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Database: PDB
Entry: 5FAG
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HEADER    ISOMERASE                               11-DEC-15   5FAG              
TITLE     ALANINE RACEMASE FROM STREPTOMYCES COELICOLOR A3(2) WITH BOUND        
TITLE    2 PROPIONATE INHIBITOR                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE;                                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR A3(2);                  
SOURCE   3 ORGANISM_TAXID: 100226;                                              
SOURCE   4 GENE: ALR, SCO4745, SC6G4.23;                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET-15B                                    
KEYWDS    ISOMERASE, PLP, ALANINE RACEMASE, PROPIONATE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.TASSONI,N.S.PANNU                                                   
REVDAT   3   01-FEB-17 5FAG    1       JRNL                                     
REVDAT   2   25-JAN-17 5FAG    1       JRNL                                     
REVDAT   1   21-DEC-16 5FAG    0                                                
JRNL        AUTH   R.TASSONI,L.T.VAN DER AART,M.UBBINK,G.P.VAN WEZEL,N.S.PANNU  
JRNL        TITL   STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF THE ALANINE    
JRNL        TITL 2 RACEMASE FROM STREPTOMYCES COELICOLOR A3(2).                 
JRNL        REF    BIOCHEM. BIOPHYS. RES.        V. 483   122 2017              
JRNL        REF  2 COMMUN.                                                      
JRNL        REFN                   ESSN 1090-2104                               
JRNL        PMID   28042035                                                     
JRNL        DOI    10.1016/J.BBRC.2016.12.183                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.51 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
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) : 1.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.06                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 212779                         
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 11051                           
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) : 1.51                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.55                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 14019                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 697                          
REMARK   3   BIN FREE R VALUE                    : 0.4300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11384                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 113                                     
REMARK   3   SOLVENT ATOMS            : 804                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.51000                                             
REMARK   3    B22 (A**2) : 2.34000                                              
REMARK   3    B33 (A**2) : -0.50000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.64000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.086         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.086         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.783         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12235 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 11706 ; 0.011 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16775 ; 1.978 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 26845 ; 1.755 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1659 ; 5.902 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   521 ;32.453 ;21.440       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1795 ;13.811 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   159 ;18.180 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1838 ; 0.121 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14200 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2827 ; 0.008 ; 0.020       
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):  6271 ; 3.134 ; 3.026       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  6270 ; 3.134 ; 3.026       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7865 ; 4.022 ; 4.532       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  7866 ; 4.022 ; 4.532       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5964 ; 3.778 ; 3.405       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  5959 ; 3.777 ; 3.404       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  8842 ; 5.413 ; 4.964       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 14362 ; 6.600 ;25.065       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 14363 ; 6.602 ;25.067       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A    10    390       B    10    390   46356  0.08  0.05     
REMARK   3    2     A    10    390       C    10    390   46214  0.08  0.05     
REMARK   3    3     A    10    390       D    10    390   45990  0.07  0.05     
REMARK   3    4     B    10    391       C    10    391   46124  0.07  0.05     
REMARK   3    5     B    10    391       D    10    391   45726  0.07  0.05     
REMARK   3    6     C    10    391       D    10    391   45988  0.07  0.05     
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5FAG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000216276.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.968622                           
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 224162                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.510                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.060                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.01600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 5FAC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PROPANE PH 8.5, 0.2 M     
REMARK 280  NANO3, 20% (W/V) PEG3350, VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 293.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       44.29000            
REMARK 290   SMTRY3   2  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: 8720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 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   -18                                                      
REMARK 465     GLY A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     MET B   -18                                                      
