GenomeNet

Database: PDB
Entry: 1BG3
LinkDB: 1BG3
Original site: 1BG3 
HEADER    HEXOKINASE                              04-JUN-98   1BG3              
TITLE     RAT BRAIN HEXOKINASE TYPE I COMPLEX WITH GLUCOSE AND                  
TITLE    2 INHIBITOR GLUCOSE-6-PHOSPHATE                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEXOKINASE;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ATP-D-HEXOSE-6-PHOSPHOTRANSFERASE;                          
COMPND   5 EC: 2.7.1.1;                                                         
COMPND   6 OTHER_DETAILS: BOTH MONOMERS HAVE TWO SMALL BREAKS AT KNOWN          
COMPND   7 OR LIKELY TRYPSIN CLEAVAGE SITES. ALTHOUGH ENZYME IS ACTIVE          
COMPND   8 AS A MONOMER, DIMERIZATION OCCURS AT HIGH PROTEIN                    
COMPND   9 CONCENTRATION, PARTICULARLY IN THE PRESENCE OF THE                   
COMPND  10 INHIBITOR G6P                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 ORGAN: BRAIN;                                                        
SOURCE   6 TISSUE: BRAIN                                                        
KEYWDS    HEXOKINASE, PHOSPHOTRANSFERASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.MULICHAK,R.M.GARAVITO                                             
REVDAT   3   04-AUG-09 1BG3    1       ATOM   COMPND CONECT HET                 
REVDAT   3 2                   1       HETATM HETNAM LINK   SITE                
REVDAT   2   24-FEB-09 1BG3    1       VERSN                                    
REVDAT   1   08-JUN-99 1BG3    0                                                
JRNL        AUTH   A.M.MULICHAK,J.E.WILSON,K.PADMANABHAN,R.M.GARAVITO           
JRNL        TITL   THE STRUCTURE OF MAMMALIAN HEXOKINASE-1.                     
JRNL        REF    NAT.STRUCT.BIOL.              V.   5   555 1998              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   9665168                                                      
JRNL        DOI    10.1038/811                                                  
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 71.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 46567                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2404                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.90                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 37.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1227                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 180                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3352                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 104                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.77                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.32                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
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  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH3.CHO                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BG3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : AUG-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 153                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MSC FOCUSSING MIRRORS              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS II                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : R-AXIS                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54454                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 79.0                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 59.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: HEXOKINASE FROM SCHISTOSOMA MANSONI                  
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       38.55000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: ALTHOUGH ENZYME IS ACTIVE AS A MONOMER, DIMERIZATION         
REMARK 300 OCCURS AT HIGH PROTEIN CONCENTRATION, PARTICULARLY IN THE            
REMARK 300 PRESENCE OF THE INHIBITOR G6P                                        
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 BOTH MONOMERS HAVE TWO SMALL BREAKS AT KNOWN OR LIKELY               
REMARK 400 TRYPSIN CLEAVAGE SITES.                                              
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    98                                                      
REMARK 465     HIS A    99                                                      
REMARK 465     GLU A   100                                                      
REMARK 465     LYS A   101                                                      
REMARK 465     ASN A   102                                                      
REMARK 465     GLN A   103                                                      
REMARK 465     GLY A   548                                                      
REMARK 465     LYS A   549                                                      
REMARK 465     LYS A   550                                                      
REMARK 465     ARG A   912                                                      
REMARK 465     GLY A   913                                                      
REMARK 465     ASP A   914                                                      
REMARK 465     PRO A   915                                                      
REMARK 465     SER A   916                                                      
REMARK 465     ILE A   917                                                      
REMARK 465     ALA A   918                                                      
REMARK 465     ASN B    98                                                      
REMARK 465     HIS B    99                                                      
REMARK 465     GLU B   100                                                      
REMARK 465     LYS B   101                                                      
REMARK 465     ASN B   102                                                      
