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Database: PDB
Entry: 5HG1
LinkDB: 5HG1
Original site: 5HG1 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       07-JAN-16   5HG1              
TITLE     CRYSTAL STRUCTURE OF HUMAN HEXOKINASE 2 WITH CMPD 1, A C-2-SUBSTITUTED
TITLE    2 GLUCOSAMINE                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEXOKINASE-2;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HEXOKINASE TYPE II,HK II,MUSCLE FORM HEXOKINASE;            
COMPND   5 EC: 2.7.1.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HK2;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    METABOLISM, INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.CAMPOBASSO,B.ZHAO,A.SMALLWOOD                                       
REVDAT   2   29-JUL-20 5HG1    1       COMPND REMARK HETNAM SITE                
REVDAT   1   30-MAR-16 5HG1    0                                                
JRNL        AUTH   H.LIN,J.ZENG,R.XIE,M.J.SCHULZ,R.TEDESCO,J.QU,K.F.ERHARD,     
JRNL        AUTH 2 J.F.MACK,K.RAHA,A.R.RENDINA,L.M.SZEWCZUK,P.M.KRATZ,          
JRNL        AUTH 3 A.J.JUREWICZ,T.CECCONIE,S.MARTENS,P.J.MCDEVITT,J.D.MARTIN,   
JRNL        AUTH 4 S.B.CHEN,Y.JIANG,L.NICKELS,B.J.SCHWARTZ,A.SMALLWOOD,B.ZHAO,  
JRNL        AUTH 5 N.CAMPOBASSO,Y.QIAN,J.BRIAND,C.M.ROMINGER,C.OLEYKOWSKI,      
JRNL        AUTH 6 M.A.HARDWICKE,J.I.LUENGO                                     
JRNL        TITL   DISCOVERY OF A NOVEL 2,6-DISUBSTITUTED GLUCOSAMINE SERIES OF 
JRNL        TITL 2 POTENT AND SELECTIVE HEXOKINASE 2 INHIBITORS.                
JRNL        REF    ACS MED.CHEM.LETT.            V.   7   217 2016              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   26985301                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.5B00214                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.76 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.76                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 51597                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2476                            
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 71.5231 -  7.2189    0.99     2862   153  0.1910 0.2279        
REMARK   3     2  7.2189 -  5.7306    1.00     2803   122  0.2239 0.2603        
REMARK   3     3  5.7306 -  5.0065    1.00     2791   126  0.1967 0.2068        
REMARK   3     4  5.0065 -  4.5488    1.00     2756   125  0.1699 0.2281        
REMARK   3     5  4.5488 -  4.2228    1.00     2720   149  0.1763 0.2159        
REMARK   3     6  4.2228 -  3.9739    1.00     2738   133  0.1936 0.2690        
REMARK   3     7  3.9739 -  3.7749    1.00     2704   152  0.2129 0.2931        
REMARK   3     8  3.7749 -  3.6105    1.00     2731   138  0.2203 0.2504        
REMARK   3     9  3.6105 -  3.4715    1.00     2720   123  0.2269 0.2635        
REMARK   3    10  3.4715 -  3.3518    1.00     2707   149  0.2408 0.3070        
REMARK   3    11  3.3518 -  3.2470    1.00     2700   138  0.2581 0.3334        
REMARK   3    12  3.2470 -  3.1541    1.00     2685   159  0.2801 0.3240        
REMARK   3    13  3.1541 -  3.0711    1.00     2681   171  0.2800 0.3174        
REMARK   3    14  3.0711 -  2.9962    1.00     2705   134  0.2875 0.3318        
REMARK   3    15  2.9962 -  2.9281    1.00     2740   100  0.2895 0.3719        
REMARK   3    16  2.9281 -  2.8657    1.00     2705   130  0.2922 0.3908        
REMARK   3    17  2.8657 -  2.8084    1.00     2661   134  0.3096 0.3385        
REMARK   3    18  2.8084 -  2.7554    1.00     2712   140  0.3338 0.3849        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.820           
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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           6701                                  
REMARK   3   ANGLE     :  1.234           9041                                  
REMARK   3   CHIRALITY :  0.069           1043                                  
REMARK   3   PLANARITY :  0.009           1173                                  
REMARK   3   DIHEDRAL  : 10.852           5455                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5HG1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000216979.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5 - 6                              
