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Database: PDB
Entry: 3CEM
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Original site: 3CEM 
HEADER    TRANSFERASE                             29-FEB-08   3CEM              
TITLE     HUMAN GLYCOGEN PHOSPHORYLASE (TENSE STATE) IN COMPLEX WITH THE        
TITLE    2 ALLOSTERIC INHIBITOR AVE9423                                         
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_COMMON: HUMAN;                                              
SOURCE   4 GENE: PYGL;                                                          
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    PROTEIN LIGAND COMPLEX, TENSE STATE, ALLOSTERIC INHIBITOR, ALLOSTERIC 
KEYWDS   2 ENZYME, CARBOHYDRATE METABOLISM, DISEASE MUTATION, GLYCOGEN          
KEYWDS   3 METABOLISM, GLYCOGEN STORAGE DISEASE, GLYCOSYLTRANSFERASE,           
KEYWDS   4 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, PYRIDOXAL PHOSPHATE, TRANSFERASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.U.WENDT,M.K.DREYER,O.ANDERKA,T.KLABUNDE,P.LOENZE,E.DEFOSSA,         
AUTHOR   2 D.SCHMOLL                                                            
REVDAT   4   13-JUL-11 3CEM    1       VERSN                                    
REVDAT   3   24-FEB-09 3CEM    1       VERSN                                    
REVDAT   2   03-JUN-08 3CEM    1       JRNL                                     
REVDAT   1   27-MAY-08 3CEM    0                                                
JRNL        AUTH   O.ANDERKA,P.LOENZE,T.KLABUNDE,M.K.DREYER,E.DEFOSSA,          
JRNL        AUTH 2 K.U.WENDT,D.SCHMOLL                                          
JRNL        TITL   THERMODYNAMIC CHARACTERIZATION OF ALLOSTERIC GLYCOGEN        
JRNL        TITL 2 PHOSPHORYLASE INHIBITORS.                                    
JRNL        REF    BIOCHEMISTRY                  V.  47  4683 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18373353                                                     
JRNL        DOI    10.1021/BI702397D                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.47 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) : 2.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 76582                          
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) : 0.159                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5343                            
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) : 2.47                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.53                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5322                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2140                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 378                          
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12898                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 130                                     
REMARK   3   SOLVENT ATOMS            : 501                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.351         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.238         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.161         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.119         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13370 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18103 ; 1.845 ; 1.968       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1590 ; 7.069 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   648 ;36.761 ;24.275       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2377 ;18.454 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    80 ;20.164 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1966 ; 0.127 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10128 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  6501 ; 0.230 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9090 ; 0.322 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   779 ; 0.172 ; 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):    60 ; 0.278 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.177 ; 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):  8179 ; 1.081 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12846 ; 1.809 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6031 ; 2.856 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5257 ; 4.446 ; 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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3CEM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB046681.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76587                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.470                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.390                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7 MG/ML IN 20 MM BES, 1 MM EDTA, 0.5     