REMARK 465     GLN B   103                                                      
REMARK 465     LYS B   141                                                      
REMARK 465     LYS B   142                                                      
REMARK 465     ILE B   143                                                      
REMARK 465     ARG B   912                                                      
REMARK 465     GLY B   913                                                      
REMARK 465     ASP B   914                                                      
REMARK 465     PRO B   915                                                      
REMARK 465     SER B   916                                                      
REMARK 465     ILE B   917                                                      
REMARK 465     ALA B   918                                                      
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     MET A   1    CG   SD   CE                                        
REMARK 470     ILE A   2    CG1  CG2  CD1                                       
REMARK 470     GLN A   5    CG   CD   OE1  NE2                                  
REMARK 470     TYR A   9    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A  17    CG   OD1  OD2                                       
REMARK 470     LYS A  20    CG   CD   CE   NZ                                   
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     LYS A  24    CG   CD   CE   NZ                                   
REMARK 470     LYS A  48    CG   CD   CE   NZ                                   
REMARK 470     ARG A  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  77    CG   CD   CE   NZ                                   
REMARK 470     GLN A  96    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 104    CG   OD1  ND2                                       
REMARK 470     SER A 106    OG                                                  
REMARK 470     GLU A 108    CG   CD   OE1  OE2                                  
REMARK 470     SER A 109    OG                                                  
REMARK 470     ASP A 132    CG   OD1  OD2                                       
REMARK 470     GLU A 139    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 142    CG   CD   CE   NZ                                   
REMARK 470     ASP A 145    CG   OD1  OD2                                       
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     LYS A 147    CG   CD   CE   NZ                                   
REMARK 470     LYS A 194    CG   CD   CE   NZ                                   
REMARK 470     GLU A 321    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 346    CG   CD   CE   NZ                                   
REMARK 470     LYS A 429    CG   CD   CE   NZ                                   
REMARK 470     GLU A 446    CG   CD   OE1  OE2                                  
REMARK 470     SER A 480    OG                                                  
REMARK 470     GLN A 482    CD   OE1  NE2                                       
REMARK 470     LYS A 489    CG   CD   CE   NZ                                   
REMARK 470     ARG A 500    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 501    CG   CD   CE   NZ                                   
REMARK 470     SER A 505    OG                                                  
REMARK 470     LYS A 506    CG   CD   CE   NZ                                   
REMARK 470     SER A 547    OG                                                  
REMARK 470     GLU A 565    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 595    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 642    CG   CD   CE   NZ                                   
REMARK 470     GLU A 645    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 646    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 691    CG   CD   CE   NZ                                   
REMARK 470     GLU A 697    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 727    CG   CD   CE   NZ                                   
REMARK 470     GLU A 731    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 769    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 771    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 777    CG   CD   CE   NZ                                   
REMARK 470     ARG A 794    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 798    CG   CD1  CD2                                       
REMARK 470     GLN A 806    CD   OE1  NE2                                       
REMARK 470     ASN A 810    CG   OD1  ND2                                       
REMARK 470     ASP A 852    CG   OD1  OD2                                       
REMARK 470     GLN A 877    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 885    CG   CD   CE   NZ                                   
REMARK 470     VAL A 907    CG1  CG2                                            
REMARK 470     LEU A 911    CG   CD1  CD2                                       
REMARK 470     MET B   1    CG   SD   CE                                        
REMARK 470     ILE B   2    CG1  CG2  CD1                                       
REMARK 470     GLN B   5    CG   CD   OE1  NE2                                  
REMARK 470     TYR B   9    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP B  17    CG   OD1  OD2                                       
REMARK 470     LYS B  20    CG   CD   CE   NZ                                   
REMARK 470     LYS B  21    CG   CD   CE   NZ                                   
REMARK 470     LYS B  24    CG   CD   CE   NZ                                   
REMARK 470     TYR B  27    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B  30    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  48    CD   CE   NZ                                        
REMARK 470     ARG B  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  77    CG   CD   CE   NZ                                   
