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Database: PDB
Entry: 3DDS
LinkDB: 3DDS
Original site: 3DDS 
HEADER    TRANSFERASE                             06-JUN-08   3DDS              
TITLE     CRYSTAL STRUCTURE OF GLYCOGEN PHOSPHORYLASE COMPLEXED WITH AN         
TITLE    2 ANTHRANILIMIDE BASED INHIBITOR GSK261                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOGEN PHOSPHORYLASE, LIVER FORM;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.4.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 TISSUE: LIVER ISOFORM;                                               
SOURCE   5 GENE: PYGL;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: T7 PROMOTER                               
KEYWDS    GP, GLYCOGEN PHOSPHORYLASE, DIABETES, ALLOSTERIC ENZYME, CARBOHYDRATE 
KEYWDS   2 METABOLISM, DISEASE MUTATION, GLYCOGEN METABOLISM, GLYCOGEN STORAGE  
KEYWDS   3 DISEASE, GLYCOSYLTRANSFERASE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN,    
KEYWDS   4 PYRIDOXAL PHOSPHATE, TRANSFERASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.T.NOLTE                                                             
REVDAT   3   13-JUL-11 3DDS    1       VERSN                                    
REVDAT   2   03-MAR-09 3DDS    1       JRNL                                     
REVDAT   1   27-JAN-09 3DDS    0                                                
JRNL        AUTH   S.A.THOMSON,P.BANKER,D.M.BICKETT,J.A.BOUCHERON,H.L.CARTER,   
JRNL        AUTH 2 D.C.CLANCY,J.P.COOPER,S.H.DICKERSON,D.M.GARRIDO,R.T.NOLTE,   
JRNL        AUTH 3 A.J.PEAT,L.R.SHECKLER,S.M.SPARKS,F.X.TAVARES,L.WANG,         
JRNL        AUTH 4 T.Y.WANG,J.E.WEIEL                                           
JRNL        TITL   ANTHRANILIMIDE BASED GLYCOGEN PHOSPHORYLASE INHIBITORS FOR   
JRNL        TITL 2 THE TREATMENT OF TYPE 2 DIABETES. PART 3: X-RAY              
JRNL        TITL 3 CRYSTALLOGRAPHIC CHARACTERIZATION, CORE AND UREA             
JRNL        TITL 4 OPTIMIZATION AND IN VIVO EFFICACY.                           
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  19  1177 2009              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   19138846                                                     
JRNL        DOI    10.1016/J.BMCL.2008.12.085                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.66                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 186135                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5803                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 13498                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 436                          
REMARK   3   BIN FREE R VALUE                    : 0.2710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13003                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 224                                     
REMARK   3   SOLVENT ATOMS            : 1353                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.21000                                             
REMARK   3    B22 (A**2) : -0.21000                                             
REMARK   3    B33 (A**2) : 0.31000                                              
REMARK   3    B12 (A**2) : -0.10000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.109         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.102         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.073         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.334         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13659 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  9226 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18535 ; 1.113 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22479 ; 0.842 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1640 ; 5.469 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   651 ;34.990 ;24.363       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2382 ;11.917 ;15.006       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    79 ;14.066 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2013 ; 0.061 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15219 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2806 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2786 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  9697 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6702 ; 0.178 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  6463 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1104 ; 0.117 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    21 ; 0.177 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    52 ; 0.254 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    44 ; 0.139 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8535 ; 0.570 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3288 ; 0.099 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13167 ; 0.903 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6153 ; 1.295 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5365 ; 1.967 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3DDS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB047912.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-AUG-05                          
