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Database: PDB
Entry: 3UKL
LinkDB: 3UKL
Original site: 3UKL 
HEADER    ISOMERASE                               09-NOV-11   3UKL              
TITLE     CRYSTAL STRUCTURE OF UDP-GALACTOPYRANOSE MUTASE FROM ASPERGILLUS      
TITLE    2 FUMIGATUS IN COMPLEX WITH UDP                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UDP-GALACTOPYRANOSE MUTASE;                                
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 EC: 5.4.99.9;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATUS;                          
SOURCE   3 ORGANISM_TAXID: 746128;                                              
SOURCE   4 STRAIN: CBS 144-89;                                                  
SOURCE   5 GENE: GLF, GLFA;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) GOLD;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    FLAVOENZYME, FAD, UDP, ISOMERASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.E.VAN STRAATEN,D.A.R.SANDERS                                        
REVDAT   5   28-FEB-24 3UKL    1       REMARK SEQADV                            
REVDAT   4   08-NOV-17 3UKL    1       REMARK                                   
REVDAT   3   18-JUL-12 3UKL    1       JRNL                                     
REVDAT   2   07-MAR-12 3UKL    1       JRNL                                     
REVDAT   1   22-FEB-12 3UKL    0                                                
JRNL        AUTH   K.E.VAN STRAATEN,F.H.ROUTIER,D.A.SANDERS                     
JRNL        TITL   STRUCTURAL INSIGHT INTO THE UNIQUE SUBSTRATE BINDING         
JRNL        TITL 2 MECHANISM AND FLAVIN REDOX STATE OF UDP-GALACTOPYRANOSE      
JRNL        TITL 3 MUTASE FROM ASPERGILLUS FUMIGATUS.                           
JRNL        REF    J.BIOL.CHEM.                  V. 287 10780 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22334662                                                     
JRNL        DOI    10.1074/JBC.M111.322974                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.63 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7.1_743                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.63                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 165250                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8263                            
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 48.0409 -  5.6634    0.98    16907   890  0.1576 0.1826        
REMARK   3     2  5.6634 -  4.4962    0.98    16758   882  0.1289 0.1688        
REMARK   3     3  4.4962 -  3.9282    0.97    16678   878  0.1365 0.1847        
REMARK   3     4  3.9282 -  3.5692    0.96    16425   865  0.1748 0.2240        
REMARK   3     5  3.5692 -  3.3134    0.94    16202   852  0.2043 0.2563        
REMARK   3     6  3.3134 -  3.1181    0.92    15768   830  0.2190 0.2819        
REMARK   3     7  3.1181 -  2.9620    0.89    15332   806  0.2403 0.3082        
REMARK   3     8  2.9620 -  2.8330    0.86    14773   778  0.2589 0.3146        
REMARK   3     9  2.8330 -  2.7240    0.84    14371   756  0.2868 0.3427        
REMARK   3    10  2.7240 -  2.6300    0.80    13773   726  0.3015 0.3602        
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              : 0.33                                          
REMARK   3   B_SOL              : 23.43                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.790            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.380           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.49890                                              
REMARK   3    B22 (A**2) : -2.80770                                             
REMARK   3    B33 (A**2) : -1.27510                                             
REMARK   3    B12 (A**2) : -7.82230                                             
REMARK   3    B13 (A**2) : 1.40180                                              
REMARK   3    B23 (A**2) : -2.25550                                             
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      :  0.004          33546                                  
REMARK   3   ANGLE     :  0.776          45712                                  
REMARK   3   CHIRALITY :  0.051           4940                                  
REMARK   3   PLANARITY :  0.003           5844                                  
REMARK   3   DIHEDRAL  : 17.527          12846                                  
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 : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 3993                                        
REMARK   3     RMSD               : 0.199                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 3993                                        
REMARK   3     RMSD               : 0.181                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN D AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 4004                                        
REMARK   3     RMSD               : 0.187                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 3993                                        
REMARK   3     RMSD               : 0.197                                       
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN F AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 4004                                        
REMARK   3     RMSD               : 0.188                                       
REMARK   3    NCS OPERATOR : 6                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN G AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 4004                                        
REMARK   3     RMSD               : 0.183                                       
REMARK   3    NCS OPERATOR : 7                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN H AND (RESSEQ 2:511 ) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 3993                                        
REMARK   3     RMSD               : 0.170                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3UKL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000068871.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08B1-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : COLLIMATING MIRROR                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 165288                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.630                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.3                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.550                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: REDUCED AFUGM:UDPGALP COMPLEX STRUCTURE              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS-PROPANE PH 7.5-8.5, 0.1    
REMARK 280  -0.2M SODIUM CITRATE, 15-20% PEG 3350, MICROBATCH, TEMPERATURE      
REMARK 280  295K, PH 8.5                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18230 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 76360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -162.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17840 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 76550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -135.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       17.44508            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      128.01683            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
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    GLN A  98       71.67     44.75                                   
REMARK 500    PHE A 158      -63.59   -127.26                                   
REMARK 500    ALA A 201       80.69   -155.97                                   
REMARK 500    ALA A 208      -70.56    -30.96                                   
REMARK 500    CYS A 314      -71.00    -94.03                                   
REMARK 500    PHE B 158      -62.27   -127.50                                   
REMARK 500    ALA B 201       81.08   -161.41                                   
REMARK 500    ALA B 208      -70.39    -34.01                                   
REMARK 500    CYS B 314      -71.39    -94.11                                   
REMARK 500    LYS B 380       79.66   -154.24                                   
REMARK 500    THR B 431        0.52    -69.26                                   
REMARK 500    VAL B 455       40.37   -141.86                                   
REMARK 500    PHE C 158      -59.06   -129.48                                   
REMARK 500    ALA C 201       78.05   -156.84                                   
REMARK 500    CYS C 314      -70.73    -97.03                                   
REMARK 500    LYS C 380       83.23   -154.88                                   
REMARK 500    GLU C 454      -18.93    -49.73                                   
REMARK 500    VAL C 455       37.59   -140.32                                   
REMARK 500    TYR C 483       59.74   -140.58                                   
REMARK 500    GLN D  98       72.28     43.88                                   
REMARK 500    PHE D 158      -61.64   -128.46                                   
REMARK 500    ALA D 201       79.54   -158.80                                   
REMARK 500    CYS D 314      -73.44    -96.61                                   
REMARK 500    PHE E 158      -63.53   -128.56                                   
REMARK 500    ALA E 201       79.70   -157.08                                   
REMARK 500    ALA E 208      -71.95    -32.71                                   
REMARK 500    CYS E 314      -67.56    -99.47                                   
REMARK 500    LYS E 380       77.37   -154.36                                   
REMARK 500    ASP F  59      174.23    -54.21                                   
REMARK 500    PHE F 158      -64.22   -131.49                                   
REMARK 500    ALA F 201       81.81   -162.04                                   
REMARK 500    ALA F 208      -75.54    -32.96                                   
REMARK 500    CYS F 314      -64.52    -99.46                                   
REMARK 500    PHE G 158      -67.83   -129.57                                   
REMARK 500    ALA G 201       80.31   -159.70                                   
REMARK 500    CYS G 314      -69.78    -95.64                                   
REMARK 500    LYS G 380       82.45   -151.52                                   
REMARK 500    GLU G 454      -17.64    -49.52                                   
REMARK 500    VAL G 455       40.37   -143.33                                   
REMARK 500    PHE H 158      -59.75   -126.31                                   