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51701                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.760                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 126.480                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.20                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 6.6 MGS/ML, 10MM TRIS HCL,      
REMARK 280  PH=8, 0.1 M NACL, 1MM DTT, 20MM MGCL2 WELL: 0.2 M NA CITRATE PH     
REMARK 280  5.5, 14-24 % PEG3350, 20 % ETHYLENE GLYCOL, VAPOR DIFFUSION,        
REMARK 280  TEMPERATURE 296K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.15933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       84.31867            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       84.31867            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       42.15933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 820 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 36140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     TYR A    12                                                      
REMARK 465     PHE A    13                                                      
REMARK 465     GLN A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     ALA A   113                                                      
REMARK 465     ILE A   114                                                      
REMARK 465     PRO A   115                                                      
REMARK 465     GLU A   116                                                      
REMARK 465     ASP A   117                                                      
REMARK 465     ILE A   118                                                      
REMARK 465     MET A   119                                                      
REMARK 465     ARG A   120                                                      
REMARK 465     GLY A   121                                                      
REMARK 465     SER A   122                                                      
REMARK 465     TRP A   171                                                      
REMARK 465     THR A   172                                                      
REMARK 465     LYS A   173                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     PHE A   175                                                      
REMARK 465     LYS A   176                                                      
REMARK 465     SER A   177                                                      
REMARK 465     SER A   178                                                      
REMARK 465     GLY A   179                                                      
REMARK 465     VAL A   180                                                      
REMARK 465     GLU A   181                                                      
REMARK 465     ARG A   195                                                      
REMARK 465     ARG A   196                                                      
REMARK 465     GLY A   197                                                      
REMARK 465     ASP A   198                                                      
REMARK 465     PHE A   199                                                      
REMARK 465     ASP A   200                                                      
REMARK 465     LYS A   549                                                      
REMARK 465     TRP A   550                                                      
REMARK 465     GLY A   551                                                      
REMARK 465     ALA A   914                                                      
REMARK 465     GLY A   915                                                      
REMARK 465     GLN A   916                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  20    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  41    CD   CE   NZ                                        
REMARK 470     LYS A  45    CD   CE   NZ                                        
REMARK 470     GLU A  79    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  89    CG   OD1  ND2                                       