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               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 190798                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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: PDB ENTRY 1EM6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-25% MPD, 0.1M MES BUFFER PH 6.0,      
REMARK 280  5MM CAFFEINE, 30MM GLCNAC, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 293K                                                    
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       41.20467            
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       82.40933            
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 300 REMARK: THE ACTIVE FORM IS A DIMER, AS SEEN IN THE ASYMMETRIC UNIT   
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: 5020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 58010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.7 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     GLY A    -1                                                      
REMARK 465     GLY 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     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     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     GLY B    -1                                                      
REMARK 465     GLY 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     SEP 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     PHE B   257                                                      
REMARK 465     ASN B   258                                                      
REMARK 465     VAL B   259                                                      
REMARK 465     ARG B   320                                                      
REMARK 465     GLY B   321                                                      
REMARK 465     ALA B   322                                                      
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 420    CG   CD   CE   NZ                                   
REMARK 470     ARG A 532    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 595    CD   CE   NZ                                        
REMARK 470     MET A 635    CG   SD   CE                                        
REMARK 470     LYS A 723    CE   NZ                                             
REMARK 470     LYS A 724    CG   CD   CE   NZ                                   
REMARK 470     LYS A 759    CG   CD   CE   NZ                                   
REMARK 470     ARG B 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 255    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 420    CG   CD   CE   NZ                                   
REMARK 470     LYS B 466    CD   CE   NZ                                        
REMARK 470     LYS B 554    CG   CD   CE   NZ                                   
REMARK 470     LYS B 595    CG   CD   CE   NZ                                   
REMARK 470     LYS B 723    CD   CE   NZ                                        
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   OD1  ASN B   106     O    HOH B  1591              1.91            
REMARK 500   NE2  GLN A   547     O    HOH A  1229              2.05            
REMARK 500   NE2  HIS B   522     O    HOH B  1094              2.11            
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       39.19    -90.23                                   
REMARK 500    TYR A 203     -133.13     61.67                                   
REMARK 500    PRO A 281       30.69    -86.24                                   
REMARK 500    ASP A 339     -169.54     69.39                                   
REMARK 500    ARG A 489      -73.44    -70.39                                   
REMARK 500    LEU A 492      -62.34   -146.81                                   
REMARK 500    LYS A 568      167.03    171.99                                   
REMARK 500    SER A 674      -59.74   -139.33                                   
REMARK 500    HIS A 768       31.88   -141.04                                   
REMARK 500    ILE A 824      -54.38   -126.74                                   
REMARK 500    LEU B 131       44.08    -93.19                                   
REMARK 500    TYR B 203     -137.35     60.90                                   
REMARK 500    PRO B 281       35.06    -87.07                                   
REMARK 500    ASP B 339     -170.59     67.79                                   
REMARK 500    ARG B 489      -74.10    -71.22                                   
