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Database: PDB
Entry: 1BP0
LinkDB: 1BP0
Original site: 1BP0 
HEADER    TRANSFERASE                             11-AUG-98   1BP0              
TITLE     THYMIDYLATE SYNTHASE R23I MUTANT                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (THYMIDYLATE SYNTHASE);                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.1.1.45;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOBACILLUS CASEI;                            
SOURCE   3 ORGANISM_TAXID: 1582;                                                
SOURCE   4 STRAIN: CHI-2913;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: CHI-2913;                                  
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PKPTSD;                                   
SOURCE   9 OTHER_DETAILS: SYNTHETIC GENE                                        
KEYWDS    METHYLTRANSFERASE, NUCLEOTIDE BIOSYNTHESIS, TRANSFERASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.MORSE,J.FINER-MOORE,R.M.STROUD                                      
REVDAT   8   09-AUG-23 1BP0    1       REMARK                                   
REVDAT   7   03-NOV-21 1BP0    1       REMARK SEQADV LINK                       
REVDAT   6   13-JUL-11 1BP0    1       VERSN                                    
REVDAT   5   24-FEB-09 1BP0    1       VERSN                                    
REVDAT   4   01-APR-03 1BP0    1       JRNL                                     
REVDAT   3   04-FEB-00 1BP0    1       JRNL   REMARK                            
REVDAT   2   12-JAN-00 1BP0    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   12-JAN-00 1BP0    0                                                
JRNL        AUTH   R.J.MORSE,S.KAWASE,D.V.SANTI,J.FINER-MOORE,R.M.STROUD        
JRNL        TITL   ENERGETIC CONTRIBUTIONS OF FOUR ARGININES TO                 
JRNL        TITL 2 PHOSPHATE-BINDING IN THYMIDYLATE SYNTHASE ARE MORE THAN      
JRNL        TITL 3 ADDITIVE AND DEPEND ON OPTIMIZATION OF "EFFECTIVE CHARGE     
JRNL        TITL 4 BALANCE".                                                    
JRNL        REF    BIOCHEMISTRY                  V.  39  1011 2000              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10653645                                                     
JRNL        DOI    10.1021/BI9918590                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.M.STROUD,J.S.FINER-MOORE                                   
REMARK   1  TITL   STEREOCHEMISTRY OF A MULTISTEP/BIPARTITE METHYL TRANSFER     
REMARK   1  TITL 2 REACTION: THYMIDYLATE SYNTHASE                               
REMARK   1  REF    FASEB J.                      V.   7   671 1993              
REMARK   1  REFN                   ISSN 0892-6638                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.S.FINER-MOORE,E.B.FAUMAN,P.G.FOSTER,K.M.PERRY,D.V.SANTI,   
REMARK   1  AUTH 2 R.M.STROUD                                                   
REMARK   1  TITL   REFINED STRUCTURES OF SUBSTRATE-BOUND AND PHOSPHATE-BOUND    
REMARK   1  TITL 2 THYMIDYLATE SYNTHASE FROM LACTOBACILLUS CASEI                
REMARK   1  REF    J.MOL.BIOL.                   V. 232  1101 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   L.W.HARDY,J.S.FINER-MOORE,W.R.MONTFORT,M.O.JONES,D.V.SANTI,  
REMARK   1  AUTH 2 R.M.STROUD                                                   
REMARK   1  TITL   ATOMIC STRUCTURE OF THYMIDYLATE SYNTHASE: TARGET FOR         
REMARK   1  TITL 2 RATIONAL DRUG DESIGN                                         
REMARK   1  REF    SCIENCE                       V. 235   448 1987              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000.000                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 15939                          
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) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1592                            
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           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.50                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1488                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2900                       
REMARK   3   BIN FREE R VALUE                    : 0.3880                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.10                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 165                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2590                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 51                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.39                            
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) : 0.39                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.090                           
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) : 3.790 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.650 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.260 ; 1.500                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.250 ; 2.000                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM11.WAT                                    
REMARK   3  PARAMETER FILE  3  : PARAMED.LIG                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH11.WAT                                     
REMARK   3  TOPOLOGY FILE  3   : TOPO.DUMP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BP0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000008421.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 7.0                                
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 RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE MONOCHROMETER             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16217                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.6                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : 8.40000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: 1TDM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       81.10000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      162.20000            
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      121.65000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      202.75000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       40.55000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       81.10000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      162.20000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      202.75000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      121.65000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       40.55000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 5710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     -121.65000            
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 K      K A 318  LIES ON A SPECIAL POSITION.                          