REMARK 465     GLY B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     ARG B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     ASP B     9                                                      
REMARK 465     MET C   -18                                                      
REMARK 465     GLY C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     THR C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     ARG C     7                                                      
REMARK 465     ARG C     8                                                      
REMARK 465     ASP C     9                                                      
REMARK 465     MET D   -18                                                      
REMARK 465     GLY D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     ALA D     6                                                      
REMARK 465     ARG D     7                                                      
REMARK 465     ARG D     8                                                      
REMARK 465     ASP D     9                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   C    GLU B   391     O    HOH B   605              1.51            
REMARK 500   O1   PPI C   402     O    HOH C   501              1.60            
REMARK 500   NH1  ARG B    92     O    HOH B   601              1.88            
REMARK 500   O    HOH C   580     O    HOH C   584              1.98            
REMARK 500   NH1  ARG C    17     OE1  GLU C   348              2.04            
REMARK 500   OD1  ASP B   156     NH1  ARG B   159              2.12            
REMARK 500   O    ALA A    12     O    HOH A   501              2.14            
REMARK 500   O    HOH D   639     O    HOH D   650              2.15            
REMARK 500   NH2  ARG D    30     O    HOH D   601              2.15            
REMARK 500   CZ   ARG B    92     O    HOH B   601              2.18            
REMARK 500   O    HOH A   712     O    HOH A   721              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A   8   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A 111   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 111   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 201   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 217   CG  -  CD  -  NE  ANGL. DEV. =  22.7 DEGREES          
REMARK 500    ARG A 217   CD  -  NE  -  CZ  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG A 217   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG A 217   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ARG A 328   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 328   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 342   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG B  17   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    ARG B  17   NE  -  CZ  -  NH2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ARG B  26   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG B  35   CG  -  CD  -  NE  ANGL. DEV. = -12.7 DEGREES          
REMARK 500    ARG B 210   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG B 210   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B 213   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG B 213   NE  -  CZ  -  NH2 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG B 328   CG  -  CD  -  NE  ANGL. DEV. =  13.0 DEGREES          
REMARK 500    ARG B 328   CD  -  NE  -  CZ  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG B 328   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG B 328   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG B 328   NE  -  CZ  -  NH2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG B 383   NE  -  CZ  -  NH2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG C  17   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP C 143   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG C 210   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG C 213   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG C 213   NE  -  CZ  -  NH2 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG C 308   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG D  17   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    LYS D  46   CD  -  CE  -  NZ  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    ARG D 201   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 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    ALA A  72      -72.53    -80.34                                   
REMARK 500    ARG A 148     -106.58   -113.57                                   
REMARK 500    PHE A 233     -131.95     41.13                                   
REMARK 500    SER A 282      178.69     65.95                                   
REMARK 500    SER A 312        9.52     58.02                                   
REMARK 500    SER A 313      -24.32   -142.83                                   
REMARK 500    ARG B 148     -103.79   -111.19                                   
REMARK 500    PHE B 233     -131.27     46.29                                   
REMARK 500    SER B 282     -179.38     65.66                                   
REMARK 500    SER B 313      -19.52   -142.18                                   
REMARK 500    ALA C  72      -70.03    -82.60                                   
REMARK 500    ARG C 148     -102.68   -113.77                                   
REMARK 500    ILE C 219      -10.27   -146.47                                   
REMARK 500    PHE C 233     -132.84     46.77                                   
REMARK 500    SER C 282     -178.31     62.58                                   
REMARK 500    PRO C 299       44.71    -77.80                                   
REMARK 500    SER C 313      -22.19   -142.86                                   
REMARK 500    ARG D 148     -104.01   -111.83                                   
REMARK 500    ILE D 219       -6.24   -145.07                                   
REMARK 500    PHE D 233     -135.66     49.60                                   
REMARK 500    SER D 282      179.44     69.68                                   
REMARK 500    PRO D 299       49.35    -87.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 403  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET A  42   O                                                      
REMARK 620 2 PRO A 238   O   128.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 404  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 180   OG                                                     
