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Database: PDB
Entry: 1L5Q
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Original site: 1L5Q 
HEADER    TRANSFERASE                             07-MAR-02   1L5Q              
TITLE     HUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH CAFFEINE, N-      
TITLE    2 ACETYL-BETA-D-GLUCOPYRANOSYLAMINE, AND CP-403700                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOGEN PHOSPHORYLASE, LIVER FORM;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 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 ORGAN: LIVER;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PHOSPHORYLASE, PURINE SITE, TRANSFERASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.L.EKSTROM,T.A.PAULY,M.D.CARTY,W.C.SOELLER,J.CULP,D.E.DANLEY,        
AUTHOR   2 D.J.HOOVER,J.L.TREADWAY,E.M.GIBBS,R.J.FLETTERICK,Y.S.N.DAY,          
AUTHOR   3 D.G.MYSZKA,V.L.RATH                                                  
REVDAT   4   02-MAY-12 1L5Q    1       COMPND                                   
REVDAT   3   13-JUL-11 1L5Q    1       VERSN                                    
REVDAT   2   24-FEB-09 1L5Q    1       VERSN                                    
REVDAT   1   04-DEC-02 1L5Q    0                                                
JRNL        AUTH   J.L.EKSTROM,T.A.PAULY,M.D.CARTY,W.C.SOELLER,J.CULP,          
JRNL        AUTH 2 D.E.DANLEY,D.J.HOOVER,J.L.TREADWAY,E.M.GIBBS,R.J.FLETTERICK, 
JRNL        AUTH 3 Y.S.DAY,D.G.MYSZKA,V.L.RATH                                  
JRNL        TITL   STRUCTURE-ACTIVITY ANALYSIS OF THE PURINE BINDING SITE OF    
JRNL        TITL 2 HUMAN LIVER GLYCOGEN PHOSPHORYLASE.                          
JRNL        REF    CHEM.BIOL.                    V.   9   915 2002              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   12204691                                                     
JRNL        DOI    10.1016/S1074-5521(02)00186-2                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 96040.410                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 91682                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 9197                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.39                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 11459                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2890                       
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.40                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1332                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.009                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12837                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 176                                     
REMARK   3   SOLVENT ATOMS            : 607                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.11000                                              
REMARK   3    B22 (A**2) : 0.11000                                              
REMARK   3    B33 (A**2) : -0.21000                                             
REMARK   3    B12 (A**2) : 2.22000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.27                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.36                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.32                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.37                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.200 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.910 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.870 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.750 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.32                                                 
REMARK   3   BSOL        : 45.28                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ALL.PAR                                        
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ALL.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1L5Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB015668.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRANDEIS - B4                      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 165124                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -2.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY                : 1.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 0.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.47500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS 1.1                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, MPD, PH 6.0, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 290K                                      
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       41.48333            
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       82.96667            
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000       62.35650            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000     -108.00463            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000       41.48333            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 10050 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 55750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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     MET A     0                                                      
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     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     THR A   324                                                      
REMARK 465     ASP A   831                                                      
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     MET B     0                                                      
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     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     THR B   324                                                      
REMARK 465     ASP B   831                                                      
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU B   110     O    HOH B  2040              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 490   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 490   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A 131       42.65    -88.28                                   
REMARK 500    TYR A 203     -127.64     58.22                                   