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  24        3.11    -64.49                                   
REMARK 500    HIS A  25       -7.29     68.23                                   
REMARK 500    PRO A  45       49.44    -69.07                                   
REMARK 500    LYS A  50      137.12   -170.99                                   
REMARK 500    PRO A  53       95.37    -66.38                                   
REMARK 500    MET A 101       52.21   -118.61                                   
REMARK 500    ALA A 115       28.65    -69.89                                   
REMARK 500    ALA A 116      -38.76   -143.13                                   
REMARK 500    ALA A 152       53.03   -155.45                                   
REMARK 500    ASP A 159     -168.64   -104.41                                   
REMARK 500    HIS A 174       66.27   -153.02                                   
REMARK 500    PRO A 197      127.98    -37.60                                   
REMARK 500    MET A 296      -67.72    -26.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 K A 52 IS A POSSIBLE POTASSIUM ION THAT LIES ON A MOLECULAR          
REMARK 600  AND CRYSTALLOGRAPHIC TWO-FOLD AXIS.                                 
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                               K A 318   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 183   OG                                                     
REMARK 620 2 SER A 183   OG  109.1                                              
REMARK 620 3 TRP A 185   O    84.5 113.8                                        
REMARK 620 4 TRP A 185   O   114.4  84.4 148.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CAT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATALYTIC CYSTEINE                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 318                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMP A 317                 
DBREF  1BP0 A    1   316  UNP    P00469   TYSY_LACCA       1    316             
SEQADV 1BP0 ILE A   23  UNP  P00469    ARG    23 ENGINEERED MUTATION            
SEQRES   1 A  316  MET LEU GLU GLN PRO TYR LEU ASP LEU ALA LYS LYS VAL          
SEQRES   2 A  316  LEU ASP GLU GLY HIS PHE LYS PRO ASP ILE THR HIS THR          
SEQRES   3 A  316  GLY THR TYR SER ILE PHE GLY HIS GLN MET ARG PHE ASP          
SEQRES   4 A  316  LEU SER LYS GLY PHE PRO LEU LEU THR THR LYS LYS VAL          
SEQRES   5 A  316  PRO PHE GLY LEU ILE LYS SER GLU LEU LEU TRP PHE LEU          
SEQRES   6 A  316  HIS GLY ASP THR ASN ILE ARG PHE LEU LEU GLN HIS ARG          
SEQRES   7 A  316  ASN HIS ILE TRP ASP GLU TRP ALA PHE GLU LYS TRP VAL          
SEQRES   8 A  316  LYS SER ASP GLU TYR HIS GLY PRO ASP MET THR ASP PHE          
SEQRES   9 A  316  GLY HIS ARG SER GLN LYS ASP PRO GLU PHE ALA ALA VAL          
SEQRES  10 A  316  TYR HIS GLU GLU MET ALA LYS PHE ASP ASP ARG VAL LEU          
SEQRES  11 A  316  HIS ASP ASP ALA PHE ALA ALA LYS TYR GLY ASP LEU GLY          
SEQRES  12 A  316  LEU VAL TYR GLY SER GLN TRP ARG ALA TRP HIS THR SER          
SEQRES  13 A  316  LYS GLY ASP THR ILE ASP GLN LEU GLY ASP VAL ILE GLU          
SEQRES  14 A  316  GLN ILE LYS THR HIS PRO TYR SER ARG ARG LEU ILE VAL          
SEQRES  15 A  316  SER ALA TRP ASN PRO GLU ASP VAL PRO THR MET ALA LEU          
SEQRES  16 A  316  PRO PRO CYS HIS THR LEU TYR GLN PHE TYR VAL ASN ASP          
SEQRES  17 A  316  GLY LYS LEU SER LEU GLN LEU TYR GLN ARG SER ALA ASP          
SEQRES  18 A  316  ILE PHE LEU GLY VAL PRO PHE ASN ILE ALA SER TYR ALA          
SEQRES  19 A  316  LEU LEU THR HIS LEU VAL ALA HIS GLU CYS GLY LEU GLU          
SEQRES  20 A  316  VAL GLY GLU PHE ILE HIS THR PHE GLY ASP ALA HIS LEU          
SEQRES  21 A  316  TYR VAL ASN HIS LEU ASP GLN ILE LYS GLU GLN LEU SER          
SEQRES  22 A  316  ARG THR PRO ARG PRO ALA PRO THR LEU GLN LEU ASN PRO          
SEQRES  23 A  316  ASP LYS HIS ASP ILE PHE ASP PHE ASP MET LYS ASP ILE          