REMARK 280  MM DTT, PH 6.5, 50 MM NBG, 2.5 MM AVD (AVE9423), VAPOR DIFFUSION,   
REMARK 280  HANGING DROP                                                        
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       41.14300            
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       82.28600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 56140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.9 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     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     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 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   NZ   LYS A   680     O4A  PLP A   832              1.70            
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    SER A 192   N   -  CA  -  CB  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    ARG A 277   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG A 309   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ARG A 490   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B 171   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B 184   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP B 514   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG B 575   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B 575   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 649   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B 714   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B 770   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 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    CYS A  78       63.39     36.20                                   
REMARK 500    LEU A 131       37.31    -94.56                                   
REMARK 500    TYR A 203     -142.18     67.40                                   
REMARK 500    ASP A 217       44.59     34.83                                   
REMARK 500    ASN A 235     -158.63   -150.86                                   
REMARK 500    VAL A 325      -62.38     80.11                                   
REMARK 500    ASP A 339     -163.83     63.97                                   
REMARK 500    LEU A 344      -18.07    -47.34                                   
REMARK 500    ASP A 421       68.75   -104.44                                   
REMARK 500    GLU A 434     -148.80    -54.69                                   
REMARK 500    ARG A 489      -73.09    -74.57                                   
REMARK 500    LEU A 492      -68.31   -145.92                                   
REMARK 500    LYS A 568      163.81    177.22                                   
REMARK 500    LYS A 592        3.96    -60.33                                   
REMARK 500    ASP A 593       49.06    176.54                                   
REMARK 500    PRO A 594        2.98    -64.35                                   
REMARK 500    SER A 674      -61.72   -145.79                                   
REMARK 500    THR A 676      -27.84   -141.00                                   
REMARK 500    GLN A 754       79.38   -155.12                                   
REMARK 500    HIS A 768       35.78   -143.87                                   
REMARK 500    ILE A 824      -56.11   -122.17                                   
REMARK 500    SER A 830     -144.72   -104.72                                   
REMARK 500    LEU B 131       33.97    -93.60                                   
REMARK 500    ARG B 193       70.06   -118.95                                   
REMARK 500    TYR B 203     -132.82     56.63                                   
REMARK 500    ASP B 251     -173.23   -177.00                                   
REMARK 500    ASP B 339     -164.92     69.13                                   
REMARK 500    VAL B 379      -59.85     78.71                                   
REMARK 500    LYS B 437      114.79     84.55                                   
REMARK 500    LYS B 466      -73.15   -118.52                                   
REMARK 500    GLU B 475       87.91   -156.72                                   
