HIS ASN GLY LYS VAL          
SEQRES  12 D  333  LEU PRO ARG GLU TYR LEU LYS GLU ALA TRP GLU PHE THR          
SEQRES  13 D  333  ARG LYS ARG ASN LEU ALA LEU HIS VAL ASP GLY ALA ARG          
SEQRES  14 D  333  ILE PHE ASN ALA VAL VAL ALA TYR GLY CYS GLU LEU LYS          
SEQRES  15 D  333  GLU ILE THR GLN TYR CYS ASP SER PHE THR ILE CYS LEU          
SEQRES  16 D  333  SER LLP GLY LEU GLY THR PRO VAL GLY SER LEU LEU VAL          
SEQRES  17 D  333  GLY ASN ARG ASP TYR ILE LYS ARG ALA ILE ARG TRP ARG          
SEQRES  18 D  333  LYS MET THR GLY GLY GLY MET ARG GLN SER GLY ILE LEU          
SEQRES  19 D  333  ALA ALA ALA GLY MET TYR ALA LEU LYS ASN ASN VAL ALA          
SEQRES  20 D  333  ARG LEU GLN GLU ASP HIS ASP ASN THR ALA TRP MET ALA          
SEQRES  21 D  333  GLU GLN LEU ARG GLU ALA GLY ALA ASP VAL MET ARG GLN          
SEQRES  22 D  333  ASP THR ASN MET LEU PHE VAL ARG VAL GLY GLU GLU ASN          
SEQRES  23 D  333  ALA ALA ALA LEU GLY GLU TYR MET LYS ALA ARG ASN VAL          
SEQRES  24 D  333  LEU ILE ASN ALA SER PRO ILE VAL ARG LEU VAL THR HIS          
SEQRES  25 D  333  LEU ASP VAL SER ARG ALA GLN LEU ALA GLU VAL ALA ALA          
SEQRES  26 D  333  HIS TRP ARG ALA PHE LEU ALA ARG                              
MODRES 4RJY LLP A  197  LYS                                                     
MODRES 4RJY LLP B  197  LYS                                                     
MODRES 4RJY LLP C  197  LYS                                                     
MODRES 4RJY LLP D  197  LYS                                                     
HET    LLP  A 197      24                                                       
HET    LLP  B 197      24                                                       
HET    LLP  C 197      24                                                       
HET    LLP  D 197      24                                                       
HET     NA  A 401       1                                                       
HET    SER  A 402      14                                                       
HET     NA  B 401       1                                                       
HET     NA  B 402       1                                                       
HET    SER  B 403      14                                                       
HET     NA  C 401       1                                                       
HET    SER  C 402      14                                                       
HET     NA  D 401       1                                                       
HET     NA  D 402       1                                                       
HET    SER  D 403      14                                                       
HETNAM     LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-                
HETNAM   2 LLP  PYRIDIN-4-YLMETHANE)                                            
HETNAM      NA SODIUM ION                                                       
HETNAM     SER SERINE                                                           
HETSYN     LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE                             
FORMUL   1  LLP    4(C14 H24 N3 O7 P)                                           
FORMUL   5   NA    6(NA 1+)                                                     
FORMUL   6  SER    4(C3 H7 N O3)                                                
FORMUL  15  HOH   *851(H2 O)                                                    
HELIX    1   1 SER A   13  ALA A   23  1                                  11    
HELIX    2   2 ASP A   33  GLY A   48  1                                  16    
HELIX    3   3 THR A   57  CYS A   70  1                                  14    
HELIX    4   4 GLY A   90  LEU A   95  1                                   6    
HELIX    5   5 PRO A  112  MET A  118  1                                   7    
HELIX    6   6 PRO A  145  ARG A  159  1                                  15    
HELIX    7   7 ARG A  169  GLY A  178  1                                  10    
HELIX    8   8 LEU A  181  GLN A  186  1                                   6    
HELIX    9   9 ASN A  210  THR A  224  1                                  15    
HELIX   10  10 SER A  231  ASN A  245  1                                  15    
HELIX   11  11 ARG A  248  ALA A  266  1                                  19    
HELIX   12  12 ASN A  286  ALA A  296  1                                  11    
