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Database: PDB
Entry: 4WR3
LinkDB: 4WR3
Original site: 4WR3 
HEADER    ISOMERASE                               23-OCT-14   4WR3              
TITLE     Y274F ALANINE RACEMASE FROM E. COLI                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE, BIOSYNTHETIC;                            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: ALR;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ISOMERASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.J.SQUIRE,Y.YOSAATMADJA,W.M.PATRICK                                  
REVDAT   1   04-NOV-15 4WR3    0                                                
JRNL        AUTH   C.J.SQUIRE                                                   
JRNL        TITL   Y274F ALANINE RACEMASE FROM E. COLI                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0071                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 149471                         
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                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9981                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10733                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1037                         
REMARK   3   BIN FREE R VALUE                    : 0.1830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10920                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 103                                     
REMARK   3   SOLVENT ATOMS            : 467                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.024         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.023         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.043         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.333         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11290 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 10877 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15340 ; 1.349 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 24926 ; 0.795 ; 2.996       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1435 ; 6.335 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   482 ;35.381 ;22.759       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1821 ;15.118 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   109 ;15.929 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1720 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12812 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2567 ; 0.001 ; 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):  5740 ; 1.093 ; 2.208       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5739 ; 1.093 ; 2.208       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7175 ; 1.730 ; 3.306       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  7176 ; 1.730 ; 3.307       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5550 ; 1.197 ; 2.379       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  5550 ; 1.197 ; 2.379       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  8166 ; 1.924 ; 3.505       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 12586 ; 3.367 ;17.662       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 12586 ; 3.367 ;17.662       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4WR3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204364.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-OCT-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC MIRROR                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 168143                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.860                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.720                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 22.10                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 16.40                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 2RJG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0, 1.6 M AMMONIUM       
REMARK 280  SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z                                                
