GenomeNet

Database: PDB
Entry: 2ZB2
LinkDB: 2ZB2
Original site: 2ZB2 
HEADER    TRANSFERASE                             15-OCT-07   2ZB2              
TITLE     HUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH GLCOSE AND 5-     
TITLE    2 CHLORO-N-[4-(1,2-DIHYDROXYETHYL)PHENYL]-1H-INDOLE-2-CARBOXAMIDE      
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 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: LIVER;                                                       
SOURCE   6 GENE: PYGL;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET42B                                    
KEYWDS    ALLOSTERIC SITE, ALLOSTERIC BINDING, ALLOSTERIC ENZYME, CARBOHYDRATE  
KEYWDS   2 METABOLISM, DISEASE MUTATION, GLYCOGEN METABOLISM, GLYCOGEN STORAGE  
KEYWDS   3 DISEASE, GLYCOSYLTRANSFERASE, NUCLEOTIDE-BINDING, PHOSPHORYLATION,   
KEYWDS   4 PYRIDOXAL PHOSPHATE, TRANSFERASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.KATAYAMA,K.ONDA                                                     
REVDAT   3   13-JUL-11 2ZB2    1       VERSN                                    
REVDAT   2   24-FEB-09 2ZB2    1       VERSN                                    
REVDAT   1   02-SEP-08 2ZB2    0                                                
JRNL        AUTH   K.ONDA,T.SUZUKI,R.SHIRAKI,Y.YONETOKU,K.NEGORO,K.MOMOSE,      
JRNL        AUTH 2 N.KATAYAMA,M.ORITA,T.YAMAGUCHI,M.OHTA,S.TSUKAMOTO            
JRNL        TITL   SYNTHESIS OF 5-CHLORO-N-ARYL-1H-INDOLE-2-CARBOXAMIDE         
JRNL        TITL 2 DERIVATIVES AS INHIBITORS OF HUMAN LIVER GLYCOGEN            
JRNL        TITL 3 PHOSPHORYLASE A.                                             
JRNL        REF    BIOORG.MED.CHEM.              V.  16  5452 2008              
JRNL        REFN                   ISSN 0968-0896                               
JRNL        PMID   18434170                                                     
JRNL        DOI    10.1016/J.BMC.2008.04.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX2000                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 77428                          
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) : 0.300                           
REMARK   3   R VALUE            (WORKING SET) : 0.261                           
REMARK   3   FREE R VALUE                     : 0.307                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 7726                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 77428                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.60                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE                    : 0.3390                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1230                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12876                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 140                                     
REMARK   3   SOLVENT ATOMS            : 397                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.40000                                             
REMARK   3    B22 (A**2) : -1.40000                                             
REMARK   3    B33 (A**2) : 2.80000                                              
REMARK   3    B12 (A**2) : 2.29000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.34                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.27                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.42                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.32                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.77                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 2ZB2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-OCT-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB027746.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : OSCILLATION CAMERA                 
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR                       
REMARK 200  DATA SCALING SOFTWARE          : CRYSTALCLEAR                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79745                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.420                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.37400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 1.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNX2000                                               
REMARK 200 STARTING MODEL: PDB ENTRY 1EXV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM NAMES (PH6), 22.5 % MPD, 60MM D-   
REMARK 280  GLUCOSE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K            
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       41.17933            
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       82.35867            