HELIX   13  13 SER A  316  ALA A  332  1                                  17    
HELIX   14  14 SER B    6  THR B   10  5                                   5    
HELIX   15  15 SER B   13  ALA B   23  1                                  11    
HELIX   16  16 ASP B   33  GLY B   48  1                                  16    
HELIX   17  17 THR B   57  CYS B   70  1                                  14    
HELIX   18  18 ALA B   82  PHE B   87  1                                   6    
HELIX   19  19 GLY B   90  LEU B   95  1                                   6    
HELIX   20  20 PRO B  112  MET B  118  1                                   7    
HELIX   21  21 THR B  138  LYS B  142  5                                   5    
HELIX   22  22 PRO B  145  ARG B  159  1                                  15    
HELIX   23  23 ARG B  169  GLY B  178  1                                  10    
HELIX   24  24 GLU B  180  GLN B  186  1                                   7    
HELIX   25  25 ASN B  210  THR B  224  1                                  15    
HELIX   26  26 SER B  231  ASN B  245  1                                  15    
HELIX   27  27 ARG B  248  GLU B  265  1                                  18    
HELIX   28  28 GLY B  283  ARG B  297  1                                  15    
HELIX   29  29 SER B  316  LEU B  331  1                                  16    
HELIX   30  30 SER C    6  THR C   10  5                                   5    
HELIX   31  31 SER C   13  ALA C   23  1                                  11    
HELIX   32  32 ASP C   33  GLY C   48  1                                  16    
HELIX   33  33 THR C   57  CYS C   70  1                                  14    
HELIX   34  34 GLY C   90  SER C   97  1                                   8    
HELIX   35  35 PRO C  112  LYS C  119  1                                   8    
HELIX   36  36 PRO C  145  ARG C  159  1                                  15    
HELIX   37  37 ARG C  169  GLY C  178  1                                  10    
HELIX   38  38 LEU C  181  GLN C  186  1                                   6    
HELIX   39  39 ASN C  210  THR C  224  1                                  15    
HELIX   40  40 SER C  231  ASN C  245  1                                  15    
HELIX   41  41 ARG C  248  ALA C  266  1                                  19    
HELIX   42  42 ASN C  286  ARG C  297  1                                  12    
HELIX   43  43 SER C  316  LEU C  331  1                                  16    
HELIX   44  44 SER D   13  ALA D   23  1                                  11    
HELIX   45  45 ASP D   33  GLY D   48  1                                  16    
HELIX   46  46 THR D   57  CYS D   70  1                                  14    
HELIX   47  47 ALA D   82  PHE D   87  1                                   6    
HELIX   48  48 GLY D   90  LEU D   95  1                                   6    
HELIX   49  49 PRO D  112  MET D  118  1                                   7    
HELIX   50  50 PRO D  145  ARG D  159  1                                  15    
HELIX   51  51 ARG D  169  GLY D  178  1                                  10    
HELIX   52  52 LEU D  181  GLN D  186  1                                   6    
HELIX   53  53 ASN D  210  THR D  224  1                                  15    
HELIX   54  54 SER D  231  ASN D  245  1                                  15    
HELIX   55  55 ARG D  248  ALA D  266  1                                  19    
HELIX   56  56 ASN D  286  ARG D  297  1                                  12    
HELIX   57  57 SER D  316  ALA D  332  1                                  17    
SHEET    1   A 2 ILE A   2  ASP A   3  0                                        
SHEET    2   A 2 VAL A 299  LEU A 300  1  O  LEU A 300   N  ILE A   2           
SHEET    1   B 7 ALA A  51  LEU A  55  0                                        
SHEET    2   B 7 SER A 205  GLY A 209 -1  O  GLY A 209   N  ALA A  51           
SHEET    3   B 7 SER A 190  CYS A 194 -1  N  PHE A 191   O  VAL A 208           
SHEET    4   B 7 ALA A 162  ASP A 166  1  N  VAL A 165   O  SER A 190           
SHEET    5   B 7 ARG A 129  GLU A 136  1  N  LEU A 135   O  HIS A 164           
SHEET    6   B 7 GLU A  74  GLY A  79  1  N  GLU A  75   O  LYS A 131           
SHEET    7   B 7 GLN A  99  ILE A 103  1  O  GLN A 101   N  TYR A  76           