REMARK 500    LEU B 492      -63.77   -146.25                                   
REMARK 500    ASP B 527       96.59    -48.77                                   
REMARK 500    VAL B 555      135.69      0.41                                   
REMARK 500    ASN B 558      108.09    -59.88                                   
REMARK 500    LYS B 568      168.39    177.13                                   
REMARK 500    ASP B 593       62.08   -152.87                                   
REMARK 500    PRO B 594       -5.07    -55.52                                   
REMARK 500    LEU B 640      119.73   -161.24                                   
REMARK 500    SER B 674      -59.83   -139.21                                   
REMARK 500    HIS B 768       27.57   -140.38                                   
REMARK 500    ILE B 824      -50.83   -127.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO B  249     ASN B  250                 -149.66                    
REMARK 500 ASN B  250     ASP B  251                   45.38                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN A 250        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ARG A 309        17.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS A 315        24.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 325        24.3      L          L   OUTSIDE RANGE           
REMARK 500    ARG B 426        24.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1107        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH B1059        DISTANCE =  5.07 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 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBG B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 832                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 832                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AVD A 833                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AVD B 833                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CEH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3CEJ   RELATED DB: PDB                                   
DBREF  3CEM A   23   831  UNP    P06737   PYGL_HUMAN      24    832             
DBREF  3CEM B   23   831  UNP    P06737   PYGL_HUMAN      24    832             
SEQRES   1 A  809  ASN VAL ALA GLU LEU LYS LYS SER PHE ASN ARG HIS LEU          
SEQRES   2 A  809  HIS PHE THR LEU VAL LYS ASP ARG ASN VAL ALA THR THR          
SEQRES   3 A  809  ARG ASP TYR TYR PHE ALA LEU ALA HIS THR VAL ARG ASP          
SEQRES   4 A  809  HIS LEU VAL GLY ARG TRP ILE ARG THR GLN GLN HIS TYR          
SEQRES   5 A  809  TYR ASP LYS CYS PRO LYS ARG VAL TYR TYR LEU SER LEU          
SEQRES   6 A  809  GLU PHE TYR MET GLY ARG THR LEU GLN ASN THR MET ILE          
SEQRES   7 A  809  ASN LEU GLY LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR          
SEQRES   8 A  809  GLN LEU GLY LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU          
SEQRES   9 A  809  GLU ASP ALA GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU          
SEQRES  10 A  809  ALA ALA CYS PHE LEU ASP SER MET ALA THR LEU GLY LEU          
SEQRES  11 A  809  ALA ALA TYR GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE          
SEQRES  12 A  809  PHE ASN GLN LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU          
SEQRES  13 A  809  ALA ASP ASP TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS          
SEQRES  14 A  809  SER ARG PRO GLU PHE MET LEU PRO VAL HIS PHE TYR GLY          
SEQRES  15 A  809  LYS VAL GLU HIS THR ASN THR GLY THR LYS TRP ILE ASP          
SEQRES  16 A  809  THR GLN VAL VAL LEU ALA LEU PRO TYR ASP THR PRO VAL          
SEQRES  17 A  809  PRO GLY TYR MET ASN ASN THR VAL ASN THR MET ARG LEU          
SEQRES  18 A  809  TRP SER ALA ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP          
SEQRES  19 A  809  PHE ASN VAL GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG          
SEQRES  20 A  809  ASN LEU ALA GLU ASN ILE SER ARG VAL LEU TYR PRO ASN          
SEQRES  21 A  809  ASP ASN PHE PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN          
SEQRES  22 A  809  GLU TYR PHE VAL VAL ALA ALA THR LEU GLN ASP ILE ILE          
SEQRES  23 A  809  ARG ARG PHE LYS ALA SER LYS PHE GLY SER THR ARG GLY          
SEQRES  24 A  809  ALA GLY THR VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA          
SEQRES  25 A  809  ILE GLN LEU ASN ASP THR HIS PRO ALA LEU ALA ILE PRO          
SEQRES  26 A  809  GLU LEU MET ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO          