REMARK 500    LEU B 492      -64.68   -145.67                                   
REMARK 500    LYS B 568      165.97    172.01                                   
REMARK 500    SER B 674      -60.76   -141.18                                   
REMARK 500    SER B 751       60.66   -151.04                                   
REMARK 500    HIS B 768       35.10   -146.88                                   
REMARK 500    ILE B 824      -55.80   -125.58                                   
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 B1583        DISTANCE =  5.17 ANGSTROMS                       
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 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBG B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CFF A 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CFF B 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 26B B 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 26B A 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 26B B 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 906                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3DD1   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN COMPLEX WITH RELATED LIGAND                          
REMARK 900 RELATED ID: 3DDW   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN COMPLEX WITH RELATED LIGAND                          
DBREF  3DDS A    1   846  UNP    P06737   PYGL_HUMAN       2    847             
DBREF  3DDS B    1   846  UNP    P06737   PYGL_HUMAN       2    847             
SEQADV 3DDS GLY A   -1  UNP  P06737              EXPRESSION TAG                 
SEQADV 3DDS GLY A    0  UNP  P06737              EXPRESSION TAG                 
SEQADV 3DDS GLY B   -1  UNP  P06737              EXPRESSION TAG                 
SEQADV 3DDS GLY B    0  UNP  P06737              EXPRESSION TAG                 
SEQRES   1 A  848  GLY GLY ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG          
SEQRES   2 A  848  GLN ILE SEP ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL          
SEQRES   3 A  848  ALA GLU LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE          
SEQRES   4 A  848  THR LEU VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP          
SEQRES   5 A  848  TYR TYR PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU          
SEQRES   6 A  848  VAL GLY ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP          
SEQRES   7 A  848  LYS CYS PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE          
SEQRES   8 A  848  TYR MET GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU          
SEQRES   9 A  848  GLY LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU          
SEQRES  10 A  848  GLY LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP          
SEQRES  11 A  848  ALA GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA          
SEQRES  12 A  848  CYS PHE LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA          
SEQRES  13 A  848  TYR GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN          
SEQRES  14 A  848  GLN LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP          
SEQRES  15 A  848  ASP TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG          
SEQRES  16 A  848  PRO GLU PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL          
SEQRES  17 A  848  GLU HIS THR ASN THR GLY THR LYS TRP ILE ASP THR GLN          
SEQRES  18 A  848  VAL VAL LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY          
SEQRES  19 A  848  TYR MET ASN ASN THR VAL ASN THR MET ARG LEU TRP SER          
SEQRES  20 A  848  ALA ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN          
SEQRES  21 A  848  VAL GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU          
SEQRES  22 A  848  ALA GLU ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN          
SEQRES  23 A  848  PHE PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR          
SEQRES  24 A  848  PHE VAL VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG          
SEQRES  25 A  848  PHE LYS ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY          
SEQRES  26 A  848  THR VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN          
SEQRES  27 A  848  LEU ASN ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU          
SEQRES  28 A  848  MET ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER          
SEQRES  29 A  848  LYS ALA TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR          
SEQRES  30 A  848  ASN HIS THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO          
SEQRES  31 A  848  VAL ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU          
SEQRES  32 A  848  ILE ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE          
SEQRES  33 A  848  VAL ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG          
SEQRES  34 A  848  MET SER LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN          
