GenomeNet

Database: PDB
Entry: 3NB0
LinkDB: 3NB0
Original site: 3NB0 
HEADER    TRANSFERASE                             02-JUN-10   3NB0              
TITLE     GLUCOSE-6-PHOSPHATE ACTIVATED FORM OF YEAST GLYCOGEN SYNTHASE         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOGEN [STARCH] SYNTHASE ISOFORM 2;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 2.4.1.11;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;              
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: GSY2, L8479.8, YLR258W;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    GLYCOGEN SYNTHASE, GLUCOSE-6-PHOSPHATE, YEAST, ALLOSTERIC ACTIVATION, 
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BASKARAN,T.D.HURLEY                                                 
REVDAT   3   20-OCT-10 3NB0    1       JRNL                                     
REVDAT   2   13-OCT-10 3NB0    1       JRNL                                     
REVDAT   1   06-OCT-10 3NB0    0                                                
JRNL        AUTH   S.BASKARAN,P.J.ROACH,A.A.DEPAOLI-ROACH,T.D.HURLEY            
JRNL        TITL   STRUCTURAL BASIS FOR GLUCOSE-6-PHOSPHATE ACTIVATION OF       
JRNL        TITL 2 GLYCOGEN SYNTHASE.                                           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107 17563 2010              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   20876143                                                     
JRNL        DOI    10.1073/PNAS.1006340107                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.060                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 148274                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7445                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.2380 -  7.4660    0.91     4786   273  0.1740 0.1940        
REMARK   3     2  7.4660 -  5.9300    0.99     5080   260  0.1910 0.2090        
REMARK   3     3  5.9300 -  5.1810    0.99     5040   272  0.1930 0.2200        
REMARK   3     4  5.1810 -  4.7080    0.99     5057   217  0.1720 0.2070        
REMARK   3     5  4.7080 -  4.3710    0.99     5003   278  0.1730 0.1990        
REMARK   3     6  4.3710 -  4.1130    0.99     5066   248  0.1810 0.2170        
REMARK   3     7  4.1130 -  3.9080    0.99     4983   257  0.1840 0.2100        
REMARK   3     8  3.9080 -  3.7370    0.99     4959   274  0.1940 0.2200        
REMARK   3     9  3.7370 -  3.5940    0.99     4997   270  0.1920 0.2210        
REMARK   3    10  3.5940 -  3.4700    0.99     4944   275  0.2100 0.2330        
REMARK   3    11  3.4700 -  3.3610    0.99     4920   248  0.2170 0.2440        
REMARK   3    12  3.3610 -  3.2650    0.98     4965   258  0.2370 0.2760        
REMARK   3    13  3.2650 -  3.1790    0.98     4843   246  0.2330 0.2730        
REMARK   3    14  3.1790 -  3.1020    0.97     4915   250  0.2490 0.2900        
REMARK   3    15  3.1020 -  3.0310    0.97     4826   241  0.2440 0.2590        
REMARK   3    16  3.0310 -  2.9670    0.96     4755   252  0.2390 0.2880        
REMARK   3    17  2.9670 -  2.9070    0.94     4710   263  0.2420 0.2610        
REMARK   3    18  2.9070 -  2.8520    0.94     4685   246  0.2400 0.2850        
REMARK   3    19  2.8520 -  2.8020    0.94     4658   267  0.2410 0.2710        
REMARK   3    20  2.8020 -  2.7540    0.92     4616   214  0.2390 0.3000        
REMARK   3    21  2.7540 -  2.7100    0.92     4570   252  0.2450 0.2870        
REMARK   3    22  2.7100 -  2.6680    0.91     4499   236  0.2400 0.3240        
REMARK   3    23  2.6680 -  2.6290    0.90     4487   239  0.2470 0.2750        
REMARK   3    24  2.6290 -  2.5920    0.89     4400   255  0.2510 0.2900        
REMARK   3    25  2.5920 -  2.5570    0.89     4419   247  0.2600 0.3080        
REMARK   3    26  2.5570 -  2.5230    0.87     4290   244  0.2630 0.2960        
REMARK   3    27  2.5230 -  2.4920    0.86     4252   237  0.2580 0.3010        
REMARK   3    28  2.4920 -  2.4620    0.85     4249   220  0.2550 0.3110        
REMARK   3    29  2.4620 -  2.4330    0.84     4166   206  0.2640 0.2860        
REMARK   3    30  2.4330 -  2.4060    0.74     3689   200  0.2800 0.3330        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.36                                          
REMARK   3   B_SOL              : 58.36                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 2.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.550           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.44                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.83400                                             
REMARK   3    B22 (A**2) : -9.85500                                             
REMARK   3    B33 (A**2) : 14.68900                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004          21375                                  
REMARK   3   ANGLE     :  0.737          28968                                  
REMARK   3   CHIRALITY :  0.054           3123                                  
REMARK   3   PLANARITY :  0.003           3747                                  
REMARK   3   DIHEDRAL  : 17.749           7893                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3NB0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059603.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 157186                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.200                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 3NAZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.2, 25% PEG 300,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       96.36950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      103.49100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      102.89950            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       96.36950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      103.49100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      102.89950            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       96.36950            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      103.49100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      102.89950            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       96.36950            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      103.49100            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      102.89950            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16430 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 99550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D                            
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     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A   640                                                      
REMARK 465     GLY A   641                                                      
REMARK 465     LYS A   642                                                      
REMARK 465     LYS A   643                                                      
REMARK 465     LEU A   644                                                      
REMARK 465     LYS A   645                                                      
REMARK 465     VAL A   646                                                      
REMARK 465     ALA A   647                                                      
REMARK 465     ARG A   648                                                      
REMARK 465     PRO A   649                                                      
REMARK 465     LEU A   650                                                      
REMARK 465     SER A   651                                                      
REMARK 465     VAL A   652                                                      
REMARK 465     PRO A   653                                                      
REMARK 465     GLY A   654                                                      
REMARK 465     SER A   655                                                      
REMARK 465     PRO A   656                                                      
REMARK 465     ARG A   657                                                      
REMARK 465     ASP A   658                                                      
REMARK 465     LEU A   659                                                      
REMARK 465     ARG A   660                                                      
REMARK 465     SER A   661                                                      
REMARK 465     ASN A   662                                                      
REMARK 465     SER A   663                                                      
REMARK 465     THR A   664                                                      
REMARK 465     VAL A   665                                                      
REMARK 465     TYR A   666                                                      
REMARK 465     MET A   667                                                      
REMARK 465     THR A   668                                                      
REMARK 465     PRO A   669                                                      
REMARK 465     GLY A   670                                                      
REMARK 465     ASP A   671                                                      
REMARK 465     LEU A   672                                                      
REMARK 465     GLY A   673                                                      
REMARK 465     THR A   674                                                      
REMARK 465     LEU A   675                                                      
REMARK 465     GLN A   676                                                      
REMARK 465     GLU A   677                                                      
REMARK 465     VAL A   678                                                      
REMARK 465     ASN A   679                                                      
REMARK 465     ASN A   680                                                      
REMARK 465     ALA A   681                                                      
REMARK 465     ASP A   682                                                      
REMARK 465     ASP A   683                                                      
REMARK 465     TYR A   684                                                      
REMARK 465     PHE A   685                                                      
REMARK 465     SER A   686                                                      
REMARK 465     LEU A   687                                                      
REMARK 465     GLY A   688                                                      
REMARK 465     VAL A   689                                                      
