GenomeNet

Database: PDB
Entry: 4LNM
LinkDB: 4LNM
Original site: 4LNM 
HEADER    LYASE                                   11-JUL-13   4LNM              
TITLE     STRUCTURE OF ESCHERICHIA COLI THREONINE ALDOLASE IN COMPLEX WITH      
TITLE    2 SERINE                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LOW-SPECIFICITY L-THREONINE ALDOLASE;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 4.1.2.5;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 945433;                                              
SOURCE   4 GENE: ECOM_01176, LTAE;                                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET22B(+)                                 
KEYWDS    THREONINE ALDOLASE, VITAMIN B6, PLP, ALDIMINE, FOLD TYPE 1, AMINO     
KEYWDS   2 ACID SYNTHESIS, LYASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.K.SAFO,R.CONTESTABILE,S.G.REMESH                                    
REVDAT   2   22-JAN-14 4LNM    1       JRNL                                     
REVDAT   1   06-NOV-13 4LNM    0                                                
JRNL        AUTH   M.L.DI SALVO,S.G.REMESH,M.VIVOLI,M.S.GHATGE,A.PAIARDINI,     
JRNL        AUTH 2 S.D'AGUANNO,M.K.SAFO,R.CONTESTABILE                          
JRNL        TITL   ON THE CATALYTIC MECHANISM AND STEREOSPECIFICITY OF          
JRNL        TITL 2 ESCHERICHIA COLI L-THREONINE ALDOLASE.                       
JRNL        REF    FEBS J.                       V. 281   129 2014              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   24165453                                                     
JRNL        DOI    10.1111/FEBS.12581                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3770020.020                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 30555                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1513                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.28                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2981                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2950                       
REMARK   3   BIN FREE R VALUE                    : 0.3560                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 155                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.029                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5086                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 251                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.93000                                             
REMARK   3    B22 (A**2) : -2.44000                                             
REMARK   3    B33 (A**2) : 4.36000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.28                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.38                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.43                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.900                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.150                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 44.55                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NONE                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4LNM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB080855.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
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   : 30725                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.8                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.10500                            
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) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CASPR                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 4LNJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 274 UM OF ENZYME WITH 2 MM L-SERINE,     
REMARK 280  0.2 M CALCIUM CHLORIDE HEXAHYDRATE, 0.1 M HEPES, 28% PEG 200, PH    
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.20000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.20000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       38.60000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.52500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       38.60000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.52500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       88.20000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       38.60000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.52500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       88.20000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       38.60000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.52500            
REMARK 290   SMTRY3   8  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: 17820 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 45470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       88.20000            
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     ALA A   332                                                      
REMARK 465     ARG A   333                                                      
REMARK 465     ALA B   332                                                      
REMARK 465     ARG B   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   NH1  ARG A   272     OD2  ASP A   274              1.98            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B 285   CB    GLU B 285   CG     -0.138                       
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    HIS A 126   CA  -  CB  -  CG  ANGL. DEV. =  21.6 DEGREES          
REMARK 500    ASN A 137   CB  -  CA  -  C   ANGL. DEV. =  12.6 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    THR A 138       95.71     45.98                                   
REMARK 500    TYR A 187       36.22    -98.26                                   
REMARK 500    LYS A 197     -108.84   -103.01                                   
REMARK 500    ARG A 229      -96.29    -95.80                                   
REMARK 500    GLN A 273       72.33   -159.66                                   