SEQRES  24 A  316  LYS LEU LEU ASN TYR ASP PRO TYR PRO ALA ILE LYS ALA          
SEQRES  25 A  316  PRO VAL ALA VAL                                              
HET      K  A 318       1                                                       
HET    UMP  A 317      20                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM     UMP 2'-DEOXYURIDINE 5'-MONOPHOSPHATE                                 
HETSYN     UMP DUMP                                                             
FORMUL   2    K    K 1+                                                         
FORMUL   3  UMP    C9 H13 N2 O8 P                                               
FORMUL   4  HOH   *51(H2 O)                                                     
HELIX    1   1 LEU A    2  GLU A   16  5                                  15    
HELIX    2   2 PHE A   54  LEU A   65  1                                  12    
HELIX    3   3 ILE A   71  HIS A   77  5                                   7    
HELIX    4   4 ASP A   83  VAL A   91  1                                   9    
HELIX    5   5 PHE A  104  LYS A  110  1                                   7    
HELIX    6   6 PHE A  114  HIS A  131  1                                  18    
HELIX    7   7 ASP A  133  TYR A  139  1                                   7    
HELIX    8   8 TYR A  146  ARG A  151  1                                   6    
HELIX    9   9 GLN A  163  THR A  173  1                                  11    
HELIX   10  10 PRO A  187  THR A  192  1                                   6    
HELIX   11  11 VAL A  226  CYS A  244  1                                  19    
HELIX   12  12 VAL A  262  SER A  273  5                                  12    
HELIX   13  13 ILE A  291  ASP A  293  5                                   3    
HELIX   14  14 MET A  296  ASP A  298  5                                   3    
SHEET    1   A 4 HIS A  18  LYS A  20  0                                        
SHEET    2   A 4 THR A  28  PHE A  32 -1  N  SER A  30   O  HIS A  18           
SHEET    3   A 4 ASP A 257  TYR A 261 -1  N  LEU A 260   O  TYR A  29           
SHEET    4   A 4 SER A 219  ASP A 221  1  N  ALA A 220   O  ASP A 257           
SHEET    1   B 5 HIS A  34  ASP A  39  0                                        
SHEET    2   B 5 GLU A 250  PHE A 255 -1  N  PHE A 255   O  HIS A  34           
SHEET    3   B 5 LYS A 210  GLN A 217  1  N  LEU A 213   O  ILE A 252           
SHEET    4   B 5 HIS A 199  ASN A 207 -1  N  ASN A 207   O  LYS A 210           
SHEET    5   B 5 ILE A 181  SER A 183 -1  N  VAL A 182   O  TYR A 202           
SHEET    1   C 2 THR A 281  LEU A 284  0                                        
SHEET    2   C 2 ILE A 299  LEU A 302 -1  N  LEU A 302   O  THR A 281           
LINK         OG  SER A 183                 K     K A 318     1555   1555  2.81  
LINK         OG  SER A 183                 K     K A 318    11554   1555  2.82  
LINK         O   TRP A 185                 K     K A 318     1555   1555  2.42  
LINK         O   TRP A 185                 K     K A 318    11554   1555  2.41  
SITE     1 CAT  1 CYS A 198                                                     
SITE     1 AC1  2 SER A 183  TRP A 185                                          
SITE     1 AC2 14 ARG A 178  ARG A 179  LEU A 195  CYS A 198                    
SITE     2 AC2 14 HIS A 199  GLN A 217  ARG A 218  SER A 219                    
SITE     3 AC2 14 ALA A 220  ASP A 221  ASN A 229  HIS A 259                    
SITE     4 AC2 14 TYR A 261  HOH A 358                                          
CRYST1   79.100   79.100  243.300  90.00  90.00 120.00 P 61 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012642  0.007299  0.000000        0.00000                         
SCALE2      0.000000  0.014598  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004110        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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