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Database: PDB
Entry: 3CEJ
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Original site: 3CEJ 
HEADER    TRANSFERASE                             29-FEB-08   3CEJ              
TITLE     HUMAN GLYCOGEN PHOSPHORYLASE (TENSE STATE) IN COMPLEX WITH THE        
TITLE    2 ALLOSTERIC INHIBITOR AVE2865                                         
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 3CEJ    1       VERSN                                    
REVDAT   3   24-FEB-09 3CEJ    1       VERSN                                    
REVDAT   2   03-JUN-08 3CEJ    1       JRNL                                     
REVDAT   1   27-MAY-08 3CEJ    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.    3.30 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) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.47                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 81.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 25212                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1257                            
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) : 3.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.38                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1794                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.78                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 91                           
REMARK   3   BIN FREE R VALUE                    : 0.3540                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12830                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 124                                     
REMARK   3   SOLVENT ATOMS            : 141                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.04000                                              
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : -0.06000                                             
REMARK   3    B12 (A**2) : 0.02000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.720         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.477         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.423        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.807                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13250 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17932 ; 1.259 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1574 ; 6.005 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   638 ;38.435 ;24.295       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2360 ;18.882 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;20.061 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1956 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10010 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  8031 ; 0.240 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9013 ; 0.318 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   656 ; 0.185 ; 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):    73 ; 0.248 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.152 ; 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):  8062 ; 0.354 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12744 ; 0.644 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5891 ; 0.728 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5188 ; 1.220 ; 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 3CEJ 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 RCSB046679.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
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   : 25212                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.8                               
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   (%): 57.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP, 7 MG/ML   
REMARK 280  IN 20 MM BES, 1 MM EDTA, 0.5 MM DTT, PH 6.5, 50 MM NBG, 2.5 MM      
REMARK 280  AVF (AVE2865)                                                       
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       40.62667            
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       81.25333            
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: 6910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 55150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.7 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     ASN A   250                                                      
REMARK 465     ASP A   251                                                      
REMARK 465     PHE A   252                                                      
REMARK 465     ASN A   253                                                      
REMARK 465     LEU A   254                                                      
REMARK 465     ARG A   255                                                      
REMARK 465     ASP A   256                                                      
REMARK 465     PHE A   257                                                      
REMARK 465     ASN A   258                                                      
REMARK 465     VAL A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   317                                                      
REMARK 465     SER A   318                                                      
REMARK 465     THR A   319                                                      
REMARK 465     ARG A   320                                                      
REMARK 465     GLY A   321                                                      
REMARK 465     ALA A   322                                                      
REMARK 465     GLY A   323                                                      
REMARK 465     THR A   324                                                      
REMARK 465     ASN B   250                                                      
REMARK 465     ASP B   251                                                      
REMARK 465     PHE B   252                                                      
