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Database: PDB
Entry: 3HBX
LinkDB: 3HBX
Original site: 3HBX 
HEADER    LYASE                                   05-MAY-09   3HBX              
TITLE     CRYSTAL STRUCTURE OF GAD1 FROM ARABIDOPSIS THALIANA                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE DECARBOXYLASE 1;                                 
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: GAD 1;                                                      
COMPND   5 EC: 4.1.1.15;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;                        
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: AT5G17330, GAD, GAD1, GDH1, MKP11.30, MKP11_18;                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET12B                                    
KEYWDS    CALMODULIN-BINDING, DECARBOXYLASE, LYASE, PYRIDOXAL                   
KEYWDS   2 PHOSPHATE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.GUT,P.DOMINICI,S.PILATI,M.G.GRUETTER,G.CAPITANI                     
REVDAT   3   08-DEC-09 3HBX    1       MTRIX1 MTRIX2 MTRIX3                     
REVDAT   2   15-SEP-09 3HBX    1       JRNL                                     
REVDAT   1   28-JUL-09 3HBX    0                                                
JRNL        AUTH   H.GUT,P.DOMINICI,S.PILATI,A.ASTEGNO,M.V.PETOUKHOV,           
JRNL        AUTH 2 D.I.SVERGUN,M.G.GRUTTER,G.CAPITANI                           
JRNL        TITL   A COMMON STRUCTURAL BASIS FOR PH- AND                        
JRNL        TITL 2 CALMODULIN-MEDIATED REGULATION IN PLANT GLUTAMATE            
JRNL        TITL 3 DECARBOXYLASE.                                               
JRNL        REF    J.MOL.BIOL.                   V. 392   334 2009              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   19580813                                                     
JRNL        DOI    10.1016/J.JMB.2009.06.080                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.67 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.4_29)                       
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.67                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.09                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.510                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 85127                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.610                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2223                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.0927 -  6.7077    0.91     4897   139  0.1612 0.1714        
REMARK   3     2  6.7077 -  5.3348    0.94     5062   148  0.1810 0.2145        
REMARK   3     3  5.3348 -  4.6636    0.94     5014   166  0.1674 0.1719        
REMARK   3     4  4.6636 -  4.2386    0.95     5057   150  0.1643 0.1775        
REMARK   3     5  4.2386 -  3.9356    0.96     5158   167  0.1777 0.1781        
REMARK   3     6  3.9356 -  3.7040    0.97     5190   133  0.1794 0.2026        
REMARK   3     7  3.7040 -  3.5188    0.97     5262   168  0.1993 0.2307        
REMARK   3     8  3.5188 -  3.3659    0.98     5253   130  0.2078 0.2269        
REMARK   3     9  3.3659 -  3.2365    0.98     5338   150  0.2226 0.2406        
REMARK   3    10  3.2365 -  3.1250    0.98     5246   178  0.2415 0.2577        
REMARK   3    11  3.1250 -  3.0273    0.98     5278   144  0.2540 0.2659        
REMARK   3    12  3.0273 -  2.9409    0.99     5346   117  0.2655 0.3089        
REMARK   3    13  2.9409 -  2.8635    0.98     5350   113  0.2756 0.2683        
REMARK   3    14  2.8635 -  2.7937    0.98     5333    97  0.2785 0.3089        
REMARK   3    15  2.7937 -  2.7303    0.97     5189   126  0.2870 0.3461        
REMARK   3    16  2.7303 -  2.6720    0.91     4931    97  0.3029 0.3526        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 28.07                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.160           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.54800                                             
REMARK   3    B22 (A**2) : -8.54800                                             
REMARK   3    B33 (A**2) : 17.09700                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002          21624                                  
REMARK   3   ANGLE     :  0.606          29356                                  
REMARK   3   CHIRALITY :  0.043           3240                                  
REMARK   3   PLANARITY :  0.002           3788                                  
REMARK   3   DIHEDRAL  : 14.335           7978                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and backbone and resseq 300:314     
REMARK   3     SELECTION          : chain B and backbone and resseq 300:314     
REMARK   3     ATOM PAIRS NUMBER  : 60                                          
REMARK   3     RMSD               : 0.019                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: chain A and backbone and resseq 300:314     
REMARK   3     SELECTION          : chain C and backbone and resseq 300:314     
REMARK   3     ATOM PAIRS NUMBER  : 60                                          
REMARK   3     RMSD               : 0.015                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: chain A and backbone and resseq 300:314     
REMARK   3     SELECTION          : chain D and backbone and resseq 300:314     
REMARK   3     ATOM PAIRS NUMBER  : 60                                          
REMARK   3     RMSD               : 0.012                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: chain A and backbone and resseq 300:314     
REMARK   3     SELECTION          : chain E and backbone and resseq 300:314     
REMARK   3     ATOM PAIRS NUMBER  : 60                                          
REMARK   3     RMSD               : 0.012                                       
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: chain A and backbone and resseq 300:314     
REMARK   3     SELECTION          : chain F and backbone and resseq 300:314     
REMARK   3     ATOM PAIRS NUMBER  : 60                                          
REMARK   3     RMSD               : 0.017                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 12:111 or resseq        
REMARK   3                          117:148 or resseq 150:255 or resseq         
REMARK   3                          260:276 or resseq 278:299 or resseq         
REMARK   3                          315:404 or resseq 415:447 )                 
REMARK   3     SELECTION          : chain B and (resseq 12:111 or resseq        
REMARK   3                          117:148 or resseq 150:255 or resseq         
REMARK   3                          260:276 or resseq 278:299 or resseq         
REMARK   3                          315:404 or resseq 415:447 )                 
REMARK   3     ATOM PAIRS NUMBER  : 3202                                        
REMARK   3     RMSD               : 0.009                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 12:111 or resseq        
REMARK   3                          117:148 or resseq 150:255 or resseq         
REMARK   3                          260:276 or resseq 278:299 or resseq         
REMARK   3                          315:404 or resseq 415:447 )                 
REMARK   3     SELECTION          : chain C and (resseq 12:111 or resseq        
REMARK   3                          117:148 or resseq 150:255 or resseq         
REMARK   3                          260:276 or resseq 278:299 or resseq         
REMARK   3                          315:404 or resseq 415:447 )                 
REMARK   3     ATOM PAIRS NUMBER  : 3202                                        
REMARK   3     RMSD               : 0.008                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 12:111 or resseq        
REMARK   3                          117:148 or resseq 150:255 or resseq         
REMARK   3                          260:276 or resseq 278:299 or resseq         
REMARK   3                          315:404 or resseq 415:447 )                 
REMARK   3     SELECTION          : chain D and (resseq 12:111 or resseq        
REMARK   3                          117:148 or resseq 150:255 or resseq         
REMARK   3                          260:276 or resseq 278:299 or resseq         
REMARK   3                          315:404 or resseq 415:447 )                 
REMARK   3     ATOM PAIRS NUMBER  : 3202                                        
REMARK   3     RMSD               : 0.008                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 12:111 or resseq        
REMARK   3                          117:148 or resseq 150:255 or resseq         
REMARK   3                          260:276 or resseq 278:299 or resseq         
REMARK   3                          315:404 or resseq 415:447 )                 
REMARK   3     SELECTION          : chain E and (resseq 12:111 or resseq        
REMARK   3                          117:148 or resseq 150:255 or resseq         
REMARK   3                          260:276 or resseq 278:299 or resseq         
REMARK   3                          315:404 or resseq 415:447 )                 
REMARK   3     ATOM PAIRS NUMBER  : 3202                                        
REMARK   3     RMSD               : 0.007                                       
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 12:111 or resseq        
REMARK   3                          117:148 or resseq 150:255 or resseq         
REMARK   3                          260:276 or resseq 278:299 or resseq         
REMARK   3                          315:404 or resseq 415:447 )                 
REMARK   3     SELECTION          : chain F and (resseq 12:111 or resseq        
REMARK   3                          117:148 or resseq 150:255 or resseq         
REMARK   3                          260:276 or resseq 278:299 or resseq         
REMARK   3                          315:404 or resseq 415:447 )                 
REMARK   3     ATOM PAIRS NUMBER  : 3202                                        
REMARK   3     RMSD               : 0.009                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3HBX COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052945.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-FEB-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.90002                            
REMARK 200  MONOCHROMATOR                  : LN2 COOLED FIXED-EXIT SI(111)      
