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Database: PDB
Entry: 1DBT
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Original site: 1DBT 
HEADER    LYASE                                   03-NOV-99   1DBT              
TITLE     CRYSTAL STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE                       
TITLE    2 DECARBOXYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH UMP              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OROTIDINE 5'-PHOSPHATE DECARBOXYLASE;                      
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 EC: 4.1.1.23;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET-16B                                   
KEYWDS    DECARBOXYLASE, UMP, TIM BARREL, LYASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.C.APPLEBY,C.L.KINSLAND,T.P.BEGLEY,S.E.EALICK                        
REVDAT   4   24-FEB-09 1DBT    1       VERSN                                    
REVDAT   3   01-APR-03 1DBT    1       JRNL                                     
REVDAT   2   23-JUN-00 1DBT    3       HET    HETNAM FORMUL HETATM              
REVDAT   2 2                   3       CONECT                                   
REVDAT   1   06-MAR-00 1DBT    0                                                
JRNL        AUTH   T.C.APPLEBY,C.KINSLAND,T.P.BEGLEY,S.E.EALICK                 
JRNL        TITL   THE CRYSTAL STRUCTURE AND MECHANISM OF OROTIDINE             
JRNL        TITL 2 5'-MONOPHOSPHATE DECARBOXYLASE.                              
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  97  2005 2000              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   10681442                                                     
JRNL        DOI    10.1073/PNAS.259441296                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 29146                          
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) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2911                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4204                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190                       
REMARK   3   BIN FREE R VALUE                    : 0.2670                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.50                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 495                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5371                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 226                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.19                            
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) : 0.30                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.26                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.74                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NATIVE DATA USED TO REFINE MODEL          
REMARK   3  GENERATED FROM MAD PHASES                                           
REMARK   4                                                                      
REMARK   4 1DBT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB009952.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-AUG-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03321                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29779                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.23400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% (W/V) PEG 4000, 100MM HEPES PH       
REMARK 280  7.1, 5% 2-PROPANOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  295K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       39.20500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.88000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.20500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.88000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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       78.41000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       89.76000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   238                                                      
REMARK 465     SER A   239                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     ILE B   237                                                      
REMARK 465     LYS B   238                                                      
REMARK 465     SER B   239                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     ILE C   237                                                      
