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Database: PDB
Entry: 4LNL
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Original site: 4LNL 
HEADER    LYASE                                   11-JUL-13   4LNL              
TITLE     STRUCTURE OF ESCHERICHIA COLI THREONINE ALDOLASE IN COMPLEX WITH ALLO-
TITLE    2 THR                                                                  
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                                                              
REVDAT   2   22-JAN-14 4LNL    1       JRNL                                     
REVDAT   1   06-NOV-13 4LNL    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) : 29.05                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3053392.070                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 37206                          
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) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1881                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
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) : 2.18                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3540                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE                    : 0.2720                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 206                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5096                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 466                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.40000                                             
REMARK   3    B22 (A**2) : -1.12000                                             
REMARK   3    B33 (A**2) : 1.52000                                              
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) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.18                            
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) : 0.29                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.24                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.600                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 2.040                           
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        : 0.38                                                 
REMARK   3   BSOL        : 65.28                                                
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 4LNL 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 RCSB080854.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUL-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                         : 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   : 37247                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.10900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8000                             
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     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.600                              
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 1LW5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 480 UM OF ENZYME, 28 MM L-THREONINE,     
REMARK 280  0.2 M MAGNESIUM CHLORIDE HEXAHYDRATE, 0.1 M HEPES, 30% PEG 400,     
REMARK 280  PH 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       88.00000            
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       88.00000            
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       38.20000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.44500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       38.20000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.44500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       88.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       38.20000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.44500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       88.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       38.20000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.44500            
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: 17340 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 44510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 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       88.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CL    CL A 405  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 688  LIES ON A SPECIAL POSITION.                          
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 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 A 136   CD    GLU A 136   OE1    -0.135                       
REMARK 500    GLU A 136   CD    GLU A 136   OE2    -0.120                       
REMARK 500    ASN A 137   C     ASN A 137   O      -0.220                       
REMARK 500    THR A 138   C     THR A 138   O      -0.134                       
REMARK 500    SER B 134   C     SER B 134   O      -0.129                       
REMARK 500    GLU B 136   CD    GLU B 136   OE1    -0.170                       
REMARK 500    GLU B 136   CD    GLU B 136   OE2    -0.187                       
REMARK 500    GLU B 136   C     GLU B 136   O      -0.130                       
REMARK 500    ASN B 137   C     ASN B 137   O      -0.159                       
REMARK 500    THR B 138   C     THR B 138   O      -0.180                       
REMARK 500    ASN B 140   C     ASN B 140   O      -0.155                       
REMARK 500    GLY B 141   C     GLY B 141   O      -0.113                       
REMARK 500    LYS B 142   CE    LYS B 142   NZ     -0.194                       
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    LEU A 135   CA  -  CB  -  CG  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    LEU A 135   CB  -  CG  -  CD1 ANGL. DEV. =  11.1 DEGREES          
REMARK 500    LEU A 135   CB  -  CG  -  CD2 ANGL. DEV. =  11.6 DEGREES          
REMARK 500    PRO B  34   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    LEU B 135   CB  -  CG  -  CD2 ANGL. DEV. =  11.6 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    TYR A  85      -52.62   -122.30                                   