REMARK 200  OPTICS                         : DYNAMICALLY BENDABLE MIRROR        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 85232                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.45900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1PMM (E. COLI GADB)                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 UL PROTEIN SOLUTION (1.9 MG/ML         
REMARK 280  GAD1, 50 MM HEPES PH 7.2, 150 MM NACL AND 10 UM PLP) + 1 UL         
REMARK 280  RESERVOIR SOLUTION (100 MM NA ACETATE PH 5.5, 720 MM NA             
REMARK 280  FORMATE, 9 % PEG 8000 AND 9 % PEG 1000), VAPOR DIFFUSION,           
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290                                                                      
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      133.71733            
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       66.85867            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     ASP A    11                                                      
REMARK 465     SER A   449                                                      
REMARK 465     ARG A   450                                                      
REMARK 465     VAL A   451                                                      
REMARK 465     ILE A   452                                                      
REMARK 465     HIS A   453                                                      
REMARK 465     LYS A   454                                                      
REMARK 465     ILE A   455                                                      
REMARK 465     SER A   456                                                      
REMARK 465     LEU A   457                                                      
REMARK 465     GLY A   458                                                      
REMARK 465     GLN A   459                                                      
REMARK 465     GLU A   460                                                      
REMARK 465     LYS A   461                                                      
REMARK 465     SER A   462                                                      
REMARK 465     GLU A   463                                                      
REMARK 465     SER A   464                                                      
REMARK 465     ASN A   465                                                      
REMARK 465     SER A   466                                                      
REMARK 465     ASP A   467                                                      
REMARK 465     ASN A   468                                                      
REMARK 465     LEU A   469                                                      
REMARK 465     MET A   470                                                      
REMARK 465     VAL A   471                                                      
REMARK 465     THR A   472                                                      
REMARK 465     VAL A   473                                                      
REMARK 465     LYS A   474                                                      
REMARK 465     LYS A   475                                                      
REMARK 465     SER A   476                                                      
REMARK 465     ASP A   477                                                      
REMARK 465     ILE A   478                                                      
REMARK 465     ASP A   479                                                      
REMARK 465     LYS A   480                                                      
REMARK 465     GLN A   481                                                      
REMARK 465     ARG A   482                                                      
REMARK 465     ASP A   483                                                      
REMARK 465     ILE A   484                                                      
REMARK 465     ILE A   485                                                      
REMARK 465     THR A   486                                                      
REMARK 465     GLY A   487                                                      
REMARK 465     TRP A   488                                                      
REMARK 465     LYS A   489                                                      
REMARK 465     LYS A   490                                                      
REMARK 465     PHE A   491                                                      
REMARK 465     VAL A   492                                                      
REMARK 465     ALA A   493                                                      
REMARK 465     ASP A   494                                                      
REMARK 465     ARG A   495                                                      
REMARK 465     LYS A   496                                                      
REMARK 465     LYS A   497                                                      
REMARK 465     THR A   498                                                      
REMARK 465     SER A   499                                                      
REMARK 465     GLY A   500                                                      
REMARK 465     ILE A   501                                                      
REMARK 465     CYS A   502                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     VAL B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     ASP B    11                                                      
REMARK 465     SER B   449                                                      
REMARK 465     ARG B   450                                                      
REMARK 465     VAL B   451                                                      
REMARK 465     ILE B   452                                                      
REMARK 465     HIS B   453                                                      
REMARK 465     LYS B   454                                                      
REMARK 465     ILE B   455                                                      
REMARK 465     SER B   456                                                      
REMARK 465     LEU B   457                                                      
REMARK 465     GLY B   458                                                      
REMARK 465     GLN B   459                                                      
REMARK 465     GLU B   460                                                      
REMARK 465     LYS B   461                                                      
REMARK 465     SER B   462                                                      
REMARK 465     GLU B   463                                                      
REMARK 465     SER B   464                                                      
REMARK 465     ASN B   465                                                      
REMARK 465     SER B   466                                                      
REMARK 465     ASP B   467                                                      
REMARK 465     ASN B   468                                                      
REMARK 465     LEU B   469                                                      
REMARK 465     MET B   470                                                      
REMARK 465     VAL B   471                                                      
REMARK 465     THR B   472                                                      
REMARK 465     VAL B   473                                                      
REMARK 465     LYS B   474                                                      
REMARK 465     LYS B   475                                                      
REMARK 465     SER B   476                                                      
REMARK 465     ASP B   477                                                      
REMARK 465     ILE B   478                                                      
REMARK 465     ASP B   479                                                      
REMARK 465     LYS B   480                                                      
REMARK 465     GLN B   481                                                      
REMARK 465     ARG B   482                                                      
REMARK 465     ASP B   483                                                      
REMARK 465     ILE B   484                                                      
REMARK 465     ILE B   485                                                      
REMARK 465     THR B   486                                                      
REMARK 465     GLY B   487                                                      
REMARK 465     TRP B   488                                                      
REMARK 465     LYS B   489                                                      
REMARK 465     LYS B   490                                                      
REMARK 465     PHE B   491                                                      
REMARK 465     VAL B   492                                                      
REMARK 465     ALA B   493                                                      
REMARK 465     ASP B   494                                                      
REMARK 465     ARG B   495                                                      
REMARK 465     LYS B   496                                                      
REMARK 465     LYS B   497                                                      
REMARK 465     THR B   498                                                      
REMARK 465     SER B   499                                                      
REMARK 465     GLY B   500                                                      
REMARK 465     ILE B   501                                                      
REMARK 465     CYS B   502                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     VAL C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     GLU C     9                                                      
REMARK 465     SER C    10                                                      
REMARK 465     ASP C    11                                                      
REMARK 465     SER C   449                                                      
REMARK 465     ARG C   450                                                      
REMARK 465     VAL C   451                                                      
REMARK 465     ILE C   452                                                      
REMARK 465     HIS C   453                                                      
REMARK 465     LYS C   454                                                      
REMARK 465     ILE C   455                                                      
