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Database: PDB
Entry: 2ATI
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HEADER    TRANSFERASE                             25-AUG-05   2ATI              
TITLE     GLYCOGEN PHOSPHORYLASE INHIBITORS                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOGEN PHOSPHORYLASE, LIVER FORM;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: LIVER GLYCOGEN PHOSPHORYLASE A;                             
COMPND   5 EC: 2.4.1.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    GLYCOGEN PHOSPHORYLASE, TRANSFERASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.KLABUNDE,K.U.WENDT,D.KADEREIT,V.BRACHVOGEL,H.J.BURGER,A.W.HERLING,  
AUTHOR   2 N.G.OIKONOMAKOS,D.SCHMOLL,E.SARUBBI,E.VON ROEDERN,K.SCHOENAFINGER,   
AUTHOR   3 E.DEFOSSA                                                            
REVDAT   3   13-JUL-11 2ATI    1       VERSN                                    
REVDAT   2   24-FEB-09 2ATI    1       VERSN                                    
REVDAT   1   25-AUG-06 2ATI    0                                                
JRNL        AUTH   T.KLABUNDE,K.U.WENDT,D.KADEREIT,V.BRACHVOGEL,H.J.BURGER,     
JRNL        AUTH 2 A.W.HERLING,N.G.OIKONOMAKOS,M.N.KOSMOPOULOU,D.SCHMOLL,       
JRNL        AUTH 3 E.SARUBBI,E.VON ROEDERN,E.DEFOSSA                            
JRNL        TITL   ACYL UREAS AS HUMAN LIVER GLYCOGEN PHOSPHORYLASE INHIBITORS  
JRNL        TITL 2 FOR THE TREATMENT OF TYPE 2 DIABETES.                        
JRNL        REF    J.MED.CHEM.                   V.  48  6178 2005              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   16190745                                                     
JRNL        DOI    10.1021/JM049034Y                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   N.G.OIKONOMAKOS,M.N.KOSMOPOULOU,E.D.CHRYSINA,D.D.LEONIDAS,   
REMARK   1  AUTH 2 I.D.KOSTAS,K.U.WENDT,T.KLABUNDE,E.DEFOSSA                    
REMARK   1  TITL   CRYSTALLOGRAPHIC STUDIES ON ACYL UREAS, A NEW CLASS OF       
REMARK   1  TITL 2 GLYCOGEN PHOSPHORYLASE INHIBITORS, AS POTENTIAL ANTIDIABETIC 
REMARK   1  TITL 3 DRUGS                                                        
REMARK   1  REF    PROTEIN SCI.                  V.  14  1760 2005              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   1  PMID   15987904                                                     
REMARK   1  DOI    10.1110/PS.051432405                                         
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   V.L.RATH,M.AMMIRATI,P.K.LEMOTTE,K.F.FENNELL,M.N.MANSOUR,     
REMARK   1  AUTH 2 D.E.DANLEY,T.R.HYNES,G.K.SCHULTE,D.J.WASILKO,J.PANDIT        
REMARK   1  TITL   ACTIVATION OF HUMAN LIVER GLYCOGEN PHOSPHORYLASE BY          
REMARK   1  TITL 2 ALTERATION OF THE SECONDARY STRUCTURE AND PACKING OF THE     
REMARK   1  TITL 3 CATALYTIC CORE                                               
REMARK   1  REF    MOL.CELL                      V.   6   139 2000              
REMARK   1  REFN                   ISSN 1097-2765                               
REMARK   1  PMID   10949035                                                     
REMARK   1  DOI    10.1016/S1097-2765(00)00015-0                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 167664                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 8384                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 167664               
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12842                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 759                                     
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ATI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-AUG-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB034292.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 167664                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 500.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.06667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       82.13333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 57060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     ARG A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     ILE A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     ILE A    15                                                      
REMARK 465     ARG A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     ILE A    18                                                      
REMARK 465     VAL A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     VAL A    21                                                      
REMARK 465     GLU A    22                                                      
REMARK 465     ASN A   250                                                      
REMARK 465     ASP A   251                                                      
REMARK 465     PHE A   252                                                      
REMARK 465     ASN A   253                                                      