REMARK 290       6555   X-Y,X,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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        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: 8270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 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: 7070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 B     1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLN C     2                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLN D     2                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 172    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 356    CD   CE   NZ                                        
REMARK 470     LYS C 167    CG   CD   CE   NZ                                   
REMARK 470     GLU C 327    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 333    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 336    CG   CD   OE1  OE2                                  
REMARK 470     HIS D 142    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS D 167    CG   CD   CE   NZ                                   
REMARK 470     GLU D 336    CG   CD   OE1  OE2                                  
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   3     -167.62    -78.15                                   
REMARK 500    ARG A 129      -80.16   -108.13                                   
REMARK 500    ARG A 162       38.23   -143.71                                   
REMARK 500    ALA A 193     -154.73   -103.86                                   
REMARK 500    PHE A 205     -136.47     60.51                                   
REMARK 500    GLU A 221       44.05   -109.72                                   
REMARK 500    SER A 239     -157.41   -160.96                                   
REMARK 500    LEU A 329       87.64   -158.93                                   
REMARK 500    ALA B   3     -152.25    -92.46                                   
REMARK 500    ARG B 129      -84.09   -107.78                                   
REMARK 500    ARG B 162       39.08   -143.75                                   
REMARK 500    PRO B 186     -169.26    -68.88                                   
REMARK 500    ALA B 193     -151.30   -108.11                                   
REMARK 500    PHE B 205     -135.78     43.79                                   
REMARK 500    GLU B 221       57.50   -107.93                                   
REMARK 500    ARG B 223      -10.85     83.19                                   
REMARK 500    SER B 239     -151.37   -160.45                                   
REMARK 500    LEU B 329       82.35   -151.72                                   
REMARK 500    ARG B 348       56.86    -90.08                                   
REMARK 500    ARG C 129      -84.98    -99.92                                   
REMARK 500    ARG C 162       39.01   -143.28                                   
REMARK 500    ALA C 193     -155.11    -99.37                                   
REMARK 500    PHE C 205     -137.85     49.01                                   
REMARK 500    SER C 239     -160.27   -161.07                                   
REMARK 500    LEU C 329       78.21   -150.11                                   
REMARK 500    ARG C 348       51.51    -90.15                                   
REMARK 500    ALA D   4      108.47    -56.10                                   
REMARK 500    ARG D 129      -80.04   -113.13                                   
REMARK 500    ARG D 162       37.03   -147.63                                   
REMARK 500    GLU D 183      103.00    -40.07                                   
REMARK 500    ALA D 193     -155.74   -108.83                                   
REMARK 500    PHE D 205     -138.01     47.54                                   
REMARK 500    GLU D 221       51.21   -114.56                                   
REMARK 500    ARG D 223       -5.97     87.86                                   
REMARK 500    SER D 239     -157.90   -160.26                                   
REMARK 500    LEU D 329       88.99   -151.06                                   
REMARK 500    ARG D 348       57.12    -99.16                                   
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 PLP A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP C 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP D 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 1002                