SEQRES  35 A  848  MET ALA HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN          
SEQRES  36 A  848  GLY VAL ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS          
SEQRES  37 A  848  VAL PHE LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE          
SEQRES  38 A  848  GLN ASN LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU          
SEQRES  39 A  848  LEU LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU          
SEQRES  40 A  848  LYS ILE GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU          
SEQRES  41 A  848  THR LYS LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU          
SEQRES  42 A  848  ARG GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS          
SEQRES  43 A  848  PHE SER GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE          
SEQRES  44 A  848  ASN PRO SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE          
SEQRES  45 A  848  HIS GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL          
SEQRES  46 A  848  ILE THR MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS          
SEQRES  47 A  848  LEU PHE VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA          
SEQRES  48 A  848  ALA PRO GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU          
SEQRES  49 A  848  ILE THR SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET          
SEQRES  50 A  848  VAL GLY SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR          
SEQRES  51 A  848  ARG VAL SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP          
SEQRES  52 A  848  LEU SER GLU GLN ILE SER THR ALA GLY THR GLU ALA SER          
SEQRES  53 A  848  GLY THR GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU          
SEQRES  54 A  848  THR ILE GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA          
SEQRES  55 A  848  GLU GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET          
SEQRES  56 A  848  ARG ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR          
SEQRES  57 A  848  GLU ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS          
SEQRES  58 A  848  LEU VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO          
SEQRES  59 A  848  LYS GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU          
SEQRES  60 A  848  PHE TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU          
SEQRES  61 A  848  ALA TYR VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR          
SEQRES  62 A  848  MET ASN PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN          
SEQRES  63 A  848  ILE ALA ALA SER GLY LYS PHE SER SER ASP ARG THR ILE          
SEQRES  64 A  848  LYS GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER          
SEQRES  65 A  848  ASP LEU LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL          
SEQRES  66 A  848  ASN GLY ASN                                                  
SEQRES   1 B  848  GLY GLY ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG          
SEQRES   2 B  848  GLN ILE SEP ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL          
SEQRES   3 B  848  ALA GLU LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE          
SEQRES   4 B  848  THR LEU VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP          
SEQRES   5 B  848  TYR TYR PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU          
SEQRES   6 B  848  VAL GLY ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP          
SEQRES   7 B  848  LYS CYS PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE          
SEQRES   8 B  848  TYR MET GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU          
SEQRES   9 B  848  GLY LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU          
SEQRES  10 B  848  GLY LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP          
SEQRES  11 B  848  ALA GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA          
SEQRES  12 B  848  CYS PHE LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA          
SEQRES  13 B  848  TYR GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN          
SEQRES  14 B  848  GLN LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP          
SEQRES  15 B  848  ASP TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG          
SEQRES  16 B  848  PRO GLU PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL          
SEQRES  17 B  848  GLU HIS THR ASN THR GLY THR LYS TRP ILE ASP THR GLN          
SEQRES  18 B  848  VAL VAL LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY          
SEQRES  19 B  848  TYR MET ASN ASN THR VAL ASN THR MET ARG LEU TRP SER          
SEQRES  20 B  848  ALA ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN          
SEQRES  21 B  848  VAL GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU          
SEQRES  22 B  848  ALA GLU ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN          
SEQRES  23 B  848  PHE PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR          