REMARK 620 2 HOH A 698   O   122.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 504  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 180   OG                                                     
REMARK 620 2 HIS B 181   O    75.7                                              
REMARK 620 3 HOH B 606   O   119.7 116.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 503  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA B 326   O                                                      
REMARK 620 2 ARG B 328   O   109.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 403  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA C 231   O                                                      
REMARK 620 2 HIS C 232   O    81.8                                              
REMARK 620 3 LEU C 235   O   145.1  66.7                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PPI A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PPI B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PPI B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PPI B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PPI B 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 B 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PPI C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PPI D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PPI D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PLP B 502 and LYS B    
REMARK 800  46                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PLP C 401 and LYS C    
REMARK 800  46                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PLP D 502 and LYS D    
REMARK 800  46                                                                  
DBREF  5FAG A    1   391  UNP    O86786   ALR_STRCO        1    391             
DBREF  5FAG B    1   391  UNP    O86786   ALR_STRCO        1    391             
DBREF  5FAG C    1   391  UNP    O86786   ALR_STRCO        1    391             
DBREF  5FAG D    1   391  UNP    O86786   ALR_STRCO        1    391             
SEQADV 5FAG MET A  -18  UNP  O86786              INITIATING METHIONINE          
SEQADV 5FAG GLY A  -17  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER A  -16  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS A  -15  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS A  -14  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS A  -13  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS A  -12  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS A  -11  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS A  -10  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER A   -9  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER A   -8  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG GLY A   -7  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG LEU A   -6  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG VAL A   -5  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG PRO A   -4  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG ARG A   -3  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG GLY A   -2  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER A   -1  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS A    0  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG MET B  -18  UNP  O86786              INITIATING METHIONINE          
SEQADV 5FAG GLY B  -17  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER B  -16  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS B  -15  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS B  -14  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS B  -13  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS B  -12  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS B  -11  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS B  -10  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER B   -9  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER B   -8  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG GLY B   -7  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG LEU B   -6  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG VAL B   -5  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG PRO B   -4  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG ARG B   -3  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG GLY B   -2  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER B   -1  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS B    0  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG MET C  -18  UNP  O86786              INITIATING METHIONINE          
SEQADV 5FAG GLY C  -17  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER C  -16  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS C  -15  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS C  -14  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS C  -13  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS C  -12  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS C  -11  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS C  -10  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER C   -9  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER C   -8  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG GLY C   -7  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG LEU C   -6  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG VAL C   -5  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG PRO C   -4  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG ARG C   -3  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG GLY C   -2  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER C   -1  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS C    0  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG MET D  -18  UNP  O86786              INITIATING METHIONINE          
SEQADV 5FAG GLY D  -17  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER D  -16  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS D  -15  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS D  -14  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS D  -13  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS D  -12  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS D  -11  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS D  -10  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER D   -9  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER D   -8  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG GLY D   -7  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG LEU D   -6  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG VAL D   -5  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG PRO D   -4  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG ARG D   -3  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG GLY D   -2  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG SER D   -1  UNP  O86786              EXPRESSION TAG                 