DBREF  4WR3 A    1   359  UNP    P0A6B4   ALR1_ECOLI       1    359             
DBREF  4WR3 B    1   359  UNP    P0A6B4   ALR1_ECOLI       1    359             
DBREF  4WR3 C    1   359  UNP    P0A6B4   ALR1_ECOLI       1    359             
DBREF  4WR3 D    1   359  UNP    P0A6B4   ALR1_ECOLI       1    359             
SEQADV 4WR3 PHE A  274  UNP  P0A6B4    TYR   274 ENGINEERED MUTATION            
SEQADV 4WR3 PHE B  274  UNP  P0A6B4    TYR   274 ENGINEERED MUTATION            
SEQADV 4WR3 PHE C  274  UNP  P0A6B4    TYR   274 ENGINEERED MUTATION            
SEQADV 4WR3 PHE D  274  UNP  P0A6B4    TYR   274 ENGINEERED MUTATION            
SEQRES   1 A  359  MET GLN ALA ALA THR VAL VAL ILE ASN ARG ARG ALA LEU          
SEQRES   2 A  359  ARG HIS ASN LEU GLN ARG LEU ARG GLU LEU ALA PRO ALA          
SEQRES   3 A  359  SER LYS MET VAL ALA VAL VAL LYS ALA ASN ALA TYR GLY          
SEQRES   4 A  359  HIS GLY LEU LEU GLU THR ALA ARG THR LEU PRO ASP ALA          
SEQRES   5 A  359  ASP ALA PHE GLY VAL ALA ARG LEU GLU GLU ALA LEU ARG          
SEQRES   6 A  359  LEU ARG ALA GLY GLY ILE THR LYS PRO VAL LEU LEU LEU          
SEQRES   7 A  359  GLU GLY PHE PHE ASP ALA ARG ASP LEU PRO THR ILE SER          
SEQRES   8 A  359  ALA GLN HIS PHE HIS THR ALA VAL HIS ASN GLU GLU GLN          
SEQRES   9 A  359  LEU ALA ALA LEU GLU GLU ALA SER LEU ASP GLU PRO VAL          
SEQRES  10 A  359  THR VAL TRP MET LYS LEU ASP THR GLY MET HIS ARG LEU          
SEQRES  11 A  359  GLY VAL ARG PRO GLU GLN ALA GLU ALA PHE TYR HIS ARG          
SEQRES  12 A  359  LEU THR GLN CYS LYS ASN VAL ARG GLN PRO VAL ASN ILE          
SEQRES  13 A  359  VAL SER HIS PHE ALA ARG ALA ASP GLU PRO LYS CYS GLY          
SEQRES  14 A  359  ALA THR GLU LYS GLN LEU ALA ILE PHE ASN THR PHE CYS          
SEQRES  15 A  359  GLU GLY LYS PRO GLY GLN ARG SER ILE ALA ALA SER GLY          
SEQRES  16 A  359  GLY ILE LEU LEU TRP PRO GLN SER HIS PHE ASP TRP VAL          
SEQRES  17 A  359  ARG PRO GLY ILE ILE LEU TYR GLY VAL SER PRO LEU GLU          
SEQRES  18 A  359  ASP ARG SER THR GLY ALA ASP PHE GLY CYS GLN PRO VAL          
SEQRES  19 A  359  MET SER LEU THR SER SER LEU ILE ALA VAL ARG GLU HIS          
SEQRES  20 A  359  LYS ALA GLY GLU PRO VAL GLY TYR GLY GLY THR TRP VAL          
SEQRES  21 A  359  SER GLU ARG ASP THR ARG LEU GLY VAL VAL ALA MET GLY          
SEQRES  22 A  359  PHE GLY ASP GLY TYR PRO ARG ALA ALA PRO SER GLY THR          
SEQRES  23 A  359  PRO VAL LEU VAL ASN GLY ARG GLU VAL PRO ILE VAL GLY          
SEQRES  24 A  359  ARG VAL ALA MET ASP MET ILE CYS VAL ASP LEU GLY PRO          
SEQRES  25 A  359  GLN ALA GLN ASP LYS ALA GLY ASP PRO VAL ILE LEU TRP          
SEQRES  26 A  359  GLY GLU GLY LEU PRO VAL GLU ARG ILE ALA GLU MET THR          
SEQRES  27 A  359  LYS VAL SER ALA TYR GLU LEU ILE THR ARG LEU THR SER          
SEQRES  28 A  359  ARG VAL ALA MET LYS TYR VAL ASP                              
SEQRES   1 B  359  MET GLN ALA ALA THR VAL VAL ILE ASN ARG ARG ALA LEU          
SEQRES   2 B  359  ARG HIS ASN LEU GLN ARG LEU ARG GLU LEU ALA PRO ALA          
SEQRES   3 B  359  SER LYS MET VAL ALA VAL VAL LYS ALA ASN ALA TYR GLY          
SEQRES   4 B  359  HIS GLY LEU LEU GLU THR ALA ARG THR LEU PRO ASP ALA          
SEQRES   5 B  359  ASP ALA PHE GLY VAL ALA ARG LEU GLU GLU ALA LEU ARG          
SEQRES   6 B  359  LEU ARG ALA GLY GLY ILE THR LYS PRO VAL LEU LEU LEU          
SEQRES   7 B  359  GLU GLY PHE PHE ASP ALA ARG ASP LEU PRO THR ILE SER          
SEQRES   8 B  359  ALA GLN HIS PHE HIS THR ALA VAL HIS ASN GLU GLU GLN          
SEQRES   9 B  359  LEU ALA ALA LEU GLU GLU ALA SER LEU ASP GLU PRO VAL          
SEQRES  10 B  359  THR VAL TRP MET LYS LEU ASP THR GLY MET HIS ARG LEU          
SEQRES  11 B  359  GLY VAL ARG PRO GLU GLN ALA GLU ALA PHE TYR HIS ARG          
SEQRES  12 B  359  LEU THR GLN CYS LYS ASN VAL ARG GLN PRO VAL ASN ILE          
SEQRES  13 B  359  VAL SER HIS PHE ALA ARG ALA ASP GLU PRO LYS CYS GLY          
SEQRES  14 B  359  ALA THR GLU LYS GLN LEU ALA ILE PHE ASN THR PHE CYS          
SEQRES  15 B  359  GLU GLY LYS PRO GLY GLN ARG SER ILE ALA ALA SER GLY          
SEQRES  16 B  359  GLY ILE LEU LEU TRP PRO GLN SER HIS PHE ASP TRP VAL          
SEQRES  17 B  359  ARG PRO GLY ILE ILE LEU TYR GLY VAL SER PRO LEU GLU          
SEQRES  18 B  359  ASP ARG SER THR GLY ALA ASP PHE GLY CYS GLN PRO VAL          