REMARK 500    ASN A 235       13.44   -149.74                                   
REMARK 500    ASN A 236       -0.73     69.86                                   
REMARK 500    PRO A 281       23.72    -72.90                                   
REMARK 500    ASP A 339     -173.48     71.32                                   
REMARK 500    VAL A 354      -70.09    -82.93                                   
REMARK 500    GLU A 434       64.10    -51.77                                   
REMARK 500    ALA A 456      143.98   -172.46                                   
REMARK 500    LYS A 466      -72.47   -117.15                                   
REMARK 500    LEU A 492      -70.22   -149.40                                   
REMARK 500    LYS A 568      170.38    176.46                                   
REMARK 500    SER A 674      -63.05   -148.54                                   
REMARK 500    GLN A 754       82.09   -158.53                                   
REMARK 500    ILE A 824      -56.03   -133.28                                   
REMARK 500    LEU B 131       42.00    -87.00                                   
REMARK 500    TYR B 203     -128.70     57.68                                   
REMARK 500    ASN B 235       14.10   -147.72                                   
REMARK 500    ASN B 236       -2.36     69.35                                   
REMARK 500    PRO B 281       24.85    -74.13                                   
REMARK 500    ASP B 339     -173.49     71.69                                   
REMARK 500    GLU B 434       63.03    -51.32                                   
REMARK 500    ALA B 456      144.96   -173.26                                   
REMARK 500    LYS B 466      -72.20   -115.41                                   
REMARK 500    LEU B 492      -69.49   -147.76                                   
REMARK 500    LYS B 568      171.26    179.76                                   
REMARK 500    SER B 674      -60.33   -149.84                                   
REMARK 500    GLN B 754       82.18   -158.93                                   
REMARK 500    ILE B 824      -56.45   -131.73                                   
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 NBG A 861                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBG B 1861                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 860                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 1860                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 700 A 862                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 700 B 1862                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CFF A 863                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CFF B 1863                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CFF A 864                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CFF B 1864                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1L5R   RELATED DB: PDB                                   
REMARK 900 HUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH                  
REMARK 900 RIBOFLAVIN, N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE AND CP-403,          
REMARK 900 700                                                                  
REMARK 900 RELATED ID: 1L5S   RELATED DB: PDB                                   
REMARK 900 HUMAN LIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH URIC               
REMARK 900 ACID, N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE, AND CP-403,700            
REMARK 900 RELATED ID: 1L7X   RELATED DB: PDB                                   
REMARK 900 HUMAN LIVER GLYCOGEN PHOSPHORYLASE B COMPLEXED WITH                  
REMARK 900 CAFFEINE, N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE, AND CP-403,           
REMARK 900 700                                                                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE NUMBERING OF THE SEQUENCE IS SHIFTED BY ONE                      
REMARK 999 IN AGREEMENT WITH THE CONVENTION IN THE LITERATURE                   
REMARK 999 FOR THIS PROTEIN.                                                    
DBREF  1L5Q A    0   846  UNP    P06737   PHS1_HUMAN       1    847             
DBREF  1L5Q B    0   846  UNP    P06737   PHS1_HUMAN       1    847             
SEQRES   1 A  847  MET ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN          
SEQRES   2 A  847  ILE SER ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA          
SEQRES   3 A  847  GLU LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR          
SEQRES   4 A  847  LEU VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR          
SEQRES   5 A  847  TYR PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL          
SEQRES   6 A  847  GLY ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS          
SEQRES   7 A  847  CYS PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR          
SEQRES   8 A  847  MET GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY          
SEQRES   9 A  847  LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY          
SEQRES  10 A  847  LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA          
SEQRES  11 A  847  GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS          
SEQRES  12 A  847  PHE LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR          
SEQRES  13 A  847  GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN          
SEQRES  14 A  847  LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP          
SEQRES  15 A  847  TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO          
SEQRES  16 A  847  GLU PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU          
SEQRES  17 A  847  HIS THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL          
SEQRES  18 A  847  VAL LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR          
SEQRES  19 A  847  MET ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA          
SEQRES  20 A  847  ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL          
SEQRES  21 A  847  GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA          
SEQRES  22 A  847  GLU ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE          
SEQRES  23 A  847  PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE          
SEQRES  24 A  847  VAL VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE          