SEQADV 5FAG HIS D    0  UNP  O86786              EXPRESSION TAG                 
SEQRES   1 A  410  MET GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 A  410  VAL PRO ARG GLY SER HIS MET SER GLU THR THR ALA ARG          
SEQRES   3 A  410  ARG ASP ALA ASP ALA VAL LEU ARG ALA ARG ALA GLU ILE          
SEQRES   4 A  410  ASP LEU ALA ALA LEU ARG ALA ASN VAL ARG ALA LEU ARG          
SEQRES   5 A  410  GLU ARG ALA PRO GLY ALA ALA LEU MET ALA VAL VAL LYS          
SEQRES   6 A  410  ALA ASP ALA TYR GLY HIS GLY ALA ILE PRO CYS ALA ARG          
SEQRES   7 A  410  ALA ALA VAL ALA ALA GLY ALA THR TRP LEU GLY THR ALA          
SEQRES   8 A  410  THR PRO GLN GLU ALA LEU ALA LEU ARG ALA ALA GLU PRO          
SEQRES   9 A  410  GLY LEU PRO ASP ASP VAL ARG ILE MET CYS TRP LEU TRP          
SEQRES  10 A  410  THR PRO GLY GLY PRO TRP ARG GLU ALA VAL GLU ALA ARG          
SEQRES  11 A  410  LEU ASP VAL SER VAL SER ALA MET TRP ALA MET GLU GLU          
SEQRES  12 A  410  VAL THR GLY ALA ALA ARG ALA ALA GLY VAL PRO ALA ARG          
SEQRES  13 A  410  VAL GLN LEU KCX ALA ASP THR GLY LEU GLY ARG GLY GLY          
SEQRES  14 A  410  CYS GLN PRO GLY ALA ASP TRP GLU ARG LEU VAL GLY ALA          
SEQRES  15 A  410  ALA LEU ARG ALA GLU GLU GLU GLY LEU LEU ARG VAL THR          
SEQRES  16 A  410  GLY LEU TRP SER HIS PHE ALA CYS ALA ASP GLU PRO GLY          
SEQRES  17 A  410  HIS PRO SER ILE ALA ALA GLN LEU THR ARG PHE ARG GLU          
SEQRES  18 A  410  MET THR ALA TYR ALA GLU GLN ARG GLY LEU ARG PRO GLU          
SEQRES  19 A  410  VAL ARG HIS ILE ALA ASN SER PRO ALA THR LEU THR LEU          
SEQRES  20 A  410  PRO ASP ALA HIS PHE ASP LEU VAL ARG PRO GLY ILE ALA          
SEQRES  21 A  410  MET TYR GLY VAL SER PRO SER PRO GLU ILE GLY THR PRO          
SEQRES  22 A  410  ALA ASP PHE GLY LEU ARG PRO VAL MET THR LEU ALA ALA          
SEQRES  23 A  410  SER LEU ALA LEU VAL LYS GLN VAL PRO GLY GLY HIS GLY          
SEQRES  24 A  410  VAL SER TYR GLY HIS HIS TYR THR THR PRO GLY GLU THR          
SEQRES  25 A  410  THR LEU GLY LEU VAL PRO LEU GLY TYR ALA ASP GLY ILE          
SEQRES  26 A  410  PRO ARG HIS ALA SER SER SER GLY PRO VAL LEU VAL ASP          
SEQRES  27 A  410  GLY LYS TRP ARG THR VAL ALA GLY ARG ILE ALA MET ASP          
SEQRES  28 A  410  GLN PHE VAL VAL ASP LEU GLY GLY ASP ARG PRO GLU PRO          
SEQRES  29 A  410  GLY ALA GLU ALA VAL LEU PHE GLY PRO GLY ASP ARG GLY          
SEQRES  30 A  410  GLU PRO THR ALA GLU ASP TRP ALA GLN ALA ALA GLY THR          
SEQRES  31 A  410  ILE ALA TYR GLU ILE VAL THR ARG ILE GLY SER ARG VAL          
SEQRES  32 A  410  PRO ARG VAL TYR VAL ASN GLU                                  
SEQRES   1 B  410  MET GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 B  410  VAL PRO ARG GLY SER HIS MET SER GLU THR THR ALA ARG          
SEQRES   3 B  410  ARG ASP ALA ASP ALA VAL LEU ARG ALA ARG ALA GLU ILE          
SEQRES   4 B  410  ASP LEU ALA ALA LEU ARG ALA ASN VAL ARG ALA LEU ARG          
SEQRES   5 B  410  GLU ARG ALA PRO GLY ALA ALA LEU MET ALA VAL VAL LYS          
SEQRES   6 B  410  ALA ASP ALA TYR GLY HIS GLY ALA ILE PRO CYS ALA ARG          
SEQRES   7 B  410  ALA ALA VAL ALA ALA GLY ALA THR TRP LEU GLY THR ALA          
SEQRES   8 B  410  THR PRO GLN GLU ALA LEU ALA LEU ARG ALA ALA GLU PRO          
SEQRES   9 B  410  GLY LEU PRO ASP ASP VAL ARG ILE MET CYS TRP LEU TRP          
SEQRES  10 B  410  THR PRO GLY GLY PRO TRP ARG GLU ALA VAL GLU ALA ARG          
SEQRES  11 B  410  LEU ASP VAL SER VAL SER ALA MET TRP ALA MET GLU GLU          
SEQRES  12 B  410  VAL THR GLY ALA ALA ARG ALA ALA GLY VAL PRO ALA ARG          
SEQRES  13 B  410  VAL GLN LEU KCX ALA ASP THR GLY LEU GLY ARG GLY GLY          
SEQRES  14 B  410  CYS GLN PRO GLY ALA ASP TRP GLU ARG LEU VAL GLY ALA          
SEQRES  15 B  410  ALA LEU ARG ALA GLU GLU GLU GLY LEU LEU ARG VAL THR          
SEQRES  16 B  410  GLY LEU TRP SER HIS PHE ALA CYS ALA ASP GLU PRO GLY          
SEQRES  17 B  410  HIS PRO SER ILE ALA ALA GLN LEU THR ARG PHE ARG GLU          
SEQRES  18 B  410  MET THR ALA TYR ALA GLU GLN ARG GLY LEU ARG PRO GLU          
SEQRES  19 B  410  VAL ARG HIS ILE ALA ASN SER PRO ALA THR LEU THR LEU          
SEQRES  20 B  410  PRO ASP ALA HIS PHE ASP LEU VAL ARG PRO GLY ILE ALA          
SEQRES  21 B  410  MET TYR GLY VAL SER PRO SER PRO GLU ILE GLY THR PRO          
SEQRES  22 B  410  ALA ASP PHE GLY LEU ARG PRO VAL MET THR LEU ALA ALA          
SEQRES  23 B  410  SER LEU ALA LEU VAL LYS GLN VAL PRO GLY GLY HIS GLY          
SEQRES  24 B  410  VAL SER TYR GLY HIS HIS TYR THR THR PRO GLY GLU THR          
SEQRES  25 B  410  THR LEU GLY LEU VAL PRO LEU GLY TYR ALA ASP GLY ILE          
SEQRES  26 B  410  PRO ARG HIS ALA SER SER SER GLY PRO VAL LEU VAL ASP          
SEQRES  27 B  410  GLY LYS TRP ARG THR VAL ALA GLY ARG ILE ALA MET ASP          
SEQRES  28 B  410  GLN PHE VAL VAL ASP LEU GLY GLY ASP ARG PRO GLU PRO          
SEQRES  29 B  410  GLY ALA GLU ALA VAL LEU PHE GLY PRO GLY ASP ARG GLY          
SEQRES  30 B  410  GLU PRO THR ALA GLU ASP TRP ALA GLN ALA ALA GLY THR          
SEQRES  31 B  410  ILE ALA TYR GLU ILE VAL THR ARG ILE GLY SER ARG VAL          
SEQRES  32 B  410  PRO ARG VAL TYR VAL ASN GLU                                  
SEQRES   1 C  410  MET GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 C  410  VAL PRO ARG GLY SER HIS MET SER GLU THR THR ALA ARG          
SEQRES   3 C  410  ARG ASP ALA ASP ALA VAL LEU ARG ALA ARG ALA GLU ILE          
SEQRES   4 C  410  ASP LEU ALA ALA LEU ARG ALA ASN VAL ARG ALA LEU ARG          
SEQRES   5 C  410  GLU ARG ALA PRO GLY ALA ALA LEU MET ALA VAL VAL LYS          
SEQRES   6 C  410  ALA ASP ALA TYR GLY HIS GLY ALA ILE PRO CYS ALA ARG          
SEQRES   7 C  410  ALA ALA VAL ALA ALA GLY ALA THR TRP LEU GLY THR ALA          
SEQRES   8 C  410  THR PRO GLN GLU ALA LEU ALA LEU ARG ALA ALA GLU PRO          
SEQRES   9 C  410  GLY LEU PRO ASP ASP VAL ARG ILE MET CYS TRP LEU TRP          
SEQRES  10 C  410  THR PRO GLY GLY PRO TRP ARG GLU ALA VAL GLU ALA ARG          
SEQRES  11 C  410  LEU ASP VAL SER VAL SER ALA MET TRP ALA MET GLU GLU          
SEQRES  12 C  410  VAL THR GLY ALA ALA ARG ALA ALA GLY VAL PRO ALA ARG          
