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Database: PDB
Entry: 6G2U
LinkDB: 6G2U
Original site: 6G2U 
HEADER    OXIDOREDUCTASE                          23-MAR-18   6G2U              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN GLUTAMATE DEHYDROGENASE 2 (HGDH2)      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE DEHYDROGENASE 2, MITOCHONDRIAL;                  
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: GDH 2;                                                      
COMPND   5 EC: 1.4.1.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: OUR CONSTRUCT LACKS THE 53 N-TERMINAL RESIDUES WHICH  
COMPND   8 CORRESPOND TO A LEADER PEPTIDE                                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GLUD2, GLUDP1;                                                 
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PFASTBACDUAL                          
KEYWDS    GLUTAMATE, DEHYDROGENASE, OXIDOREDUCTASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.F.FADOULOGLOU,C.DIMOVASILI,M.PROVIDAKI,D.KOTSIFAKI,I.SARROU,        
AUTHOR   2 A.PLAITAKIS,I.ZAGANAS,M.KOKKINIDIS                                   
REVDAT   3   10-FEB-21 6G2U    1       JRNL   LINK                              
REVDAT   2   06-NOV-19 6G2U    1       REMARK                                   
REVDAT   1   10-APR-19 6G2U    0                                                
JRNL        AUTH   C.DIMOVASILI,V.E.FADOULOGLOU,A.KEFALA,M.PROVIDAKI,           
JRNL        AUTH 2 D.KOTSIFAKI,K.KANAVOURAS,I.SARROU,A.PLAITAKIS,I.ZAGANAS,     
JRNL        AUTH 3 M.KOKKINIDIS                                                 
JRNL        TITL   CRYSTAL STRUCTURE OF GLUTAMATE DEHYDROGENASE 2, A POSITIVELY 
JRNL        TITL 2 SELECTED NOVEL HUMAN ENZYME INVOLVED IN BRAIN BIOLOGY AND    
JRNL        TITL 3 CANCER PATHOPHYSIOLOGY.                                      
JRNL        REF    J.NEUROCHEM.                               2021              
JRNL        REFN                   ESSN 1471-4159                               
JRNL        PMID   33421122                                                     
JRNL        DOI    10.1111/JNC.15296                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.93 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.12_2829                                     
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.65                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.894                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 160982                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.004                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8056                            
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 47.6573 -  9.0970    0.99     5166   279  0.1988 0.2072        
REMARK   3     2  9.0970 -  7.2287    1.00     5173   268  0.1604 0.2262        
REMARK   3     3  7.2287 -  6.3173    1.00     5156   271  0.1824 0.2384        
REMARK   3     4  6.3173 -  5.7408    1.00     5170   272  0.1845 0.2282        
REMARK   3     5  5.7408 -  5.3299    1.00     5112   278  0.1859 0.2577        
REMARK   3     6  5.3299 -  5.0160    1.00     5229   281  0.1719 0.2176        
REMARK   3     7  5.0160 -  4.7650    1.00     5156   271  0.1586 0.2139        
REMARK   3     8  4.7650 -  4.5578    1.00     5162   274  0.1526 0.2300        
REMARK   3     9  4.5578 -  4.3824    1.00     5106   270  0.1464 0.2089        
REMARK   3    10  4.3824 -  4.2313    1.00     5243   273  0.1549 0.2193        
REMARK   3    11  4.2313 -  4.0991    1.00     5211   279  0.1598 0.2200        
REMARK   3    12  4.0991 -  3.9820    1.00     5133   271  0.1601 0.2223        
REMARK   3    13  3.9820 -  3.8772    1.00     5145   277  0.1616 0.1867        
REMARK   3    14  3.8772 -  3.7826    1.00     5204   272  0.1679 0.2340        
REMARK   3    15  3.7826 -  3.6967    1.00     5099   272  0.1779 0.2372        
REMARK   3    16  3.6967 -  3.6180    1.00     5224   273  0.2036 0.2373        
REMARK   3    17  3.6180 -  3.5457    1.00     5143   271  0.2079 0.2707        
REMARK   3    18  3.5457 -  3.4788    1.00     5197   276  0.2082 0.2536        
REMARK   3    19  3.4788 -  3.4167    1.00     5155   267  0.2153 0.3061        
REMARK   3    20  3.4167 -  3.3588    1.00     5191   275  0.2233 0.2943        
REMARK   3    21  3.3588 -  3.3046    1.00     5135   267  0.2202 0.2998        
REMARK   3    22  3.3046 -  3.2538    1.00     5225   271  0.2511 0.3370        
REMARK   3    23  3.2538 -  3.2059    1.00     5067   263  0.2646 0.3552        
REMARK   3    24  3.2059 -  3.1608    1.00     5276   280  0.2742 0.3000        
REMARK   3    25  3.1608 -  3.1181    1.00     5112   268  0.2748 0.3228        
REMARK   3    26  3.1181 -  3.0776    1.00     5225   275  0.2861 0.3402        
REMARK   3    27  3.0776 -  3.0391    1.00     5102   267  0.2877 0.3444        
REMARK   3    28  3.0391 -  3.0025    1.00     5153   269  0.2854 0.3298        
REMARK   3    29  3.0025 -  2.9676    1.00     5250   271  0.2847 0.3534        
REMARK   3    30  2.9676 -  2.9343    0.58     3006   155  0.4003 0.5065        
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)     : 0.403            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.743           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.35                          
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      :  0.002          22969                                  
REMARK   3   ANGLE     :  0.387          30970                                  
REMARK   3   CHIRALITY :  0.039           3280                                  
REMARK   3   PLANARITY :  0.003           4041                                  
REMARK   3   DIHEDRAL  :  1.723          13576                                  
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 6G2U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009176.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83838                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.930                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.150                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 13.60                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.93                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.70                              
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1L1F                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, MPD, NACL, SODIUM PHOSPHATE,   
REMARK 280  PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      216.65750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      216.65750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       60.89750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       74.65200            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.89750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       74.65200            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      216.65750            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.89750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       74.65200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      216.65750            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.89750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       74.65200            
REMARK 290   SMTRY3   8  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 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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 819  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH E 816  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH E 978  LIES ON A SPECIAL POSITION.                          
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     SER A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     VAL A   502                                                      
REMARK 465     THR A   503                                                      
REMARK 465     PHE A   504                                                      
REMARK 465     THR A   505                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     ARG B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     ASP B     9                                                      
REMARK 465     ASP B    10                                                      
REMARK 465     VAL B   502                                                      
REMARK 465     THR B   503                                                      
REMARK 465     PHE B   504                                                      
REMARK 465     THR B   505                                                      
REMARK 465     SER C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     ASP C     6                                                      
REMARK 465     ARG C     7                                                      
REMARK 465     GLU C     8                                                      
REMARK 465     ASP C     9                                                      
REMARK 465     ASP C    10                                                      
REMARK 465     VAL C   502                                                      
REMARK 465     THR C   503                                                      
REMARK 465     PHE C   504                                                      
REMARK 465     THR C   505                                                      
REMARK 465     SER D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     VAL D     4                                                      
REMARK 465     ALA D     5                                                      
REMARK 465     ASP D     6                                                      
REMARK 465     ARG D     7                                                      
REMARK 465     PHE D   504                                                      
REMARK 465     THR D   505                                                      
REMARK 465     SER E     1                                                      
REMARK 465     GLU E     2                                                      
REMARK 465     LEU E     3                                                      
REMARK 465     VAL E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     ASP E     6                                                      
REMARK 465     ARG E     7                                                      
REMARK 465     GLU E     8                                                      
REMARK 465     ASP E     9                                                      
REMARK 465     VAL E   502                                                      
REMARK 465     THR E   503                                                      
REMARK 465     PHE E   504                                                      
REMARK 465     THR E   505                                                      
REMARK 465     SER F     1                                                      
REMARK 465     GLU F     2                                                      
REMARK 465     LEU F     3                                                      
REMARK 465     VAL F     4                                                      
REMARK 465     ALA F     5                                                      
REMARK 465     ASP F     6                                                      
REMARK 465     ARG F     7                                                      
REMARK 465     PHE F   504                                                      
REMARK 465     THR F   505                                                      
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     GLU A   8    OE2                                                 
REMARK 470     ASN A  12    ND2                                                 
REMARK 470     LYS A  15    CE   NZ                                             