REMARK 465     LEU A   254                                                      
REMARK 465     ARG A   255                                                      
REMARK 465     ASP A   256                                                      
REMARK 465     PHE A   257                                                      
REMARK 465     ASN A   258                                                      
REMARK 465     VAL A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   317                                                      
REMARK 465     SER A   318                                                      
REMARK 465     THR A   319                                                      
REMARK 465     ARG A   320                                                      
REMARK 465     GLY A   321                                                      
REMARK 465     ALA A   322                                                      
REMARK 465     GLY A   323                                                      
REMARK 465     LEU A   832                                                      
REMARK 465     LYS A   833                                                      
REMARK 465     ILE A   834                                                      
REMARK 465     SER A   835                                                      
REMARK 465     LEU A   836                                                      
REMARK 465     SER A   837                                                      
REMARK 465     ASN A   838                                                      
REMARK 465     GLU A   839                                                      
REMARK 465     SER A   840                                                      
REMARK 465     ASN A   841                                                      
REMARK 465     LYS A   842                                                      
REMARK 465     VAL A   843                                                      
REMARK 465     ASN A   844                                                      
REMARK 465     GLY A   845                                                      
REMARK 465     ASN A   846                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     LYS B     9                                                      
REMARK 465     ARG B    10                                                      
REMARK 465     ARG B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     ILE B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     ILE B    15                                                      
REMARK 465     ARG B    16                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     ILE B    18                                                      
REMARK 465     VAL B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     VAL B    21                                                      
REMARK 465     GLU B    22                                                      
REMARK 465     ASN B   250                                                      
REMARK 465     ASP B   251                                                      
REMARK 465     PHE B   252                                                      
REMARK 465     ASN B   253                                                      
REMARK 465     LEU B   254                                                      
REMARK 465     ARG B   255                                                      
REMARK 465     ASP B   256                                                      
REMARK 465     PHE B   257                                                      
REMARK 465     ASN B   258                                                      
REMARK 465     VAL B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   317                                                      
REMARK 465     SER B   318                                                      
REMARK 465     THR B   319                                                      
REMARK 465     ARG B   320                                                      
REMARK 465     GLY B   321                                                      
REMARK 465     ALA B   322                                                      
REMARK 465     GLY B   323                                                      
REMARK 465     LEU B   832                                                      
REMARK 465     LYS B   833                                                      
REMARK 465     ILE B   834                                                      
REMARK 465     SER B   835                                                      
REMARK 465     LEU B   836                                                      
REMARK 465     SER B   837                                                      
REMARK 465     ASN B   838                                                      
REMARK 465     GLU B   839                                                      
REMARK 465     SER B   840                                                      
REMARK 465     ASN B   841                                                      