REMARK 470     ASN B 104    CG   OD1  ND2                                       
REMARK 470     SER B 106    OG                                                  
REMARK 470     GLU B 108    CG   CD   OE1  OE2                                  
REMARK 470     SER B 109    OG                                                  
REMARK 470     GLU B 116    CG   CD   OE1  OE2                                  
REMARK 470     SER B 122    OG                                                  
REMARK 470     GLU B 139    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 144    CG   CD   CE   NZ                                   
REMARK 470     LYS B 146    CG   CD   CE   NZ                                   
REMARK 470     LYS B 147    CG   CD   CE   NZ                                   
REMARK 470     ARG B 159    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 161    OG                                                  
REMARK 470     LYS B 162    CG   CD   CE   NZ                                   
REMARK 470     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     LYS B 194    CG   CD   CE   NZ                                   
REMARK 470     ARG B 196    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 222    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 243    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 252    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 290    CG   CD   CE   NZ                                   
REMARK 470     GLU B 321    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 347    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 353    CG   CD   CE   NZ                                   
REMARK 470     SER B 447    OG                                                  
REMARK 470     ARG B 462    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 489    CG   CD   CE   NZ                                   
REMARK 470     ARG B 490    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 502    CD   OE1  OE2                                       
REMARK 470     LYS B 506    CG   CD   CE   NZ                                   
REMARK 470     LYS B 549    CG   CD   CE   NZ                                   
REMARK 470     LYS B 550    CG   CD   CE   NZ                                   
REMARK 470     ARG B 551    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 565    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 645    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 648    CG   OD1  OD2                                       
REMARK 470     ASP B 650    CG   OD1  OD2                                       
REMARK 470     LYS B 691    CG   CD   CE   NZ                                   
REMARK 470     GLU B 697    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 700    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 738    CG   CD   CE   NZ                                   
REMARK 470     LYS B 763    CG   CD   CE   NZ                                   
REMARK 470     ARG B 769    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 771    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 785    CG   CD   CE   NZ                                   
REMARK 470     ARG B 794    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 806    CG   CD   OE1  NE2                                  
REMARK 470     SER B 811    OG                                                  
REMARK 470     GLN B 877    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 885    CD   CE   NZ                                        
REMARK 470     ARG B 910    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 254   CD  -  NE  -  CZ  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ARG A 254   NE  -  CZ  -  NH1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG A 254   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG A 279   CD  -  NE  -  CZ  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG A 279   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG A 279   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ARG A 381   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG A 381   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG A 381   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ARG A 425   CD  -  NE  -  CZ  ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG A 425   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 425   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ARG A 490   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    SER A 514   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    ARG B 254   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B 254   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG B 279   CD  -  NE  -  CZ  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG B 279   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG B 279   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ARG B 381   NE  -  CZ  -  NH1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG B 381   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ARG B 425   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG B 425   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    SER B 514   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A   2       -9.89    -55.18                                   
REMARK 500    ALA A   3      -71.90    -76.55                                   
REMARK 500    LEU A  26       42.87   -104.08                                   
REMARK 500    PRO A 115      162.87    -48.90                                   
REMARK 500    GLU A 116       46.08    -73.17                                   
REMARK 500    ASN A 117      -31.57   -143.91                                   
REMARK 500    SER A 155       46.66    -71.33                                   
REMARK 500    ALA A 166       74.83   -161.60                                   
REMARK 500    LYS A 173     -111.28     63.70                                   