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: 10060 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     ARG A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     ILE A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     ILE A    15                                                      
REMARK 465     ARG A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     ILE A    18                                                      
REMARK 465     VAL A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     VAL A    21                                                      
REMARK 465     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   317                                                      
REMARK 465     SER A   318                                                      
REMARK 465     THR A   319                                                      
REMARK 465     ARG A   320                                                      
REMARK 465     ASP A   831                                                      
REMARK 465     LEU A   832                                                      
REMARK 465     LYS A   833                                                      
REMARK 465     ILE A   834                                                      
REMARK 465     SER A   835                                                      
REMARK 465     LEU A   836                                                      
REMARK 465     SER A   837                                                      
REMARK 465     ASN A   838                                                      
REMARK 465     GLU A   839                                                      
REMARK 465     SER A   840                                                      
REMARK 465     ASN A   841                                                      
REMARK 465     LYS A   842                                                      
REMARK 465     VAL A   843                                                      
REMARK 465     ASN A   844                                                      
REMARK 465     GLY A   845                                                      
REMARK 465     ASN A   846                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     LYS B     9                                                      
REMARK 465     ARG B    10                                                      
REMARK 465     ARG B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     ILE B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     ILE B    15                                                      
REMARK 465     ARG B    16                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     ILE B    18                                                      
REMARK 465     VAL B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     VAL B    21                                                      
REMARK 465     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     LYS B   315                                                      
REMARK 465     PHE B   316                                                      
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     ASP B   831                                                      
REMARK 465     LEU B   832                                                      
REMARK 465     LYS B   833                                                      
REMARK 465     ILE B   834                                                      
REMARK 465     SER B   835                                                      
REMARK 465     LEU B   836                                                      
REMARK 465     SER B   837                                                      
REMARK 465     ASN B   838                                                      
REMARK 465     GLU B   839                                                      
REMARK 465     SER B   840                                                      
REMARK 465     ASN B   841                                                      
REMARK 465     LYS B   842                                                      
REMARK 465     VAL B   843                                                      
REMARK 465     ASN B   844                                                      
REMARK 465     GLY B   845                                                      
REMARK 465     ASN B   846                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS B 595    CG   CD   CE   NZ                                   
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    ARG A  43       -5.26    -55.96                                   
REMARK 500    LEU A  95      -77.90    -43.03                                   
REMARK 500    LEU A 131       42.69    -87.02                                   