REMARK 500    ALA H 201       81.67   -159.58                                   
REMARK 500    ALA H 208      -72.70    -29.08                                   
REMARK 500    ARG H 235       80.86   -153.71                                   
REMARK 500    ASP H 312       31.41    -94.52                                   
REMARK 500    CYS H 314      -70.51    -96.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG E 303         0.13    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP A 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 512                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP B 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP C 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP D 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP E 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD E 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP F 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD F 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 512                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP G 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD G 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP H 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD H 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 1                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UKA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UNLIGANDED AFUGM                                
REMARK 900 RELATED ID: 3UKF   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF AFUGM:UDPGALP COMPLEX (REDUCED)                 
REMARK 900 RELATED ID: 3UKH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF AFUGM:UDPGALP COMPLEX (NON-REDUCED)             
REMARK 900 RELATED ID: 3UKK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF R182K-AFUGM IN COMPLEX WITH UDPGALP             
REMARK 900 RELATED ID: 3UKP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UKQ   RELATED DB: PDB                                   
DBREF  3UKL A    2   510  UNP    Q4W1X2   Q4W1X2_ASPFM     2    510             
DBREF  3UKL B    2   510  UNP    Q4W1X2   Q4W1X2_ASPFM     2    510             
DBREF  3UKL C    2   510  UNP    Q4W1X2   Q4W1X2_ASPFM     2    510             
DBREF  3UKL D    2   510  UNP    Q4W1X2   Q4W1X2_ASPFM     2    510             
DBREF  3UKL E    2   510  UNP    Q4W1X2   Q4W1X2_ASPFM     2    510             
DBREF  3UKL F    2   510  UNP    Q4W1X2   Q4W1X2_ASPFM     2    510             
DBREF  3UKL G    2   510  UNP    Q4W1X2   Q4W1X2_ASPFM     2    510             
DBREF  3UKL H    2   510  UNP    Q4W1X2   Q4W1X2_ASPFM     2    510             
SEQADV 3UKL LEU A  511  UNP  Q4W1X2              EXPRESSION TAG                 
SEQADV 3UKL LEU B  511  UNP  Q4W1X2              EXPRESSION TAG                 
SEQADV 3UKL LEU C  511  UNP  Q4W1X2              EXPRESSION TAG                 
SEQADV 3UKL LEU D  511  UNP  Q4W1X2              EXPRESSION TAG                 
SEQADV 3UKL LEU E  511  UNP  Q4W1X2              EXPRESSION TAG                 
SEQADV 3UKL LEU F  511  UNP  Q4W1X2              EXPRESSION TAG                 
SEQADV 3UKL LEU G  511  UNP  Q4W1X2              EXPRESSION TAG                 
SEQADV 3UKL LEU H  511  UNP  Q4W1X2              EXPRESSION TAG                 
SEQRES   1 A  510  THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY          
SEQRES   2 A  510  ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN          
SEQRES   3 A  510  GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN          
SEQRES   4 A  510  GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO          
SEQRES   5 A  510  GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE          
SEQRES   6 A  510  SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA          
SEQRES   7 A  510  LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE          
SEQRES   8 A  510  SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO          
SEQRES   9 A  510  PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN          
SEQRES  10 A  510  VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU          
SEQRES  11 A  510  ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU          
SEQRES  12 A  510  TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU          
SEQRES  13 A  510  PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO          
SEQRES  14 A  510  THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL          
SEQRES  15 A  510  ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE          
SEQRES  16 A  510  LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR          
SEQRES  17 A  510  PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP          
SEQRES  18 A  510  ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG          
SEQRES  19 A  510  PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN          
SEQRES  20 A  510  ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY          
SEQRES  21 A  510  TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU          
SEQRES  22 A  510  ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR          
SEQRES  23 A  510  LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL          
SEQRES  24 A  510  GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS          
SEQRES  25 A  510  CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR          
SEQRES  26 A  510  ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN          
SEQRES  27 A  510  PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA          
SEQRES  28 A  510  ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY          
SEQRES  29 A  510  PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER          
SEQRES  30 A  510  MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS          
SEQRES  31 A  510  ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR          
SEQRES  32 A  510  ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS          
SEQRES  33 A  510  GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU          
SEQRES  34 A  510  THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP          
SEQRES  35 A  510  SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY          
SEQRES  36 A  510  ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL          
SEQRES  37 A  510  ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN          
SEQRES  38 A  510  TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG          
SEQRES  39 A  510  ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS          
SEQRES  40 A  510  ALA GLN LEU                                                  
SEQRES   1 B  510  THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY          
SEQRES   2 B  510  ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN          
SEQRES   3 B  510  GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN          
SEQRES   4 B  510  GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO          
SEQRES   5 B  510  GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE          
SEQRES   6 B  510  SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA          
SEQRES   7 B  510  LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE          
SEQRES   8 B  510  SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO          
SEQRES   9 B  510  PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN          
SEQRES  10 B  510  VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU          
SEQRES  11 B  510  ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU          
SEQRES  12 B  510  TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU          
SEQRES  13 B  510  PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO          
SEQRES  14 B  510  THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL          
SEQRES  15 B  510  ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE          
SEQRES  16 B  510  LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR          
SEQRES  17 B  510  PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP          
SEQRES  18 B  510  ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG          
SEQRES  19 B  510  PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN          
SEQRES  20 B  510  ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY          
SEQRES  21 B  510  TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU          
SEQRES  22 B  510  ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR          
SEQRES  23 B  510  LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL          
SEQRES  24 B  510  GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS          
SEQRES  25 B  510  CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR          
SEQRES  26 B  510  ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN          
SEQRES  27 B  510  PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA          
SEQRES  28 B  510  ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY          
SEQRES  29 B  510  PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER          
SEQRES  30 B  510  MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS          
SEQRES  31 B  510  ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR          
SEQRES  32 B  510  ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS          
SEQRES  33 B  510  GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU          
SEQRES  34 B  510  THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP          
SEQRES  35 B  510  SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY          
SEQRES  36 B  510  ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL          
SEQRES  37 B  510  ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN          
SEQRES  38 B  510  TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG          
SEQRES  39 B  510  ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS          
SEQRES  40 B  510  ALA GLN LEU                                                  
SEQRES   1 C  510  THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY          
SEQRES   2 C  510  ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN          
SEQRES   3 C  510  GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN          
SEQRES   4 C  510  GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO          
SEQRES   5 C  510  GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE          
SEQRES   6 C  510  SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA          
SEQRES   7 C  510  LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE          