REMARK 500    LYS A 176       74.67   -168.43                                   
REMARK 500    GLN A 222        5.19    -68.90                                   
REMARK 500    GLN A 291       38.48     39.69                                   
REMARK 500    SER A 298      150.47    -48.07                                   
REMARK 500    ASP A 345      -78.16    -46.29                                   
REMARK 500    ASP A 439       66.80   -106.19                                   
REMARK 500    LYS A 501      -72.54    -34.68                                   
REMARK 500    PHE A 515       40.69    -77.10                                   
REMARK 500    PRO A 520      123.79    -35.36                                   
REMARK 500    THR A 552      138.18   -173.88                                   
REMARK 500    ASP A 612        0.42    -68.45                                   
REMARK 500    SER A 618      140.77   -175.19                                   
REMARK 500    LYS A 621     -142.16     61.57                                   
REMARK 500    LYS A 624       42.21   -152.27                                   
REMARK 500    LYS A 642      -70.15    -61.56                                   
REMARK 500    ASP A 719        1.20    -67.78                                   
REMARK 500    ILE A 745      -41.94   -138.33                                   
REMARK 500    PHE A 871      -70.64    -21.68                                   
REMARK 500    LEU B  26       42.64   -104.46                                   
REMARK 500    PHE B  67       40.77   -109.15                                   
REMARK 500    SER B 155       48.31    -74.38                                   
REMARK 500    ASP B 164       31.80    -97.95                                   
REMARK 500    ALA B 166       75.80   -165.17                                   
REMARK 500    LYS B 173     -112.63     61.64                                   
REMARK 500    LYS B 176       71.96   -167.28                                   
REMARK 500    GLN B 222       -6.86    -59.77                                   
REMARK 500    ASP B 251      -87.33   -136.82                                   
REMARK 500    SER B 298      150.37    -47.44                                   
REMARK 500    ASP B 345      -84.96    -43.19                                   
REMARK 500    ASP B 439       64.27   -105.40                                   
REMARK 500    SER B 447        5.00    -67.30                                   
REMARK 500    PHE B 515       40.83    -80.08                                   
REMARK 500    PRO B 520      126.13    -33.95                                   
REMARK 500    LYS B 550     -131.42   -108.38                                   
REMARK 500    ARG B 551      149.66    174.62                                   
REMARK 500    LYS B 621     -141.60     61.30                                   
REMARK 500    LYS B 624       43.36   -154.77                                   
REMARK 500    VAL B 651       83.23    -65.25                                   
REMARK 500    ASP B 719        0.23    -68.09                                   
REMARK 500    ILE B 745      -40.84   -138.81                                   
REMARK 500    PHE B 782       76.74   -101.71                                   
REMARK 500    PHE B 871      -70.59    -20.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 490         0.14    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     ASP B 145        23.0      L          L   OUTSIDE RANGE          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1001                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P A 1002                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1003                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P A 1004                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC B 1001                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P B 1002                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC B 1003                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P B 1004                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1005                 
DBREF  1BG3 A    1   918  UNP    P05708   HXK1_RAT         1    918             
DBREF  1BG3 B    1   918  UNP    P05708   HXK1_RAT         1    918             
SEQRES   1 A  918  MET ILE ALA ALA GLN LEU LEU ALA TYR TYR PHE THR GLU          
SEQRES   2 A  918  LEU LYS ASP ASP GLN VAL LYS LYS ILE ASP LYS TYR LEU          
SEQRES   3 A  918  TYR ALA MET ARG LEU SER ASP GLU ILE LEU ILE ASP ILE          
SEQRES   4 A  918  LEU THR ARG PHE LYS LYS GLU MET LYS ASN GLY LEU SER          
SEQRES   5 A  918  ARG ASP TYR ASN PRO THR ALA SER VAL LYS MET LEU PRO          
SEQRES   6 A  918  THR PHE VAL ARG SER ILE PRO ASP GLY SER GLU LYS GLY          
SEQRES   7 A  918  ASP PHE ILE ALA LEU ASP LEU GLY GLY SER SER PHE ARG          
SEQRES   8 A  918  ILE LEU ARG VAL GLN VAL ASN HIS GLU LYS ASN GLN ASN          
SEQRES   9 A  918  VAL SER MET GLU SER GLU ILE TYR ASP THR PRO GLU ASN          
SEQRES  10 A  918  ILE VAL HIS GLY SER GLY THR GLN LEU PHE ASP HIS VAL          
SEQRES  11 A  918  ALA ASP CYS LEU GLY ASP PHE MET GLU LYS LYS LYS ILE          
SEQRES  12 A  918  LYS ASP LYS LYS LEU PRO VAL GLY PHE THR PHE SER PHE          
SEQRES  13 A  918  PRO CYS ARG GLN SER LYS ILE ASP GLU ALA VAL LEU ILE          
SEQRES  14 A  918  THR TRP THR LYS ARG PHE LYS ALA SER GLY VAL GLU GLY          
SEQRES  15 A  918  ALA ASP VAL VAL LYS LEU LEU ASN LYS ALA ILE LYS LYS          
SEQRES  16 A  918  ARG GLY ASP TYR ASP ALA ASN ILE VAL ALA VAL VAL ASN          
SEQRES  17 A  918  ASP THR VAL GLY THR MET MET THR CYS GLY TYR ASP ASP          
SEQRES  18 A  918  GLN GLN CYS GLU VAL GLY LEU ILE ILE GLY THR GLY THR          
SEQRES  19 A  918  ASN ALA CYS TYR MET GLU GLU LEU ARG HIS ILE ASP LEU          
SEQRES  20 A  918  VAL GLU GLY ASP GLU GLY ARG MET CYS ILE ASN THR GLU          