REMARK 470     PHE A  90    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A  91    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A  93    CG   CD1  CD2                                       
REMARK 470     LYS A  96    CD   CE   NZ                                        
REMARK 470     ASP A  99    CG   OD1  OD2                                       
REMARK 470     ASN A 100    CB   CG   OD1  ND2                                  
REMARK 470     LEU A 102    CG   CD1  CD2                                       
REMARK 470     LYS A 104    CG   CD   CE   NZ                                   
REMARK 470     VAL A 105    CG1  CG2                                            
REMARK 470     GLU A 106    CG   CD   OE1  OE2                                  
REMARK 470     MET A 107    CG   SD   CE                                        
REMARK 470     GLU A 108    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 110    CD   OE1  NE2                                       
REMARK 470     HIS A 129    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 132    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 136    CG   OD1  ND2                                       
REMARK 470     MET A 138    CG   SD   CE                                        
REMARK 470     ASP A 139    CG   OD1  OD2                                       
REMARK 470     LYS A 140    CG   CD   CE   NZ                                   
REMARK 470     LEU A 141    CD1  CD2                                            
REMARK 470     GLN A 142    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 144    CG   CD   CE   NZ                                   
REMARK 470     ASP A 145    CG   OD1  OD2                                       
REMARK 470     LYS A 146    CD   CE   NZ                                        
REMARK 470     LYS A 147    CG   CD   CE   NZ                                   
REMARK 470     SER A 155    OG                                                  
REMARK 470     PHE A 156    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE A 167    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 168    CG   CD1  CD2                                       
REMARK 470     VAL A 169    CG1  CG2                                            
REMARK 470     SER A 170    OG                                                  
REMARK 470     ARG A 183    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 188    CG   CD1  CD2                                       
REMARK 470     ILE A 189    CG1  CG2  CD1                                       
REMARK 470     ILE A 193    CG1  CG2  CD1                                       
REMARK 470     ILE A 201    CG1  CG2  CD1                                       
REMARK 470     ASP A 202    CG   OD1  OD2                                       
REMARK 470     GLU A 366    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 404    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 406    CG   CD1  CD2                                       
REMARK 470     GLU A 446    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 447    CG   OD1  OD2                                       
REMARK 470     LYS A 451    CG   CD   CE   NZ                                   
REMARK 470     LYS A 472    CG   CD   CE   NZ                                   
REMARK 470     LYS A 525    CG   CD   CE   NZ                                   
REMARK 470     ARG A 546    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN A 564    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 565    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 592    CB   CG   CD   CE   NZ                              
REMARK 470     SER A 595    OG                                                  
REMARK 470     LYS A 624    CG   CD   CE   NZ                                   
REMARK 470     LEU A 649    CD1  CD2                                            
REMARK 470     GLU A 697    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 700    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 810    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 873    CD   CE   NZ                                        