REMARK 465     LYS B   842                                                      
REMARK 465     VAL B   843                                                      
REMARK 465     ASN B   844                                                      
REMARK 465     GLY B   845                                                      
REMARK 465     ASN B   846                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 136   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A 131       38.86    -92.70                                   
REMARK 500    TYR A 203     -132.89     58.92                                   
REMARK 500    PRO A 281       27.19    -70.31                                   
REMARK 500    VAL A 325      -12.40     42.60                                   
REMARK 500    ASP A 339     -168.66     73.66                                   
REMARK 500    VAL A 379      -40.95   -131.40                                   
REMARK 500    LEU A 492      -68.22   -152.69                                   
REMARK 500    ILE A 666       30.21    -99.14                                   
REMARK 500    SER A 674      -69.71   -148.89                                   
REMARK 500    PHE A 709       73.66   -103.22                                   
REMARK 500    SER A 751       76.87   -150.38                                   
REMARK 500    LYS A 772       61.77     27.90                                   
REMARK 500    LEU B 131       40.10    -89.78                                   
REMARK 500    PHE B 166      150.02    -49.20                                   
REMARK 500    ARG B 193       76.79   -119.84                                   
REMARK 500    TYR B 203     -132.51     57.84                                   
REMARK 500    PRO B 281       31.81    -72.62                                   
REMARK 500    ASP B 339     -175.51     75.05                                   
REMARK 500    LYS B 466      -73.07   -118.16                                   
REMARK 500    LEU B 492      -65.96   -153.40                                   
REMARK 500    SER B 674      -64.75   -149.78                                   
REMARK 500    PHE B 709       78.28   -101.63                                   
REMARK 500    LYS B 772       62.24     36.02                                   
REMARK 500    ILE B 824      -57.58   -121.56                                   
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    TYR A  52         0.07    SIDE CHAIN                              
REMARK 500    TYR B  52         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A 325        22.3      L          L   OUTSIDE RANGE           
REMARK 500    TRP A 491        24.9      L          L   OUTSIDE RANGE           
REMARK 500    THR B  94        24.0      L          L   OUTSIDE RANGE           
REMARK 500    TRP B 491        24.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2493        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH A2637        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH A2736        DISTANCE =  7.40 ANGSTROMS                       
REMARK 525    HOH A2775        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A2834        DISTANCE =  5.61 ANGSTROMS                       
REMARK 525    HOH B2844        DISTANCE =  5.88 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 847                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 847                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IHU A 848                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IHU B 848                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 1001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1WUT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1WUY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1WV0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1WV1   RELATED DB: PDB                                   
DBREF  2ATI A    1   846  UNP    P06737   PYGL_HUMAN       1    846             
DBREF  2ATI B    1   846  UNP    P06737   PYGL_HUMAN       1    846             
SEQRES   1 A  846  ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN ILE          
SEQRES   2 A  846  SER ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA GLU          
SEQRES   3 A  846  LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR LEU          
SEQRES   4 A  846  VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR TYR          
SEQRES   5 A  846  PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY          
SEQRES   6 A  846  ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS CYS          
SEQRES   7 A  846  PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR MET          
SEQRES   8 A  846  GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY LEU          
SEQRES   9 A  846  GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY LEU          
SEQRES  10 A  846  ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY          
SEQRES  11 A  846  LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE          