REMARK 500    ALA A  89       26.10     49.59                                   
REMARK 500    LYS A 197     -110.06   -105.46                                   
REMARK 500    ARG A 229      -97.30    -93.27                                   
REMARK 500    THR A 275     -120.50     44.94                                   
REMARK 500    ALA A 287      -77.54    -44.85                                   
REMARK 500    SER A 304      164.15    173.21                                   
REMARK 500    LYS B 131      -35.55   -135.99                                   
REMARK 500    TYR B 187       30.16    -92.71                                   
REMARK 500    LYS B 197     -110.72   -111.68                                   
REMARK 500    ARG B 229     -101.39    -93.34                                   
REMARK 500    GLU B 265       42.15    -76.01                                   
REMARK 500    THR B 275     -122.77     34.53                                   
REMARK 500    SER B 304      166.11    177.86                                   
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    SER A 134        24.5      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 135        24.4      L          L   OUTSIDE RANGE           
REMARK 500    LEU B 135        24.5      L          L   OUTSIDE RANGE           
REMARK 500    LYS B 142        24.9      L          L   OUTSIDE RANGE           
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 636        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH A 684        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH B 640        DISTANCE =  5.17 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                              MG A 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 196   O                                                      
REMARK 620 2 THR A 201   O    84.7                                              
REMARK 620 3 THR A  10   OG1  85.5 105.5                                        
REMARK 620 4 THR A  10   O   153.9 110.2  70.1                                  
REMARK 620 5 THR A   8   O    85.4 153.5  98.1  88.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  10   O                                                      
REMARK 620 2 THR B 201   O   101.3                                              
REMARK 620 3 SER B 196   O   153.9  85.4                                        
REMARK 620 4 THR B   8   O   100.0 154.6  81.5                                  
REMARK 620 5 THR B  10   OG1  66.1  99.7  87.9 101.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B  97   OG                                                     
REMARK 620 2 SER A  97   OG  139.5                                              
REMARK 620 3 ALA A  93   O   111.1 108.3                                        
REMARK 620 4 HOH A 707   O    74.9  75.6 124.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2BO A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2BK A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLG B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 404                 
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: 4LNM   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF ESCHERICHIA COLI THREONINE ALDOLASE IN COMPLEX          
REMARK 900 WITH SERINE                                                          
DBREF  4LNL A    1   333  UNP    E7U392   E7U392_ECOLX     1    333             
DBREF  4LNL B    1   333  UNP    E7U392   E7U392_ECOLX     1    333             
SEQADV 4LNL THR A  256  UNP  E7U392    ALA   256 CONFLICT                       
SEQADV 4LNL ALA A  257  UNP  E7U392    THR   257 CONFLICT                       
SEQADV 4LNL THR B  256  UNP  E7U392    ALA   256 CONFLICT                       
SEQADV 4LNL 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     MG  A 401       1                                                       
HET    2BO  A 402      23                                                       
HET    2BK  A 403      23                                                       
HET    EPE  A 404      15                                                       
HET     CL  A 405       1                                                       
HET     MG  B 401       1                                                       
HET     MG  B 402       1                                                       
HET    PLG  B 403      20                                                       
HET    EPE  B 404      15                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     2BO N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-          
HETNAM   2 2BO  4-YL}METHYL)-L-THREONINE                                        
HETNAM     2BK N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-          
HETNAM   2 2BK  4-YL}METHYL)-L-ALLOTHREONINE                                    
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PLG N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-              
HETNAM   2 PLG  PYRIDIN-4-YL-METHANE]                                           
HETSYN     EPE HEPES                                                            
HETSYN     PLG N-PYRIDOXYL-GLYCINE-5-MONOPHOSPHATE                              
FORMUL   3   MG    3(MG 2+)                                                     
FORMUL   4  2BO    C12 H19 N2 O8 P                                              
FORMUL   5  2BK    C12 H19 N2 O8 P                                              
FORMUL   6  EPE    2(C8 H18 N2 O4 S)                                            
FORMUL   7   CL    CL 1-                                                        
FORMUL  10  PLG    C10 H15 N2 O7 P                                              
FORMUL  12  HOH   *466(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 ALA A   82  PHE A   87  1                                   6    
HELIX    5   5 GLY A   90  LEU A   95  1                                   6    
HELIX    6   6 PRO A  112  ILE A  120  1                                   9    
