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Database: PDB
Entry: 3RSZ
LinkDB: 3RSZ
Original site: 3RSZ 
HEADER    TRANSFERASE                             02-MAY-11   3RSZ              
TITLE     MALTODEXTRAN BOUND BASAL STATE CONFORMATION OF YEAST GLYCOGEN SYNTHASE
TITLE    2 ISOFORM 2                                                            
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;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: GLYCOGEN [STARCH] SYNTHASE ISOFORM 2;                      
COMPND   9 CHAIN: E, F;                                                         
COMPND  10 ENGINEERED: 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;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  13 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;              
SOURCE  14 ORGANISM_TAXID: 4932;                                                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    MALTODEXTRAN BINDING, ROSSMANN FOLD, GLYCOSYL TRANSFERASE, GLYCOGEN   
KEYWDS   2 BINDING, TRANSFERASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BASKARAN,T.D.HURLEY                                                 
REVDAT   3   12-OCT-11 3RSZ    1       JRNL                                     
REVDAT   2   17-AUG-11 3RSZ    1       AUTHOR                                   
REVDAT   1   10-AUG-11 3RSZ    0                                                
JRNL        AUTH   S.BASKARAN,V.M.CHIKWANA,C.J.CONTRERAS,K.D.DAVIS,W.A.WILSON,  
JRNL        AUTH 2 A.A.DEPAOLI-ROACH,P.J.ROACH,T.D.HURLEY                       
JRNL        TITL   MULTIPLE GLYCOGEN-BINDING SITES IN EUKARYOTIC GLYCOGEN       
JRNL        TITL 2 SYNTHASE ARE REQUIRED FOR HIGH CATALYTIC EFFICIENCY TOWARD   
JRNL        TITL 3 GLYCOGEN.                                                    
JRNL        REF    J.BIOL.CHEM.                  V. 286 33999 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21835915                                                     
JRNL        DOI    10.1074/JBC.M111.264531                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
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) : 3.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.56                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 73079                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3673                            
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 47.5699 -  8.8960    0.95     2617   156  0.2014 0.2453        
REMARK   3     2  8.8960 -  7.0685    1.00     2747   125  0.1624 0.2067        
REMARK   3     3  7.0685 -  6.1771    1.00     2709   150  0.1948 0.2495        
REMARK   3     4  6.1771 -  5.6133    1.00     2718   136  0.2234 0.2816        
REMARK   3     5  5.6133 -  5.2115    1.00     2689   147  0.2040 0.2455        
REMARK   3     6  5.2115 -  4.9046    1.00     2685   153  0.1775 0.2014        
REMARK   3     7  4.9046 -  4.6592    1.00     2702   155  0.1694 0.2011        
REMARK   3     8  4.6592 -  4.4565    1.00     2735   132  0.1686 0.2038        
REMARK   3     9  4.4565 -  4.2851    1.00     2654   160  0.1798 0.2320        
REMARK   3    10  4.2851 -  4.1373    1.00     2710   148  0.1817 0.2193        
REMARK   3    11  4.1373 -  4.0080    1.00     2678   162  0.1953 0.2328        
REMARK   3    12  4.0080 -  3.8935    1.00     2662   158  0.2030 0.2341        
REMARK   3    13  3.8935 -  3.7910    1.00     2687   144  0.2062 0.2235        
REMARK   3    14  3.7910 -  3.6986    1.00     2684   145  0.2134 0.2330        
REMARK   3    15  3.6986 -  3.6145    1.00     2746   136  0.2220 0.2760        
REMARK   3    16  3.6145 -  3.5376    1.00     2672   143  0.2326 0.2368        
REMARK   3    17  3.5376 -  3.4669    1.00     2666   152  0.2455 0.2638        
REMARK   3    18  3.4669 -  3.4015    1.00     2703   147  0.2411 0.2991        
REMARK   3    19  3.4015 -  3.3407    1.00     2661   144  0.2596 0.2582        
REMARK   3    20  3.3407 -  3.2841    1.00     2719   129  0.2592 0.3113        
REMARK   3    21  3.2841 -  3.2312    1.00     2677   123  0.2651 0.2801        
REMARK   3    22  3.2312 -  3.1815    1.00     2722   123  0.2897 0.3329        
REMARK   3    23  3.1815 -  3.1347    1.00     2714   132  0.2838 0.3317        
REMARK   3    24  3.1347 -  3.0905    0.98     2643   134  0.3142 0.3062        
REMARK   3    25  3.0905 -  3.0488    0.97     2601   129  0.3059 0.3539        
REMARK   3    26  3.0488 -  3.0092    0.82     2205   110  0.3440 0.3813        
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              : 0.33                                          
REMARK   3   B_SOL              : 49.46                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.540           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.19120                                              
REMARK   3    B22 (A**2) : 4.18230                                              
REMARK   3    B33 (A**2) : -12.37350                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 4.97990                                              
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      :  0.008          20465                                  
REMARK   3   ANGLE     :  1.152          27731                                  
REMARK   3   CHIRALITY :  0.082           3057                                  
REMARK   3   PLANARITY :  0.004           3539                                  
REMARK   3   DIHEDRAL  : 17.254           7545                                  
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 : 4                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 1:204 or resseq 207:    
REMARK   3                          276 or resseq 284:400 or resseq 413:539 or  
REMARK   3                          resseq 545:638 ) and backbone               
REMARK   3     SELECTION          : chain B and (resseq 1:204 or resseq 207:    
REMARK   3                          276 or resseq 284:400 or resseq 413:539 or  
REMARK   3                          resseq 545:638 ) and backbone               
REMARK   3     ATOM PAIRS NUMBER  : 2424                                        
REMARK   3     RMSD               : 0.031                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain C and (resseq 1:204 or resseq 207:    
REMARK   3                          276 or resseq 284:400 or resseq 413:539 or  
REMARK   3                          resseq 545:638 ) and backbone               