SEQRES   8 C  510  SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO          
SEQRES   9 C  510  PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN          
SEQRES  10 C  510  VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU          
SEQRES  11 C  510  ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU          
SEQRES  12 C  510  TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU          
SEQRES  13 C  510  PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO          
SEQRES  14 C  510  THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL          
SEQRES  15 C  510  ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE          
SEQRES  16 C  510  LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR          
SEQRES  17 C  510  PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP          
SEQRES  18 C  510  ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG          
SEQRES  19 C  510  PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN          
SEQRES  20 C  510  ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY          
SEQRES  21 C  510  TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU          
SEQRES  22 C  510  ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR          
SEQRES  23 C  510  LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL          
SEQRES  24 C  510  GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS          
SEQRES  25 C  510  CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR          
SEQRES  26 C  510  ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN          
SEQRES  27 C  510  PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA          
SEQRES  28 C  510  ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY          
SEQRES  29 C  510  PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER          
SEQRES  30 C  510  MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS          
SEQRES  31 C  510  ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR          
SEQRES  32 C  510  ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS          
SEQRES  33 C  510  GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU          
SEQRES  34 C  510  THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP          
SEQRES  35 C  510  SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY          
SEQRES  36 C  510  ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL          
SEQRES  37 C  510  ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN          
SEQRES  38 C  510  TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG          
SEQRES  39 C  510  ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS          
SEQRES  40 C  510  ALA GLN LEU                                                  
SEQRES   1 D  510  THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY          
SEQRES   2 D  510  ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN          
SEQRES   3 D  510  GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN          
SEQRES   4 D  510  GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO          
SEQRES   5 D  510  GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE          
SEQRES   6 D  510  SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA          
SEQRES   7 D  510  LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE          
SEQRES   8 D  510  SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO          
SEQRES   9 D  510  PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN          
SEQRES  10 D  510  VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU          
SEQRES  11 D  510  ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU          
SEQRES  12 D  510  TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU          
SEQRES  13 D  510  PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO          
SEQRES  14 D  510  THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL          
SEQRES  15 D  510  ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE          
SEQRES  16 D  510  LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR          
SEQRES  17 D  510  PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP          
SEQRES  18 D  510  ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG          
SEQRES  19 D  510  PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN          
SEQRES  20 D  510  ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY          
SEQRES  21 D  510  TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU          
SEQRES  22 D  510  ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR          
SEQRES  23 D  510  LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL          
SEQRES  24 D  510  GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS          
SEQRES  25 D  510  CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR          
SEQRES  26 D  510  ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN          
SEQRES  27 D  510  PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA          
SEQRES  28 D  510  ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY          
SEQRES  29 D  510  PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER          
SEQRES  30 D  510  MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS          
SEQRES  31 D  510  ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR          
SEQRES  32 D  510  ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS          
SEQRES  33 D  510  GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU          
SEQRES  34 D  510  THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP          
SEQRES  35 D  510  SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY          
SEQRES  36 D  510  ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL          
SEQRES  37 D  510  ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN          
SEQRES  38 D  510  TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG          
SEQRES  39 D  510  ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS          
SEQRES  40 D  510  ALA GLN LEU                                                  
SEQRES   1 E  510  THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY          
SEQRES   2 E  510  ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN          
SEQRES   3 E  510  GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN          
SEQRES   4 E  510  GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO          
SEQRES   5 E  510  GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE          
SEQRES   6 E  510  SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA          
SEQRES   7 E  510  LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE          
SEQRES   8 E  510  SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO          
SEQRES   9 E  510  PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN          
SEQRES  10 E  510  VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU          
SEQRES  11 E  510  ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU          
SEQRES  12 E  510  TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU          
SEQRES  13 E  510  PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO          
SEQRES  14 E  510  THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL          
SEQRES  15 E  510  ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE          
SEQRES  16 E  510  LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR          
SEQRES  17 E  510  PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP          
SEQRES  18 E  510  ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG          
SEQRES  19 E  510  PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN          
SEQRES  20 E  510  ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY          
SEQRES  21 E  510  TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU          
SEQRES  22 E  510  ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR          
SEQRES  23 E  510  LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL          
SEQRES  24 E  510  GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS          
SEQRES  25 E  510  CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR          
SEQRES  26 E  510  ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN          
SEQRES  27 E  510  PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA          
SEQRES  28 E  510  ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY          
SEQRES  29 E  510  PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER          
SEQRES  30 E  510  MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS          
SEQRES  31 E  510  ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR          
SEQRES  32 E  510  ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS          
SEQRES  33 E  510  GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU          
SEQRES  34 E  510  THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP          
SEQRES  35 E  510  SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY          
SEQRES  36 E  510  ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL          
SEQRES  37 E  510  ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN          
SEQRES  38 E  510  TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG          
SEQRES  39 E  510  ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS          
SEQRES  40 E  510  ALA GLN LEU                                                  
SEQRES   1 F  510  THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY          
SEQRES   2 F  510  ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN          
SEQRES   3 F  510  GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN          
SEQRES   4 F  510  GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO          
SEQRES   5 F  510  GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE          
SEQRES   6 F  510  SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA          
SEQRES   7 F  510  LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE          
SEQRES   8 F  510  SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO          
SEQRES   9 F  510  PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN          
SEQRES  10 F  510  VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU          
SEQRES  11 F  510  ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU          
SEQRES  12 F  510  TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU          
SEQRES  13 F  510  PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO          
SEQRES  14 F  510  THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL          
SEQRES  15 F  510  ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE          