SEQRES  12 A  846  LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY          
SEQRES  13 A  846  TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN LYS          
SEQRES  14 A  846  ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP TRP          
SEQRES  15 A  846  LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO GLU          
SEQRES  16 A  846  PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU HIS          
SEQRES  17 A  846  THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL VAL          
SEQRES  18 A  846  LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR MET          
SEQRES  19 A  846  ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA ARG          
SEQRES  20 A  846  ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL GLY          
SEQRES  21 A  846  ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU          
SEQRES  22 A  846  ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE          
SEQRES  23 A  846  GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL          
SEQRES  24 A  846  VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS          
SEQRES  25 A  846  ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY THR VAL          
SEQRES  26 A  846  PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU ASN          
SEQRES  27 A  846  ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET ARG          
SEQRES  28 A  846  ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS ALA          
SEQRES  29 A  846  TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN HIS          
SEQRES  30 A  846  THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL ASP          
SEQRES  31 A  846  LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE ILE          
SEQRES  32 A  846  TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL ALA          
SEQRES  33 A  846  LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET SER          
SEQRES  34 A  846  LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET ALA          
SEQRES  35 A  846  HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY VAL          
SEQRES  36 A  846  ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL PHE          
SEQRES  37 A  846  LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN ASN          
SEQRES  38 A  846  LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU LEU          
SEQRES  39 A  846  CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS ILE          
SEQRES  40 A  846  GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR LYS          
SEQRES  41 A  846  LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG GLU          
SEQRES  42 A  846  LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE SER          
SEQRES  43 A  846  GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN PRO          
SEQRES  44 A  846  SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU          
SEQRES  45 A  846  TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR          
SEQRES  46 A  846  MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU PHE          
SEQRES  47 A  846  VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA PRO          
SEQRES  48 A  846  GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR          
SEQRES  49 A  846  SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL GLY          
SEQRES  50 A  846  SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG VAL          
SEQRES  51 A  846  SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU SER          
SEQRES  52 A  846  GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR          
SEQRES  53 A  846  GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE          
SEQRES  54 A  846  GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU          
SEQRES  55 A  846  ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG ILE          
SEQRES  56 A  846  ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU ALA          
SEQRES  57 A  846  LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU VAL          
SEQRES  58 A  846  ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS GLN          
SEQRES  59 A  846  PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE TYR          
SEQRES  60 A  846  HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA TYR          
SEQRES  61 A  846  VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET ASN          
SEQRES  62 A  846  PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE ALA          
SEQRES  63 A  846  ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS GLU          
SEQRES  64 A  846  TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP LEU          
SEQRES  65 A  846  LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN GLY          
SEQRES  66 A  846  ASN                                                          
SEQRES   1 B  846  ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN ILE          
SEQRES   2 B  846  SER ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA GLU          
SEQRES   3 B  846  LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR LEU          