REMARK   3     SELECTION          : chain D and (resseq 1:204 or resseq 207:    
REMARK   3                          276 or resseq 284:400 or resseq 413:539 or  
REMARK   3                          resseq 545:638 ) and backbone               
REMARK   3     ATOM PAIRS NUMBER  : 2432                                        
REMARK   3     RMSD               : 0.032                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 1:204 or resseq 207:    
REMARK   3                          276 or resseq 284:400 or resseq 413:539 or  
REMARK   3                          resseq 545:638 ) and sidechain              
REMARK   3     SELECTION          : chain B and (resseq 1:204 or resseq 207:    
REMARK   3                          276 or resseq 284:400 or resseq 413:539 or  
REMARK   3                          resseq 545:638 ) and sidechain              
REMARK   3     ATOM PAIRS NUMBER  : 2466                                        
REMARK   3     RMSD               : 0.010                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain C and (resseq 1:204 or resseq 207:    
REMARK   3                          276 or resseq 284:400 or resseq 413:539 or  
REMARK   3                          resseq 545:638 ) and sidechain              
REMARK   3     SELECTION          : chain D and (resseq 1:204 or resseq 207:    
REMARK   3                          276 or resseq 284:400 or resseq 413:539 or  
REMARK   3                          resseq 545:638 ) and sidechain              
REMARK   3     ATOM PAIRS NUMBER  : 2470                                        
REMARK   3     RMSD               : 0.011                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3RSZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065338.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 8.0                                
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) : 1.0                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73079                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : 0.07500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.44900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3NAZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3400, 0.1M LITHIUM SULFATE,      
REMARK 280  0.1M TRIS HCL, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE   
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       83.36550            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY FOR THE MAIN POLYMERIC CHAIN IS A    
REMARK 300 TETRAMER                                                             
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17760 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 96430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -224.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D, F, E                      
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     SER A   206                                                      
REMARK 465     PHE A   207                                                      
REMARK 465     ALA A   278                                                      
REMARK 465     PHE A   279                                                      
REMARK 465     HIS A   280                                                      
REMARK 465     GLU A   281                                                      
REMARK 465     PHE A   282                                                      
REMARK 465     GLN A   283                                                      
REMARK 465     ASN A   284                                                      
REMARK 465     HIS A   402                                                      
REMARK 465     ASN A   403                                                      
REMARK 465     GLY A   404                                                      
REMARK 465     LEU A   405                                                      
REMARK 465     THR A   406                                                      
REMARK 465     THR A   407                                                      
REMARK 465     GLU A   408                                                      
REMARK 465     LEU A   409                                                      
REMARK 465     PRO A   410                                                      
REMARK 465     THR A   411                                                      
REMARK 465     ASP A   412                                                      
REMARK 465     LEU A   413                                                      
REMARK 465     GLY A   414                                                      
REMARK 465     ILE A   541                                                      
REMARK 465     GLU A   542                                                      
REMARK 465     THR A   543                                                      
REMARK 465     ASN A   544                                                      
REMARK 465     GLN A   545                                                      
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     SER B   206                                                      
REMARK 465     PHE B   207                                                      
REMARK 465     ALA B   278                                                      
REMARK 465     PHE B   279                                                      
REMARK 465     HIS B   280                                                      
REMARK 465     GLU B   281                                                      
REMARK 465     PHE B   282                                                      
REMARK 465     GLN B   283                                                      
REMARK 465     ASN B   284                                                      
REMARK 465     HIS B   402                                                      
REMARK 465     ASN B   403                                                      
REMARK 465     GLY B   404                                                      
REMARK 465     LEU B   405                                                      
REMARK 465     THR B   406                                                      
REMARK 465     THR B   407                                                      
REMARK 465     GLU B   408                                                      
REMARK 465     LEU B   409                                                      