REMARK 465     ASN B   253                                                      
REMARK 465     LEU B   254                                                      
REMARK 465     ARG B   255                                                      
REMARK 465     ASP B   256                                                      
REMARK 465     PHE B   257                                                      
REMARK 465     ASN B   258                                                      
REMARK 465     VAL B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   317                                                      
REMARK 465     SER B   318                                                      
REMARK 465     THR B   319                                                      
REMARK 465     ARG B   320                                                      
REMARK 465     GLY B   321                                                      
REMARK 465     ALA B   322                                                      
REMARK 465     GLY B   323                                                      
REMARK 465     THR B   324                                                      
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 B   680     O4A  PLP B   832              1.94            
REMARK 500   OG1  THR B   668     O    PHE B   771              2.15            
REMARK 500   O    LYS B   680     N    MET B   682              2.18            
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    HIS A  62       36.27    -81.16                                   
REMARK 500    LEU A  63      -40.16   -145.96                                   
REMARK 500    CYS A  78       74.64     50.68                                   
REMARK 500    ALA A 129       77.40    -67.77                                   
REMARK 500    ASN A 133      -71.08    -82.23                                   
REMARK 500    MET A 147      -35.55    -35.33                                   
REMARK 500    TYR A 155     -156.00   -132.59                                   
REMARK 500    ASP A 172       41.98     71.06                                   
REMARK 500    ASP A 180       58.59    -94.89                                   
REMARK 500    ASP A 181       54.63    -62.39                                   
REMARK 500    TYR A 203     -152.25     67.11                                   
REMARK 500    THR A 211       39.71    -84.93                                   
REMARK 500    ASN A 235       -0.69   -156.05                                   
REMARK 500    ASN A 236      -14.15     72.36                                   
REMARK 500    ARG A 247      163.13    177.92                                   
REMARK 500    ARG A 277      -72.06    -79.42                                   
REMARK 500    ASN A 284       62.94     29.20                                   
REMARK 500    SER A 314     -154.39    -80.74                                   
REMARK 500    LYS A 315       42.39    -98.34                                   
REMARK 500    ASP A 339     -172.49     64.56                                   
REMARK 500    PHE A 353      -72.31    -79.72                                   
REMARK 500    LYS A 358       36.50     39.86                                   
REMARK 500    TRP A 361      -71.02    -36.66                                   
REMARK 500    VAL A 379      -62.84   -127.86                                   
REMARK 500    LEU A 380      124.73    -34.10                                   
REMARK 500    GLU A 433       39.62    -81.72                                   
REMARK 500    LYS A 457      -57.75    -27.36                                   
REMARK 500    LYS A 464      -75.36    -67.28                                   
REMARK 500    LYS A 466      -70.74   -105.65                                   
REMARK 500    GLU A 475      101.44   -166.92                                   
REMARK 500    ASP A 477       -2.23    -59.79                                   
REMARK 500    ASN A 484      170.66    -55.82                                   
REMARK 500    ILE A 486      114.54   -160.85                                   
REMARK 500    PRO A 488        1.73    -66.70                                   
REMARK 500    ARG A 489      -70.81    -80.49                                   
REMARK 500    LEU A 492      -76.83   -129.43                                   
REMARK 500    GLU A 509       17.33   -144.43                                   
REMARK 500    SER A 516       34.21    -59.51                                   
REMARK 500    LYS A 520        0.69    -63.55                                   
REMARK 500    ASP A 527      112.15    -27.97                                   
REMARK 500    LYS A 554       70.44   -104.60                                   
REMARK 500    LYS A 568     -177.28    176.99                                   
REMARK 500    LYS A 591      -70.26    -65.14                                   
REMARK 500    LYS A 592      -35.95    -37.98                                   
REMARK 500    ASP A 593      102.91   -162.23                                   
REMARK 500    ASN A 647       64.42     34.20                                   
REMARK 500    ALA A 659       49.86   -100.08                                   
REMARK 500    ILE A 666       47.96   -101.13                                   
REMARK 500    ALA A 669      108.76    -50.04                                   
REMARK 500    SER A 674      -48.04   -166.88                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     100 RAMACHANDRAN OUTLIERS.                        
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 A 894        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH B 871        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH B 897        DISTANCE =  5.19 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 AVF A 833                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AVF B 833                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CEH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3CEM   RELATED DB: PDB                                   