REMARK 465     LYS C   238                                                      
REMARK 465     SER C   239                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   ND2  ASN A     4     ND2  ASN A     4     2765     2.07            
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 120      -85.75    -85.57                                   
REMARK 500    ASN A 192     -134.68     57.88                                   
REMARK 500    GLN B  26     -110.12     58.27                                   
REMARK 500    THR B 120      -94.62    -85.76                                   
REMARK 500    ASN B 192     -125.01     58.00                                   
REMARK 500    THR C 120      -90.72    -87.73                                   
REMARK 500    ASN C 192     -120.90     58.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U5P A 250                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U5P B 251                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U5P C 252                 
DBREF  1DBT A    1   239  UNP    P25971   PYRF_BACSU       1    239             
DBREF  1DBT B    1   239  UNP    P25971   PYRF_BACSU       1    239             
DBREF  1DBT C    1   239  UNP    P25971   PYRF_BACSU       1    239             
SEQRES   1 A  239  MET LYS ASN ASN LEU PRO ILE ILE ALA LEU ASP PHE ALA          
SEQRES   2 A  239  SER ALA GLU GLU THR LEU ALA PHE LEU ALA PRO PHE GLN          
SEQRES   3 A  239  GLN GLU PRO LEU PHE VAL LYS VAL GLY MET GLU LEU PHE          
SEQRES   4 A  239  TYR GLN GLU GLY PRO SER ILE VAL LYS GLN LEU LYS GLU          
SEQRES   5 A  239  ARG ASN CYS GLU LEU PHE LEU ASP LEU LYS LEU HIS ASP          
SEQRES   6 A  239  ILE PRO THR THR VAL ASN LYS ALA MET LYS ARG LEU ALA          
SEQRES   7 A  239  SER LEU GLY VAL ASP LEU VAL ASN VAL HIS ALA ALA GLY          
SEQRES   8 A  239  GLY LYS LYS MET MET GLN ALA ALA LEU GLU GLY LEU GLU          
SEQRES   9 A  239  GLU GLY THR PRO ALA GLY LYS LYS ARG PRO SER LEU ILE          
SEQRES  10 A  239  ALA VAL THR GLN LEU THR SER THR SER GLU GLN ILE MET          
SEQRES  11 A  239  LYS ASP GLU LEU LEU ILE GLU LYS SER LEU ILE ASP THR          
SEQRES  12 A  239  VAL VAL HIS TYR SER LYS GLN ALA GLU GLU SER GLY LEU          
SEQRES  13 A  239  ASP GLY VAL VAL CYS SER VAL HIS GLU ALA LYS ALA ILE          
SEQRES  14 A  239  TYR GLN ALA VAL SER PRO SER PHE LEU THR VAL THR PRO          
SEQRES  15 A  239  GLY ILE ARG MET SER GLU ASP ALA ALA ASN ASP GLN VAL          
SEQRES  16 A  239  ARG VAL ALA THR PRO ALA ILE ALA ARG GLU LYS GLY SER          
SEQRES  17 A  239  SER ALA ILE VAL VAL GLY ARG SER ILE THR LYS ALA GLU          
SEQRES  18 A  239  ASP PRO VAL LYS ALA TYR LYS ALA VAL ARG LEU GLU TRP          
SEQRES  19 A  239  GLU GLY ILE LYS SER                                          
SEQRES   1 B  239  MET LYS ASN ASN LEU PRO ILE ILE ALA LEU ASP PHE ALA          
SEQRES   2 B  239  SER ALA GLU GLU THR LEU ALA PHE LEU ALA PRO PHE GLN          
SEQRES   3 B  239  GLN GLU PRO LEU PHE VAL LYS VAL GLY MET GLU LEU PHE          
SEQRES   4 B  239  TYR GLN GLU GLY PRO SER ILE VAL LYS GLN LEU LYS GLU          
SEQRES   5 B  239  ARG ASN CYS GLU LEU PHE LEU ASP LEU LYS LEU HIS ASP          
SEQRES   6 B  239  ILE PRO THR THR VAL ASN LYS ALA MET LYS ARG LEU ALA          
SEQRES   7 B  239  SER LEU GLY VAL ASP LEU VAL ASN VAL HIS ALA ALA GLY          
SEQRES   8 B  239  GLY LYS LYS MET MET GLN ALA ALA LEU GLU GLY LEU GLU          
SEQRES   9 B  239  GLU GLY THR PRO ALA GLY LYS LYS ARG PRO SER LEU ILE          
SEQRES  10 B  239  ALA VAL THR GLN LEU THR SER THR SER GLU GLN ILE MET          
SEQRES  11 B  239  LYS ASP GLU LEU LEU ILE GLU LYS SER LEU ILE ASP THR          
SEQRES  12 B  239  VAL VAL HIS TYR SER LYS GLN ALA GLU GLU SER GLY LEU          
SEQRES  13 B  239  ASP GLY VAL VAL CYS SER VAL HIS GLU ALA LYS ALA ILE          
SEQRES  14 B  239  TYR GLN ALA VAL SER PRO SER PHE LEU THR VAL THR PRO          
SEQRES  15 B  239  GLY ILE ARG MET SER GLU ASP ALA ALA ASN ASP GLN VAL          
SEQRES  16 B  239  ARG VAL ALA THR PRO ALA ILE ALA ARG GLU LYS GLY SER          
SEQRES  17 B  239  SER ALA ILE VAL VAL GLY ARG SER ILE THR LYS ALA GLU          
SEQRES  18 B  239  ASP PRO VAL LYS ALA TYR LYS ALA VAL ARG LEU GLU TRP          
SEQRES  19 B  239  GLU GLY ILE LYS SER                                          