REMARK 465     PRO B   410                                                      
REMARK 465     THR B   411                                                      
REMARK 465     ASP B   412                                                      
REMARK 465     LEU B   413                                                      
REMARK 465     GLY B   414                                                      
REMARK 465     ILE B   541                                                      
REMARK 465     GLU B   542                                                      
REMARK 465     THR B   543                                                      
REMARK 465     ASN B   544                                                      
REMARK 465     GLN B   545                                                      
REMARK 465     GLY B   640                                                      
REMARK 465     GLY B   641                                                      
REMARK 465     LYS B   642                                                      
REMARK 465     LYS B   643                                                      
REMARK 465     LEU B   644                                                      
REMARK 465     LYS B   645                                                      
REMARK 465     VAL B   646                                                      
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     SER C   206                                                      
REMARK 465     PHE C   207                                                      
REMARK 465     ALA C   278                                                      
REMARK 465     PHE C   279                                                      
REMARK 465     HIS C   280                                                      
REMARK 465     GLU C   281                                                      
REMARK 465     PHE C   282                                                      
REMARK 465     GLN C   283                                                      
REMARK 465     HIS C   402                                                      
REMARK 465     ASN C   403                                                      
REMARK 465     GLY C   404                                                      
REMARK 465     LEU C   405                                                      
REMARK 465     THR C   406                                                      
REMARK 465     THR C   407                                                      
REMARK 465     GLU C   408                                                      
REMARK 465     LEU C   409                                                      
REMARK 465     PRO C   410                                                      
REMARK 465     THR C   411                                                      
REMARK 465     ASP C   412                                                      
REMARK 465     LEU C   413                                                      
REMARK 465     ILE C   541                                                      
REMARK 465     GLU C   542                                                      
REMARK 465     THR C   543                                                      
REMARK 465     ASN C   544                                                      
REMARK 465     GLN C   545                                                      
REMARK 465     GLY C   640                                                      
REMARK 465     GLY C   641                                                      
REMARK 465     LYS C   642                                                      
REMARK 465     LYS C   643                                                      
REMARK 465     LEU C   644                                                      
REMARK 465     LYS C   645                                                      
REMARK 465     VAL C   646                                                      
REMARK 465     ALA C   647                                                      
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     ALA D   278                                                      
REMARK 465     PHE D   279                                                      
REMARK 465     HIS D   280                                                      
REMARK 465     GLU D   281                                                      
REMARK 465     PHE D   282                                                      
REMARK 465     GLN D   283                                                      
REMARK 465     HIS D   402                                                      
REMARK 465     ASN D   403                                                      
REMARK 465     GLY D   404                                                      
REMARK 465     LEU D   405                                                      
REMARK 465     THR D   406                                                      
REMARK 465     THR D   407                                                      
REMARK 465     GLU D   408                                                      
REMARK 465     LEU D   409                                                      
REMARK 465     PRO D   410                                                      
REMARK 465     THR D   411                                                      
REMARK 465     ASP D   412                                                      
REMARK 465     LEU D   413                                                      
REMARK 465     ILE D   541                                                      
REMARK 465     GLU D   542                                                      
REMARK 465     THR D   543                                                      
REMARK 465     ASN D   544                                                      
REMARK 465     GLN D   545                                                      
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 465     UNK E     5                                                      
REMARK 465     UNK E     6                                                      
REMARK 465     UNK E     7                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     UNK E    4   O                                                   