REMARK 470     GLU A  18    OE2                                                 
REMARK 470     GLU A  42    OE1                                                 
REMARK 470     ILE A  55    CD1                                                 
REMARK 470     LEU A  65    CD1                                                 
REMARK 470     ILE A  69    CD1                                                 
REMARK 470     ARG A  70    NH2                                                 
REMARK 470     TYR A  82    OH                                                  
REMARK 470     ASP A 102    OD1  OD2                                            
REMARK 470     ASP A 106    OD2                                                 
REMARK 470     GLU A 107    OE2                                                 
REMARK 470     LYS A 138    CD   CE   NZ                                        
REMARK 470     ASN A 143    OD1  ND2                                            
REMARK 470     ASP A 248    OD2                                                 
REMARK 470     LYS A 273    NZ                                                  
REMARK 470     GLU A 279    OE1  OE2                                            
REMARK 470     SER A 280    OG                                                  
REMARK 470     ASP A 281    CG   OD1  OD2                                       
REMARK 470     ILE A 284    CG2                                                 
REMARK 470     SER A 304    OG                                                  
REMARK 470     ILE A 305    CG2                                                 
REMARK 470     LEU A 306    CG   CD1  CD2                                       
REMARK 470     LYS A 312    NZ                                                  
REMARK 470     GLU A 315    CD   OE1  OE2                                       
REMARK 470     ILE A 318    CD1                                                 
REMARK 470     LYS A 333    NZ                                                  
REMARK 470     LYS A 337    NZ                                                  
REMARK 470     LYS A 362    CD   CE   NZ                                        
REMARK 470     LEU A 413    CD1                                                 
REMARK 470     VAL A 417    CG1                                                 
REMARK 470     ILE A 444    CG2                                                 
REMARK 470     GLU A 462    OE1                                                 
REMARK 470     MET A 473    CE                                                  
REMARK 470     LYS A 495    CD   CE   NZ                                        
REMARK 470     PHE B  13    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     ARG B  23    CZ   NH1  NH2                                       
REMARK 470     VAL B  28    CG1                                                 
REMARK 470     LEU B  32    CD2                                                 
REMARK 470     SER B  41    OG                                                  
REMARK 470     GLU B  43    CD   OE1  OE2                                       
REMARK 470     ARG B  50    NE   CZ   NH1  NH2                                  
REMARK 470     ILE B  55    CG2                                                 
REMARK 470     GLU B  77    OE2                                                 
REMARK 470     GLU B 107    CD   OE1  OE2                                       
REMARK 470     THR B 141    CG2                                                 
REMARK 470     ASN B 143    OD1  ND2                                            
REMARK 470     MET B 154    CE                                                  
REMARK 470     MET B 173    CE                                                  
REMARK 470     ILE B 207    CD1                                                 
REMARK 470     ILE B 231    CG2  CD1                                            
REMARK 470     SER B 235    OG                                                  
REMARK 470     MET B 237    CE                                                  
REMARK 470     ILE B 239    CG1  CG2  CD1                                       
REMARK 470     LEU B 240    CB   CG   CD1  CD2                                  
REMARK 470     MET B 242    CE                                                  
REMARK 470     ARG B 247    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 250    OG1  CG2                                            
REMARK 470     VAL B 252    CG1  CG2                                            
REMARK 470     VAL B 253    CG1  CG2                                            
REMARK 470     GLN B 254    CD   OE1  NE2                                       
REMARK 470     VAL B 259    CG1  CG2                                            
REMARK 470     LEU B 261    CD2                                                 
REMARK 470     MET B 264    CE                                                  
REMARK 470     LEU B 267    CD1  CD2                                            
REMARK 470     ALA B 272    CB                                                  
REMARK 470     LYS B 273    CB   CG   CD   CE   NZ                              
REMARK 470     ILE B 275    CG2  CD1                                            
REMARK 470     ALA B 276    CB                                                  
REMARK 470     VAL B 277    CB   CG1  CG2                                       
REMARK 470     GLU B 279    OE1                                                 
REMARK 470     ASP B 281    OD2                                                 
REMARK 470     ILE B 284    CB   CG1  CG2  CD1                                  
REMARK 470     ASN B 286    ND2                                                 
REMARK 470     ASP B 288    CB   CG   OD1  OD2                                  
REMARK 470     ILE B 290    CG2  CD1                                            
REMARK 470     LYS B 293    NZ                                                  
REMARK 470     GLU B 294    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 295    CG   CD1  CD2                                       
REMARK 470     ASP B 297    OD1  OD2                                            
REMARK 470     LYS B 299    NZ                                                  
REMARK 470     LEU B 300    CG   CD1  CD2                                       
REMARK 470     GLN B 301    CD   OE1  NE2                                       
REMARK 470     ILE B 305    CG1  CD1                                            
REMARK 470     LEU B 306    CD1  CD2                                            
REMARK 470     LYS B 310    CG   CD   CE   NZ                                   
REMARK 470     ALA B 311    CB                                                  
REMARK 470     LYS B 312    CB   CG   CD   CE   NZ                              
REMARK 470     TYR B 314    OH                                                  
REMARK 470     GLU B 315    CD   OE1  OE2                                       
REMARK 470     SER B 317    CB   OG                                             
REMARK 470     ILE B 318    CG1  CG2  CD1                                       
REMARK 470     LEU B 319    CG   CD1  CD2                                       
REMARK 470     VAL B 321    CG1  CG2                                            
REMARK 470     ASP B 322    OD2                                                 
REMARK 470     CYS B 323    CB   SG                                             
REMARK 470     ILE B 325    CG2  CD1                                            
REMARK 470     LEU B 326    CB   CG   CD1  CD2                                  
REMARK 470     ILE B 327    CG2  CD1                                            
REMARK 470     ALA B 329    CB                                                  
REMARK 470     ALA B 330    CB                                                  
REMARK 470     THR B 331    OG1  CG2                                            
REMARK 470     LYS B 333    CD   CE   NZ                                        
REMARK 470     GLN B 334    OE1  NE2                                            
REMARK 470     LEU B 335    CD1  CD2                                            
REMARK 470     THR B 336    CB   OG1  CG2                                       
REMARK 470     LYS B 337    NZ                                                  
REMARK 470     SER B 338    CB   OG                                             
REMARK 470     ASN B 339    OD1  ND2                                            
REMARK 470     ALA B 340    CB                                                  
REMARK 470     VAL B 343    CB   CG1  CG2                                       
REMARK 470     LYS B 344    CB   CG   CD   CE   NZ                              
REMARK 470     ALA B 345    CB                                                  
REMARK 470     LYS B 346    CG   CD   CE   NZ                                   
REMARK 470     ILE B 347    CG1  CG2  CD1                                       
REMARK 470     ILE B 348    CB   CG1  CG2  CD1                                  
REMARK 470     ALA B 349    CB                                                  
REMARK 470     ALA B 352    CB                                                  
REMARK 470     THR B 356    CG2                                                 
REMARK 470     THR B 357    CG2                                                 
REMARK 470     GLU B 359    OE1  OE2                                            
REMARK 470     LYS B 362    CG   CD   CE   NZ                                   
REMARK 470     ILE B 363    CG2  CD1                                            
REMARK 470     LEU B 365    CD1  CD2                                            
REMARK 470     ILE B 369    CD1                                                 
REMARK 470     LEU B 370    CG   CD1  CD2                                       
REMARK 470     VAL B 371    CG1  CG2                                            
REMARK 470     ILE B 372    CG2                                                 
REMARK 470     LEU B 377    CD2                                                 
REMARK 470     TYR B 405    OH                                                  
REMARK 470     GLU B 406    OE2                                                 
REMARK 470     LEU B 413    CD1  CD2                                            
REMARK 470     LEU B 415    CD1  CD2                                            
REMARK 470     ARG B 423    NH1                                                 
REMARK 470     LYS B 427    CB   CG   CD   CE   NZ                              
REMARK 470     GLU B 439    OE1                                                 
REMARK 470     LYS B 450    CE   NZ                                             
REMARK 470     GLU B 462    OE2                                                 
REMARK 470     ARG B 466    NH2                                                 
REMARK 470     MET B 473    CE                                                  
REMARK 470     LEU B 479    CD2                                                 
REMARK 470     LEU B 481    CD1  CD2                                            
REMARK 470     ILE B 490    CD1                                                 
REMARK 470     GLU B 491    OE2                                                 
REMARK 470     LYS B 495    CE   NZ                                             
REMARK 470     TYR B 497    OH                                                  
REMARK 470     ASN C  12    CB   CG   OD1  ND2                                  
REMARK 470     PHE C  13    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE C  14    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     VAL C  28    CG1  CG2                                            
REMARK 470     ASP C  30    OD1  OD2                                            
REMARK 470     LYS C  31    CE   NZ                                             
REMARK 470     LYS C  34    CD   CE   NZ                                        
REMARK 470     ASP C  35    OD1  OD2                                            