SEQRES  19 B  359  MET SER LEU THR SER SER LEU ILE ALA VAL ARG GLU HIS          
SEQRES  20 B  359  LYS ALA GLY GLU PRO VAL GLY TYR GLY GLY THR TRP VAL          
SEQRES  21 B  359  SER GLU ARG ASP THR ARG LEU GLY VAL VAL ALA MET GLY          
SEQRES  22 B  359  PHE GLY ASP GLY TYR PRO ARG ALA ALA PRO SER GLY THR          
SEQRES  23 B  359  PRO VAL LEU VAL ASN GLY ARG GLU VAL PRO ILE VAL GLY          
SEQRES  24 B  359  ARG VAL ALA MET ASP MET ILE CYS VAL ASP LEU GLY PRO          
SEQRES  25 B  359  GLN ALA GLN ASP LYS ALA GLY ASP PRO VAL ILE LEU TRP          
SEQRES  26 B  359  GLY GLU GLY LEU PRO VAL GLU ARG ILE ALA GLU MET THR          
SEQRES  27 B  359  LYS VAL SER ALA TYR GLU LEU ILE THR ARG LEU THR SER          
SEQRES  28 B  359  ARG VAL ALA MET LYS TYR VAL ASP                              
SEQRES   1 C  359  MET GLN ALA ALA THR VAL VAL ILE ASN ARG ARG ALA LEU          
SEQRES   2 C  359  ARG HIS ASN LEU GLN ARG LEU ARG GLU LEU ALA PRO ALA          
SEQRES   3 C  359  SER LYS MET VAL ALA VAL VAL LYS ALA ASN ALA TYR GLY          
SEQRES   4 C  359  HIS GLY LEU LEU GLU THR ALA ARG THR LEU PRO ASP ALA          
SEQRES   5 C  359  ASP ALA PHE GLY VAL ALA ARG LEU GLU GLU ALA LEU ARG          
SEQRES   6 C  359  LEU ARG ALA GLY GLY ILE THR LYS PRO VAL LEU LEU LEU          
SEQRES   7 C  359  GLU GLY PHE PHE ASP ALA ARG ASP LEU PRO THR ILE SER          
SEQRES   8 C  359  ALA GLN HIS PHE HIS THR ALA VAL HIS ASN GLU GLU GLN          
SEQRES   9 C  359  LEU ALA ALA LEU GLU GLU ALA SER LEU ASP GLU PRO VAL          
SEQRES  10 C  359  THR VAL TRP MET LYS LEU ASP THR GLY MET HIS ARG LEU          
SEQRES  11 C  359  GLY VAL ARG PRO GLU GLN ALA GLU ALA PHE TYR HIS ARG          
SEQRES  12 C  359  LEU THR GLN CYS LYS ASN VAL ARG GLN PRO VAL ASN ILE          
SEQRES  13 C  359  VAL SER HIS PHE ALA ARG ALA ASP GLU PRO LYS CYS GLY          
SEQRES  14 C  359  ALA THR GLU LYS GLN LEU ALA ILE PHE ASN THR PHE CYS          
SEQRES  15 C  359  GLU GLY LYS PRO GLY GLN ARG SER ILE ALA ALA SER GLY          
SEQRES  16 C  359  GLY ILE LEU LEU TRP PRO GLN SER HIS PHE ASP TRP VAL          
SEQRES  17 C  359  ARG PRO GLY ILE ILE LEU TYR GLY VAL SER PRO LEU GLU          
SEQRES  18 C  359  ASP ARG SER THR GLY ALA ASP PHE GLY CYS GLN PRO VAL          
SEQRES  19 C  359  MET SER LEU THR SER SER LEU ILE ALA VAL ARG GLU HIS          
SEQRES  20 C  359  LYS ALA GLY GLU PRO VAL GLY TYR GLY GLY THR TRP VAL          
SEQRES  21 C  359  SER GLU ARG ASP THR ARG LEU GLY VAL VAL ALA MET GLY          
SEQRES  22 C  359  PHE GLY ASP GLY TYR PRO ARG ALA ALA PRO SER GLY THR          
SEQRES  23 C  359  PRO VAL LEU VAL ASN GLY ARG GLU VAL PRO ILE VAL GLY          
SEQRES  24 C  359  ARG VAL ALA MET ASP MET ILE CYS VAL ASP LEU GLY PRO          
SEQRES  25 C  359  GLN ALA GLN ASP LYS ALA GLY ASP PRO VAL ILE LEU TRP          
SEQRES  26 C  359  GLY GLU GLY LEU PRO VAL GLU ARG ILE ALA GLU MET THR          
SEQRES  27 C  359  LYS VAL SER ALA TYR GLU LEU ILE THR ARG LEU THR SER          
SEQRES  28 C  359  ARG VAL ALA MET LYS TYR VAL ASP                              
SEQRES   1 D  359  MET GLN ALA ALA THR VAL VAL ILE ASN ARG ARG ALA LEU          
SEQRES   2 D  359  ARG HIS ASN LEU GLN ARG LEU ARG GLU LEU ALA PRO ALA          
SEQRES   3 D  359  SER LYS MET VAL ALA VAL VAL LYS ALA ASN ALA TYR GLY          
SEQRES   4 D  359  HIS GLY LEU LEU GLU THR ALA ARG THR LEU PRO ASP ALA          
SEQRES   5 D  359  ASP ALA PHE GLY VAL ALA ARG LEU GLU GLU ALA LEU ARG          
SEQRES   6 D  359  LEU ARG ALA GLY GLY ILE THR LYS PRO VAL LEU LEU LEU          
SEQRES   7 D  359  GLU GLY PHE PHE ASP ALA ARG ASP LEU PRO THR ILE SER          
SEQRES   8 D  359  ALA GLN HIS PHE HIS THR ALA VAL HIS ASN GLU GLU GLN          
SEQRES   9 D  359  LEU ALA ALA LEU GLU GLU ALA SER LEU ASP GLU PRO VAL          
SEQRES  10 D  359  THR VAL TRP MET LYS LEU ASP THR GLY MET HIS ARG LEU          
SEQRES  11 D  359  GLY VAL ARG PRO GLU GLN ALA GLU ALA PHE TYR HIS ARG          
SEQRES  12 D  359  LEU THR GLN CYS LYS ASN VAL ARG GLN PRO VAL ASN ILE          
SEQRES  13 D  359  VAL SER HIS PHE ALA ARG ALA ASP GLU PRO LYS CYS GLY          
SEQRES  14 D  359  ALA THR GLU LYS GLN LEU ALA ILE PHE ASN THR PHE CYS          
SEQRES  15 D  359  GLU GLY LYS PRO GLY GLN ARG SER ILE ALA ALA SER GLY          