SEQRES   1 C  239  MET LYS ASN ASN LEU PRO ILE ILE ALA LEU ASP PHE ALA          
SEQRES   2 C  239  SER ALA GLU GLU THR LEU ALA PHE LEU ALA PRO PHE GLN          
SEQRES   3 C  239  GLN GLU PRO LEU PHE VAL LYS VAL GLY MET GLU LEU PHE          
SEQRES   4 C  239  TYR GLN GLU GLY PRO SER ILE VAL LYS GLN LEU LYS GLU          
SEQRES   5 C  239  ARG ASN CYS GLU LEU PHE LEU ASP LEU LYS LEU HIS ASP          
SEQRES   6 C  239  ILE PRO THR THR VAL ASN LYS ALA MET LYS ARG LEU ALA          
SEQRES   7 C  239  SER LEU GLY VAL ASP LEU VAL ASN VAL HIS ALA ALA GLY          
SEQRES   8 C  239  GLY LYS LYS MET MET GLN ALA ALA LEU GLU GLY LEU GLU          
SEQRES   9 C  239  GLU GLY THR PRO ALA GLY LYS LYS ARG PRO SER LEU ILE          
SEQRES  10 C  239  ALA VAL THR GLN LEU THR SER THR SER GLU GLN ILE MET          
SEQRES  11 C  239  LYS ASP GLU LEU LEU ILE GLU LYS SER LEU ILE ASP THR          
SEQRES  12 C  239  VAL VAL HIS TYR SER LYS GLN ALA GLU GLU SER GLY LEU          
SEQRES  13 C  239  ASP GLY VAL VAL CYS SER VAL HIS GLU ALA LYS ALA ILE          
SEQRES  14 C  239  TYR GLN ALA VAL SER PRO SER PHE LEU THR VAL THR PRO          
SEQRES  15 C  239  GLY ILE ARG MET SER GLU ASP ALA ALA ASN ASP GLN VAL          
SEQRES  16 C  239  ARG VAL ALA THR PRO ALA ILE ALA ARG GLU LYS GLY SER          
SEQRES  17 C  239  SER ALA ILE VAL VAL GLY ARG SER ILE THR LYS ALA GLU          
SEQRES  18 C  239  ASP PRO VAL LYS ALA TYR LYS ALA VAL ARG LEU GLU TRP          
SEQRES  19 C  239  GLU GLY ILE LYS SER                                          
HET    U5P  A 250      21                                                       
HET    U5P  B 251      21                                                       
HET    U5P  C 252      21                                                       
HETNAM     U5P URIDINE-5'-MONOPHOSPHATE                                         
FORMUL   4  U5P    3(C9 H13 N2 O9 P)                                            
FORMUL   7  HOH   *226(H2 O)                                                    
HELIX    1   1 SER A   14  LEU A   22  1                                   9    
HELIX    2   2 ALA A   23  GLN A   26  5                                   4    
HELIX    3   3 GLY A   35  GLY A   43  1                                   9    
HELIX    4   4 GLY A   43  ARG A   53  1                                  11    
HELIX    5   5 ILE A   66  SER A   79  1                                  14    
HELIX    6   6 GLY A   92  THR A  107  1                                  16    
HELIX    7   7 SER A  126  GLU A  133  1                                   8    
HELIX    8   8 SER A  139  SER A  154  1                                  16    
HELIX    9   9 SER A  162  HIS A  164  5                                   3    
HELIX   10  10 GLU A  165  TYR A  170  1                                   6    
HELIX   11  11 THR A  199  LYS A  206  1                                   8    
HELIX   12  12 GLY A  214  LYS A  219  1                                   6    
HELIX   13  13 ASP A  222  GLY A  236  1                                  15    
HELIX   14  14 SER B   14  ALA B   23  1                                  10    
HELIX   15  15 PRO B   24  GLN B   26  5                                   3    
HELIX   16  16 GLY B   35  GLY B   43  1                                   9    
HELIX   17  17 GLY B   43  ARG B   53  1                                  11    
HELIX   18  18 ILE B   66  ALA B   78  1                                  13    
HELIX   19  19 GLY B   92  THR B  107  1                                  16    
HELIX   20  20 SER B  126  GLU B  133  1                                   8    
HELIX   21  21 SER B  139  SER B  154  1                                  16    
HELIX   22  22 SER B  162  HIS B  164  5                                   3    
HELIX   23  23 GLU B  165  GLN B  171  1                                   7    
HELIX   24  24 THR B  199  LYS B  206  1                                   8    
HELIX   25  25 GLY B  214  LYS B  219  1                                   6    
HELIX   26  26 ASP B  222  GLY B  236  1                                  15    
HELIX   27  27 SER C   14  ALA C   23  1                                  10    
HELIX   28  28 PRO C   24  GLN C   26  5                                   3    
HELIX   29  29 GLY C   35  GLY C   43  1                                   9    
HELIX   30  30 PRO C   44  GLU C   52  1                                   9    