REMARK 465     ASN A   690                                                      
REMARK 465     PRO A   691                                                      
REMARK 465     ALA A   692                                                      
REMARK 465     ALA A   693                                                      
REMARK 465     ASP A   694                                                      
REMARK 465     ASP A   695                                                      
REMARK 465     ASP A   696                                                      
REMARK 465     ASP A   697                                                      
REMARK 465     ASP A   698                                                      
REMARK 465     GLY A   699                                                      
REMARK 465     PRO A   700                                                      
REMARK 465     TYR A   701                                                      
REMARK 465     ALA A   702                                                      
REMARK 465     ASP A   703                                                      
REMARK 465     ASP A   704                                                      
REMARK 465     SER A   705                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   647                                                      
REMARK 465     ARG B   648                                                      
REMARK 465     PRO B   649                                                      
REMARK 465     LEU B   650                                                      
REMARK 465     SER B   651                                                      
REMARK 465     VAL B   652                                                      
REMARK 465     PRO B   653                                                      
REMARK 465     GLY B   654                                                      
REMARK 465     SER B   655                                                      
REMARK 465     PRO B   656                                                      
REMARK 465     ARG B   657                                                      
REMARK 465     ASP B   658                                                      
REMARK 465     LEU B   659                                                      
REMARK 465     ARG B   660                                                      
REMARK 465     SER B   661                                                      
REMARK 465     ASN B   662                                                      
REMARK 465     SER B   663                                                      
REMARK 465     THR B   664                                                      
REMARK 465     VAL B   665                                                      
REMARK 465     TYR B   666                                                      
REMARK 465     MET B   667                                                      
REMARK 465     THR B   668                                                      
REMARK 465     PRO B   669                                                      
REMARK 465     GLY B   670                                                      
REMARK 465     ASP B   671                                                      
REMARK 465     LEU B   672                                                      
REMARK 465     GLY B   673                                                      
REMARK 465     THR B   674                                                      
REMARK 465     LEU B   675                                                      
REMARK 465     GLN B   676                                                      
REMARK 465     GLU B   677                                                      
REMARK 465     VAL B   678                                                      
REMARK 465     ASN B   679                                                      
REMARK 465     ASN B   680                                                      
REMARK 465     ALA B   681                                                      
REMARK 465     ASP B   682                                                      
REMARK 465     ASP B   683                                                      
REMARK 465     TYR B   684                                                      
REMARK 465     PHE B   685                                                      
REMARK 465     SER B   686                                                      
REMARK 465     LEU B   687                                                      
REMARK 465     GLY B   688                                                      
REMARK 465     VAL B   689                                                      
REMARK 465     ASN B   690                                                      
REMARK 465     PRO B   691                                                      
REMARK 465     ALA B   692                                                      
REMARK 465     ALA B   693                                                      
REMARK 465     ASP B   694                                                      
REMARK 465     ASP B   695                                                      
REMARK 465     ASP B   696                                                      
REMARK 465     ASP B   697                                                      
REMARK 465     ASP B   698                                                      
REMARK 465     GLY B   699                                                      
REMARK 465     PRO B   700                                                      
REMARK 465     TYR B   701                                                      
REMARK 465     ALA B   702                                                      
REMARK 465     ASP B   703                                                      
REMARK 465     ASP B   704                                                      
REMARK 465     SER B   705                                                      
REMARK 465     MET C   -19                                                      
REMARK 465     GLY C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ARG C   648                                                      
REMARK 465     PRO C   649                                                      
REMARK 465     LEU C   650                                                      
REMARK 465     SER C   651                                                      
REMARK 465     VAL C   652                                                      
REMARK 465     PRO C   653                                                      
REMARK 465     GLY C   654                                                      
REMARK 465     SER C   655                                                      
REMARK 465     PRO C   656                                                      
REMARK 465     ARG C   657                                                      
REMARK 465     ASP C   658                                                      
REMARK 465     LEU C   659                                                      
REMARK 465     ARG C   660                                                      
REMARK 465     SER C   661                                                      
REMARK 465     ASN C   662                                                      
REMARK 465     SER C   663                                                      
REMARK 465     THR C   664                                                      
REMARK 465     VAL C   665                                                      
REMARK 465     TYR C   666                                                      
REMARK 465     MET C   667                                                      
REMARK 465     THR C   668                                                      
REMARK 465     PRO C   669                                                      
REMARK 465     GLY C   670                                                      
REMARK 465     ASP C   671                                                      
REMARK 465     LEU C   672                                                      
REMARK 465     GLY C   673                                                      
REMARK 465     THR C   674                                                      
REMARK 465     LEU C   675                                                      
REMARK 465     GLN C   676                                                      
REMARK 465     GLU C   677                                                      
REMARK 465     VAL C   678                                                      
REMARK 465     ASN C   679                                                      
REMARK 465     ASN C   680                                                      
REMARK 465     ALA C   681                                                      
REMARK 465     ASP C   682                                                      
REMARK 465     ASP C   683                                                      
REMARK 465     TYR C   684                                                      
REMARK 465     PHE C   685                                                      
REMARK 465     SER C   686                                                      
REMARK 465     LEU C   687                                                      
REMARK 465     GLY C   688                                                      
REMARK 465     VAL C   689                                                      
REMARK 465     ASN C   690                                                      
REMARK 465     PRO C   691                                                      
REMARK 465     ALA C   692                                                      
REMARK 465     ALA C   693                                                      
REMARK 465     ASP C   694                                                      
REMARK 465     ASP C   695                                                      
REMARK 465     ASP C   696                                                      
REMARK 465     ASP C   697                                                      
REMARK 465     ASP C   698                                                      
REMARK 465     GLY C   699                                                      
REMARK 465     PRO C   700                                                      
REMARK 465     TYR C   701                                                      
REMARK 465     ALA C   702                                                      
REMARK 465     ASP C   703                                                      