REMARK 465     SER C   456                                                      
REMARK 465     LEU C   457                                                      
REMARK 465     GLY C   458                                                      
REMARK 465     GLN C   459                                                      
REMARK 465     GLU C   460                                                      
REMARK 465     LYS C   461                                                      
REMARK 465     SER C   462                                                      
REMARK 465     GLU C   463                                                      
REMARK 465     SER C   464                                                      
REMARK 465     ASN C   465                                                      
REMARK 465     SER C   466                                                      
REMARK 465     ASP C   467                                                      
REMARK 465     ASN C   468                                                      
REMARK 465     LEU C   469                                                      
REMARK 465     MET C   470                                                      
REMARK 465     VAL C   471                                                      
REMARK 465     THR C   472                                                      
REMARK 465     VAL C   473                                                      
REMARK 465     LYS C   474                                                      
REMARK 465     LYS C   475                                                      
REMARK 465     SER C   476                                                      
REMARK 465     ASP C   477                                                      
REMARK 465     ILE C   478                                                      
REMARK 465     ASP C   479                                                      
REMARK 465     LYS C   480                                                      
REMARK 465     GLN C   481                                                      
REMARK 465     ARG C   482                                                      
REMARK 465     ASP C   483                                                      
REMARK 465     ILE C   484                                                      
REMARK 465     ILE C   485                                                      
REMARK 465     THR C   486                                                      
REMARK 465     GLY C   487                                                      
REMARK 465     TRP C   488                                                      
REMARK 465     LYS C   489                                                      
REMARK 465     LYS C   490                                                      
REMARK 465     PHE C   491                                                      
REMARK 465     VAL C   492                                                      
REMARK 465     ALA C   493                                                      
REMARK 465     ASP C   494                                                      
REMARK 465     ARG C   495                                                      
REMARK 465     LYS C   496                                                      
REMARK 465     LYS C   497                                                      
REMARK 465     THR C   498                                                      
REMARK 465     SER C   499                                                      
REMARK 465     GLY C   500                                                      
REMARK 465     ILE C   501                                                      
REMARK 465     CYS C   502                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     ALA D     6                                                      
REMARK 465     VAL D     7                                                      
REMARK 465     SER D     8                                                      
REMARK 465     GLU D     9                                                      
REMARK 465     SER D    10                                                      
REMARK 465     ASP D    11                                                      
REMARK 465     PRO D   448                                                      
REMARK 465     SER D   449                                                      
REMARK 465     ARG D   450                                                      
REMARK 465     VAL D   451                                                      
REMARK 465     ILE D   452                                                      
REMARK 465     HIS D   453                                                      
REMARK 465     LYS D   454                                                      
REMARK 465     ILE D   455                                                      
REMARK 465     SER D   456                                                      
REMARK 465     LEU D   457                                                      
REMARK 465     GLY D   458                                                      
REMARK 465     GLN D   459                                                      
REMARK 465     GLU D   460                                                      
REMARK 465     LYS D   461                                                      
REMARK 465     SER D   462                                                      
REMARK 465     GLU D   463                                                      
REMARK 465     SER D   464                                                      
REMARK 465     ASN D   465                                                      
REMARK 465     SER D   466                                                      
REMARK 465     ASP D   467                                                      
REMARK 465     ASN D   468                                                      
REMARK 465     LEU D   469                                                      
REMARK 465     MET D   470                                                      
REMARK 465     VAL D   471                                                      
REMARK 465     THR D   472                                                      
REMARK 465     VAL D   473                                                      
REMARK 465     LYS D   474                                                      
REMARK 465     LYS D   475                                                      
REMARK 465     SER D   476                                                      
REMARK 465     ASP D   477                                                      
REMARK 465     ILE D   478                                                      
REMARK 465     ASP D   479                                                      
REMARK 465     LYS D   480                                                      
REMARK 465     GLN D   481                                                      
REMARK 465     ARG D   482                                                      
REMARK 465     ASP D   483                                                      
REMARK 465     ILE D   484                                                      
REMARK 465     ILE D   485                                                      
REMARK 465     THR D   486                                                      
REMARK 465     GLY D   487                                                      
REMARK 465     TRP D   488                                                      
REMARK 465     LYS D   489                                                      
REMARK 465     LYS D   490                                                      
REMARK 465     PHE D   491                                                      
REMARK 465     VAL D   492                                                      
REMARK 465     ALA D   493                                                      
REMARK 465     ASP D   494                                                      
REMARK 465     ARG D   495                                                      
REMARK 465     LYS D   496                                                      
REMARK 465     LYS D   497                                                      
REMARK 465     THR D   498                                                      
REMARK 465     SER D   499                                                      
REMARK 465     GLY D   500                                                      
REMARK 465     ILE D   501                                                      
REMARK 465     CYS D   502                                                      
REMARK 465     MET E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     LEU E     3                                                      
REMARK 465     SER E     4                                                      
REMARK 465     HIS E     5                                                      
REMARK 465     ALA E     6                                                      
REMARK 465     VAL E     7                                                      
REMARK 465     SER E     8                                                      
REMARK 465     GLU E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     ASP E    11                                                      
REMARK 465     PRO E   448                                                      
REMARK 465     SER E   449                                                      
REMARK 465     ARG E   450                                                      
REMARK 465     VAL E   451                                                      
REMARK 465     ILE E   452                                                      
REMARK 465     HIS E   453                                                      
REMARK 465     LYS E   454                                                      
REMARK 465     ILE E   455                                                      
REMARK 465     SER E   456                                                      
REMARK 465     LEU E   457                                                      
REMARK 465     GLY E   458                                                      
REMARK 465     GLN E   459                                                      
REMARK 465     GLU E   460                                                      
REMARK 465     LYS E   461                                                      
REMARK 465     SER E   462                                                      