SEQRES  21 A  918  TRP GLY ALA PHE GLY ASP ASP GLY SER LEU GLU ASP ILE          
SEQRES  22 A  918  ARG THR GLU PHE ASP ARG GLU LEU ASP ARG GLY SER LEU          
SEQRES  23 A  918  ASN PRO GLY LYS GLN LEU PHE GLU LYS MET VAL SER GLY          
SEQRES  24 A  918  MET TYR MET GLY GLU LEU VAL ARG LEU ILE LEU VAL LYS          
SEQRES  25 A  918  MET ALA LYS GLU GLY LEU LEU PHE GLU GLY ARG ILE THR          
SEQRES  26 A  918  PRO GLU LEU LEU THR ARG GLY LYS PHE ASN THR SER ASP          
SEQRES  27 A  918  VAL SER ALA ILE GLU LYS ASP LYS GLU GLY ILE GLN ASN          
SEQRES  28 A  918  ALA LYS GLU ILE LEU THR ARG LEU GLY VAL GLU PRO SER          
SEQRES  29 A  918  ASP VAL ASP CYS VAL SER VAL GLN HIS ILE CYS THR ILE          
SEQRES  30 A  918  VAL SER PHE ARG SER ALA ASN LEU VAL ALA ALA THR LEU          
SEQRES  31 A  918  GLY ALA ILE LEU ASN ARG LEU ARG ASP ASN LYS GLY THR          
SEQRES  32 A  918  PRO ARG LEU ARG THR THR VAL GLY VAL ASP GLY SER LEU          
SEQRES  33 A  918  TYR LYS MET HIS PRO GLN TYR SER ARG ARG PHE HIS LYS          
SEQRES  34 A  918  THR LEU ARG ARG LEU VAL PRO ASP SER ASP VAL ARG PHE          
SEQRES  35 A  918  LEU LEU SER GLU SER GLY THR GLY LYS GLY ALA ALA MET          
SEQRES  36 A  918  VAL THR ALA VAL ALA TYR ARG LEU ALA GLU GLN HIS ARG          
SEQRES  37 A  918  GLN ILE GLU GLU THR LEU ALA HIS PHE ARG LEU SER LYS          
SEQRES  38 A  918  GLN THR LEU MET GLU VAL LYS LYS ARG LEU ARG THR GLU          
SEQRES  39 A  918  MET GLU MET GLY LEU ARG LYS GLU THR ASN SER LYS ALA          
SEQRES  40 A  918  THR VAL LYS MET LEU PRO SER PHE VAL ARG SER ILE PRO          
SEQRES  41 A  918  ASP GLY THR GLU HIS GLY ASP PHE LEU ALA LEU ASP LEU          
SEQRES  42 A  918  GLY GLY THR ASN PHE ARG VAL LEU LEU VAL LYS ILE ARG          
SEQRES  43 A  918  SER GLY LYS LYS ARG THR VAL GLU MET HIS ASN LYS ILE          
SEQRES  44 A  918  TYR SER ILE PRO LEU GLU ILE MET GLN GLY THR GLY ASP          
SEQRES  45 A  918  GLU LEU PHE ASP HIS ILE VAL SER CYS ILE SER ASP PHE          
SEQRES  46 A  918  LEU ASP TYR MET GLY ILE LYS GLY PRO ARG MET PRO LEU          
SEQRES  47 A  918  GLY PHE THR PHE SER PHE PRO CYS HIS GLN THR ASN LEU          
SEQRES  48 A  918  ASP CYS GLY ILE LEU ILE SER TRP THR LYS GLY PHE LYS          
SEQRES  49 A  918  ALA THR ASP CYS GLU GLY HIS ASP VAL ALA SER LEU LEU          
SEQRES  50 A  918  ARG ASP ALA VAL LYS ARG ARG GLU GLU PHE ASP LEU ASP          
SEQRES  51 A  918  VAL VAL ALA VAL VAL ASN ASP THR VAL GLY THR MET MET          
SEQRES  52 A  918  THR CYS ALA TYR GLU GLU PRO THR CYS GLU ILE GLY LEU          
SEQRES  53 A  918  ILE VAL GLY THR GLY THR ASN ALA CYS TYR MET GLU GLU          
SEQRES  54 A  918  MET LYS ASN VAL GLU MET VAL GLU GLY ASN GLN GLY GLN          
SEQRES  55 A  918  MET CYS ILE ASN MET GLU TRP GLY ALA PHE GLY ASP ASN          
SEQRES  56 A  918  GLY CYS LEU ASP ASP ILE ARG THR ASP PHE ASP LYS VAL          
SEQRES  57 A  918  VAL ASP GLU TYR SER LEU ASN SER GLY LYS GLN ARG PHE          
SEQRES  58 A  918  GLU LYS MET ILE SER GLY MET TYR LEU GLY GLU ILE VAL          
SEQRES  59 A  918  ARG ASN ILE LEU ILE ASP PHE THR LYS LYS GLY PHE LEU          
SEQRES  60 A  918  PHE ARG GLY GLN ILE SER GLU PRO LEU LYS THR ARG GLY          
SEQRES  61 A  918  ILE PHE GLU THR LYS PHE LEU SER GLN ILE GLU SER ASP          
SEQRES  62 A  918  ARG LEU ALA LEU LEU GLN VAL ARG ALA ILE LEU GLN GLN          
SEQRES  63 A  918  LEU GLY LEU ASN SER THR CYS ASP ASP SER ILE LEU VAL          
SEQRES  64 A  918  LYS THR VAL CYS GLY VAL VAL SER LYS ARG ALA ALA GLN          
SEQRES  65 A  918  LEU CYS GLY ALA GLY MET ALA ALA VAL VAL GLU LYS ILE          
SEQRES  66 A  918  ARG GLU ASN ARG GLY LEU ASP HIS LEU ASN VAL THR VAL          
SEQRES  67 A  918  GLY VAL ASP GLY THR LEU TYR LYS LEU HIS PRO HIS PHE          
SEQRES  68 A  918  SER ARG ILE MET HIS GLN THR VAL LYS GLU LEU SER PRO          
SEQRES  69 A  918  LYS CYS THR VAL SER PHE LEU LEU SER GLU ASP GLY SER          
SEQRES  70 A  918  GLY LYS GLY ALA ALA LEU ILE THR ALA VAL GLY VAL ARG          
SEQRES  71 A  918  LEU ARG GLY ASP PRO SER ILE ALA                              
SEQRES   1 B  918  MET ILE ALA ALA GLN LEU LEU ALA TYR TYR PHE THR GLU          
SEQRES   2 B  918  LEU LYS ASP ASP GLN VAL LYS LYS ILE ASP LYS TYR LEU          
SEQRES   3 B  918  TYR ALA MET ARG LEU SER ASP GLU ILE LEU ILE ASP ILE          
SEQRES   4 B  918  LEU THR ARG PHE LYS LYS GLU MET LYS ASN GLY LEU SER          
SEQRES   5 B  918  ARG ASP TYR ASN PRO THR ALA SER VAL LYS MET LEU PRO          
SEQRES   6 B  918  THR PHE VAL ARG SER ILE PRO ASP GLY SER GLU LYS GLY          
SEQRES   7 B  918  ASP PHE ILE ALA LEU ASP LEU GLY GLY SER SER PHE ARG          
SEQRES   8 B  918  ILE LEU ARG VAL GLN VAL ASN HIS GLU LYS ASN GLN ASN          
SEQRES   9 B  918  VAL SER MET GLU SER GLU ILE TYR ASP THR PRO GLU ASN          
SEQRES  10 B  918  ILE VAL HIS GLY SER GLY THR GLN LEU PHE ASP HIS VAL          
SEQRES  11 B  918  ALA ASP CYS LEU GLY ASP PHE MET GLU LYS LYS LYS ILE          
SEQRES  12 B  918  LYS ASP LYS LYS LEU PRO VAL GLY PHE THR PHE SER PHE          
SEQRES  13 B  918  PRO CYS ARG GLN SER LYS ILE ASP GLU ALA VAL LEU ILE          
SEQRES  14 B  918  THR TRP THR LYS ARG PHE LYS ALA SER GLY VAL GLU GLY          
SEQRES  15 B  918  ALA ASP VAL VAL LYS LEU LEU ASN LYS ALA ILE LYS LYS          
SEQRES  16 B  918  ARG GLY ASP TYR ASP ALA ASN ILE VAL ALA VAL VAL ASN          
SEQRES  17 B  918  ASP THR VAL GLY THR MET MET THR CYS GLY TYR ASP ASP          
SEQRES  18 B  918  GLN GLN CYS GLU VAL GLY LEU ILE ILE GLY THR GLY THR          
SEQRES  19 B  918  ASN ALA CYS TYR MET GLU GLU LEU ARG HIS ILE ASP LEU          
SEQRES  20 B  918  VAL GLU GLY ASP GLU GLY ARG MET CYS ILE ASN THR GLU          
SEQRES  21 B  918  TRP GLY ALA PHE GLY ASP ASP GLY SER LEU GLU ASP ILE          
SEQRES  22 B  918  ARG THR GLU PHE ASP ARG GLU LEU ASP ARG GLY SER LEU          
SEQRES  23 B  918  ASN PRO GLY LYS GLN LEU PHE GLU LYS MET VAL SER GLY          
SEQRES  24 B  918  MET TYR MET GLY GLU LEU VAL ARG LEU ILE LEU VAL LYS          