REMARK 465     ASP C   704                                                      
REMARK 465     SER C   705                                                      
REMARK 465     MET D   -19                                                      
REMARK 465     GLY D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D   206                                                      
REMARK 465     PHE D   207                                                      
REMARK 465     GLY D   640                                                      
REMARK 465     GLY D   641                                                      
REMARK 465     LYS D   642                                                      
REMARK 465     LYS D   643                                                      
REMARK 465     LEU D   644                                                      
REMARK 465     LYS D   645                                                      
REMARK 465     VAL D   646                                                      
REMARK 465     ALA D   647                                                      
REMARK 465     ARG D   648                                                      
REMARK 465     PRO D   649                                                      
REMARK 465     LEU D   650                                                      
REMARK 465     SER D   651                                                      
REMARK 465     VAL D   652                                                      
REMARK 465     PRO D   653                                                      
REMARK 465     GLY D   654                                                      
REMARK 465     SER D   655                                                      
REMARK 465     PRO D   656                                                      
REMARK 465     ARG D   657                                                      
REMARK 465     ASP D   658                                                      
REMARK 465     LEU D   659                                                      
REMARK 465     ARG D   660                                                      
REMARK 465     SER D   661                                                      
REMARK 465     ASN D   662                                                      
REMARK 465     SER D   663                                                      
REMARK 465     THR D   664                                                      
REMARK 465     VAL D   665                                                      
REMARK 465     TYR D   666                                                      
REMARK 465     MET D   667                                                      
REMARK 465     THR D   668                                                      
REMARK 465     PRO D   669                                                      
REMARK 465     GLY D   670                                                      
REMARK 465     ASP D   671                                                      
REMARK 465     LEU D   672                                                      
REMARK 465     GLY D   673                                                      
REMARK 465     THR D   674                                                      
REMARK 465     LEU D   675                                                      
REMARK 465     GLN D   676                                                      
REMARK 465     GLU D   677                                                      
REMARK 465     VAL D   678                                                      
REMARK 465     ASN D   679                                                      
REMARK 465     ASN D   680                                                      
REMARK 465     ALA D   681                                                      
REMARK 465     ASP D   682                                                      
REMARK 465     ASP D   683                                                      
REMARK 465     TYR D   684                                                      
REMARK 465     PHE D   685                                                      
REMARK 465     SER D   686                                                      
REMARK 465     LEU D   687                                                      
REMARK 465     GLY D   688                                                      
REMARK 465     VAL D   689                                                      
REMARK 465     ASN D   690                                                      
REMARK 465     PRO D   691                                                      
REMARK 465     ALA D   692                                                      
REMARK 465     ALA D   693                                                      
REMARK 465     ASP D   694                                                      
REMARK 465     ASP D   695                                                      
REMARK 465     ASP D   696                                                      
REMARK 465     ASP D   697                                                      
REMARK 465     ASP D   698                                                      
REMARK 465     GLY D   699                                                      
REMARK 465     PRO D   700                                                      
REMARK 465     TYR D   701                                                      
REMARK 465     ALA D   702                                                      
REMARK 465     ASP D   703                                                      
REMARK 465     ASP D   704                                                      
REMARK 465     SER D   705                                                      
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     SER B 535    OG                                                  
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    ASN A  19      101.38   -165.60                                   
REMARK 500    LYS A  40     -129.03     55.26                                   
REMARK 500    THR A  53      -15.78   -142.46                                   
REMARK 500    ARG A  86       -5.38   -141.60                                   
REMARK 500    LEU A  96       71.95    -68.98                                   
REMARK 500    ALA A 100       71.55     27.34                                   
REMARK 500    SER A 110       -1.90    -56.83                                   
REMARK 500    VAL A 111       10.73   -145.15                                   
REMARK 500    TYR A 114        2.89    -60.51                                   
REMARK 500    SER A 115      -71.48    -42.42                                   
REMARK 500    SER A 130       89.21   -167.14                                   
REMARK 500    GLN A 160      -62.88   -100.80                                   
REMARK 500    GLU A 169      151.69     80.20                                   
REMARK 500    ALA A 194     -165.22    179.01                                   
REMARK 500    LYS A 260       33.83     71.62                                   
REMARK 500    LEU A 267       77.12   -119.98                                   
REMARK 500    TYR A 321       81.09    -68.17                                   
REMARK 500    SER A 363     -176.00     76.25                                   
REMARK 500    PRO A 478       49.57    -74.57                                   
REMARK 500    GLU A 509       85.46   -172.06                                   
REMARK 500    LEU A 625       17.87    -63.38                                   
REMARK 500    VAL A 626      -82.52   -131.58                                   
REMARK 500    GLU A 628     -174.84   -173.14                                   
REMARK 500    VAL B  17      -76.38    -44.75                                   
REMARK 500    LYS B  40     -124.01     56.04                                   
REMARK 500    THR B  53      -11.53   -146.24                                   
REMARK 500    SER B 130       66.33   -160.05                                   
REMARK 500    GLU B 169      151.45     76.96                                   
REMARK 500    ALA B 194     -175.55    177.20                                   
REMARK 500    HIS B 220      -71.23    -49.19                                   
REMARK 500    TYR B 321       89.16    -65.81                                   
REMARK 500    SER B 363     -175.40     73.49                                   
REMARK 500    PRO B 401       40.83   -103.73                                   
REMARK 500    ASP B 449       68.24     60.58                                   
REMARK 500    PRO B 478       41.55    -69.39                                   
REMARK 500    LYS B 642       53.22   -162.59                                   
REMARK 500    LYS B 643       93.37    -55.78                                   
REMARK 500    VAL C  17      -75.68    -55.38                                   
REMARK 500    ALA C  18       40.35    -98.49                                   
REMARK 500    ASN C  19      123.38   -177.14                                   
REMARK 500    LYS C  40     -127.01     57.42                                   
REMARK 500    ALA C  52      -71.80    -85.59                                   
REMARK 500    PRO C 131      170.20    -58.20                                   
REMARK 500    GLU C 169      154.29     68.17                                   
REMARK 500    ALA C 194     -172.41   -173.95                                   
REMARK 500    CYS C 212       39.68   -152.66                                   
REMARK 500    CYS C 304       29.43   -143.78                                   
REMARK 500    SER C 363     -177.76     86.63                                   
REMARK 500    PRO C 435      155.72    -47.15                                   
REMARK 500    PRO C 478       48.61    -78.45                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      74 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 835        DISTANCE =  5.16 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P A 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P B 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P C 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P D 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 1002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1RZU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2BIS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2QZS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NAZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NCH   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CRYSTALLIZED SEQUENCE HAS BEEN REFERENCED TO UNP ENTRY P27472.   