SEQRES   4 B  846  VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR TYR          
SEQRES   5 B  846  PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY          
SEQRES   6 B  846  ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS CYS          
SEQRES   7 B  846  PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR MET          
SEQRES   8 B  846  GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY LEU          
SEQRES   9 B  846  GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY LEU          
SEQRES  10 B  846  ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY          
SEQRES  11 B  846  LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE          
SEQRES  12 B  846  LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY          
SEQRES  13 B  846  TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN LYS          
SEQRES  14 B  846  ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP TRP          
SEQRES  15 B  846  LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO GLU          
SEQRES  16 B  846  PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU HIS          
SEQRES  17 B  846  THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL VAL          
SEQRES  18 B  846  LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR MET          
SEQRES  19 B  846  ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA ARG          
SEQRES  20 B  846  ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL GLY          
SEQRES  21 B  846  ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU          
SEQRES  22 B  846  ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE          
SEQRES  23 B  846  GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL          
SEQRES  24 B  846  VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS          
SEQRES  25 B  846  ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY THR VAL          
SEQRES  26 B  846  PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU ASN          
SEQRES  27 B  846  ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET ARG          
SEQRES  28 B  846  ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS ALA          
SEQRES  29 B  846  TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN HIS          
SEQRES  30 B  846  THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL ASP          
SEQRES  31 B  846  LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE ILE          
SEQRES  32 B  846  TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL ALA          
SEQRES  33 B  846  LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET SER          
SEQRES  34 B  846  LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET ALA          
SEQRES  35 B  846  HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY VAL          
SEQRES  36 B  846  ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL PHE          
SEQRES  37 B  846  LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN ASN          
SEQRES  38 B  846  LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU LEU          
SEQRES  39 B  846  CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS ILE          
SEQRES  40 B  846  GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR LYS          
SEQRES  41 B  846  LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG GLU          
SEQRES  42 B  846  LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE SER          
SEQRES  43 B  846  GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN PRO          
SEQRES  44 B  846  SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU          
SEQRES  45 B  846  TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR          
SEQRES  46 B  846  MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU PHE          
SEQRES  47 B  846  VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA PRO          
SEQRES  48 B  846  GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR          
SEQRES  49 B  846  SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL GLY          
SEQRES  50 B  846  SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG VAL          
SEQRES  51 B  846  SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU SER          
SEQRES  52 B  846  GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR          
SEQRES  53 B  846  GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE          
SEQRES  54 B  846  GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU          
SEQRES  55 B  846  ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG ILE          
SEQRES  56 B  846  ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU ALA          
SEQRES  57 B  846  LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU VAL          
SEQRES  58 B  846  ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS GLN          
SEQRES  59 B  846  PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE TYR          
SEQRES  60 B  846  HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA TYR          
SEQRES  61 B  846  VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET ASN          
SEQRES  62 B  846  PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE ALA          