REMARK 480     UNK F    5   O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    PHE B   307     NH2  ARG D   399              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A   7       79.54   -115.12                                   
REMARK 500    THR A  15       -8.33    -56.13                                   
REMARK 500    ARG A  20       95.66    -67.62                                   
REMARK 500    LYS A  40     -116.95     35.96                                   
REMARK 500    ALA A  68       -8.53    -57.42                                   
REMARK 500    TYR A 114        5.48    -46.85                                   
REMARK 500    SER A 115      -72.06    -50.39                                   
REMARK 500    VAL A 126       12.76   -155.22                                   
REMARK 500    SER A 130       78.52   -168.41                                   
REMARK 500    GLU A 169      151.65     77.74                                   
REMARK 500    ARG A 183       36.04     34.91                                   
REMARK 500    ALA A 194      168.14    160.03                                   
REMARK 500    SER A 204      -88.87   -103.59                                   
REMARK 500    PHE A 209      -87.36   -142.34                                   
REMARK 500    TYR A 210       -9.31    -48.97                                   
REMARK 500    ASN A 211      -65.16    -99.64                                   
REMARK 500    SER A 215       19.79   -144.51                                   
REMARK 500    PHE A 276      -64.52   -103.59                                   
REMARK 500    CYS A 304       59.29   -150.73                                   
REMARK 500    ARG A 341      -38.42    -38.01                                   
REMARK 500    SER A 363     -169.38     68.72                                   
REMARK 500    PRO A 435      130.52    -31.38                                   
REMARK 500    VAL A 448       48.49    -91.19                                   
REMARK 500    ASP A 449       59.32    149.88                                   
REMARK 500    ILE A 487      -72.91    -90.61                                   
REMARK 500    TRP A 511      -68.40   -124.36                                   
REMARK 500    THR A 527     -159.57   -119.79                                   
REMARK 500    ASP A 539       61.54   -109.51                                   
REMARK 500    LYS A 578      121.75    -17.36                                   
REMARK 500    GLU A 628     -175.59    167.38                                   
REMARK 500    ASN B   7       78.30   -114.70                                   
REMARK 500    THR B  15       -7.14    -57.44                                   
REMARK 500    ARG B  20       96.91    -68.01                                   
REMARK 500    LYS B  40     -116.81     37.85                                   
REMARK 500    ALA B  68       -7.29    -58.25                                   
REMARK 500    TYR B 114        7.47    -47.79                                   
REMARK 500    SER B 115      -72.36    -51.87                                   
REMARK 500    VAL B 126       14.08   -156.51                                   
REMARK 500    SER B 130       77.83   -168.79                                   
REMARK 500    GLU B 169      150.96     77.98                                   
REMARK 500    ARG B 183       37.16     35.60                                   
REMARK 500    ALA B 194      168.15    159.82                                   
REMARK 500    SER B 204      -82.25   -102.99                                   
REMARK 500    PHE B 209      -87.44   -141.82                                   
REMARK 500    TYR B 210       -9.74    -48.24                                   
REMARK 500    ASN B 211      -65.80    -99.59                                   
REMARK 500    SER B 215       19.06   -145.77                                   
REMARK 500    CYS B 304       62.56   -151.80                                   
REMARK 500    TYR B 340      -71.58    -55.41                                   
REMARK 500    ARG B 341      -38.35    -35.80                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     123 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU C 285        22.7      L          L   OUTSIDE RANGE           
REMARK 500    LEU D 285        22.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 908                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 908                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 804                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3NAZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NCH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3O3C   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AUTHORS SEQUENCE MATCHES WITH GENBANK ENTRY CODE AAA88716. SEE       
REMARK 999 SEQADV REMARK                                                        
DBREF  3RSZ A    1   705  UNP    P27472   GYS2_YEAST       1    705             
DBREF  3RSZ B    1   705  UNP    P27472   GYS2_YEAST       1    705             
DBREF  3RSZ C    1   705  UNP    P27472   GYS2_YEAST       1    705             
DBREF  3RSZ D    1   705  UNP    P27472   GYS2_YEAST       1    705             
DBREF  3RSZ E    3     7  PDB    3RSZ     3RSZ             3      7             
DBREF  3RSZ F    1     5  PDB    3RSZ     3RSZ             1      5             
SEQADV 3RSZ MET A  -19  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ GLY A  -18  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER A  -17  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER A  -16  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS A  -15  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS A  -14  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS A  -13  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS A  -12  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS A  -11  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS A  -10  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER A   -9  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER A   -8  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ GLY A   -7  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ LEU A   -6  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ VAL A   -5  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ PRO A   -4  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ ARG A   -3  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ GLY A   -2  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER A   -1  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS A    0  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER A  535  UNP  P27472    ALA   535 SEE REMARK 999                 