SEQRES  13 C  410  VAL GLN LEU KCX ALA ASP THR GLY LEU GLY ARG GLY GLY          
SEQRES  14 C  410  CYS GLN PRO GLY ALA ASP TRP GLU ARG LEU VAL GLY ALA          
SEQRES  15 C  410  ALA LEU ARG ALA GLU GLU GLU GLY LEU LEU ARG VAL THR          
SEQRES  16 C  410  GLY LEU TRP SER HIS PHE ALA CYS ALA ASP GLU PRO GLY          
SEQRES  17 C  410  HIS PRO SER ILE ALA ALA GLN LEU THR ARG PHE ARG GLU          
SEQRES  18 C  410  MET THR ALA TYR ALA GLU GLN ARG GLY LEU ARG PRO GLU          
SEQRES  19 C  410  VAL ARG HIS ILE ALA ASN SER PRO ALA THR LEU THR LEU          
SEQRES  20 C  410  PRO ASP ALA HIS PHE ASP LEU VAL ARG PRO GLY ILE ALA          
SEQRES  21 C  410  MET TYR GLY VAL SER PRO SER PRO GLU ILE GLY THR PRO          
SEQRES  22 C  410  ALA ASP PHE GLY LEU ARG PRO VAL MET THR LEU ALA ALA          
SEQRES  23 C  410  SER LEU ALA LEU VAL LYS GLN VAL PRO GLY GLY HIS GLY          
SEQRES  24 C  410  VAL SER TYR GLY HIS HIS TYR THR THR PRO GLY GLU THR          
SEQRES  25 C  410  THR LEU GLY LEU VAL PRO LEU GLY TYR ALA ASP GLY ILE          
SEQRES  26 C  410  PRO ARG HIS ALA SER SER SER GLY PRO VAL LEU VAL ASP          
SEQRES  27 C  410  GLY LYS TRP ARG THR VAL ALA GLY ARG ILE ALA MET ASP          
SEQRES  28 C  410  GLN PHE VAL VAL ASP LEU GLY GLY ASP ARG PRO GLU PRO          
SEQRES  29 C  410  GLY ALA GLU ALA VAL LEU PHE GLY PRO GLY ASP ARG GLY          
SEQRES  30 C  410  GLU PRO THR ALA GLU ASP TRP ALA GLN ALA ALA GLY THR          
SEQRES  31 C  410  ILE ALA TYR GLU ILE VAL THR ARG ILE GLY SER ARG VAL          
SEQRES  32 C  410  PRO ARG VAL TYR VAL ASN GLU                                  
SEQRES   1 D  410  MET GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 D  410  VAL PRO ARG GLY SER HIS MET SER GLU THR THR ALA ARG          
SEQRES   3 D  410  ARG ASP ALA ASP ALA VAL LEU ARG ALA ARG ALA GLU ILE          
SEQRES   4 D  410  ASP LEU ALA ALA LEU ARG ALA ASN VAL ARG ALA LEU ARG          
SEQRES   5 D  410  GLU ARG ALA PRO GLY ALA ALA LEU MET ALA VAL VAL LYS          
SEQRES   6 D  410  ALA ASP ALA TYR GLY HIS GLY ALA ILE PRO CYS ALA ARG          
SEQRES   7 D  410  ALA ALA VAL ALA ALA GLY ALA THR TRP LEU GLY THR ALA          
SEQRES   8 D  410  THR PRO GLN GLU ALA LEU ALA LEU ARG ALA ALA GLU PRO          
SEQRES   9 D  410  GLY LEU PRO ASP ASP VAL ARG ILE MET CYS TRP LEU TRP          
SEQRES  10 D  410  THR PRO GLY GLY PRO TRP ARG GLU ALA VAL GLU ALA ARG          
SEQRES  11 D  410  LEU ASP VAL SER VAL SER ALA MET TRP ALA MET GLU GLU          
SEQRES  12 D  410  VAL THR GLY ALA ALA ARG ALA ALA GLY VAL PRO ALA ARG          
SEQRES  13 D  410  VAL GLN LEU KCX ALA ASP THR GLY LEU GLY ARG GLY GLY          
SEQRES  14 D  410  CYS GLN PRO GLY ALA ASP TRP GLU ARG LEU VAL GLY ALA          
SEQRES  15 D  410  ALA LEU ARG ALA GLU GLU GLU GLY LEU LEU ARG VAL THR          
SEQRES  16 D  410  GLY LEU TRP SER HIS PHE ALA CYS ALA ASP GLU PRO GLY          
SEQRES  17 D  410  HIS PRO SER ILE ALA ALA GLN LEU THR ARG PHE ARG GLU          
SEQRES  18 D  410  MET THR ALA TYR ALA GLU GLN ARG GLY LEU ARG PRO GLU          
SEQRES  19 D  410  VAL ARG HIS ILE ALA ASN SER PRO ALA THR LEU THR LEU          
SEQRES  20 D  410  PRO ASP ALA HIS PHE ASP LEU VAL ARG PRO GLY ILE ALA          
SEQRES  21 D  410  MET TYR GLY VAL SER PRO SER PRO GLU ILE GLY THR PRO          
SEQRES  22 D  410  ALA ASP PHE GLY LEU ARG PRO VAL MET THR LEU ALA ALA          
SEQRES  23 D  410  SER LEU ALA LEU VAL LYS GLN VAL PRO GLY GLY HIS GLY          
SEQRES  24 D  410  VAL SER TYR GLY HIS HIS TYR THR THR PRO GLY GLU THR          
SEQRES  25 D  410  THR LEU GLY LEU VAL PRO LEU GLY TYR ALA ASP GLY ILE          
SEQRES  26 D  410  PRO ARG HIS ALA SER SER SER GLY PRO VAL LEU VAL ASP          
SEQRES  27 D  410  GLY LYS TRP ARG THR VAL ALA GLY ARG ILE ALA MET ASP          
SEQRES  28 D  410  GLN PHE VAL VAL ASP LEU GLY GLY ASP ARG PRO GLU PRO          
SEQRES  29 D  410  GLY ALA GLU ALA VAL LEU PHE GLY PRO GLY ASP ARG GLY          
SEQRES  30 D  410  GLU PRO THR ALA GLU ASP TRP ALA GLN ALA ALA GLY THR          
SEQRES  31 D  410  ILE ALA TYR GLU ILE VAL THR ARG ILE GLY SER ARG VAL          
SEQRES  32 D  410  PRO ARG VAL TYR VAL ASN GLU                                  
MODRES 5FAG KCX A  141  LYS  MODIFIED RESIDUE                                   
MODRES 5FAG KCX B  141  LYS  MODIFIED RESIDUE                                   
MODRES 5FAG KCX C  141  LYS  MODIFIED RESIDUE                                   
MODRES 5FAG KCX D  141  LYS  MODIFIED RESIDUE                                   
HET    KCX  A 141      12                                                       
HET    KCX  B 141      12                                                       
HET    KCX  C 141      12                                                       
HET    KCX  D 141      12                                                       
HET    PLP  A 401      15                                                       
HET    PPI  A 402       5                                                       
HET     NA  A 403       1                                                       
HET     NA  A 404       1                                                       
HET    NO3  A 405       4                                                       
HET    PPI  B 501       5                                                       
HET    PLP  B 502      15                                                       
HET     NA  B 503       1                                                       
HET     NA  B 504       1                                                       
HET    PPI  B 505       5                                                       
HET    PPI  B 506       5                                                       
HET    PPI  B 507       5                                                       
HET    NO3  B 508       4                                                       
HET    PLP  C 401      15                                                       
HET    PPI  C 402       5                                                       
HET     NA  C 403       1                                                       
HET    PPI  D 501       5                                                       
HET    PLP  D 502      15                                                       
HET    PPI  D 503       5                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     PPI PROPANOIC ACID                                                   
HETNAM      NA SODIUM ION                                                       
