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Database: PDB
Entry: 4FS9
LinkDB: 4FS9
Original site: 4FS9 
HEADER    ISOMERASE                               27-JUN-12   4FS9              
TITLE     COMPLEX STRUCTURE OF A BROAD SPECIFICITY AMINO ACID RACEMASE (BAR)    
TITLE    2 WITHIN THE REACTIVE INTERMEDIATE                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BROAD SPECIFICITY AMINO ACID RACEMASE;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: BAR;                                                        
COMPND   5 EC: 5.1.1.10;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;                             
SOURCE   3 ORGANISM_TAXID: 303;                                                 
SOURCE   4 STRAIN: DSM84;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    ISOMERASE, PLP BINDING, RACEMIZATION                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.C.WANG,H.M.WU                                                       
REVDAT   1   06-MAR-13 4FS9    0                                                
JRNL        AUTH   H.M.WU,Y.C.KUAN,C.H.CHU,W.H.HSU,W.C.WANG                     
JRNL        TITL   CRYSTAL STRUCTURES OF LYSINE-PREFERRED RACEMASES, THE        
JRNL        TITL 2 NON-ANTIBIOTIC SELECTABLE MARKERS FOR TRANSGENIC PLANTS      
JRNL        REF    PLOS ONE                      V.   7 48301 2012              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   23118975                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0048301                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 20576                          
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1072                            
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1292                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.86                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.3330                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5840                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 95                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.55000                                             
REMARK   3    B22 (A**2) : -7.22000                                             
REMARK   3    B33 (A**2) : 10.42000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -3.91000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.374         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.271         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.631        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5988 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8110 ; 1.376 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   766 ; 7.819 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   264 ;39.156 ;23.864       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1002 ;23.182 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;21.726 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   928 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4492 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  3806 ; 1.018 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6080 ; 1.762 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2182 ; 1.004 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2030 ; 1.647 ; 3.000       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     26       A     409      4                      
REMARK   3           1     B     26       B     409      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2920 ;  0.33 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2920 ;  1.00 ;  2.00           
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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4FS9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073291.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL12B2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : FIXED-EXIT DOUBLE CRYSTAL          