REMARK 999 HOWEVER, RESIDUE A535S IS ANNOTATED IN REMARK 999 GENBANK ENTRY      
REMARK 999 ACCESSION CODE AAA88716                                              
DBREF  3NB0 A    1   705  UNP    P27472   GYS2_YEAST       1    705             
DBREF  3NB0 B    1   705  UNP    P27472   GYS2_YEAST       1    705             
DBREF  3NB0 C    1   705  UNP    P27472   GYS2_YEAST       1    705             
DBREF  3NB0 D    1   705  UNP    P27472   GYS2_YEAST       1    705             
SEQADV 3NB0 MET A  -19  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 GLY A  -18  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER A  -17  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER A  -16  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS A  -15  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS A  -14  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS A  -13  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS A  -12  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS A  -11  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS A  -10  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER A   -9  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER A   -8  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 GLY A   -7  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 LEU A   -6  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 VAL A   -5  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 PRO A   -4  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 ARG A   -3  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 GLY A   -2  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER A   -1  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS A    0  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER A  535  UNP  P27472    ALA   535 SEE REMARK 999                 
SEQADV 3NB0 ALA A  589  UNP  P27472    ARG   589 ENGINEERED MUTATION            
SEQADV 3NB0 ALA A  592  UNP  P27472    ARG   592 ENGINEERED MUTATION            
SEQADV 3NB0 MET B  -19  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 GLY B  -18  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER B  -17  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER B  -16  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS B  -15  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS B  -14  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS B  -13  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS B  -12  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS B  -11  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS B  -10  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER B   -9  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER B   -8  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 GLY B   -7  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 LEU B   -6  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 VAL B   -5  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 PRO B   -4  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 ARG B   -3  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 GLY B   -2  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER B   -1  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS B    0  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER B  535  UNP  P27472    ALA   535 SEE REMARK 999                 
SEQADV 3NB0 ALA B  589  UNP  P27472    ARG   589 ENGINEERED MUTATION            
SEQADV 3NB0 ALA B  592  UNP  P27472    ARG   592 ENGINEERED MUTATION            
SEQADV 3NB0 MET C  -19  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 GLY C  -18  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER C  -17  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER C  -16  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS C  -15  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS C  -14  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS C  -13  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS C  -12  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS C  -11  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS C  -10  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER C   -9  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER C   -8  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 GLY C   -7  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 LEU C   -6  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 VAL C   -5  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 PRO C   -4  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 ARG C   -3  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 GLY C   -2  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER C   -1  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS C    0  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER C  535  UNP  P27472    ALA   535 SEE REMARK 999                 
SEQADV 3NB0 ALA C  589  UNP  P27472    ARG   589 ENGINEERED MUTATION            
SEQADV 3NB0 ALA C  592  UNP  P27472    ARG   592 ENGINEERED MUTATION            
SEQADV 3NB0 MET D  -19  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 GLY D  -18  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER D  -17  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER D  -16  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS D  -15  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS D  -14  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS D  -13  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS D  -12  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS D  -11  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS D  -10  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER D   -9  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER D   -8  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 GLY D   -7  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 LEU D   -6  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 VAL D   -5  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 PRO D   -4  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 ARG D   -3  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 GLY D   -2  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER D   -1  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 HIS D    0  UNP  P27472              EXPRESSION TAG                 
SEQADV 3NB0 SER D  535  UNP  P27472    ALA   535 SEE REMARK 999                 
SEQADV 3NB0 ALA D  589  UNP  P27472    ARG   589 ENGINEERED MUTATION            
SEQADV 3NB0 ALA D  592  UNP  P27472    ARG   592 ENGINEERED MUTATION            
SEQRES   1 A  725  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  725  LEU VAL PRO ARG GLY SER HIS MET SER ARG ASP LEU GLN          
SEQRES   3 A  725  ASN HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN          
SEQRES   4 A  725  ARG VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA          
SEQRES   5 A  725  PRO ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU          
SEQRES   6 A  725  ILE GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL          
SEQRES   7 A  725  ASP ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP          
SEQRES   8 A  725  GLU MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU          
SEQRES   9 A  725  SER ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE          
SEQRES  10 A  725  GLU GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER          
SEQRES  11 A  725  VAL ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP          
SEQRES  12 A  725  SER LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU          
SEQRES  13 A  725  THR ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP          
SEQRES  14 A  725  PHE LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA          
SEQRES  15 A  725  ILE VAL ALA HIS PHE HIS GLU TRP LEU ALA GLY VAL ALA          
SEQRES  16 A  725  LEU PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR          
SEQRES  17 A  725  ILE PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU          
SEQRES  18 A  725  CYS ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU          
SEQRES  19 A  725  SER VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE          
SEQRES  20 A  725  TYR HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER          
SEQRES  21 A  725  ALA ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE          
SEQRES  22 A  725  GLU ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE          
SEQRES  23 A  725  LEU PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE          
SEQRES  24 A  725  HIS GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS          
SEQRES  25 A  725  ILE ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE          
SEQRES  26 A  725  ASP PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA          
SEQRES  27 A  725  GLY ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE          
SEQRES  28 A  725  ILE GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL          
SEQRES  29 A  725  SER GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET          