SEQADV 3RSZ ALA A  580  UNP  P27472    ARG   580 ENGINEERED MUTATION            
SEQADV 3RSZ ALA A  581  UNP  P27472    ARG   581 ENGINEERED MUTATION            
SEQADV 3RSZ ALA A  583  UNP  P27472    ARG   583 ENGINEERED MUTATION            
SEQADV 3RSZ MET B  -19  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ GLY B  -18  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER B  -17  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER B  -16  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS B  -15  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS B  -14  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS B  -13  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS B  -12  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS B  -11  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS B  -10  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER B   -9  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER B   -8  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ GLY B   -7  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ LEU B   -6  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ VAL B   -5  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ PRO B   -4  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ ARG B   -3  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ GLY B   -2  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER B   -1  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS B    0  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER B  535  UNP  P27472    ALA   535 SEE REMARK 999                 
SEQADV 3RSZ ALA B  580  UNP  P27472    ARG   580 ENGINEERED MUTATION            
SEQADV 3RSZ ALA B  581  UNP  P27472    ARG   581 ENGINEERED MUTATION            
SEQADV 3RSZ ALA B  583  UNP  P27472    ARG   583 ENGINEERED MUTATION            
SEQADV 3RSZ MET C  -19  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ GLY C  -18  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER C  -17  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER C  -16  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS C  -15  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS C  -14  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS C  -13  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS C  -12  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS C  -11  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS C  -10  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER C   -9  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER C   -8  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ GLY C   -7  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ LEU C   -6  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ VAL C   -5  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ PRO C   -4  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ ARG C   -3  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ GLY C   -2  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER C   -1  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS C    0  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER C  535  UNP  P27472    ALA   535 SEE REMARK 999                 
SEQADV 3RSZ ALA C  580  UNP  P27472    ARG   580 ENGINEERED MUTATION            
SEQADV 3RSZ ALA C  581  UNP  P27472    ARG   581 ENGINEERED MUTATION            
SEQADV 3RSZ ALA C  583  UNP  P27472    ARG   583 ENGINEERED MUTATION            
SEQADV 3RSZ MET D  -19  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ GLY D  -18  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER D  -17  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER D  -16  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS D  -15  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS D  -14  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS D  -13  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS D  -12  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS D  -11  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS D  -10  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER D   -9  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER D   -8  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ GLY D   -7  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ LEU D   -6  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ VAL D   -5  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ PRO D   -4  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ ARG D   -3  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ GLY D   -2  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER D   -1  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ HIS D    0  UNP  P27472              EXPRESSION TAG                 
SEQADV 3RSZ SER D  535  UNP  P27472    ALA   535 SEE REMARK 999                 
SEQADV 3RSZ ALA D  580  UNP  P27472    ARG   580 ENGINEERED MUTATION            
SEQADV 3RSZ ALA D  581  UNP  P27472    ARG   581 ENGINEERED MUTATION            
SEQADV 3RSZ ALA D  583  UNP  P27472    ARG   583 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 ALA ALA GLN ALA ILE ASN GLN ARG ASN ARG THR GLU          
SEQRES  48 A  725  ARG 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 ALA ALA GLN ALA ILE ASN GLN ARG ASN ARG THR GLU          
SEQRES  48 B  725  ARG 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 ALA ALA GLN ALA ILE ASN GLN ARG ASN ARG THR GLU          
SEQRES  48 C  725  ARG 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 ALA ALA GLN ALA ILE ASN GLN ARG ASN ARG THR GLU          
SEQRES  48 D  725  ARG 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                      
SEQRES   1 E    5  UNK UNK UNK UNK UNK                                          
SEQRES   1 F    5  UNK UNK UNK UNK UNK                                          
HET    SO4  A 801       5                                                       
HET    SO4  A 802       5                                                       
HET    SO4  D 803       5                                                       
HET    SO4  A 804       5                                                       
HET    GLC  A 901      11                                                       