REMARK 470     GLN C  44    NE2                                                 
REMARK 470     ARG C  50    NH1                                                 
REMARK 470     ILE C  52    CG2  CD1                                            
REMARK 470     ILE C  55    CG2  CD1                                            
REMARK 470     ARG C  70    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR C  82    OH                                                  
REMARK 470     ASP C 106    OD2                                                 
REMARK 470     LYS C 134    CE   NZ                                             
REMARK 470     LYS C 147    CE   NZ                                             
REMARK 470     MET C 173    CE                                                  
REMARK 470     VAL C 223    CG1  CG2                                            
REMARK 470     ILE C 227    CG2  CD1                                            
REMARK 470     ILE C 231    CG2  CD1                                            
REMARK 470     SER C 235    OG                                                  
REMARK 470     MET C 237    CE                                                  
REMARK 470     SER C 238    OG                                                  
REMARK 470     ILE C 239    CG1  CG2  CD1                                       
REMARK 470     LEU C 240    CD1  CD2                                            
REMARK 470     ARG C 247    NH1                                                 
REMARK 470     ASP C 248    OD1                                                 
REMARK 470     THR C 250    OG1  CG2                                            
REMARK 470     VAL C 252    CB   CG1  CG2                                       
REMARK 470     VAL C 253    CG1  CG2                                            
REMARK 470     GLN C 254    CG   CD   OE1  NE2                                  
REMARK 470     VAL C 259    CG1  CG2                                            
REMARK 470     LEU C 261    CD1  CD2                                            
REMARK 470     SER C 263    OG                                                  
REMARK 470     MET C 264    CE                                                  
REMARK 470     LEU C 267    CD1  CD2                                            
REMARK 470     ALA C 272    CB                                                  
REMARK 470     LYS C 273    CG   CD   CE   NZ                                   
REMARK 470     ILE C 275    CG1  CG2  CD1                                       
REMARK 470     ALA C 276    CB                                                  
REMARK 470     VAL C 277    CB   CG1  CG2                                       
REMARK 470     GLU C 279    OE1                                                 
REMARK 470     SER C 280    OG                                                  
REMARK 470     SER C 283    OG                                                  
REMARK 470     ILE C 284    CG1  CG2  CD1                                       
REMARK 470     TRP C 285    CB   CG   CD1  CD2  NE1  CE2  CE3                   
REMARK 470     TRP C 285    CZ2  CZ3  CH2                                       
REMARK 470     ASN C 286    ND2                                                 
REMARK 470     ASP C 288    CG   OD1  OD2                                       
REMARK 470     ILE C 290    CG1  CG2  CD1                                       
REMARK 470     GLU C 294    CD   OE1  OE2                                       
REMARK 470     LEU C 295    CG   CD1  CD2                                       
REMARK 470     LEU C 300    CG   CD1  CD2                                       
REMARK 470     GLN C 301    NE2                                                 
REMARK 470     SER C 304    CB   OG                                             
REMARK 470     ILE C 305    CB   CG1  CG2  CD1                                  
REMARK 470     LEU C 306    CB   CG   CD1  CD2                                  
REMARK 470     LYS C 310    CD   CE   NZ                                        
REMARK 470     ALA C 311    CB                                                  
REMARK 470     LYS C 312    CB   CG   CD   CE   NZ                              
REMARK 470     GLU C 315    CG   CD   OE1  OE2                                  
REMARK 470     SER C 317    CB   OG                                             
REMARK 470     ILE C 318    CB   CG1  CG2  CD1                                  
REMARK 470     LEU C 319    CB   CG   CD1  CD2                                  
REMARK 470     GLU C 320    CB   CG   CD   OE1  OE2                             
REMARK 470     VAL C 321    CB   CG1  CG2                                       
REMARK 470     ASP C 322    CB   CG   OD1  OD2                                  
REMARK 470     CYS C 323    CB   SG                                             
REMARK 470     ASP C 324    CB   CG   OD1  OD2                                  
REMARK 470     ILE C 325    CB   CG1  CG2  CD1                                  
REMARK 470     LEU C 326    CB   CG   CD1  CD2                                  
REMARK 470     ILE C 327    CB   CG1  CG2  CD1                                  
REMARK 470     PRO C 328    CB   CG   CD                                        
REMARK 470     ALA C 329    CB                                                  
REMARK 470     ALA C 330    CB                                                  
REMARK 470     THR C 331    OG1  CG2                                            
REMARK 470     GLU C 332    OE1  OE2                                            
REMARK 470     LYS C 333    CD   CE   NZ                                        
REMARK 470     GLN C 334    OE1  NE2                                            
REMARK 470     LEU C 335    CG   CD1  CD2                                       
REMARK 470     LYS C 337    CB   CG   CD   CE   NZ                              
REMARK 470     SER C 338    CB   OG                                             
REMARK 470     ASN C 339    ND2                                                 
REMARK 470     ALA C 340    CB                                                  
REMARK 470     PRO C 341    CG   CD                                             
REMARK 470     ARG C 342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL C 343    CB   CG1  CG2                                       
REMARK 470     LYS C 344    CB   CG   CD   CE   NZ                              
REMARK 470     ALA C 345    CB                                                  
REMARK 470     LYS C 346    CB   CG   CD   CE   NZ                              
REMARK 470     ILE C 347    CB   CG1  CG2  CD1                                  
REMARK 470     ILE C 348    CB   CG1  CG2  CD1                                  
REMARK 470     ALA C 349    CB                                                  
REMARK 470     ALA C 352    CB                                                  
REMARK 470     THR C 356    OG1  CG2                                            
REMARK 470     GLU C 359    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS C 362    CG   CD   CE   NZ                                   
REMARK 470     ILE C 363    CG2                                                 
REMARK 470     LEU C 365    CG   CD1  CD2                                       
REMARK 470     GLU C 366    OE1                                                 
REMARK 470     ASN C 368    CG   OD1  ND2                                       
REMARK 470     ILE C 369    CG1  CG2  CD1                                       
REMARK 470     LEU C 370    CG   CD1  CD2                                       
REMARK 470     VAL C 371    CB   CG1  CG2                                       
REMARK 470     ILE C 372    CB   CG1  CG2  CD1                                  
REMARK 470     PRO C 373    CG   CD                                             
REMARK 470     ASP C 374    OD1                                                 
REMARK 470     LEU C 375    CD2                                                 
REMARK 470     LEU C 377    CD1  CD2                                            
REMARK 470     LYS C 404    NZ                                                  
REMARK 470     GLU C 406    OE1                                                 
REMARK 470     VAL C 417    CG1  CG2                                            
REMARK 470     LEU C 421    CD1  CD2                                            
REMARK 470     GLU C 439    OE1  OE2                                            
REMARK 470     GLU C 462    OE1                                                 
REMARK 470     MET C 473    CE                                                  
REMARK 470     LEU C 479    CD1  CD2                                            
REMARK 470     ALA C 484    CB                                                  
REMARK 470     ILE C 490    CD1                                                 
REMARK 470     GLU C 491    OE1  OE2                                            
REMARK 470     LYS C 495    CE   NZ                                             
REMARK 470     VAL C 496    CG1  CG2                                            
REMARK 470     ARG D  23    NH1  NH2                                            
REMARK 470     ASP D  30    OD2                                                 
REMARK 470     ASP D  35    OD1  OD2                                            
REMARK 470     GLN D  44    OE1  NE2                                            
REMARK 470     ARG D  50    NH1                                                 
REMARK 470     ARG D  98    NH1  NH2                                            
REMARK 470     GLU D 107    OE2                                                 
REMARK 470     LYS D 109    NZ                                                  
REMARK 470     LYS D 138    CG   CD   CE   NZ                                   
REMARK 470     MET D 173    CE                                                  
REMARK 470     ILE D 239    CD1                                                 
REMARK 470     ASP D 248    CB   CG   OD1  OD2                                  
REMARK 470     LYS D 312    NZ                                                  
REMARK 470     GLU D 315    OE1                                                 
REMARK 470     GLN D 334    OE1  NE2                                            
REMARK 470     LYS D 337    NZ                                                  
REMARK 470     LYS D 344    NZ                                                  
REMARK 470     LYS D 362    CD   CE   NZ                                        
REMARK 470     LEU D 413    CD1                                                 
REMARK 470     LEU D 414    CD1                                                 
REMARK 470     VAL D 417    CG1                                                 
REMARK 470     LYS D 427    NZ                                                  
REMARK 470     ILE D 434    CG2                                                 
REMARK 470     GLU D 439    OE2                                                 
REMARK 470     LYS D 450    NZ                                                  
REMARK 470     GLU D 462    OE1                                                 
REMARK 470     MET D 473    SD   CE                                             
REMARK 470     LYS D 474    CE   NZ                                             
REMARK 470     ASN D 476    ND2                                                 
REMARK 470     GLU D 491    OE2                                                 
REMARK 470     LYS D 495    CD   CE   NZ                                        
REMARK 470     VAL D 502    CB   CG1  CG2                                       
REMARK 470     THR D 503    CB   OG1  CG2                                       
REMARK 470     ARG E  23    NH1  NH2                                            
REMARK 470     LYS E  34    NZ                                                  