SEQRES  30 A  725  PRO ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS          
SEQRES  31 A  725  GLY GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS          
SEQRES  32 A  725  GLU VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS          
SEQRES  33 A  725  ALA ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU          
SEQRES  34 A  725  PRO THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS          
SEQRES  35 A  725  VAL MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO          
SEQRES  36 A  725  GLU GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL          
SEQRES  37 A  725  ASP ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN          
SEQRES  38 A  725  VAL GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET          
SEQRES  39 A  725  ILE PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE          
SEQRES  40 A  725  LEU GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS          
SEQRES  41 A  725  LEU GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR          
SEQRES  42 A  725  THR PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE          
SEQRES  43 A  725  THR THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP          
SEQRES  44 A  725  LEU ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR          
SEQRES  45 A  725  ILE VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL          
SEQRES  46 A  725  GLU GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS          
SEQRES  47 A  725  THR ARG ARG GLN ARG ILE ASN GLN ARG ASN ALA THR GLU          
SEQRES  48 A  725  ALA LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU          
SEQRES  49 A  725  GLU TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY          
SEQRES  50 A  725  TYR PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU          
SEQRES  51 A  725  ASN ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS          
SEQRES  52 A  725  LEU LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO          
SEQRES  53 A  725  ARG ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO          
SEQRES  54 A  725  GLY ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP          
SEQRES  55 A  725  ASP TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP          
SEQRES  56 A  725  ASP ASP ASP GLY PRO TYR ALA ASP ASP SER                      
SEQRES   1 B  725  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  725  LEU VAL PRO ARG GLY SER HIS MET SER ARG ASP LEU GLN          
SEQRES   3 B  725  ASN HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN          
SEQRES   4 B  725  ARG VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA          
SEQRES   5 B  725  PRO ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU          
SEQRES   6 B  725  ILE GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL          
SEQRES   7 B  725  ASP ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP          
SEQRES   8 B  725  GLU MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU          
SEQRES   9 B  725  SER ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE          
SEQRES  10 B  725  GLU GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER          
SEQRES  11 B  725  VAL ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP          
SEQRES  12 B  725  SER LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU          
SEQRES  13 B  725  THR ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP          
SEQRES  14 B  725  PHE LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA          
SEQRES  15 B  725  ILE VAL ALA HIS PHE HIS GLU TRP LEU ALA GLY VAL ALA          
SEQRES  16 B  725  LEU PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR          
SEQRES  17 B  725  ILE PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU          
SEQRES  18 B  725  CYS ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU          
SEQRES  19 B  725  SER VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE          
SEQRES  20 B  725  TYR HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER          
SEQRES  21 B  725  ALA ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE          
SEQRES  22 B  725  GLU ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE          
SEQRES  23 B  725  LEU PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE          
SEQRES  24 B  725  HIS GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS          
SEQRES  25 B  725  ILE ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE          
SEQRES  26 B  725  ASP PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA          
SEQRES  27 B  725  GLY ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE          
SEQRES  28 B  725  ILE GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL          
SEQRES  29 B  725  SER GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET          
SEQRES  30 B  725  PRO ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS          
SEQRES  31 B  725  GLY GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS          
SEQRES  32 B  725  GLU VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS          
SEQRES  33 B  725  ALA ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU          
SEQRES  34 B  725  PRO THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS          
SEQRES  35 B  725  VAL MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO          
SEQRES  36 B  725  GLU GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL          
SEQRES  37 B  725  ASP ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN          
SEQRES  38 B  725  VAL GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET          
SEQRES  39 B  725  ILE PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE          
SEQRES  40 B  725  LEU GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS          
SEQRES  41 B  725  LEU GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR          
SEQRES  42 B  725  THR PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE          
SEQRES  43 B  725  THR THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP          
SEQRES  44 B  725  LEU ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR          
SEQRES  45 B  725  ILE VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL          
SEQRES  46 B  725  GLU GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS          
SEQRES  47 B  725  THR ARG ARG GLN ARG ILE ASN GLN ARG ASN ALA THR GLU          
SEQRES  48 B  725  ALA LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU          
SEQRES  49 B  725  GLU TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY          
SEQRES  50 B  725  TYR PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU          
SEQRES  51 B  725  ASN ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS          
SEQRES  52 B  725  LEU LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO          
SEQRES  53 B  725  ARG ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO          
SEQRES  54 B  725  GLY ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP          
SEQRES  55 B  725  ASP TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP          
SEQRES  56 B  725  ASP ASP ASP GLY PRO TYR ALA ASP ASP SER                      
SEQRES   1 C  725  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  725  LEU VAL PRO ARG GLY SER HIS MET SER ARG ASP LEU GLN          
SEQRES   3 C  725  ASN HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN          
SEQRES   4 C  725  ARG VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA          
SEQRES   5 C  725  PRO ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU          
SEQRES   6 C  725  ILE GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL          
SEQRES   7 C  725  ASP ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP          
SEQRES   8 C  725  GLU MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU          
SEQRES   9 C  725  SER ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE          
SEQRES  10 C  725  GLU GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER          
SEQRES  11 C  725  VAL ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP          
SEQRES  12 C  725  SER LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU          
SEQRES  13 C  725  THR ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP          
SEQRES  14 C  725  PHE LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA          
SEQRES  15 C  725  ILE VAL ALA HIS PHE HIS GLU TRP LEU ALA GLY VAL ALA          
SEQRES  16 C  725  LEU PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR          
SEQRES  17 C  725  ILE PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU          
SEQRES  18 C  725  CYS ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU          
SEQRES  19 C  725  SER VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE          
SEQRES  20 C  725  TYR HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER          
SEQRES  21 C  725  ALA ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE          
SEQRES  22 C  725  GLU ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE          