REMARK 465     GLU E   463                                                      
REMARK 465     SER E   464                                                      
REMARK 465     ASN E   465                                                      
REMARK 465     SER E   466                                                      
REMARK 465     ASP E   467                                                      
REMARK 465     ASN E   468                                                      
REMARK 465     LEU E   469                                                      
REMARK 465     MET E   470                                                      
REMARK 465     VAL E   471                                                      
REMARK 465     THR E   472                                                      
REMARK 465     VAL E   473                                                      
REMARK 465     LYS E   474                                                      
REMARK 465     LYS E   475                                                      
REMARK 465     SER E   476                                                      
REMARK 465     ASP E   477                                                      
REMARK 465     ILE E   478                                                      
REMARK 465     ASP E   479                                                      
REMARK 465     LYS E   480                                                      
REMARK 465     GLN E   481                                                      
REMARK 465     ARG E   482                                                      
REMARK 465     ASP E   483                                                      
REMARK 465     ILE E   484                                                      
REMARK 465     ILE E   485                                                      
REMARK 465     THR E   486                                                      
REMARK 465     GLY E   487                                                      
REMARK 465     TRP E   488                                                      
REMARK 465     LYS E   489                                                      
REMARK 465     LYS E   490                                                      
REMARK 465     PHE E   491                                                      
REMARK 465     VAL E   492                                                      
REMARK 465     ALA E   493                                                      
REMARK 465     ASP E   494                                                      
REMARK 465     ARG E   495                                                      
REMARK 465     LYS E   496                                                      
REMARK 465     LYS E   497                                                      
REMARK 465     THR E   498                                                      
REMARK 465     SER E   499                                                      
REMARK 465     GLY E   500                                                      
REMARK 465     ILE E   501                                                      
REMARK 465     CYS E   502                                                      
REMARK 465     MET F     1                                                      
REMARK 465     VAL F     2                                                      
REMARK 465     LEU F     3                                                      
REMARK 465     SER F     4                                                      
REMARK 465     HIS F     5                                                      
REMARK 465     ALA F     6                                                      
REMARK 465     VAL F     7                                                      
REMARK 465     SER F     8                                                      
REMARK 465     GLU F     9                                                      
REMARK 465     SER F    10                                                      
REMARK 465     ASP F    11                                                      
REMARK 465     SER F   449                                                      
REMARK 465     ARG F   450                                                      
REMARK 465     VAL F   451                                                      
REMARK 465     ILE F   452                                                      
REMARK 465     HIS F   453                                                      
REMARK 465     LYS F   454                                                      
REMARK 465     ILE F   455                                                      
REMARK 465     SER F   456                                                      
REMARK 465     LEU F   457                                                      
REMARK 465     GLY F   458                                                      
REMARK 465     GLN F   459                                                      
REMARK 465     GLU F   460                                                      
REMARK 465     LYS F   461                                                      
REMARK 465     SER F   462                                                      
REMARK 465     GLU F   463                                                      
REMARK 465     SER F   464                                                      
REMARK 465     ASN F   465                                                      
REMARK 465     SER F   466                                                      
REMARK 465     ASP F   467                                                      
REMARK 465     ASN F   468                                                      
REMARK 465     LEU F   469                                                      
REMARK 465     MET F   470                                                      
REMARK 465     VAL F   471                                                      
REMARK 465     THR F   472                                                      
REMARK 465     VAL F   473                                                      
REMARK 465     LYS F   474                                                      
REMARK 465     LYS F   475                                                      
REMARK 465     SER F   476                                                      
REMARK 465     ASP F   477                                                      
REMARK 465     ILE F   478                                                      
REMARK 465     ASP F   479                                                      
REMARK 465     LYS F   480                                                      
REMARK 465     GLN F   481                                                      
REMARK 465     ARG F   482                                                      
REMARK 465     ASP F   483                                                      
REMARK 465     ILE F   484                                                      
REMARK 465     ILE F   485                                                      
REMARK 465     THR F   486                                                      
REMARK 465     GLY F   487                                                      
REMARK 465     TRP F   488                                                      
REMARK 465     LYS F   489                                                      
REMARK 465     LYS F   490                                                      
REMARK 465     PHE F   491                                                      
REMARK 465     VAL F   492                                                      
REMARK 465     ALA F   493                                                      
REMARK 465     ASP F   494                                                      
REMARK 465     ARG F   495                                                      
REMARK 465     LYS F   496                                                      
REMARK 465     LYS F   497                                                      
REMARK 465     THR F   498                                                      
REMARK 465     SER F   499                                                      
REMARK 465     GLY F   500                                                      
REMARK 465     ILE F   501                                                      
REMARK 465     CYS F   502                                                      
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    PHE A  30      -53.52   -122.22                                   
REMARK 500    PRO A 111       86.87    -69.72                                   
REMARK 500    GLU A 113     -159.55    -74.57                                   
REMARK 500    ASN A 215       14.69   -148.56                                   
REMARK 500    ASP A 238       58.00   -107.52                                   
REMARK 500    ILE A 251      -51.04   -120.09                                   
REMARK 500    TRP A 261      -15.10   -141.01                                   
REMARK 500    ASP A 262     -146.70    -99.94                                   
REMARK 500    ASN A 305       22.09   -152.54                                   
REMARK 500    PHE A 318      -95.16   -125.05                                   
REMARK 500    PRO A 374       87.37    -63.14                                   
REMARK 500    ASP A 382       81.19     67.03                                   
REMARK 500    SER A 383       42.98    -83.58                                   
REMARK 500    SER A 384      -78.18    -79.60                                   
REMARK 500    ASN A 410       56.98    -95.48                                   
REMARK 500    GLN A 412        0.85    -67.31                                   
REMARK 500    PHE B  30      -53.45   -121.62                                   
REMARK 500    ASN B 215       15.19   -148.61                                   
REMARK 500    ASP B 238       57.99   -106.97                                   
REMARK 500    ALA B 245       40.34   -104.62                                   
REMARK 500    TRP B 261      -15.45   -140.96                                   
REMARK 500    ASP B 262     -146.55    -99.74                                   
REMARK 500    ASN B 305       15.51   -150.97                                   
REMARK 500    PHE B 318      -94.94   -125.08                                   
REMARK 500    PRO B 374       87.09    -63.30                                   
REMARK 500    ASP B 382       81.40     67.20                                   