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21656                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
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) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
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: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4DYJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BICINE (PH9.0), 0.1M NACL, 20%      
REMARK 280  PEG-MME 550, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       71.20900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.05450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       71.20900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       59.05450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 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      HOH B 630  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     PHE A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     LEU A    15                                                      
REMARK 465     ILE A    16                                                      
REMARK 465     THR A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     PRO A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     TYR A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     PHE B     3                                                      
REMARK 465     ARG B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     LEU B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     LEU B    15                                                      
REMARK 465     ILE B    16                                                      
REMARK 465     THR B    17                                                      
REMARK 465     GLY B    18                                                      
REMARK 465     GLN B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     PRO B    21                                                      
REMARK 465     LEU B    22                                                      
REMARK 465     TYR B    23                                                      
REMARK 465     ALA B    24                                                      
REMARK 465     ALA B    25                                                      
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    LEU A  53      -72.18    -34.22                                   
REMARK 500    ALA A  65       26.16     83.16                                   
REMARK 500    ALA A  78       47.58     70.19                                   
REMARK 500    PRO A  88      -59.04    -28.86                                   
REMARK 500    GLN A  93       36.59    -80.54                                   
REMARK 500    ALA A 101      -52.07   -126.62                                   
REMARK 500    PHE A 114       92.07    -68.29                                   
REMARK 500    SER A 143      144.87   -173.40                                   
REMARK 500    ASN A 168       28.82    -75.99                                   
REMARK 500    ARG A 174      -74.40   -134.37                                   
REMARK 500    VAL A 200       -2.96   -145.97                                   
REMARK 500    SER A 246      -75.11    -51.08                                   
REMARK 500    VAL A 252       64.32   -111.88                                   
REMARK 500    LEU A 257     -142.01     51.53                                   
REMARK 500    VAL A 271      110.08    -18.81                                   
REMARK 500    ALA A 289      158.66    175.51                                   
REMARK 500    ALA A 295      127.56    -32.66                                   
REMARK 500    ARG A 309     -131.52   -105.04                                   
REMARK 500    TYR A 324       97.79    -62.34                                   
REMARK 500    ASN A 330       26.51     42.52                                   
REMARK 500    SER A 348      174.54    -58.36                                   