SEQRES  16 D  359  GLY ILE LEU LEU TRP PRO GLN SER HIS PHE ASP TRP VAL          
SEQRES  17 D  359  ARG PRO GLY ILE ILE LEU TYR GLY VAL SER PRO LEU GLU          
SEQRES  18 D  359  ASP ARG SER THR GLY ALA ASP PHE GLY CYS GLN PRO VAL          
SEQRES  19 D  359  MET SER LEU THR SER SER LEU ILE ALA VAL ARG GLU HIS          
SEQRES  20 D  359  LYS ALA GLY GLU PRO VAL GLY TYR GLY GLY THR TRP VAL          
SEQRES  21 D  359  SER GLU ARG ASP THR ARG LEU GLY VAL VAL ALA MET GLY          
SEQRES  22 D  359  PHE GLY ASP GLY TYR PRO ARG ALA ALA PRO SER GLY THR          
SEQRES  23 D  359  PRO VAL LEU VAL ASN GLY ARG GLU VAL PRO ILE VAL GLY          
SEQRES  24 D  359  ARG VAL ALA MET ASP MET ILE CYS VAL ASP LEU GLY PRO          
SEQRES  25 D  359  GLN ALA GLN ASP LYS ALA GLY ASP PRO VAL ILE LEU TRP          
SEQRES  26 D  359  GLY GLU GLY LEU PRO VAL GLU ARG ILE ALA GLU MET THR          
SEQRES  27 D  359  LYS VAL SER ALA TYR GLU LEU ILE THR ARG LEU THR SER          
SEQRES  28 D  359  ARG VAL ALA MET LYS TYR VAL ASP                              
HET    PLP  A1001      15                                                       
HET    SO4  A1002       5                                                       
HET    SO4  A1003       5                                                       
HET    GOL  A1004       6                                                       
HET    PLP  B1001      15                                                       
HET    SO4  B1002       5                                                       
HET    SO4  B1003       5                                                       
HET    GOL  B1004       6                                                       
HET    PLP  C1001      15                                                       
HET    SO4  C1002       5                                                       
HET    PLP  D1001      15                                                       
HET    GOL  D1002       6                                                       
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  PLP    4(C8 H10 N O6 P)                                             
FORMUL   6  SO4    5(O4 S 2-)                                                   
FORMUL   8  GOL    3(C3 H8 O3)                                                  
FORMUL  17  HOH   *467(H2 O)                                                    
HELIX    1 AA1 ARG A   10  ALA A   24  1                                  15    
HELIX    2 AA2 VAL A   33  GLY A   39  1                                   7    
HELIX    3 AA3 GLY A   41  LEU A   49  1                                   9    
HELIX    4 AA4 ARG A   59  GLY A   69  1                                  11    
HELIX    5 AA5 ASP A   83  ARG A   85  5                                   3    
HELIX    6 AA6 ASP A   86  GLN A   93  1                                   8    
HELIX    7 AA7 ASN A  101  ALA A  111  1                                  11    
HELIX    8 AA8 ARG A  133  GLN A  146  1                                  14    
HELIX    9 AA9 GLY A  169  GLU A  183  1                                  15    
HELIX   10 AB1 ALA A  193  TRP A  200  1                                   8    
HELIX   11 AB2 PRO A  201  HIS A  204  5                                   4    
HELIX   12 AB3 GLY A  211  GLY A  216  5                                   6    
HELIX   13 AB4 THR A  225  GLY A  230  5                                   6    
HELIX   14 AB5 GLY A  254  THR A  258  5                                   5    
HELIX   15 AB6 PRO A  330  LYS A  339  1                                  10    
HELIX   16 AB7 SER A  341  ARG A  348  1                                   8    
HELIX   17 AB8 ARG B   10  ALA B   24  1                                  15    
HELIX   18 AB9 VAL B   33  GLY B   39  1                                   7    
HELIX   19 AC1 GLY B   41  LEU B   49  1                                   9    
HELIX   20 AC2 ARG B   59  GLY B   69  1                                  11    
HELIX   21 AC3 ASP B   83  ARG B   85  5                                   3    
HELIX   22 AC4 ASP B   86  HIS B   94  1                                   9    
HELIX   23 AC5 ASN B  101  ALA B  111  1                                  11    
HELIX   24 AC6 ARG B  133  GLN B  146  1                                  14    