SEQRES  25 A  847  LYS ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY THR          
SEQRES  26 A  847  VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU          
SEQRES  27 A  847  ASN ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET          
SEQRES  28 A  847  ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS          
SEQRES  29 A  847  ALA TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN          
SEQRES  30 A  847  HIS THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL          
SEQRES  31 A  847  ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE          
SEQRES  32 A  847  ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL          
SEQRES  33 A  847  ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET          
SEQRES  34 A  847  SER LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET          
SEQRES  35 A  847  ALA HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY          
SEQRES  36 A  847  VAL ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL          
SEQRES  37 A  847  PHE LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN          
SEQRES  38 A  847  ASN LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU          
SEQRES  39 A  847  LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS          
SEQRES  40 A  847  ILE GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR          
SEQRES  41 A  847  LYS LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG          
SEQRES  42 A  847  GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE          
SEQRES  43 A  847  SER GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN          
SEQRES  44 A  847  PRO SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS          
SEQRES  45 A  847  GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE          
SEQRES  46 A  847  THR MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU          
SEQRES  47 A  847  PHE VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA          
SEQRES  48 A  847  PRO GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE          
SEQRES  49 A  847  THR SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL          
SEQRES  50 A  847  GLY SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG          
SEQRES  51 A  847  VAL SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU          
SEQRES  52 A  847  SER GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY          
SEQRES  53 A  847  THR GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR          
SEQRES  54 A  847  ILE GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU          
SEQRES  55 A  847  GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG          
SEQRES  56 A  847  ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU          
SEQRES  57 A  847  ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU          
SEQRES  58 A  847  VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS          
SEQRES  59 A  847  GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE          
SEQRES  60 A  847  TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA          
SEQRES  61 A  847  TYR VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET          
SEQRES  62 A  847  ASN PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE          
SEQRES  63 A  847  ALA ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS          
SEQRES  64 A  847  GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP          
SEQRES  65 A  847  LEU LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN          
SEQRES  66 A  847  GLY ASN                                                      
SEQRES   1 B  847  MET ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN          
SEQRES   2 B  847  ILE SER ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA          
SEQRES   3 B  847  GLU LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR          
SEQRES   4 B  847  LEU VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR          
SEQRES   5 B  847  TYR PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL          
SEQRES   6 B  847  GLY ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS          
SEQRES   7 B  847  CYS PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR          
SEQRES   8 B  847  MET GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY          
SEQRES   9 B  847  LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY          
SEQRES  10 B  847  LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA          
SEQRES  11 B  847  GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS          
SEQRES  12 B  847  PHE LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR          
SEQRES  13 B  847  GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN          
SEQRES  14 B  847  LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP          
SEQRES  15 B  847  TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO          
SEQRES  16 B  847  GLU PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU          
SEQRES  17 B  847  HIS THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL          
SEQRES  18 B  847  VAL LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR          
SEQRES  19 B  847  MET ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA          
SEQRES  20 B  847  ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL          
SEQRES  21 B  847  GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA          
SEQRES  22 B  847  GLU ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE          
SEQRES  23 B  847  PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE          
SEQRES  24 B  847  VAL VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE          
SEQRES  25 B  847  LYS ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY THR          
SEQRES  26 B  847  VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU          
SEQRES  27 B  847  ASN ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET          
SEQRES  28 B  847  ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS          
SEQRES  29 B  847  ALA TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN          
SEQRES  30 B  847  HIS THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL          
SEQRES  31 B  847  ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE          
SEQRES  32 B  847  ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL          
SEQRES  33 B  847  ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET          