HETNAM     NO3 NITRATE ION                                                      
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   1  KCX    4(C7 H14 N2 O4)                                              
FORMUL   5  PLP    4(C8 H10 N O6 P)                                             
FORMUL   6  PPI    8(C3 H6 O2)                                                  
FORMUL   7   NA    5(NA 1+)                                                     
FORMUL   9  NO3    2(N O3 1-)                                                   
FORMUL  24  HOH   *804(H2 O)                                                    
HELIX    1 AA1 SER A    2  VAL A   13  1                                  12    
HELIX    2 AA2 LEU A   22  ALA A   36  1                                  15    
HELIX    3 AA3 VAL A   45  GLY A   51  1                                   7    
HELIX    4 AA4 GLY A   53  ALA A   64  1                                  12    
HELIX    5 AA5 THR A   73  ALA A   82  1                                  10    
HELIX    6 AA6 PRO A  103  ALA A  110  1                                   8    
HELIX    7 AA7 ALA A  118  GLY A  133  1                                  16    
HELIX    8 AA8 GLY A  154  GLU A  170  1                                  17    
HELIX    9 AA9 HIS A  190  ARG A  210  1                                  21    
HELIX   10 AB1 ASN A  221  LEU A  228  1                                   8    
HELIX   11 AB2 PRO A  229  HIS A  232  5                                   4    
HELIX   12 AB3 PRO A  238  TYR A  243  1                                   6    
HELIX   13 AB4 PRO A  254  GLY A  258  5                                   5    
HELIX   14 AB5 SER A  282  HIS A  286  5                                   5    
HELIX   15 AB6 GLY A  301  GLY A  305  5                                   5    
HELIX   16 AB7 PRO A  307  SER A  311  5                                   5    
HELIX   17 AB8 THR A  361  ALA A  369  1                                   9    
HELIX   18 AB9 ILE A  372  ARG A  379  1                                   8    
HELIX   19 AC1 ASP B   11  LEU B   14  5                                   4    
HELIX   20 AC2 LEU B   22  ALA B   36  1                                  15    
HELIX   21 AC3 VAL B   45  HIS B   52  1                                   8    
HELIX   22 AC4 GLY B   53  ALA B   64  1                                  12    
HELIX   23 AC5 THR B   73  ALA B   82  1                                  10    
HELIX   24 AC6 PRO B  103  ALA B  110  1                                   8    
HELIX   25 AC7 ALA B  118  GLY B  133  1                                  16    
HELIX   26 AC8 GLY B  154  GLU B  170  1                                  17    
HELIX   27 AC9 HIS B  190  ARG B  210  1                                  21    
HELIX   28 AD1 ASN B  221  LEU B  228  1                                   8    
HELIX   29 AD2 PRO B  229  HIS B  232  5                                   4    
HELIX   30 AD3 PRO B  238  TYR B  243  1                                   6    
HELIX   31 AD4 PRO B  254  GLY B  258  5                                   5    
HELIX   32 AD5 SER B  282  HIS B  286  5                                   5    
HELIX   33 AD6 GLY B  301  GLY B  305  5                                   5    
HELIX   34 AD7 PRO B  307  SER B  311  5                                   5    
HELIX   35 AD8 THR B  361  GLY B  370  1                                  10    
HELIX   36 AD9 ILE B  372  ARG B  379  1                                   8    
HELIX   37 AE1 ASP C   11  LEU C   14  5                                   4    
HELIX   38 AE2 LEU C   22  ALA C   36  1                                  15    
HELIX   39 AE3 VAL C   45  GLY C   51  1                                   7    
HELIX   40 AE4 GLY C   53  ALA C   64  1                                  12    
HELIX   41 AE5 THR C   73  ALA C   82  1                                  10    
HELIX   42 AE6 PRO C  103  ALA C  110  1                                   8    
HELIX   43 AE7 ALA C  118  GLY C  133  1                                  16    
HELIX   44 AE8 GLY C  154  GLU C  170  1                                  17    
HELIX   45 AE9 HIS C  190  ARG C  210  1                                  21    
HELIX   46 AF1 ASN C  221  LEU C  228  1                                   8    
HELIX   47 AF2 PRO C  229  HIS C  232  5                                   4    
HELIX   48 AF3 PRO C  238  TYR C  243  1                                   6    
HELIX   49 AF4 PRO C  254  GLY C  258  5                                   5    
HELIX   50 AF5 SER C  282  HIS C  286  5                                   5    
HELIX   51 AF6 GLY C  301  GLY C  305  5                                   5    
HELIX   52 AF7 PRO C  307  SER C  311  5                                   5    
HELIX   53 AF8 THR C  361  GLY C  370  1                                  10    
HELIX   54 AF9 ILE C  372  ARG C  379  1                                   8    
HELIX   55 AG1 ASP D   11  LEU D   14  5                                   4    
HELIX   56 AG2 LEU D   22  ALA D   36  1                                  15    
HELIX   57 AG3 VAL D   45  GLY D   51  1                                   7    
HELIX   58 AG4 GLY D   53  ALA D   64  1                                  12    
HELIX   59 AG5 THR D   73  ALA D   82  1                                  10    
HELIX   60 AG6 PRO D  103  ALA D  110  1                                   8    
HELIX   61 AG7 ALA D  118  GLY D  133  1                                  16    
HELIX   62 AG8 GLY D  154  GLU D  170  1                                  17    
HELIX   63 AG9 HIS D  190  ARG D  210  1                                  21    
HELIX   64 AH1 ASN D  221  LEU D  228  1                                   8    
HELIX   65 AH2 PRO D  229  HIS D  232  5                                   4    
HELIX   66 AH3 PRO D  238  TYR D  243  1                                   6    
HELIX   67 AH4 PRO D  254  GLY D  258  5                                   5    
HELIX   68 AH5 SER D  282  HIS D  286  5                                   5    
HELIX   69 AH6 GLY D  301  GLY D  305  5                                   5    
HELIX   70 AH7 PRO D  307  SER D  311  5                                   5    
HELIX   71 AH8 THR D  361  ALA D  369  1                                   9    
HELIX   72 AH9 ILE D  372  ARG D  379  1                                   8    
SHEET    1 AA1 6 LYS A 321  THR A 324  0                                        