HELIX   25 AC7 GLY B  169  GLU B  183  1                                  15    
HELIX   26 AC8 ALA B  193  TRP B  200  1                                   8    
HELIX   27 AC9 PRO B  201  HIS B  204  5                                   4    
HELIX   28 AD1 GLY B  211  GLY B  216  5                                   6    
HELIX   29 AD2 THR B  225  GLY B  230  5                                   6    
HELIX   30 AD3 GLY B  254  THR B  258  5                                   5    
HELIX   31 AD4 PRO B  330  LYS B  339  1                                  10    
HELIX   32 AD5 SER B  341  ARG B  348  1                                   8    
HELIX   33 AD6 ARG C   10  ALA C   24  1                                  15    
HELIX   34 AD7 VAL C   33  GLY C   39  1                                   7    
HELIX   35 AD8 GLY C   41  LEU C   49  1                                   9    
HELIX   36 AD9 ARG C   59  GLY C   69  1                                  11    
HELIX   37 AE1 ASP C   83  ARG C   85  5                                   3    
HELIX   38 AE2 ASP C   86  HIS C   94  1                                   9    
HELIX   39 AE3 ASN C  101  ALA C  111  1                                  11    
HELIX   40 AE4 ARG C  133  CYS C  147  1                                  15    
HELIX   41 AE5 GLY C  169  GLU C  183  1                                  15    
HELIX   42 AE6 ALA C  193  TRP C  200  1                                   8    
HELIX   43 AE7 PRO C  201  HIS C  204  5                                   4    
HELIX   44 AE8 GLY C  211  GLY C  216  5                                   6    
HELIX   45 AE9 THR C  225  GLY C  230  5                                   6    
HELIX   46 AF1 GLY C  254  THR C  258  5                                   5    
HELIX   47 AF2 PRO C  330  LYS C  339  1                                  10    
HELIX   48 AF3 SER C  341  ARG C  348  1                                   8    
HELIX   49 AF4 ARG D   10  ALA D   24  1                                  15    
HELIX   50 AF5 VAL D   33  GLY D   39  1                                   7    
HELIX   51 AF6 GLY D   41  LEU D   49  1                                   9    
HELIX   52 AF7 ARG D   59  GLY D   69  1                                  11    
HELIX   53 AF8 ASP D   83  ARG D   85  5                                   3    
HELIX   54 AF9 ASP D   86  GLN D   93  1                                   8    
HELIX   55 AG1 ASN D  101  ALA D  111  1                                  11    
HELIX   56 AG2 ARG D  133  GLU D  135  5                                   3    
HELIX   57 AG3 GLN D  136  THR D  145  1                                  10    
HELIX   58 AG4 GLY D  169  GLU D  183  1                                  15    
HELIX   59 AG5 ALA D  193  TRP D  200  1                                   8    
HELIX   60 AG6 PRO D  201  HIS D  204  5                                   4    
HELIX   61 AG7 GLY D  211  GLY D  216  5                                   6    
HELIX   62 AG8 THR D  225  GLY D  230  5                                   6    
HELIX   63 AG9 GLY D  254  THR D  258  5                                   5    
HELIX   64 AH1 PRO D  330  LYS D  339  1                                  10    
HELIX   65 AH2 SER D  341  ARG D  348  1                                   8    
SHEET    1 AA1 6 ARG A 293  PRO A 296  0                                        
SHEET    2 AA1 6 PRO A 287  VAL A 290 -1  N  VAL A 288   O  VAL A 295           
SHEET    3 AA1 6 PRO A 321  TRP A 325 -1  O  ILE A 323   N  LEU A 289           
SHEET    4 AA1 6 MET A 235  HIS A 247 -1  N  LEU A 237   O  TRP A 325           
SHEET    5 AA1 6 THR A 265  ALA A 271 -1  O  VAL A 269   N  ILE A 242           
SHEET    6 AA1 6 MET A 305  ASP A 309 -1  O  ILE A 306   N  VAL A 270           
SHEET    1 AA2 6 ARG A 293  PRO A 296  0                                        
SHEET    2 AA2 6 PRO A 287  VAL A 290 -1  N  VAL A 288   O  VAL A 295           
SHEET    3 AA2 6 PRO A 321  TRP A 325 -1  O  ILE A 323   N  LEU A 289           
SHEET    4 AA2 6 MET A 235  HIS A 247 -1  N  LEU A 237   O  TRP A 325           
SHEET    5 AA2 6 THR A   5  ASN A   9 -1  N  THR A   5   O  THR A 238           
SHEET    6 AA2 6 ALA A 354  VAL A 358  1  O  ALA A 354   N  VAL A   6           
SHEET    1 AA3 8 ARG A 189  SER A 190  0                                        