REMARK 470     LYS A 880    NZ                                                  
REMARK 470     GLU A 894    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 913    CG   CD   OE1  OE2                                  
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   OG   SER A   897     O3   BG6 A  1003              1.27            
REMARK 500   O    THR A   232     OG   SER A   298              2.00            
REMARK 500   O    VAL A   185     N    LEU A   188              2.14            
REMARK 500   OD2  ASP A    33     NH1  ARG A   433              2.14            
REMARK 500   NH1  ARG A    44     OE2  GLU A    48              2.15            
REMARK 500   OD1  ASP A    23     NE   ARG A   373              2.16            
REMARK 500   N    ASP A    73     OE2  GLU A    76              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 251   N   -  CA  -  C   ANGL. DEV. =  18.5 DEGREES          
REMARK 500    PHE A 871   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 140      -71.67    -83.47                                   
REMARK 500    GLU A 165      150.07    170.26                                   
REMARK 500    SER A 166      163.30    175.38                                   
REMARK 500    VAL A 185     -104.25     63.36                                   
REMARK 500    VAL A 186      -38.53    -38.95                                   
REMARK 500    ASP A 251      -54.78   -139.90                                   
REMARK 500    GLU A 252       84.47     63.73                                   
REMARK 500    ILE A 297      -51.85   -133.23                                   
REMARK 500    GLU A 317       -1.17     84.12                                   
REMARK 500    LYS A 346      -70.53    -48.22                                   
REMARK 500    ASP A 362       74.93   -111.83                                   
REMARK 500    THR A 364     -172.12    -64.37                                   
REMARK 500    LYS A 592     -116.45     51.86                                   
REMARK 500    PRO A 605       92.22    -69.51                                   
REMARK 500    LYS A 621     -130.63     58.09                                   
REMARK 500    CYS A 628      -55.64   -127.21                                   
REMARK 500    GLU A 646      -73.71   -114.52                                   
REMARK 500    LEU A 795     -112.50     58.35                                   
REMARK 500    GLU A 894      -23.15     74.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 CYS A  438     ASP A  439                  142.46                    
REMARK 500 LEU A  807     GLY A  808                 -143.36                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    PHE A 782         0.06    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5HEX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HFU   RELATED DB: PDB                                   
DBREF  5HG1 A   17   916  UNP    P52789   HXK2_HUMAN      17    916             
SEQADV 5HG1 MET A   -5  UNP  P52789              INITIATING METHIONINE          
SEQADV 5HG1 GLY A   -4  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 SER A   -3  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 SER A   -2  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 HIS A   -1  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 HIS A    0  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 HIS A    1  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 HIS A    2  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 HIS A    3  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 HIS A    4  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 SER A    5  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 SER A    6  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 GLY A    7  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 LEU A    8  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 GLU A    9  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 ASN A   10  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 LEU A   11  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 TYR A   12  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 PHE A   13  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 GLN A   14  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 GLY A   15  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HG1 SER A   16  UNP  P52789              EXPRESSION TAG                 