SEQRES  24 B  848  PHE VAL VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG          
SEQRES  25 B  848  PHE LYS ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY          
SEQRES  26 B  848  THR VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN          
SEQRES  27 B  848  LEU ASN ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU          
SEQRES  28 B  848  MET ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER          
SEQRES  29 B  848  LYS ALA TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR          
SEQRES  30 B  848  ASN HIS THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO          
SEQRES  31 B  848  VAL ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU          
SEQRES  32 B  848  ILE ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE          
SEQRES  33 B  848  VAL ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG          
SEQRES  34 B  848  MET SER LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN          
SEQRES  35 B  848  MET ALA HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN          
SEQRES  36 B  848  GLY VAL ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS          
SEQRES  37 B  848  VAL PHE LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE          
SEQRES  38 B  848  GLN ASN LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU          
SEQRES  39 B  848  LEU LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU          
SEQRES  40 B  848  LYS ILE GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU          
SEQRES  41 B  848  THR LYS LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU          
SEQRES  42 B  848  ARG GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS          
SEQRES  43 B  848  PHE SER GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE          
SEQRES  44 B  848  ASN PRO SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE          
SEQRES  45 B  848  HIS GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL          
SEQRES  46 B  848  ILE THR MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS          
SEQRES  47 B  848  LEU PHE VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA          
SEQRES  48 B  848  ALA PRO GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU          
SEQRES  49 B  848  ILE THR SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET          
SEQRES  50 B  848  VAL GLY SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR          
SEQRES  51 B  848  ARG VAL SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP          
SEQRES  52 B  848  LEU SER GLU GLN ILE SER THR ALA GLY THR GLU ALA SER          
SEQRES  53 B  848  GLY THR GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU          
SEQRES  54 B  848  THR ILE GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA          
SEQRES  55 B  848  GLU GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET          
SEQRES  56 B  848  ARG ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR          
SEQRES  57 B  848  GLU ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS          
SEQRES  58 B  848  LEU VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO          
SEQRES  59 B  848  LYS GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU          
SEQRES  60 B  848  PHE TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU          
SEQRES  61 B  848  ALA TYR VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR          
SEQRES  62 B  848  MET ASN PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN          
SEQRES  63 B  848  ILE ALA ALA SER GLY LYS PHE SER SER ASP ARG THR ILE          
SEQRES  64 B  848  LYS GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER          
SEQRES  65 B  848  ASP LEU LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL          
SEQRES  66 B  848  ASN GLY ASN                                                  
MODRES 3DDS SEP A   14  SER  PHOSPHOSERINE                                      
HET    SEP  A  14      10                                                       
HET    NBG  A 901      15                                                       
HET    NBG  B 901      15                                                       
HET    PO4  A 902       5                                                       
HET    PLP  A 903      15                                                       
HET    CFF  A 904      14                                                       
HET    26B  A 905      37                                                       
HET    PLP  B 902      15                                                       
HET    CFF  B 903      14                                                       
HET    MES  B 904      12                                                       
HET    26B  B 905      37                                                       
HET    26B  B 906      37                                                       