REMARK 500    THR A 357       -9.34    -45.78                                   
REMARK 500    ASN A 366     -169.67    -64.12                                   
REMARK 500    ALA A 375       93.67     10.32                                   
REMARK 500    LEU A 391      166.03    -49.73                                   
REMARK 500    LEU B  53      -71.30    -59.16                                   
REMARK 500    LEU B  60      -71.48    -45.22                                   
REMARK 500    GLN B  61      -39.44    -30.26                                   
REMARK 500    ALA B  65       17.99     86.65                                   
REMARK 500    SER B  68      121.27    179.35                                   
REMARK 500    ALA B  78       61.74     63.51                                   
REMARK 500    ASN B 168       49.64    -89.98                                   
REMARK 500    SER B 173       64.61     60.79                                   
REMARK 500    ARG B 174      -57.48   -144.48                                   
REMARK 500    GLU B 209       88.87    -69.67                                   
REMARK 500    LYS B 230      -79.90    -60.32                                   
REMARK 500    LYS B 233       73.96     59.13                                   
REMARK 500    ASN B 245     -160.25    -69.34                                   
REMARK 500    SER B 246      -76.31    -61.81                                   
REMARK 500    LEU B 257     -147.81     39.85                                   
REMARK 500    THR B 270     -154.94   -147.89                                   
REMARK 500    ARG B 303       18.20     48.18                                   
REMARK 500    THR B 304      -25.56    -36.45                                   
REMARK 500    THR B 317       47.62    -77.13                                   
REMARK 500    TYR B 324       90.75    -67.65                                   
REMARK 500    LYS B 331      -38.81   -131.63                                   
REMARK 500    ALA B 375       87.28     -8.20                                   
REMARK 500    GLU B 386      -61.13    -27.99                                   
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 PE1 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE1 B 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DYJ   RELATED DB: PDB                                   
REMARK 900 APO FORM OF BAR                                                      
REMARK 900 RELATED ID: 4DZA   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 A SEQUENCE DATABASE REFERENCE FOR THIS PROTEIN DOES NOT CURRENTLY    
REMARK 999 EXIST.                                                               
DBREF  4FS9 A    1   409  PDB    4FS9     4FS9             1    409             
DBREF  4FS9 B    1   409  PDB    4FS9     4FS9             1    409             
SEQRES   1 A  409  MET PRO PHE ARG ARG THR LEU LEU ALA ALA SER LEU ALA          
SEQRES   2 A  409  LEU LEU ILE THR GLY GLN ALA PRO LEU TYR ALA ALA PRO          
SEQRES   3 A  409  PRO LEU SER MET ASP ASN GLY THR ASN ALA LEU THR VAL          
SEQRES   4 A  409  GLN ASN SER ASN ALA TRP VAL GLU VAL SER ALA SER ALA          
SEQRES   5 A  409  LEU GLN HIS ASN ILE ARG THR LEU GLN ALA GLU LEU ALA          
SEQRES   6 A  409  GLY LYS SER ARG LEU CYS ALA VAL LEU LYS ALA ASP ALA          
SEQRES   7 A  409  TYR GLY HIS GLY ILE GLY LEU VAL MET PRO SER ILE ILE          
SEQRES   8 A  409  ALA GLN GLY VAL PRO CYS VAL ALA VAL ALA SER ASN GLU          
SEQRES   9 A  409  GLU ALA ARG VAL VAL ARG ALA SER GLY PHE THR GLY GLN          
SEQRES  10 A  409  LEU VAL ARG VAL ARG LEU ALA SER LEU SER GLU LEU GLU          
SEQRES  11 A  409  ASP ALA LEU GLN TYR ASP MET GLU GLU LEU VAL GLY SER          
SEQRES  12 A  409  ALA GLU PHE ALA ARG GLN VAL ASP ALA ILE ALA ALA ARG          
SEQRES  13 A  409  HIS GLY LYS THR LEU ARG ILE HIS MET ALA LEU ASN SER          
SEQRES  14 A  409  SER GLY MET SER ARG ASN GLY VAL GLU MET ALA THR TRP          
SEQRES  15 A  409  SER GLY ARG GLY GLU ALA LEU GLN ILE THR ASP GLN LYS          