HET    GLC  A 902      11                                                       
HET    GLC  A 903      11                                                       
HET    GLC  A 904      12                                                       
HET    GLC  A 905      11                                                       
HET    GLC  A 906      11                                                       
HET    GLC  A 907      11                                                       
HET    GLC  A 908      12                                                       
HET    SO4  B 801       5                                                       
HET    SO4  B 802       5                                                       
HET    SO4  B 706       5                                                       
HET    SO4  C 803       5                                                       
HET    SO4  C 706       5                                                       
HET    SO4  B 804       5                                                       
HET    GLC  B 901      11                                                       
HET    GLC  B 902      11                                                       
HET    GLC  B 903      11                                                       
HET    GLC  B 904      12                                                       
HET    GLC  B 905      11                                                       
HET    GLC  B 906      11                                                       
HET    GLC  B 907      11                                                       
HET    GLC  B 908      12                                                       
HET    SO4  C 801       5                                                       
HET    SO4  C 804       5                                                       
HET    SO4  D 801       5                                                       
HET    SO4  D 802       5                                                       
HET    SO4  A 803       5                                                       
HET    SO4  D 804       5                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
FORMUL   7  SO4    16(O4 S 2-)                                                  
FORMUL  11  GLC    16(C6 H12 O6)                                                
HELIX    1   1 GLY A   23  LYS A   40  1                                  18    
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  ARG A   86  1                                  14    
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 ASN A  211  VAL A  216  5                                   6    
HELIX   12  12 ASP A  217  PHE A  225  1                                   9    
HELIX   13  13 ILE A  227  ALA A  241  1                                  15    
HELIX   14  14 SER A  248  LEU A  259  1                                  12    
HELIX   15  15 ASN A  272  PHE A  276  5                                   5    
HELIX   16  16 LEU A  285  PHE A  301  1                                  17    
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 LYS A  418  ALA A  431  1                                  14    
HELIX   21  21 ASP A  453  VAL A  462  1                                  10    
HELIX   22  22 ASP A  491  CYS A  499  1                                   9    
HELIX   23  23 GLY A  512  MET A  521  1                                  10    
HELIX   24  24 SER A  531  GLU A  538  1                                   8    
HELIX   25  25 ALA A  546  TYR A  549  5                                   4    
HELIX   26  26 ALA A  560  LYS A  578  1                                  19    
HELIX   27  27 THR A  579  SER A  594  1                                  16    
HELIX   28  28 ASP A  595  LEU A  597  5                                   3    
HELIX   29  29 ASP A  598  GLY A  603  1                                   6    
HELIX   30  30 GLY A  603  TYR A  618  1                                  16    
HELIX   31  31 TYR A  618  GLY A  627  1                                  10    
HELIX   32  32 ASN A  634  ALA A  639  1                                   6    
HELIX   33  33 GLY B   23  LYS B   40  1                                  18    
HELIX   34  34 THR B   53  GLU B   57  1                                   5    
HELIX   35  35 LYS B   65  PHE B   69  5                                   5    
HELIX   36  36 MET B   73  ARG B   86  1                                  14    
HELIX   37  37 LEU B  108  GLY B  113  5                                   6    
HELIX   38  38 TYR B  114  GLY B  127  1                                  14    
HELIX   39  39 ASP B  134  ASP B  158  1                                  25    
HELIX   40  40 TRP B  170  GLY B  173  5                                   4    
HELIX   41  41 VAL B  174  ARG B  182  1                                   9    
HELIX   42  42 THR B  195  CYS B  202  1                                   8    
HELIX   43  43 ASN B  211  VAL B  216  5                                   6    
HELIX   44  44 ASP B  217  PHE B  225  1                                   9    
HELIX   45  45 ILE B  227  ALA B  241  1                                  15    
HELIX   46  46 SER B  248  LEU B  259  1                                  12    
HELIX   47  47 ASN B  272  PHE B  276  5                                   5    
HELIX   48  48 LEU B  285  PHE B  301  1                                  17    
HELIX   49  49 ASP B  308  ASP B  310  5                                   3    
HELIX   50  50 GLY B  327  SER B  345  1                                  19    
HELIX   51  51 THR B  365  TYR B  400  1                                  36    
HELIX   52  52 LYS B  418  ALA B  431  1                                  14    
HELIX   53  53 ASP B  453  VAL B  462  1                                  10    
HELIX   54  54 ASP B  491  CYS B  499  1                                   9    
HELIX   55  55 GLY B  512  MET B  521  1                                  10    
HELIX   56  56 SER B  531  GLU B  538  1                                   8    
HELIX   57  57 ALA B  546  TYR B  549  5                                   4    
HELIX   58  58 ALA B  560  LYS B  578  1                                  19    
HELIX   59  59 THR B  579  SER B  594  1                                  16    
HELIX   60  60 ASP B  595  LEU B  597  5                                   3    
HELIX   61  61 ASP B  598  GLY B  603  1                                   6    