HET    MPD  A 906       8                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     NBG 1-N-ACETYL-BETA-D-GLUCOSAMINE                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     CFF CAFFEINE                                                         
HETNAM     26B O-TERT-BUTYL-N-[(3-{[(2,4,6-TRIMETHYLPHENYL)                     
HETNAM   2 26B  CARBAMOYL]AMINO}NAPHTHALEN-2-YL)CARBONYL]-L-THREONINE           
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
HETSYN     CFF 3,7-DIHYDRO-1,3,7-TRIMETHYL-1H-PURINE-2,6-DIONE                  
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3  NBG    2(C8 H15 N O6)                                               
FORMUL   5  PO4    O4 P 3-                                                      
FORMUL   6  PLP    2(C8 H10 N O6 P)                                             
FORMUL   7  CFF    2(C8 H10 N4 O2)                                              
FORMUL   8  26B    3(C29 H35 N3 O5)                                             
FORMUL  11  MES    C6 H13 N O4 S                                                
FORMUL  14  MPD    C6 H14 O2                                                    
FORMUL  15  HOH   *1353(H2 O)                                                   
HELIX    1   1 GLY A   17  THR A   38  1                                  22    
HELIX    2   2 ASP A   42  ALA A   46  5                                   5    
HELIX    3   3 THR A   47  HIS A   62  1                                  16    
HELIX    4   4 LEU A   63  CYS A   78  1                                  16    
HELIX    5   5 THR A   94  LEU A  102  1                                   9    
HELIX    6   6 LEU A  104  LEU A  115  1                                  12    
HELIX    7   7 ASP A  118  ILE A  125  1                                   8    
HELIX    8   8 GLY A  134  LEU A  150  1                                  17    
HELIX    9   9 PRO A  194  MET A  197  5                                   4    
HELIX   10  10 ASP A  261  ASP A  268  1                                   8    
HELIX   11  11 ASP A  268  ASN A  274  1                                   7    
HELIX   12  12 ILE A  275  ARG A  277  5                                   3    
HELIX   13  13 LYS A  289  SER A  314  1                                  26    
HELIX   14  14 ALA A  328  GLN A  332  1                                   5    
HELIX   15  15 LEU A  344  ILE A  356  1                                  13    
HELIX   16  16 PRO A  360  THR A  371  1                                  12    
HELIX   17  17 LEU A  380  LEU A  384  5                                   5    
HELIX   18  18 VAL A  389  LEU A  396  1                                   8    
HELIX   19  19 LEU A  396  PHE A  418  1                                  23    
HELIX   20  20 ASP A  421  SER A  429  1                                   9    
HELIX   21  21 MET A  441  GLY A  448  1                                   8    
HELIX   22  22 ALA A  456  LYS A  466  1                                  11    
HELIX   23  23 PHE A  468  GLU A  475  1                                   8    
HELIX   24  24 ASN A  496  GLY A  508  1                                  13    
HELIX   25  25 GLU A  509  LYS A  513  5                                   5    
HELIX   26  26 ASP A  514  LEU A  525  5                                  12    
HELIX   27  27 ASP A  527  TYR A  553  1                                  27    
HELIX   28  28 ARG A  575  ASP A  593  1                                  19    
HELIX   29  29 TYR A  613  ASP A  633  1                                  21    
HELIX   30  30 VAL A  636  SER A  638  5                                   3    
HELIX   31  31 ARG A  649  ILE A  657  1                                   9    
HELIX   32  32 PRO A  658  THR A  660  5                                   3    
HELIX   33  33 THR A  676  ASN A  684  1                                   9    
HELIX   34  34 ALA A  695  GLY A  704  1                                  10    
HELIX   35  35 GLU A  705  LEU A  708  5                                   4    
HELIX   36  36 ARG A  714  GLY A  725  1                                  12    
HELIX   37  37 GLU A  727  LEU A  735  1                                   9    
HELIX   38  38 LEU A  735  GLY A  748  1                                  14    
HELIX   39  39 PHE A  758  HIS A  768  1                                  11    
HELIX   40  40 LYS A  772  MET A  792  1                                  21    
HELIX   41  41 ASN A  793  ALA A  806  1                                  14    
HELIX   42  42 ALA A  807  PHE A  811  5                                   5    
HELIX   43  43 SER A  812  ILE A  824  1                                  13    
HELIX   44  44 ASN B   23  THR B   38  1                                  16    
HELIX   45  45 ASP B   42  ALA B   46  5                                   5    
HELIX   46  46 THR B   47  HIS B   62  1                                  16    