REMARK 500    TYR A 203     -126.32     66.70                                   
REMARK 500    ASN A 235       22.13   -151.50                                   
REMARK 500    ASN A 236      -12.15     66.66                                   
REMARK 500    ASP A 251      178.95    -47.53                                   
REMARK 500    PRO A 281       38.07    -78.30                                   
REMARK 500    VAL A 325      -72.52    -94.88                                   
REMARK 500    ASP A 339     -172.15     70.82                                   
REMARK 500    PRO A 419        4.73    -64.19                                   
REMARK 500    GLU A 434      156.46    -46.48                                   
REMARK 500    ALA A 456      141.38   -172.08                                   
REMARK 500    ASN A 484      173.45    -59.18                                   
REMARK 500    LEU A 492      -72.94   -156.13                                   
REMARK 500    ASP A 510      -37.59    -36.52                                   
REMARK 500    ASP A 514       73.06   -162.78                                   
REMARK 500    GLN A 517        0.58    -65.87                                   
REMARK 500    VAL A 555      158.64    -36.40                                   
REMARK 500    LYS A 568      169.90    174.62                                   
REMARK 500    PRO A 594       23.98    -64.84                                   
REMARK 500    SER A 674      -64.41   -162.27                                   
REMARK 500    ILE A 715      -76.70    -32.93                                   
REMARK 500    PRO A 736      -73.05    -46.97                                   
REMARK 500    SER A 751       65.85   -168.13                                   
REMARK 500    HIS A 768       22.69   -151.83                                   
REMARK 500    ASN A 793       75.57   -115.85                                   
REMARK 500    PHE A 811       24.54    -78.75                                   
REMARK 500    ILE A 824      -49.99   -132.11                                   
REMARK 500    PRO A 829      109.61    -55.23                                   
REMARK 500    ASN B  23        0.00    168.55                                   
REMARK 500    ARG B  43       -5.15    -56.12                                   
REMARK 500    CYS B  78       59.28     39.91                                   
REMARK 500    LEU B  95      -76.90    -44.93                                   
REMARK 500    LEU B 131       42.44    -85.26                                   
REMARK 500    TYR B 203     -128.46     66.62                                   
REMARK 500    ASN B 235       21.16   -151.53                                   
REMARK 500    ASN B 236      -14.82     68.68                                   
REMARK 500    PRO B 281       39.14    -78.75                                   
REMARK 500    PHE B 326       -9.31    -54.08                                   
REMARK 500    ASP B 339     -173.49     69.57                                   
REMARK 500    PRO B 419        3.65    -64.36                                   
REMARK 500    GLU B 434      156.77    -45.93                                   
REMARK 500    ALA B 456      142.83   -171.67                                   
REMARK 500    LEU B 492      -72.41   -156.85                                   
REMARK 500    ASP B 510      -38.80    -35.52                                   
REMARK 500    ASP B 514       72.81   -161.53                                   
REMARK 500    GLN B 517        1.04    -66.86                                   
REMARK 500    VAL B 555      158.08    -36.22                                   
REMARK 500    LYS B 568      171.70    173.62                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      61 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 865        DISTANCE =  5.58 ANGSTROMS                       
REMARK 525    HOH A 899        DISTANCE =  8.26 ANGSTROMS                       
REMARK 525    HOH A 947        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH A 969        DISTANCE = 10.41 ANGSTROMS                       
REMARK 525    HOH A1020        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH B 949        DISTANCE = 12.52 ANGSTROMS                       
REMARK 525    HOH B 959        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH B 995        DISTANCE =  5.61 ANGSTROMS                       