SEQRES   1 A  922  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  922  LEU GLU ASN LEU TYR PHE GLN GLY SER ASP GLN VAL GLN          
SEQRES   3 A  922  LYS VAL ASP GLN TYR LEU TYR HIS MET ARG LEU SER ASP          
SEQRES   4 A  922  GLU THR LEU LEU GLU ILE SER LYS ARG PHE ARG LYS GLU          
SEQRES   5 A  922  MET GLU LYS GLY LEU GLY ALA THR THR HIS PRO THR ALA          
SEQRES   6 A  922  ALA VAL LYS MET LEU PRO THR PHE VAL ARG SER THR PRO          
SEQRES   7 A  922  ASP GLY THR GLU HIS GLY GLU PHE LEU ALA LEU ASP LEU          
SEQRES   8 A  922  GLY GLY THR ASN PHE ARG VAL LEU TRP VAL LYS VAL THR          
SEQRES   9 A  922  ASP ASN GLY LEU GLN LYS VAL GLU MET GLU ASN GLN ILE          
SEQRES  10 A  922  TYR ALA ILE PRO GLU ASP ILE MET ARG GLY SER GLY THR          
SEQRES  11 A  922  GLN LEU PHE ASP HIS ILE ALA GLU CYS LEU ALA ASN PHE          
SEQRES  12 A  922  MET ASP LYS LEU GLN ILE LYS ASP LYS LYS LEU PRO LEU          
SEQRES  13 A  922  GLY PHE THR PHE SER PHE PRO CYS HIS GLN THR LYS LEU          
SEQRES  14 A  922  ASP GLU SER PHE LEU VAL SER TRP THR LYS GLY PHE LYS          
SEQRES  15 A  922  SER SER GLY VAL GLU GLY ARG ASP VAL VAL ALA LEU ILE          
SEQRES  16 A  922  ARG LYS ALA ILE GLN ARG ARG GLY ASP PHE ASP ILE ASP          
SEQRES  17 A  922  ILE VAL ALA VAL VAL ASN ASP THR VAL GLY THR MET MET          
SEQRES  18 A  922  THR CYS GLY TYR ASP ASP HIS ASN CYS GLU ILE GLY LEU          
SEQRES  19 A  922  ILE VAL GLY THR GLY SER ASN ALA CYS TYR MET GLU GLU          
SEQRES  20 A  922  MET ARG HIS ILE ASP MET VAL GLU GLY ASP GLU GLY ARG          
SEQRES  21 A  922  MET CYS ILE ASN MET GLU TRP GLY ALA PHE GLY ASP ASP          
SEQRES  22 A  922  GLY SER LEU ASN ASP ILE ARG THR GLU PHE ASP GLN GLU          
SEQRES  23 A  922  ILE ASP MET GLY SER LEU ASN PRO GLY LYS GLN LEU PHE          
SEQRES  24 A  922  GLU LYS MET ILE SER GLY MET TYR MET GLY GLU LEU VAL          
SEQRES  25 A  922  ARG LEU ILE LEU VAL LYS MET ALA LYS GLU GLU LEU LEU          
SEQRES  26 A  922  PHE GLY GLY LYS LEU SER PRO GLU LEU LEU ASN THR GLY          
SEQRES  27 A  922  ARG PHE GLU THR LYS ASP ILE SER ASP ILE GLU GLY GLU          
SEQRES  28 A  922  LYS ASP GLY ILE ARG LYS ALA ARG GLU VAL LEU MET ARG          
SEQRES  29 A  922  LEU GLY LEU ASP PRO THR GLN GLU ASP CYS VAL ALA THR          
SEQRES  30 A  922  HIS ARG ILE CYS GLN ILE VAL SER THR ARG SER ALA SER          
SEQRES  31 A  922  LEU CYS ALA ALA THR LEU ALA ALA VAL LEU GLN ARG ILE          
SEQRES  32 A  922  LYS GLU ASN LYS GLY GLU GLU ARG LEU ARG SER THR ILE          
SEQRES  33 A  922  GLY VAL ASP GLY SER VAL TYR LYS LYS HIS PRO HIS PHE          
SEQRES  34 A  922  ALA LYS ARG LEU HIS LYS THR VAL ARG ARG LEU VAL PRO          
SEQRES  35 A  922  GLY CYS ASP VAL ARG PHE LEU ARG SER GLU ASP GLY SER          
SEQRES  36 A  922  GLY LYS GLY ALA ALA MET VAL THR ALA VAL ALA TYR ARG          
SEQRES  37 A  922  LEU ALA ASP GLN HIS ARG ALA ARG GLN LYS THR LEU GLU          
SEQRES  38 A  922  HIS LEU GLN LEU SER HIS ASP GLN LEU LEU GLU VAL LYS          
SEQRES  39 A  922  ARG ARG MET LYS VAL GLU MET GLU ARG GLY LEU SER LYS          
SEQRES  40 A  922  GLU THR HIS ALA SER ALA PRO VAL LYS MET LEU PRO THR          
SEQRES  41 A  922  TYR VAL CYS ALA THR PRO ASP GLY THR GLU LYS GLY ASP          
SEQRES  42 A  922  PHE LEU ALA LEU ASP LEU GLY GLY THR ASN PHE ARG VAL          
SEQRES  43 A  922  LEU LEU VAL ARG VAL ARG ASN GLY LYS TRP GLY GLY VAL          
SEQRES  44 A  922  GLU MET HIS ASN LYS ILE TYR ALA ILE PRO GLN GLU VAL          
SEQRES  45 A  922  MET HIS GLY THR GLY ASP GLU LEU PHE ASP HIS ILE VAL          
SEQRES  46 A  922  GLN CYS ILE ALA ASP PHE LEU GLU TYR MET GLY MET LYS          
SEQRES  47 A  922  GLY VAL SER LEU PRO LEU GLY PHE THR PHE SER PHE PRO          
SEQRES  48 A  922  CYS GLN GLN ASN SER LEU ASP GLU SER ILE LEU LEU LYS          
SEQRES  49 A  922  TRP THR LYS GLY PHE LYS ALA SER GLY CYS GLU GLY GLU          