HELIX   47  47 LEU B   63  CYS B   78  1                                  16    
HELIX   48  48 THR B   94  LEU B  102  1                                   9    
HELIX   49  49 LEU B  104  LEU B  115  1                                  12    
HELIX   50  50 ASP B  118  GLU B  124  1                                   7    
HELIX   51  51 GLY B  134  LEU B  150  1                                  17    
HELIX   52  52 PRO B  194  MET B  197  5                                   4    
HELIX   53  53 ASP B  261  ASP B  268  1                                   8    
HELIX   54  54 ASP B  268  ASN B  274  1                                   7    
HELIX   55  55 ILE B  275  ARG B  277  5                                   3    
HELIX   56  56 LYS B  289  SER B  314  1                                  26    
HELIX   57  57 LYS B  315  SER B  318  5                                   4    
HELIX   58  58 THR B  324  ASP B  327  5                                   4    
HELIX   59  59 ALA B  328  GLN B  332  1                                   5    
HELIX   60  60 LEU B  344  ILE B  356  1                                  13    
HELIX   61  61 PRO B  360  THR B  371  1                                  12    
HELIX   62  62 LEU B  380  LEU B  384  5                                   5    
HELIX   63  63 VAL B  389  LEU B  396  1                                   8    
HELIX   64  64 LEU B  396  PHE B  418  1                                  23    
HELIX   65  65 ASP B  421  SER B  429  1                                   9    
HELIX   66  66 MET B  441  GLY B  448  1                                   8    
HELIX   67  67 ALA B  456  LYS B  466  1                                  11    
HELIX   68  68 PHE B  468  GLU B  475  1                                   8    
HELIX   69  69 ASN B  496  GLY B  508  1                                  13    
HELIX   70  70 GLU B  509  LYS B  513  5                                   5    
HELIX   71  71 ASP B  514  LEU B  525  5                                  12    
HELIX   72  72 ASP B  527  LYS B  554  1                                  28    
HELIX   73  73 ARG B  575  ASP B  593  1                                  19    
HELIX   74  74 TYR B  613  ASP B  633  1                                  21    
HELIX   75  75 VAL B  636  SER B  638  5                                   3    
HELIX   76  76 ARG B  649  ILE B  657  1                                   9    
HELIX   77  77 PRO B  658  THR B  660  5                                   3    
HELIX   78  78 THR B  676  ASN B  684  1                                   9    
HELIX   79  79 ALA B  695  GLY B  704  1                                  10    
HELIX   80  80 GLU B  705  LEU B  708  5                                   4    
HELIX   81  81 ARG B  714  GLY B  725  1                                  12    
HELIX   82  82 ALA B  728  LEU B  735  1                                   8    
HELIX   83  83 LEU B  735  GLY B  748  1                                  14    
HELIX   84  84 PHE B  758  HIS B  768  1                                  11    
HELIX   85  85 LYS B  772  MET B  792  1                                  21    
HELIX   86  86 ASN B  793  ALA B  807  1                                  15    
HELIX   87  87 SER B  808  PHE B  811  5                                   4    
HELIX   88  88 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  SER A 245   N  LEU A 224           
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  ALA A 129   N  GLY A  92           
SHEET    1   D 2 ASN A 167  ARG A 171  0                                        
SHEET    2   D 2 TRP A 174  GLU A 178 -1  O  VAL A 176   N  LYS A 169           
SHEET    1   E 2 LYS A 205  THR A 209  0                                        
SHEET    2   E 2 GLY A 212  ILE A 216 -1  O  ILE A 216   N  LYS A 205           
SHEET    1   F 2 THR A 319  ARG A 320  0                                        
SHEET    2   F 2 GLY A 323  THR A 324 -1  O  GLY A 323   N  ARG A 320           
SHEET    1   G 3 ARG A 386  PRO A 388  0                                        
SHEET    2   G 3 ARG A 438  ASN A 440 -1  O  ILE A 439   N  TRP A 387           
SHEET    3   G 3 ILE A 431  GLU A 432 -1  N  GLU A 432   O  ARG A 438           
SHEET    1   H 6 LEU A 640  LEU A 645  0                                        
SHEET    2   H 6 ARG A 601  GLY A 606  1  N  VAL A 603   O  LYS A 641           
SHEET    3   H 6 MET A 562  VAL A 567  1  N  ASP A 564   O  ILE A 604           
SHEET    4   H 6 LEU A 662  GLN A 665  1  O  LEU A 662   N  VAL A 565           
SHEET    5   H 6 LEU A 687  GLY A 690  1  O  LEU A 687   N  SER A 663           
SHEET    6   H 6 PHE A 709  ILE A 710  1  O  PHE A 709   N  THR A 688           
SHEET    1   I 3 LYS B 191  SER B 192  0                                        
SHEET    2   I 3 GLN B 219  PRO B 231 -1  O  ASP B 227   N  LYS B 191           