REMARK 525    HOH B1008        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH B1009        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH B1096        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH B1111        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH B1125        DISTANCE =  9.22 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 847                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 847                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 848                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 849                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A46 A 850                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 848                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 849                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A46 B 850                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 851                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 852                 
DBREF  2ZB2 A    0   846  UNP    P06737   PYGL_HUMAN       1    847             
DBREF  2ZB2 B    0   846  UNP    P06737   PYGL_HUMAN       1    847             
SEQADV 2ZB2 GLY A   -2  UNP  P06737              EXPRESSION TAG                 
SEQADV 2ZB2 SER A   -1  UNP  P06737              EXPRESSION TAG                 
SEQADV 2ZB2 GLY B   -2  UNP  P06737              EXPRESSION TAG                 
SEQADV 2ZB2 SER B   -1  UNP  P06737              EXPRESSION TAG                 
SEQRES   1 A  849  GLY SER MET ALA LYS PRO LEU THR ASP GLN GLU LYS ARG          
SEQRES   2 A  849  ARG GLN ILE SER ILE ARG GLY ILE VAL GLY VAL GLU ASN          
SEQRES   3 A  849  VAL ALA GLU LEU LYS LYS SER PHE ASN ARG HIS LEU HIS          
SEQRES   4 A  849  PHE THR LEU VAL LYS ASP ARG ASN VAL ALA THR THR ARG          
SEQRES   5 A  849  ASP TYR TYR PHE ALA LEU ALA HIS THR VAL ARG ASP HIS          
SEQRES   6 A  849  LEU VAL GLY ARG TRP ILE ARG THR GLN GLN HIS TYR TYR          
SEQRES   7 A  849  ASP LYS CYS PRO LYS ARG VAL TYR TYR LEU SER LEU GLU          
SEQRES   8 A  849  PHE TYR MET GLY ARG THR LEU GLN ASN THR MET ILE ASN          
SEQRES   9 A  849  LEU GLY LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN          
SEQRES  10 A  849  LEU GLY LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU          
SEQRES  11 A  849  ASP ALA GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA          
SEQRES  12 A  849  ALA CYS PHE LEU ASP SER MET ALA THR LEU GLY LEU ALA          
SEQRES  13 A  849  ALA TYR GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE          
SEQRES  14 A  849  ASN GLN LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA          
SEQRES  15 A  849  ASP ASP TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS SER          
SEQRES  16 A  849  ARG PRO GLU PHE MET LEU PRO VAL HIS PHE TYR GLY LYS          
SEQRES  17 A  849  VAL GLU HIS THR ASN THR GLY THR LYS TRP ILE ASP THR          
SEQRES  18 A  849  GLN VAL VAL LEU ALA LEU PRO TYR ASP THR PRO VAL PRO          
SEQRES  19 A  849  GLY TYR MET ASN ASN THR VAL ASN THR MET ARG LEU TRP          
SEQRES  20 A  849  SER ALA ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE          
SEQRES  21 A  849  ASN VAL GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN          
SEQRES  22 A  849  LEU ALA GLU ASN ILE SER ARG VAL LEU TYR PRO ASN ASP          
SEQRES  23 A  849  ASN PHE PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU          
SEQRES  24 A  849  TYR PHE VAL VAL ALA ALA THR LEU GLN ASP ILE ILE ARG          
SEQRES  25 A  849  ARG PHE LYS ALA SER LYS PHE GLY SER THR ARG GLY ALA          
SEQRES  26 A  849  GLY THR VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE          
SEQRES  27 A  849  GLN LEU ASN ASP THR HIS PRO ALA LEU ALA ILE PRO GLU          
SEQRES  28 A  849  LEU MET ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP          
SEQRES  29 A  849  SER LYS ALA TRP GLU LEU THR GLN LYS THR PHE ALA TYR          
SEQRES  30 A  849  THR ASN HIS THR VAL LEU PRO GLU ALA LEU GLU ARG TRP          
SEQRES  31 A  849  PRO VAL ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU          
SEQRES  32 A  849  GLU ILE ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG          
SEQRES  33 A  849  ILE VAL ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG          
SEQRES  34 A  849  ARG MET SER LEU ILE GLU GLU GLU GLY SER LYS ARG ILE          
SEQRES  35 A  849  ASN MET ALA HIS LEU CYS ILE VAL GLY SER HIS ALA VAL          
SEQRES  36 A  849  ASN GLY VAL ALA LYS ILE HIS SER ASP ILE VAL LYS THR          
SEQRES  37 A  849  LYS VAL PHE LYS ASP PHE SER GLU LEU GLU PRO ASP LYS          
SEQRES  38 A  849  PHE GLN ASN LYS THR ASN GLY ILE THR PRO ARG ARG TRP          
SEQRES  39 A  849  LEU LEU LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA          
SEQRES  40 A  849  GLU LYS ILE GLY GLU ASP TYR VAL LYS ASP LEU SER GLN          
SEQRES  41 A  849  LEU THR LYS LEU HIS SER PHE LEU GLY ASP ASP VAL PHE          
SEQRES  42 A  849  LEU ARG GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU          