SEQRES  16 F  510  LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR          
SEQRES  17 F  510  PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP          
SEQRES  18 F  510  ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG          
SEQRES  19 F  510  PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN          
SEQRES  20 F  510  ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY          
SEQRES  21 F  510  TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU          
SEQRES  22 F  510  ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR          
SEQRES  23 F  510  LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL          
SEQRES  24 F  510  GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS          
SEQRES  25 F  510  CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR          
SEQRES  26 F  510  ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN          
SEQRES  27 F  510  PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA          
SEQRES  28 F  510  ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY          
SEQRES  29 F  510  PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER          
SEQRES  30 F  510  MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS          
SEQRES  31 F  510  ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR          
SEQRES  32 F  510  ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS          
SEQRES  33 F  510  GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU          
SEQRES  34 F  510  THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP          
SEQRES  35 F  510  SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY          
SEQRES  36 F  510  ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL          
SEQRES  37 F  510  ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN          
SEQRES  38 F  510  TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG          
SEQRES  39 F  510  ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS          
SEQRES  40 F  510  ALA GLN LEU                                                  
SEQRES   1 G  510  THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY          
SEQRES   2 G  510  ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN          
SEQRES   3 G  510  GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN          
SEQRES   4 G  510  GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO          
SEQRES   5 G  510  GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE          
SEQRES   6 G  510  SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA          
SEQRES   7 G  510  LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE          
SEQRES   8 G  510  SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO          
SEQRES   9 G  510  PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN          
SEQRES  10 G  510  VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU          
SEQRES  11 G  510  ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU          
SEQRES  12 G  510  TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU          
SEQRES  13 G  510  PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO          
SEQRES  14 G  510  THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL          
SEQRES  15 G  510  ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE          
SEQRES  16 G  510  LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR          
SEQRES  17 G  510  PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP          
SEQRES  18 G  510  ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG          
SEQRES  19 G  510  PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN          
SEQRES  20 G  510  ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY          
SEQRES  21 G  510  TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU          
SEQRES  22 G  510  ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR          
SEQRES  23 G  510  LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL          
SEQRES  24 G  510  GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS          
SEQRES  25 G  510  CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR          
SEQRES  26 G  510  ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN          
SEQRES  27 G  510  PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA          
SEQRES  28 G  510  ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY          
SEQRES  29 G  510  PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER          
SEQRES  30 G  510  MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS          
SEQRES  31 G  510  ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR          
SEQRES  32 G  510  ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS          
SEQRES  33 G  510  GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU          
SEQRES  34 G  510  THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP          
SEQRES  35 G  510  SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY          
SEQRES  36 G  510  ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL          
SEQRES  37 G  510  ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN          
SEQRES  38 G  510  TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG          
SEQRES  39 G  510  ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS          
SEQRES  40 G  510  ALA GLN LEU                                                  
SEQRES   1 H  510  THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY          
SEQRES   2 H  510  ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN          
SEQRES   3 H  510  GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN          
SEQRES   4 H  510  GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO          
SEQRES   5 H  510  GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE          
SEQRES   6 H  510  SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA          
SEQRES   7 H  510  LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE          
SEQRES   8 H  510  SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO          
SEQRES   9 H  510  PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN          
SEQRES  10 H  510  VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU          
SEQRES  11 H  510  ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU          
SEQRES  12 H  510  TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU          
SEQRES  13 H  510  PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO          
SEQRES  14 H  510  THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL          
SEQRES  15 H  510  ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE          
SEQRES  16 H  510  LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR          
SEQRES  17 H  510  PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP          
SEQRES  18 H  510  ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG          
SEQRES  19 H  510  PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN          
SEQRES  20 H  510  ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY          
SEQRES  21 H  510  TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU          
SEQRES  22 H  510  ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR          
SEQRES  23 H  510  LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL          
SEQRES  24 H  510  GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS          
SEQRES  25 H  510  CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR          
SEQRES  26 H  510  ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN          
SEQRES  27 H  510  PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA          
SEQRES  28 H  510  ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY          
SEQRES  29 H  510  PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER          
SEQRES  30 H  510  MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS          
SEQRES  31 H  510  ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR          
SEQRES  32 H  510  ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS          
SEQRES  33 H  510  GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU          
SEQRES  34 H  510  THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP          
SEQRES  35 H  510  SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY          
SEQRES  36 H  510  ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL          
SEQRES  37 H  510  ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN          
SEQRES  38 H  510  TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG          
SEQRES  39 H  510  ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS          
SEQRES  40 H  510  ALA GLN LEU                                                  
HET    UDP  A 800      25                                                       
HET    FAD  A 602      53                                                       
HET     CL  A   1       1                                                       
HET     CL  A 512       1                                                       
HET    UDP  B 800      25                                                       
HET    FAD  B 604      53                                                       
HET     CL  B   1       1                                                       
HET    UDP  C 800      25                                                       
HET    FAD  C 600      53                                                       
HET     CL  C   1       1                                                       
HET    UDP  D 800      25                                                       
HET    FAD  D 601      53                                                       
HET    UDP  E 800      25                                                       
HET    FAD  E 606      53                                                       
HET     CL  E   1       1                                                       
HET    UDP  F 800      25                                                       
HET    FAD  F 603      53                                                       
HET     CL  F   1       1                                                       
HET     CL  F 512       1                                                       
HET    UDP  G 800      25                                                       
HET    FAD  G 607      53                                                       
HET    UDP  H 800      25                                                       
HET    FAD  H 605      53                                                       