SEQRES  23 C  725  LEU PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE          
SEQRES  24 C  725  HIS GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS          
SEQRES  25 C  725  ILE ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE          
SEQRES  26 C  725  ASP PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA          
SEQRES  27 C  725  GLY ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE          
SEQRES  28 C  725  ILE GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL          
SEQRES  29 C  725  SER GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET          
SEQRES  30 C  725  PRO ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS          
SEQRES  31 C  725  GLY GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS          
SEQRES  32 C  725  GLU VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS          
SEQRES  33 C  725  ALA ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU          
SEQRES  34 C  725  PRO THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS          
SEQRES  35 C  725  VAL MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO          
SEQRES  36 C  725  GLU GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL          
SEQRES  37 C  725  ASP ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN          
SEQRES  38 C  725  VAL GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET          
SEQRES  39 C  725  ILE PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE          
SEQRES  40 C  725  LEU GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS          
SEQRES  41 C  725  LEU GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR          
SEQRES  42 C  725  THR PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE          
SEQRES  43 C  725  THR THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP          
SEQRES  44 C  725  LEU ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR          
SEQRES  45 C  725  ILE VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL          
SEQRES  46 C  725  GLU GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS          
SEQRES  47 C  725  THR ARG ARG GLN ARG ILE ASN GLN ARG ASN ALA THR GLU          
SEQRES  48 C  725  ALA LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU          
SEQRES  49 C  725  GLU TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY          
SEQRES  50 C  725  TYR PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU          
SEQRES  51 C  725  ASN ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS          
SEQRES  52 C  725  LEU LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO          
SEQRES  53 C  725  ARG ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO          
SEQRES  54 C  725  GLY ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP          
SEQRES  55 C  725  ASP TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP          
SEQRES  56 C  725  ASP ASP ASP GLY PRO TYR ALA ASP ASP SER                      
SEQRES   1 D  725  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  725  LEU VAL PRO ARG GLY SER HIS MET SER ARG ASP LEU GLN          
SEQRES   3 D  725  ASN HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN          
SEQRES   4 D  725  ARG VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA          
SEQRES   5 D  725  PRO ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU          
SEQRES   6 D  725  ILE GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL          
SEQRES   7 D  725  ASP ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP          
SEQRES   8 D  725  GLU MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU          
SEQRES   9 D  725  SER ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE          
SEQRES  10 D  725  GLU GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER          
SEQRES  11 D  725  VAL ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP          
SEQRES  12 D  725  SER LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU          
SEQRES  13 D  725  THR ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP          
SEQRES  14 D  725  PHE LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA          
SEQRES  15 D  725  ILE VAL ALA HIS PHE HIS GLU TRP LEU ALA GLY VAL ALA          
SEQRES  16 D  725  LEU PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR          
SEQRES  17 D  725  ILE PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU          
SEQRES  18 D  725  CYS ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU          
SEQRES  19 D  725  SER VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE          
SEQRES  20 D  725  TYR HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER          
SEQRES  21 D  725  ALA ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE          
SEQRES  22 D  725  GLU ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE          
SEQRES  23 D  725  LEU PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE          
SEQRES  24 D  725  HIS GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS          
SEQRES  25 D  725  ILE ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE          
SEQRES  26 D  725  ASP PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA          
SEQRES  27 D  725  GLY ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE          
SEQRES  28 D  725  ILE GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL          
SEQRES  29 D  725  SER GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET          
SEQRES  30 D  725  PRO ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS          
SEQRES  31 D  725  GLY GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS          
SEQRES  32 D  725  GLU VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS          
SEQRES  33 D  725  ALA ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU          
SEQRES  34 D  725  PRO THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS          
SEQRES  35 D  725  VAL MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO          
SEQRES  36 D  725  GLU GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL          
SEQRES  37 D  725  ASP ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN          
SEQRES  38 D  725  VAL GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET          
SEQRES  39 D  725  ILE PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE          
SEQRES  40 D  725  LEU GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS          
SEQRES  41 D  725  LEU GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR          
SEQRES  42 D  725  THR PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE          
SEQRES  43 D  725  THR THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP          
SEQRES  44 D  725  LEU ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR          
SEQRES  45 D  725  ILE VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL          
SEQRES  46 D  725  GLU GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS          
SEQRES  47 D  725  THR ARG ARG GLN ARG ILE ASN GLN ARG ASN ALA THR GLU          
SEQRES  48 D  725  ALA LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU          
SEQRES  49 D  725  GLU TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY          
SEQRES  50 D  725  TYR PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU          
SEQRES  51 D  725  ASN ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS          
SEQRES  52 D  725  LEU LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO          
SEQRES  53 D  725  ARG ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO          
SEQRES  54 D  725  GLY ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP          
SEQRES  55 D  725  ASP TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP          
SEQRES  56 D  725  ASP ASP ASP GLY PRO TYR ALA ASP ASP SER                      
HET    G6P  A 901      16                                                       
HET    G6P  A 902      16                                                       
HET    PEG  A1001       7                                                       
HET    PEG  B1002       7                                                       
HET    G6P  B 901      16                                                       
HET    G6P  B 902      16                                                       
HET    PEG  B1001       7                                                       
HET    PEG  B 706       7                                                       
HET    G6P  C 901      16                                                       
HET    PEG  C1001       7                                                       
HET    G6P  D 901      16                                                       
HET    PEG  D1002       7                                                       
HETNAM     G6P ALPHA-D-GLUCOSE-6-PHOSPHATE                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   5  G6P    6(C6 H13 O9 P)                                               
FORMUL   7  PEG    6(C4 H10 O3)                                                 