SEQRES  63 B  846  ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS GLU          
SEQRES  64 B  846  TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP LEU          
SEQRES  65 B  846  LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN GLY          
SEQRES  66 B  846  ASN                                                          
HET    GLC  A 847      12                                                       
HET    GLC  B 847      12                                                       
HET    IHU  A 848      23                                                       
HET    IHU  B 848      23                                                       
HET    PLP  A1001      15                                                       
HET    PLP  B1001      15                                                       
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     IHU N-(2-CHLORO-4-FLUOROBENZOYL)-N'-(5-HYDROXY-2-                    
HETNAM   2 IHU  METHOXYPHENYL)UREA                                              
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETSYN     IHU 1-(2-CHLORO-4-FLUORO-BENZOYL)-3-(5-HYDROXY-2-METHOXY-            
HETSYN   2 IHU  PHENYL)-UREA                                                    
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   3  GLC    2(C6 H12 O6)                                                 
FORMUL   5  IHU    2(C15 H12 CL F N2 O4)                                        
FORMUL   7  PLP    2(C8 H10 N O6 P)                                             
FORMUL   9  HOH   *759(H2 O)                                                    
HELIX    1   1 ASN A   23  THR A   38  1                                  16    
HELIX    2   2 THR A   47  HIS A   62  1                                  16    
HELIX    3   3 LEU A   63  CYS A   78  1                                  16    
HELIX    4   4 THR A   94  LEU A  102  1                                   9    
HELIX    5   5 LEU A  104  LEU A  115  1                                  12    
HELIX    6   6 ASP A  118  GLU A  124  1                                   7    
HELIX    7   7 GLY A  134  LEU A  150  1                                  17    
HELIX    8   8 PRO A  194  MET A  197  5                                   4    
HELIX    9   9 ASP A  261  ASP A  268  1                                   8    
HELIX   10  10 ARG A  269  ASN A  274  1                                   6    
HELIX   11  11 ILE A  275  ARG A  277  5                                   3    
HELIX   12  12 LYS A  289  SER A  314  1                                  26    
HELIX   13  13 ALA A  328  ASP A  331  5                                   4    
HELIX   14  14 LEU A  344  ILE A  356  1                                  13    
HELIX   15  15 PRO A  360  THR A  371  1                                  12    
HELIX   16  16 LEU A  380  LEU A  384  5                                   5    
HELIX   17  17 VAL A  389  LEU A  396  1                                   8    
HELIX   18  18 LEU A  396  PHE A  418  1                                  23    
HELIX   19  19 ASP A  421  SER A  429  1                                   9    
HELIX   20  20 MET A  441  GLY A  448  1                                   8    
HELIX   21  21 ALA A  456  LYS A  466  1                                  11    
HELIX   22  22 PHE A  468  GLU A  473  1                                   6    
HELIX   23  23 ASN A  496  GLY A  508  1                                  13    
HELIX   24  24 GLU A  509  LYS A  513  5                                   5    
HELIX   25  25 ASP A  514  LEU A  525  5                                  12    
HELIX   26  26 ASP A  527  TYR A  553  1                                  27    
HELIX   27  27 ARG A  575  ASP A  593  1                                  19    
HELIX   28  28 TYR A  613  ASN A  632  1                                  20    
HELIX   29  29 VAL A  636  SER A  638  5                                   3    
HELIX   30  30 ARG A  649  ILE A  657  1                                   9    
HELIX   31  31 PRO A  658  THR A  660  5                                   3    
HELIX   32  32 THR A  676  ASN A  684  1                                   9    
HELIX   33  33 ALA A  695  GLY A  704  1                                  10    
HELIX   34  34 GLU A  705  LEU A  708  5                                   4    
HELIX   35  35 ARG A  714  GLY A  725  1                                  12    
HELIX   36  36 GLU A  727  LEU A  735  1                                   9    
HELIX   37  37 LEU A  735  ASN A  747  1                                  13    
HELIX   38  38 PHE A  758  HIS A  768  1                                  11    
HELIX   39  39 LYS A  772  MET A  792  1                                  21    
HELIX   40  40 ASN A  793  ALA A  807  1                                  15    
HELIX   41  41 SER A  808  PHE A  811  5                                   4    
HELIX   42  42 SER A  812  ILE A  824  1                                  13    
HELIX   43  43 ASN B   23  THR B   38  1                                  16    