SEQRES  25 B  918  MET ALA LYS GLU GLY LEU LEU PHE GLU GLY ARG ILE THR          
SEQRES  26 B  918  PRO GLU LEU LEU THR ARG GLY LYS PHE ASN THR SER ASP          
SEQRES  27 B  918  VAL SER ALA ILE GLU LYS ASP LYS GLU GLY ILE GLN ASN          
SEQRES  28 B  918  ALA LYS GLU ILE LEU THR ARG LEU GLY VAL GLU PRO SER          
SEQRES  29 B  918  ASP VAL ASP CYS VAL SER VAL GLN HIS ILE CYS THR ILE          
SEQRES  30 B  918  VAL SER PHE ARG SER ALA ASN LEU VAL ALA ALA THR LEU          
SEQRES  31 B  918  GLY ALA ILE LEU ASN ARG LEU ARG ASP ASN LYS GLY THR          
SEQRES  32 B  918  PRO ARG LEU ARG THR THR VAL GLY VAL ASP GLY SER LEU          
SEQRES  33 B  918  TYR LYS MET HIS PRO GLN TYR SER ARG ARG PHE HIS LYS          
SEQRES  34 B  918  THR LEU ARG ARG LEU VAL PRO ASP SER ASP VAL ARG PHE          
SEQRES  35 B  918  LEU LEU SER GLU SER GLY THR GLY LYS GLY ALA ALA MET          
SEQRES  36 B  918  VAL THR ALA VAL ALA TYR ARG LEU ALA GLU GLN HIS ARG          
SEQRES  37 B  918  GLN ILE GLU GLU THR LEU ALA HIS PHE ARG LEU SER LYS          
SEQRES  38 B  918  GLN THR LEU MET GLU VAL LYS LYS ARG LEU ARG THR GLU          
SEQRES  39 B  918  MET GLU MET GLY LEU ARG LYS GLU THR ASN SER LYS ALA          
SEQRES  40 B  918  THR VAL LYS MET LEU PRO SER PHE VAL ARG SER ILE PRO          
SEQRES  41 B  918  ASP GLY THR GLU HIS GLY ASP PHE LEU ALA LEU ASP LEU          
SEQRES  42 B  918  GLY GLY THR ASN PHE ARG VAL LEU LEU VAL LYS ILE ARG          
SEQRES  43 B  918  SER GLY LYS LYS ARG THR VAL GLU MET HIS ASN LYS ILE          
SEQRES  44 B  918  TYR SER ILE PRO LEU GLU ILE MET GLN GLY THR GLY ASP          
SEQRES  45 B  918  GLU LEU PHE ASP HIS ILE VAL SER CYS ILE SER ASP PHE          
SEQRES  46 B  918  LEU ASP TYR MET GLY ILE LYS GLY PRO ARG MET PRO LEU          
SEQRES  47 B  918  GLY PHE THR PHE SER PHE PRO CYS HIS GLN THR ASN LEU          
SEQRES  48 B  918  ASP CYS GLY ILE LEU ILE SER TRP THR LYS GLY PHE LYS          
SEQRES  49 B  918  ALA THR ASP CYS GLU GLY HIS ASP VAL ALA SER LEU LEU          
SEQRES  50 B  918  ARG ASP ALA VAL LYS ARG ARG GLU GLU PHE ASP LEU ASP          
SEQRES  51 B  918  VAL VAL ALA VAL VAL ASN ASP THR VAL GLY THR MET MET          
SEQRES  52 B  918  THR CYS ALA TYR GLU GLU PRO THR CYS GLU ILE GLY LEU          
SEQRES  53 B  918  ILE VAL GLY THR GLY THR ASN ALA CYS TYR MET GLU GLU          
SEQRES  54 B  918  MET LYS ASN VAL GLU MET VAL GLU GLY ASN GLN GLY GLN          
SEQRES  55 B  918  MET CYS ILE ASN MET GLU TRP GLY ALA PHE GLY ASP ASN          
SEQRES  56 B  918  GLY CYS LEU ASP ASP ILE ARG THR ASP PHE ASP LYS VAL          
SEQRES  57 B  918  VAL ASP GLU TYR SER LEU ASN SER GLY LYS GLN ARG PHE          
SEQRES  58 B  918  GLU LYS MET ILE SER GLY MET TYR LEU GLY GLU ILE VAL          
SEQRES  59 B  918  ARG ASN ILE LEU ILE ASP PHE THR LYS LYS GLY PHE LEU          
SEQRES  60 B  918  PHE ARG GLY GLN ILE SER GLU PRO LEU LYS THR ARG GLY          
SEQRES  61 B  918  ILE PHE GLU THR LYS PHE LEU SER GLN ILE GLU SER ASP          
SEQRES  62 B  918  ARG LEU ALA LEU LEU GLN VAL ARG ALA ILE LEU GLN GLN          
SEQRES  63 B  918  LEU GLY LEU ASN SER THR CYS ASP ASP SER ILE LEU VAL          
SEQRES  64 B  918  LYS THR VAL CYS GLY VAL VAL SER LYS ARG ALA ALA GLN          
SEQRES  65 B  918  LEU CYS GLY ALA GLY MET ALA ALA VAL VAL GLU LYS ILE          
SEQRES  66 B  918  ARG GLU ASN ARG GLY LEU ASP HIS LEU ASN VAL THR VAL          
SEQRES  67 B  918  GLY VAL ASP GLY THR LEU TYR LYS LEU HIS PRO HIS PHE          
SEQRES  68 B  918  SER ARG ILE MET HIS GLN THR VAL LYS GLU LEU SER PRO          
SEQRES  69 B  918  LYS CYS THR VAL SER PHE LEU LEU SER GLU ASP GLY SER          
SEQRES  70 B  918  GLY LYS GLY ALA ALA LEU ILE THR ALA VAL GLY VAL ARG          
SEQRES  71 B  918  LEU ARG GLY ASP PRO SER ILE ALA                              
HET    BGC  A1001      12                                                       
HET    G6P  A1002      16                                                       
HET    BGC  A1003      12                                                       
HET    G6P  A1004      16                                                       
HET     CA  A1005       1                                                       
HET    BGC  B1001      12                                                       
HET    G6P  B1002      16                                                       
HET    BGC  B1003      12                                                       
HET    G6P  B1004      16                                                       
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     G6P ALPHA-D-GLUCOSE-6-PHOSPHATE                                      
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  BGC    4(C6 H12 O6)                                                 
FORMUL   4  G6P    4(C6 H13 O9 P)                                               
FORMUL   7   CA    CA 2+                                                        
FORMUL  12  HOH   *234(H2 O)                                                    
HELIX    1   1 ILE A    2  TYR A   25  1                                  24    
HELIX    2   2 TYR A   27  MET A   29  5                                   3    
HELIX    3   3 ASP A   33  LEU A   51  1                                  19    
HELIX    4   4 ARG A   53  THR A   58  1                                   6    
HELIX    5   5 GLY A  123  LYS A  141  1                                  19    
HELIX    6   6 VAL A  185  ARG A  196  1                                  12    
HELIX    7   7 ASP A  209  ASP A  220  1                                  12    
HELIX    8   8 LEU A  242  HIS A  244  5                                   3    
HELIX    9   9 TRP A  261  ALA A  263  5                                   3    
HELIX   10  10 GLU A  276  ARG A  283  1                                   8    
HELIX   11  11 GLU A  294  VAL A  297  1                                   4    
HELIX   12  12 MET A  302  LYS A  315  1                                  14    
