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Database: PDB
Entry: 2PA3
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Original site: 2PA3 
HEADER    OXIDOREDUCTASE                          27-MAR-07   2PA3              
TITLE     CRYSTAL STRUCTURE OF SERINE BOUND G336V MUTANT OF E.COLI              
TITLE    2 PHOSPHOGLYCERATE DEHYDROGENASE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-3-PHOSPHOGLYCERATE DEHYDROGENASE;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PGDH;                                                       
COMPND   5 EC: 1.1.1.95;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: SERA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;                                  
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRC99                                    
KEYWDS    OXIDOREDUCTASE, PHOSPHOGLYCERATE DEHYDROGENASE, SERINE BIOSYNTHESIS   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.DEY,J.C.SACCHETTINI                                                 
REVDAT   4   13-JUL-11 2PA3    1       VERSN                                    
REVDAT   3   24-FEB-09 2PA3    1       VERSN                                    
REVDAT   2   17-JUL-07 2PA3    1       JRNL                                     
REVDAT   1   24-APR-07 2PA3    0                                                
JRNL        AUTH   S.DEY,Z.HU,X.L.XU,J.C.SACCHETTINI,G.A.GRANT                  
JRNL        TITL   THE EFFECT OF HINGE MUTATIONS ON EFFECTOR BINDING AND DOMAIN 
JRNL        TITL 2 ROTATION IN ESCHERICHIA COLI D-3-PHOSPHOGLYCERATE            
JRNL        TITL 3 DEHYDROGENASE.                                               
JRNL        REF    J.BIOL.CHEM.                  V. 282 18418 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17459882                                                     
JRNL        DOI    10.1074/JBC.M701174200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.74 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 28694                          
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 + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1528                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.74                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.81                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2058                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.49                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 106                          
REMARK   3   BIN FREE R VALUE                    : 0.5410                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3076                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 18                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.08000                                              
REMARK   3    B22 (A**2) : 1.08000                                              
REMARK   3    B33 (A**2) : -1.61000                                             
REMARK   3    B12 (A**2) : 0.54000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.268         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.234         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.173         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.615         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3195 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4340 ; 1.811 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   405 ; 6.064 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   133 ;35.823 ;24.962       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   541 ;21.634 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;25.788 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   507 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2373 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1413 ; 0.269 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2146 ; 0.345 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   184 ; 0.189 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    84 ; 0.243 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.337 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2060 ; 3.989 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3238 ; 5.947 ; 7.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1238 ; 7.734 ; 9.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1102 ;10.015 ;11.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2PA3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB042156.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30270                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.740                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 20.400                             
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 39.7800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 16.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.59400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.230                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1PSD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG1000, 0.1M NA/K PHOSPHATE, 0.2M   
REMARK 280  MGCL2, PH 6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 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+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+2/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+1/3                                            