SEQRES  16 A  409  HIS LEU LYS LEU VAL ALA LEU MET THR HIS PHE ALA VAL          
SEQRES  17 A  409  GLU ASP LYS ASP ASP VAL ARG LYS GLY LEU ALA ALA PHE          
SEQRES  18 A  409  ASN GLU GLN THR ASP TRP LEU ILE LYS HIS ALA LYS LEU          
SEQRES  19 A  409  ASP ARG SER LYS LEU THR LEU HIS ALA ALA ASN SER PHE          
SEQRES  20 A  409  ALA THR LEU GLU VAL PRO GLU ALA ARG LEU ASP MET VAL          
SEQRES  21 A  409  ARG THR GLY GLY ALA LEU PHE GLY ASP THR VAL PRO ALA          
SEQRES  22 A  409  ARG THR GLU TYR GLN ARG ALA MET GLN PHE LYS SER HIS          
SEQRES  23 A  409  VAL ALA ALA VAL HIS SER TYR PRO ALA GLY ASN THR VAL          
SEQRES  24 A  409  GLY TYR ASP ARG THR PHE THR LEU ALA ARG ASP SER ARG          
SEQRES  25 A  409  LEU ALA ASN ILE THR VAL GLY TYR SER ASP GLY TYR ARG          
SEQRES  26 A  409  ARG VAL PHE THR ASN LYS GLY HIS VAL LEU ILE ASN GLY          
SEQRES  27 A  409  HIS ARG ILE PRO VAL VAL GLY LYS VAL SER MET ASN THR          
SEQRES  28 A  409  LEU MET VAL ASP VAL THR ASP PHE PRO ASP VAL LYS GLY          
SEQRES  29 A  409  GLY ASN GLU VAL VAL LEU PHE GLY LYS GLN ALA GLY GLY          
SEQRES  30 A  409  GLU ILE THR GLN ALA GLU MET GLU GLU ILE ASN GLY ALA          
SEQRES  31 A  409  LEU LEU ALA ASP LEU TYR THR VAL TRP GLY SER SER ASN          
SEQRES  32 A  409  PRO LYS ILE LEU VAL ASP                                      
SEQRES   1 B  409  MET PRO PHE ARG ARG THR LEU LEU ALA ALA SER LEU ALA          
SEQRES   2 B  409  LEU LEU ILE THR GLY GLN ALA PRO LEU TYR ALA ALA PRO          
SEQRES   3 B  409  PRO LEU SER MET ASP ASN GLY THR ASN ALA LEU THR VAL          
SEQRES   4 B  409  GLN ASN SER ASN ALA TRP VAL GLU VAL SER ALA SER ALA          
SEQRES   5 B  409  LEU GLN HIS ASN ILE ARG THR LEU GLN ALA GLU LEU ALA          
SEQRES   6 B  409  GLY LYS SER ARG LEU CYS ALA VAL LEU LYS ALA ASP ALA          
SEQRES   7 B  409  TYR GLY HIS GLY ILE GLY LEU VAL MET PRO SER ILE ILE          
SEQRES   8 B  409  ALA GLN GLY VAL PRO CYS VAL ALA VAL ALA SER ASN GLU          
SEQRES   9 B  409  GLU ALA ARG VAL VAL ARG ALA SER GLY PHE THR GLY GLN          
SEQRES  10 B  409  LEU VAL ARG VAL ARG LEU ALA SER LEU SER GLU LEU GLU          
SEQRES  11 B  409  ASP ALA LEU GLN TYR ASP MET GLU GLU LEU VAL GLY SER          
SEQRES  12 B  409  ALA GLU PHE ALA ARG GLN VAL ASP ALA ILE ALA ALA ARG          
SEQRES  13 B  409  HIS GLY LYS THR LEU ARG ILE HIS MET ALA LEU ASN SER          
SEQRES  14 B  409  SER GLY MET SER ARG ASN GLY VAL GLU MET ALA THR TRP          
SEQRES  15 B  409  SER GLY ARG GLY GLU ALA LEU GLN ILE THR ASP GLN LYS          
SEQRES  16 B  409  HIS LEU LYS LEU VAL ALA LEU MET THR HIS PHE ALA VAL          
SEQRES  17 B  409  GLU ASP LYS ASP ASP VAL ARG LYS GLY LEU ALA ALA PHE          
SEQRES  18 B  409  ASN GLU GLN THR ASP TRP LEU ILE LYS HIS ALA LYS LEU          
SEQRES  19 B  409  ASP ARG SER LYS LEU THR LEU HIS ALA ALA ASN SER PHE          
SEQRES  20 B  409  ALA THR LEU GLU VAL PRO GLU ALA ARG LEU ASP MET VAL          
SEQRES  21 B  409  ARG THR GLY GLY ALA LEU PHE GLY ASP THR VAL PRO ALA          
SEQRES  22 B  409  ARG THR GLU TYR GLN ARG ALA MET GLN PHE LYS SER HIS          
SEQRES  23 B  409  VAL ALA ALA VAL HIS SER TYR PRO ALA GLY ASN THR VAL          
SEQRES  24 B  409  GLY TYR ASP ARG THR PHE THR LEU ALA ARG ASP SER ARG          
SEQRES  25 B  409  LEU ALA ASN ILE THR VAL GLY TYR SER ASP GLY TYR ARG          
SEQRES  26 B  409  ARG VAL PHE THR ASN LYS GLY HIS VAL LEU ILE ASN GLY          
SEQRES  27 B  409  HIS ARG ILE PRO VAL VAL GLY LYS VAL SER MET ASN THR          
SEQRES  28 B  409  LEU MET VAL ASP VAL THR ASP PHE PRO ASP VAL LYS GLY          
SEQRES  29 B  409  GLY ASN GLU VAL VAL LEU PHE GLY LYS GLN ALA GLY GLY          
SEQRES  30 B  409  GLU ILE THR GLN ALA GLU MET GLU GLU ILE ASN GLY ALA          
SEQRES  31 B  409  LEU LEU ALA ASP LEU TYR THR VAL TRP GLY SER SER ASN          
SEQRES  32 B  409  PRO LYS ILE LEU VAL ASP                                      
HET    PE1  A 501      25                                                       