SEQRES  27 A  809  TRP SER LYS ALA TRP GLU LEU THR GLN LYS THR PHE ALA          
SEQRES  28 A  809  TYR THR ASN HIS THR VAL LEU PRO GLU ALA LEU GLU ARG          
SEQRES  29 A  809  TRP PRO VAL ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS          
SEQRES  30 A  809  LEU GLU ILE ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP          
SEQRES  31 A  809  ARG ILE VAL ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU          
SEQRES  32 A  809  ARG ARG MET SER LEU ILE GLU GLU GLU GLY SER LYS ARG          
SEQRES  33 A  809  ILE ASN MET ALA HIS LEU CYS ILE VAL GLY SER HIS ALA          
SEQRES  34 A  809  VAL ASN GLY VAL ALA LYS ILE HIS SER ASP ILE VAL LYS          
SEQRES  35 A  809  THR LYS VAL PHE LYS ASP PHE SER GLU LEU GLU PRO ASP          
SEQRES  36 A  809  LYS PHE GLN ASN LYS THR ASN GLY ILE THR PRO ARG ARG          
SEQRES  37 A  809  TRP LEU LEU LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE          
SEQRES  38 A  809  ALA GLU LYS ILE GLY GLU ASP TYR VAL LYS ASP LEU SER          
SEQRES  39 A  809  GLN LEU THR LYS LEU HIS SER PHE LEU GLY ASP ASP VAL          
SEQRES  40 A  809  PHE LEU ARG GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS          
SEQRES  41 A  809  LEU LYS PHE SER GLN PHE LEU GLU THR GLU TYR LYS VAL          
SEQRES  42 A  809  LYS ILE ASN PRO SER SER MET PHE ASP VAL GLN VAL LYS          
SEQRES  43 A  809  ARG ILE HIS GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU          
SEQRES  44 A  809  HIS VAL ILE THR MET TYR ASN ARG ILE LYS LYS ASP PRO          
SEQRES  45 A  809  LYS LYS LEU PHE VAL PRO ARG THR VAL ILE ILE GLY GLY          
SEQRES  46 A  809  LYS ALA ALA PRO GLY TYR HIS MET ALA LYS MET ILE ILE          
SEQRES  47 A  809  LYS LEU ILE THR SER VAL ALA ASP VAL VAL ASN ASN ASP          
SEQRES  48 A  809  PRO MET VAL GLY SER LYS LEU LYS VAL ILE PHE LEU GLU          
SEQRES  49 A  809  ASN TYR ARG VAL SER LEU ALA GLU LYS VAL ILE PRO ALA          
SEQRES  50 A  809  THR ASP LEU SER GLU GLN ILE SER THR ALA GLY THR GLU          
SEQRES  51 A  809  ALA SER GLY THR GLY ASN MET LYS PHE MET LEU ASN GLY          
SEQRES  52 A  809  ALA LEU THR ILE GLY THR MET ASP GLY ALA ASN VAL GLU          
SEQRES  53 A  809  MET ALA GLU GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE          
SEQRES  54 A  809  GLY MET ARG ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS          
SEQRES  55 A  809  GLY TYR GLU ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU          
SEQRES  56 A  809  LEU LYS LEU VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE          
SEQRES  57 A  809  SER PRO LYS GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN          
SEQRES  58 A  809  MET LEU PHE TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP          
SEQRES  59 A  809  TYR GLU ALA TYR VAL LYS CYS GLN ASP LYS VAL SER GLN          
SEQRES  60 A  809  LEU TYR MET ASN PRO LYS ALA TRP ASN THR MET VAL LEU          
SEQRES  61 A  809  LYS ASN ILE ALA ALA SER GLY LYS PHE SER SER ASP ARG          
SEQRES  62 A  809  THR ILE LYS GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU          
SEQRES  63 A  809  PRO SER ASP                                                  
SEQRES   1 B  809  ASN VAL ALA GLU LEU LYS LYS SER PHE ASN ARG HIS LEU          
SEQRES   2 B  809  HIS PHE THR LEU VAL LYS ASP ARG ASN VAL ALA THR THR          
SEQRES   3 B  809  ARG ASP TYR TYR PHE ALA LEU ALA HIS THR VAL ARG ASP          
SEQRES   4 B  809  HIS LEU VAL GLY ARG TRP ILE ARG THR GLN GLN HIS TYR          
SEQRES   5 B  809  TYR ASP LYS CYS PRO LYS ARG VAL TYR TYR LEU SER LEU          
SEQRES   6 B  809  GLU PHE TYR MET GLY ARG THR LEU GLN ASN THR MET ILE          
SEQRES   7 B  809  ASN LEU GLY LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR          
SEQRES   8 B  809  GLN LEU GLY LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU          
SEQRES   9 B  809  GLU ASP ALA GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU          
SEQRES  10 B  809  ALA ALA CYS PHE LEU ASP SER MET ALA THR LEU GLY LEU          
SEQRES  11 B  809  ALA ALA TYR GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE          
SEQRES  12 B  809  PHE ASN GLN LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU          
SEQRES  13 B  809  ALA ASP ASP TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS          
SEQRES  14 B  809  SER ARG PRO GLU PHE MET LEU PRO VAL HIS PHE TYR GLY          
SEQRES  15 B  809  LYS VAL GLU HIS THR ASN THR GLY THR LYS TRP ILE ASP          