SEQRES  50 A  922  ASP VAL VAL THR LEU LEU LYS GLU ALA ILE HIS ARG ARG          
SEQRES  51 A  922  GLU GLU PHE ASP LEU ASP VAL VAL ALA VAL VAL ASN ASP          
SEQRES  52 A  922  THR VAL GLY THR MET MET THR CYS GLY PHE GLU ASP PRO          
SEQRES  53 A  922  HIS CYS GLU VAL GLY LEU ILE VAL GLY THR GLY SER ASN          
SEQRES  54 A  922  ALA CYS TYR MET GLU GLU MET ARG ASN VAL GLU LEU VAL          
SEQRES  55 A  922  GLU GLY GLU GLU GLY ARG MET CYS VAL ASN MET GLU TRP          
SEQRES  56 A  922  GLY ALA PHE GLY ASP ASN GLY CYS LEU ASP ASP PHE ARG          
SEQRES  57 A  922  THR GLU PHE ASP VAL ALA VAL ASP GLU LEU SER LEU ASN          
SEQRES  58 A  922  PRO GLY LYS GLN ARG PHE GLU LYS MET ILE SER GLY MET          
SEQRES  59 A  922  TYR LEU GLY GLU ILE VAL ARG ASN ILE LEU ILE ASP PHE          
SEQRES  60 A  922  THR LYS ARG GLY LEU LEU PHE ARG GLY ARG ILE SER GLU          
SEQRES  61 A  922  ARG LEU LYS THR ARG GLY ILE PHE GLU THR LYS PHE LEU          
SEQRES  62 A  922  SER GLN ILE GLU SER ASP CYS LEU ALA LEU LEU GLN VAL          
SEQRES  63 A  922  ARG ALA ILE LEU GLN HIS LEU GLY LEU GLU SER THR CYS          
SEQRES  64 A  922  ASP ASP SER ILE ILE VAL LYS GLU VAL CYS THR VAL VAL          
SEQRES  65 A  922  ALA ARG ARG ALA ALA GLN LEU CYS GLY ALA GLY MET ALA          
SEQRES  66 A  922  ALA VAL VAL ASP ARG ILE ARG GLU ASN ARG GLY LEU ASP          
SEQRES  67 A  922  ALA LEU LYS VAL THR VAL GLY VAL ASP GLY THR LEU TYR          
SEQRES  68 A  922  LYS LEU HIS PRO HIS PHE ALA LYS VAL MET HIS GLU THR          
SEQRES  69 A  922  VAL LYS ASP LEU ALA PRO LYS CYS ASP VAL SER PHE LEU          
SEQRES  70 A  922  GLN SER GLU ASP GLY SER GLY LYS GLY ALA ALA LEU ILE          
SEQRES  71 A  922  THR ALA VAL ALA CYS ARG ILE ARG GLU ALA GLY GLN              
HET    62C  A1001      41                                                       
HET    62C  A1002      41                                                       
HET    BG6  A1003      16                                                       
HET    FLC  A1004      18                                                       
HETNAM     62C 2-DEOXY-2-{[(2E)-3-(3,4-DICHLOROPHENYL)PROP-2-                   
HETNAM   2 62C  ENOYL]AMINO}-ALPHA-D-GLUCOPYRANOSE                              
HETNAM     BG6 6-O-PHOSPHONO-BETA-D-GLUCOPYRANOSE                               
HETNAM     FLC CITRATE ANION                                                    
FORMUL   2  62C    2(C15 H17 CL2 N O6)                                          
FORMUL   4  BG6    C6 H13 O9 P                                                  
FORMUL   5  FLC    C6 H5 O7 3-                                                  
FORMUL   6  HOH   *8(H2 O)                                                      
HELIX    1 AA1 ASP A   17  LEU A   26  1                                  10    
HELIX    2 AA2 TYR A   27  ARG A   30  5                                   4    
HELIX    3 AA3 SER A   32  GLY A   52  1                                  21    
HELIX    4 AA4 THR A   55  ALA A   59  5                                   5    
HELIX    5 AA5 THR A  124  ASP A  128  1                                   5    
HELIX    6 AA6 GLU A  132  PHE A  137  1                                   6    
HELIX    7 AA7 MET A  138  LYS A  140  5                                   3    
HELIX    8 AA8 GLN A  142  LYS A  146  5                                   5    
HELIX    9 AA9 ALA A  187  ALA A  192  1                                   6    
HELIX   10 AB1 ASN A  208  ASP A  221  1                                  14    
HELIX   11 AB2 ARG A  243  ILE A  245  5                                   3    
HELIX   12 AB3 GLU A  260  PHE A  264  5                                   5    
HELIX   13 AB4 THR A  275  SER A  285  1                                  11    
HELIX   14 AB5 GLN A  291  MET A  296  1                                   6    
HELIX   15 AB6 TYR A  301  GLU A  316  1                                  16    
HELIX   16 AB7 LEU A  319  LYS A  323  5                                   5    
HELIX   17 AB8 PRO A  326  ASN A  330  5                                   5    
HELIX   18 AB9 GLU A  335  GLU A  345  1                                  11    