SEQRES  43 A  849  LYS PHE SER GLN PHE LEU GLU THR GLU TYR LYS VAL LYS          
SEQRES  44 A  849  ILE ASN PRO SER SER MET PHE ASP VAL GLN VAL LYS ARG          
SEQRES  45 A  849  ILE HIS GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS          
SEQRES  46 A  849  VAL ILE THR MET TYR ASN ARG ILE LYS LYS ASP PRO LYS          
SEQRES  47 A  849  LYS LEU PHE VAL PRO ARG THR VAL ILE ILE GLY GLY LYS          
SEQRES  48 A  849  ALA ALA PRO GLY TYR HIS MET ALA LYS MET ILE ILE LYS          
SEQRES  49 A  849  LEU ILE THR SER VAL ALA ASP VAL VAL ASN ASN ASP PRO          
SEQRES  50 A  849  MET VAL GLY SER LYS LEU LYS VAL ILE PHE LEU GLU ASN          
SEQRES  51 A  849  TYR ARG VAL SER LEU ALA GLU LYS VAL ILE PRO ALA THR          
SEQRES  52 A  849  ASP LEU SER GLU GLN ILE SER THR ALA GLY THR GLU ALA          
SEQRES  53 A  849  SER GLY THR GLY ASN MET LYS PHE MET LEU ASN GLY ALA          
SEQRES  54 A  849  LEU THR ILE GLY THR MET ASP GLY ALA ASN VAL GLU MET          
SEQRES  55 A  849  ALA GLU GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY          
SEQRES  56 A  849  MET ARG ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY          
SEQRES  57 A  849  TYR GLU ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU          
SEQRES  58 A  849  LYS LEU VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE SER          
SEQRES  59 A  849  PRO LYS GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN MET          
SEQRES  60 A  849  LEU PHE TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR          
SEQRES  61 A  849  GLU ALA TYR VAL LYS CYS GLN ASP LYS VAL SER GLN LEU          
SEQRES  62 A  849  TYR MET ASN PRO LYS ALA TRP ASN THR MET VAL LEU LYS          
SEQRES  63 A  849  ASN ILE ALA ALA SER GLY LYS PHE SER SER ASP ARG THR          
SEQRES  64 A  849  ILE LYS GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO          
SEQRES  65 A  849  SER ASP LEU LYS ILE SER LEU SER ASN GLU SER ASN LYS          
SEQRES  66 A  849  VAL ASN GLY ASN                                              
SEQRES   1 B  849  GLY SER MET ALA LYS PRO LEU THR ASP GLN GLU LYS ARG          
SEQRES   2 B  849  ARG GLN ILE SER ILE ARG GLY ILE VAL GLY VAL GLU ASN          
SEQRES   3 B  849  VAL ALA GLU LEU LYS LYS SER PHE ASN ARG HIS LEU HIS          
SEQRES   4 B  849  PHE THR LEU VAL LYS ASP ARG ASN VAL ALA THR THR ARG          
SEQRES   5 B  849  ASP TYR TYR PHE ALA LEU ALA HIS THR VAL ARG ASP HIS          
SEQRES   6 B  849  LEU VAL GLY ARG TRP ILE ARG THR GLN GLN HIS TYR TYR          
SEQRES   7 B  849  ASP LYS CYS PRO LYS ARG VAL TYR TYR LEU SER LEU GLU          
SEQRES   8 B  849  PHE TYR MET GLY ARG THR LEU GLN ASN THR MET ILE ASN          
SEQRES   9 B  849  LEU GLY LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN          
SEQRES  10 B  849  LEU GLY LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU          
SEQRES  11 B  849  ASP ALA GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA          
SEQRES  12 B  849  ALA CYS PHE LEU ASP SER MET ALA THR LEU GLY LEU ALA          
SEQRES  13 B  849  ALA TYR GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE          
SEQRES  14 B  849  ASN GLN LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA          
SEQRES  15 B  849  ASP ASP TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS SER          
SEQRES  16 B  849  ARG PRO GLU PHE MET LEU PRO VAL HIS PHE TYR GLY LYS          
SEQRES  17 B  849  VAL GLU HIS THR ASN THR GLY THR LYS TRP ILE ASP THR          
SEQRES  18 B  849  GLN VAL VAL LEU ALA LEU PRO TYR ASP THR PRO VAL PRO          
SEQRES  19 B  849  GLY TYR MET ASN ASN THR VAL ASN THR MET ARG LEU TRP          
SEQRES  20 B  849  SER ALA ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE          
SEQRES  21 B  849  ASN VAL GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN          
SEQRES  22 B  849  LEU ALA GLU ASN ILE SER ARG VAL LEU TYR PRO ASN ASP          
SEQRES  23 B  849  ASN PHE PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU          
SEQRES  24 B  849  TYR PHE VAL VAL ALA ALA THR LEU GLN ASP ILE ILE ARG          
SEQRES  25 B  849  ARG PHE LYS ALA SER LYS PHE GLY SER THR ARG GLY ALA          
SEQRES  26 B  849  GLY THR VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE          
SEQRES  27 B  849  GLN LEU ASN ASP THR HIS PRO ALA LEU ALA ILE PRO GLU          
SEQRES  28 B  849  LEU MET ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP          
SEQRES  29 B  849  SER LYS ALA TRP GLU LEU THR GLN LYS THR PHE ALA TYR          
SEQRES  30 B  849  THR ASN HIS THR VAL LEU PRO GLU ALA LEU GLU ARG TRP          
SEQRES  31 B  849  PRO VAL ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU          
SEQRES  32 B  849  GLU ILE ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG          
SEQRES  33 B  849  ILE VAL ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG          