SEQRES  16 B  809  THR GLN VAL VAL LEU ALA LEU PRO TYR ASP THR PRO VAL          
SEQRES  17 B  809  PRO GLY TYR MET ASN ASN THR VAL ASN THR MET ARG LEU          
SEQRES  18 B  809  TRP SER ALA ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP          
SEQRES  19 B  809  PHE ASN VAL GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG          
SEQRES  20 B  809  ASN LEU ALA GLU ASN ILE SER ARG VAL LEU TYR PRO ASN          
SEQRES  21 B  809  ASP ASN PHE PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN          
SEQRES  22 B  809  GLU TYR PHE VAL VAL ALA ALA THR LEU GLN ASP ILE ILE          
SEQRES  23 B  809  ARG ARG PHE LYS ALA SER LYS PHE GLY SER THR ARG GLY          
SEQRES  24 B  809  ALA GLY THR VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA          
SEQRES  25 B  809  ILE GLN LEU ASN ASP THR HIS PRO ALA LEU ALA ILE PRO          
SEQRES  26 B  809  GLU LEU MET ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO          
SEQRES  27 B  809  TRP SER LYS ALA TRP GLU LEU THR GLN LYS THR PHE ALA          
SEQRES  28 B  809  TYR THR ASN HIS THR VAL LEU PRO GLU ALA LEU GLU ARG          
SEQRES  29 B  809  TRP PRO VAL ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS          
SEQRES  30 B  809  LEU GLU ILE ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP          
SEQRES  31 B  809  ARG ILE VAL ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU          
SEQRES  32 B  809  ARG ARG MET SER LEU ILE GLU GLU GLU GLY SER LYS ARG          
SEQRES  33 B  809  ILE ASN MET ALA HIS LEU CYS ILE VAL GLY SER HIS ALA          
SEQRES  34 B  809  VAL ASN GLY VAL ALA LYS ILE HIS SER ASP ILE VAL LYS          
SEQRES  35 B  809  THR LYS VAL PHE LYS ASP PHE SER GLU LEU GLU PRO ASP          
SEQRES  36 B  809  LYS PHE GLN ASN LYS THR ASN GLY ILE THR PRO ARG ARG          
SEQRES  37 B  809  TRP LEU LEU LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE          
SEQRES  38 B  809  ALA GLU LYS ILE GLY GLU ASP TYR VAL LYS ASP LEU SER          
SEQRES  39 B  809  GLN LEU THR LYS LEU HIS SER PHE LEU GLY ASP ASP VAL          
SEQRES  40 B  809  PHE LEU ARG GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS          
SEQRES  41 B  809  LEU LYS PHE SER GLN PHE LEU GLU THR GLU TYR LYS VAL          
SEQRES  42 B  809  LYS ILE ASN PRO SER SER MET PHE ASP VAL GLN VAL LYS          
SEQRES  43 B  809  ARG ILE HIS GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU          
SEQRES  44 B  809  HIS VAL ILE THR MET TYR ASN ARG ILE LYS LYS ASP PRO          
SEQRES  45 B  809  LYS LYS LEU PHE VAL PRO ARG THR VAL ILE ILE GLY GLY          
SEQRES  46 B  809  LYS ALA ALA PRO GLY TYR HIS MET ALA LYS MET ILE ILE          
SEQRES  47 B  809  LYS LEU ILE THR SER VAL ALA ASP VAL VAL ASN ASN ASP          
SEQRES  48 B  809  PRO MET VAL GLY SER LYS LEU LYS VAL ILE PHE LEU GLU          
SEQRES  49 B  809  ASN TYR ARG VAL SER LEU ALA GLU LYS VAL ILE PRO ALA          
SEQRES  50 B  809  THR ASP LEU SER GLU GLN ILE SER THR ALA GLY THR GLU          
SEQRES  51 B  809  ALA SER GLY THR GLY ASN MET LYS PHE MET LEU ASN GLY          
SEQRES  52 B  809  ALA LEU THR ILE GLY THR MET ASP GLY ALA ASN VAL GLU          
SEQRES  53 B  809  MET ALA GLU GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE          
SEQRES  54 B  809  GLY MET ARG ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS          
SEQRES  55 B  809  GLY TYR GLU ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU          
SEQRES  56 B  809  LEU LYS LEU VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE          
SEQRES  57 B  809  SER PRO LYS GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN          
SEQRES  58 B  809  MET LEU PHE TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP          
SEQRES  59 B  809  TYR GLU ALA TYR VAL LYS CYS GLN ASP LYS VAL SER GLN          
SEQRES  60 B  809  LEU TYR MET ASN PRO LYS ALA TRP ASN THR MET VAL LEU          
SEQRES  61 B  809  LYS ASN ILE ALA ALA SER GLY LYS PHE SER SER ASP ARG          
SEQRES  62 B  809  THR ILE LYS GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU          
SEQRES  63 B  809  PRO SER ASP                                                  
HET    NBG  A   1      15                                                       
HET    NBG  B   2      15                                                       
HET    PLP  A 832      16                                                       
HET    AVD  A 833      34                                                       