REMARK 500    SER B 383       42.86    -83.69                                   
REMARK 500    SER B 384      -78.19    -79.57                                   
REMARK 500    ASN B 410       59.07   -103.10                                   
REMARK 500    PHE C  30      -53.73   -122.01                                   
REMARK 500    PRO C 111       84.87    -69.66                                   
REMARK 500    GLU C 113       55.80    -98.98                                   
REMARK 500    GLU C 114      -72.04     68.59                                   
REMARK 500    ASN C 215       14.86   -148.49                                   
REMARK 500    ASP C 238       57.74   -107.63                                   
REMARK 500    TRP C 261      -15.53   -141.31                                   
REMARK 500    ASP C 262     -146.83    -99.99                                   
REMARK 500    ASN C 305       26.82   -153.67                                   
REMARK 500    PHE C 318      -95.05   -125.67                                   
REMARK 500    PRO C 374       87.53    -63.39                                   
REMARK 500    ASP C 382       81.34     66.97                                   
REMARK 500    SER C 383       42.97    -83.61                                   
REMARK 500    SER C 384      -78.36    -79.67                                   
REMARK 500    ALA C 411       30.76   -158.23                                   
REMARK 500    PHE D  30      -53.37   -122.24                                   
REMARK 500    GLU D 113       46.49   -100.16                                   
REMARK 500    GLU D 114      -55.24     72.98                                   
REMARK 500    ASN D 215       15.10   -148.51                                   
REMARK 500    ASP D 238       58.28   -107.34                                   
REMARK 500    TRP D 261      -15.11   -141.23                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      84 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3HBX A    1   502  UNP    Q42521   DCE1_ARATH      12    513             
DBREF  3HBX B    1   502  UNP    Q42521   DCE1_ARATH      12    513             
DBREF  3HBX C    1   502  UNP    Q42521   DCE1_ARATH      12    513             
DBREF  3HBX D    1   502  UNP    Q42521   DCE1_ARATH      12    513             
DBREF  3HBX E    1   502  UNP    Q42521   DCE1_ARATH      12    513             
DBREF  3HBX F    1   502  UNP    Q42521   DCE1_ARATH      12    513             
SEQRES   1 A  502  MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER          
SEQRES   2 A  502  VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER          
SEQRES   3 A  502  LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS          
SEQRES   4 A  502  GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU          
SEQRES   5 A  502  ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR          
SEQRES   6 A  502  THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER          
SEQRES   7 A  502  SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO          
SEQRES   8 A  502  VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE          
SEQRES   9 A  502  ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR          
SEQRES  10 A  502  ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE          
SEQRES  11 A  502  MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN          
SEQRES  12 A  502  LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN          
SEQRES  13 A  502  ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS          
SEQRES  14 A  502  PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS          
SEQRES  15 A  502  LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA          
SEQRES  16 A  502  VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA          
SEQRES  17 A  502  ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL          
SEQRES  18 A  502  LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU          
SEQRES  19 A  502  THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER          
SEQRES  20 A  502  GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU          
SEQRES  21 A  502  TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL          
SEQRES  22 A  502  SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY          
SEQRES  23 A  502  TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU          
SEQRES  24 A  502  LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO          
SEQRES  25 A  502  THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL          
SEQRES  26 A  502  ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU          
SEQRES  27 A  502  GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET          
SEQRES  28 A  502  ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE          
SEQRES  29 A  502  ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA          
SEQRES  30 A  502  PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU          
SEQRES  31 A  502  ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO          
SEQRES  32 A  502  ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL          
SEQRES  33 A  502  LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU          
SEQRES  34 A  502  ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG          
SEQRES  35 A  502  GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE          
SEQRES  36 A  502  SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN          
SEQRES  37 A  502  LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN          
SEQRES  38 A  502  ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP          
SEQRES  39 A  502  ARG LYS LYS THR SER GLY ILE CYS                              
SEQRES   1 B  502  MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER          
SEQRES   2 B  502  VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER          
SEQRES   3 B  502  LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS          
SEQRES   4 B  502  GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU          
SEQRES   5 B  502  ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR          
SEQRES   6 B  502  THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER          
SEQRES   7 B  502  SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO          
SEQRES   8 B  502  VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE          
SEQRES   9 B  502  ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR          
SEQRES  10 B  502  ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE          
SEQRES  11 B  502  MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN          
SEQRES  12 B  502  LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN          
SEQRES  13 B  502  ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS          
SEQRES  14 B  502  PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS          
SEQRES  15 B  502  LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA          
SEQRES  16 B  502  VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA          
SEQRES  17 B  502  ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL          
SEQRES  18 B  502  LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU          
SEQRES  19 B  502  THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER          
SEQRES  20 B  502  GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU          
SEQRES  21 B  502  TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL          
SEQRES  22 B  502  SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY          
SEQRES  23 B  502  TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU          
SEQRES  24 B  502  LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO          
SEQRES  25 B  502  THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL          
SEQRES  26 B  502  ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU          
SEQRES  27 B  502  GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET          
SEQRES  28 B  502  ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE          
SEQRES  29 B  502  ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA          
SEQRES  30 B  502  PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU          
SEQRES  31 B  502  ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO          
SEQRES  32 B  502  ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL          
SEQRES  33 B  502  LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU          
SEQRES  34 B  502  ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG          
SEQRES  35 B  502  GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE          
SEQRES  36 B  502  SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN          
SEQRES  37 B  502  LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN          
SEQRES  38 B  502  ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP          
SEQRES  39 B  502  ARG LYS LYS THR SER GLY ILE CYS                              
SEQRES   1 C  502  MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER          
SEQRES   2 C  502  VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER          
SEQRES   3 C  502  LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS          
SEQRES   4 C  502  GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU          
SEQRES   5 C  502  ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR          
SEQRES   6 C  502  THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER          
SEQRES   7 C  502  SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO          
SEQRES   8 C  502  VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE          
SEQRES   9 C  502  ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR          
SEQRES  10 C  502  ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE          
SEQRES  11 C  502  MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN          
SEQRES  12 C  502  LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN          
SEQRES  13 C  502  ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS          
SEQRES  14 C  502  PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS          
SEQRES  15 C  502  LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA          
SEQRES  16 C  502  VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA          
SEQRES  17 C  502  ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL          
SEQRES  18 C  502  LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU          