REMARK 470     GLU E  43    OE1  OE2                                            
REMARK 470     TYR E  82    OH                                                  
REMARK 470     ASP E 102    OD1  OD2                                            
REMARK 470     GLU E 107    OE1                                                 
REMARK 470     LYS E 138    CD   CE   NZ                                        
REMARK 470     MET E 173    CE                                                  
REMARK 470     ILE E 239    CD1                                                 
REMARK 470     SER E 280    OG                                                  
REMARK 470     ASP E 281    OD1                                                 
REMARK 470     ILE E 305    CG2  CD1                                            
REMARK 470     LEU E 306    CD1  CD2                                            
REMARK 470     LYS E 310    CE   NZ                                             
REMARK 470     LYS E 312    CD   CE   NZ                                        
REMARK 470     LYS E 362    NZ                                                  
REMARK 470     LEU E 365    CD1  CD2                                            
REMARK 470     GLU E 366    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 406    OE1  OE2                                            
REMARK 470     GLU E 439    OE1                                                 
REMARK 470     GLU E 462    OE2                                                 
REMARK 470     ARG E 466    NH1                                                 
REMARK 470     ASN E 476    ND2                                                 
REMARK 470     GLU E 491    OE1                                                 
REMARK 470     LYS F  15    NZ                                                  
REMARK 470     ASP F  30    OD2                                                 
REMARK 470     GLN F  39    OE1  NE2                                            
REMARK 470     ARG F  50    NH1  NH2                                            
REMARK 470     ARG F  70    NH2                                                 
REMARK 470     GLU F  77    OE1  OE2                                            
REMARK 470     GLU F  80    OE1  OE2                                            
REMARK 470     ARG F  98    NH2                                                 
REMARK 470     ASP F 106    OD2                                                 
REMARK 470     GLU F 107    OE1  OE2                                            
REMARK 470     LYS F 109    NZ                                                  
REMARK 470     SER F 113    OG                                                  
REMARK 470     LYS F 134    CE   NZ                                             
REMARK 470     ASN F 136    ND2                                                 
REMARK 470     ASP F 167    OD1                                                 
REMARK 470     MET F 173    CE                                                  
REMARK 470     SER F 189    OG                                                  
REMARK 470     ARG F 247    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP F 248    CG   OD1  OD2                                       
REMARK 470     LYS F 249    NZ                                                  
REMARK 470     LYS F 273    CG   CD   CE   NZ                                   
REMARK 470     SER F 280    OG                                                  
REMARK 470     ASP F 281    OD1  OD2                                            
REMARK 470     GLU F 294    OE1                                                 
REMARK 470     LEU F 300    CD1                                                 
REMARK 470     LYS F 312    NZ                                                  
REMARK 470     LYS F 346    CE   NZ                                             
REMARK 470     GLU F 366    OE1  OE2                                            
REMARK 470     SER F 397    OG                                                  
REMARK 470     THR F 402    CG2                                                 
REMARK 470     LEU F 421    CD1  CD2                                            
REMARK 470     LYS F 427    NZ                                                  
REMARK 470     VAL F 435    CG1  CG2                                            
REMARK 470     GLU F 439    OE1                                                 
REMARK 470     ASP F 442    OD1                                                 
REMARK 470     GLU F 462    OE2                                                 
REMARK 470     ARG F 466    NH2                                                 
REMARK 470     MET F 473    CE                                                  
REMARK 470     GLU F 491    OE2                                                 
REMARK 470     VAL F 502    CB   CG1  CG2                                       
REMARK 470     THR F 503    CB   OG1  CG2                                       
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    ASP A   9       67.09   -160.83                                   
REMARK 500    SER A  66       85.85   -159.98                                   
REMARK 500    PRO A 169     -177.76    -64.59                                   
REMARK 500    ASP A 172     -142.16   -160.49                                   
REMARK 500    THR A 190      -86.75   -121.20                                   
REMARK 500    PHE A 256       50.69    -99.17                                   
REMARK 500    GLU A 279     -157.24   -112.49                                   
REMARK 500    ASN A 286      113.76   -163.87                                   
REMARK 500    LYS A 310       35.33    -86.44                                   
REMARK 500    CYS A 323     -168.38   -164.40                                   
REMARK 500    ALA A 330     -125.34   -144.49                                   
REMARK 500    TYR A 376      -53.76   -120.46                                   
REMARK 500    ASN A 378       35.50    -92.42                                   
REMARK 500    SER B  66       79.32   -153.54                                   
REMARK 500    LYS B 134       69.76   -100.25                                   
REMARK 500    VAL B 166      -60.54   -108.54                                   
REMARK 500    ASP B 172     -133.09   -143.80                                   
REMARK 500    THR B 190      -84.16   -120.07                                   
REMARK 500    ASN B 286      113.10   -162.15                                   
REMARK 500    ALA B 330      -91.87   -132.43                                   
REMARK 500    PHE C  14      -80.20   -113.72                                   
REMARK 500    SER C  66       87.76   -151.57                                   
REMARK 500    HIS C  86      -73.85    -70.08                                   
REMARK 500    LYS C 130      132.12   -174.80                                   
REMARK 500    PRO C 169     -179.11    -65.63                                   
REMARK 500    ASP C 172     -137.95   -153.47                                   
REMARK 500    THR C 190      -94.48   -127.59                                   
REMARK 500    PHE C 256       51.26    -96.69                                   
REMARK 500    ASN C 286      108.69   -164.31                                   
REMARK 500    HIS C 302     -144.07   -122.53                                   
REMARK 500    CYS C 323     -146.21   -158.16                                   
REMARK 500    ASP C 324      -35.99   -133.14                                   
REMARK 500    ALA C 330     -120.76   -132.38                                   
REMARK 500    ASN C 378       39.84    -92.47                                   
REMARK 500    ARG D  37       53.39    -94.85                                   
REMARK 500    PRO D 169     -177.65    -67.30                                   
REMARK 500    ASP D 172     -138.67   -157.37                                   
REMARK 500    THR D 190      -90.03   -124.47                                   
REMARK 500    PHE D 256       42.84    -91.86                                   
REMARK 500    GLU D 279     -160.88   -128.88                                   
REMARK 500    ASN D 286      104.98   -165.48                                   
REMARK 500    PRO D 328       99.54    -68.31                                   
REMARK 500    ALA D 330     -114.07   -129.60                                   
REMARK 500    THR D 331     -157.23    -95.02                                   
REMARK 500    GLU D 350       98.59    -69.81                                   
REMARK 500    GLN E  39       47.97    -92.21                                   
REMARK 500    SER E  66       74.25   -158.87                                   
REMARK 500    TYR E  99       77.46   -116.45                                   
REMARK 500    ASP E 167      119.99   -160.76                                   
REMARK 500    ASP E 172     -149.63   -155.96                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      67 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 986        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH A 987        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH A 988        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH A 989        DISTANCE =  6.65 ANGSTROMS                       
REMARK 525    HOH A 990        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH A 991        DISTANCE =  6.72 ANGSTROMS                       
REMARK 525    HOH A 992        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH A 993        DISTANCE =  7.06 ANGSTROMS                       
REMARK 525    HOH A 994        DISTANCE =  7.09 ANGSTROMS                       
REMARK 525    HOH A 995        DISTANCE =  7.18 ANGSTROMS                       
REMARK 525    HOH A 996        DISTANCE =  7.25 ANGSTROMS                       
REMARK 525    HOH B 892        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH B 893        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH B 894        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH B 895        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH B 896        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH B 897        DISTANCE = 18.20 ANGSTROMS                       
REMARK 525    HOH C 926        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH C 927        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH C 928        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH C 929        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH C 930        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH C 931        DISTANCE =  6.60 ANGSTROMS                       
REMARK 525    HOH C 932        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH C 933        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH C 934        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH C 935        DISTANCE =  7.95 ANGSTROMS                       
REMARK 525    HOH D1050        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH D1051        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH D1052        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH D1053        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH D1054        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH D1055        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH D1056        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH D1057        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH D1058        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH D1059        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH D1060        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH D1061        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH D1062        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH D1063        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH D1064        DISTANCE =  8.41 ANGSTROMS                       