HET    PLP  B 832      16                                                       
HET    AVD  B 833      34                                                       
HETNAM     NBG 1-N-ACETYL-BETA-D-GLUCOSAMINE                                    
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     AVD 1-(2-CARBOXYPHENYL)-7-CHLORO-6-[(2-CHLORO-4,6-                   
HETNAM   2 AVD  DIFLUOROPHENYL)AMINO]-4-OXO-1,4-DIHYDROQUINOLINE-3-             
HETNAM   3 AVD  CARBOXYLIC ACID                                                 
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   3  NBG    2(C8 H15 N O6)                                               
FORMUL   5  PLP    2(C8 H10 N O6 P)                                             
FORMUL   6  AVD    2(C23 H12 CL2 F2 N2 O5)                                      
FORMUL   9  HOH   *501(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  ILE A  125  1                                   8    
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  ASN A  274  1                                  14    
HELIX   10  10 ILE A  275  ARG A  277  5                                   3    
HELIX   11  11 LYS A  289  ALA A  313  1                                  25    
HELIX   12  12 VAL A  325  ASP A  327  5                                   3    
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 HIS A  571  LYS A  574  5                                   4    
HELIX   28  28 ARG A  575  LYS A  592  1                                  18    
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 ALA A  728  LEU A  735  1                                   8    
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  807  1                                  15    
HELIX   42  42 SER A  808  PHE A  811  5                                   4    
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 THR B   47  CYS B   78  1                                  32    
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  126  1                                   9    
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  ALA B  313  1                                  25    
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 VAL B  389  LEU B  396  1                                   8    
HELIX   59  59 LEU B  396  PHE B  418  1                                  23    
HELIX   60  60 ASP B  421  SER B  429  1                                   9    
HELIX   61  61 MET B  441  GLY B  448  1                                   8    
HELIX   62  62 ALA B  456  LYS B  466  1                                  11    
HELIX   63  63 PHE B  468  GLU B  475  1                                   8    
HELIX   64  64 ASN B  496  GLY B  508  1                                  13    
HELIX   65  65 GLU B  509  LYS B  513  5                                   5    
HELIX   66  66 ASP B  514  LEU B  525  5                                  12    
HELIX   67  67 ASP B  527  TYR B  553  1                                  27    
HELIX   68  68 HIS B  571  LYS B  574  5                                   4    
HELIX   69  69 ARG B  575  LYS B  592  1                                  18    
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  GLY B  748  1                                  14    
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  806  1                                  14    
HELIX   83  83 ALA B  807  PHE B  811  5                                   5    
HELIX   84  84 SER B  812  ILE B  824  1                                  13    
SHEET    1   A 3 LYS A 191  SER A 192  0                                        
SHEET    2   A 3 GLN A 219  PRO A 231 -1  O  ASP A 227   N  LYS A 191           
SHEET    3   A 3 LEU A 198  PHE A 202 -1  N  LEU A 198   O  ALA A 223           
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  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  GLN A 336   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 VAL A 452  GLY A 454  1  O  ASN A 453   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 3 ARG A 386  PRO A 388  0                                        
SHEET    2   F 3 ARG A 438  ASN A 440 -1  O  ILE A 439   N  TRP A 387           
SHEET    3   F 3 ILE A 431  GLU A 432 -1  N  GLU A 432   O  ARG A 438           
SHEET    1   G 6 LEU A 640  LEU A 645  0                                        
SHEET    2   G 6 ARG A 601  GLY A 606  1  N  VAL A 603   O  LYS A 641           
SHEET    3   G 6 MET A 562  VAL A 567  1  N  GLN A 566   O  ILE A 604           
SHEET    4   G 6 LEU A 662  GLN A 665  1  O  LEU A 662   N  VAL A 565           