HET     CL  H   1       1                                                       
HETNAM     UDP URIDINE-5'-DIPHOSPHATE                                           
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   9  UDP    8(C9 H14 N2 O12 P2)                                          
FORMUL  10  FAD    8(C27 H33 N9 O15 P2)                                         
FORMUL  11   CL    8(CL 1-)                                                     
FORMUL  33  HOH   *1039(H2 O)                                                   
HELIX    1   1 GLY A   16  ASP A   30  1                                  15    
HELIX    2   2 GLY A   44  ALA A   47  5                                   4    
HELIX    3   3 TYR A   69  LEU A   80  1                                  12    
HELIX    4   4 LYS A   82  ASP A   84  5                                   3    
HELIX    5   5 PRO A  105  LEU A  113  5                                   9    
HELIX    6   6 PRO A  114  ARG A  133  1                                  20    
HELIX    7   7 THR A  141  PHE A  158  1                                  18    
HELIX    8   8 PHE A  158  ALA A  168  1                                  11    
HELIX    9   9 PRO A  170  MET A  174  5                                   5    
HELIX   10  10 ASN A  187  GLY A  198  1                                  12    
HELIX   11  11 GLY A  216  THR A  228  1                                  13    
HELIX   12  12 LEU A  229  GLU A  232  5                                   4    
HELIX   13  13 GLU A  238  GLY A  240  5                                   3    
HELIX   14  14 ALA A  270  ASN A  279  1                                  10    
HELIX   15  15 ASP A  280  LYS A  288  1                                   9    
HELIX   16  16 PHE A  331  TYR A  334  5                                   4    
HELIX   17  17 SER A  335  GLN A  339  5                                   5    
HELIX   18  18 ASN A  383  THR A  398  1                                  16    
HELIX   19  19 GLU A  425  ASP A  439  1                                  15    
HELIX   20  20 ARG A  452  GLY A  456  5                                   5    
HELIX   21  21 ASN A  457  GLY A  475  1                                  19    
HELIX   22  22 GLU A  478  TYR A  483  1                                   6    
HELIX   23  23 TYR A  483  GLY A  489  1                                   7    
HELIX   24  24 ASP A  499  LEU A  511  1                                  13    
HELIX   25  25 GLY B   16  ASP B   30  1                                  15    
HELIX   26  26 GLY B   44  SER B   48  5                                   5    
HELIX   27  27 TYR B   69  LEU B   80  1                                  12    
HELIX   28  28 LYS B   82  ASP B   84  5                                   3    
HELIX   29  29 PRO B  105  LEU B  113  5                                   9    
HELIX   30  30 PRO B  114  ARG B  133  1                                  20    
HELIX   31  31 THR B  141  PHE B  158  1                                  18    
HELIX   32  32 PHE B  158  ALA B  168  1                                  11    
HELIX   33  33 PRO B  170  MET B  174  5                                   5    
HELIX   34  34 ASN B  187  GLY B  198  1                                  12    
HELIX   35  35 THR B  218  THR B  228  1                                  11    
HELIX   36  36 LEU B  229  GLU B  232  5                                   4    
HELIX   37  37 GLU B  238  GLY B  240  5                                   3    
HELIX   38  38 ALA B  270  ASN B  279  1                                  10    
HELIX   39  39 ASP B  280  LYS B  288  1                                   9    
HELIX   40  40 PHE B  331  TYR B  334  5                                   4    
HELIX   41  41 SER B  335  GLN B  339  5                                   5    
HELIX   42  42 ASN B  383  THR B  398  1                                  16    
HELIX   43  43 GLU B  425  ASP B  439  1                                  15    
HELIX   44  44 ARG B  452  GLY B  456  5                                   5    
HELIX   45  45 ASN B  457  GLY B  475  1                                  19    
HELIX   46  46 GLU B  478  TYR B  483  1                                   6    
HELIX   47  47 TYR B  483  GLY B  489  1                                   7    
HELIX   48  48 ASP B  499  LEU B  511  1                                  13    
HELIX   49  49 GLY C   16  ASP C   30  1                                  15    
HELIX   50  50 GLY C   44  ALA C   47  5                                   4    
HELIX   51  51 TYR C   69  LEU C   80  1                                  12    
HELIX   52  52 LYS C   82  ASP C   84  5                                   3    
HELIX   53  53 PRO C  105  LEU C  113  5                                   9    
HELIX   54  54 PRO C  114  ARG C  133  1                                  20    
HELIX   55  55 THR C  141  PHE C  158  1                                  18    
HELIX   56  56 PHE C  158  ALA C  168  1                                  11    
HELIX   57  57 PRO C  170  MET C  174  5                                   5    
HELIX   58  58 ASN C  187  GLY C  198  1                                  12    
HELIX   59  59 GLY C  216  THR C  228  1                                  13    
HELIX   60  60 LEU C  229  GLU C  232  5                                   4    
HELIX   61  61 GLU C  238  GLY C  240  5                                   3    
HELIX   62  62 ALA C  270  ASN C  279  1                                  10    
HELIX   63  63 ASP C  280  LYS C  288  1                                   9    
HELIX   64  64 PHE C  331  TYR C  334  5                                   4    
HELIX   65  65 SER C  335  GLN C  339  5                                   5    
HELIX   66  66 ASN C  383  THR C  398  1                                  16    
HELIX   67  67 GLU C  425  ASP C  439  1                                  15    
HELIX   68  68 ARG C  452  GLY C  456  5                                   5    
HELIX   69  69 ASN C  457  GLY C  475  1                                  19    
HELIX   70  70 GLU C  478  TYR C  483  1                                   6    
HELIX   71  71 TYR C  483  GLY C  489  1                                   7    
HELIX   72  72 ASP C  499  LEU C  511  1                                  13    
HELIX   73  73 GLY D   16  ASP D   30  1                                  15    
HELIX   74  74 GLY D   44  ALA D   47  5                                   4    
HELIX   75  75 TYR D   69  LEU D   80  1                                  12    
HELIX   76  76 LYS D   82  ASP D   84  5                                   3    
HELIX   77  77 PRO D  105  LEU D  113  5                                   9    
HELIX   78  78 PRO D  114  ARG D  133  1                                  20    
HELIX   79  79 THR D  141  PHE D  158  1                                  18    
HELIX   80  80 PHE D  158  ALA D  168  1                                  11    
HELIX   81  81 PRO D  170  MET D  174  5                                   5    
HELIX   82  82 CYS D  176  GLY D  180  5                                   5    
HELIX   83  83 ASN D  187  GLY D  198  1                                  12    
HELIX   84  84 GLY D  217  THR D  228  1                                  12    
HELIX   85  85 LEU D  229  GLU D  232  5                                   4    
HELIX   86  86 GLU D  238  GLY D  240  5                                   3    
HELIX   87  87 ALA D  247  ASN D  249  5                                   3    
HELIX   88  88 ALA D  270  ASN D  279  1                                  10    
HELIX   89  89 ASP D  280  LYS D  288  1                                   9    
HELIX   90  90 PHE D  331  TYR D  334  5                                   4    
HELIX   91  91 ASN D  383  THR D  398  1                                  16    
HELIX   92  92 GLU D  425  ASP D  439  1                                  15    
HELIX   93  93 ARG D  452  GLY D  456  5                                   5    
HELIX   94  94 ASN D  457  GLY D  475  1                                  19    
HELIX   95  95 GLU D  478  TYR D  483  1                                   6    
HELIX   96  96 TYR D  483  GLY D  489  1                                   7    
HELIX   97  97 ASP D  499  LEU D  511  1                                  13    
HELIX   98  98 GLY E   16  ASP E   30  1                                  15    
HELIX   99  99 GLY E   44  SER E   48  5                                   5    
HELIX  100 100 TYR E   69  LEU E   80  1                                  12    
HELIX  101 101 LYS E   82  ASP E   84  5                                   3    
HELIX  102 102 PRO E  105  LEU E  113  5                                   9    
HELIX  103 103 PRO E  114  ARG E  133  1                                  20    
HELIX  104 104 THR E  141  PHE E  158  1                                  18    
HELIX  105 105 PHE E  158  ALA E  168  1                                  11    
HELIX  106 106 PRO E  170  MET E  174  5                                   5    
HELIX  107 107 ASN E  187  GLY E  198  1                                  12    
HELIX  108 108 THR E  218  THR E  228  1                                  11    
HELIX  109 109 LEU E  229  GLU E  232  5                                   4    
HELIX  110 110 GLU E  238  GLY E  240  5                                   3    
HELIX  111 111 ALA E  270  ASN E  279  1                                  10    
HELIX  112 112 ASP E  280  LYS E  288  1                                   9    
HELIX  113 113 PHE E  331  TYR E  334  5                                   4    
HELIX  114 114 SER E  335  GLN E  339  5                                   5    
HELIX  115 115 ASN E  383  THR E  398  1                                  16    
HELIX  116 116 GLU E  425  ASP E  439  1                                  15    
HELIX  117 117 ARG E  452  GLY E  456  5                                   5    
HELIX  118 118 ASN E  457  GLY E  475  1                                  19    
HELIX  119 119 GLU E  478  TYR E  483  1                                   6    
HELIX  120 120 TYR E  483  GLY E  489  1                                   7    
HELIX  121 121 ASP E  499  LEU E  511  1                                  13    
HELIX  122 122 GLY F   16  ASP F   30  1                                  15    
HELIX  123 123 GLY F   44  SER F   48  5                                   5    
HELIX  124 124 TYR F   69  LEU F   80  1                                  12    
HELIX  125 125 LYS F   82  ASP F   84  5                                   3    
HELIX  126 126 PRO F  105  LEU F  113  5                                   9    