HELIX   31  31 ILE C   66  ALA C   78  1                                  13    
HELIX   32  32 GLY C   92  THR C  107  1                                  16    
HELIX   33  33 SER C  126  GLU C  133  1                                   8    
HELIX   34  34 SER C  139  SER C  154  1                                  16    
HELIX   35  35 SER C  162  HIS C  164  5                                   3    
HELIX   36  36 GLU C  165  TYR C  170  1                                   6    
HELIX   37  37 THR C  199  LYS C  206  1                                   8    
HELIX   38  38 GLY C  214  LYS C  219  1                                   6    
HELIX   39  39 ASP C  222  GLY C  236  1                                  15    
SHEET    1   A 9 ILE A   7  ALA A   9  0                                        
SHEET    2   A 9 PHE A  31  VAL A  34  1  O  PHE A  31   N  ILE A   8           
SHEET    3   A 9 GLU A  56  LEU A  63  1  O  GLU A  56   N  VAL A  32           
SHEET    4   A 9 LEU A  84  HIS A  88  1  O  LEU A  84   N  LEU A  59           
SHEET    5   A 9 SER A 115  VAL A 119  1  O  SER A 115   N  VAL A  85           
SHEET    6   A 9 GLY A 158  VAL A 160  1  O  GLY A 158   N  ALA A 118           
SHEET    7   A 9 LEU A 178  THR A 181  1  O  LEU A 178   N  VAL A 159           
SHEET    8   A 9 ALA A 210  VAL A 213  1  O  ALA A 210   N  THR A 181           
SHEET    9   A 9 ILE A   7  ALA A   9  1  N  ILE A   7   O  ILE A 211           
SHEET    1   B 9 ILE B   7  LEU B  10  0                                        
SHEET    2   B 9 PHE B  31  VAL B  34  1  O  PHE B  31   N  ILE B   8           
SHEET    3   B 9 GLU B  56  LEU B  63  1  O  GLU B  56   N  VAL B  32           
SHEET    4   B 9 LEU B  84  HIS B  88  1  O  LEU B  84   N  LEU B  59           
SHEET    5   B 9 SER B 115  VAL B 119  1  O  SER B 115   N  VAL B  85           
SHEET    6   B 9 GLY B 158  VAL B 160  1  O  GLY B 158   N  ALA B 118           
SHEET    7   B 9 LEU B 178  THR B 181  1  O  LEU B 178   N  VAL B 159           
SHEET    8   B 9 ALA B 210  VAL B 213  1  O  ALA B 210   N  THR B 181           
SHEET    9   B 9 ILE B   7  LEU B  10  1  N  ILE B   7   O  ILE B 211           
SHEET    1   C 9 ILE C   7  ALA C   9  0                                        
SHEET    2   C 9 PHE C  31  VAL C  34  1  O  PHE C  31   N  ILE C   8           
SHEET    3   C 9 GLU C  56  LEU C  63  1  O  GLU C  56   N  VAL C  32           
SHEET    4   C 9 LEU C  84  HIS C  88  1  O  LEU C  84   N  LEU C  59           
SHEET    5   C 9 SER C 115  VAL C 119  1  O  SER C 115   N  VAL C  85           
SHEET    6   C 9 GLY C 158  VAL C 160  1  O  GLY C 158   N  ALA C 118           
SHEET    7   C 9 LEU C 178  THR C 181  1  O  LEU C 178   N  VAL C 159           
SHEET    8   C 9 ALA C 210  VAL C 213  1  O  ALA C 210   N  THR C 181           
SHEET    9   C 9 ILE C   7  ALA C   9  1  N  ILE C   7   O  ILE C 211           
SITE     1 AC1 19 ASP A  11  LYS A  33  LYS A  62  LEU A 122                    
SITE     2 AC1 19 THR A 123  VAL A 160  PRO A 182  ARG A 185                    
SITE     3 AC1 19 GLN A 194  VAL A 212  GLY A 214  ARG A 215                    
SITE     4 AC1 19 HOH A 254  HOH A 255  HOH A 268  HOH A 273                    
SITE     5 AC1 19 ASP B  65  ILE B  66  THR B  69                               
SITE     1 AC2 19 ASP A  65  ILE A  66  THR A  69  ASP B  11                    
SITE     2 AC2 19 LYS B  33  LYS B  62  LEU B 122  THR B 123                    
SITE     3 AC2 19 VAL B 160  PRO B 182  ARG B 185  GLN B 194                    
SITE     4 AC2 19 VAL B 212  GLY B 214  ARG B 215  HOH B 264                    
SITE     5 AC2 19 HOH B 271  HOH B 278  HOH B 284                               
SITE     1 AC3 19 ASP C  11  LYS C  33  LYS C  62  ASP C  65                    
SITE     2 AC3 19 ILE C  66  THR C  69  LEU C 122  THR C 123                    
SITE     3 AC3 19 VAL C 160  PRO C 182  ARG C 185  GLN C 194                    
SITE     4 AC3 19 VAL C 212  GLY C 214  ARG C 215  HOH C 256                    
SITE     5 AC3 19 HOH C 261  HOH C 264  HOH C 275                               
CRYST1   78.410   89.760  105.900  90.00  90.00  90.00 P 21 21 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      0.012753  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011141  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009443        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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