SHEET    1   C 3 VAL A 270  ASP A 274  0                                        
SHEET    2   C 3 MET A 277  ARG A 281 -1  O  PHE A 279   N  ARG A 272           
SHEET    3   C 3 ILE A 306  VAL A 310 -1  O  LEU A 309   N  LEU A 278           
SHEET    1   D 2 ILE B   2  ASP B   3  0                                        
SHEET    2   D 2 VAL B 299  LEU B 300  1  O  LEU B 300   N  ILE B   2           
SHEET    1   E 7 ALA B  51  LEU B  55  0                                        
SHEET    2   E 7 SER B 205  GLY B 209 -1  O  SER B 205   N  LEU B  55           
SHEET    3   E 7 SER B 190  CYS B 194 -1  N  ILE B 193   O  LEU B 206           
SHEET    4   E 7 ALA B 162  ASP B 166  1  N  VAL B 165   O  SER B 190           
SHEET    5   E 7 ARG B 129  GLU B 136  1  N  LEU B 135   O  ASP B 166           
SHEET    6   E 7 GLU B  74  GLY B  79  1  N  GLU B  75   O  ARG B 129           
SHEET    7   E 7 GLN B  99  ILE B 103  1  O  GLN B  99   N  GLU B  74           
SHEET    1   F 3 VAL B 270  ASP B 274  0                                        
SHEET    2   F 3 MET B 277  ARG B 281 -1  O  PHE B 279   N  ARG B 272           
SHEET    3   F 3 ILE B 306  VAL B 310 -1  O  VAL B 307   N  VAL B 280           
SHEET    1   G 2 ILE C   2  ASP C   3  0                                        
SHEET    2   G 2 VAL C 299  LEU C 300  1  O  LEU C 300   N  ILE C   2           
SHEET    1   H 7 ALA C  51  LEU C  55  0                                        
SHEET    2   H 7 SER C 205  GLY C 209 -1  O  SER C 205   N  LEU C  55           
SHEET    3   H 7 SER C 190  CYS C 194 -1  N  ILE C 193   O  LEU C 206           
SHEET    4   H 7 ALA C 162  ASP C 166  1  N  VAL C 165   O  SER C 190           
SHEET    5   H 7 ARG C 129  GLU C 136  1  N  LEU C 135   O  ASP C 166           
SHEET    6   H 7 GLU C  74  GLY C  79  1  N  GLU C  75   O  LYS C 131           
SHEET    7   H 7 GLN C  99  ILE C 103  1  O  GLN C 101   N  TYR C  76           
SHEET    1   I 3 VAL C 270  ASP C 274  0                                        
SHEET    2   I 3 MET C 277  ARG C 281 -1  O  PHE C 279   N  MET C 271           
SHEET    3   I 3 ILE C 306  VAL C 310 -1  O  VAL C 307   N  VAL C 280           
SHEET    1   J 2 ILE D   2  ASP D   3  0                                        
SHEET    2   J 2 VAL D 299  LEU D 300  1  O  LEU D 300   N  ILE D   2           
SHEET    1   K 7 ALA D  51  LEU D  55  0                                        
SHEET    2   K 7 SER D 205  GLY D 209 -1  O  GLY D 209   N  ALA D  51           
SHEET    3   K 7 SER D 190  CYS D 194 -1  N  PHE D 191   O  VAL D 208           
SHEET    4   K 7 ALA D 162  ASP D 166  1  N  VAL D 165   O  SER D 190           
SHEET    5   K 7 ARG D 129  GLU D 136  1  N  LYS D 131   O  ALA D 162           
SHEET    6   K 7 GLU D  74  GLY D  79  1  N  GLU D  75   O  LYS D 131           
SHEET    7   K 7 GLN D  99  ILE D 103  1  O  GLN D 101   N  TYR D  76           
SHEET    1   L 3 ASP D 269  ASP D 274  0                                        
SHEET    2   L 3 MET D 277  ARG D 281 -1  O  ARG D 281   N  ASP D 269           
SHEET    3   L 3 ILE D 306  VAL D 310 -1  O  LEU D 309   N  LEU D 278           
LINK         OG1 THR A  10                NA    NA A 401     1555   1555  2.51  
LINK         O   THR C  10                NA    NA C 401     1555   1555  2.52  
LINK         O   SER B 196                NA    NA B 402     1555   1555  2.53  
LINK         O   THR B  10                NA    NA B 402     1555   1555  2.55  
LINK         O   SER C 196                NA    NA C 401     1555   1555  2.57  
LINK         O   SER A 196                NA    NA A 401     1555   1555  2.61  
LINK         O   THR A  10                NA    NA A 401     1555   1555  2.63  
LINK         OG1 THR C  10                NA    NA C 401     1555   1555  2.71  
LINK         O   SER D 196                NA    NA D 402     1555   1555  2.72  
LINK         O   THR D  10                NA    NA D 402     1555   1555  2.73  
LINK         O   THR D 201                NA    NA D 402     1555   1555  2.76  
LINK         OG  SER D  97                NA    NA D 401     1555   1555  2.76  
LINK         OG  SER A  97                NA    NA D 401     1555   1555  2.76  
LINK         OG1 THR B  10                NA    NA B 402     1555   1555  2.77  
LINK         O   THR B 201                NA    NA B 402     1555   1555  2.80  