SHEET    3   I 3 LEU B 198  PHE B 202 -1  N  LEU B 198   O  ALA B 223           
SHEET    1   J 9 LYS B 191  SER B 192  0                                        
SHEET    2   J 9 GLN B 219  PRO B 231 -1  O  ASP B 227   N  LYS B 191           
SHEET    3   J 9 VAL B 238  ARG B 247 -1  O  SER B 245   N  LEU B 224           
SHEET    4   J 9 ALA B 153  ILE B 159  1  N  GLY B 156   O  ARG B 242           
SHEET    5   J 9 ARG B  81  LEU B  85  1  N  TYR B  84   O  TYR B 155           
SHEET    6   J 9 VAL B 333  ASN B 338  1  O  ALA B 334   N  TYR B  83           
SHEET    7   J 9 PHE B 372  THR B 375  1  O  ALA B 373   N  LEU B 337           
SHEET    8   J 9 ALA B 451  GLY B 454  1  O  ALA B 451   N  TYR B 374           
SHEET    9   J 9 PHE B 479  ASN B 481  1  O  GLN B 480   N  VAL B 452           
SHEET    1   K 2 PHE B  89  TYR B  90  0                                        
SHEET    2   K 2 GLY B 130  LEU B 131 -1  O  LEU B 131   N  PHE B  89           
SHEET    1   L 2 ASN B 167  ARG B 171  0                                        
SHEET    2   L 2 TRP B 174  GLU B 178 -1  O  TRP B 174   N  ARG B 171           
SHEET    1   M 2 LYS B 205  THR B 209  0                                        
SHEET    2   M 2 GLY B 212  ILE B 216 -1  O  LYS B 214   N  GLU B 207           
SHEET    1   N 3 ARG B 386  PRO B 388  0                                        
SHEET    2   N 3 ARG B 438  ASN B 440 -1  O  ILE B 439   N  TRP B 387           
SHEET    3   N 3 ILE B 431  GLU B 432 -1  N  GLU B 432   O  ARG B 438           
SHEET    1   O 6 LEU B 640  LEU B 645  0                                        
SHEET    2   O 6 ARG B 601  GLY B 606  1  N  VAL B 603   O  LYS B 641           
SHEET    3   O 6 MET B 562  VAL B 567  1  N  ASP B 564   O  ILE B 604           
SHEET    4   O 6 LEU B 662  GLN B 665  1  O  LEU B 662   N  VAL B 565           
SHEET    5   O 6 LEU B 687  GLY B 690  1  O  LEU B 687   N  SER B 663           
SHEET    6   O 6 PHE B 709  ILE B 710  1  O  PHE B 709   N  THR B 688           
LINK         C   ILE A  13                 N   SEP A  14     1555   1555  1.33  
LINK         C   SEP A  14                 N   ILE A  15     1555   1555  1.33  
LINK         NZ  LYS A 680                 C4A PLP A 903     1555   1555  1.26  
LINK         NZ  LYS B 680                 C4A PLP B 902     1555   1555  1.28  
SITE     1 AC1 11 GLY A 135  LEU A 136  ASN A 284  ASP A 339                    
SITE     2 AC1 11 HIS A 377  ASN A 484  TYR A 573  GLU A 672                    
SITE     3 AC1 11 ALA A 673  SER A 674  GLY A 675                               
SITE     1 AC2 10 LEU B 136  ASN B 284  ASP B 339  HIS B 377                    
SITE     2 AC2 10 ASN B 484  TYR B 573  GLU B 672  ALA B 673                    
SITE     3 AC2 10 SER B 674  GLY B 675                                          
SITE     1 AC3  3 ILE A  15  ARG A  16  LYS B 205                               
SITE     1 AC4 11 TYR A  90  GLY A 134  TRP A 491  LYS A 568                    
SITE     2 AC4 11 LYS A 574  TYR A 648  ARG A 649  GLY A 675                    
SITE     3 AC4 11 THR A 676  GLY A 677  LYS A 680                               
SITE     1 AC5 12 TYR B  90  GLY B 134  TRP B 491  LYS B 568                    
SITE     2 AC5 12 LYS B 574  TYR B 648  ARG B 649  ALA B 653                    
SITE     3 AC5 12 GLY B 675  THR B 676  GLY B 677  LYS B 680                    
SITE     1 AC6  6 ASN A 282  PHE A 285  HIS A 571  ALA A 610                    
SITE     2 AC6  6 GLY A 612  TYR A 613                                          
SITE     1 AC7  6 ASN B 282  PHE B 285  HIS B 571  ALA B 610                    
SITE     2 AC7  6 GLY B 612  TYR B 613                                          
SITE     1 AC8  5 ILE B 170  ASP B 172  GLY B 173  GLU B 552                    
SITE     2 AC8  5 GLU B 646                                                     
SITE     1 AC9 10 LYS A  41  ASP A  42  GLN B  71  GLN B  72                    
SITE     2 AC9 10 ARG B 193  PHE B 196  ASP B 227  THR B 240                    
SITE     3 AC9 10 ARG B 310  ALA B 313                                          
SITE     1 BC1 10 GLN A  71  GLN A  72  ARG A 193  PHE A 196                    
SITE     2 BC1 10 ASP A 227  THR A 240  ARG A 310  ALA A 313                    
SITE     3 BC1 10 LYS B  41  ASP B  42                                          
SITE     1 BC2  8 ARG B  43  TYR B  51  GLY B 116  LEU B 531                    
SITE     2 BC2  8 ARG B 532  MET B 792  ASN B 793  PRO B 794                    
SITE     1 BC3  4 TRP A 215  ARG A 351  ILE A 356  GLY B 508                    
CRYST1  124.403  124.403  123.614  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      0.008038  0.004641  0.000000        0.00000                         
SCALE2      0.000000  0.009282  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008090        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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