REMARK 525    HOH D1065        DISTANCE = 16.19 ANGSTROMS                       
REMARK 525    HOH E 980        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH E 981        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH E 982        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH E 983        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH E 984        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH E 985        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH E 986        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH E 987        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH E 988        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH E 989        DISTANCE =  6.67 ANGSTROMS                       
REMARK 525    HOH E 990        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH E 991        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH E 992        DISTANCE =  7.12 ANGSTROMS                       
REMARK 525    HOH E 993        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH E 994        DISTANCE =  7.88 ANGSTROMS                       
REMARK 525    HOH E 995        DISTANCE =  8.23 ANGSTROMS                       
REMARK 525    HOH E 996        DISTANCE =  8.41 ANGSTROMS                       
REMARK 525    HOH F 924        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH F 925        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH F 926        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH F 927        DISTANCE =  6.36 ANGSTROMS                       
REMARK 525    HOH F 928        DISTANCE =  6.40 ANGSTROMS                       
REMARK 525    HOH F 929        DISTANCE =  6.40 ANGSTROMS                       
REMARK 525    HOH F 930        DISTANCE =  6.76 ANGSTROMS                       
REMARK 525    HOH F 931        DISTANCE =  6.81 ANGSTROMS                       
REMARK 525    HOH F 932        DISTANCE =  7.28 ANGSTROMS                       
REMARK 525    HOH F 933        DISTANCE =  7.51 ANGSTROMS                       
REMARK 525    HOH F 934        DISTANCE =  8.16 ANGSTROMS                       
REMARK 525    HOH F 935        DISTANCE =  9.16 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 611  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 853   O                                                      
REMARK 620 2 HOH B 862   O    61.4                                              
REMARK 620 3 HOH D 802   O   103.6 111.6                                        
REMARK 620 4 HOH D 982   O   122.5  64.6  78.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 607  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 845   O                                                      
REMARK 620 2 HOH C 857   O   123.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA F 608  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 725   O                                                      
REMARK 620 2 ASP F 195   O   112.6                                              
REMARK 620 3 HOH F 788   O   108.3 137.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 603  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE D  55   O                                                      
REMARK 620 2 ILE D  56   O    77.3                                              
REMARK 620 3 PRO D  58   O    81.7  77.4                                        
REMARK 620 4 ASN D  60   OD1  89.4 157.1  82.3                                  
REMARK 620 5 HIS D  86   O   153.6 119.2  82.3  67.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 612  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 172   O                                                      
REMARK 620 2 THR D 175   O    64.3                                              
REMARK 620 3 HOH D 937   O   145.0  84.3                                        
REMARK 620 4 HOH D1001   O   114.2 125.8  71.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 607                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 608                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 609                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 607                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 608                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 610                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 611                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 612                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 617                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 618                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA E 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 610                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 611                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 F 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 F 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 F 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 F 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 F 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA F 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA F 607                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA F 608                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 609                  
DBREF  6G2U A    1   505  UNP    P49448   DHE4_HUMAN      54    558             
DBREF  6G2U B    1   505  UNP    P49448   DHE4_HUMAN      54    558             
DBREF  6G2U C    1   505  UNP    P49448   DHE4_HUMAN      54    558             
DBREF  6G2U D    1   505  UNP    P49448   DHE4_HUMAN      54    558             
DBREF  6G2U E    1   505  UNP    P49448   DHE4_HUMAN      54    558             
DBREF  6G2U F    1   505  UNP    P49448   DHE4_HUMAN      54    558             
SEQRES   1 A  505  SER GLU LEU VAL ALA ASP ARG GLU ASP ASP PRO ASN PHE          
SEQRES   2 A  505  PHE LYS MET VAL GLU GLY PHE PHE ASP ARG GLY ALA SER          
SEQRES   3 A  505  ILE VAL GLU ASP LYS LEU VAL LYS ASP LEU ARG THR GLN          
SEQRES   4 A  505  GLU SER GLU GLU GLN LYS ARG ASN ARG VAL ARG GLY ILE          
SEQRES   5 A  505  LEU ARG ILE ILE LYS PRO CYS ASN HIS VAL LEU SER LEU          
SEQRES   6 A  505  SER PHE PRO ILE ARG ARG ASP ASP GLY SER TRP GLU VAL          
SEQRES   7 A  505  ILE GLU GLY TYR ARG ALA GLN HIS SER GLN HIS ARG THR          
SEQRES   8 A  505  PRO CYS LYS GLY GLY ILE ARG TYR SER THR ASP VAL SER          
SEQRES   9 A  505  VAL ASP GLU VAL LYS ALA LEU ALA SER LEU MET THR TYR          
SEQRES  10 A  505  LYS CYS ALA VAL VAL ASP VAL PRO PHE GLY GLY ALA LYS          
SEQRES  11 A  505  ALA GLY VAL LYS ILE ASN PRO LYS ASN TYR THR GLU ASN          
SEQRES  12 A  505  GLU LEU GLU LYS ILE THR ARG ARG PHE THR MET GLU LEU          
SEQRES  13 A  505  ALA LYS LYS GLY PHE ILE GLY PRO GLY VAL ASP VAL PRO          
SEQRES  14 A  505  ALA PRO ASP MET ASN THR GLY GLU ARG GLU MET SER TRP          
SEQRES  15 A  505  ILE ALA ASP THR TYR ALA SER THR ILE GLY HIS TYR ASP          
SEQRES  16 A  505  ILE ASN ALA HIS ALA CYS VAL THR GLY LYS PRO ILE SER          
SEQRES  17 A  505  GLN GLY GLY ILE HIS GLY ARG ILE SER ALA THR GLY ARG          
SEQRES  18 A  505  GLY VAL PHE HIS GLY ILE GLU ASN PHE ILE ASN GLU ALA          
SEQRES  19 A  505  SER TYR MET SER ILE LEU GLY MET THR PRO GLY PHE ARG          
SEQRES  20 A  505  ASP LYS THR PHE VAL VAL GLN GLY PHE GLY ASN VAL GLY          
SEQRES  21 A  505  LEU HIS SER MET ARG TYR LEU HIS ARG PHE GLY ALA LYS          
SEQRES  22 A  505  CYS ILE ALA VAL GLY GLU SER ASP GLY SER ILE TRP ASN          
SEQRES  23 A  505  PRO ASP GLY ILE ASP PRO LYS GLU LEU GLU ASP PHE LYS          
SEQRES  24 A  505  LEU GLN HIS GLY SER ILE LEU GLY PHE PRO LYS ALA LYS          
SEQRES  25 A  505  PRO TYR GLU GLY SER ILE LEU GLU VAL ASP CYS ASP ILE          
SEQRES  26 A  505  LEU ILE PRO ALA ALA THR GLU LYS GLN LEU THR LYS SER          
SEQRES  27 A  505  ASN ALA PRO ARG VAL LYS ALA LYS ILE ILE ALA GLU GLY          
SEQRES  28 A  505  ALA ASN GLY PRO THR THR PRO GLU ALA ASP LYS ILE PHE          
SEQRES  29 A  505  LEU GLU ARG ASN ILE LEU VAL ILE PRO ASP LEU TYR LEU          
SEQRES  30 A  505  ASN ALA GLY GLY VAL THR VAL SER TYR PHE GLU TRP LEU          
SEQRES  31 A  505  LYS ASN LEU ASN HIS VAL SER TYR GLY ARG LEU THR PHE          
SEQRES  32 A  505  LYS TYR GLU ARG ASP SER ASN TYR HIS LEU LEU LEU SER          
SEQRES  33 A  505  VAL GLN GLU SER LEU GLU ARG LYS PHE GLY LYS HIS GLY          
SEQRES  34 A  505  GLY THR ILE PRO ILE VAL PRO THR ALA GLU PHE GLN ASP          
SEQRES  35 A  505  SER ILE SER GLY ALA SER GLU LYS ASP ILE VAL HIS SER          
SEQRES  36 A  505  ALA LEU ALA TYR THR MET GLU ARG SER ALA ARG GLN ILE          
SEQRES  37 A  505  MET HIS THR ALA MET LYS TYR ASN LEU GLY LEU ASP LEU          
SEQRES  38 A  505  ARG THR ALA ALA TYR VAL ASN ALA ILE GLU LYS VAL PHE          
SEQRES  39 A  505  LYS VAL TYR SER GLU ALA GLY VAL THR PHE THR                  
SEQRES   1 B  505  SER GLU LEU VAL ALA ASP ARG GLU ASP ASP PRO ASN PHE          
SEQRES   2 B  505  PHE LYS MET VAL GLU GLY PHE PHE ASP ARG GLY ALA SER          
SEQRES   3 B  505  ILE VAL GLU ASP LYS LEU VAL LYS ASP LEU ARG THR GLN          
SEQRES   4 B  505  GLU SER GLU GLU GLN LYS ARG ASN ARG VAL ARG GLY ILE          
SEQRES   5 B  505  LEU ARG ILE ILE LYS PRO CYS ASN HIS VAL LEU SER LEU          
SEQRES   6 B  505  SER PHE PRO ILE ARG ARG ASP ASP GLY SER TRP GLU VAL          
SEQRES   7 B  505  ILE GLU GLY TYR ARG ALA GLN HIS SER GLN HIS ARG THR          
SEQRES   8 B  505  PRO CYS LYS GLY GLY ILE ARG TYR SER THR ASP VAL SER          
SEQRES   9 B  505  VAL ASP GLU VAL LYS ALA LEU ALA SER LEU MET THR TYR          
SEQRES  10 B  505  LYS CYS ALA VAL VAL ASP VAL PRO PHE GLY GLY ALA LYS          
SEQRES  11 B  505  ALA GLY VAL LYS ILE ASN PRO LYS ASN TYR THR GLU ASN          
SEQRES  12 B  505  GLU LEU GLU LYS ILE THR ARG ARG PHE THR MET GLU LEU          
SEQRES  13 B  505  ALA LYS LYS GLY PHE ILE GLY PRO GLY VAL ASP VAL PRO          
SEQRES  14 B  505  ALA PRO ASP MET ASN THR GLY GLU ARG GLU MET SER TRP          
SEQRES  15 B  505  ILE ALA ASP THR TYR ALA SER THR ILE GLY HIS TYR ASP          
SEQRES  16 B  505  ILE ASN ALA HIS ALA CYS VAL THR GLY LYS PRO ILE SER          
SEQRES  17 B  505  GLN GLY GLY ILE HIS GLY ARG ILE SER ALA THR GLY ARG          
SEQRES  18 B  505  GLY VAL PHE HIS GLY ILE GLU ASN PHE ILE ASN GLU ALA          
SEQRES  19 B  505  SER TYR MET SER ILE LEU GLY MET THR PRO GLY PHE ARG          
SEQRES  20 B  505  ASP LYS THR PHE VAL VAL GLN GLY PHE GLY ASN VAL GLY          
SEQRES  21 B  505  LEU HIS SER MET ARG TYR LEU HIS ARG PHE GLY ALA LYS          
SEQRES  22 B  505  CYS ILE ALA VAL GLY GLU SER ASP GLY SER ILE TRP ASN          
SEQRES  23 B  505  PRO ASP GLY ILE ASP PRO LYS GLU LEU GLU ASP PHE LYS          
SEQRES  24 B  505  LEU GLN HIS GLY SER ILE LEU GLY PHE PRO LYS ALA LYS          
SEQRES  25 B  505  PRO TYR GLU GLY SER ILE LEU GLU VAL ASP CYS ASP ILE          
SEQRES  26 B  505  LEU ILE PRO ALA ALA THR GLU LYS GLN LEU THR LYS SER          
SEQRES  27 B  505  ASN ALA PRO ARG VAL LYS ALA LYS ILE ILE ALA GLU GLY          
SEQRES  28 B  505  ALA ASN GLY PRO THR THR PRO GLU ALA ASP LYS ILE PHE          
SEQRES  29 B  505  LEU GLU ARG ASN ILE LEU VAL ILE PRO ASP LEU TYR LEU          
SEQRES  30 B  505  ASN ALA GLY GLY VAL THR VAL SER TYR PHE GLU TRP LEU          
SEQRES  31 B  505  LYS ASN LEU ASN HIS VAL SER TYR GLY ARG LEU THR PHE          
SEQRES  32 B  505  LYS TYR GLU ARG ASP SER ASN TYR HIS LEU LEU LEU SER          
SEQRES  33 B  505  VAL GLN GLU SER LEU GLU ARG LYS PHE GLY LYS HIS GLY          
SEQRES  34 B  505  GLY THR ILE PRO ILE VAL PRO THR ALA GLU PHE GLN ASP          
SEQRES  35 B  505  SER ILE SER GLY ALA SER GLU LYS ASP ILE VAL HIS SER          
SEQRES  36 B  505  ALA LEU ALA TYR THR MET GLU ARG SER ALA ARG GLN ILE          
SEQRES  37 B  505  MET HIS THR ALA MET LYS TYR ASN LEU GLY LEU ASP LEU          
SEQRES  38 B  505  ARG THR ALA ALA TYR VAL ASN ALA ILE GLU LYS VAL PHE          