REMARK 500    THR A 275     -128.64     14.86                                   
REMARK 500    GLU A 285       12.01     42.13                                   
REMARK 500    SER A 304      160.08    175.85                                   
REMARK 500    PHE A 330       20.75    -68.75                                   
REMARK 500    ALA B  89       25.73     48.05                                   
REMARK 500    ILE B 125        0.20    -61.00                                   
REMARK 500    LYS B 131      -34.31   -141.91                                   
REMARK 500    THR B 138       84.25     59.08                                   
REMARK 500    LYS B 197     -110.43   -117.44                                   
REMARK 500    ARG B 229     -106.21    -88.00                                   
REMARK 500    THR B 275     -130.06     34.35                                   
REMARK 500    GLU B 285      -86.64    -67.93                                   
REMARK 500    ASN B 286       -1.64    -50.78                                   
REMARK 500    ALA B 287      -73.96    -61.92                                   
REMARK 500    SER B 304      160.43    174.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN A  137     THR A  138                 -137.51                    
REMARK 500 ARG A  272     GLN A  273                 -146.86                    
REMARK 500 ASN B  137     THR B  138                 -141.35                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN A 137        24.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              CA A 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 201   O                                                      
REMARK 620 2 SER A 196   O    82.1                                              
REMARK 620 3 THR A  10   O   108.7 150.3                                        
REMARK 620 4 THR A   8   O   153.2  87.4  92.5                                  
REMARK 620 5 THR A  10   OG1 102.3  84.2  66.6 101.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 404  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B  97   OG                                                     
REMARK 620 2 SER A  97   OG  148.8                                              
REMARK 620 3 HOH B 625   O    70.0  85.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 201   O                                                      
REMARK 620 2 THR B  10   O   113.1                                              
REMARK 620 3 THR B  10   OG1 113.6  62.7                                        
REMARK 620 4 SER B 196   O    93.7 148.4  91.9                                  
REMARK 620 5 THR B   8   O   146.9  88.4  98.4  76.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLG A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LNJ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF ESCHERICHIA COLI THREONINE ALDOLASE IN                  
REMARK 900 UNLIGANDED FORM                                                      
REMARK 900 RELATED ID: 4LNL   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF ESCHERICHIA COLI THREONINE ALDOLASE IN COMPLEX          
REMARK 900 WITH ALLO-THR                                                        
DBREF  4LNM A    1   333  UNP    E7U392   E7U392_ECOLX     1    333             
DBREF  4LNM B    1   333  UNP    E7U392   E7U392_ECOLX     1    333             
SEQADV 4LNM THR A  256  UNP  E7U392    ALA   256 CONFLICT                       
SEQADV 4LNM ALA A  257  UNP  E7U392    THR   257 CONFLICT                       
SEQADV 4LNM THR B  256  UNP  E7U392    ALA   256 CONFLICT                       
SEQADV 4LNM ALA B  257  UNP  E7U392    THR   257 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 LYS 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 LYS 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                              
HET    PLG  A 401      40                                                       
HET     CA  A 402       1                                                       
HET    PLR  A 403      30                                                       
HET     CA  A 404       1                                                       
HET    EPE  A 405      15                                                       
HET     CA  B 401       1                                                       
HET    EPE  B 402      15                                                       
HETNAM     PLG N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-              
HETNAM   2 PLG  PYRIDIN-4-YL-METHANE]                                           
HETNAM      CA CALCIUM ION                                                      
HETNAM     PLR (5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL DIHYDROGEN            
HETNAM   2 PLR  PHOSPHATE                                                       
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETSYN     PLG N-PYRIDOXYL-GLYCINE-5-MONOPHOSPHATE                              
HETSYN     PLR 4'-DEOXYPYRIDOXINE PHOSPHATE                                     
HETSYN     EPE HEPES                                                            
FORMUL   3  PLG    C10 H15 N2 O7 P                                              
FORMUL   4   CA    3(CA 2+)                                                     
FORMUL   5  PLR    C8 H12 N O5 P                                                
FORMUL   7  EPE    2(C8 H18 N2 O4 S)                                            
FORMUL  10  HOH   *251(H2 O)                                                    
HELIX    1   1 SER A    6  THR A   10  5                                   5    
HELIX    2   2 SER A   13  ALA A   22  1                                  10    
HELIX    3   3 ASP A   27  GLY A   31  5                                   5    
HELIX    4   4 ASP A   33  GLY A   48  1                                  16    
HELIX    5   5 THR A   57  CYS A   70  1                                  14    
HELIX    6   6 ALA A   82  PHE A   87  1                                   6    
HELIX    7   7 GLY A   90  LEU A   95  1                                   6    
HELIX    8   8 PRO A  112  ILE A  120  1                                   9    