SEQRES  34 B  847  SER LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET          
SEQRES  35 B  847  ALA HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY          
SEQRES  36 B  847  VAL ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL          
SEQRES  37 B  847  PHE LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN          
SEQRES  38 B  847  ASN LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU          
SEQRES  39 B  847  LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS          
SEQRES  40 B  847  ILE GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR          
SEQRES  41 B  847  LYS LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG          
SEQRES  42 B  847  GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE          
SEQRES  43 B  847  SER GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN          
SEQRES  44 B  847  PRO SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS          
SEQRES  45 B  847  GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE          
SEQRES  46 B  847  THR MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU          
SEQRES  47 B  847  PHE VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA          
SEQRES  48 B  847  PRO GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE          
SEQRES  49 B  847  THR SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL          
SEQRES  50 B  847  GLY SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG          
SEQRES  51 B  847  VAL SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU          
SEQRES  52 B  847  SER GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY          
SEQRES  53 B  847  THR GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR          
SEQRES  54 B  847  ILE GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU          
SEQRES  55 B  847  GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG          
SEQRES  56 B  847  ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU          
SEQRES  57 B  847  ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU          
SEQRES  58 B  847  VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS          
SEQRES  59 B  847  GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE          
SEQRES  60 B  847  TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA          
SEQRES  61 B  847  TYR VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET          
SEQRES  62 B  847  ASN PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE          
SEQRES  63 B  847  ALA ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS          
SEQRES  64 B  847  GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP          
SEQRES  65 B  847  LEU LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN          
SEQRES  66 B  847  GLY ASN                                                      
HET    NBG  A 861      15                                                       
HET    NBG  B1861      15                                                       
HET    PLP  A 860      15                                                       
HET    PLP  B1860      15                                                       
HET    700  A 862      30                                                       
HET    700  B1862      30                                                       
HET    CFF  A 863      14                                                       
HET    CFF  B1863      14                                                       
HET    CFF  A 864      14                                                       
HET    CFF  B1864      14                                                       
HETNAM     NBG 1-N-ACETYL-BETA-D-GLUCOSAMINE                                    
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     700 [5-CHLORO-1H-INDOL-2-CARBONYL-PHENYLALANINYL]-                   
HETNAM   2 700  AZETIDINE-3-CARBOXYLIC ACID                                     
HETNAM     CFF CAFFEINE                                                         
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
HETSYN     700 CP403700, (S)-1-{2-[(5-CHLORO-1H-INDOLE-2-CARBONYL)-             
HETSYN   2 700  AMINO]-3-PHENYL-PROPIONYL}-AZETIDINE-3-CARBOXYLATE              
HETSYN     CFF 3,7-DIHYDRO-1,3,7-TRIMETHYL-1H-PURINE-2,6-DIONE                  
FORMUL   3  NBG    2(C8 H15 N O6)                                               
FORMUL   5  PLP    2(C8 H10 N O6 P)                                             
FORMUL   7  700    2(C22 H20 CL N3 O4)                                          
FORMUL   9  CFF    4(C8 H10 N4 O2)                                              
FORMUL  13  HOH   *607(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  126  1                                   9    
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 ASP A  268  ASN A  274  1                                   7    
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  GLN A  332  1                                   5    
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  475  1                                   8    
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  ASP A  633  1                                  21    
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  GLY A  748  1                                  14    
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  ASP B   61  1                                  15    
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 ASP B  268  ASN B  274  1                                   7    
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 ASP B  421  SER B  429  1                                   9    
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  LYS B  513  5                                   5    
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  ASP B  633  1                                  21    
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 GLU B  727  LEU B  735  1                                   9    
HELIX   79  79 LEU B  735  ASN B  747  1                                  13    
HELIX   80  80 PHE B  758  HIS B  768  1                                  11    
HELIX   81  81 LYS B  772  MET B  792  1                                  21    
HELIX   82  82 ASN B  793  ALA B  807  1                                  15    
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 LEU A 198  THR A 209  0                                        