HELIX  127 127 PRO F  114  ARG F  133  1                                  20    
HELIX  128 128 THR F  141  PHE F  158  1                                  18    
HELIX  129 129 PHE F  158  ALA F  168  1                                  11    
HELIX  130 130 PRO F  170  MET F  174  5                                   5    
HELIX  131 131 CYS F  176  GLY F  180  5                                   5    
HELIX  132 132 ASN F  187  GLY F  198  1                                  12    
HELIX  133 133 THR F  218  THR F  228  1                                  11    
HELIX  134 134 LEU F  229  GLU F  232  5                                   4    
HELIX  135 135 GLU F  238  GLY F  240  5                                   3    
HELIX  136 136 ALA F  270  ASN F  279  1                                  10    
HELIX  137 137 ASP F  280  LYS F  288  1                                   9    
HELIX  138 138 PHE F  331  TYR F  334  5                                   4    
HELIX  139 139 SER F  335  GLN F  339  5                                   5    
HELIX  140 140 ASN F  383  THR F  398  1                                  16    
HELIX  141 141 GLU F  425  ASP F  439  1                                  15    
HELIX  142 142 ARG F  452  GLY F  456  5                                   5    
HELIX  143 143 ASN F  457  GLY F  475  1                                  19    
HELIX  144 144 GLU F  478  TYR F  483  1                                   6    
HELIX  145 145 TYR F  483  GLY F  489  1                                   7    
HELIX  146 146 ASP F  499  LEU F  511  1                                  13    
HELIX  147 147 GLY G   16  ASP G   30  1                                  15    
HELIX  148 148 GLY G   44  ALA G   47  5                                   4    
HELIX  149 149 TYR G   69  LEU G   80  1                                  12    
HELIX  150 150 LYS G   82  ASP G   84  5                                   3    
HELIX  151 151 PRO G  105  LEU G  113  5                                   9    
HELIX  152 152 PRO G  114  ARG G  133  1                                  20    
HELIX  153 153 THR G  141  PHE G  158  1                                  18    
HELIX  154 154 PHE G  158  ALA G  168  1                                  11    
HELIX  155 155 PRO G  170  MET G  174  5                                   5    
HELIX  156 156 CYS G  176  GLY G  180  5                                   5    
HELIX  157 157 ASN G  187  GLY G  198  1                                  12    
HELIX  158 158 THR G  218  THR G  228  1                                  11    
HELIX  159 159 LEU G  229  GLU G  232  5                                   4    
HELIX  160 160 GLU G  238  GLY G  240  5                                   3    
HELIX  161 161 ALA G  270  ASN G  279  1                                  10    
HELIX  162 162 ASP G  280  LYS G  288  1                                   9    
HELIX  163 163 PHE G  331  TYR G  334  5                                   4    
HELIX  164 164 SER G  335  GLN G  339  5                                   5    
HELIX  165 165 ASN G  383  THR G  398  1                                  16    
HELIX  166 166 GLU G  425  ASP G  439  1                                  15    
HELIX  167 167 ARG G  452  GLY G  456  5                                   5    
HELIX  168 168 ASN G  457  GLY G  475  1                                  19    
HELIX  169 169 GLU G  478  TYR G  483  1                                   6    
HELIX  170 170 TYR G  483  GLY G  489  1                                   7    
HELIX  171 171 ASP G  499  ALA G  509  1                                  11    
HELIX  172 172 GLY H   16  ASP H   30  1                                  15    
HELIX  173 173 GLY H   44  SER H   48  5                                   5    
HELIX  174 174 TYR H   69  LEU H   80  1                                  12    
HELIX  175 175 LYS H   82  ASP H   84  5                                   3    
HELIX  176 176 PRO H  105  LEU H  113  5                                   9    
HELIX  177 177 PRO H  114  ARG H  133  1                                  20    
HELIX  178 178 THR H  141  PHE H  158  1                                  18    
HELIX  179 179 PHE H  158  ALA H  168  1                                  11    
HELIX  180 180 PRO H  170  MET H  174  5                                   5    
HELIX  181 181 ASN H  187  GLY H  198  1                                  12    
HELIX  182 182 THR H  218  ASN H  227  1                                  10    
HELIX  183 183 THR H  228  LEU H  229  5                                   2    
HELIX  184 184 PRO H  230  GLU H  232  5                                   3    
HELIX  185 185 GLU H  238  GLY H  240  5                                   3    
HELIX  186 186 ALA H  270  ASN H  279  1                                  10    
HELIX  187 187 ASP H  280  LYS H  288  1                                   9    
HELIX  188 188 PHE H  331  TYR H  334  5                                   4    
HELIX  189 189 ASN H  383  THR H  398  1                                  16    
HELIX  190 190 GLU H  425  ASP H  439  1                                  15    
HELIX  191 191 ARG H  452  GLY H  456  5                                   5    
HELIX  192 192 ASN H  457  GLY H  475  1                                  19    
HELIX  193 193 GLU H  478  TYR H  483  1                                   6    
HELIX  194 194 TYR H  483  GLY H  489  1                                   7    
HELIX  195 195 ASP H  499  LEU H  511  1                                  13    
SHEET    1   A 6 THR A 234  PHE A 236  0                                        
SHEET    2   A 6 TRP A  34  ASP A  38  1  N  ASP A  38   O  ARG A 235           
SHEET    3   A 6 ILE A   6  ILE A  13  1  N  VAL A  12   O  MET A  35           
SHEET    4   A 6 THR A 259  SER A 267  1  O  GLY A 261   N  ILE A   6           
SHEET    5   A 6 THR A 251  LEU A 254 -1  N  VAL A 252   O  ILE A 260           
SHEET    6   A 6 VAL A 242  ASN A 246 -1  N  THR A 243   O  THR A 253           
SHEET    1   B 5 THR A 234  PHE A 236  0                                        
SHEET    2   B 5 TRP A  34  ASP A  38  1  N  ASP A  38   O  ARG A 235           
SHEET    3   B 5 ILE A   6  ILE A  13  1  N  VAL A  12   O  MET A  35           
SHEET    4   B 5 THR A 259  SER A 267  1  O  GLY A 261   N  ILE A   6           
SHEET    5   B 5 ILE A 442  SER A 444  1  O  TRP A 443   N  LEU A 265           
SHEET    1   C 2 THR A  49  VAL A  51  0                                        
SHEET    2   C 2 LEU A  57  ASP A  59 -1  O  TYR A  58   N  ASP A  50           
SHEET    1   D 2 TRP A  86  GLN A  90  0                                        
SHEET    2   D 2 THR A 209  PRO A 213 -1  O  PHE A 210   N  HIS A  89           
SHEET    1   E 8 GLN A 100  PRO A 103  0                                        
SHEET    2   E 8 SER A  93  CYS A  97 -1  N  VAL A  95   O  VAL A 102           
SHEET    3   E 8 TRP A 315  TYR A 317  1  O  TYR A 317   N  ARG A  96           
SHEET    4   E 8 ARG A 327  THR A 329 -1  O  ALA A 328   N  LEU A 316           
SHEET    5   E 8 TYR A 367  GLU A 376 -1  O  MET A 371   N  THR A 329           
SHEET    6   E 8 TYR A 292  ARG A 303 -1  N  ILE A 298   O  LEU A 372           
SHEET    7   E 8 GLU A 406  PRO A 420 -1  O  PHE A 415   N  THR A 295           
SHEET    8   E 8 GLN A 350  LEU A 351 -1  N  GLN A 350   O  ILE A 407           
SHEET    1   F 6 THR B 234  PHE B 236  0                                        
SHEET    2   F 6 TRP B  34  ASP B  38  1  N  ILE B  36   O  ARG B 235           
SHEET    3   F 6 ILE B   6  ILE B  13  1  N  VAL B  12   O  MET B  35           
SHEET    4   F 6 THR B 259  SER B 267  1  O  GLY B 261   N  ILE B   6           
SHEET    5   F 6 THR B 251  LEU B 254 -1  N  VAL B 252   O  ILE B 260           
SHEET    6   F 6 VAL B 242  ASN B 246 -1  N  LYS B 244   O  THR B 253           
SHEET    1   G 5 THR B 234  PHE B 236  0                                        
SHEET    2   G 5 TRP B  34  ASP B  38  1  N  ILE B  36   O  ARG B 235           
SHEET    3   G 5 ILE B   6  ILE B  13  1  N  VAL B  12   O  MET B  35           
SHEET    4   G 5 THR B 259  SER B 267  1  O  GLY B 261   N  ILE B   6           
SHEET    5   G 5 ILE B 442  SER B 444  1  O  TRP B 443   N  LEU B 265           
SHEET    1   H 2 ASP B  50  VAL B  51  0                                        
SHEET    2   H 2 LEU B  57  TYR B  58 -1  O  TYR B  58   N  ASP B  50           
SHEET    1   I 2 TRP B  86  GLN B  90  0                                        
SHEET    2   I 2 THR B 209  PRO B 213 -1  O  PHE B 210   N  HIS B  89           
SHEET    1   J 8 GLN B 100  PRO B 103  0                                        
SHEET    2   J 8 SER B  93  CYS B  97 -1  N  VAL B  95   O  VAL B 102           
SHEET    3   J 8 TRP B 315  TYR B 317  1  O  TYR B 317   N  ARG B  96           
SHEET    4   J 8 ARG B 327  THR B 329 -1  O  ALA B 328   N  LEU B 316           
SHEET    5   J 8 TYR B 367  GLU B 376 -1  O  MET B 371   N  THR B 329           
SHEET    6   J 8 TYR B 292  ARG B 303 -1  N  ILE B 298   O  LEU B 372           
SHEET    7   J 8 GLU B 406  PRO B 420 -1  O  VAL B 408   N  GLY B 301           
SHEET    8   J 8 GLN B 350  LEU B 351 -1  N  GLN B 350   O  ILE B 407           
SHEET    1   K 2 LEU B 346  PRO B 347  0                                        
SHEET    2   K 2 ALA B 362  LYS B 363 -1  O  LYS B 363   N  LEU B 346           
SHEET    1   L 4 ILE C   6  SER C   7  0                                        
SHEET    2   L 4 THR C 259  GLY C 261  1  O  GLY C 261   N  ILE C   6           
SHEET    3   L 4 THR C 251  LEU C 254 -1  N  VAL C 252   O  ILE C 260           
SHEET    4   L 4 VAL C 242  ASN C 246 -1  N  THR C 243   O  THR C 253           
SHEET    1   M 5 THR C 234  PHE C 236  0                                        
SHEET    2   M 5 TRP C  34  ASP C  38  1  N  ASP C  38   O  ARG C 235           
SHEET    3   M 5 VAL C  10  ILE C  13  1  N  VAL C  12   O  MET C  35           
SHEET    4   M 5 LYS C 264  SER C 267  1  O  VAL C 266   N  LEU C  11           
SHEET    5   M 5 ILE C 442  SER C 444  1  O  TRP C 443   N  LEU C 265           
SHEET    1   N 2 THR C  49  VAL C  51  0                                        
SHEET    2   N 2 LEU C  57  ASP C  59 -1  O  TYR C  58   N  ASP C  50           
SHEET    1   O 2 TRP C  86  GLN C  90  0                                        
SHEET    2   O 2 THR C 209  PRO C 213 -1  O  PHE C 210   N  HIS C  89           
SHEET    1   P 8 GLN C 100  PRO C 103  0                                        
SHEET    2   P 8 SER C  93  CYS C  97 -1  N  VAL C  95   O  VAL C 102           
SHEET    3   P 8 TRP C 315  TYR C 317  1  O  TYR C 317   N  ARG C  96           