DBREF  3CEJ A   23   831  UNP    P06737   PYGL_HUMAN      24    832             
DBREF  3CEJ 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    AVF  A 833      31                                                       
HET    PLP  B 832      16                                                       
HET    AVF  B 833      31                                                       
HETNAM     NBG 1-N-ACETYL-BETA-D-GLUCOSAMINE                                    
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     AVF 1-{2-[3-(2-CHLORO-4,5-DIFLUORO-BENZOYL)-UREIDO]-4-               
HETNAM   2 AVF  FLUORO-PHENYL}-PIPERIDINE-4-CARBOXYLIC ACID                     
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
HETSYN     AVF 1-[2-({[(2-CHLORO-4,5-DIFLUOROPHENYL)                            
HETSYN   2 AVF  CARBONYL]CARBAMOYL}AMINO)-4-FLUOROPHENYL]PIPERIDINE-4-          
HETSYN   3 AVF  CARBOXYLIC ACID                                                 
FORMUL   3  NBG    2(C8 H15 N O6)                                               
FORMUL   5  PLP    2(C8 H10 N O6 P)                                             
FORMUL   6  AVF    2(C20 H17 CL F3 N3 O4)                                       
FORMUL   9  HOH   *141(H2 O)                                                    
HELIX    1   1 ASN A   23  THR A   38  1                                  16    
HELIX    2   2 THR A   47  CYS A   78  1                                  32    
HELIX    3   3 THR A   94  LEU A  102  1                                   9    
HELIX    4   4 LEU A  104  LEU A  115  1                                  12    
HELIX    5   5 ASP A  118  GLU A  126  1                                   9    
HELIX    6   6 GLY A  134  LEU A  150  1                                  17    
HELIX    7   7 PRO A  194  MET A  197  5                                   4    
HELIX    8   8 ASP A  261  ASP A  268  1                                   8    
HELIX    9   9 ARG A  269  ALA A  272  5                                   4    
HELIX   10  10 LYS A  289  SER A  314  1                                  26    
HELIX   11  11 ALA A  328  GLN A  332  1                                   5    
HELIX   12  12 LEU A  344  ASP A  355  1                                  12    
HELIX   13  13 PRO A  360  THR A  371  1                                  12    
HELIX   14  14 LEU A  380  LEU A  384  5                                   5    
HELIX   15  15 VAL A  389  LEU A  396  1                                   8    
HELIX   16  16 LEU A  396  PHE A  418  1                                  23    
HELIX   17  17 ARG A  424  SER A  429  1                                   6    
HELIX   18  18 MET A  441  SER A  449  1                                   9    
HELIX   19  19 ALA A  456  LYS A  466  1                                  11    
HELIX   20  20 PHE A  468  GLU A  475  1                                   8    
HELIX   21  21 ASN A  496  ILE A  507  1                                  12    
HELIX   22  22 GLU A  509  LYS A  513  5                                   5    
HELIX   23  23 GLN A  517  LEU A  525  5                                   9    
HELIX   24  24 ASP A  527  TYR A  553  1                                  27    
HELIX   25  25 ARG A  575  ASP A  593  1                                  19    
HELIX   26  26 TYR A  613  ASP A  633  1                                  21    
HELIX   27  27 VAL A  636  SER A  638  5                                   3    
HELIX   28  28 ARG A  649  ILE A  657  1                                   9    
HELIX   29  29 PRO A  658  THR A  660  5                                   3    
HELIX   30  30 THR A  676  LEU A  683  1                                   8    
HELIX   31  31 ALA A  695  GLY A  704  1                                  10    
HELIX   32  32 ARG A  714  GLY A  725  1                                  12    
HELIX   33  33 ALA A  728  ALA A  734  1                                   7    
HELIX   34  34 LEU A  735  GLY A  748  1                                  14    
HELIX   35  35 PHE A  758  HIS A  768  1                                  11    
HELIX   36  36 ASP A  776  ASN A  793  1                                  18    
HELIX   37  37 ASN A  793  ALA A  807  1                                  15    
HELIX   38  38 SER A  808  PHE A  811  5                                   4    
HELIX   39  39 SER A  812  ILE A  824  1                                  13    
HELIX   40  40 ASN B   23  THR B   38  1                                  16    
HELIX   41  41 THR B   47  CYS B   78  1                                  32    
HELIX   42  42 THR B   94  LEU B  102  1                                   9    
HELIX   43  43 LEU B  104  LEU B  115  1                                  12    
HELIX   44  44 ASP B  118  GLU B  126  1                                   9    
HELIX   45  45 GLY B  134  LEU B  150  1                                  17    
HELIX   46  46 ASP B  261  ASN B  274  1                                  14    
HELIX   47  47 LYS B  289  SER B  314  1                                  26    
HELIX   48  48 ALA B  328  GLN B  332  1                                   5    
HELIX   49  49 THR B  340  ALA B  343  5                                   4    
HELIX   50  50 LEU B  344  ASP B  355  1                                  12    
HELIX   51  51 PRO B  360  THR B  371  1                                  12    
HELIX   52  52 VAL B  389  LEU B  396  1                                   8    
HELIX   53  53 LEU B  396  PHE B  418  1                                  23    
HELIX   54  54 ASP B  421  MET B  428  1                                   8    
HELIX   55  55 MET B  441  SER B  449  1                                   9    
HELIX   56  56 ALA B  456  LYS B  466  1                                  11    
HELIX   57  57 PHE B  468  GLU B  473  1                                   6    
HELIX   58  58 GLU B  475  ASP B  477  5                                   3    