SHEET    2   A 3 GLY A 212  PRO A 231 -1  O  LYS A 214   N  GLU A 207           
SHEET    3   A 3 LYS A 191  SER A 192 -1  N  LYS A 191   O  ASP A 227           
SHEET    1   B 9 LEU A 198  THR A 209  0                                        
SHEET    2   B 9 GLY A 212  PRO A 231 -1  O  LYS A 214   N  GLU A 207           
SHEET    3   B 9 VAL A 238  ARG A 247 -1  O  ARG A 247   N  LEU A 222           
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  TRP A 174   N  ARG A 171           
SHEET    1   E 3 ARG A 386  PRO A 388  0                                        
SHEET    2   E 3 ARG A 438  ASN A 440 -1  O  ILE A 439   N  TRP A 387           
SHEET    3   E 3 ILE A 431  GLU A 432 -1  N  GLU A 432   O  ARG A 438           
SHEET    1   F 6 LEU A 640  LEU A 645  0                                        
SHEET    2   F 6 ARG A 601  GLY A 606  1  N  VAL A 603   O  LYS A 641           
SHEET    3   F 6 MET A 562  VAL A 567  1  N  ASP A 564   O  ILE A 604           
SHEET    4   F 6 LEU A 662  GLN A 665  1  O  LEU A 662   N  VAL A 565           
SHEET    5   F 6 LEU A 687  GLY A 690  1  O  LEU A 687   N  SER A 663           
SHEET    6   F 6 PHE A 709  ILE A 710  1  O  PHE A 709   N  GLY A 690           
SHEET    1   G 3 LEU B 198  THR B 209  0                                        
SHEET    2   G 3 GLY B 212  PRO B 231 -1  O  LYS B 214   N  GLU B 207           
SHEET    3   G 3 LYS B 191  SER B 192 -1  N  LYS B 191   O  ASP B 227           
SHEET    1   H 9 LEU B 198  THR B 209  0                                        
SHEET    2   H 9 GLY B 212  PRO B 231 -1  O  LYS B 214   N  GLU B 207           
SHEET    3   H 9 VAL B 238  ARG B 247 -1  O  ARG B 247   N  LEU B 222           
SHEET    4   H 9 ALA B 154  ILE B 159  1  N  GLY B 156   O  ARG B 242           
SHEET    5   H 9 ARG B  81  LEU B  85  1  N  TYR B  84   O  TYR B 155           
SHEET    6   H 9 VAL B 333  ASN B 338  1  O  ALA B 334   N  TYR B  83           
SHEET    7   H 9 PHE B 372  THR B 375  1  O  ALA B 373   N  LEU B 337           
SHEET    8   H 9 ALA B 451  GLY B 454  1  O  ALA B 451   N  TYR B 374           
SHEET    9   H 9 PHE B 479  ASN B 481  1  O  GLN B 480   N  VAL B 452           
SHEET    1   I 2 PHE B  89  GLY B  92  0                                        
SHEET    2   I 2 ALA B 129  LEU B 131 -1  O  LEU B 131   N  PHE B  89           
SHEET    1   J 2 ASN B 167  ARG B 171  0                                        
SHEET    2   J 2 TRP B 174  GLU B 178 -1  O  TRP B 174   N  ARG B 171           
SHEET    1   K 3 ARG B 386  PRO B 388  0                                        
SHEET    2   K 3 ARG B 438  ASN B 440 -1  O  ILE B 439   N  TRP B 387           
SHEET    3   K 3 ILE B 431  GLU B 432 -1  N  GLU B 432   O  ARG B 438           
SHEET    1   L 6 LEU B 640  LEU B 645  0                                        
SHEET    2   L 6 ARG B 601  GLY B 606  1  N  VAL B 603   O  LYS B 641           
SHEET    3   L 6 MET B 562  VAL B 567  1  N  ASP B 564   O  ILE B 604           
SHEET    4   L 6 LEU B 662  GLN B 665  1  O  LEU B 662   N  VAL B 565           
SHEET    5   L 6 LEU B 687  GLY B 690  1  O  LEU B 687   N  SER B 663           
SHEET    6   L 6 PHE B 709  ILE B 710  1  O  PHE B 709   N  GLY B 690           
LINK         C4A PLP A 860                 NZ  LYS A 680     1555   1555  1.46  
LINK         C4A PLP B1860                 NZ  LYS B 680     1555   1555  1.40  
SITE     1 AC1 14 LEU A 136  ASN A 284  HIS A 377  VAL A 455                    
SITE     2 AC1 14 ASN A 484  TYR A 573  GLU A 672  ALA A 673                    
SITE     3 AC1 14 SER A 674  GLY A 675  HOH A2196  HOH A2199                    
SITE     4 AC1 14 HOH A2228  HOH A2582                                          
SITE     1 AC2 16 GLY B 135  LEU B 136  ASN B 284  ASP B 339                    
SITE     2 AC2 16 HIS B 377  ASN B 484  TYR B 573  GLU B 672                    
SITE     3 AC2 16 ALA B 673  SER B 674  GLY B 675  HOH B2009                    
SITE     4 AC2 16 HOH B2208  HOH B2209  HOH B2323  HOH B2357                    
SITE     1 AC3 18 TYR A  90  GLY A 134  GLY A 135  TRP A 491                    
SITE     2 AC3 18 LYS A 568  LYS A 574  TYR A 648  ARG A 649                    
SITE     3 AC3 18 VAL A 650  GLY A 675  THR A 676  GLY A 677                    
SITE     4 AC3 18 LYS A 680  HOH A2002  HOH A2155  HOH A2161                    
SITE     5 AC3 18 HOH A2199  HOH A2244                                          
SITE     1 AC4 18 TYR B  90  GLY B 134  TRP B 491  LYS B 568                    
SITE     2 AC4 18 LYS B 574  TYR B 648  ARG B 649  VAL B 650                    
SITE     3 AC4 18 GLY B 675  THR B 676  GLY B 677  LYS B 680                    
SITE     4 AC4 18 HOH B2013  HOH B2028  HOH B2073  HOH B2236                    
SITE     5 AC4 18 HOH B2323  HOH B2326                                          
SITE     1 AC5 16 ARG A  60  LEU A  63  VAL A  64  TRP A  67                    
SITE     2 AC5 16 PRO A 188  GLU A 190  LYS A 191  SER A 192                    
SITE     3 AC5 16 HOH A2043  HOH A2321  THR B  38  VAL B  40                    
SITE     4 AC5 16 PHE B  53  HIS B  57  TYR B 185  PRO B 188                    
SITE     1 AC6 17 THR A  38  VAL A  40  PHE A  53  HIS A  57                    
SITE     2 AC6 17 TYR A 185  PRO A 188  ARG B  60  LEU B  63                    
SITE     3 AC6 17 VAL B  64  TRP B  67  PRO B 188  GLU B 190                    
SITE     4 AC6 17 LYS B 191  HOH B2005  HOH B2007  HOH B2011                    
SITE     5 AC6 17 HOH B2069                                                     
SITE     1 AC7  7 ASN A 282  PHE A 285  ALA A 610  GLY A 612                    
SITE     2 AC7  7 TYR A 613  HOH A2001  HOH A2004                               
SITE     1 AC8  9 ASN B 282  PHE B 285  HIS B 571  ALA B 610                    
SITE     2 AC8  9 GLY B 612  TYR B 613  HOH B2099  HOH B2407                    
SITE     3 AC8  9 HOH B2565                                                     
SITE     1 AC9  4 TRP A 174  HIS A 614  HOH A2081  HOH A2511                    
SITE     1 BC1  2 TRP B 174  HIS B 614                                          
CRYST1  124.713  124.713  124.450  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      0.008018  0.004629  0.000000        0.00000                         
SCALE2      0.000000  0.009259  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008035        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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