SEQRES  34 B  849  ARG MET SER LEU ILE GLU GLU GLU GLY SER LYS ARG ILE          
SEQRES  35 B  849  ASN MET ALA HIS LEU CYS ILE VAL GLY SER HIS ALA VAL          
SEQRES  36 B  849  ASN GLY VAL ALA LYS ILE HIS SER ASP ILE VAL LYS THR          
SEQRES  37 B  849  LYS VAL PHE LYS ASP PHE SER GLU LEU GLU PRO ASP LYS          
SEQRES  38 B  849  PHE GLN ASN LYS THR ASN GLY ILE THR PRO ARG ARG TRP          
SEQRES  39 B  849  LEU LEU LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA          
SEQRES  40 B  849  GLU LYS ILE GLY GLU ASP TYR VAL LYS ASP LEU SER GLN          
SEQRES  41 B  849  LEU THR LYS LEU HIS SER PHE LEU GLY ASP ASP VAL PHE          
SEQRES  42 B  849  LEU ARG GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU          
SEQRES  43 B  849  LYS PHE SER GLN PHE LEU GLU THR GLU TYR LYS VAL LYS          
SEQRES  44 B  849  ILE ASN PRO SER SER MET PHE ASP VAL GLN VAL LYS ARG          
SEQRES  45 B  849  ILE HIS GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS          
SEQRES  46 B  849  VAL ILE THR MET TYR ASN ARG ILE LYS LYS ASP PRO LYS          
SEQRES  47 B  849  LYS LEU PHE VAL PRO ARG THR VAL ILE ILE GLY GLY LYS          
SEQRES  48 B  849  ALA ALA PRO GLY TYR HIS MET ALA LYS MET ILE ILE LYS          
SEQRES  49 B  849  LEU ILE THR SER VAL ALA ASP VAL VAL ASN ASN ASP PRO          
SEQRES  50 B  849  MET VAL GLY SER LYS LEU LYS VAL ILE PHE LEU GLU ASN          
SEQRES  51 B  849  TYR ARG VAL SER LEU ALA GLU LYS VAL ILE PRO ALA THR          
SEQRES  52 B  849  ASP LEU SER GLU GLN ILE SER THR ALA GLY THR GLU ALA          
SEQRES  53 B  849  SER GLY THR GLY ASN MET LYS PHE MET LEU ASN GLY ALA          
SEQRES  54 B  849  LEU THR ILE GLY THR MET ASP GLY ALA ASN VAL GLU MET          
SEQRES  55 B  849  ALA GLU GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY          
SEQRES  56 B  849  MET ARG ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY          
SEQRES  57 B  849  TYR GLU ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU          
SEQRES  58 B  849  LYS LEU VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE SER          
SEQRES  59 B  849  PRO LYS GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN MET          
SEQRES  60 B  849  LEU PHE TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR          
SEQRES  61 B  849  GLU ALA TYR VAL LYS CYS GLN ASP LYS VAL SER GLN LEU          
SEQRES  62 B  849  TYR MET ASN PRO LYS ALA TRP ASN THR MET VAL LEU LYS          
SEQRES  63 B  849  ASN ILE ALA ALA SER GLY LYS PHE SER SER ASP ARG THR          
SEQRES  64 B  849  ILE LYS GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO          
SEQRES  65 B  849  SER ASP LEU LYS ILE SER LEU SER ASN GLU SER ASN LYS          
SEQRES  66 B  849  VAL ASN GLY ASN                                              
HET    GLC  A 847      12                                                       
HET    GLC  B 847      12                                                       
HET    MES  A 848      12                                                       
HET    PLP  A 849      15                                                       
HET    A46  A 850      23                                                       
HET    MES  B 848      12                                                       
HET    PLP  B 849      15                                                       
HET    A46  B 850      23                                                       
HET    MPD  B 851       8                                                       
HET    MPD  B 852       8                                                       
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     A46 5-CHLORO-N-{4-[(1R)-1,2-DIHYDROXYETHYL]PHENYL}-1H-               
HETNAM   2 A46  INDOLE-2-CARBOXAMIDE                                            
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   3  GLC    2(C6 H12 O6)                                                 
FORMUL   5  MES    2(C6 H13 N O4 S)                                             
FORMUL   6  PLP    2(C8 H10 N O6 P)                                             
FORMUL   7  A46    2(C17 H15 CL N2 O3)                                          
FORMUL  11  MPD    2(C6 H14 O2)                                                 
FORMUL  13  HOH   *397(H2 O)                                                    
HELIX    1   1 GLU A   22  THR A   38  1                                  17    
HELIX    2   2 THR A   47  HIS A   62  1                                  16    
HELIX    3   3 LEU A   63  CYS A   78  1                                  16    
HELIX    4   4 THR A   94  LEU A  102  1                                   9    
HELIX    5   5 LEU A  104  LEU A  115  1                                  12    
HELIX    6   6 ASP A  118  GLU A  124  1                                   7    