HELIX   62  62 GLY B  603  TYR B  618  1                                  16    
HELIX   63  63 TYR B  618  GLY B  627  1                                  10    
HELIX   64  64 ASN B  634  ALA B  639  1                                   6    
HELIX   65  65 GLY C   23  LYS C   31  1                                   9    
HELIX   66  66 LYS C   31  LYS C   40  1                                  10    
HELIX   67  67 THR C   53  GLU C   57  1                                   5    
HELIX   68  68 LYS C   65  PHE C   69  5                                   5    
HELIX   69  69 SER C   70  GLU C   72  5                                   3    
HELIX   70  70 MET C   73  ARG C   86  1                                  14    
HELIX   71  71 LEU C  108  GLY C  113  5                                   6    
HELIX   72  72 TYR C  114  GLY C  127  1                                  14    
HELIX   73  73 ASP C  134  ASP C  158  1                                  25    
HELIX   74  74 TRP C  170  GLY C  173  5                                   4    
HELIX   75  75 VAL C  174  ARG C  182  1                                   9    
HELIX   76  76 THR C  195  CYS C  202  1                                   8    
HELIX   77  77 ASP C  217  GLY C  226  1                                  10    
HELIX   78  78 ILE C  227  ALA C  241  1                                  15    
HELIX   79  79 SER C  248  LEU C  259  1                                  12    
HELIX   80  80 ASN C  272  PHE C  276  5                                   5    
HELIX   81  81 LEU C  285  PHE C  301  1                                  17    
HELIX   82  82 ASP C  308  ASP C  310  5                                   3    
HELIX   83  83 GLY C  327  SER C  345  1                                  19    
HELIX   84  84 THR C  365  TYR C  400  1                                  36    
HELIX   85  85 LYS C  418  ALA C  431  1                                  14    
HELIX   86  86 ASP C  453  VAL C  462  1                                  10    
HELIX   87  87 ASP C  491  CYS C  499  1                                   9    
HELIX   88  88 GLY C  512  MET C  521  1                                  10    
HELIX   89  89 SER C  531  ASP C  539  1                                   9    
HELIX   90  90 LEU C  540  LEU C  540  5                                   1    
HELIX   91  91 ALA C  546  TYR C  549  5                                   4    
HELIX   92  92 ALA C  560  LYS C  578  1                                  19    
HELIX   93  93 THR C  579  SER C  594  1                                  16    
HELIX   94  94 ASP C  595  LEU C  597  5                                   3    
HELIX   95  95 ASP C  598  TYR C  618  1                                  21    
HELIX   96  96 TYR C  618  GLY C  627  1                                  10    
HELIX   97  97 ASN C  634  ALA C  639  1                                   6    
HELIX   98  98 GLY D   23  LYS D   31  1                                   9    
HELIX   99  99 LYS D   31  LYS D   40  1                                  10    
HELIX  100 100 THR D   53  GLU D   57  1                                   5    
HELIX  101 101 LYS D   65  PHE D   69  5                                   5    
HELIX  102 102 MET D   73  ARG D   86  1                                  14    
HELIX  103 103 LEU D  108  GLY D  113  5                                   6    
HELIX  104 104 TYR D  114  GLY D  127  1                                  14    
HELIX  105 105 ASP D  134  ASP D  158  1                                  25    
HELIX  106 106 TRP D  170  GLY D  173  5                                   4    
HELIX  107 107 VAL D  174  ARG D  182  1                                   9    
HELIX  108 108 THR D  195  CYS D  202  1                                   8    
HELIX  109 109 ASP D  217  GLY D  226  1                                  10    
HELIX  110 110 ILE D  227  ALA D  241  1                                  15    
HELIX  111 111 SER D  248  LEU D  259  1                                  12    
HELIX  112 112 ASN D  272  PHE D  276  5                                   5    
HELIX  113 113 LEU D  285  PHE D  301  1                                  17    
HELIX  114 114 ASP D  308  ASP D  310  5                                   3    
HELIX  115 115 GLY D  327  SER D  345  1                                  19    
HELIX  116 116 THR D  365  TYR D  400  1                                  36    
HELIX  117 117 LYS D  418  ALA D  431  1                                  14    
HELIX  118 118 ASP D  453  VAL D  462  1                                  10    
HELIX  119 119 ASP D  491  CYS D  499  1                                   9    
HELIX  120 120 GLY D  512  MET D  521  1                                  10    
HELIX  121 121 SER D  531  ASP D  539  1                                   9    
HELIX  122 122 LEU D  540  LEU D  540  5                                   1    
HELIX  123 123 ALA D  546  TYR D  549  5                                   4    
HELIX  124 124 ALA D  560  LYS D  578  1                                  19    
HELIX  125 125 THR D  579  SER D  594  1                                  16    
HELIX  126 126 ASP D  595  LEU D  597  5                                   3    
HELIX  127 127 ASP D  598  TYR D  618  1                                  21    
HELIX  128 128 TYR D  618  GLY D  627  1                                  10    
HELIX  129 129 ASN D  634  ALA D  639  1                                   6    
HELIX  130 130 UNK F    1  UNK F    5  5                                   5    
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  THR A  13  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 186  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  LEU A 313   O  THR A 350           
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  SER A 363           
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  VAL B 103   N  GLY B  93           
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  HIS B  44           
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 186  THR B 192  1  O  ILE B 189   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  LEU B 313   O  THR B 350           
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  SER B 363           
SHEET    1   G 8 VAL C  58  ILE C  60  0                                        
SHEET    2   G 8 PHE C  90  TRP C  95 -1  O  ARG C  94   N  ASP C  59           