SHEET    2 AA1 6 PRO A 315  VAL A 318 -1  N  VAL A 316   O  ARG A 323           
SHEET    3 AA1 6 GLU A 348  PHE A 352 -1  O  VAL A 350   N  LEU A 317           
SHEET    4 AA1 6 MET A 263  SER A 268 -1  N  ALA A 267   O  ALA A 349           
SHEET    5 AA1 6 ALA A  16  ASP A  21 -1  N  GLU A  19   O  THR A 264           
SHEET    6 AA1 6 ARG A 386  VAL A 389  1  O  VAL A 387   N  ILE A  20           
SHEET    1 AA2 8 VAL A 216  HIS A 218  0                                        
SHEET    2 AA2 8 LEU A 173  TRP A 179  1  N  THR A 176   O  VAL A 216           
SHEET    3 AA2 8 ALA A 136  KCX A 141  1  N  VAL A 138   O  ARG A 174           
SHEET    4 AA2 8 ASP A 113  VAL A 116  1  N  VAL A 114   O  GLN A 139           
SHEET    5 AA2 8 ARG A  92  CYS A  95  1  N  ILE A  93   O  ASP A 113           
SHEET    6 AA2 8 TRP A  68  THR A  71  1  N  LEU A  69   O  MET A  94           
SHEET    7 AA2 8 ALA A  40  VAL A  44  1  N  ALA A  43   O  TRP A  68           
SHEET    8 AA2 8 LEU A 235  VAL A 236  1  O  VAL A 236   N  MET A  42           
SHEET    1 AA3 3 LEU A 271  VAL A 275  0                                        
SHEET    2 AA3 3 THR A 293  VAL A 298 -1  O  LEU A 295   N  LYS A 273           
SHEET    3 AA3 3 PHE A 334  ASP A 337 -1  O  PHE A 334   N  VAL A 298           
SHEET    1 AA4 2 GLY A 280  VAL A 281  0                                        
SHEET    2 AA4 2 TYR A 287  THR A 288 -1  O  TYR A 287   N  VAL A 281           
SHEET    1 AA5 6 LYS B 321  THR B 324  0                                        
SHEET    2 AA5 6 PRO B 315  VAL B 318 -1  N  VAL B 316   O  ARG B 323           
SHEET    3 AA5 6 GLU B 348  PHE B 352 -1  O  VAL B 350   N  LEU B 317           
SHEET    4 AA5 6 MET B 263  SER B 268 -1  N  ALA B 267   O  ALA B 349           
SHEET    5 AA5 6 ALA B  16  ASP B  21 -1  N  GLU B  19   O  THR B 264           
SHEET    6 AA5 6 ARG B 386  VAL B 389  1  O  VAL B 387   N  ILE B  20           
SHEET    1 AA6 8 VAL B 216  HIS B 218  0                                        
SHEET    2 AA6 8 LEU B 173  TRP B 179  1  N  THR B 176   O  VAL B 216           
SHEET    3 AA6 8 ALA B 136  KCX B 141  1  N  VAL B 138   O  ARG B 174           
SHEET    4 AA6 8 ASP B 113  VAL B 116  1  N  VAL B 114   O  GLN B 139           
SHEET    5 AA6 8 ARG B  92  CYS B  95  1  N  ILE B  93   O  ASP B 113           
SHEET    6 AA6 8 TRP B  68  THR B  71  1  N  LEU B  69   O  MET B  94           
SHEET    7 AA6 8 ALA B  40  VAL B  44  1  N  ALA B  43   O  TRP B  68           
SHEET    8 AA6 8 LEU B 235  VAL B 236  1  O  VAL B 236   N  MET B  42           
SHEET    1 AA7 3 LEU B 271  VAL B 275  0                                        
SHEET    2 AA7 3 THR B 293  VAL B 298 -1  O  THR B 293   N  VAL B 275           
SHEET    3 AA7 3 PHE B 334  ASP B 337 -1  O  PHE B 334   N  VAL B 298           
SHEET    1 AA8 2 GLY B 280  VAL B 281  0                                        
SHEET    2 AA8 2 TYR B 287  THR B 288 -1  O  TYR B 287   N  VAL B 281           
SHEET    1 AA9 6 LYS C 321  THR C 324  0                                        
SHEET    2 AA9 6 PRO C 315  VAL C 318 -1  N  VAL C 316   O  ARG C 323           
SHEET    3 AA9 6 GLU C 348  PHE C 352 -1  O  VAL C 350   N  LEU C 317           
SHEET    4 AA9 6 MET C 263  SER C 268 -1  N  ALA C 267   O  ALA C 349           
SHEET    5 AA9 6 ALA C  16  ASP C  21 -1  N  GLU C  19   O  THR C 264           
SHEET    6 AA9 6 ARG C 386  VAL C 389  1  O  VAL C 387   N  ILE C  20           
SHEET    1 AB1 8 VAL C 216  HIS C 218  0                                        
SHEET    2 AB1 8 LEU C 173  TRP C 179  1  N  THR C 176   O  VAL C 216           
SHEET    3 AB1 8 ALA C 136  KCX C 141  1  N  VAL C 138   O  ARG C 174           
SHEET    4 AB1 8 ASP C 113  VAL C 116  1  N  VAL C 114   O  ARG C 137           
SHEET    5 AB1 8 ARG C  92  CYS C  95  1  N  ILE C  93   O  ASP C 113           
SHEET    6 AB1 8 TRP C  68  THR C  71  1  N  LEU C  69   O  MET C  94           
SHEET    7 AB1 8 ALA C  40  VAL C  44  1  N  ALA C  43   O  TRP C  68           
SHEET    8 AB1 8 LEU C 235  VAL C 236  1  O  VAL C 236   N  MET C  42           
SHEET    1 AB2 3 LEU C 271  VAL C 275  0                                        
SHEET    2 AB2 3 THR C 293  VAL C 298 -1  O  LEU C 295   N  LYS C 273           
SHEET    3 AB2 3 PHE C 334  ASP C 337 -1  O  PHE C 334   N  VAL C 298           
SHEET    1 AB3 2 GLY C 280  VAL C 281  0                                        
SHEET    2 AB3 2 TYR C 287  THR C 288 -1  O  TYR C 287   N  VAL C 281           
SHEET    1 AB4 6 LYS D 321  THR D 324  0                                        
SHEET    2 AB4 6 PRO D 315  VAL D 318 -1  N  VAL D 316   O  ARG D 323           
SHEET    3 AB4 6 GLU D 348  PHE D 352 -1  O  VAL D 350   N  LEU D 317           
SHEET    4 AB4 6 MET D 263  SER D 268 -1  N  ALA D 267   O  ALA D 349           
SHEET    5 AB4 6 ALA D  16  ASP D  21 -1  N  GLU D  19   O  THR D 264           
SHEET    6 AB4 6 ARG D 386  VAL D 389  1  O  VAL D 387   N  ILE D  20           
SHEET    1 AB5 8 VAL D 216  HIS D 218  0                                        
SHEET    2 AB5 8 LEU D 173  TRP D 179  1  N  THR D 176   O  VAL D 216           
SHEET    3 AB5 8 ALA D 136  KCX D 141  1  N  VAL D 138   O  ARG D 174           
SHEET    4 AB5 8 ASP D 113  VAL D 116  1  N  VAL D 114   O  ARG D 137           
SHEET    5 AB5 8 ARG D  92  CYS D  95  1  N  ILE D  93   O  ASP D 113           
SHEET    6 AB5 8 TRP D  68  THR D  71  1  N  LEU D  69   O  MET D  94           
SHEET    7 AB5 8 ALA D  40  VAL D  44  1  N  ALA D  43   O  TRP D  68           
SHEET    8 AB5 8 LEU D 235  VAL D 236  1  O  VAL D 236   N  MET D  42           
SHEET    1 AB6 3 LEU D 271  VAL D 275  0                                        
SHEET    2 AB6 3 THR D 293  VAL D 298 -1  O  LEU D 295   N  LYS D 273           
SHEET    3 AB6 3 PHE D 334  ASP D 337 -1  O  PHE D 334   N  VAL D 298           
SHEET    1 AB7 2 GLY D 280  VAL D 281  0                                        
SHEET    2 AB7 2 TYR D 287  THR D 288 -1  O  TYR D 287   N  VAL D 281           
LINK         O   MET A  42                NA    NA A 403     1555   1555  2.80  
LINK         NZ  LYS A  46                 C4A PLP A 401     1555   1555  1.30  
LINK         C   LEU A 140                 N   KCX A 141     1555   1555  1.33  
LINK         C   KCX A 141                 N   ALA A 142     1555   1555  1.33  
LINK         OG  SER A 180                NA    NA A 404     1555   1555  3.04  
LINK         O   PRO A 238                NA    NA A 403     1555   1555  2.77  