SHEET    2 AA3 8 ASN A 155  VAL A 157  1  N  ILE A 156   O  SER A 190           
SHEET    3 AA3 8 VAL A 119  LYS A 122  1  N  MET A 121   O  ASN A 155           
SHEET    4 AA3 8 PHE A  95  VAL A  99  1  N  VAL A  99   O  LYS A 122           
SHEET    5 AA3 8 VAL A  75  LEU A  77  1  N  LEU A  77   O  HIS A  96           
SHEET    6 AA3 8 ALA A  54  VAL A  57  1  N  VAL A  57   O  LEU A  76           
SHEET    7 AA3 8 LYS A  28  VAL A  32  1  N  ALA A  31   O  ALA A  54           
SHEET    8 AA3 8 TRP A 207  VAL A 208  1  O  VAL A 208   N  LYS A  28           
SHEET    1 AA4 2 PRO A 252  VAL A 253  0                                        
SHEET    2 AA4 2 TRP A 259  VAL A 260 -1  O  TRP A 259   N  VAL A 253           
SHEET    1 AA5 9 ALA B 354  VAL B 358  0                                        
SHEET    2 AA5 9 THR B   5  ASN B   9  1  N  VAL B   6   O  ALA B 354           
SHEET    3 AA5 9 MET B 235  HIS B 247 -1  O  THR B 238   N  THR B   5           
SHEET    4 AA5 9 PRO B 321  TRP B 325 -1  O  LEU B 324   N  LEU B 237           
SHEET    5 AA5 9 PRO B 287  VAL B 290 -1  N  LEU B 289   O  ILE B 323           
SHEET    6 AA5 9 ARG B 293  VAL B 298 -1  O  VAL B 295   N  VAL B 288           
SHEET    7 AA5 9 ILE B 306  ASP B 309 -1  O  CYS B 307   N  VAL B 298           
SHEET    8 AA5 9 THR B 265  VAL B 270 -1  N  VAL B 270   O  ILE B 306           
SHEET    9 AA5 9 MET B 235  HIS B 247 -1  N  ARG B 245   O  LEU B 267           
SHEET    1 AA6 8 ARG B 189  SER B 190  0                                        
SHEET    2 AA6 8 ASN B 155  VAL B 157  1  N  ILE B 156   O  SER B 190           
SHEET    3 AA6 8 VAL B 119  LYS B 122  1  N  MET B 121   O  ASN B 155           
SHEET    4 AA6 8 PHE B  95  VAL B  99  1  N  VAL B  99   O  LYS B 122           
SHEET    5 AA6 8 VAL B  75  LEU B  77  1  N  LEU B  77   O  HIS B  96           
SHEET    6 AA6 8 ALA B  54  VAL B  57  1  N  PHE B  55   O  LEU B  76           
SHEET    7 AA6 8 LYS B  28  VAL B  32  1  N  ALA B  31   O  GLY B  56           
SHEET    8 AA6 8 TRP B 207  VAL B 208  1  O  VAL B 208   N  VAL B  30           
SHEET    1 AA7 2 PRO B 252  VAL B 253  0                                        
SHEET    2 AA7 2 TRP B 259  VAL B 260 -1  O  TRP B 259   N  VAL B 253           
SHEET    1 AA8 6 ARG C 293  PRO C 296  0                                        
SHEET    2 AA8 6 PRO C 287  VAL C 290 -1  N  VAL C 290   O  ARG C 293           
SHEET    3 AA8 6 PRO C 321  TRP C 325 -1  O  ILE C 323   N  LEU C 289           
SHEET    4 AA8 6 MET C 235  HIS C 247 -1  N  SER C 239   O  VAL C 322           
SHEET    5 AA8 6 THR C 265  VAL C 270 -1  O  LEU C 267   N  ARG C 245           
SHEET    6 AA8 6 ILE C 306  ASP C 309 -1  O  ILE C 306   N  VAL C 270           
SHEET    1 AA9 6 ARG C 293  PRO C 296  0                                        
SHEET    2 AA9 6 PRO C 287  VAL C 290 -1  N  VAL C 290   O  ARG C 293           
SHEET    3 AA9 6 PRO C 321  TRP C 325 -1  O  ILE C 323   N  LEU C 289           
SHEET    4 AA9 6 MET C 235  HIS C 247 -1  N  SER C 239   O  VAL C 322           
SHEET    5 AA9 6 THR C   5  ASN C   9 -1  N  VAL C   7   O  SER C 236           
SHEET    6 AA9 6 ALA C 354  VAL C 358  1  O  ALA C 354   N  VAL C   6           
SHEET    1 AB1 8 ARG C 189  SER C 190  0                                        
SHEET    2 AB1 8 VAL C 150  VAL C 157  1  N  ILE C 156   O  SER C 190           
SHEET    3 AB1 8 VAL C 117  LYS C 122  1  N  MET C 121   O  ASN C 155           
SHEET    4 AB1 8 HIS C  96  VAL C  99  1  N  THR C  97   O  TRP C 120           
SHEET    5 AB1 8 VAL C  75  LEU C  77  1  N  LEU C  77   O  HIS C  96           
SHEET    6 AB1 8 ALA C  54  VAL C  57  1  N  PHE C  55   O  LEU C  76           
SHEET    7 AB1 8 LYS C  28  VAL C  32  1  N  ALA C  31   O  ALA C  54           
SHEET    8 AB1 8 TRP C 207  VAL C 208  1  O  VAL C 208   N  LYS C  28           
SHEET    1 AB2 2 PRO C 252  VAL C 253  0                                        
SHEET    2 AB2 2 TRP C 259  VAL C 260 -1  O  TRP C 259   N  VAL C 253           
SHEET    1 AB3 6 ARG D 293  PRO D 296  0                                        
SHEET    2 AB3 6 PRO D 287  VAL D 290 -1  N  VAL D 290   O  ARG D 293           
SHEET    3 AB3 6 PRO D 321  TRP D 325 -1  O  ILE D 323   N  LEU D 289           
SHEET    4 AB3 6 MET D 235  HIS D 247 -1  N  LEU D 237   O  LEU D 324           