HELIX   13  13 PRO A  326  LEU A  329  1                                   4    
HELIX   14  14 THR A  336  ILE A  342  1                                   7    
HELIX   15  15 GLY A  348  ARG A  358  1                                  11    
HELIX   16  16 ASP A  365  LYS A  401  1                                  37    
HELIX   17  17 SER A  415  MET A  419  1                                   5    
HELIX   18  18 TYR A  423  LEU A  434  1                                  12    
HELIX   19  19 GLY A  450  PHE A  477  1                                  28    
HELIX   20  20 LYS A  481  LEU A  499  1                                  19    
HELIX   21  21 LYS A  501  LYS A  506  1                                   6    
HELIX   22  22 LEU A  564  MET A  567  1                                   4    
HELIX   23  23 GLY A  571  MET A  589  1                                  19    
HELIX   24  24 VAL A  633  ARG A  644  1                                  12    
HELIX   25  25 ASP A  657  ALA A  666  1                                  10    
HELIX   26  26 MET A  690  ASN A  692  5                                   3    
HELIX   27  27 TRP A  709  ALA A  711  5                                   3    
HELIX   28  28 ASP A  724  GLU A  731  1                                   8    
HELIX   29  29 ARG A  740  MET A  744  1                                   5    
HELIX   30  30 LEU A  750  LYS A  763  1                                  14    
HELIX   31  31 GLU A  774  LYS A  777  1                                   4    
HELIX   32  32 THR A  784  ILE A  790  1                                   7    
HELIX   33  33 LEU A  797  GLN A  806  1                                  10    
HELIX   34  34 CYS A  813  ASN A  848  1                                  36    
HELIX   35  35 THR A  863  LEU A  867  1                                   5    
HELIX   36  36 PHE A  871  LEU A  882  1                                  12    
HELIX   37  37 GLY A  896  VAL A  909  1                                  14    
HELIX   38  38 ILE B    2  TYR B   25  1                                  24    
HELIX   39  39 TYR B   27  MET B   29  5                                   3    
HELIX   40  40 ASP B   33  LEU B   51  1                                  19    
HELIX   41  41 ARG B   53  THR B   58  1                                   6    
HELIX   42  42 GLU B  116  VAL B  119  1                                   4    
HELIX   43  43 GLY B  123  GLU B  139  1                                  17    
HELIX   44  44 VAL B  185  ARG B  196  1                                  12    
HELIX   45  45 ASP B  209  ASP B  220  1                                  12    
HELIX   46  46 LEU B  242  HIS B  244  5                                   3    
HELIX   47  47 TRP B  261  ALA B  263  5                                   3    
HELIX   48  48 GLU B  276  GLY B  284  1                                   9    
HELIX   49  49 GLU B  294  VAL B  297  1                                   4    
HELIX   50  50 MET B  302  GLU B  316  1                                  15    
HELIX   51  51 PRO B  326  LEU B  329  1                                   4    
HELIX   52  52 THR B  336  ILE B  342  1                                   7    
HELIX   53  53 GLU B  347  ARG B  358  5                                  12    
HELIX   54  54 ASP B  365  LYS B  401  1                                  37    
HELIX   55  55 SER B  415  MET B  419  1                                   5    
HELIX   56  56 TYR B  423  LEU B  434  1                                  12    
HELIX   57  57 GLY B  450  PHE B  477  1                                  28    
HELIX   58  58 LYS B  481  LEU B  499  1                                  19    
HELIX   59  59 LYS B  501  ASN B  504  1                                   4    
HELIX   60  60 LEU B  564  MET B  567  1                                   4    
HELIX   61  61 GLY B  571  MET B  589  1                                  19    
HELIX   62  62 VAL B  633  ARG B  644  1                                  12    
HELIX   63  63 ASP B  657  GLU B  668  1                                  12    
HELIX   64  64 TRP B  709  ALA B  711  5                                   3    
HELIX   65  65 ASP B  724  GLU B  731  1                                   8    
HELIX   66  66 ARG B  740  LYS B  743  1                                   4    
HELIX   67  67 LEU B  750  LYS B  763  1                                  14    
HELIX   68  68 GLU B  774  LYS B  777  1                                   4    
HELIX   69  69 THR B  784  ILE B  790  1                                   7    
HELIX   70  70 LEU B  797  GLN B  806  1                                  10    
HELIX   71  71 CYS B  813  ASN B  848  1                                  36    
HELIX   72  72 THR B  863  LEU B  867  1                                   5    
HELIX   73  73 PHE B  871  LEU B  882  1                                  12    
HELIX   74  74 GLY B  896  GLY B  908  1                                  13    
SHEET    1   A 5 ASN A 202  VAL A 207  0                                        
SHEET    2   A 5 PRO A 149  PHE A 154  1  N  VAL A 150   O  ASN A 202           
SHEET    3   A 5 GLY A  78  LEU A  85  1  N  ILE A  81   O  GLY A 151           
SHEET    4   A 5 ARG A  91  VAL A  97 -1  N  VAL A  97   O  GLY A  78           
SHEET    5   A 5 SER A 106  GLU A 108 -1  N  GLU A 108   O  ARG A  94           
SHEET    1   B 5 ARG A 254  ASN A 258  0                                        
SHEET    2   B 5 THR A 234  GLU A 241 -1  N  GLU A 240   O  MET A 255           
SHEET    3   B 5 CYS A 224  ILE A 230 -1  N  ILE A 229   O  ASN A 235           
SHEET    4   B 5 THR A 409  ASP A 413  1  N  THR A 409   O  GLU A 225           
SHEET    5   B 5 ARG A 441  LEU A 444  1  N  ARG A 441   O  VAL A 410           
SHEET    1   C 6 MET A 511  PRO A 513  0                                        
SHEET    2   C 6 GLN A 702  MET A 707 -1  N  ASN A 706   O  LEU A 512           