HELIX    7   7 GLY A  135  LEU A  150  1                                  16    
HELIX    8   8 PRO A  194  MET A  197  5                                   4    
HELIX    9   9 GLY A  260  ASP A  268  1                                   9    
HELIX   10  10 ASP A  268  ASN A  274  1                                   7    
HELIX   11  11 ILE A  275  ARG A  277  5                                   3    
HELIX   12  12 LYS A  289  ALA A  313  1                                  25    
HELIX   13  13 VAL A  325  ASP A  331  5                                   7    
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  THR A  551  1                                  25    
HELIX   27  27 ARG A  575  ASP A  593  1                                  19    
HELIX   28  28 TYR A  613  ASN A  632  1                                  20    
HELIX   29  29 VAL A  636  SER A  638  5                                   3    
HELIX   30  30 ARG A  649  ILE A  657  1                                   9    
HELIX   31  31 PRO A  658  THR A  660  5                                   3    
HELIX   32  32 THR A  676  ASN A  684  1                                   9    
HELIX   33  33 ALA A  695  GLY A  704  1                                  10    
HELIX   34  34 GLU A  705  LEU A  708  5                                   4    
HELIX   35  35 ARG A  714  GLY A  725  1                                  12    
HELIX   36  36 ALA A  728  LEU A  735  1                                   8    
HELIX   37  37 LEU A  735  GLY A  748  1                                  14    
HELIX   38  38 PHE A  758  HIS A  768  1                                  11    
HELIX   39  39 LYS A  772  MET A  792  1                                  21    
HELIX   40  40 ASN A  793  ALA A  806  1                                  14    
HELIX   41  41 ALA A  807  PHE A  811  5                                   5    
HELIX   42  42 SER A  812  ILE A  824  1                                  13    
HELIX   43  43 ASN B   23  THR B   38  1                                  16    
HELIX   44  44 THR B   47  HIS B   62  1                                  16    
HELIX   45  45 LEU B   63  CYS B   78  1                                  16    
HELIX   46  46 THR B   94  LEU B  102  1                                   9    
HELIX   47  47 LEU B  104  LEU B  115  1                                  12    
HELIX   48  48 ASP B  118  GLU B  124  1                                   7    
HELIX   49  49 GLY B  135  LEU B  150  1                                  16    
HELIX   50  50 PRO B  194  MET B  197  5                                   4    
HELIX   51  51 GLY B  260  ASP B  268  1                                   9    
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 THR B  324  ASP B  331  5                                   8    
HELIX   56  56 LEU B  344  ILE B  356  1                                  13    
HELIX   57  57 PRO B  360  THR B  371  1                                  12    
HELIX   58  58 LEU B  380  LEU B  384  5                                   5    
HELIX   59  59 VAL B  389  LEU B  396  1                                   8    
HELIX   60  60 LEU B  396  PHE B  418  1                                  23    
HELIX   61  61 ASP B  421  SER B  429  1                                   9    
HELIX   62  62 MET B  441  GLY B  448  1                                   8    
HELIX   63  63 ALA B  456  LYS B  466  1                                  11    
HELIX   64  64 PHE B  468  GLU B  475  1                                   8    
HELIX   65  65 ASN B  496  GLY B  508  1                                  13    
HELIX   66  66 GLU B  509  LYS B  513  5                                   5    
HELIX   67  67 ASP B  514  LEU B  525  5                                  12    
HELIX   68  68 ASP B  527  THR B  551  1                                  25    
HELIX   69  69 ARG B  575  ASP B  593  1                                  19    
HELIX   70  70 TYR B  613  ASN B  632  1                                  20    
HELIX   71  71 VAL B  636  SER B  638  5                                   3    
HELIX   72  72 ARG B  649  ILE B  657  1                                   9    
HELIX   73  73 PRO B  658  THR B  660  5                                   3    
HELIX   74  74 THR B  676  ASN B  684  1                                   9    
HELIX   75  75 ALA B  695  GLY B  704  1                                  10    
HELIX   76  76 GLU B  705  LEU B  708  5                                   4    
HELIX   77  77 ARG B  714  GLY B  725  1                                  12    
HELIX   78  78 ALA B  728  LEU B  735  1                                   8    
HELIX   79  79 LEU B  735  GLY B  748  1                                  14    