SHEET    4   P 8 ARG C 327  THR C 329 -1  O  ALA C 328   N  LEU C 316           
SHEET    5   P 8 TYR C 367  GLU C 376 -1  O  MET C 371   N  THR C 329           
SHEET    6   P 8 TYR C 292  ARG C 303 -1  N  ILE C 298   O  LEU C 372           
SHEET    7   P 8 GLU C 406  PRO C 420 -1  O  TYR C 411   N  GLY C 299           
SHEET    8   P 8 GLN C 350  LEU C 351 -1  N  GLN C 350   O  ILE C 407           
SHEET    1   Q 6 THR D 234  PHE D 236  0                                        
SHEET    2   Q 6 TRP D  34  ASP D  38  1  N  ASP D  38   O  ARG D 235           
SHEET    3   Q 6 ILE D   6  ILE D  13  1  N  VAL D  12   O  MET D  35           
SHEET    4   Q 6 THR D 259  SER D 267  1  O  GLY D 261   N  ILE D   6           
SHEET    5   Q 6 THR D 251  LEU D 254 -1  N  VAL D 252   O  ILE D 260           
SHEET    6   Q 6 VAL D 242  ASN D 246 -1  N  LYS D 244   O  THR D 253           
SHEET    1   R 5 THR D 234  PHE D 236  0                                        
SHEET    2   R 5 TRP D  34  ASP D  38  1  N  ASP D  38   O  ARG D 235           
SHEET    3   R 5 ILE D   6  ILE D  13  1  N  VAL D  12   O  MET D  35           
SHEET    4   R 5 THR D 259  SER D 267  1  O  GLY D 261   N  ILE D   6           
SHEET    5   R 5 ILE D 442  SER D 444  1  O  TRP D 443   N  LEU D 265           
SHEET    1   S 2 THR D  49  VAL D  51  0                                        
SHEET    2   S 2 LEU D  57  ASP D  59 -1  O  TYR D  58   N  ASP D  50           
SHEET    1   T 2 TRP D  86  GLN D  90  0                                        
SHEET    2   T 2 THR D 209  PRO D 213 -1  O  PHE D 210   N  HIS D  89           
SHEET    1   U 8 GLN D 100  PRO D 103  0                                        
SHEET    2   U 8 SER D  93  CYS D  97 -1  N  VAL D  95   O  VAL D 102           
SHEET    3   U 8 TRP D 315  TYR D 317  1  O  TYR D 317   N  ARG D  96           
SHEET    4   U 8 ARG D 327  THR D 329 -1  O  ALA D 328   N  LEU D 316           
SHEET    5   U 8 TYR D 367  GLU D 376 -1  O  MET D 371   N  THR D 329           
SHEET    6   U 8 TYR D 292  ARG D 303 -1  N  ILE D 298   O  LEU D 372           
SHEET    7   U 8 GLU D 406  PRO D 420 -1  O  TYR D 411   N  GLY D 299           
SHEET    8   U 8 GLN D 350  LEU D 351 -1  N  GLN D 350   O  ILE D 407           
SHEET    1   V 6 THR E 234  PHE E 236  0                                        
SHEET    2   V 6 TRP E  34  ASP E  38  1  N  ASP E  38   O  ARG E 235           
SHEET    3   V 6 ILE E   6  ILE E  13  1  N  VAL E  12   O  MET E  35           
SHEET    4   V 6 THR E 259  SER E 267  1  O  GLY E 261   N  ILE E   6           
SHEET    5   V 6 THR E 251  LEU E 254 -1  N  VAL E 252   O  ILE E 260           
SHEET    6   V 6 VAL E 242  ASN E 246 -1  N  THR E 243   O  THR E 253           
SHEET    1   W 5 THR E 234  PHE E 236  0                                        
SHEET    2   W 5 TRP E  34  ASP E  38  1  N  ASP E  38   O  ARG E 235           
SHEET    3   W 5 ILE E   6  ILE E  13  1  N  VAL E  12   O  MET E  35           
SHEET    4   W 5 THR E 259  SER E 267  1  O  GLY E 261   N  ILE E   6           
SHEET    5   W 5 ILE E 442  SER E 444  1  O  TRP E 443   N  LEU E 265           
SHEET    1   X 2 ASP E  50  VAL E  51  0                                        
SHEET    2   X 2 LEU E  57  TYR E  58 -1  O  TYR E  58   N  ASP E  50           
SHEET    1   Y 2 TRP E  86  GLN E  90  0                                        
SHEET    2   Y 2 THR E 209  PRO E 213 -1  O  PHE E 210   N  HIS E  89           
SHEET    1   Z 8 GLN E 100  PRO E 103  0                                        
SHEET    2   Z 8 SER E  93  CYS E  97 -1  N  VAL E  95   O  VAL E 102           
SHEET    3   Z 8 TRP E 315  TYR E 317  1  O  TYR E 317   N  ARG E  96           
SHEET    4   Z 8 ARG E 327  THR E 329 -1  O  ALA E 328   N  LEU E 316           
SHEET    5   Z 8 TYR E 367  GLU E 376 -1  O  MET E 371   N  THR E 329           
SHEET    6   Z 8 TYR E 292  ARG E 303 -1  N  ILE E 298   O  LEU E 372           
SHEET    7   Z 8 GLU E 406  PRO E 420 -1  O  TYR E 411   N  GLY E 299           
SHEET    8   Z 8 GLN E 350  LEU E 351 -1  N  GLN E 350   O  ILE E 407           
SHEET    1  AA 4 ILE F   6  SER F   7  0                                        
SHEET    2  AA 4 THR F 259  GLY F 261  1  O  GLY F 261   N  ILE F   6           
SHEET    3  AA 4 THR F 251  LEU F 254 -1  N  VAL F 252   O  ILE F 260           
SHEET    4  AA 4 VAL F 242  ASN F 246 -1  N  THR F 243   O  THR F 253           
SHEET    1  AB 5 THR F 234  PHE F 236  0                                        
SHEET    2  AB 5 TRP F  34  ASP F  38  1  N  ILE F  36   O  ARG F 235           
SHEET    3  AB 5 VAL F  10  ILE F  13  1  N  VAL F  12   O  MET F  35           
SHEET    4  AB 5 LYS F 264  SER F 267  1  O  VAL F 266   N  LEU F  11           
SHEET    5  AB 5 ILE F 442  SER F 444  1  O  TRP F 443   N  LEU F 265           
SHEET    1  AC 2 ASP F  50  VAL F  51  0                                        
SHEET    2  AC 2 LEU F  57  TYR F  58 -1  O  TYR F  58   N  ASP F  50           
SHEET    1  AD 2 TRP F  86  GLN F  90  0                                        
SHEET    2  AD 2 THR F 209  PRO F 213 -1  O  PHE F 210   N  HIS F  89           
SHEET    1  AE 8 GLN F 100  PRO F 103  0                                        
SHEET    2  AE 8 SER F  93  CYS F  97 -1  N  VAL F  95   O  VAL F 102           
SHEET    3  AE 8 TRP F 315  TYR F 317  1  O  TYR F 317   N  ARG F  96           
SHEET    4  AE 8 ARG F 327  THR F 329 -1  O  ALA F 328   N  LEU F 316           
SHEET    5  AE 8 TYR F 367  GLU F 376 -1  O  MET F 371   N  THR F 329           
SHEET    6  AE 8 TYR F 292  ARG F 303 -1  N  ILE F 298   O  LEU F 372           
SHEET    7  AE 8 GLU F 406  PRO F 420 -1  O  TYR F 411   N  GLY F 299           
SHEET    8  AE 8 GLN F 350  LEU F 351 -1  N  GLN F 350   O  ILE F 407           
SHEET    1  AF 2 LEU F 346  PRO F 347  0                                        
SHEET    2  AF 2 ALA F 362  LYS F 363 -1  O  LYS F 363   N  LEU F 346           
SHEET    1  AG 6 THR G 234  PHE G 236  0                                        
SHEET    2  AG 6 TRP G  34  ASP G  38  1  N  ASP G  38   O  ARG G 235           
SHEET    3  AG 6 ILE G   6  ILE G  13  1  N  VAL G  12   O  MET G  35           
SHEET    4  AG 6 THR G 259  SER G 267  1  O  GLY G 261   N  ILE G   6           
SHEET    5  AG 6 THR G 251  LEU G 254 -1  N  VAL G 252   O  ILE G 260           
SHEET    6  AG 6 VAL G 242  ASN G 246 -1  N  THR G 243   O  THR G 253           
SHEET    1  AH 5 THR G 234  PHE G 236  0                                        
SHEET    2  AH 5 TRP G  34  ASP G  38  1  N  ASP G  38   O  ARG G 235           
SHEET    3  AH 5 ILE G   6  ILE G  13  1  N  VAL G  12   O  MET G  35           
SHEET    4  AH 5 THR G 259  SER G 267  1  O  GLY G 261   N  ILE G   6           
SHEET    5  AH 5 ILE G 442  SER G 444  1  O  TRP G 443   N  LEU G 265           
SHEET    1  AI 2 THR G  49  VAL G  51  0                                        
SHEET    2  AI 2 LEU G  57  ASP G  59 -1  O  TYR G  58   N  ASP G  50           
SHEET    1  AJ 2 TRP G  86  GLN G  90  0                                        
SHEET    2  AJ 2 THR G 209  PRO G 213 -1  O  PHE G 210   N  HIS G  89           
SHEET    1  AK 8 GLN G 100  PRO G 103  0                                        
SHEET    2  AK 8 SER G  93  CYS G  97 -1  N  VAL G  95   O  VAL G 102           
SHEET    3  AK 8 TRP G 315  TYR G 317  1  O  TYR G 317   N  ARG G  96           
SHEET    4  AK 8 ARG G 327  THR G 329 -1  O  ALA G 328   N  LEU G 316           
SHEET    5  AK 8 TYR G 367  GLU G 376 -1  O  MET G 371   N  THR G 329           
SHEET    6  AK 8 TYR G 292  ARG G 303 -1  N  HIS G 296   O  VAL G 374           
SHEET    7  AK 8 GLU G 406  PRO G 420 -1  O  VAL G 408   N  GLY G 301           
SHEET    8  AK 8 GLN G 350  LEU G 351 -1  N  GLN G 350   O  ILE G 407           
SHEET    1  AL 6 THR H 234  PHE H 236  0                                        
SHEET    2  AL 6 TRP H  34  ASP H  38  1  N  ASP H  38   O  ARG H 235           
SHEET    3  AL 6 ILE H   6  ILE H  13  1  N  VAL H  12   O  MET H  35           
SHEET    4  AL 6 THR H 259  SER H 267  1  O  GLY H 261   N  ILE H   6           
SHEET    5  AL 6 THR H 251  LEU H 254 -1  N  VAL H 252   O  ILE H 260           
SHEET    6  AL 6 VAL H 242  ASN H 246 -1  N  LYS H 244   O  THR H 253           
SHEET    1  AM 5 THR H 234  PHE H 236  0                                        
SHEET    2  AM 5 TRP H  34  ASP H  38  1  N  ASP H  38   O  ARG H 235           
SHEET    3  AM 5 ILE H   6  ILE H  13  1  N  VAL H  12   O  MET H  35           
SHEET    4  AM 5 THR H 259  SER H 267  1  O  GLY H 261   N  ILE H   6           
SHEET    5  AM 5 ILE H 442  SER H 444  1  O  TRP H 443   N  LEU H 265           
SHEET    1  AN 2 ASP H  50  VAL H  51  0                                        
SHEET    2  AN 2 LEU H  57  TYR H  58 -1  O  TYR H  58   N  ASP H  50           
SHEET    1  AO 2 TRP H  86  GLN H  90  0                                        
SHEET    2  AO 2 THR H 209  PRO H 213 -1  O  PHE H 210   N  HIS H  89           
SHEET    1  AP 8 GLN H 100  PRO H 103  0                                        
SHEET    2  AP 8 SER H  93  CYS H  97 -1  N  VAL H  95   O  VAL H 102           
SHEET    3  AP 8 TRP H 315  TYR H 317  1  O  TYR H 317   N  ARG H  96           
SHEET    4  AP 8 ARG H 327  THR H 329 -1  O  ALA H 328   N  LEU H 316           
SHEET    5  AP 8 TYR H 367  GLU H 376 -1  O  MET H 371   N  THR H 329           
SHEET    6  AP 8 TYR H 292  ARG H 303 -1  N  ILE H 298   O  LEU H 372           
SHEET    7  AP 8 GLU H 406  PRO H 420 -1  O  TYR H 411   N  GLY H 299           
SHEET    8  AP 8 GLN H 350  LEU H 351 -1  N  GLN H 350   O  ILE H 407           
SHEET    1  AQ 2 LEU H 346  PRO H 347  0                                        
SHEET    2  AQ 2 ALA H 362  LYS H 363 -1  O  LYS H 363   N  LEU H 346           
CISPEP   1 TYR A  104    PRO A  105          0        -0.43                     
CISPEP   2 GLY A  365    PRO A  366          0         1.45                     
CISPEP   3 TYR B  104    PRO B  105          0        -0.91                     
CISPEP   4 GLY B  365    PRO B  366          0         0.40                     
CISPEP   5 TYR C  104    PRO C  105          0         0.11                     
CISPEP   6 GLY C  365    PRO C  366          0        -1.19                     
CISPEP   7 TYR D  104    PRO D  105          0        -2.14                     
CISPEP   8 GLY D  365    PRO D  366          0        -1.88                     
CISPEP   9 TYR E  104    PRO E  105          0        -2.90                     
CISPEP  10 GLY E  365    PRO E  366          0         1.84                     
CISPEP  11 TYR F  104    PRO F  105          0        -3.53                     