LINK         OG  SER B  97                NA    NA B 401     1555   1555  2.80  
LINK         O   THR A   8                NA    NA A 401     1555   1555  2.81  
LINK         O   THR D   8                NA    NA D 402     1555   1555  2.87  
LINK         OG  SER C  97                NA    NA B 401     1555   1555  2.89  
LINK         O   THR C 201                NA    NA C 401     1555   1555  2.93  
LINK         O   THR C   8                NA    NA C 401     1555   1555  2.95  
LINK         O   ALA B  93                NA    NA B 401     1555   1555  2.96  
LINK         O   THR A 201                NA    NA A 401     1555   1555  2.98  
LINK         O   ALA D  93                NA    NA D 401     1555   1555  2.98  
LINK         O   THR B   8                NA    NA B 402     1555   1555  3.03  
LINK         OG1 THR D  10                NA    NA D 402     1555   1555  3.04  
LINK         O   ALA A  93                NA    NA D 401     1555   1555  3.14  
LINK         O   VAL B  94                NA    NA B 401     1555   1555  3.15  
LINK         O   ALA C  93                NA    NA B 401     1555   1555  3.18  
LINK        NA    NA B 401                 O   HOH A 679     1555   1555  2.68  
LINK        NA    NA B 401                 O   HOH C 641     1555   1555  2.75  
LINK        NA    NA D 401                 O   HOH C 641     1555   1555  2.97  
LINK        NA    NA D 401                 O   HOH A 679     1555   1555  3.16  
LINK         C   SER A 196                 N   LLP A 197     1555   1555  1.32  
LINK         C   LLP A 197                 N   GLY A 198     1555   1555  1.33  
LINK         C   SER B 196                 N   LLP B 197     1555   1555  1.32  
LINK         C   LLP B 197                 N   GLY B 198     1555   1555  1.33  
LINK         C   SER C 196                 N   LLP C 197     1555   1555  1.33  
LINK         C   LLP C 197                 N   GLY C 198     1555   1555  1.33  
LINK         C   SER D 196                 N   LLP D 197     1555   1555  1.33  
LINK         C   LLP D 197                 N   GLY D 198     1555   1555  1.33  
SITE     1 AC1  5 THR A   8  THR A  10  SER A 196  THR A 201                    
SITE     2 AC1  5 GLN B 230                                                     
SITE     1 AC2 13 SER A   6  HIS A  83  ARG A 169  LLP A 197                    
SITE     2 AC2 13 ARG A 308  HOH A 680  HOH A 682  HOH A 706                    
SITE     3 AC2 13 HOH A 709  HOH A 726  HOH A 727  ARG B 229                    
SITE     4 AC2 13 HIS D 126                                                     
SITE     1 AC3  8 HOH A 679  ALA B  93  VAL B  94  SER B  97                    
SITE     2 AC3  8 ALA C  93  VAL C  94  SER C  97  HOH C 641                    
SITE     1 AC4  5 GLN A 230  THR B   8  THR B  10  SER B 196                    
SITE     2 AC4  5 THR B 201                                                     
SITE     1 AC5 10 ARG A 229  SER B   6  HIS B  83  ARG B 169                    
SITE     2 AC5 10 ARG B 308  HOH B 586  HOH B 664  HOH B 666                    
SITE     3 AC5 10 HOH B 667  HIS C 126                                          
SITE     1 AC6  5 THR C   8  THR C  10  SER C 196  THR C 201                    
SITE     2 AC6  5 GLN D 230                                                     
SITE     1 AC7  8 HIS B 126  SER C   6  HIS C  83  ARG C 169                    
SITE     2 AC7  8 ARG C 308  HOH C 647  HOH C 674  ARG D 229                    
SITE     1 AC8  7 ALA A  93  VAL A  94  SER A  97  HOH C 641                    
SITE     2 AC8  7 ALA D  93  VAL D  94  SER D  97                               
SITE     1 AC9  5 GLN C 230  THR D   8  THR D  10  SER D 196                    
SITE     2 AC9  5 THR D 201                                                     
SITE     1 BC1 12 HIS A 126  ARG C 229  HOH C 676  SER D   6                    
SITE     2 BC1 12 HIS D  83  ARG D 169  ARG D 308  HOH D 602                    
SITE     3 BC1 12 HOH D 631  HOH D 692  HOH D 693  HOH D 696                    
CRYST1   77.160  104.880   84.910  90.00  92.49  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012960  0.000000  0.000564        0.00000                         
SCALE2      0.000000  0.009535  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011788        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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