HET    PE1  B 501      25                                                       
HETNAM     PE1 N~2~-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)                      
HETNAM   2 PE1  METHYL]PYRIDIN-4-YL}METHYL)-L-LYSINE                            
HETSYN     PE1 PYRIDOXYL-GLUTAMIC ACID-5'-MONOPHOSPHATE                         
FORMUL   3  PE1    2(C14 H24 N3 O7 P)                                           
FORMUL   5  HOH   *95(H2 O)                                                     
HELIX    1   1 ALA A   50  ALA A   65  1                                  16    
HELIX    2   2 LEU A   74  HIS A   81  1                                   8    
HELIX    3   3 GLY A   82  GLN A   93  1                                  12    
HELIX    4   4 SER A  102  ALA A  111  1                                  10    
HELIX    5   5 SER A  125  LEU A  133  1                                   9    
HELIX    6   6 GLN A  134  ASP A  136  5                                   3    
HELIX    7   7 SER A  143  GLY A  158  1                                  16    
HELIX    8   8 THR A  181  GLN A  194  1                                  14    
HELIX    9   9 ASP A  210  ALA A  232  1                                  23    
HELIX   10  10 ASP A  235  LEU A  239  5                                   5    
HELIX   11  11 ASN A  245  VAL A  252  1                                   8    
HELIX   12  12 PRO A  253  LEU A  257  5                                   5    
HELIX   13  13 GLY A  263  GLY A  268  1                                   6    
HELIX   14  14 GLY A  300  THR A  304  5                                   5    
HELIX   15  15 ARG A  325  THR A  329  5                                   5    
HELIX   16  16 THR A  380  GLY A  389  1                                  10    
HELIX   17  17 LEU A  392  ASN A  403  1                                  12    
HELIX   18  18 ALA B   50  ALA B   65  1                                  16    
HELIX   19  19 LEU B   74  HIS B   81  1                                   8    
HELIX   20  20 GLY B   82  GLN B   93  1                                  12    
HELIX   21  21 SER B  102  SER B  112  1                                  11    
HELIX   22  22 SER B  125  ALA B  132  1                                   8    
HELIX   23  23 LEU B  133  ASP B  136  5                                   4    
HELIX   24  24 SER B  143  GLY B  158  1                                  16    
HELIX   25  25 THR B  181  ASP B  193  1                                  13    
HELIX   26  26 ASP B  210  ALA B  232  1                                  23    
HELIX   27  27 ASN B  245  VAL B  252  1                                   8    
HELIX   28  28 PRO B  253  LEU B  257  5                                   5    
HELIX   29  29 GLY B  263  GLY B  268  1                                   6    
HELIX   30  30 GLY B  300  THR B  304  5                                   5    
HELIX   31  31 GLY B  319  GLY B  323  5                                   5    
HELIX   32  32 ARG B  325  THR B  329  5                                   5    
HELIX   33  33 THR B  380  GLY B  389  1                                  10    
HELIX   34  34 LEU B  392  ASN B  403  1                                  12    
SHEET    1   A 2 SER A  29  MET A  30  0                                        
SHEET    2   A 2 MET B  30  ASP B  31 -1  O  MET B  30   N  MET A  30           
SHEET    1   B 5 HIS A 339  PRO A 342  0                                        
SHEET    2   B 5 HIS A 333  ILE A 336 -1  N  ILE A 336   O  HIS A 339           
SHEET    3   B 5 GLU A 367  GLN A 374 -1  O  VAL A 369   N  LEU A 335           
SHEET    4   B 5 MET A 281  TYR A 293 -1  N  PHE A 283   O  PHE A 371           
SHEET    5   B 5 GLY A 377  ILE A 379  0                                        
SHEET    1   C 6 LEU A 352  ASP A 355  0                                        
SHEET    2   C 6 SER A 311  ILE A 316 -1  N  ALA A 314   O  VAL A 354           