CISPEP  12 GLY F  365    PRO F  366          0        -0.83                     
CISPEP  13 TYR G  104    PRO G  105          0        -3.72                     
CISPEP  14 GLY G  365    PRO G  366          0         0.50                     
CISPEP  15 TYR H  104    PRO H  105          0        -0.44                     
CISPEP  16 GLY H  365    PRO H  366          0        -0.06                     
SITE     1 AC1 16 TYR A 104  PHE A 106  GLN A 107  PHE A 142                    
SITE     2 AC1 16 PHE A 158  MET A 159  ASN A 163  TRP A 167                    
SITE     3 AC1 16 ARG A 182  VAL A 183  TYR A 317  ARG A 327                    
SITE     4 AC1 16 TYR A 419  TYR A 453  HOH A 554  HOH A1052                    
SITE     1 AC2 30 GLY A  14  GLY A  16  PRO A  17  THR A  18                    
SITE     2 AC2 30 ASP A  38  SER A  39  GLY A  45  LEU A  46                    
SITE     3 AC2 30 VAL A  60  GLY A  62  HIS A  63  VAL A  64                    
SITE     4 AC2 30 GLY A 240  LYS A 241  VAL A 242  MET A 269                    
SITE     5 AC2 30 THR A 295  GLU A 373  GLY A 418  TYR A 419                    
SITE     6 AC2 30 GLY A 446  ARG A 447  GLY A 456  ASN A 457                    
SITE     7 AC2 30 GLN A 458  SER A 461  HOH A 653  HOH A 798                    
SITE     8 AC2 30 HOH A 807  HOH A 833                                          
SITE     1 AC3  1 GLN A 358                                                     
SITE     1 AC4  1 ALA A 270                                                     
SITE     1 AC5 17 VAL B  95  TYR B 104  PHE B 106  GLN B 107                    
SITE     2 AC5 17 PHE B 158  MET B 159  ASN B 163  TRP B 167                    
SITE     3 AC5 17 ARG B 182  VAL B 183  TYR B 317  ARG B 327                    
SITE     4 AC5 17 TYR B 419  TYR B 453  HOH B 566  HOH B 936                    
SITE     5 AC5 17 HOH B1053                                                     
SITE     1 AC6 29 GLY B  14  GLY B  16  PRO B  17  THR B  18                    
SITE     2 AC6 29 ASP B  38  SER B  39  GLY B  45  LEU B  46                    
SITE     3 AC6 29 VAL B  60  GLY B  62  HIS B  63  VAL B  64                    
SITE     4 AC6 29 GLY B 240  VAL B 242  THR B 295  GLU B 373                    
SITE     5 AC6 29 GLY B 418  TYR B 419  GLY B 446  ARG B 447                    
SITE     6 AC6 29 GLY B 456  ASN B 457  GLN B 458  SER B 461                    
SITE     7 AC6 29 HOH B 558  HOH B 588  HOH B 605  HOH B 606                    
SITE     8 AC6 29 HOH B 808                                                     
SITE     1 AC7 17 VAL C  95  TYR C 104  PHE C 106  GLN C 107                    
SITE     2 AC7 17 PHE C 158  MET C 159  ASN C 163  TRP C 167                    
SITE     3 AC7 17 ARG C 182  VAL C 183  TYR C 317  ARG C 327                    
SITE     4 AC7 17 TYR C 419  TYR C 453  HOH C 589  HOH C 969                    
SITE     5 AC7 17 HOH C1054                                                     
SITE     1 AC8 25 GLY C  14  GLY C  16  PRO C  17  THR C  18                    
SITE     2 AC8 25 ASP C  38  SER C  39  GLY C  45  LEU C  46                    
SITE     3 AC8 25 VAL C  60  HIS C  63  VAL C  64  GLY C 240                    
SITE     4 AC8 25 VAL C 242  MET C 269  GLU C 373  GLY C 418                    
SITE     5 AC8 25 GLY C 446  ARG C 447  GLY C 456  ASN C 457                    
SITE     6 AC8 25 GLN C 458  SER C 461  HOH C 514  HOH C 519                    
SITE     7 AC8 25 HOH C 619                                                     
SITE     1 AC9  2 GLN C 358  HOH C 618                                          
SITE     1 BC1 16 VAL D  95  TYR D 104  PHE D 106  GLN D 107                    
SITE     2 BC1 16 PHE D 142  PHE D 158  MET D 159  ASN D 163                    
SITE     3 BC1 16 TRP D 167  ARG D 182  VAL D 183  TYR D 317                    
SITE     4 BC1 16 ARG D 327  TYR D 419  TYR D 453  HOH D 546                    
SITE     1 BC2 31 GLY D  14  GLY D  16  PRO D  17  THR D  18                    
SITE     2 BC2 31 ASP D  38  SER D  39  GLY D  45  LEU D  46                    
SITE     3 BC2 31 ALA D  47  VAL D  60  GLY D  62  HIS D  63                    
SITE     4 BC2 31 VAL D  64  GLY D 240  LYS D 241  VAL D 242                    
SITE     5 BC2 31 MET D 269  THR D 295  GLU D 373  GLY D 418                    
SITE     6 BC2 31 TYR D 419  GLY D 446  ARG D 447  GLY D 456                    
SITE     7 BC2 31 ASN D 457  GLN D 458  SER D 461  HOH D 517                    
SITE     8 BC2 31 HOH D 558  HOH D 585  HOH D 799                               
SITE     1 BC3 15 TYR E 104  PHE E 106  GLN E 107  PHE E 158                    
SITE     2 BC3 15 MET E 159  ASN E 163  TRP E 167  ARG E 182                    
SITE     3 BC3 15 VAL E 183  TYR E 317  ARG E 327  TYR E 419                    
SITE     4 BC3 15 TYR E 453  HOH E 547  HOH E 576                               
SITE     1 BC4 29 GLY E  14  GLY E  16  PRO E  17  THR E  18                    
SITE     2 BC4 29 ASP E  38  SER E  39  GLY E  45  LEU E  46                    
SITE     3 BC4 29 VAL E  60  GLY E  62  HIS E  63  VAL E  64                    
SITE     4 BC4 29 GLY E 240  VAL E 242  MET E 269  THR E 295                    
SITE     5 BC4 29 GLU E 373  GLY E 418  TYR E 419  GLY E 446                    
SITE     6 BC4 29 ARG E 447  GLY E 456  ASN E 457  GLN E 458                    
SITE     7 BC4 29 SER E 461  HOH E 517  HOH E 558  HOH E 586                    
SITE     8 BC4 29 HOH E 809                                                     
SITE     1 BC5 16 VAL F  95  TYR F 104  PHE F 106  GLN F 107                    
SITE     2 BC5 16 PHE F 158  MET F 159  ASN F 163  TRP F 167                    
SITE     3 BC5 16 ARG F 182  VAL F 183  TYR F 317  ARG F 327                    
SITE     4 BC5 16 TYR F 419  TYR F 453  HOH F 555  HOH F 564                    
SITE     1 BC6 28 GLY F  14  GLY F  16  PRO F  17  THR F  18                    
SITE     2 BC6 28 ASP F  38  SER F  39  GLY F  45  LEU F  46                    
SITE     3 BC6 28 ALA F  47  VAL F  60  GLY F  62  HIS F  63                    
SITE     4 BC6 28 VAL F  64  GLY F 240  VAL F 242  MET F 269                    
SITE     5 BC6 28 THR F 295  GLU F 373  GLY F 418  TYR F 419                    
SITE     6 BC6 28 GLY F 446  ARG F 447  GLY F 456  ASN F 457                    
SITE     7 BC6 28 GLN F 458  SER F 461  HOH F 513  HOH F 515                    
SITE     1 BC7  1 GLN F 358                                                     
SITE     1 BC8  1 ALA F 270                                                     
SITE     1 BC9 14 TYR G 104  PHE G 106  GLN G 107  PHE G 158                    
SITE     2 BC9 14 MET G 159  ASN G 163  TRP G 167  ARG G 182                    
SITE     3 BC9 14 VAL G 183  TYR G 317  ARG G 327  TYR G 419                    
SITE     4 BC9 14 TYR G 453  HOH G1049                                          
SITE     1 CC1 29 GLY G  14  GLY G  16  PRO G  17  THR G  18                    
SITE     2 CC1 29 ASP G  38  SER G  39  GLY G  45  LEU G  46                    
SITE     3 CC1 29 ALA G  47  VAL G  60  HIS G  63  VAL G  64                    
SITE     4 CC1 29 GLY G 240  LYS G 241  VAL G 242  MET G 269                    
SITE     5 CC1 29 THR G 295  GLU G 373  GLY G 418  TYR G 419                    
SITE     6 CC1 29 GLY G 446  ARG G 447  GLY G 456  ASN G 457                    
SITE     7 CC1 29 GLN G 458  SER G 461  HOH G 512  HOH G 554                    
SITE     8 CC1 29 HOH G 556                                                     
SITE     1 CC2 15 VAL H  95  TYR H 104  PHE H 106  GLN H 107                    
SITE     2 CC2 15 PHE H 158  MET H 159  ASN H 163  TRP H 167                    
SITE     3 CC2 15 ARG H 182  VAL H 183  TYR H 317  ARG H 327                    
SITE     4 CC2 15 TYR H 419  TYR H 453  HOH H 875                               
SITE     1 CC3 27 GLY H  14  GLY H  16  PRO H  17  THR H  18                    
SITE     2 CC3 27 ASP H  38  SER H  39  GLY H  45  LEU H  46                    
SITE     3 CC3 27 VAL H  60  GLY H  62  HIS H  63  VAL H  64                    
SITE     4 CC3 27 GLY H 240  VAL H 242  MET H 269  THR H 295                    
SITE     5 CC3 27 GLU H 373  GLY H 418  TYR H 419  GLY H 446                    
SITE     6 CC3 27 ARG H 447  GLY H 456  ASN H 457  GLN H 458                    
SITE     7 CC3 27 SER H 461  HOH H 806  HOH H 810                               
SITE     1 CC4  1 GLN H 358                                                     
CRYST1   71.440  129.200  172.820  90.07  84.22  82.24 P 1           8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013998 -0.001907 -0.001446        0.00000                         
SCALE2      0.000000  0.007811  0.000117        0.00000                         
SCALE3      0.000000  0.000000  0.005817        0.00000                         
MTRIX1   1 -0.979090  0.001222  0.203423       36.90060    1                    
MTRIX2   1 -0.081816 -0.917906 -0.388271       61.17880    1                    
MTRIX3   1  0.186248 -0.396795  0.898813        9.11182    1                    
MTRIX1   2 -0.964122  0.264699 -0.020057      -15.26790    1                    
MTRIX2   2  0.264773  0.964310 -0.001090      -63.38590    1                    
MTRIX3   2  0.019052 -0.006361 -0.999798      -35.45130    1                    
MTRIX1   3  0.941516 -0.254810 -0.220497       12.87460    1                    
MTRIX2   3 -0.254864 -0.966551  0.028701       56.56320    1                    
MTRIX3   3 -0.220435  0.029174 -0.974965       49.72250    1                    
MTRIX1   4  0.999941  0.001828  0.010696       31.63910    1                    
MTRIX2   4  0.002285  0.928161 -0.372172      -84.80250    1                    
MTRIX3   4 -0.010608  0.372174  0.928102       42.95640    1                    
MTRIX1   5 -0.965160  0.260191  0.027679       33.72860    1                    
MTRIX2   5  0.251940  0.895533  0.366806      -11.12920    1                    
MTRIX3   5  0.070653  0.360999 -0.929886       34.10220    1                    
MTRIX1   6  0.947826 -0.263300 -0.179721       27.81470    1                    
MTRIX2   6 -0.178165 -0.905015  0.386270       15.12450    1                    
MTRIX3   6 -0.264355 -0.334096 -0.904708      -48.50650    1                    
MTRIX1   7 -0.978944  0.003155  0.204106        6.53731    1                    
MTRIX2   7 -0.009579 -0.999489 -0.030490       -8.02302    1                    
MTRIX3   7  0.203905 -0.031803  0.978474       86.22690    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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