HELIX    7   7 PRO A  145  ASN A  160  1                                  16    
HELIX    8   8 ARG A  169  GLY A  178  1                                  10    
HELIX    9   9 LEU A  181  GLN A  186  1                                   6    
HELIX   10  10 ASN A  210  GLY A  225  1                                  16    
HELIX   11  11 SER A  231  ASN A  245  1                                  15    
HELIX   12  12 ARG A  248  GLY A  267  1                                  20    
HELIX   13  13 ASN A  286  ARG A  297  1                                  12    
HELIX   14  14 SER A  316  ALA A  332  1                                  17    
HELIX   15  15 SER B    6  THR B   10  5                                   5    
HELIX   16  16 SER B   13  ALA B   23  1                                  11    
HELIX   17  17 ASP B   33  GLY B   48  1                                  16    
HELIX   18  18 THR B   57  CYS B   70  1                                  14    
HELIX   19  19 ALA B   82  PHE B   87  1                                   6    
HELIX   20  20 GLY B   90  LEU B   95  1                                   6    
HELIX   21  21 PRO B  112  ILE B  120  1                                   9    
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 LEU B  181  GLN B  186  1                                   6    
HELIX   25  25 ASN B  210  GLY B  225  1                                  16    
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  ALA B  296  1                                  14    
HELIX   29  29 SER B  316  LEU B  331  1                                  16    
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  SER A 190           
SHEET    5   B 7 ARG A 129  GLU A 136  1  N  LEU A 135   O  ASP A 166           
SHEET    6   B 7 GLU A  74  GLY A  79  1  N  ILE A  77   O  LEU A 132           
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  VAL A 307   N  VAL A 280           
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  HIS B 164           
SHEET    6   E 7 GLU B  74  GLY B  79  1  N  ILE B  77   O  LEU B 132           
SHEET    7   E 7 GLN B  99  ILE B 103  1  O  GLN B 101   N  TYR B  76           
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  LEU B 309   N  LEU B 278           
LINK         O   SER A 196                MG    MG A 401     1555   1555  2.50  
LINK         O   THR A 201                MG    MG A 401     1555   1555  2.61  
LINK         O   THR B  10                MG    MG B 401     1555   1555  2.61  
LINK         O   THR B 201                MG    MG B 401     1555   1555  2.65  
LINK         OG1 THR A  10                MG    MG A 401     1555   1555  2.68  
LINK         OG  SER B  97                MG    MG B 402     1555   1555  2.70  
LINK         O   SER B 196                MG    MG B 401     1555   1555  2.73  
LINK         O   THR A  10                MG    MG A 401     1555   1555  2.76  
LINK         O   THR B   8                MG    MG B 401     1555   1555  2.77  
LINK         OG  SER A  97                MG    MG B 402     1555   1555  2.78  
LINK         OG1 THR B  10                MG    MG B 401     1555   1555  2.82  
LINK         O   THR A   8                MG    MG A 401     1555   1555  2.87  
LINK         O   ALA A  93                MG    MG B 402     1555   1555  2.93  
LINK        MG    MG B 402                 O   HOH A 707     1555   1555  2.70  
CISPEP   1 ASN A  137    THR A  138          0        -2.22                     
CISPEP   2 ASN B  137    THR B  138          0         2.64                     
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 22 SER A   6  THR A  57  GLY A  58  THR A  59                    
SITE     2 AC2 22 ASN A  62  HIS A  83  GLU A 136  ASP A 166                    
SITE     3 AC2 22 ALA A 168  ARG A 169  LYS A 197  ARG A 308                    
SITE     4 AC2 22 HOH A 525  HOH A 610  HOH A 611  HOH A 612                    
SITE     5 AC2 22 HOH A 689  HOH A 746  HIS B 126  ARG B 229                    
SITE     6 AC2 22 HOH B 564  HOH B 662                                          
SITE     1 AC3 22 SER A   6  THR A  57  GLY A  58  THR A  59                    
SITE     2 AC3 22 ASN A  62  HIS A  83  GLU A 136  ASP A 166                    
SITE     3 AC3 22 ALA A 168  ARG A 169  LYS A 197  ARG A 308                    
SITE     4 AC3 22 HOH A 525  HOH A 574  HOH A 610  HOH A 611                    
SITE     5 AC3 22 HOH A 612  HOH A 689  HOH A 746  HIS B 126                    
SITE     6 AC3 22 ARG B 229  HOH B 662                                          
SITE     1 AC4 12 ARG A 157  ASN A 160  LEU A 161  ALA A 162                    
SITE     2 AC4 12 ASP A 189  ASN A 210  ARG A 216  HOH A 533                    
SITE     3 AC4 12 HOH A 664  HOH A 692  HOH A 693  LYS B 158                    
SITE     1 AC5  2 GLU A  71  ARG A  72                                          
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  7 ALA A  93  VAL A  94  SER A  97  HOH A 707                    
SITE     2 AC7  7 ALA B  93  VAL B  94  SER B  97                               
SITE     1 AC8 19 ARG A 229  SER B   6  THR B  57  GLY B  58                    
SITE     2 AC8 19 THR B  59  ASN B  62  HIS B  83  GLU B 136                    
SITE     3 AC8 19 ASP B 166  ALA B 168  ARG B 169  LYS B 197                    
SITE     4 AC8 19 ARG B 308  HOH B 538  HOH B 592  HOH B 594                    
SITE     5 AC8 19 HOH B 598  HOH B 669  HOH B 685                               
SITE     1 AC9 11 GLU A 154  LYS A 158  HOH A 517  ASN B 160                    
SITE     2 AC9 11 ASP B 189  ASN B 210  ASP B 212  TYR B 213                    
SITE     3 AC9 11 ARG B 216  HOH B 513  HOH B 548                               
CRYST1   76.400  100.890  176.000  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      0.013089  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009912  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005682        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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