HELIX   59  59 ASN B  496  ILE B  507  1                                  12    
HELIX   60  60 ASP B  514  LEU B  525  5                                  12    
HELIX   61  61 ASP B  527  TYR B  553  1                                  27    
HELIX   62  62 HIS B  571  LYS B  574  5                                   4    
HELIX   63  63 ARG B  575  LYS B  592  1                                  18    
HELIX   64  64 TYR B  613  ASP B  633  1                                  21    
HELIX   65  65 ARG B  649  ILE B  657  1                                   9    
HELIX   66  66 PRO B  658  THR B  660  5                                   3    
HELIX   67  67 THR B  676  LEU B  683  1                                   8    
HELIX   68  68 ALA B  695  GLY B  704  1                                  10    
HELIX   69  69 GLU B  705  LEU B  708  5                                   4    
HELIX   70  70 ARG B  714  GLY B  725  1                                  12    
HELIX   71  71 ALA B  728  GLU B  733  1                                   6    
HELIX   72  72 LEU B  735  GLY B  748  1                                  14    
HELIX   73  73 PHE B  758  HIS B  768  1                                  11    
HELIX   74  74 ASP B  776  MET B  792  1                                  17    
HELIX   75  75 ASN B  793  SER B  808  1                                  16    
HELIX   76  76 GLY B  809  PHE B  811  5                                   3    
HELIX   77  77 SER B  812  ILE B  824  1                                  13    
SHEET    1   A 5 ARG A  81  LEU A  85  0                                        
SHEET    2   A 5 VAL A 333  ASN A 338  1  O  GLN A 336   N  TYR A  83           
SHEET    3   A 5 PHE A 372  ASN A 376  1  O  ALA A 373   N  LEU A 337           
SHEET    4   A 5 VAL A 452  GLY A 454  1  O  ASN A 453   N  ASN A 376           
SHEET    5   A 5 PHE A 479  ASN A 481  1  O  GLN A 480   N  VAL A 452           
SHEET    1   B 2 PHE A  89  GLY A  92  0                                        
SHEET    2   B 2 ALA A 129  LEU A 131 -1  O  LEU A 131   N  PHE A  89           
SHEET    1   C 4 TYR A 157  ILE A 159  0                                        
SHEET    2   C 4 VAL A 238  ARG A 247  1  O  ARG A 242   N  GLY A 158           
SHEET    3   C 4 GLN A 219  PRO A 231 -1  N  TYR A 226   O  LEU A 243           
SHEET    4   C 4 LYS A 191  SER A 192 -1  N  LYS A 191   O  ASP A 227           
SHEET    1   D 4 TYR A 157  ILE A 159  0                                        
SHEET    2   D 4 VAL A 238  ARG A 247  1  O  ARG A 242   N  GLY A 158           
SHEET    3   D 4 GLN A 219  PRO A 231 -1  N  TYR A 226   O  LEU A 243           
SHEET    4   D 4 LEU A 198  PHE A 202 -1  N  LEU A 198   O  ALA A 223           
SHEET    1   E 2 ASN A 167  ILE A 170  0                                        
SHEET    2   E 2 GLN A 175  GLU A 178 -1  O  VAL A 176   N  LYS A 169           
SHEET    1   F 2 GLU A 207  THR A 209  0                                        
SHEET    2   F 2 GLY A 212  LYS A 214 -1  O  LYS A 214   N  GLU A 207           
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  ILE A 643           
SHEET    3   H 6 MET A 562  VAL A 567  1  N  GLN A 566   O  ILE A 604           
SHEET    4   H 6 LEU A 662  GLN A 665  1  O  LEU A 662   N  PHE A 563           
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  PHE B 202   O  GLN B 219           
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  LEU B 243   N  TYR B 226           
SHEET    4   J 9 ALA B 154  ILE B 159  1  N  GLY B 156   O  ARG B 242           
SHEET    5   J 9 ARG B  81  LEU B  85  1  N  VAL B  82   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 VAL B 452  GLY B 454  1  O  ASN B 453   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  GLU B 178   N  ASN B 167           
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  ILE B 605   O  LEU B 645           
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  PHE B 563           
SHEET    5   O 6 LEU B 687  THR B 691  1  O  ILE B 689   N  GLN B 665           
SHEET    6   O 6 PHE B 709  PHE B 711  1  O  PHE B 709   N  GLY B 690           
LINK         NZ  LYS A 680                 C4A PLP A 832     1555   1555  1.85  
LINK         NZ  LYS B 680                 C4A PLP B 832     1555   1555  1.49  
SITE     1 AC1 12 LEU A 136  LEU A 139  ASN A 284  HIS A 377                    
SITE     2 AC1 12 THR A 378  ASN A 484  TYR A 573  GLU A 672                    
SITE     3 AC1 12 ALA A 673  SER A 674  GLY A 675  THR A 676                    
SITE     1 AC2  9 LEU B 136  ASN B 284  HIS B 377  ASN B 484                    
SITE     2 AC2  9 TYR B 573  GLU B 672  ALA B 673  SER B 674                    
SITE     3 AC2  9 GLY B 675                                                     
SITE     1 AC3 11 GLY A 135  TRP A 491  LYS A 568  LYS A 574                    
SITE     2 AC3 11 TYR A 648  ARG A 649  GLY A 675  THR A 676                    
SITE     3 AC3 11 GLY A 677  ASN A 678  LYS A 680                               
SITE     1 AC4  9 GLY B 135  LYS B 568  LYS B 574  TYR B 648                    
SITE     2 AC4  9 ARG B 649  ALA B 653  THR B 676  GLY B 677                    
SITE     3 AC4  9 LYS B 680                                                     
SITE     1 AC5 12 TRP A  67  ILE A  68  GLN A  71  GLN A  72                    
SITE     2 AC5 12 LYS A 191  ARG A 193  ARG A 309  ARG A 310                    
SITE     3 AC5 12 LEU B  39  LYS B  41  ASP B  42  ASN B  44                    
SITE     1 AC6 12 LEU A  39  LYS A  41  ASP A  42  ASN A  44                    
SITE     2 AC6 12 TRP B  67  ILE B  68  GLN B  71  GLN B  72                    
SITE     3 AC6 12 LYS B 191  ARG B 193  PHE B 196  ARG B 310                    
CRYST1  123.270  123.270  121.880  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      0.008112  0.004684  0.000000        0.00000                         
SCALE2      0.000000  0.009367  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008205        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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