SEQRES  19 C  502  THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER          
SEQRES  20 C  502  GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU          
SEQRES  21 C  502  TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL          
SEQRES  22 C  502  SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY          
SEQRES  23 C  502  TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU          
SEQRES  24 C  502  LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO          
SEQRES  25 C  502  THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL          
SEQRES  26 C  502  ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU          
SEQRES  27 C  502  GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET          
SEQRES  28 C  502  ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE          
SEQRES  29 C  502  ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA          
SEQRES  30 C  502  PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU          
SEQRES  31 C  502  ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO          
SEQRES  32 C  502  ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL          
SEQRES  33 C  502  LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU          
SEQRES  34 C  502  ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG          
SEQRES  35 C  502  GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE          
SEQRES  36 C  502  SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN          
SEQRES  37 C  502  LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN          
SEQRES  38 C  502  ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP          
SEQRES  39 C  502  ARG LYS LYS THR SER GLY ILE CYS                              
SEQRES   1 D  502  MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER          
SEQRES   2 D  502  VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER          
SEQRES   3 D  502  LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS          
SEQRES   4 D  502  GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU          
SEQRES   5 D  502  ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR          
SEQRES   6 D  502  THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER          
SEQRES   7 D  502  SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO          
SEQRES   8 D  502  VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE          
SEQRES   9 D  502  ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR          
SEQRES  10 D  502  ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE          
SEQRES  11 D  502  MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN          
SEQRES  12 D  502  LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN          
SEQRES  13 D  502  ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS          
SEQRES  14 D  502  PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS          
SEQRES  15 D  502  LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA          
SEQRES  16 D  502  VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA          
SEQRES  17 D  502  ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL          
SEQRES  18 D  502  LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU          
SEQRES  19 D  502  THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER          
SEQRES  20 D  502  GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU          
SEQRES  21 D  502  TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL          
SEQRES  22 D  502  SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY          
SEQRES  23 D  502  TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU          
SEQRES  24 D  502  LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO          
SEQRES  25 D  502  THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL          
SEQRES  26 D  502  ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU          
SEQRES  27 D  502  GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET          
SEQRES  28 D  502  ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE          
SEQRES  29 D  502  ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA          
SEQRES  30 D  502  PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU          
SEQRES  31 D  502  ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO          
SEQRES  32 D  502  ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL          
SEQRES  33 D  502  LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU          
SEQRES  34 D  502  ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG          
SEQRES  35 D  502  GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE          
SEQRES  36 D  502  SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN          
SEQRES  37 D  502  LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN          
SEQRES  38 D  502  ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP          
SEQRES  39 D  502  ARG LYS LYS THR SER GLY ILE CYS                              
SEQRES   1 E  502  MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER          
SEQRES   2 E  502  VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER          
SEQRES   3 E  502  LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS          
SEQRES   4 E  502  GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU          
SEQRES   5 E  502  ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR          
SEQRES   6 E  502  THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER          
SEQRES   7 E  502  SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO          
SEQRES   8 E  502  VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE          
SEQRES   9 E  502  ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR          
SEQRES  10 E  502  ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE          
SEQRES  11 E  502  MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN          
SEQRES  12 E  502  LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN          
SEQRES  13 E  502  ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS          
SEQRES  14 E  502  PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS          
SEQRES  15 E  502  LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA          
SEQRES  16 E  502  VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA          
SEQRES  17 E  502  ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL          
SEQRES  18 E  502  LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU          
SEQRES  19 E  502  THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER          
SEQRES  20 E  502  GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU          
SEQRES  21 E  502  TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL          
SEQRES  22 E  502  SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY          
SEQRES  23 E  502  TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU          
SEQRES  24 E  502  LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO          
SEQRES  25 E  502  THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL          
SEQRES  26 E  502  ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU          
SEQRES  27 E  502  GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET          
SEQRES  28 E  502  ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE          
SEQRES  29 E  502  ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA          
SEQRES  30 E  502  PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU          
SEQRES  31 E  502  ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO          
SEQRES  32 E  502  ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL          
SEQRES  33 E  502  LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU          
SEQRES  34 E  502  ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG          
SEQRES  35 E  502  GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE          
SEQRES  36 E  502  SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN          
SEQRES  37 E  502  LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN          
SEQRES  38 E  502  ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP          
SEQRES  39 E  502  ARG LYS LYS THR SER GLY ILE CYS                              
SEQRES   1 F  502  MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER          
SEQRES   2 F  502  VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER          
SEQRES   3 F  502  LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS          
SEQRES   4 F  502  GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU          
SEQRES   5 F  502  ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR          
SEQRES   6 F  502  THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER          
SEQRES   7 F  502  SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO          
SEQRES   8 F  502  VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE          
SEQRES   9 F  502  ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR          
SEQRES  10 F  502  ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE          
SEQRES  11 F  502  MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN          
SEQRES  12 F  502  LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN          
SEQRES  13 F  502  ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS          
SEQRES  14 F  502  PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS          
SEQRES  15 F  502  LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA          
SEQRES  16 F  502  VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA          
SEQRES  17 F  502  ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL          
SEQRES  18 F  502  LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU          
SEQRES  19 F  502  THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER          
SEQRES  20 F  502  GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU          
SEQRES  21 F  502  TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL          
SEQRES  22 F  502  SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY          
SEQRES  23 F  502  TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU          
SEQRES  24 F  502  LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO          
SEQRES  25 F  502  THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL          
SEQRES  26 F  502  ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU          
SEQRES  27 F  502  GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET          