SEQRES  39 B  505  LYS VAL TYR SER GLU ALA GLY VAL THR PHE THR                  
SEQRES   1 C  505  SER GLU LEU VAL ALA ASP ARG GLU ASP ASP PRO ASN PHE          
SEQRES   2 C  505  PHE LYS MET VAL GLU GLY PHE PHE ASP ARG GLY ALA SER          
SEQRES   3 C  505  ILE VAL GLU ASP LYS LEU VAL LYS ASP LEU ARG THR GLN          
SEQRES   4 C  505  GLU SER GLU GLU GLN LYS ARG ASN ARG VAL ARG GLY ILE          
SEQRES   5 C  505  LEU ARG ILE ILE LYS PRO CYS ASN HIS VAL LEU SER LEU          
SEQRES   6 C  505  SER PHE PRO ILE ARG ARG ASP ASP GLY SER TRP GLU VAL          
SEQRES   7 C  505  ILE GLU GLY TYR ARG ALA GLN HIS SER GLN HIS ARG THR          
SEQRES   8 C  505  PRO CYS LYS GLY GLY ILE ARG TYR SER THR ASP VAL SER          
SEQRES   9 C  505  VAL ASP GLU VAL LYS ALA LEU ALA SER LEU MET THR TYR          
SEQRES  10 C  505  LYS CYS ALA VAL VAL ASP VAL PRO PHE GLY GLY ALA LYS          
SEQRES  11 C  505  ALA GLY VAL LYS ILE ASN PRO LYS ASN TYR THR GLU ASN          
SEQRES  12 C  505  GLU LEU GLU LYS ILE THR ARG ARG PHE THR MET GLU LEU          
SEQRES  13 C  505  ALA LYS LYS GLY PHE ILE GLY PRO GLY VAL ASP VAL PRO          
SEQRES  14 C  505  ALA PRO ASP MET ASN THR GLY GLU ARG GLU MET SER TRP          
SEQRES  15 C  505  ILE ALA ASP THR TYR ALA SER THR ILE GLY HIS TYR ASP          
SEQRES  16 C  505  ILE ASN ALA HIS ALA CYS VAL THR GLY LYS PRO ILE SER          
SEQRES  17 C  505  GLN GLY GLY ILE HIS GLY ARG ILE SER ALA THR GLY ARG          
SEQRES  18 C  505  GLY VAL PHE HIS GLY ILE GLU ASN PHE ILE ASN GLU ALA          
SEQRES  19 C  505  SER TYR MET SER ILE LEU GLY MET THR PRO GLY PHE ARG          
SEQRES  20 C  505  ASP LYS THR PHE VAL VAL GLN GLY PHE GLY ASN VAL GLY          
SEQRES  21 C  505  LEU HIS SER MET ARG TYR LEU HIS ARG PHE GLY ALA LYS          
SEQRES  22 C  505  CYS ILE ALA VAL GLY GLU SER ASP GLY SER ILE TRP ASN          
SEQRES  23 C  505  PRO ASP GLY ILE ASP PRO LYS GLU LEU GLU ASP PHE LYS          
SEQRES  24 C  505  LEU GLN HIS GLY SER ILE LEU GLY PHE PRO LYS ALA LYS          
SEQRES  25 C  505  PRO TYR GLU GLY SER ILE LEU GLU VAL ASP CYS ASP ILE          
SEQRES  26 C  505  LEU ILE PRO ALA ALA THR GLU LYS GLN LEU THR LYS SER          
SEQRES  27 C  505  ASN ALA PRO ARG VAL LYS ALA LYS ILE ILE ALA GLU GLY          
SEQRES  28 C  505  ALA ASN GLY PRO THR THR PRO GLU ALA ASP LYS ILE PHE          
SEQRES  29 C  505  LEU GLU ARG ASN ILE LEU VAL ILE PRO ASP LEU TYR LEU          
SEQRES  30 C  505  ASN ALA GLY GLY VAL THR VAL SER TYR PHE GLU TRP LEU          
SEQRES  31 C  505  LYS ASN LEU ASN HIS VAL SER TYR GLY ARG LEU THR PHE          
SEQRES  32 C  505  LYS TYR GLU ARG ASP SER ASN TYR HIS LEU LEU LEU SER          
SEQRES  33 C  505  VAL GLN GLU SER LEU GLU ARG LYS PHE GLY LYS HIS GLY          
SEQRES  34 C  505  GLY THR ILE PRO ILE VAL PRO THR ALA GLU PHE GLN ASP          
SEQRES  35 C  505  SER ILE SER GLY ALA SER GLU LYS ASP ILE VAL HIS SER          
SEQRES  36 C  505  ALA LEU ALA TYR THR MET GLU ARG SER ALA ARG GLN ILE          
SEQRES  37 C  505  MET HIS THR ALA MET LYS TYR ASN LEU GLY LEU ASP LEU          
SEQRES  38 C  505  ARG THR ALA ALA TYR VAL ASN ALA ILE GLU LYS VAL PHE          
SEQRES  39 C  505  LYS VAL TYR SER GLU ALA GLY VAL THR PHE THR                  
SEQRES   1 D  505  SER GLU LEU VAL ALA ASP ARG GLU ASP ASP PRO ASN PHE          
SEQRES   2 D  505  PHE LYS MET VAL GLU GLY PHE PHE ASP ARG GLY ALA SER          
SEQRES   3 D  505  ILE VAL GLU ASP LYS LEU VAL LYS ASP LEU ARG THR GLN          
SEQRES   4 D  505  GLU SER GLU GLU GLN LYS ARG ASN ARG VAL ARG GLY ILE          
SEQRES   5 D  505  LEU ARG ILE ILE LYS PRO CYS ASN HIS VAL LEU SER LEU          
SEQRES   6 D  505  SER PHE PRO ILE ARG ARG ASP ASP GLY SER TRP GLU VAL          
SEQRES   7 D  505  ILE GLU GLY TYR ARG ALA GLN HIS SER GLN HIS ARG THR          
SEQRES   8 D  505  PRO CYS LYS GLY GLY ILE ARG TYR SER THR ASP VAL SER          
SEQRES   9 D  505  VAL ASP GLU VAL LYS ALA LEU ALA SER LEU MET THR TYR          
SEQRES  10 D  505  LYS CYS ALA VAL VAL ASP VAL PRO PHE GLY GLY ALA LYS          
SEQRES  11 D  505  ALA GLY VAL LYS ILE ASN PRO LYS ASN TYR THR GLU ASN          
SEQRES  12 D  505  GLU LEU GLU LYS ILE THR ARG ARG PHE THR MET GLU LEU          
SEQRES  13 D  505  ALA LYS LYS GLY PHE ILE GLY PRO GLY VAL ASP VAL PRO          
SEQRES  14 D  505  ALA PRO ASP MET ASN THR GLY GLU ARG GLU MET SER TRP          
SEQRES  15 D  505  ILE ALA ASP THR TYR ALA SER THR ILE GLY HIS TYR ASP          
SEQRES  16 D  505  ILE ASN ALA HIS ALA CYS VAL THR GLY LYS PRO ILE SER          
SEQRES  17 D  505  GLN GLY GLY ILE HIS GLY ARG ILE SER ALA THR GLY ARG          
SEQRES  18 D  505  GLY VAL PHE HIS GLY ILE GLU ASN PHE ILE ASN GLU ALA          
SEQRES  19 D  505  SER TYR MET SER ILE LEU GLY MET THR PRO GLY PHE ARG          
SEQRES  20 D  505  ASP LYS THR PHE VAL VAL GLN GLY PHE GLY ASN VAL GLY          
SEQRES  21 D  505  LEU HIS SER MET ARG TYR LEU HIS ARG PHE GLY ALA LYS          
SEQRES  22 D  505  CYS ILE ALA VAL GLY GLU SER ASP GLY SER ILE TRP ASN          
SEQRES  23 D  505  PRO ASP GLY ILE ASP PRO LYS GLU LEU GLU ASP PHE LYS          
SEQRES  24 D  505  LEU GLN HIS GLY SER ILE LEU GLY PHE PRO LYS ALA LYS          
SEQRES  25 D  505  PRO TYR GLU GLY SER ILE LEU GLU VAL ASP CYS ASP ILE          
SEQRES  26 D  505  LEU ILE PRO ALA ALA THR GLU LYS GLN LEU THR LYS SER          
SEQRES  27 D  505  ASN ALA PRO ARG VAL LYS ALA LYS ILE ILE ALA GLU GLY          
SEQRES  28 D  505  ALA ASN GLY PRO THR THR PRO GLU ALA ASP LYS ILE PHE          
SEQRES  29 D  505  LEU GLU ARG ASN ILE LEU VAL ILE PRO ASP LEU TYR LEU          
SEQRES  30 D  505  ASN ALA GLY GLY VAL THR VAL SER TYR PHE GLU TRP LEU          
SEQRES  31 D  505  LYS ASN LEU ASN HIS VAL SER TYR GLY ARG LEU THR PHE          
SEQRES  32 D  505  LYS TYR GLU ARG ASP SER ASN TYR HIS LEU LEU LEU SER          
SEQRES  33 D  505  VAL GLN GLU SER LEU GLU ARG LYS PHE GLY LYS HIS GLY          
SEQRES  34 D  505  GLY THR ILE PRO ILE VAL PRO THR ALA GLU PHE GLN ASP          
SEQRES  35 D  505  SER ILE SER GLY ALA SER GLU LYS ASP ILE VAL HIS SER          
SEQRES  36 D  505  ALA LEU ALA TYR THR MET GLU ARG SER ALA ARG GLN ILE          
SEQRES  37 D  505  MET HIS THR ALA MET LYS TYR ASN LEU GLY LEU ASP LEU          
SEQRES  38 D  505  ARG THR ALA ALA TYR VAL ASN ALA ILE GLU LYS VAL PHE          
SEQRES  39 D  505  LYS VAL TYR SER GLU ALA GLY VAL THR PHE THR                  
SEQRES   1 E  505  SER GLU LEU VAL ALA ASP ARG GLU ASP ASP PRO ASN PHE          
SEQRES   2 E  505  PHE LYS MET VAL GLU GLY PHE PHE ASP ARG GLY ALA SER          
SEQRES   3 E  505  ILE VAL GLU ASP LYS LEU VAL LYS ASP LEU ARG THR GLN          
SEQRES   4 E  505  GLU SER GLU GLU GLN LYS ARG ASN ARG VAL ARG GLY ILE          
SEQRES   5 E  505  LEU ARG ILE ILE LYS PRO CYS ASN HIS VAL LEU SER LEU          
SEQRES   6 E  505  SER PHE PRO ILE ARG ARG ASP ASP GLY SER TRP GLU VAL          
SEQRES   7 E  505  ILE GLU GLY TYR ARG ALA GLN HIS SER GLN HIS ARG THR          
SEQRES   8 E  505  PRO CYS LYS GLY GLY ILE ARG TYR SER THR ASP VAL SER          
SEQRES   9 E  505  VAL ASP GLU VAL LYS ALA LEU ALA SER LEU MET THR TYR          
SEQRES  10 E  505  LYS CYS ALA VAL VAL ASP VAL PRO PHE GLY GLY ALA LYS          
SEQRES  11 E  505  ALA GLY VAL LYS ILE ASN PRO LYS ASN TYR THR GLU ASN          
SEQRES  12 E  505  GLU LEU GLU LYS ILE THR ARG ARG PHE THR MET GLU LEU          
SEQRES  13 E  505  ALA LYS LYS GLY PHE ILE GLY PRO GLY VAL ASP VAL PRO          
SEQRES  14 E  505  ALA PRO ASP MET ASN THR GLY GLU ARG GLU MET SER TRP          
SEQRES  15 E  505  ILE ALA ASP THR TYR ALA SER THR ILE GLY HIS TYR ASP          
SEQRES  16 E  505  ILE ASN ALA HIS ALA CYS VAL THR GLY LYS PRO ILE SER          
SEQRES  17 E  505  GLN GLY GLY ILE HIS GLY ARG ILE SER ALA THR GLY ARG          
SEQRES  18 E  505  GLY VAL PHE HIS GLY ILE GLU ASN PHE ILE ASN GLU ALA          
SEQRES  19 E  505  SER TYR MET SER ILE LEU GLY MET THR PRO GLY PHE ARG          
SEQRES  20 E  505  ASP LYS THR PHE VAL VAL GLN GLY PHE GLY ASN VAL GLY          
SEQRES  21 E  505  LEU HIS SER MET ARG TYR LEU HIS ARG PHE GLY ALA LYS          
SEQRES  22 E  505  CYS ILE ALA VAL GLY GLU SER ASP GLY SER ILE TRP ASN          
SEQRES  23 E  505  PRO ASP GLY ILE ASP PRO LYS GLU LEU GLU ASP PHE LYS          
SEQRES  24 E  505  LEU GLN HIS GLY SER ILE LEU GLY PHE PRO LYS ALA LYS          
SEQRES  25 E  505  PRO TYR GLU GLY SER ILE LEU GLU VAL ASP CYS ASP ILE          
SEQRES  26 E  505  LEU ILE PRO ALA ALA THR GLU LYS GLN LEU THR LYS SER          
SEQRES  27 E  505  ASN ALA PRO ARG VAL LYS ALA LYS ILE ILE ALA GLU GLY          
SEQRES  28 E  505  ALA ASN GLY PRO THR THR PRO GLU ALA ASP LYS ILE PHE          
SEQRES  29 E  505  LEU GLU ARG ASN ILE LEU VAL ILE PRO ASP LEU TYR LEU          
SEQRES  30 E  505  ASN ALA GLY GLY VAL THR VAL SER TYR PHE GLU TRP LEU          
SEQRES  31 E  505  LYS ASN LEU ASN HIS VAL SER TYR GLY ARG LEU THR PHE          
SEQRES  32 E  505  LYS TYR GLU ARG ASP SER ASN TYR HIS LEU LEU LEU SER          
SEQRES  33 E  505  VAL GLN GLU SER LEU GLU ARG LYS PHE GLY LYS HIS GLY          
SEQRES  34 E  505  GLY THR ILE PRO ILE VAL PRO THR ALA GLU PHE GLN ASP          
SEQRES  35 E  505  SER ILE SER GLY ALA SER GLU LYS ASP ILE VAL HIS SER          
SEQRES  36 E  505  ALA LEU ALA TYR THR MET GLU ARG SER ALA ARG GLN ILE          
SEQRES  37 E  505  MET HIS THR ALA MET LYS TYR ASN LEU GLY LEU ASP LEU          
SEQRES  38 E  505  ARG THR ALA ALA TYR VAL ASN ALA ILE GLU LYS VAL PHE          
SEQRES  39 E  505  LYS VAL TYR SER GLU ALA GLY VAL THR PHE THR                  
SEQRES   1 F  505  SER GLU LEU VAL ALA ASP ARG GLU ASP ASP PRO ASN PHE          
SEQRES   2 F  505  PHE LYS MET VAL GLU GLY PHE PHE ASP ARG GLY ALA SER          
SEQRES   3 F  505  ILE VAL GLU ASP LYS LEU VAL LYS ASP LEU ARG THR GLN          
SEQRES   4 F  505  GLU SER GLU GLU GLN LYS ARG ASN ARG VAL ARG GLY ILE          
SEQRES   5 F  505  LEU ARG ILE ILE LYS PRO CYS ASN HIS VAL LEU SER LEU          
SEQRES   6 F  505  SER PHE PRO ILE ARG ARG ASP ASP GLY SER TRP GLU VAL          
SEQRES   7 F  505  ILE GLU GLY TYR ARG ALA GLN HIS SER GLN HIS ARG THR          
SEQRES   8 F  505  PRO CYS LYS GLY GLY ILE ARG TYR SER THR ASP VAL SER          
SEQRES   9 F  505  VAL ASP GLU VAL LYS ALA LEU ALA SER LEU MET THR TYR          
SEQRES  10 F  505  LYS CYS ALA VAL VAL ASP VAL PRO PHE GLY GLY ALA LYS          
SEQRES  11 F  505  ALA GLY VAL LYS ILE ASN PRO LYS ASN TYR THR GLU ASN          
SEQRES  12 F  505  GLU LEU GLU LYS ILE THR ARG ARG PHE THR MET GLU LEU          
SEQRES  13 F  505  ALA LYS LYS GLY PHE ILE GLY PRO GLY VAL ASP VAL PRO          
SEQRES  14 F  505  ALA PRO ASP MET ASN THR GLY GLU ARG GLU MET SER TRP          
SEQRES  15 F  505  ILE ALA ASP THR TYR ALA SER THR ILE GLY HIS TYR ASP          
SEQRES  16 F  505  ILE ASN ALA HIS ALA CYS VAL THR GLY LYS PRO ILE SER          
SEQRES  17 F  505  GLN GLY GLY ILE HIS GLY ARG ILE SER ALA THR GLY ARG          
SEQRES  18 F  505  GLY VAL PHE HIS GLY ILE GLU ASN PHE ILE ASN GLU ALA          
SEQRES  19 F  505  SER TYR MET SER ILE LEU GLY MET THR PRO GLY PHE ARG          
SEQRES  20 F  505  ASP LYS THR PHE VAL VAL GLN GLY PHE GLY ASN VAL GLY          
SEQRES  21 F  505  LEU HIS SER MET ARG TYR LEU HIS ARG PHE GLY ALA LYS          
SEQRES  22 F  505  CYS ILE ALA VAL GLY GLU SER ASP GLY SER ILE TRP ASN          
SEQRES  23 F  505  PRO ASP GLY ILE ASP PRO LYS GLU LEU GLU ASP PHE LYS          
SEQRES  24 F  505  LEU GLN HIS GLY SER ILE LEU GLY PHE PRO LYS ALA LYS          
SEQRES  25 F  505  PRO TYR GLU GLY SER ILE LEU GLU VAL ASP CYS ASP ILE          
SEQRES  26 F  505  LEU ILE PRO ALA ALA THR GLU LYS GLN LEU THR LYS SER          
SEQRES  27 F  505  ASN ALA PRO ARG VAL LYS ALA LYS ILE ILE ALA GLU GLY          
SEQRES  28 F  505  ALA ASN GLY PRO THR THR PRO GLU ALA ASP LYS ILE PHE          
SEQRES  29 F  505  LEU GLU ARG ASN ILE LEU VAL ILE PRO ASP LEU TYR LEU          
SEQRES  30 F  505  ASN ALA GLY GLY VAL THR VAL SER TYR PHE GLU TRP LEU          
SEQRES  31 F  505  LYS ASN LEU ASN HIS VAL SER TYR GLY ARG LEU THR PHE          
SEQRES  32 F  505  LYS TYR GLU ARG ASP SER ASN TYR HIS LEU LEU LEU SER          