FORMUL  17  HOH   *524(H2 O)                                                    
HELIX    1   1 GLY A   22  LYS A   40  1                                  19    
HELIX    2   2 THR A   53  GLU A   57  1                                   5    
HELIX    3   3 LYS A   65  PHE A   69  5                                   5    
HELIX    4   4 MET A   73  SER A   85  1                                  13    
HELIX    5   5 LEU A  108  GLY A  113  5                                   6    
HELIX    6   6 TYR A  114  GLY A  127  1                                  14    
HELIX    7   7 ASP A  134  ASP A  158  1                                  25    
HELIX    8   8 TRP A  170  GLY A  173  5                                   4    
HELIX    9   9 VAL A  174  ARG A  182  1                                   9    
HELIX   10  10 THR A  195  CYS A  202  1                                   8    
HELIX   11  11 ASP A  208  LEU A  213  1                                   6    
HELIX   12  12 GLU A  214  VAL A  216  5                                   3    
HELIX   13  13 ASP A  217  PHE A  225  1                                   9    
HELIX   14  14 ILE A  227  ALA A  241  1                                  15    
HELIX   15  15 SER A  248  LEU A  259  1                                  12    
HELIX   16  16 HIS A  280  PHE A  301  1                                  22    
HELIX   17  17 ASP A  308  ASP A  310  5                                   3    
HELIX   18  18 GLY A  327  SER A  345  1                                  19    
HELIX   19  19 THR A  365  TYR A  400  1                                  36    
HELIX   20  20 ASP A  412  LEU A  417  1                                   6    
HELIX   21  21 LYS A  418  ARG A  433  1                                  16    
HELIX   22  22 ASP A  449  ASN A  452  5                                   4    
HELIX   23  23 ASP A  453  GLN A  463  1                                  11    
HELIX   24  24 ASP A  491  CYS A  499  1                                   9    
HELIX   25  25 GLY A  512  MET A  521  1                                  10    
HELIX   26  26 SER A  531  ASP A  539  1                                   9    
HELIX   27  27 GLU A  542  TYR A  549  1                                   8    
HELIX   28  28 ALA A  560  LYS A  577  1                                  18    
HELIX   29  29 THR A  579  LEU A  593  1                                  15    
HELIX   30  30 SER A  594  LEU A  597  5                                   4    
HELIX   31  31 ASP A  598  TYR A  618  1                                  21    
HELIX   32  32 TYR A  618  LEU A  625  1                                   8    
HELIX   33  33 ASN A  634  ALA A  639  1                                   6    
HELIX   34  34 GLY B   23  LYS B   40  1                                  18    
HELIX   35  35 THR B   53  GLU B   57  1                                   5    
HELIX   36  36 LYS B   65  PHE B   69  5                                   5    
HELIX   37  37 SER B   70  GLU B   72  5                                   3    
HELIX   38  38 MET B   73  SER B   85  1                                  13    
HELIX   39  39 LEU B  108  GLY B  113  5                                   6    
HELIX   40  40 TYR B  114  VAL B  126  1                                  13    
HELIX   41  41 ASP B  134  ASP B  158  1                                  25    
HELIX   42  42 TRP B  170  GLY B  173  5                                   4    
HELIX   43  43 VAL B  174  ARG B  182  1                                   9    
HELIX   44  44 THR B  195  SER B  204  1                                  10    
HELIX   45  45 ASP B  217  PHE B  225  1                                   9    
HELIX   46  46 ILE B  227  ALA B  241  1                                  15    
HELIX   47  47 SER B  248  LEU B  259  1                                  12    
HELIX   48  48 HIS B  280  PHE B  301  1                                  22    
HELIX   49  49 ASP B  308  ASP B  310  5                                   3    
HELIX   50  50 GLY B  327  GLY B  346  1                                  20    
HELIX   51  51 THR B  365  TYR B  400  1                                  36    
HELIX   52  52 ASP B  412  LEU B  417  1                                   6    
HELIX   53  53 LYS B  418  ALA B  431  1                                  14    
HELIX   54  54 ASP B  453  GLN B  463  1                                  11    
HELIX   55  55 ASP B  491  CYS B  499  1                                   9    
HELIX   56  56 GLY B  512  MET B  521  1                                  10    
HELIX   57  57 SER B  531  ASP B  539  1                                   9    
HELIX   58  58 GLU B  542  LYS B  547  1                                   6    
HELIX   59  59 ALA B  560  LYS B  578  1                                  19    
HELIX   60  60 THR B  579  LEU B  593  1                                  15    
HELIX   61  61 SER B  594  LEU B  597  5                                   4    
HELIX   62  62 ASP B  598  TYR B  618  1                                  21    
HELIX   63  63 TYR B  618  GLY B  627  1                                  10    
HELIX   64  64 ASN B  634  GLY B  640  1                                   7    
HELIX   65  65 GLY C   22  LYS C   40  1                                  19    
HELIX   66  66 THR C   53  GLU C   57  1                                   5    
HELIX   67  67 LYS C   65  PHE C   69  5                                   5    
HELIX   68  68 SER C   70  GLU C   72  5                                   3    
HELIX   69  69 MET C   73  ARG C   86  1                                  14    
HELIX   70  70 LEU C  108  GLY C  113  5                                   6    
HELIX   71  71 TYR C  114  GLY C  127  1                                  14    
HELIX   72  72 ASP C  134  ASP C  158  1                                  25    
HELIX   73  73 TRP C  170  GLY C  173  5                                   4    
HELIX   74  74 VAL C  174  ARG C  183  1                                  10    
HELIX   75  75 THR C  195  SER C  204  1                                  10    
HELIX   76  76 ASP C  217  PHE C  225  1                                   9    
HELIX   77  77 ILE C  227  ALA C  241  1                                  15    
HELIX   78  78 SER C  248  LEU C  259  1                                  12    
HELIX   79  79 HIS C  280  PHE C  301  1                                  22    
HELIX   80  80 ASP C  308  ASP C  310  5                                   3    
HELIX   81  81 GLY C  327  GLY C  346  1                                  20    
HELIX   82  82 THR C  365  TYR C  400  1                                  36    
HELIX   83  83 ASP C  412  LEU C  416  5                                   5    
HELIX   84  84 LYS C  418  ARG C  433  1                                  16    
HELIX   85  85 ASP C  453  GLN C  463  1                                  11    
HELIX   86  86 ASP C  491  CYS C  499  1                                   9    
HELIX   87  87 GLY C  512  MET C  521  1                                  10    
HELIX   88  88 SER C  531  ILE C  541  1                                  11    
HELIX   89  89 GLU C  542  TYR C  549  5                                   8    
HELIX   90  90 ALA C  560  LYS C  577  1                                  18    
HELIX   91  91 THR C  579  SER C  594  1                                  16    
HELIX   92  92 ASP C  595  LEU C  597  5                                   3    
HELIX   93  93 ASP C  598  TYR C  618  1                                  21    
HELIX   94  94 TYR C  618  GLY C  627  1                                  10    
HELIX   95  95 ASN C  634  GLY C  640  1                                   7    
HELIX   96  96 GLY D   22  LYS D   40  1                                  19    
HELIX   97  97 THR D   53  GLU D   57  1                                   5    
HELIX   98  98 LYS D   65  PHE D   69  5                                   5    
HELIX   99  99 MET D   73  ARG D   86  1                                  14    
HELIX  100 100 LEU D  108  GLY D  113  5                                   6    
HELIX  101 101 TYR D  114  VAL D  126  1                                  13    
HELIX  102 102 ASP D  134  ASP D  158  1                                  25    
HELIX  103 103 TRP D  170  GLY D  173  5                                   4    
HELIX  104 104 VAL D  174  ARG D  183  1                                  10    
HELIX  105 105 THR D  195  ALA D  203  1                                   9    
HELIX  106 106 ASP D  217  GLY D  226  1                                  10    
HELIX  107 107 ILE D  227  ALA D  241  1                                  15    
HELIX  108 108 SER D  248  LEU D  259  1                                  12    
HELIX  109 109 HIS D  280  PHE D  301  1                                  22    
HELIX  110 110 ASP D  308  ASP D  310  5                                   3    
HELIX  111 111 GLY D  327  SER D  345  1                                  19    
HELIX  112 112 THR D  365  TYR D  400  1                                  36    
HELIX  113 113 ASP D  412  LEU D  417  1                                   6    