SEQRES  28 F  502  ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE          
SEQRES  29 F  502  ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA          
SEQRES  30 F  502  PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU          
SEQRES  31 F  502  ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO          
SEQRES  32 F  502  ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL          
SEQRES  33 F  502  LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU          
SEQRES  34 F  502  ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG          
SEQRES  35 F  502  GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE          
SEQRES  36 F  502  SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN          
SEQRES  37 F  502  LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN          
SEQRES  38 F  502  ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP          
SEQRES  39 F  502  ARG LYS LYS THR SER GLY ILE CYS                              
MODRES 3HBX LLP A  277  LYS                                                     
MODRES 3HBX LLP B  277  LYS                                                     
MODRES 3HBX LLP C  277  LYS                                                     
MODRES 3HBX LLP D  277  LYS                                                     
MODRES 3HBX LLP E  277  LYS                                                     
MODRES 3HBX LLP F  277  LYS                                                     
HET    LLP  A 277      24                                                       
HET    LLP  B 277      24                                                       
HET    LLP  C 277      24                                                       
HET    LLP  D 277      24                                                       
HET    LLP  E 277      24                                                       
HET    LLP  F 277      24                                                       
HETNAM     LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-                
HETNAM   2 LLP  PYRIDIN-4-YLMETHANE)                                            
HETSYN     LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE                             
FORMUL   1  LLP    6(C14 H24 N3 O7 P)                                           
FORMUL   7  HOH   *314(H2 O)                                                    
HELIX    1   1 ARG A   21  THR A   25  5                                   5    
HELIX    2   2 PRO A   38  LEU A   50  1                                  13    
HELIX    3   3 MET A   51  ASP A   53  5                                   3    
HELIX    4   4 ASN A   55  ASN A   59  5                                   5    
HELIX    5   5 GLU A   69  SER A   79  1                                  11    
HELIX    6   6 TYR A   90  PHE A  108  1                                  19    
HELIX    7   7 GLY A  125  GLU A  148  1                                  24    
HELIX    8   8 GLN A  164  PHE A  174  1                                  11    
HELIX    9   9 ASP A  191  VAL A  199  1                                   9    
HELIX   10  10 ASP A  220  GLY A  236  1                                  17    
HELIX   11  11 SER A  247  PHE A  250  5                                   4    
HELIX   12  12 ILE A  251  TYR A  256  1                                   6    
HELIX   13  13 ASN A  292  LEU A  296  5                                   5    
HELIX   14  14 PRO A  297  ILE A  301  5                                   5    
HELIX   15  15 SER A  322  LYS A  360  1                                  39    
HELIX   16  16 THR A  387  ARG A  397  1                                  11    
HELIX   17  17 SER A  426  GLU A  446  1                                  21    
HELIX   18  18 ARG B   21  THR B   25  5                                   5    
HELIX   19  19 PRO B   38  LEU B   50  1                                  13    
HELIX   20  20 MET B   51  ASP B   53  5                                   3    
HELIX   21  21 ASN B   55  ASN B   59  5                                   5    
HELIX   22  22 GLU B   69  SER B   79  1                                  11    
HELIX   23  23 TYR B   90  PHE B  108  1                                  19    
HELIX   24  24 GLY B  125  GLU B  148  1                                  24    
HELIX   25  25 GLN B  164  PHE B  174  1                                  11    
HELIX   26  26 ASP B  191  VAL B  199  1                                   9    
HELIX   27  27 ASP B  220  GLY B  236  1                                  17    
HELIX   28  28 SER B  247  PHE B  250  5                                   4    
HELIX   29  29 ILE B  251  TYR B  256  1                                   6    
HELIX   30  30 ASN B  292  LEU B  296  5                                   5    
HELIX   31  31 PRO B  297  ILE B  301  5                                   5    
HELIX   32  32 SER B  322  LYS B  360  1                                  39    
HELIX   33  33 THR B  387  ARG B  397  1                                  11    
HELIX   34  34 SER B  426  GLU B  446  1                                  21    
HELIX   35  35 ARG C   21  THR C   25  5                                   5    
HELIX   36  36 PRO C   38  LEU C   50  1                                  13    
HELIX   37  37 MET C   51  ASP C   53  5                                   3    
HELIX   38  38 ASN C   55  ASN C   59  5                                   5    
HELIX   39  39 GLU C   69  SER C   79  1                                  11    
HELIX   40  40 TYR C   90  PHE C  108  1                                  19    
HELIX   41  41 GLY C  125  GLU C  148  1                                  24    
HELIX   42  42 GLN C  164  PHE C  174  1                                  11    
HELIX   43  43 ASP C  191  VAL C  199  1                                   9    
HELIX   44  44 ASP C  220  GLY C  236  1                                  17    
HELIX   45  45 SER C  247  PHE C  250  5                                   4    
HELIX   46  46 ILE C  251  TYR C  256  1                                   6    
HELIX   47  47 ASN C  292  LEU C  296  5                                   5    
HELIX   48  48 PRO C  297  ILE C  301  5                                   5    
HELIX   49  49 SER C  322  LYS C  360  1                                  39    
HELIX   50  50 THR C  387  ARG C  397  1                                  11    
HELIX   51  51 SER C  426  GLU C  446  1                                  21    
HELIX   52  52 ARG D   21  THR D   25  5                                   5    
HELIX   53  53 PRO D   38  LEU D   50  1                                  13    
HELIX   54  54 MET D   51  ASP D   53  5                                   3    
HELIX   55  55 ASN D   55  ASN D   59  5                                   5    
HELIX   56  56 GLU D   69  SER D   79  1                                  11    
HELIX   57  57 TYR D   90  PHE D  108  1                                  19    
HELIX   58  58 GLY D  125  GLU D  148  1                                  24    
HELIX   59  59 GLN D  164  PHE D  174  1                                  11    
HELIX   60  60 ASP D  191  VAL D  199  1                                   9    
HELIX   61  61 ASP D  220  GLY D  236  1                                  17    
HELIX   62  62 SER D  247  PHE D  250  5                                   4    
HELIX   63  63 ILE D  251  TYR D  256  1                                   6    
HELIX   64  64 ASN D  292  LEU D  296  5                                   5    
HELIX   65  65 PRO D  297  ILE D  301  5                                   5    
HELIX   66  66 SER D  322  LYS D  360  1                                  39    
HELIX   67  67 THR D  387  ARG D  397  1                                  11    
HELIX   68  68 SER D  426  GLU D  446  1                                  21    
HELIX   69  69 ARG E   21  THR E   25  5                                   5    
HELIX   70  70 PRO E   38  LEU E   50  1                                  13    
HELIX   71  71 MET E   51  ASP E   53  5                                   3    
HELIX   72  72 ASN E   55  ASN E   59  5                                   5    
HELIX   73  73 GLU E   69  SER E   79  1                                  11    
HELIX   74  74 TYR E   90  PHE E  108  1                                  19    
HELIX   75  75 GLY E  125  GLU E  148  1                                  24    
HELIX   76  76 GLN E  164  PHE E  174  1                                  11    
HELIX   77  77 ASP E  191  VAL E  199  1                                   9    
HELIX   78  78 ASP E  220  GLY E  236  1                                  17    
HELIX   79  79 SER E  247  PHE E  250  5                                   4    
HELIX   80  80 ILE E  251  TYR E  256  1                                   6    
HELIX   81  81 ASN E  292  LEU E  296  5                                   5    
HELIX   82  82 PRO E  297  ILE E  301  5                                   5    
HELIX   83  83 SER E  322  LYS E  360  1                                  39    
HELIX   84  84 THR E  387  ARG E  397  1                                  11    
HELIX   85  85 SER E  426  GLU E  446  1                                  21    
HELIX   86  86 ARG F   21  THR F   25  5                                   5    
HELIX   87  87 PRO F   38  LEU F   50  1                                  13    
HELIX   88  88 MET F   51  ASP F   53  5                                   3    
HELIX   89  89 ASN F   55  ASN F   59  5                                   5    
HELIX   90  90 GLU F   69  SER F   79  1                                  11    
HELIX   91  91 TYR F   90  PHE F  108  1                                  19    
HELIX   92  92 GLY F  125  GLU F  148  1                                  24    
HELIX   93  93 GLN F  164  PHE F  174  1                                  11    
HELIX   94  94 ASP F  191  VAL F  199  1                                   9    
HELIX   95  95 ASP F  220  GLY F  236  1                                  17    
HELIX   96  96 SER F  247  PHE F  250  5                                   4    
HELIX   97  97 ILE F  251  TYR F  256  1                                   6    
HELIX   98  98 ASN F  292  LEU F  296  5                                   5    
HELIX   99  99 PRO F  297  ILE F  301  5                                   5    
HELIX  100 100 SER F  322  LYS F  360  1                                  39    
HELIX  101 101 THR F  387  ARG F  397  1                                  11    
HELIX  102 102 SER F  426  GLU F  446  1                                  21    