HELIX    9   9 PRO A  145  ARG A  159  1                                  15    
HELIX   10  10 ARG A  169  GLY A  178  1                                  10    
HELIX   11  11 LEU A  181  GLN A  186  1                                   6    
HELIX   12  12 ASN A  210  GLY A  225  1                                  16    
HELIX   13  13 SER A  231  ASN A  245  1                                  15    
HELIX   14  14 ARG A  248  GLY A  267  1                                  20    
HELIX   15  15 ALA A  289  ARG A  297  1                                   9    
HELIX   16  16 SER A  316  PHE A  330  1                                  15    
HELIX   17  17 SER B   13  ALA B   23  1                                  11    
HELIX   18  18 ASP B   33  SER B   47  1                                  15    
HELIX   19  19 THR B   57  CYS B   70  1                                  14    
HELIX   20  20 ALA B   82  PHE B   87  1                                   6    
HELIX   21  21 GLY B   90  LEU B   95  1                                   6    
HELIX   22  22 PRO B  112  ILE B  120  1                                   9    
HELIX   23  23 PRO B  145  ASN B  160  1                                  16    
HELIX   24  24 ARG B  169  GLY B  178  1                                  10    
HELIX   25  25 GLU B  180  GLN B  186  1                                   7    
HELIX   26  26 ASN B  210  GLY B  225  1                                  16    
HELIX   27  27 SER B  231  ASN B  245  1                                  15    
HELIX   28  28 ARG B  248  GLY B  267  1                                  20    
HELIX   29  29 GLU B  285  ARG B  297  1                                  13    
HELIX   30  30 SER B  316  PHE B  330  1                                  15    
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  SER A 205   N  LEU A  55           
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  THR A 192           
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  MET A 271           
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  PHE B 191   O  VAL B 208           
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  ILE B  77   O  SER B 134           
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  MET B 277   N  ASP B 274           
SHEET    3   F 3 ILE B 306  VAL B 310 -1  O  VAL B 307   N  VAL B 280           
LINK         O   THR A 201                CA    CA A 402     1555   1555  2.71  
LINK         OG  SER B  97                CA    CA A 404     1555   1555  2.74  
LINK         O   THR B 201                CA    CA B 401     1555   1555  2.74  
LINK         O   SER A 196                CA    CA A 402     1555   1555  2.74  
LINK         O   THR A  10                CA    CA A 402     1555   1555  2.78  
LINK         O   THR B  10                CA    CA B 401     1555   1555  2.78  
LINK         OG  SER A  97                CA    CA A 404     1555   1555  2.85  
LINK         OG1 THR B  10                CA    CA B 401     1555   1555  2.86  
LINK         O   THR A   8                CA    CA A 402     1555   1555  2.92  
LINK         OG1 THR A  10                CA    CA A 402     1555   1555  2.95  
LINK         O   SER B 196                CA    CA B 401     1555   1555  2.98  
LINK         O   THR B   8                CA    CA B 401     1555   1555  3.14  
LINK        CA    CA A 404                 O   HOH B 625     1555   1555  2.92  
LINK         NZ  LYS A 197                 C4AAPLR A 403     1555   1555  1.51  
LINK         NZ  LYS B 197                 C4ABPLR A 403     1555   1555  1.56  
LINK         NZ  LYS B 197                 N  APLG A 401     1555   1555  2.03  
LINK         NZ  LYS B 197                 C4AAPLG A 401     1555   1555  2.13  
SITE     1 AC1 31 SER A   6  THR A  57  GLY A  58  THR A  59                    
SITE     2 AC1 31 HIS A  83  GLU A 136  ASP A 166  ALA A 168                    
SITE     3 AC1 31 ARG A 169  LYS A 197  LYS A 222  ARG A 229                    
SITE     4 AC1 31 ARG A 308  PLR A 403  HOH A 574  SER B   6                    
SITE     5 AC1 31 THR B  57  GLY B  58  THR B  59  HIS B  83                    
SITE     6 AC1 31 GLU B 136  ASP B 166  ALA B 168  ARG B 169                    
SITE     7 AC1 31 LYS B 197  ARG B 229  ARG B 308  HOH B 502                    
SITE     8 AC1 31 HOH B 591  HOH B 592  HOH B 638                               
SITE     1 AC2  5 THR A   8  THR A  10  SER A 196  THR A 201                    
SITE     2 AC2  5 GLN B 230                                                     
SITE     1 AC3 26 THR A  57  GLY A  58  THR A  59  HIS A  83                    
SITE     2 AC3 26 GLU A 136  ASP A 166  ALA A 168  ARG A 169                    
SITE     3 AC3 26 LYS A 197  LYS A 222  ARG A 229  PLG A 401                    
SITE     4 AC3 26 HOH A 555  HOH A 574  THR B  57  GLY B  58                    
SITE     5 AC3 26 THR B  59  HIS B  83  GLU B 136  ASP B 166                    
SITE     6 AC3 26 ALA B 168  ARG B 169  LYS B 197  ARG B 229                    
SITE     7 AC3 26 HOH B 591  HOH B 592                                          
SITE     1 AC4  7 ALA A  93  VAL A  94  SER A  97  ALA B  93                    
SITE     2 AC4  7 VAL B  94  SER B  97  HOH B 625                               
SITE     1 AC5  9 ARG A 157  ASN A 160  LEU A 161  ASP A 189                    
SITE     2 AC5  9 ASN A 210  TYR A 213  ARG A 216  HOH A 543                    
SITE     3 AC5  9 LYS B 158                                                     
SITE     1 AC6  5 GLN A 230  THR B   8  THR B  10  SER B 196                    
SITE     2 AC6  5 THR B 201                                                     
SITE     1 AC7  6 GLU A 154  ASN B 160  ASP B 189  ASN B 210                    
SITE     2 AC7  6 ASP B 212  TYR B 213                                          
CRYST1   77.200  101.050  176.400  90.00  90.00  90.00 C 2 2 21     16          
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      0.012953  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009896  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005669        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system