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      109.10667            
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       54.55333            
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  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      109.10667            
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       54.55333            
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      109.10667            
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       54.55333            
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      109.10667            
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        0.00000            
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       54.55333            
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,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 19000 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 63830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 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       76.39450            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000     -132.31916            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000     -109.10667            
REMARK 350   BIOMT1   4  0.500000  0.866025  0.000000       76.39450            
REMARK 350   BIOMT2   4  0.866025 -0.500000  0.000000     -132.31916            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000     -109.10667            
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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     VAL A     4                                                      
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    ILE A 381   CG1 -  CB  -  CG2 ANGL. DEV. = -14.8 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    ARG A  60     -132.22   -133.58                                   
REMARK 500    PHE A  82       62.51    -64.51                                   
REMARK 500    THR A  86        2.58   -154.37                                   
REMARK 500    ASN A 103     -159.44   -154.62                                   
REMARK 500    LEU A 142       74.92   -115.29                                   
REMARK 500    ALA A 191      172.32    -57.73                                   
REMARK 500    ASN A 219       20.38     45.67                                   
REMARK 500    SER A 239      -89.40    -88.64                                   
REMARK 500    ASP A 245       91.23    -64.31                                   
REMARK 500    PRO A 270      133.92    -37.82                                   
REMARK 500    ASN A 273        2.26    -60.16                                   
REMARK 500    ASN A 286       21.60    -79.56                                   
REMARK 500    SER A 323       -1.38     75.34                                   
REMARK 500    VAL A 336      155.04    -17.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     SER A  451                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SER A 451                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI A 450                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2P9C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2P9E   RELATED DB: PDB                                   
DBREF  2PA3 A    1   410  UNP    P0A9T0   SERA_ECOLI       1    410             
SEQADV 2PA3 ALA A   81  UNP  P0A9T0    CYS    81 ENGINEERED                     
SEQADV 2PA3 ALA A   83  UNP  P0A9T0    CYS    83 ENGINEERED                     
SEQADV 2PA3 ALA A  250  UNP  P0A9T0    CYS   250 ENGINEERED                     
SEQADV 2PA3 ALA A  282  UNP  P0A9T0    CYS   282 ENGINEERED                     
SEQADV 2PA3 VAL A  336  UNP  P0A9T0    GLY   336 ENGINEERED                     
SEQRES   1 A  410  MET ALA LYS VAL SER LEU GLU LYS ASP LYS ILE LYS PHE          
SEQRES   2 A  410  LEU LEU VAL GLU GLY VAL HIS GLN LYS ALA LEU GLU SER          
SEQRES   3 A  410  LEU ARG ALA ALA GLY TYR THR ASN ILE GLU PHE HIS LYS          
SEQRES   4 A  410  GLY ALA LEU ASP ASP GLU GLN LEU LYS GLU SER ILE ARG          
SEQRES   5 A  410  ASP ALA HIS PHE ILE GLY LEU ARG SER ARG THR HIS LEU          
SEQRES   6 A  410  THR GLU ASP VAL ILE ASN ALA ALA GLU LYS LEU VAL ALA          
SEQRES   7 A  410  ILE GLY ALA PHE ALA ILE GLY THR ASN GLN VAL ASP LEU          
SEQRES   8 A  410  ASP ALA ALA ALA LYS ARG GLY ILE PRO VAL PHE ASN ALA          
SEQRES   9 A  410  PRO PHE SER ASN THR ARG SER VAL ALA GLU LEU VAL ILE          
SEQRES  10 A  410  GLY GLU LEU LEU LEU LEU LEU ARG GLY VAL PRO GLU ALA          
SEQRES  11 A  410  ASN ALA LYS ALA HIS ARG GLY VAL TRP ASN LYS LEU ALA          
SEQRES  12 A  410  ALA GLY SER PHE GLU ALA ARG GLY LYS LYS LEU GLY ILE          
SEQRES  13 A  410  ILE GLY TYR GLY HIS ILE GLY THR GLN LEU GLY ILE LEU          
SEQRES  14 A  410  ALA GLU SER LEU GLY MET TYR VAL TYR PHE TYR ASP ILE          
SEQRES  15 A  410  GLU ASN LYS LEU PRO LEU GLY ASN ALA THR GLN VAL GLN          
SEQRES  16 A  410  HIS LEU SER ASP LEU LEU ASN MET SER ASP VAL VAL SER          
SEQRES  17 A  410  LEU HIS VAL PRO GLU ASN PRO SER THR LYS ASN MET MET          
SEQRES  18 A  410  GLY ALA LYS GLU ILE SER LEU MET LYS PRO GLY SER LEU          
SEQRES  19 A  410  LEU ILE ASN ALA SER ARG GLY THR VAL VAL ASP ILE PRO          