SHEET    5 AB3 6 THR D 265  VAL D 270 -1  O  VAL D 269   N  ILE D 242           
SHEET    6 AB3 6 ILE D 306  ASP D 309 -1  O  ILE D 306   N  VAL D 270           
SHEET    1 AB4 6 ARG D 293  PRO D 296  0                                        
SHEET    2 AB4 6 PRO D 287  VAL D 290 -1  N  VAL D 290   O  ARG D 293           
SHEET    3 AB4 6 PRO D 321  TRP D 325 -1  O  ILE D 323   N  LEU D 289           
SHEET    4 AB4 6 MET D 235  HIS D 247 -1  N  LEU D 237   O  LEU D 324           
SHEET    5 AB4 6 THR D   5  ASN D   9 -1  N  THR D   5   O  THR D 238           
SHEET    6 AB4 6 ALA D 354  VAL D 358  1  O  LYS D 356   N  ILE D   8           
SHEET    1 AB5 8 ARG D 189  SER D 190  0                                        
SHEET    2 AB5 8 ASN D 155  VAL D 157  1  N  ILE D 156   O  SER D 190           
SHEET    3 AB5 8 VAL D 119  LYS D 122  1  N  MET D 121   O  ASN D 155           
SHEET    4 AB5 8 PHE D  95  VAL D  99  1  N  THR D  97   O  TRP D 120           
SHEET    5 AB5 8 VAL D  75  LEU D  77  1  N  LEU D  77   O  HIS D  96           
SHEET    6 AB5 8 ALA D  54  VAL D  57  1  N  PHE D  55   O  LEU D  76           
SHEET    7 AB5 8 LYS D  28  VAL D  32  1  N  ALA D  31   O  ALA D  54           
SHEET    8 AB5 8 TRP D 207  VAL D 208  1  O  VAL D 208   N  LYS D  28           
SHEET    1 AB6 2 PRO D 252  VAL D 253  0                                        
SHEET    2 AB6 2 TRP D 259  VAL D 260 -1  O  TRP D 259   N  VAL D 253           
LINK         NZ  LYS A  34                 C4A PLP A1001     1555   1555  1.32  
LINK         NZ  LYS B  34                 C4A PLP B1001     1555   1555  1.30  
LINK         NZ  LYS C  34                 C4A PLP C1001     1555   1555  1.28  
LINK         NZ  LYS D  34                 C4A PLP D1001     1555   1555  1.29  
CISPEP   1 GLN A  152    PRO A  153          0         1.12                     
CISPEP   2 GLN B  152    PRO B  153          0        -4.18                     
CISPEP   3 GLN C  152    PRO C  153          0         1.63                     
CISPEP   4 GLN D  152    PRO D  153          0         3.94                     
SITE     1 AC1 11 TYR A  38  HIS A 159  ALA A 193  SER A 194                    
SITE     2 AC1 11 ARG A 209  GLY A 211  ILE A 212  TYR A 343                    
SITE     3 AC1 11 HOH A1161  HOH A1210  GOL B1004                               
SITE     1 AC2  3 ARG A 129  LEU A 130  HIS A 159                               
SITE     1 AC3  2 ARG A 266  ARG B  19                                          
SITE     1 AC4  5 TYR A 255  ALA A 302  MET A 303  ASP A 304                    
SITE     2 AC4  5 ARG B 129                                                     
SITE     1 AC5 11 TYR B  38  HIS B 159  ALA B 193  SER B 194                    
SITE     2 AC5 11 ARG B 209  GLY B 211  ILE B 212  TYR B 343                    
SITE     3 AC5 11 HOH B1164  HOH B1222  HOH B1239                               
SITE     1 AC6  4 ARG B 129  LEU B 130  HIS B 159  HOH B1251                    
SITE     1 AC7  4 ARG A  19  ARG B 266  HOH B1244  HOH B1262                    
SITE     1 AC8  7 ARG A 129  PLP A1001  TYR B 255  ALA B 302                    
SITE     2 AC8  7 MET B 303  ASP B 304  MET B 305                               
SITE     1 AC9  9 TYR C  38  ALA C 193  SER C 194  ARG C 209                    
SITE     2 AC9  9 GLY C 211  ILE C 212  TYR C 343  HOH C1105                    
SITE     3 AC9  9 GOL D1002                                                     
SITE     1 AD1  2 ARG C  19  ARG D 266                                          
SITE     1 AD2  7 TYR D  38  ALA D 193  SER D 194  ARG D 209                    
SITE     2 AD2  7 GLY D 211  ILE D 212  TYR D 343                               
SITE     1 AD3  7 ARG C 129  PLP C1001  TYR D 255  ALA D 302                    
SITE     2 AD3  7 MET D 303  ASP D 304  MET D 305                               
CRYST1  148.079  148.079  163.689  90.00  90.00 120.00 P 6          24          
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      0.006753  0.003899  0.000000        0.00000                         
SCALE2      0.000000  0.007798  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006109        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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