HELIX   44  44 THR B   47  HIS B   62  1                                  16    
HELIX   45  45 LEU B   63  CYS B   78  1                                  16    
HELIX   46  46 THR B   94  LEU B  102  1                                   9    
HELIX   47  47 LEU B  104  LEU B  115  1                                  12    
HELIX   48  48 ASP B  118  GLU B  124  1                                   7    
HELIX   49  49 GLY B  134  LEU B  150  1                                  17    
HELIX   50  50 PRO B  194  MET B  197  5                                   4    
HELIX   51  51 ASP B  261  ASP B  268  1                                   8    
HELIX   52  52 ARG B  269  ASN B  274  1                                   6    
HELIX   53  53 ILE B  275  ARG B  277  5                                   3    
HELIX   54  54 LYS B  289  SER B  314  1                                  26    
HELIX   55  55 ALA B  328  GLN B  332  1                                   5    
HELIX   56  56 LEU B  344  ILE B  356  1                                  13    
HELIX   57  57 PRO B  360  THR B  371  1                                  12    
HELIX   58  58 LEU B  380  LEU B  384  5                                   5    
HELIX   59  59 VAL B  389  LEU B  396  1                                   8    
HELIX   60  60 LEU B  396  PHE B  418  1                                  23    
HELIX   61  61 VAL B  422  SER B  429  1                                   8    
HELIX   62  62 MET B  441  GLY B  448  1                                   8    
HELIX   63  63 ALA B  456  LYS B  466  1                                  11    
HELIX   64  64 PHE B  468  GLU B  475  1                                   8    
HELIX   65  65 ASN B  496  GLY B  508  1                                  13    
HELIX   66  66 GLU B  509  VAL B  512  5                                   4    
HELIX   67  67 ASP B  514  LEU B  525  5                                  12    
HELIX   68  68 ASP B  527  TYR B  553  1                                  27    
HELIX   69  69 ARG B  575  ASP B  593  1                                  19    
HELIX   70  70 TYR B  613  ASN B  632  1                                  20    
HELIX   71  71 VAL B  636  SER B  638  5                                   3    
HELIX   72  72 ARG B  649  ILE B  657  1                                   9    
HELIX   73  73 PRO B  658  THR B  660  5                                   3    
HELIX   74  74 THR B  676  ASN B  684  1                                   9    
HELIX   75  75 ALA B  695  GLY B  704  1                                  10    
HELIX   76  76 GLU B  705  LEU B  708  5                                   4    
HELIX   77  77 ARG B  714  GLY B  725  1                                  12    
HELIX   78  78 ALA B  728  LEU B  735  1                                   8    
HELIX   79  79 LEU B  735  GLY B  748  1                                  14    
HELIX   80  80 PHE B  758  HIS B  768  1                                  11    
HELIX   81  81 ASP B  776  MET B  792  1                                  17    
HELIX   82  82 ASN B  793  ALA B  806  1                                  14    
HELIX   83  83 SER B  808  PHE B  811  5                                   4    
HELIX   84  84 SER B  812  ILE B  824  1                                  13    
SHEET    1   A 3 LYS A 191  SER A 192  0                                        
SHEET    2   A 3 GLN A 219  PRO A 231 -1  O  ASP A 227   N  LYS A 191           
SHEET    3   A 3 LEU A 198  PHE A 202 -1  N  PHE A 202   O  GLN A 219           
SHEET    1   B 9 LYS A 191  SER A 192  0                                        
SHEET    2   B 9 GLN A 219  PRO A 231 -1  O  ASP A 227   N  LYS A 191           
SHEET    3   B 9 VAL A 238  ARG A 247 -1  O  LEU A 243   N  TYR A 226           
SHEET    4   B 9 ALA A 154  ILE A 159  1  N  GLY A 156   O  ARG A 242           
SHEET    5   B 9 ARG A  81  LEU A  85  1  N  TYR A  84   O  TYR A 155           
SHEET    6   B 9 VAL A 333  ASN A 338  1  O  ALA A 334   N  TYR A  83           
SHEET    7   B 9 PHE A 372  THR A 375  1  O  ALA A 373   N  LEU A 337           
SHEET    8   B 9 ALA A 451  GLY A 454  1  O  ALA A 451   N  TYR A 374           
SHEET    9   B 9 PHE A 479  ASN A 481  1  O  GLN A 480   N  VAL A 452           
SHEET    1   C 2 PHE A  89  GLY A  92  0                                        
SHEET    2   C 2 ALA A 129  LEU A 131 -1  O  LEU A 131   N  PHE A  89           
SHEET    1   D 2 ASN A 167  ARG A 171  0                                        
SHEET    2   D 2 TRP A 174  GLU A 178 -1  O  GLU A 178   N  ASN A 167           
SHEET    1   E 2 LYS A 205  THR A 209  0                                        
SHEET    2   E 2 GLY A 212  ILE A 216 -1  O  LYS A 214   N  GLU A 207           
SHEET    1   F 3 ARG A 386  PRO A 388  0                                        
SHEET    2   F 3 ARG A 438  ASN A 440 -1  O  ILE A 439   N  TRP A 387           
SHEET    3   F 3 ILE A 431  GLU A 432 -1  N  GLU A 432   O  ARG A 438           
SHEET    1   G 6 LEU A 640  LEU A 645  0                                        