SEQRES  20 A  410  ALA LEU ALA ASP ALA LEU ALA SER LYS HIS LEU ALA GLY          
SEQRES  21 A  410  ALA ALA ILE ASP VAL PHE PRO THR GLU PRO ALA THR ASN          
SEQRES  22 A  410  SER ASP PRO PHE THR SER PRO LEU ALA GLU PHE ASP ASN          
SEQRES  23 A  410  VAL LEU LEU THR PRO HIS ILE GLY GLY SER THR GLN GLU          
SEQRES  24 A  410  ALA GLN GLU ASN ILE GLY LEU GLU VAL ALA GLY LYS LEU          
SEQRES  25 A  410  ILE LYS TYR SER ASP ASN GLY SER THR LEU SER ALA VAL          
SEQRES  26 A  410  ASN PHE PRO GLU VAL SER LEU PRO LEU HIS VAL GLY ARG          
SEQRES  27 A  410  ARG LEU MET HIS ILE HIS GLU ASN ARG PRO GLY VAL LEU          
SEQRES  28 A  410  THR ALA LEU ASN LYS ILE PHE ALA GLU GLN GLY VAL ASN          
SEQRES  29 A  410  ILE ALA ALA GLN TYR LEU GLN THR SER ALA GLN MET GLY          
SEQRES  30 A  410  TYR VAL VAL ILE ASP ILE GLU ALA ASP GLU ASP VAL ALA          
SEQRES  31 A  410  GLU LYS ALA LEU GLN ALA MET LYS ALA ILE PRO GLY THR          
SEQRES  32 A  410  ILE ARG ALA ARG LEU LEU TYR                                  
HET    SER  A 451       6                                                       
HET    NAI  A 450      44                                                       
HETNAM     SER SERINE                                                           
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETSYN     NAI NADH                                                             
FORMUL   2  SER    C3 H7 N O3                                                   
FORMUL   3  NAI    C21 H29 N7 O14 P2                                            
FORMUL   4  HOH   *18(H2 O)                                                     
HELIX    1   1 GLU A    7  ILE A   11  5                                   5    
HELIX    2   2 HIS A   20  ALA A   30  1                                  11    
HELIX    3   3 ASP A   43  ILE A   51  1                                   9    
HELIX    4   4 THR A   66  ALA A   73  1                                   8    
HELIX    5   5 ASP A   90  ARG A   97  1                                   8    
HELIX    6   6 ASN A  108  ARG A  125  1                                  18    
HELIX    7   7 GLY A  126  ARG A  136  1                                  11    
HELIX    8   8 LEU A  142  SER A  146  5                                   5    
HELIX    9   9 GLY A  160  LEU A  173  1                                  14    
HELIX   10  10 HIS A  196  SER A  204  1                                   9    
HELIX   11  11 GLY A  222  LEU A  228  1                                   7    
HELIX   12  12 ASP A  245  SER A  255  1                                  11    
HELIX   13  13 SER A  279  PHE A  284  5                                   6    
HELIX   14  14 THR A  297  GLY A  319  1                                  23    
HELIX   15  15 GLY A  349  GLU A  360  1                                  12    
HELIX   16  16 ASP A  386  ILE A  400  1                                  15    
SHEET    1   A 5 ILE A  35  PHE A  37  0                                        
SHEET    2   A 5 PHE A  13  LEU A  15  1  N  PHE A  13   O  GLU A  36           
SHEET    3   A 5 PHE A  56  LEU A  59  1  O  PHE A  56   N  LEU A  14           
SHEET    4   A 5 ALA A  78  ALA A  81  1  O  GLY A  80   N  ILE A  57           
SHEET    5   A 5 VAL A 101  PHE A 102  1  O  PHE A 102   N  ALA A  81           
SHEET    1   B 6 TYR A 176  TYR A 180  0                                        
SHEET    2   B 6 LYS A 153  ILE A 157  1  N  ILE A 156   O  TYR A 178           
SHEET    3   B 6 VAL A 206  LEU A 209  1  O  VAL A 206   N  GLY A 155           
SHEET    4   B 6 SER A 233  ASN A 237  1  O  ILE A 236   N  VAL A 207           
SHEET    5   B 6 LEU A 258  ILE A 263  1  O  ALA A 262   N  ASN A 237           
SHEET    6   B 6 VAL A 287  LEU A 289  1  O  LEU A 288   N  ALA A 261           
SHEET    1   C 4 ASN A 364  THR A 372  0                                        
SHEET    2   C 4 MET A 376  GLU A 384 -1  O  TYR A 378   N  GLN A 371           
SHEET    3   C 4 ARG A 338  GLU A 345 -1  N  ARG A 338   O  ILE A 383           
SHEET    4   C 4 THR A 403  ARG A 407 -1  O  ARG A 405   N  ILE A 343           
SITE     1 AC1  9 HIS A 344  ASN A 346  ARG A 347  PRO A 348                    
SITE     2 AC1  9 GLY A 349  LEU A 351  ASN A 364  ILE A 365                    
SITE     3 AC1  9 HOH A 467                                                     
SITE     1 AC2 25 ILE A  84  PHE A 106  ASN A 108  VAL A 112                    
SITE     2 AC2 25 TYR A 159  GLY A 160  HIS A 161  ILE A 162                    
SITE     3 AC2 25 TYR A 180  ASP A 181  ILE A 182  LYS A 185                    
SITE     4 AC2 25 HIS A 210  VAL A 211  PRO A 212  SER A 216                    
SITE     5 AC2 25 THR A 217  MET A 220  ALA A 238  SER A 239                    
SITE     6 AC2 25 ARG A 240  ASP A 264  HIS A 292  GLY A 294                    
SITE     7 AC2 25 GLY A 295                                                     
CRYST1  152.789  152.789  163.660  90.00  90.00 120.00 P 62 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      0.006545  0.003779  0.000000        0.00000                         
SCALE2      0.000000  0.007557  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006110        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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