HELIX  114 114 LYS D  418  ARG D  433  1                                  16    
HELIX  115 115 ASP D  449  ASN D  452  5                                   4    
HELIX  116 116 ASP D  453  GLN D  463  1                                  11    
HELIX  117 117 ASP D  491  CYS D  499  1                                   9    
HELIX  118 118 GLY D  512  MET D  521  1                                  10    
HELIX  119 119 SER D  531  GLU D  538  1                                   8    
HELIX  120 120 GLU D  542  TYR D  549  1                                   8    
HELIX  121 121 ALA D  560  LYS D  577  1                                  18    
HELIX  122 122 THR D  579  SER D  594  1                                  16    
HELIX  123 123 ASP D  595  LEU D  597  5                                   3    
HELIX  124 124 ASP D  598  TYR D  618  1                                  21    
HELIX  125 125 TYR D  618  GLY D  627  1                                  10    
SHEET    1   A 9 VAL A  58  ILE A  60  0                                        
SHEET    2   A 9 PHE A  90  TRP A  95 -1  O  ARG A  94   N  ASP A  59           
SHEET    3   A 9 LYS A 102  PHE A 106 -1  O  VAL A 103   N  GLY A  93           
SHEET    4   A 9 TYR A  43  PRO A  48  1  N  LEU A  45   O  ILE A 104           
SHEET    5   A 9 ASP A   4  ALA A  14  1  N  GLU A  12   O  HIS A  44           
SHEET    6   A 9 HIS A 161  HIS A 168  1  O  HIS A 166   N  THR A  13           
SHEET    7   A 9 VAL A 187  THR A 192  1  O  ILE A 189   N  PHE A 167           
SHEET    8   A 9 VAL A 243  THR A 246  1  O  THR A 245   N  PHE A 190           
SHEET    9   A 9 GLY A 265  ILE A 266  1  O  GLY A 265   N  THR A 246           
SHEET    1   B 6 VAL A 472  PHE A 476  0                                        
SHEET    2   B 6 THR A 350  VAL A 356  1  N  VAL A 351   O  LYS A 473           
SHEET    3   B 6 THR A 312  ALA A 318  1  N  PHE A 315   O  PHE A 354           
SHEET    4   B 6 LEU A 501  VAL A 503  1  O  VAL A 503   N  PHE A 316           
SHEET    5   B 6 SER A 525  THR A 528  1  O  ILE A 526   N  GLY A 502           
SHEET    6   B 6 ILE A 551  VAL A 554  1  O  TYR A 552   N  THR A 527           
SHEET    1   C 2 ASN A 361  PHE A 364  0                                        
SHEET    2   C 2 HIS A 445  MET A 447 -1  O  ASN A 446   N  ASN A 362           
SHEET    1   D 9 VAL B  58  ILE B  60  0                                        
SHEET    2   D 9 PHE B  90  TRP B  95 -1  O  ARG B  94   N  ASP B  59           
SHEET    3   D 9 LYS B 102  PHE B 106 -1  O  LEU B 105   N  VAL B  91           
SHEET    4   D 9 TYR B  43  PRO B  48  1  N  LEU B  45   O  ILE B 104           
SHEET    5   D 9 ASP B   4  THR B  13  1  N  GLU B  12   O  ILE B  46           
SHEET    6   D 9 HIS B 161  HIS B 168  1  O  HIS B 166   N  THR B  13           
SHEET    7   D 9 VAL B 187  THR B 191  1  O  THR B 191   N  PHE B 167           
SHEET    8   D 9 VAL B 243  THR B 246  1  O  THR B 245   N  PHE B 190           
SHEET    9   D 9 GLY B 265  ILE B 266  1  O  GLY B 265   N  THR B 246           
SHEET    1   E 6 VAL B 472  PHE B 476  0                                        
SHEET    2   E 6 THR B 350  VAL B 356  1  N  VAL B 351   O  LYS B 473           
SHEET    3   E 6 THR B 312  ALA B 318  1  N  PHE B 315   O  PHE B 354           
SHEET    4   E 6 LEU B 501  VAL B 503  1  O  VAL B 503   N  PHE B 316           
SHEET    5   E 6 SER B 525  THR B 528  1  O  ILE B 526   N  GLY B 502           
SHEET    6   E 6 ILE B 551  VAL B 554  1  O  TYR B 552   N  THR B 527           
SHEET    1   F 2 ASN B 361  PHE B 364  0                                        
SHEET    2   F 2 HIS B 445  MET B 447 -1  O  ASN B 446   N  ASN B 362           
SHEET    1   G 9 VAL C  58  ILE C  60  0                                        
SHEET    2   G 9 PHE C  90  TRP C  95 -1  O  ARG C  94   N  ASP C  59           
SHEET    3   G 9 LYS C 102  PHE C 106 -1  O  VAL C 103   N  GLY C  93           
SHEET    4   G 9 TYR C  43  PRO C  48  1  N  LEU C  45   O  ILE C 104           
SHEET    5   G 9 ASP C   4  THR C  13  1  N  GLU C  12   O  ILE C  46           
SHEET    6   G 9 HIS C 161  HIS C 168  1  O  HIS C 166   N  PHE C  11           
SHEET    7   G 9 VAL C 187  THR C 192  1  O  ILE C 189   N  PHE C 167           
SHEET    8   G 9 VAL C 243  THR C 246  1  O  THR C 245   N  PHE C 190           
SHEET    9   G 9 GLY C 265  ILE C 266  1  O  GLY C 265   N  THR C 246           
SHEET    1   H 6 VAL C 472  PHE C 476  0                                        
SHEET    2   H 6 THR C 350  VAL C 356  1  N  VAL C 351   O  LYS C 473           
SHEET    3   H 6 THR C 312  ALA C 318  1  N  LEU C 313   O  VAL C 352           
SHEET    4   H 6 LEU C 501  VAL C 503  1  O  VAL C 503   N  PHE C 316           
SHEET    5   H 6 SER C 525  THR C 528  1  O  ILE C 526   N  GLY C 502           
SHEET    6   H 6 ILE C 551  VAL C 554  1  O  TYR C 552   N  THR C 527           
SHEET    1   I 2 ASN C 361  PHE C 364  0                                        
SHEET    2   I 2 HIS C 445  MET C 447 -1  O  ASN C 446   N  ASN C 362           
SHEET    1   J 9 VAL D  58  ILE D  60  0                                        
SHEET    2   J 9 PHE D  90  TRP D  95 -1  O  ARG D  94   N  ASP D  59           
SHEET    3   J 9 LYS D 102  PHE D 106 -1  O  LEU D 105   N  VAL D  91           
SHEET    4   J 9 TYR D  43  PRO D  48  1  N  LEU D  45   O  ILE D 104           
SHEET    5   J 9 ASP D   4  THR D  13  1  N  GLU D  12   O  ILE D  46           
SHEET    6   J 9 HIS D 161  HIS D 168  1  O  HIS D 166   N  PHE D  11           
SHEET    7   J 9 VAL D 187  THR D 192  1  O  VAL D 187   N  ALA D 165           
SHEET    8   J 9 VAL D 243  THR D 246  1  O  THR D 245   N  PHE D 190           
SHEET    9   J 9 GLY D 265  ILE D 266  1  O  GLY D 265   N  THR D 246           
SHEET    1   K 6 VAL D 472  PHE D 476  0                                        
SHEET    2   K 6 THR D 350  VAL D 356  1  N  VAL D 351   O  LYS D 473           
SHEET    3   K 6 THR D 312  ALA D 318  1  N  LEU D 313   O  THR D 350           
SHEET    4   K 6 LEU D 501  VAL D 503  1  O  VAL D 503   N  PHE D 316           
SHEET    5   K 6 SER D 525  THR D 528  1  O  ILE D 526   N  GLY D 502           
SHEET    6   K 6 ILE D 551  VAL D 554  1  O  VAL D 554   N  THR D 527           
SHEET    1   L 2 ASN D 361  PHE D 364  0                                        
SHEET    2   L 2 HIS D 445  MET D 447 -1  O  ASN D 446   N  ASN D 362           
CISPEP   1 TYR A  400    PRO A  401          0         2.44                     
CISPEP   2 TYR B  400    PRO B  401          0        -0.05                     
CISPEP   3 TYR C  400    PRO C  401          0         2.53                     
CISPEP   4 TYR D  400    PRO D  401          0         3.61                     
SITE     1 AC1 14 GLN A 283  ASN A 284  HIS A 286  LYS A 290                    
SITE     2 AC1 14 HIS A 500  ARG A 580  ARG A 583  ARG A 587                    
SITE     3 AC1 14 HOH A 796  HOH A 803  HOH A 861  HOH A 865                    
SITE     4 AC1 14 HIS B 280  HOH B 808                                          
SITE     1 AC2  7 ARG A 199  ARG A 320  LYS A 326  TYR A 513                    
SITE     2 AC2  7 THR A 514  HOH A 814  HOH A 850                               
SITE     1 AC3  3 LYS A 391  PHE A 394  HIS C 383                               
SITE     1 AC4  4 ILE A 274  LYS A 275  GLN A 277  ARG B 581                    
SITE     1 AC5 10 HIS A 280  HOH A 839  GLN B 283  ASN B 284                    
SITE     2 AC5 10 HIS B 286  LYS B 290  HIS B 500  ARG B 580                    
SITE     3 AC5 10 ARG B 583  ARG B 587                                          
SITE     1 AC6 10 GLY B  23  GLU B 169  HIS B 193  ARG B 199                    
SITE     2 AC6 10 ARG B 320  LYS B 326  TYR B 513  HOH B 774                    
SITE     3 AC6 10 HOH B 790  HOH B 823                                          
SITE     1 AC7  4 LYS B 391  PHE B 394  GLU D 291  HIS D 383                    
SITE     1 AC8  5 GLU B 291  ARG B 298  HIS B 383  PHE D 394                    
SITE     2 AC8  5 HOH D 789                                                     
SITE     1 AC9 11 GLN C 283  ASN C 284  HIS C 286  ALA C 287                    
SITE     2 AC9 11 LYS C 290  HIS C 500  ARG C 580  ARG C 583                    
SITE     3 AC9 11 ARG C 587  HIS D 280  HOH D 747                               
SITE     1 BC1  4 GLU A 291  ARG A 298  LYS C 391  PHE C 394                    
SITE     1 BC2  9 HIS C 280  GLN D 283  ASN D 284  HIS D 286                    
SITE     2 BC2  9 LYS D 290  HIS D 500  ARG D 580  ARG D 583                    
SITE     3 BC2  9 ARG D 587                                                     
SITE     1 BC3  2 TYR D 340  HOH D 765                                          
CRYST1  192.739  206.982  205.799  90.00  90.00  90.00 I 2 2 2      32          
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      0.005188  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004831  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004859        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system