SHEET    3   G 8 LYS C 102  PHE C 106 -1  O  VAL C 103   N  GLY C  93           
SHEET    4   G 8 TYR C  43  PRO C  48  1  N  LEU C  45   O  ILE C 104           
SHEET    5   G 8 ASP C   4  THR C  13  1  N  GLU C  12   O  ILE C  46           
SHEET    6   G 8 HIS C 161  HIS C 168  1  O  HIS C 166   N  THR C  13           
SHEET    7   G 8 VAL C 187  THR C 192  1  O  VAL C 187   N  ALA C 165           
SHEET    8   G 8 VAL C 243  THR C 246  1  O  VAL C 243   N  PHE C 190           
SHEET    1   H 6 VAL C 472  PHE C 476  0                                        
SHEET    2   H 6 THR C 350  VAL C 356  1  N  ALA C 353   O  ILE C 475           
SHEET    3   H 6 THR C 312  ALA C 318  1  N  PHE C 315   O  PHE C 354           
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 8 VAL D  58  ILE D  60  0                                        
SHEET    2   J 8 PHE D  90  TRP D  95 -1  O  ARG D  94   N  ASP D  59           
SHEET    3   J 8 LYS D 102  PHE D 106 -1  O  VAL D 103   N  GLY D  93           
SHEET    4   J 8 TYR D  43  PRO D  48  1  N  GLY D  47   O  PHE D 106           
SHEET    5   J 8 ASP D   4  THR D  13  1  N  GLU D  12   O  ILE D  46           
SHEET    6   J 8 HIS D 161  HIS D 168  1  O  HIS D 166   N  THR D  13           
SHEET    7   J 8 VAL D 187  THR D 192  1  O  VAL D 187   N  ALA D 165           
SHEET    8   J 8 VAL D 243  THR D 246  1  O  VAL D 243   N  PHE D 190           
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  PHE D 315   O  PHE D 354           
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  TYR D 552   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           
LINK         C1  GLC B 903                 O4  GLC B 904     1555   1555  1.42  
LINK         C1  GLC A 903                 O4  GLC A 904     1555   1555  1.43  
LINK         C1  GLC A 906                 O4  GLC A 907     1555   1555  1.44  
LINK         C1  GLC B 906                 O4  GLC B 907     1555   1555  1.45  
LINK         C1  GLC A 907                 O4  GLC A 908     1555   1555  1.45  
LINK         C1  GLC B 905                 O4  GLC B 906     1555   1555  1.46  
LINK         C1  GLC B 902                 O4  GLC B 903     1555   1555  1.46  
LINK         C1  GLC B 907                 O4  GLC B 908     1555   1555  1.46  
LINK         C1  GLC B 901                 O4  GLC B 902     1555   1555  1.46  
LINK         C1  GLC A 905                 O4  GLC A 906     1555   1555  1.47  
LINK         C1  GLC A 902                 O4  GLC A 903     1555   1555  1.47  
LINK         C1  GLC A 901                 O4  GLC A 902     1555   1555  1.50  
CISPEP   1 TYR A  400    PRO A  401          0        -3.30                     
CISPEP   2 TYR B  400    PRO B  401          0         0.05                     
CISPEP   3 TYR C  400    PRO C  401          0        -1.83                     
CISPEP   4 TYR D  400    PRO D  401          0        -5.06                     
SITE     1 AC1  4 ARG A  20  SER A  26  LYS A  29  LYS A 275                    
SITE     1 AC2  3 ARG A 320  GLY A 512  TYR A 513                               
SITE     1 AC3  3 ARG A  20  ARG D 427  ARG D 428                               
SITE     1 AC4  3 GLN A 582  ASN A 585  ARG A 589                               
SITE     1 AC5  3 HIS A 156  ARG A 182  GLC A 902                               
SITE     1 AC6  4 GLY A 152  GLU A 153  GLC A 901  GLC A 903                    
SITE     1 AC7  6 ARG A  86  ALA A 148  GLY A 152  ARG A 182                    
SITE     2 AC7  6 GLC A 902  GLC A 904                                          
SITE     1 AC8  4 GLU A 117  TRP A 118  ASP A 121  GLC A 903                    
SITE     1 AC9  3 GLY A 437  LEU A 439  GLC A 906                               
SITE     1 BC1  4 LEU A 439  PHE A 465  GLC A 905  GLC A 907                    
SITE     1 BC2  7 PRO A 441  ILE A 442  VAL A 443  ASP A 450                    
SITE     2 BC2  7 ARG A 460  GLC A 906  GLC A 908                               
SITE     1 BC3  8 THR A 365  GLU A 367  VAL A 443  HIS A 445                    
SITE     2 BC3  8 ASN A 446  MET A 447  ASP A 450  GLC A 907                    
SITE     1 BC4  3 ARG B  20  SER B  26  LYS B  29                               
SITE     1 BC5  4 ARG B 320  LYS B 326  GLY B 512  TYR B 513                    
SITE     1 BC6  3 ARG B 427  ARG B 428  ARG C  20                               
SITE     1 BC7  3 ARG B  20  ARG C 427  ARG C 428                               
SITE     1 BC8  4 ARG C 199  ARG C 320  LYS C 326  GLY C 512                    
SITE     1 BC9  3 GLN B 582  ASN B 585  ARG B 589                               
SITE     1 CC1  2 HIS B 156  GLC B 902                                          
SITE     1 CC2  4 GLY B 152  GLU B 153  GLC B 901  GLC B 903                    
SITE     1 CC3  7 ARG B  86  ALA B 148  TRP B 149  GLY B 152                    
SITE     2 CC3  7 ARG B 182  GLC B 902  GLC B 904                               
SITE     1 CC4  4 GLU B 117  TRP B 118  ASP B 121  GLC B 903                    
SITE     1 CC5  1 GLC B 906                                                     
SITE     1 CC6  4 LEU B 439  PHE B 465  GLC B 905  GLC B 907                    
SITE     1 CC7  6 PRO B 441  ILE B 442  ASP B 450  ARG B 460                    
SITE     2 CC7  6 GLC B 906  GLC B 908                                          
SITE     1 CC8  7 GLU B 367  VAL B 443  HIS B 445  ASN B 446                    
SITE     2 CC8  7 MET B 447  ASP B 450  GLC B 907                               
SITE     1 CC9  4 ARG C  20  SER C  26  LYS C  29  LYS C 275                    
SITE     1 DC1  2 ASN C 585  ARG C 589                                          
SITE     1 DC2  5 ARG D 320  LYS D 326  GLY D 512  TYR D 513                    
SITE     2 DC2  5 THR D 514                                                     
SITE     1 DC3  4 ARG D  20  SER D  26  LYS D  29  LYS D 275                    
SITE     1 DC4  3 ARG A 427  ARG A 428  ARG D  20                               
SITE     1 DC5  3 GLN D 582  ASN D 585  ARG D 589                               
CRYST1   96.557  166.731  121.136  90.00 103.25  90.00 P 1 21 1      8          
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      0.010357  0.000000  0.002439        0.00000                         
SCALE2      0.000000  0.005998  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008481        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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