LINK         NZ  LYS B  46                 C4A PLP B 502     1555   1555  1.34  
LINK         C   LEU B 140                 N   KCX B 141     1555   1555  1.33  
LINK         C   KCX B 141                 N   ALA B 142     1555   1555  1.33  
LINK         OG  SER B 180                NA    NA B 504     1555   1555  3.11  
LINK         O   HIS B 181                NA    NA B 504     1555   1555  3.17  
LINK         O   ALA B 326                NA    NA B 503     1555   1555  2.72  
LINK         O   ARG B 328                NA    NA B 503     1555   1555  2.83  
LINK         NZ  LYS C  46                 C4A PLP C 401     1555   1555  1.29  
LINK         C   LEU C 140                 N   KCX C 141     1555   1555  1.33  
LINK         C   KCX C 141                 N   ALA C 142     1555   1555  1.32  
LINK         O   ALA C 231                NA    NA C 403     1555   1555  2.62  
LINK         O   HIS C 232                NA    NA C 403     1555   1555  2.94  
LINK         O   LEU C 235                NA    NA C 403     1555   1555  2.73  
LINK         NZ  LYS D  46                 C4A PLP D 502     1555   1555  1.28  
LINK         C   LEU D 140                 N   KCX D 141     1555   1555  1.34  
LINK         C   KCX D 141                 N   ALA D 142     1555   1555  1.33  
LINK        NA    NA A 404                 O   HOH A 698     1555   1555  3.05  
LINK        NA    NA B 504                 O   HOH B 606     1555   1555  3.06  
CISPEP   1 GLU A   84    PRO A   85          0        -1.92                     
CISPEP   2 GLU B   84    PRO B   85          0        -8.10                     
CISPEP   3 GLU C   84    PRO C   85          0         2.61                     
CISPEP   4 GLU D   84    PRO D   85          0        -0.03                     
CISPEP   5 GLU D   84    PRO D   85          0        -1.25                     
SITE     1 AC1 13 LYS A  46  TYR A  50  TRP A  96  KCX A 141                    
SITE     2 AC1 13 TRP A 179  SER A 222  ARG A 237  PRO A 238                    
SITE     3 AC1 13 GLY A 239  ILE A 240  TYR A 374  HOH A 600                    
SITE     4 AC1 13 PPI B 501                                                     
SITE     1 AC2  9 TYR A 283  ALA A 330  MET A 331  HOH A 559                    
SITE     2 AC2  9 HOH A 566  LYS B  46  TYR B  50  ARG B 148                    
SITE     3 AC2  9 PLP B 502                                                     
SITE     1 AC3  5 MET A  42  ALA A  43  VAL A  44  PRO A 238                    
SITE     2 AC3  5 GLY A 239                                                     
SITE     1 AC4  9 ALA A 142  ASP A 143  THR A 144  GLY A 145                    
SITE     2 AC4  9 LEU A 146  SER A 180  HIS A 181  GLN A 196                    
SITE     3 AC4  9 HOH A 698                                                     
SITE     1 AC5  8 ARG A  26  ARG A  30  ALA A  63  ALA A  64                    
SITE     2 AC5  8 HOH A 532  HOH A 606  ARG C 260  ASP C 356                    
SITE     1 AC6  8 LYS A  46  PLP A 401  HOH A 600  TYR B 283                    
SITE     2 AC6  8 ALA B 330  MET B 331  HOH B 663  HOH B 672                    
SITE     1 AC7  5 SER B 282  ALA B 326  ARG B 328  PHE B 334                    
SITE     2 AC7  5 VAL B 335                                                     
SITE     1 AC8  8 ASP B 143  THR B 144  GLY B 145  LEU B 146                    
SITE     2 AC8  8 SER B 180  HIS B 181  GLN B 196  HOH B 606                    
SITE     1 AC9  4 GLY B 154  GLU B 158  TYR B 206  HOH B 812                    
SITE     1 AD1  2 TYR B 388  GLU B 391                                          
SITE     1 AD2  5 GLU B 208  ARG B 217  ARG C 166  GLU C 169                    
SITE     2 AD2  5 HOH C 505                                                     
SITE     1 AD3  8 ARG B  26  ARG B  30  ALA B  63  ALA B  64                    
SITE     2 AD3  8 HOH B 733  HOH B 776  ARG D 260  ASP D 356                    
SITE     1 AD4  9 TYR C 283  TYR C 302  ALA C 330  MET C 331                    
SITE     2 AD4  9 HOH C 501  LYS D  46  TYR D 374  PLP D 502                    
SITE     3 AD4  9 HOH D 725                                                     
SITE     1 AD5  6 HIS C 218  ILE C 219  ALA C 220  ALA C 231                    
SITE     2 AD5  6 HIS C 232  LEU C 235                                          
SITE     1 AD6  8 LYS C  46  PLP C 401  HOH C 551  TYR D 283                    
SITE     2 AD6  8 ALA D 330  MET D 331  HOH D 636  HOH D 664                    
SITE     1 AD7  7 TYR D 287  THR D 324  VAL D 325  ALA D 326                    
SITE     2 AD7  7 ASP D 337  HOH D 692  HOH D 709                               
SITE     1 AD8 24 MET A 331  ASP A 332  PPI A 402  HOH A 517                    
SITE     2 AD8 24 VAL B  44  VAL B  45  ALA B  47  ASP B  48                    
SITE     3 AD8 24 ALA B  49  TYR B  50  GLY B  70  ALA B  72                    
SITE     4 AD8 24 TRP B  96  KCX B 141  TRP B 179  HIS B 181                    
SITE     5 AD8 24 ASN B 221  SER B 222  ARG B 237  PRO B 238                    
SITE     6 AD8 24 GLY B 239  ILE B 240  TYR B 374  HOH B 664                    
SITE     1 AD9 23 VAL C  44  VAL C  45  ALA C  47  ASP C  48                    
SITE     2 AD9 23 ALA C  49  TYR C  50  GLY C  70  ALA C  72                    
SITE     3 AD9 23 TRP C  96  KCX C 141  TRP C 179  HIS C 181                    
SITE     4 AD9 23 ASN C 221  SER C 222  ARG C 237  PRO C 238                    
SITE     5 AD9 23 GLY C 239  ILE C 240  TYR C 374  HOH C 507                    
SITE     6 AD9 23 HOH C 551  ASP D 332  PPI D 501                               
SITE     1 AE1 21 ASP C 332  PPI C 402  VAL D  44  VAL D  45                    
SITE     2 AE1 21 ALA D  47  ASP D  48  ALA D  49  TYR D  50                    
SITE     3 AE1 21 GLY D  70  ALA D  72  TRP D  96  KCX D 141                    
SITE     4 AE1 21 TRP D 179  HIS D 181  ASN D 221  SER D 222                    
SITE     5 AE1 21 ARG D 237  PRO D 238  GLY D 239  ILE D 240                    
SITE     6 AE1 21 TYR D 374                                                     
CRYST1   79.950   88.580  108.880  90.00 102.60  90.00 P 1 21 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      0.012508  0.000000  0.002795        0.00000                         
SCALE2      0.000000  0.011289  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009411        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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