HELIX   19 AC1 GLY A  348  LEU A  359  1                                  12    
HELIX   20 AC2 THR A  364  GLY A  402  1                                  39    
HELIX   21 AC3 GLY A  414  HIS A  420  1                                   7    
HELIX   22 AC4 HIS A  422  VAL A  435  1                                  14    
HELIX   23 AC5 LYS A  451  HIS A  476  1                                  26    
HELIX   24 AC6 SER A  480  SER A  500  1                                  21    
HELIX   25 AC7 PRO A  563  HIS A  568  1                                   6    
HELIX   26 AC8 THR A  570  MET A  589  1                                  20    
HELIX   27 AC9 ASP A  632  GLU A  645  1                                  14    
HELIX   28 AD1 ASN A  656  ASP A  669  1                                  14    
HELIX   29 AD2 GLU A  708  PHE A  712  5                                   5    
HELIX   30 AD3 LEU A  718  ARG A  722  5                                   5    
HELIX   31 AD4 THR A  723  LEU A  732  1                                  10    
HELIX   32 AD5 GLN A  739  SER A  746  1                                   8    
HELIX   33 AD6 MET A  748  ARG A  764  1                                  17    
HELIX   34 AD7 LEU A  767  ARG A  771  5                                   5    
HELIX   35 AD8 GLU A  774  THR A  778  5                                   5    
HELIX   36 AD9 GLU A  783  SER A  792  1                                  10    
HELIX   37 AE1 LEU A  797  LEU A  807  1                                  11    
HELIX   38 AE2 THR A  812  ARG A  849  1                                  38    
HELIX   39 AE3 GLY A  862  HIS A  868  1                                   7    
HELIX   40 AE4 HIS A  870  ALA A  883  1                                  14    
HELIX   41 AE5 SER A  897  GLU A  913  1                                  17    
SHEET    1 AA1 6 LEU A  64  PRO A  65  0                                        
SHEET    2 AA1 6 ARG A 254  ASN A 258 -1  O  ASN A 258   N  LEU A  64           
SHEET    3 AA1 6 SER A 234  GLU A 241 -1  N  GLU A 240   O  MET A 255           
SHEET    4 AA1 6 ILE A 226  VAL A 230 -1  N  ILE A 229   O  ASN A 235           
SHEET    5 AA1 6 LEU A 406  ASP A 413  1  O  GLY A 411   N  ILE A 226           
SHEET    6 AA1 6 CYS A 438  ARG A 444  1  O  LEU A 443   N  VAL A 412           
SHEET    1 AA2 5 GLU A 106  MET A 107  0                                        
SHEET    2 AA2 5 VAL A  92  VAL A  97 -1  N  LYS A  96   O  GLU A 106           
SHEET    3 AA2 5 GLY A  78  ASP A  84 -1  N  PHE A  80   O  VAL A  95           
SHEET    4 AA2 5 LEU A 150  THR A 153  1  O  GLY A 151   N  LEU A  81           
SHEET    5 AA2 5 VAL A 204  VAL A 207  1  O  VAL A 207   N  PHE A 152           
SHEET    1 AA3 6 LEU A 512  PRO A 513  0                                        
SHEET    2 AA3 6 ARG A 702  ASN A 706 -1  O  ASN A 706   N  LEU A 512           
SHEET    3 AA3 6 SER A 682  GLU A 689 -1  N  GLU A 688   O  MET A 703           
SHEET    4 AA3 6 CYS A 672  VAL A 678 -1  N  ILE A 677   O  ASN A 683           
SHEET    5 AA3 6 LEU A 854  ASP A 861  1  O  GLY A 859   N  LEU A 676           
SHEET    6 AA3 6 CYS A 886  GLN A 892  1  O  LEU A 891   N  VAL A 860           
SHEET    1 AA4 5 VAL A 553  TYR A 560  0                                        
SHEET    2 AA4 5 PHE A 538  VAL A 545 -1  N  ARG A 544   O  GLU A 554           
SHEET    3 AA4 5 GLY A 526  LEU A 533 -1  N  ALA A 530   O  LEU A 541           
SHEET    4 AA4 5 LEU A 596  PHE A 602  1  O  THR A 601   N  LEU A 531           
SHEET    5 AA4 5 LEU A 649  VAL A 655  1  O  VAL A 655   N  PHE A 600           
SHEET    1 AA5 2 CYS A 606  SER A 610  0                                        
SHEET    2 AA5 2 GLU A 613  LEU A 616 -1  O  ILE A 615   N  GLN A 607           
CISPEP   1 ASP A  251    GLU A  252          0        25.74                     
CRYST1  165.120  165.120  126.478  90.00  90.00 120.00 P 31 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006056  0.003497  0.000000        0.00000                         
SCALE2      0.000000  0.006993  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007907        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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