SHEET    1   A 7 VAL A 119  THR A 123  0                                        
SHEET    2   A 7 GLY A 286  TRP A 290 -1  O  GLY A 286   N  THR A 123           
SHEET    3   A 7 VAL A 268  SER A 274 -1  N  ILE A 271   O  ILE A 289           
SHEET    4   A 7 ILE A 241  ASP A 244  1  N  ILE A 241   O  LYS A 269           
SHEET    5   A 7 THR A 203  ILE A 209  1  N  ALA A 208   O  ASP A 244           
SHEET    6   A 7 ASN A 156  GLY A 160  1  N  ASN A 156   O  ILE A 204           
SHEET    7   A 7 GLU A 177  VAL A 181  1  O  LYS A 179   N  ILE A 157           
SHEET    1   B 2 PHE A 302  ILE A 304  0                                        
SHEET    2   B 2 GLN A 311  THR A 313 -1  O  THR A 313   N  PHE A 302           
SHEET    1   C 4 PHE A 364  ILE A 366  0                                        
SHEET    2   C 4 LEU A 375  LEU A 380 -1  O  SER A 379   N  ASN A 365           
SHEET    3   C 4 THR A 415  VAL A 420 -1  O  LEU A 417   N  PHE A 378           
SHEET    4   C 4 ALA A 404  THR A 406 -1  N  TYR A 405   O  VAL A 416           
SHEET    1   D 7 VAL B 119  THR B 123  0                                        
SHEET    2   D 7 GLY B 286  TRP B 290 -1  O  GLY B 286   N  THR B 123           
SHEET    3   D 7 VAL B 268  SER B 274 -1  N  ILE B 271   O  ILE B 289           
SHEET    4   D 7 ILE B 241  ASP B 244  1  N  ILE B 241   O  LYS B 269           
SHEET    5   D 7 THR B 203  ILE B 209  1  N  ALA B 208   O  ASP B 244           
SHEET    6   D 7 ASN B 156  GLY B 160  1  N  ASN B 156   O  ILE B 204           
SHEET    7   D 7 GLU B 177  VAL B 181  1  O  LYS B 179   N  ILE B 157           
SHEET    1   E 2 PHE B 302  ILE B 304  0                                        
SHEET    2   E 2 GLN B 311  THR B 313 -1  O  THR B 313   N  PHE B 302           
SHEET    1   F 4 PHE B 364  ILE B 366  0                                        
SHEET    2   F 4 LEU B 375  LEU B 380 -1  O  SER B 379   N  ASN B 365           
SHEET    3   F 4 THR B 415  VAL B 420 -1  O  LEU B 417   N  PHE B 378           
SHEET    4   F 4 ALA B 404  THR B 406 -1  N  TYR B 405   O  VAL B 416           
SHEET    1   G 7 VAL C 119  THR C 123  0                                        
SHEET    2   G 7 GLY C 286  TRP C 290 -1  O  TRP C 290   N  VAL C 119           
SHEET    3   G 7 VAL C 268  SER C 274 -1  N  ILE C 271   O  ILE C 289           
SHEET    4   G 7 ILE C 241  ASP C 244  1  N  ILE C 241   O  LYS C 269           
SHEET    5   G 7 THR C 203  ILE C 209  1  N  ALA C 208   O  ASP C 244           
SHEET    6   G 7 ASN C 156  GLY C 160  1  N  ASN C 156   O  ILE C 204           
SHEET    7   G 7 GLU C 177  VAL C 181  1  O  LYS C 179   N  ILE C 157           
SHEET    1   H 2 PHE C 302  ILE C 304  0                                        
SHEET    2   H 2 GLN C 311  THR C 313 -1  O  THR C 313   N  PHE C 302           
SHEET    1   I 4 PHE C 364  ILE C 366  0                                        
SHEET    2   I 4 LEU C 375  LEU C 380 -1  O  SER C 379   N  ASN C 365           
SHEET    3   I 4 THR C 415  VAL C 420 -1  O  LEU C 417   N  PHE C 378           
SHEET    4   I 4 ALA C 404  THR C 406 -1  N  TYR C 405   O  VAL C 416           
SHEET    1   J 7 VAL D 119  THR D 123  0                                        
SHEET    2   J 7 GLY D 286  TRP D 290 -1  O  GLY D 286   N  THR D 123           
SHEET    3   J 7 VAL D 268  SER D 274 -1  N  ILE D 271   O  ILE D 289           
SHEET    4   J 7 ILE D 241  ASP D 244  1  N  ILE D 241   O  LYS D 269           
SHEET    5   J 7 THR D 203  ILE D 209  1  N  ALA D 208   O  ASP D 244           
SHEET    6   J 7 ASN D 156  GLY D 160  1  N  ASN D 156   O  ILE D 204           
SHEET    7   J 7 GLU D 177  VAL D 181  1  O  LYS D 179   N  ILE D 157           
SHEET    1   K 2 PHE D 302  ILE D 304  0                                        
SHEET    2   K 2 GLN D 311  THR D 313 -1  O  THR D 313   N  PHE D 302           
SHEET    1   L 4 PHE D 364  ILE D 366  0                                        
SHEET    2   L 4 LEU D 375  LEU D 380 -1  O  SER D 379   N  ASN D 365           
SHEET    3   L 4 THR D 415  VAL D 420 -1  O  LEU D 417   N  PHE D 378           
SHEET    4   L 4 ALA D 404  THR D 406 -1  N  TYR D 405   O  VAL D 416           
SHEET    1   M 7 VAL E 119  THR E 123  0                                        
SHEET    2   M 7 GLY E 286  TRP E 290 -1  O  GLY E 286   N  THR E 123           
SHEET    3   M 7 VAL E 268  SER E 274 -1  N  ILE E 271   O  ILE E 289           
SHEET    4   M 7 ILE E 241  ASP E 244  1  N  ILE E 241   O  LYS E 269           
SHEET    5   M 7 THR E 203  ILE E 209  1  N  ALA E 208   O  ASP E 244           
SHEET    6   M 7 ASN E 156  GLY E 160  1  N  ASN E 156   O  ILE E 204           
SHEET    7   M 7 GLU E 177  VAL E 181  1  O  LYS E 179   N  ILE E 157           
SHEET    1   N 2 PHE E 302  ILE E 304  0                                        
SHEET    2   N 2 GLN E 311  THR E 313 -1  O  THR E 313   N  PHE E 302           
SHEET    1   O 4 PHE E 364  ILE E 366  0                                        
SHEET    2   O 4 LEU E 375  LEU E 380 -1  O  SER E 379   N  ASN E 365           
SHEET    3   O 4 THR E 415  VAL E 420 -1  O  LEU E 417   N  PHE E 378           
SHEET    4   O 4 ALA E 404  THR E 406 -1  N  TYR E 405   O  VAL E 416           
SHEET    1   P 7 VAL F 119  THR F 123  0                                        
SHEET    2   P 7 GLY F 286  TRP F 290 -1  O  GLY F 286   N  THR F 123           
SHEET    3   P 7 VAL F 268  SER F 274 -1  N  ILE F 271   O  ILE F 289           
SHEET    4   P 7 ILE F 241  ASP F 244  1  N  ILE F 241   O  LYS F 269           
SHEET    5   P 7 THR F 203  ILE F 209  1  N  ALA F 208   O  ASP F 244           
SHEET    6   P 7 ASN F 156  GLY F 160  1  N  ASN F 156   O  ILE F 204           
SHEET    7   P 7 GLU F 177  VAL F 181  1  O  LYS F 179   N  ILE F 157           
SHEET    1   Q 2 PHE F 302  ILE F 304  0                                        
SHEET    2   Q 2 GLN F 311  THR F 313 -1  O  THR F 313   N  PHE F 302           
SHEET    1   R 4 PHE F 364  ILE F 366  0                                        
SHEET    2   R 4 LEU F 375  LEU F 380 -1  O  SER F 379   N  ASN F 365           
SHEET    3   R 4 THR F 415  VAL F 420 -1  O  LEU F 417   N  PHE F 378           
SHEET    4   R 4 ALA F 404  THR F 406 -1  N  TYR F 405   O  VAL F 416           
LINK         C   HIS A 276                 N   LLP A 277     1555   1555  1.33  
LINK         C   LLP A 277                 N   TYR A 278     1555   1555  1.33  
LINK         C   HIS B 276                 N   LLP B 277     1555   1555  1.33  
LINK         C   LLP B 277                 N   TYR B 278     1555   1555  1.33  
LINK         C   HIS C 276                 N   LLP C 277     1555   1555  1.33  
LINK         C   LLP C 277                 N   TYR C 278     1555   1555  1.33  
LINK         C   HIS D 276                 N   LLP D 277     1555   1555  1.33  
LINK         C   LLP D 277                 N   TYR D 278     1555   1555  1.33  
LINK         C   HIS E 276                 N   LLP E 277     1555   1555  1.33  
LINK         C   LLP E 277                 N   TYR E 278     1555   1555  1.33  
LINK         C   HIS F 276                 N   LLP F 277     1555   1555  1.33  
LINK         C   LLP F 277                 N   TYR F 278     1555   1555  1.33  
CISPEP   1 GLU A  114    ALA A  115          0         0.13                     
CISPEP   2 PRO A  409    ASN A  410          0        -0.17                     
CISPEP   3 PRO B  409    ASN B  410          0         0.93                     
CISPEP   4 PRO C  409    ASN C  410          0         0.17                     
CISPEP   5 PRO D  409    ASN D  410          0         0.80                     
CISPEP   6 PRO E  409    ASN E  410          0        -0.33                     
CISPEP   7 PRO F  409    ASN F  410          0         0.44                     
CRYST1  118.098  118.098  200.576  90.00  90.00 120.00 P 32         18          
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      0.008468  0.004889  0.000000        0.00000                         
SCALE2      0.000000  0.009777  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004986        0.00000                         
MTRIX1   1  0.318302  0.947977  0.004831      -54.36670    1                    
MTRIX2   1  0.947233 -0.317841 -0.041559       75.45140    1                    
MTRIX3   1 -0.037861  0.017805 -0.999124       -1.46108    1                    
MTRIX1   2 -0.503232  0.864004  0.015946      -48.50860    1                    
MTRIX2   2 -0.864137 -0.503243 -0.003575       88.45970    1                    
MTRIX3   2  0.004936 -0.015578  0.999866        1.23684    1                    
MTRIX1   3 -0.979238 -0.202103  0.015704       13.92040    1                    
MTRIX2   3 -0.202182  0.979341 -0.003624        1.35622    1                    
MTRIX3   3 -0.014647 -0.006724 -0.999870        0.68996    1                    
MTRIX1   4 -0.497458 -0.867314  0.017358       52.35720    1                    
MTRIX2   4  0.867356 -0.497632 -0.007499       86.29350    1                    
MTRIX3   4  0.015142  0.011325  0.999821       -0.80090    1                    
MTRIX1   5  0.667823 -0.744318  0.001814       43.75040    1                    
MTRIX2   5 -0.744144 -0.667715 -0.020149       97.96570    1                    
MTRIX3   5  0.016208  0.012106 -0.999795       -1.02356    1                    
MTRIX1   6  0.317723  0.948059 -0.015386      -54.46810    1                    
MTRIX2   6  0.948068 -0.317896 -0.010433       75.69090    1                    
MTRIX3   6 -0.014782 -0.011273 -0.999827        0.62471    1                    
MTRIX1   7 -0.500290  0.865677  0.017686      -48.81490    1                    
MTRIX2   7 -0.865653 -0.500512  0.011547       88.35250    1                    
MTRIX3   7  0.018848 -0.009533  0.999777        0.40187    1                    
MTRIX1   8 -0.979966 -0.199142  0.002942       13.77390    1                    
MTRIX2   8 -0.199138  0.979970  0.001718        1.29489    1                    
MTRIX3   8 -0.003225  0.001098 -0.999994        0.05058    1                    
MTRIX1   9 -0.499153 -0.866332  0.017746       52.19540    1                    
MTRIX2   9  0.866352 -0.499351 -0.009100       86.47640    1                    
MTRIX3   9  0.016745  0.010832  0.999801       -0.71221    1                    
MTRIX1  10  0.664267 -0.747260 -0.018753       44.00390    1                    
MTRIX2  10 -0.747290 -0.664464  0.006800       97.82600    1                    
MTRIX3  10 -0.017542  0.009497 -0.999801       -0.54785    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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