HELIX   80  80 PHE B  758  HIS B  768  1                                  11    
HELIX   81  81 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  VAL A  82   O  TYR A 155           
SHEET    6   B 9 VAL A 333  ASN A 338  1  O  ALA A 334   N  TYR A  83           
SHEET    7   B 9 PHE A 372  THR A 375  1  O  ALA A 373   N  LEU A 337           
SHEET    8   B 9 ALA A 451  GLY A 454  1  O  ALA A 451   N  TYR A 374           
SHEET    9   B 9 PHE A 479  ASN A 481  1  O  GLN A 480   N  VAL A 452           
SHEET    1   C 2 PHE A  89  GLY A  92  0                                        
SHEET    2   C 2 ALA A 129  LEU A 131 -1  O  LEU A 131   N  PHE A  89           
SHEET    1   D 2 ASN A 167  ARG A 171  0                                        
SHEET    2   D 2 TRP A 174  GLU A 178 -1  O  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  ILE A 605   O  ILE A 643           
SHEET    3   G 6 MET A 562  VAL A 567  1  N  ASP A 564   O  ILE A 604           
SHEET    4   G 6 LEU A 662  GLN A 665  1  O  GLU A 664   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  LEU B 198   O  ALA B 223           
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  VAL B  82   O  TYR B 155           
SHEET    6   I 9 VAL B 333  ASN B 338  1  O  ALA B 334   N  TYR B  83           
SHEET    7   I 9 PHE B 372  THR B 375  1  O  ALA B 373   N  LEU B 337           
SHEET    8   I 9 ALA B 451  GLY B 454  1  O  ALA B 451   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  TYR B  90  0                                        
SHEET    2   J 2 GLY B 130  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  ILE B 216   N  LYS B 205           
SHEET    1   M 3 ARG B 386  PRO B 388  0                                        
SHEET    2   M 3 ARG B 438  ASN B 440 -1  O  ILE B 439   N  TRP B 387           
SHEET    3   M 3 ILE B 431  GLU B 432 -1  N  GLU B 432   O  ARG B 438           
SHEET    1   N 6 LEU B 640  LEU B 645  0                                        
SHEET    2   N 6 ARG B 601  GLY B 606  1  N  VAL B 603   O  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 849     1555   1555  1.44  
LINK         NZ  LYS B 680                 C4A PLP B 849     1555   1555  1.40  
SITE     1 AC1 12 GLY A 134  GLY A 135  LEU A 136  ASN A 284                    
SITE     2 AC1 12 HIS A 377  ASN A 484  TYR A 573  GLU A 672                    
SITE     3 AC1 12 ALA A 673  SER A 674  GLY A 675  HOH A1008                    
SITE     1 AC2 14 GLY B 134  GLY B 135  LEU B 136  LEU B 139                    
SITE     2 AC2 14 ASN B 284  HIS B 377  ASN B 484  TYR B 573                    
SITE     3 AC2 14 GLU B 672  ALA B 673  SER B 674  GLY B 675                    
SITE     4 AC2 14 HOH B 981  HOH B1043                                          
SITE     1 AC3  6 GLN A  71  ARG A  81  TYR A 155  PHE A 196                    
SITE     2 AC3  6 ARG A 242  ARG A 310                                          
SITE     1 AC4 13 GLY A 134  GLY A 135  LYS A 568  LYS A 574                    
SITE     2 AC4 13 TYR A 648  ARG A 649  ALA A 653  GLY A 675                    
SITE     3 AC4 13 THR A 676  GLY A 677  LYS A 680  HOH A 920                    
SITE     4 AC4 13 HOH A1008                                                     
SITE     1 AC5 13 ARG A  60  LEU A  63  TRP A  67  PRO A 188                    
SITE     2 AC5 13 GLU A 190  LYS A 191  HOH A 999  THR B  38                    
SITE     3 AC5 13 PHE B  53  HIS B  57  TYR B 185  GLY B 186                    
SITE     4 AC5 13 PRO B 188                                                     
SITE     1 AC6 10 HOH A 935  GLN B  71  GLN B  72  TYR B  75                    
SITE     2 AC6 10 ARG B 193  PHE B 196  HOH B 983  HOH B1006                    
SITE     3 AC6 10 HOH B1081  HOH B1128                                          
SITE     1 AC7 13 GLY B 134  GLY B 135  TRP B 491  LYS B 568                    
SITE     2 AC7 13 LYS B 574  ARG B 649  ALA B 653  GLY B 675                    
SITE     3 AC7 13 THR B 676  GLY B 677  LYS B 680  HOH B 981                    
SITE     4 AC7 13 HOH B1003                                                     
SITE     1 AC8 11 THR A  38  PHE A  53  HIS A  57  TYR A 185                    
SITE     2 AC8 11 ARG B  60  LEU B  63  TRP B  67  PRO B 188                    
SITE     3 AC8 11 GLU B 190  LYS B 191  HOH B 969                               
SITE     1 AC9  4 TRP B  67  ILE B  68  ARG B 193  HOH B1084                    
SITE     1 BC1  4 TRP A  67  GLN A  71  ARG A 193  LYS B  41                    
CRYST1  123.819  123.819  123.538  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      0.008076  0.004663  0.000000        0.00000                         
SCALE2      0.000000  0.009326  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008095        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system