SHEET    3   C 6 MET A 281  TYR A 293 -1  N  ALA A 288   O  ASN A 315           
SHEET    4   C 6 GLU A 367  GLN A 374 -1  O  PHE A 371   N  PHE A 283           
SHEET    5   C 6 ALA A  44  SER A  49  0                                        
SHEET    6   C 6 LYS A 405  VAL A 408  1  O  ILE A 406   N  VAL A  46           
SHEET    1   D 4 GLN A 117  ARG A 120  0                                        
SHEET    2   D 4 CYS A  97  VAL A 100  1  N  VAL A 100   O  VAL A 119           
SHEET    3   D 4 ARG A  69  VAL A  73  1  N  ALA A  72   O  CYS A  97           
SHEET    4   D 4 MET A 259  THR A 262  1  O  VAL A 260   N  CYS A  71           
SHEET    1   E 4 GLU A 139  VAL A 141  0                                        
SHEET    2   E 4 LEU A 161  ALA A 166  1  O  HIS A 164   N  VAL A 141           
SHEET    3   E 4 LEU A 197  MET A 203  1  O  ALA A 201   N  MET A 165           
SHEET    4   E 4 THR A 240  LEU A 241  1  O  THR A 240   N  VAL A 200           
SHEET    1   F 2 THR A 298  VAL A 299  0                                        
SHEET    2   F 2 PHE A 305  THR A 306 -1  O  PHE A 305   N  VAL A 299           
SHEET    1   G 5 HIS B 339  PRO B 342  0                                        
SHEET    2   G 5 HIS B 333  ILE B 336 -1  N  VAL B 334   O  ILE B 341           
SHEET    3   G 5 GLU B 367  GLN B 374 -1  O  VAL B 369   N  LEU B 335           
SHEET    4   G 5 MET B 281  TYR B 293 -1  N  PHE B 283   O  PHE B 371           
SHEET    5   G 5 GLY B 377  ILE B 379  0                                        
SHEET    1   H 6 LEU B 352  ASP B 355  0                                        
SHEET    2   H 6 SER B 311  ILE B 316 -1  N  ILE B 316   O  LEU B 352           
SHEET    3   H 6 MET B 281  TYR B 293 -1  N  ALA B 288   O  ASN B 315           
SHEET    4   H 6 GLU B 367  GLN B 374 -1  O  PHE B 371   N  PHE B 283           
SHEET    5   H 6 ALA B  44  SER B  49  0                                        
SHEET    6   H 6 LYS B 405  VAL B 408  1  O  ILE B 406   N  VAL B  46           
SHEET    1   I 4 GLN B 117  ARG B 120  0                                        
SHEET    2   I 4 CYS B  97  VAL B 100  1  N  VAL B  98   O  GLN B 117           
SHEET    3   I 4 ARG B  69  VAL B  73  1  N  ALA B  72   O  ALA B  99           
SHEET    4   I 4 MET B 259  THR B 262  1  O  THR B 262   N  VAL B  73           
SHEET    1   J 4 GLU B 139  VAL B 141  0                                        
SHEET    2   J 4 LEU B 161  ALA B 166  1  O  ALA B 166   N  VAL B 141           
SHEET    3   J 4 LEU B 197  MET B 203  1  O  LYS B 198   N  ILE B 163           
SHEET    4   J 4 THR B 240  HIS B 242  1  O  HIS B 242   N  LEU B 202           
SHEET    1   K 2 THR B 298  VAL B 299  0                                        
SHEET    2   K 2 PHE B 305  THR B 306 -1  O  PHE B 305   N  VAL B 299           
SSBOND   1 CYS A   71    CYS A   97                          1555   1555  2.06  
SSBOND   2 CYS B   71    CYS B   97                          1555   1555  2.04  
SITE     1 AC1 16 LYS A  75  TYR A  79  VAL A 121  ARG A 174                    
SITE     2 AC1 16 HIS A 205  ASN A 245  SER A 246  ARG A 261                    
SITE     3 AC1 16 GLY A 263  GLY A 264  HOH A 627  HOH A 639                    
SITE     4 AC1 16 TYR B 301  TYR B 320  SER B 348  MET B 349                    
SITE     1 AC2 15 TYR A 301  TYR A 320  SER A 348  MET A 349                    
SITE     2 AC2 15 HOH A 624  LYS B  75  TYR B  79  ARG B 174                    
SITE     3 AC2 15 HIS B 205  ASN B 245  SER B 246  ARG B 261                    
SITE     4 AC2 15 THR B 262  GLY B 263  GLY B 264                               
CRYST1  142.418  118.109   74.024  90.00  99.87  90.00 C 1 2 1       8          
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      0.007022  0.000000  0.001221        0.00000                         
SCALE2      0.000000  0.008467  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013712        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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