SHEET    5   G 6 LEU A 687  GLY A 690  1  O  LEU A 687   N  SER A 663           
SHEET    6   G 6 PHE A 709  ILE A 710  1  O  PHE A 709   N  THR A 688           
SHEET    1   H 3 LYS B 191  SER B 192  0                                        
SHEET    2   H 3 GLN B 219  PRO B 231 -1  O  ASP B 227   N  LYS B 191           
SHEET    3   H 3 LEU B 198  PHE B 202 -1  N  VAL B 200   O  VAL B 221           
SHEET    1   I 9 LYS B 191  SER B 192  0                                        
SHEET    2   I 9 GLN B 219  PRO B 231 -1  O  ASP B 227   N  LYS B 191           
SHEET    3   I 9 VAL B 238  ARG B 247 -1  O  ARG B 247   N  LEU B 222           
SHEET    4   I 9 ALA B 154  ILE B 159  1  N  GLY B 156   O  ARG B 242           
SHEET    5   I 9 ARG B  81  LEU B  85  1  N  TYR B  84   O  TYR B 157           
SHEET    6   I 9 VAL B 333  ASN B 338  1  O  ALA B 334   N  TYR B  83           
SHEET    7   I 9 PHE B 372  THR B 375  1  O  ALA B 373   N  LEU B 337           
SHEET    8   I 9 VAL B 452  GLY B 454  1  O  ASN B 453   N  TYR B 374           
SHEET    9   I 9 PHE B 479  ASN B 481  1  O  GLN B 480   N  VAL B 452           
SHEET    1   J 2 PHE B  89  GLY B  92  0                                        
SHEET    2   J 2 ALA B 129  LEU B 131 -1  O  LEU B 131   N  PHE B  89           
SHEET    1   K 2 ASN B 167  ARG B 171  0                                        
SHEET    2   K 2 TRP B 174  GLU B 178 -1  O  VAL B 176   N  LYS B 169           
SHEET    1   L 2 LYS B 205  THR B 209  0                                        
SHEET    2   L 2 GLY B 212  ILE B 216 -1  O  LYS B 214   N  GLU B 207           
SHEET    1   M 3 ARG B 386  PRO B 388  0                                        
SHEET    2   M 3 ARG B 438  ASN B 440 -1  O  ILE B 439   N  TRP B 387           
SHEET    3   M 3 ILE B 431  GLU B 432 -1  N  GLU B 432   O  ARG B 438           
SHEET    1   N 6 LEU B 640  LEU B 645  0                                        
SHEET    2   N 6 ARG B 601  GLY B 606  1  N  VAL B 603   O  LYS B 641           
SHEET    3   N 6 MET B 562  VAL B 567  1  N  ASP B 564   O  ILE B 604           
SHEET    4   N 6 LEU B 662  GLN B 665  1  O  LEU B 662   N  VAL B 565           
SHEET    5   N 6 LEU B 687  GLY B 690  1  O  LEU B 687   N  SER B 663           
SHEET    6   N 6 PHE B 709  ILE B 710  1  O  PHE B 709   N  THR B 688           
LINK         NZ  LYS A 680                 C4A PLP A 832     1555   1555  1.42  
LINK         NZ  LYS B 680                 C4A PLP B 832     1555   1555  1.42  
CISPEP   1 THR A  324    VAL A  325          0         5.75                     
CISPEP   2 ASP B  251    PHE B  252          0        -8.75                     
SITE     1 AC1 10 GLY A 135  LEU A 136  ASN A 284  HIS A 377                    
SITE     2 AC1 10 ASN A 484  TYR A 573  GLU A 672  ALA A 673                    
SITE     3 AC1 10 SER A 674  GLY A 675                                          
SITE     1 AC2 10 GLY B 135  LEU B 136  ASN B 284  ASP B 339                    
SITE     2 AC2 10 HIS B 377  ASN B 484  TYR B 573  GLU B 672                    
SITE     3 AC2 10 SER B 674  GLY B 675                                          
SITE     1 AC3 10 TYR A  90  GLY A 134  TRP A 491  LYS A 568                    
SITE     2 AC3 10 LYS A 574  ARG A 649  GLY A 675  THR A 676                    
SITE     3 AC3 10 GLY A 677  LYS A 680                                          
SITE     1 AC4 11 GLY B 134  GLY B 135  TRP B 491  LYS B 568                    
SITE     2 AC4 11 LYS B 574  TYR B 648  ARG B 649  GLY B 675                    
SITE     3 AC4 11 THR B 676  GLY B 677  LYS B 680                               
SITE     1 AC5 12 TRP A  67  GLN A  71  TYR A  75  LYS A 191                    
SITE     2 AC5 12 ARG A 193  PHE A 196  ASP A 227  ARG A 242                    
SITE     3 AC5 12 ARG A 309  ARG A 310  LEU B  39  LYS B  41                    
SITE     1 AC6 11 LEU A  39  LYS A  41  TRP B  67  TYR B  75                    
SITE     2 AC6 11 LYS B 191  ARG B 193  PHE B 196  ASP B 227                    
SITE     3 AC6 11 ARG B 242  ARG B 309  ARG B 310                               
CRYST1  124.383  124.383  123.429  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      0.008040  0.004642  0.000000        0.00000                         
SCALE2      0.000000  0.009283  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008102        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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