SEQRES  33 F  505  VAL GLN GLU SER LEU GLU ARG LYS PHE GLY LYS HIS GLY          
SEQRES  34 F  505  GLY THR ILE PRO ILE VAL PRO THR ALA GLU PHE GLN ASP          
SEQRES  35 F  505  SER ILE SER GLY ALA SER GLU LYS ASP ILE VAL HIS SER          
SEQRES  36 F  505  ALA LEU ALA TYR THR MET GLU ARG SER ALA ARG GLN ILE          
SEQRES  37 F  505  MET HIS THR ALA MET LYS TYR ASN LEU GLY LEU ASP LEU          
SEQRES  38 F  505  ARG THR ALA ALA TYR VAL ASN ALA ILE GLU LYS VAL PHE          
SEQRES  39 F  505  LYS VAL TYR SER GLU ALA GLY VAL THR PHE THR                  
HET    PO4  A 601       5                                                       
HET    PO4  A 602       5                                                       
HET    PO4  A 603       5                                                       
HET    PO4  A 604       5                                                       
HET     NA  A 605       1                                                       
HET     NA  A 606       1                                                       
HET     CL  A 607       1                                                       
HET     CL  A 608       1                                                       
HET     CL  A 609       1                                                       
HET    PO4  B 601       5                                                       
HET    PO4  B 602       5                                                       
HET    PO4  B 603       5                                                       
HET    PO4  B 604       5                                                       
HET    PO4  B 605       5                                                       
HET     CL  B 606       1                                                       
HET     CL  B 607       1                                                       
HET    PO4  C 601       5                                                       
HET    PO4  C 602       5                                                       
HET    PO4  C 603       5                                                       
HET    PO4  C 604       5                                                       
HET    PO4  C 605       5                                                       
HET     NA  C 606       1                                                       
HET     NA  C 607       1                                                       
HET     CL  C 608       1                                                       
HET     CL  C 609       1                                                       
HET    PO4  D 601       5                                                       
HET    PO4  D 602       5                                                       
HET     NA  D 603       1                                                       
HET     NA  D 604       1                                                       
HET     NA  D 605       1                                                       
HET     NA  D 606       1                                                       
HET     NA  D 607       1                                                       
HET     NA  D 608       1                                                       
HET     NA  D 609       1                                                       
HET     NA  D 610       1                                                       
HET     NA  D 611       1                                                       
HET     NA  D 612       1                                                       
HET     NA  D 613       1                                                       
HET     CL  D 614       1                                                       
HET     CL  D 615       1                                                       
HET     CL  D 616       1                                                       
HET     CL  D 617       1                                                       
HET     CL  D 618       1                                                       
HET    PO4  E 601       5                                                       
HET    PO4  E 602       5                                                       
HET     NA  E 603       1                                                       
HET     NA  E 604       1                                                       
HET     NA  E 605       1                                                       
HET     CL  E 606       1                                                       
HET     CL  E 607       1                                                       
HET     CL  E 608       1                                                       
HET     CL  E 609       1                                                       
HET     CL  E 610       1                                                       
HET     CL  E 611       1                                                       
HET    PO4  F 601       5                                                       
HET    PO4  F 602       5                                                       
HET    PO4  F 603       5                                                       
HET    PO4  F 604       5                                                       
HET    PO4  F 605       5                                                       
HET     NA  F 606       1                                                       
HET     NA  F 607       1                                                       
HET     NA  F 608       1                                                       
HET     CL  F 609       1                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   7  PO4    23(O4 P 3-)                                                  
FORMUL  11   NA    21(NA 1+)                                                    
FORMUL  13   CL    19(CL 1-)                                                    
FORMUL  70  HOH   *1624(H2 O)                                                   
HELIX    1 AA1 ASN A   12  ASP A   35  1                                  24    
HELIX    2 AA2 SER A   41  LYS A   57  1                                  17    
HELIX    3 AA3 SER A  104  VAL A  122  1                                  19    
HELIX    4 AA4 ASN A  136  TYR A  140  5                                   5    
HELIX    5 AA5 THR A  141  LYS A  159  1                                  19    
HELIX    6 AA6 GLY A  176  THR A  190  1                                  15    
HELIX    7 AA7 ASN A  197  VAL A  202  5                                   6    
HELIX    8 AA8 PRO A  206  GLY A  210  5                                   5    
HELIX    9 AA9 SER A  217  ASN A  232  1                                  16    
HELIX   10 AB1 GLU A  233  GLY A  241  1                                   9    
HELIX   11 AB2 GLY A  257  PHE A  270  1                                  14    
HELIX   12 AB3 ASP A  291  GLY A  303  1                                  13    
HELIX   13 AB4 SER A  317  VAL A  321  5                                   5    
HELIX   14 AB5 ASN A  339  VAL A  343  5                                   5    
HELIX   15 AB6 THR A  357  ARG A  367  1                                  11    
HELIX   16 AB7 PRO A  373  ASN A  378  1                                   6    
HELIX   17 AB8 ALA A  379  HIS A  395  1                                  17    
HELIX   18 AB9 THR A  402  PHE A  425  1                                  24    
HELIX   19 AC1 THR A  437  SER A  445  1                                   9    
HELIX   20 AC2 SER A  448  TYR A  475  1                                  28    
HELIX   21 AC3 ASP A  480  GLU A  499  1                                  20    
HELIX   22 AC4 LYS B   15  ASP B   35  1                                  21    
HELIX   23 AC5 SER B   41  LYS B   57  1                                  17    
HELIX   24 AC6 SER B  104  VAL B  122  1                                  19    
HELIX   25 AC7 ASN B  136  TYR B  140  5                                   5    
HELIX   26 AC8 THR B  141  LYS B  159  1                                  19    
HELIX   27 AC9 GLY B  176  THR B  190  1                                  15    
HELIX   28 AD1 ASN B  197  VAL B  202  5                                   6    
HELIX   29 AD2 PRO B  206  GLY B  210  5                                   5    
HELIX   30 AD3 SER B  217  ASN B  232  1                                  16    
HELIX   31 AD4 GLU B  233  GLY B  241  1                                   9    
HELIX   32 AD5 GLY B  257  PHE B  270  1                                  14    
HELIX   33 AD6 ASP B  291  GLY B  303  1                                  13    
HELIX   34 AD7 THR B  357  ARG B  367  1                                  11    
HELIX   35 AD8 PRO B  373  ASN B  378  1                                   6    
HELIX   36 AD9 ALA B  379  HIS B  395  1                                  17    
HELIX   37 AE1 THR B  402  PHE B  425  1                                  24    
HELIX   38 AE2 THR B  437  GLY B  446  1                                  10    
HELIX   39 AE3 SER B  448  TYR B  475  1                                  28    
HELIX   40 AE4 ASP B  480  GLY B  501  1                                  22    
HELIX   41 AE5 MET C   16  ASP C   35  1                                  20    
HELIX   42 AE6 SER C   41  LYS C   57  1                                  17    
HELIX   43 AE7 SER C  104  VAL C  122  1                                  19    
HELIX   44 AE8 ASN C  136  TYR C  140  5                                   5    
HELIX   45 AE9 THR C  141  LYS C  159  1                                  19    
HELIX   46 AF1 GLY C  176  ALA C  188  1                                  13    
HELIX   47 AF2 ASN C  197  VAL C  202  5                                   6    
HELIX   48 AF3 PRO C  206  GLY C  210  5                                   5    
HELIX   49 AF4 SER C  217  ASN C  232  1                                  16    
HELIX   50 AF5 GLU C  233  GLY C  241  1                                   9    
HELIX   51 AF6 GLY C  257  PHE C  270  1                                  14    
HELIX   52 AF7 ASP C  291  HIS C  302  1                                  12    
HELIX   53 AF8 SER C  317  VAL C  321  5                                   5    
HELIX   54 AF9 THR C  357  ARG C  367  1                                  11    
HELIX   55 AG1 PRO C  373  ASN C  378  1                                   6    
HELIX   56 AG2 ALA C  379  HIS C  395  1                                  17    
HELIX   57 AG3 THR C  402  GLY C  426  1                                  25    
HELIX   58 AG4 THR C  437  GLY C  446  1                                  10    
HELIX   59 AG5 SER C  448  TYR C  475  1                                  28    
HELIX   60 AG6 ASP C  480  GLU C  499  1                                  20    
HELIX   61 AG7 ASN D   12  VAL D   28  1                                  17    
HELIX   62 AG8 VAL D   28  LEU D   36  1                                   9    
HELIX   63 AG9 SER D   41  LYS D   57  1                                  17    
HELIX   64 AH1 SER D  104  VAL D  122  1                                  19    
HELIX   65 AH2 ASN D  136  TYR D  140  5                                   5    
HELIX   66 AH3 THR D  141  LYS D  159  1                                  19    
HELIX   67 AH4 GLY D  176  THR D  190  1                                  15    
HELIX   68 AH5 ASN D  197  VAL D  202  5                                   6    
HELIX   69 AH6 PRO D  206  GLY D  210  5                                   5    
HELIX   70 AH7 SER D  217  ASN D  232  1                                  16    
HELIX   71 AH8 GLU D  233  GLY D  241  1                                   9    
HELIX   72 AH9 GLY D  257  PHE D  270  1                                  14    
HELIX   73 AI1 ASP D  291  GLY D  303  1                                  13    
HELIX   74 AI2 SER D  317  VAL D  321  5                                   5    
HELIX   75 AI3 ASN D  339  VAL D  343  5                                   5    
HELIX   76 AI4 THR D  357  ARG D  367  1                                  11    