SHEET    3   C 6 THR A 682  GLU A 689 -1  N  GLU A 688   O  MET A 703           
SHEET    4   C 6 CYS A 672  VAL A 678 -1  N  ILE A 677   O  ASN A 683           
SHEET    5   C 6 THR A 857  ASP A 861  1  N  THR A 857   O  GLU A 673           
SHEET    6   C 6 SER A 889  LEU A 892  1  N  SER A 889   O  VAL A 858           
SHEET    1   D 5 LEU A 649  VAL A 655  0                                        
SHEET    2   D 5 MET A 596  PHE A 602  1  N  MET A 596   O  ASP A 650           
SHEET    3   D 5 GLY A 526  LEU A 533  1  N  LEU A 529   O  GLY A 599           
SHEET    4   D 5 ARG A 539  ILE A 545 -1  N  ILE A 545   O  GLY A 526           
SHEET    5   D 5 VAL A 553  ILE A 559 -1  N  LYS A 558   O  VAL A 540           
SHEET    1   E 2 PRO A 157  ARG A 159  0                                        
SHEET    2   E 2 VAL A 167  THR A 170 -1  N  THR A 170   O  PRO A 157           
SHEET    1   F 2 PRO A 605  HIS A 607  0                                        
SHEET    2   F 2 ILE A 615  SER A 618 -1  N  SER A 618   O  PRO A 605           
SHEET    1   G 5 ASN B 202  VAL B 207  0                                        
SHEET    2   G 5 PRO B 149  PHE B 154  1  N  VAL B 150   O  ASN B 202           
SHEET    3   G 5 ASP B  79  LEU B  85  1  N  ILE B  81   O  GLY B 151           
SHEET    4   G 5 ARG B  91  GLN B  96 -1  N  VAL B  95   O  PHE B  80           
SHEET    5   G 5 SER B 106  GLU B 108 -1  N  GLU B 108   O  ARG B  94           
SHEET    1   H 5 ARG B 254  ASN B 258  0                                        
SHEET    2   H 5 THR B 234  GLU B 241 -1  N  GLU B 240   O  MET B 255           
SHEET    3   H 5 CYS B 224  ILE B 230 -1  N  ILE B 229   O  ASN B 235           
SHEET    4   H 5 ARG B 407  ASP B 413  1  N  THR B 409   O  GLU B 225           
SHEET    5   H 5 ASP B 439  LEU B 444  1  N  ASP B 439   O  THR B 408           
SHEET    1   I 6 MET B 511  PRO B 513  0                                        
SHEET    2   I 6 GLN B 702  MET B 707 -1  N  ASN B 706   O  LEU B 512           
SHEET    3   I 6 THR B 682  GLU B 689 -1  N  GLU B 688   O  MET B 703           
SHEET    4   I 6 CYS B 672  VAL B 678 -1  N  ILE B 677   O  ASN B 683           
SHEET    5   I 6 LEU B 854  ASP B 861  1  N  THR B 857   O  GLU B 673           
SHEET    6   I 6 CYS B 886  LEU B 892  1  N  THR B 887   O  LEU B 854           
SHEET    1   J 5 LEU B 649  VAL B 655  0                                        
SHEET    2   J 5 MET B 596  PHE B 602  1  N  MET B 596   O  ASP B 650           
SHEET    3   J 5 GLY B 526  LEU B 533  1  N  LEU B 529   O  GLY B 599           
SHEET    4   J 5 ARG B 539  SER B 547 -1  N  ILE B 545   O  GLY B 526           
SHEET    5   J 5 ARG B 551  ILE B 559 -1  N  LYS B 558   O  VAL B 540           
SHEET    1   K 2 PRO B 157  ARG B 159  0                                        
SHEET    2   K 2 VAL B 167  THR B 170 -1  N  THR B 170   O  PRO B 157           
SHEET    1   L 2 PRO B 605  HIS B 607  0                                        
SHEET    2   L 2 ILE B 615  SER B 618 -1  N  SER B 618   O  PRO B 605           
LINK        CA    CA A1005                 OD2 ASP B 365     1555   1555  3.25  
SITE     1 AC1 12 SER A 155  PHE A 156  THR A 172  LYS A 173                    
SITE     2 AC1 12 ASN A 208  ASP A 209  ILE A 229  ASN A 235                    
SITE     3 AC1 12 GLU A 260  GLN A 291  GLU A 294  HOH A2218                    
SITE     1 AC2 12 ASP A  84  GLY A  87  SER A  88  ARG A  91                    
SITE     2 AC2 12 SER A 155  ASP A 209  GLY A 231  THR A 232                    
SITE     3 AC2 12 ASP A 413  SER A 415  THR A 449  HOH A2218                    
SITE     1 AC3 11 PHE A 604  PRO A 605  THR A 620  LYS A 621                    
SITE     2 AC3 11 ASN A 656  ASP A 657  ILE A 677  ASN A 683                    
SITE     3 AC3 11 GLU A 708  GLU A 742  HOH A2226                               
SITE     1 AC4 14 ASP A 532  GLY A 535  THR A 536  SER A 603                    
SITE     2 AC4 14 ASP A 657  GLY A 679  THR A 680  ASP A 861                    
SITE     3 AC4 14 GLY A 862  THR A 863  GLY A 896  SER A 897                    
SITE     4 AC4 14 HOH A2127  HOH A2226                                          
SITE     1 AC5 10 SER B 155  PHE B 156  THR B 172  LYS B 173                    
SITE     2 AC5 10 ASN B 208  ASP B 209  ILE B 229  ASN B 235                    
SITE     3 AC5 10 GLU B 260  GLU B 294                                          
SITE     1 AC6 13 ASP B  84  GLY B  87  SER B  88  ARG B  91                    
SITE     2 AC6 13 SER B 155  ASP B 209  GLY B 231  THR B 232                    
SITE     3 AC6 13 ASP B 413  SER B 415  GLY B 448  THR B 449                    
SITE     4 AC6 13 HOH B2142                                                     
SITE     1 AC7 12 PHE B 604  PRO B 605  THR B 620  LYS B 621                    
SITE     2 AC7 12 ASN B 656  ASP B 657  THR B 658  ILE B 677                    
SITE     3 AC7 12 ASN B 683  GLU B 708  GLU B 742  HOH B2139                    
SITE     1 AC8 13 ASP B 532  GLY B 535  THR B 536  SER B 603                    
SITE     2 AC8 13 ASP B 657  GLY B 679  THR B 680  ASP B 861                    
SITE     3 AC8 13 GLY B 862  THR B 863  GLY B 896  SER B 897                    
SITE     4 AC8 13 HOH B2139                                                     
SITE     1 AC9  2 ASP A 365  ASP B 365                                          
CRYST1  132.100   77.100  137.100  90.00  96.00  90.00 P 1 21 1      4          
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      0.007570  0.000000  0.000796        0.00000                         
SCALE2      0.000000  0.012970  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007334        0.00000                         
MTRIX1   1 -0.999992  0.001479 -0.003776        2.40960    1                    
MTRIX2   1 -0.002470 -0.960616  0.277870      -45.78030    1                    
MTRIX3   1 -0.003216  0.277877  0.960610        6.54780    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system