SHEET    2   G 6 ARG A 601  GLY A 606  1  N  VAL A 603   O  LYS A 641           
SHEET    3   G 6 MET A 562  VAL A 567  1  N  ASP A 564   O  ILE A 604           
SHEET    4   G 6 LEU A 662  GLN A 665  1  O  LEU A 662   N  VAL A 565           
SHEET    5   G 6 LEU A 687  GLY A 690  1  O  LEU A 687   N  SER A 663           
SHEET    6   G 6 PHE A 709  ILE A 710  1  O  PHE A 709   N  THR A 688           
SHEET    1   H 3 LYS B 191  SER B 192  0                                        
SHEET    2   H 3 GLN B 219  PRO B 231 -1  O  ASP B 227   N  LYS B 191           
SHEET    3   H 3 LEU B 198  PHE B 202 -1  N  PHE B 202   O  GLN B 219           
SHEET    1   I 9 LYS B 191  SER B 192  0                                        
SHEET    2   I 9 GLN B 219  PRO B 231 -1  O  ASP B 227   N  LYS B 191           
SHEET    3   I 9 VAL B 238  ARG B 247 -1  O  SER B 245   N  LEU B 224           
SHEET    4   I 9 ALA B 154  ILE B 159  1  N  GLY B 156   O  ARG B 242           
SHEET    5   I 9 ARG B  81  LEU B  85  1  N  TYR B  84   O  TYR B 155           
SHEET    6   I 9 VAL B 333  ASN B 338  1  O  ALA B 334   N  TYR B  83           
SHEET    7   I 9 PHE B 372  THR B 375  1  O  ALA B 373   N  LEU B 337           
SHEET    8   I 9 ALA B 451  GLY B 454  1  O  ASN B 453   N  TYR B 374           
SHEET    9   I 9 PHE B 479  ASN B 481  1  O  GLN B 480   N  VAL B 452           
SHEET    1   J 2 PHE B  89  GLY B  92  0                                        
SHEET    2   J 2 ALA B 129  LEU B 131 -1  O  LEU B 131   N  PHE B  89           
SHEET    1   K 2 ASN B 167  ARG B 171  0                                        
SHEET    2   K 2 TRP B 174  GLU B 178 -1  O  TRP B 174   N  ARG B 171           
SHEET    1   L 2 LYS B 205  THR B 209  0                                        
SHEET    2   L 2 GLY B 212  ILE B 216 -1  O  ILE B 216   N  LYS B 205           
SHEET    1   M 3 ARG B 386  PRO B 388  0                                        
SHEET    2   M 3 ARG B 438  ASN B 440 -1  O  ILE B 439   N  TRP B 387           
SHEET    3   M 3 ILE B 431  GLU B 432 -1  N  GLU B 432   O  ARG B 438           
SHEET    1   N 6 LEU B 640  LEU B 645  0                                        
SHEET    2   N 6 ARG B 601  GLY B 606  1  N  VAL B 603   O  ILE B 643           
SHEET    3   N 6 MET B 562  VAL B 567  1  N  ASP B 564   O  ILE B 604           
SHEET    4   N 6 LEU B 662  GLN B 665  1  O  LEU B 662   N  PHE B 563           
SHEET    5   N 6 LEU B 687  GLY B 690  1  O  LEU B 687   N  SER B 663           
SHEET    6   N 6 PHE B 709  ILE B 710  1  O  PHE B 709   N  THR B 688           
LINK         C4A PLP A1001                 NZ  LYS A 680     1555   1555  1.29  
LINK         C4A PLP B1001                 NZ  LYS B 680     1555   1555  1.29  
SITE     1 AC1 13 GLY A 135  LEU A 136  ASN A 284  HIS A 377                    
SITE     2 AC1 13 VAL A 455  ASN A 484  TYR A 573  GLU A 672                    
SITE     3 AC1 13 ALA A 673  SER A 674  GLY A 675  HOH A2111                    
SITE     4 AC1 13 HOH A2361                                                     
SITE     1 AC2 16 GLY B 135  LEU B 136  LEU B 139  ASN B 284                    
SITE     2 AC2 16 HIS B 377  VAL B 455  ASN B 484  TYR B 573                    
SITE     3 AC2 16 GLU B 672  ALA B 673  SER B 674  GLY B 675                    
SITE     4 AC2 16 HOH B2039  HOH B2318  HOH B2339  HOH B2829                    
SITE     1 AC3 11 VAL A  40  ASP A  42  ASN A  44  VAL A  45                    
SITE     2 AC3 11 HOH A2141  TRP B  67  ILE B  68  GLN B  71                    
SITE     3 AC3 11 GLN B  72  LYS B 191  ARG B 193                               
SITE     1 AC4 12 TRP A  67  ILE A  68  GLN A  71  GLN A  72                    
SITE     2 AC4 12 LYS A 191  ARG A 193  VAL B  40  LYS B  41                    
SITE     3 AC4 12 ASP B  42  ASN B  44  VAL B  45  HOH B2232                    
SITE     1 AC5 17 TYR A  90  TRP A 491  LYS A 568  LYS A 574                    
SITE     2 AC5 17 TYR A 648  ARG A 649  VAL A 650  ALA A 653                    
SITE     3 AC5 17 GLY A 675  THR A 676  GLY A 677  LYS A 680                    
SITE     4 AC5 17 HOH A2013  HOH A2098  HOH A2130  HOH A2170                    
SITE     5 AC5 17 HOH A2264                                                     
SITE     1 AC6 19 TYR B  90  GLY B 135  TRP B 491  LYS B 568                    
SITE     2 AC6 19 LYS B 574  TYR B 648  ARG B 649  VAL B 650                    
SITE     3 AC6 19 GLY B 675  THR B 676  GLY B 677  LYS B 680                    
SITE     4 AC6 19 HOH B2039  HOH B2085  HOH B2117  HOH B2136                    
SITE     5 AC6 19 HOH B2159  HOH B2188  HOH B2468                               
CRYST1  124.500  124.500  123.200  90.00  90.00 120.00 P 31          6          
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      0.008032  0.004637  0.000000        0.00000                         
SCALE2      0.000000  0.009275  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008117        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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