HELIX   77 AI5 PRO D  373  ASN D  378  1                                   6    
HELIX   78 AI6 ALA D  379  HIS D  395  1                                  17    
HELIX   79 AI7 THR D  402  GLY D  426  1                                  25    
HELIX   80 AI8 THR D  437  GLY D  446  1                                  10    
HELIX   81 AI9 SER D  448  TYR D  475  1                                  28    
HELIX   82 AJ1 ASP D  480  GLY D  501  1                                  22    
HELIX   83 AJ2 ASN E   12  LEU E   36  1                                  25    
HELIX   84 AJ3 SER E   41  LYS E   57  1                                  17    
HELIX   85 AJ4 SER E  104  VAL E  122  1                                  19    
HELIX   86 AJ5 ASN E  136  TYR E  140  5                                   5    
HELIX   87 AJ6 THR E  141  LYS E  159  1                                  19    
HELIX   88 AJ7 GLY E  176  THR E  190  1                                  15    
HELIX   89 AJ8 ASN E  197  VAL E  202  5                                   6    
HELIX   90 AJ9 SER E  217  ASN E  232  1                                  16    
HELIX   91 AK1 GLU E  233  LEU E  240  1                                   8    
HELIX   92 AK2 GLY E  257  PHE E  270  1                                  14    
HELIX   93 AK3 ASP E  291  GLY E  303  1                                  13    
HELIX   94 AK4 SER E  317  VAL E  321  5                                   5    
HELIX   95 AK5 ASN E  339  VAL E  343  5                                   5    
HELIX   96 AK6 THR E  357  ARG E  367  1                                  11    
HELIX   97 AK7 PRO E  373  ASN E  378  1                                   6    
HELIX   98 AK8 ALA E  379  HIS E  395  1                                  17    
HELIX   99 AK9 THR E  402  PHE E  425  1                                  24    
HELIX  100 AL1 THR E  437  GLY E  446  1                                  10    
HELIX  101 AL2 SER E  448  TYR E  475  1                                  28    
HELIX  102 AL3 ASP E  480  GLU E  499  1                                  20    
HELIX  103 AL4 ASN F   12  LEU F   36  1                                  25    
HELIX  104 AL5 SER F   41  LYS F   57  1                                  17    
HELIX  105 AL6 SER F  104  VAL F  122  1                                  19    
HELIX  106 AL7 THR F  141  LYS F  159  1                                  19    
HELIX  107 AL8 GLY F  176  THR F  190  1                                  15    
HELIX  108 AL9 ASN F  197  VAL F  202  5                                   6    
HELIX  109 AM1 PRO F  206  GLY F  210  5                                   5    
HELIX  110 AM2 SER F  217  ASN F  232  1                                  16    
HELIX  111 AM3 GLU F  233  GLY F  241  1                                   9    
HELIX  112 AM4 ASN F  258  PHE F  270  1                                  13    
HELIX  113 AM5 ASP F  291  GLY F  303  1                                  13    
HELIX  114 AM6 ASN F  339  VAL F  343  5                                   5    
HELIX  115 AM7 THR F  357  ARG F  367  1                                  11    
HELIX  116 AM8 PRO F  373  ASN F  378  1                                   6    
HELIX  117 AM9 ALA F  379  HIS F  395  1                                  17    
HELIX  118 AN1 THR F  402  GLY F  426  1                                  25    
HELIX  119 AN2 THR F  437  GLY F  446  1                                  10    
HELIX  120 AN3 SER F  448  TYR F  475  1                                  28    
HELIX  121 AN4 ASP F  480  GLU F  499  1                                  20    
SHEET    1 AA1 5 HIS A  61  ARG A  70  0                                        
SHEET    2 AA1 5 TRP A  76  GLN A  85 -1  O  GLY A  81   N  LEU A  65           
SHEET    3 AA1 5 GLY A 127  VAL A 133 -1  O  GLY A 132   N  TYR A  82           
SHEET    4 AA1 5 CYS A  93  TYR A  99  1  N  LYS A  94   O  GLY A 127           
SHEET    5 AA1 5 ASP A 167  ALA A 170  1  O  VAL A 168   N  CYS A  93           
SHEET    1 AA2 7 LYS A 312  TYR A 314  0                                        
SHEET    2 AA2 7 SER A 283  TRP A 285 -1  N  SER A 283   O  TYR A 314           
SHEET    3 AA2 7 LYS A 273  GLY A 278 -1  N  VAL A 277   O  ILE A 284           
SHEET    4 AA2 7 THR A 250  GLN A 254  1  N  PHE A 251   O  LYS A 273           
SHEET    5 AA2 7 ILE A 325  PRO A 328  1  O  ILE A 327   N  VAL A 252           
SHEET    6 AA2 7 ILE A 347  ALA A 349  1  O  ILE A 347   N  LEU A 326           
SHEET    7 AA2 7 LEU A 370  ILE A 372  1  O  ILE A 372   N  ILE A 348           
SHEET    1 AA3 5 HIS B  61  ARG B  70  0                                        
SHEET    2 AA3 5 TRP B  76  GLN B  85 -1  O  GLY B  81   N  LEU B  65           
SHEET    3 AA3 5 GLY B 127  VAL B 133 -1  O  GLY B 132   N  TYR B  82           
SHEET    4 AA3 5 CYS B  93  TYR B  99  1  N  GLY B  96   O  ALA B 131           
SHEET    5 AA3 5 ASP B 167  PRO B 171  1  O  VAL B 168   N  CYS B  93           
SHEET    1 AA4 7 LYS B 312  PRO B 313  0                                        
SHEET    2 AA4 7 SER B 283  ILE B 290 -1  N  TRP B 285   O  LYS B 312           
SHEET    3 AA4 7 LYS B 273  GLY B 278 -1  N  CYS B 274   O  ILE B 290           
SHEET    4 AA4 7 THR B 250  GLN B 254  1  N  PHE B 251   O  ILE B 275           
SHEET    5 AA4 7 ILE B 325  PRO B 328  1  O  ILE B 327   N  VAL B 252           
SHEET    6 AA4 7 ILE B 347  ALA B 349  1  O  ILE B 347   N  LEU B 326           
SHEET    7 AA4 7 LEU B 370  ILE B 372  1  O  LEU B 370   N  ILE B 348           
SHEET    1 AA5 5 HIS C  61  ARG C  70  0                                        
SHEET    2 AA5 5 TRP C  76  GLN C  85 -1  O  GLY C  81   N  LEU C  65           
SHEET    3 AA5 5 GLY C 127  VAL C 133 -1  O  GLY C 132   N  TYR C  82           
SHEET    4 AA5 5 CYS C  93  TYR C  99  1  N  LYS C  94   O  GLY C 127           
SHEET    5 AA5 5 ASP C 167  VAL C 168  1  O  VAL C 168   N  CYS C  93           
SHEET    1 AA6 7 LYS C 312  PRO C 313  0                                        
SHEET    2 AA6 7 SER C 283  ILE C 290 -1  N  TRP C 285   O  LYS C 312           
SHEET    3 AA6 7 LYS C 273  GLY C 278 -1  N  ILE C 275   O  ASN C 286           
SHEET    4 AA6 7 THR C 250  GLN C 254  1  N  PHE C 251   O  LYS C 273           
SHEET    5 AA6 7 ILE C 325  PRO C 328  1  O  ILE C 327   N  VAL C 252           
SHEET    6 AA6 7 ILE C 347  ALA C 349  1  O  ILE C 347   N  LEU C 326           
SHEET    7 AA6 7 LEU C 370  ILE C 372  1  O  LEU C 370   N  ILE C 348           
SHEET    1 AA7 5 HIS D  61  ARG D  70  0                                        
SHEET    2 AA7 5 TRP D  76  GLN D  85 -1  O  GLY D  81   N  LEU D  65           
SHEET    3 AA7 5 GLY D 127  VAL D 133 -1  O  LYS D 130   N  ALA D  84           
SHEET    4 AA7 5 CYS D  93  TYR D  99  1  N  LYS D  94   O  GLY D 127           
SHEET    5 AA7 5 ASP D 167  ALA D 170  1  O  VAL D 168   N  CYS D  93           
SHEET    1 AA8 7 LYS D 312  PRO D 313  0                                        
SHEET    2 AA8 7 GLY D 282  TRP D 285 -1  N  TRP D 285   O  LYS D 312           
SHEET    3 AA8 7 LYS D 273  GLU D 279 -1  N  VAL D 277   O  ILE D 284           
SHEET    4 AA8 7 THR D 250  GLN D 254  1  N  PHE D 251   O  LYS D 273           
SHEET    5 AA8 7 ILE D 325  PRO D 328  1  O  ILE D 325   N  THR D 250           
SHEET    6 AA8 7 ILE D 347  ALA D 349  1  O  ALA D 349   N  LEU D 326           
SHEET    7 AA8 7 LEU D 370  ILE D 372  1  O  LEU D 370   N  ILE D 348           
SHEET    1 AA9 5 HIS E  61  ARG E  70  0                                        
SHEET    2 AA9 5 TRP E  76  GLN E  85 -1  O  GLY E  81   N  LEU E  65           
SHEET    3 AA9 5 GLY E 127  LYS E 134 -1  O  LYS E 134   N  GLU E  80           
SHEET    4 AA9 5 CYS E  93  SER E 100  1  N  LYS E  94   O  GLY E 127           
SHEET    5 AA9 5 ASP E 167  ALA E 170  1  O  VAL E 168   N  CYS E  93           
SHEET    1 AB1 7 LYS E 312  PRO E 313  0                                        
SHEET    2 AB1 7 SER E 283  TRP E 285 -1  N  TRP E 285   O  LYS E 312           
SHEET    3 AB1 7 LYS E 273  GLY E 278 -1  N  VAL E 277   O  ILE E 284           
SHEET    4 AB1 7 THR E 250  GLN E 254  1  N  VAL E 253   O  GLY E 278           
SHEET    5 AB1 7 ILE E 325  PRO E 328  1  O  ILE E 327   N  VAL E 252           
SHEET    6 AB1 7 ILE E 347  ALA E 349  1  O  ILE E 347   N  LEU E 326           
SHEET    7 AB1 7 LEU E 370  ILE E 372  1  O  LEU E 370   N  ILE E 348           
SHEET    1 AB2 5 HIS F  61  ARG F  70  0                                        
SHEET    2 AB2 5 TRP F  76  GLN F  85 -1  O  GLN F  85   N  HIS F  61           
SHEET    3 AB2 5 GLY F 127  VAL F 133 -1  O  LYS F 130   N  ALA F  84           
SHEET    4 AB2 5 CYS F  93  TYR F  99  1  N  LYS F  94   O  GLY F 127           
SHEET    5 AB2 5 ASP F 167  VAL F 168  1  O  VAL F 168   N  CYS F  93           
SHEET    1 AB3 7 LYS F 312  PRO F 313  0                                        
SHEET    2 AB3 7 SER F 283  TRP F 285 -1  N  TRP F 285   O  LYS F 312           
SHEET    3 AB3 7 LYS F 273  GLY F 278 -1  N  VAL F 277   O  ILE F 284           
SHEET    4 AB3 7 THR F 250  GLN F 254  1  N  PHE F 251   O  ILE F 275           
SHEET    5 AB3 7 ILE F 325  PRO F 328  1  O  ILE F 327   N  GLN F 254           
SHEET    6 AB3 7 ILE F 347  ALA F 349  1  O  ALA F 349   N  LEU F 326           
SHEET    7 AB3 7 LEU F 370  ILE F 372  1  O  LEU F 370   N  ILE F 348           
LINK        NA    NA A 606                 O   HOH A 859     1555   1555  2.60  
LINK         O   HOH B 853                NA    NA D 611     3655   1555  3.02  
LINK         O   HOH B 862                NA    NA D 611     3655   1555  2.94  
LINK        NA    NA C 606                 O   HOH C 826     1555   1555  3.15  
LINK        NA    NA C 607                 O   HOH C 845     1555   1555  2.91  
LINK        NA    NA C 607                 O   HOH C 857     1555   1555  3.05  
LINK         O   HOH C 725                NA    NA F 608     1555   1555  2.53  
LINK         O   HOH C 884                NA    NA F 606     1555   1555  2.97  
LINK         O   ILE D  55                NA    NA D 603     1555   1555  2.75  
LINK         O   ILE D  56                NA    NA D 603     1555   1555  2.97  
LINK         O   PRO D  58                NA    NA D 603     1555   1555  2.66  
LINK         OD1 ASN D  60                NA    NA D 603     1555   1555  2.84  
LINK         O   HIS D  86                NA    NA D 603     1555   1555  2.95  
LINK         O   ASP D 172                NA    NA D 612     1555   1555  2.78  
LINK         O   THR D 175                NA    NA D 612     1555   1555  2.82  
LINK         O   LYS D 344                NA    NA D 605     1555   1555  3.18  
LINK        NA    NA D 604                 O   HOH D 838     1555   1555  2.70  
LINK        NA    NA D 608                 O   HOH D 925     1555   1555  3.19  
LINK        NA    NA D 610                 O   HOH D 884     1555   1555  2.84  
LINK        NA    NA D 611                 O   HOH D 802     1555   1555  2.94  
LINK        NA    NA D 611                 O   HOH D 982     1555   1555  2.86  
LINK        NA    NA D 612                 O   HOH D 937     1555   1555  2.97  
LINK        NA    NA D 612                 O   HOH D1001     1555   1555  2.75  
LINK         O   ASP F 195                NA    NA F 608     1555   1555  2.61  
LINK        NA    NA F 607                 O   HOH F 834     1555   1555  2.82  
LINK        NA    NA F 608                 O   HOH F 788     1555   1555  2.60  
CISPEP   1 THR A   91    PRO A   92          0         3.02                     
CISPEP   2 THR B   91    PRO B   92          0        -0.09                     
CISPEP   3 THR C   91    PRO C   92          0         2.22                     
CISPEP   4 THR D   91    PRO D   92          0        -2.16                     
CISPEP   5 THR E   91    PRO E   92          0        -0.37                     
CISPEP   6 THR F   91    PRO F   92          0        -0.46                     
SITE     1 AC1  6 SER A 397  ARG A 400  HOH A 738  HOH A 785                    
SITE     2 AC1  6 ASP D 123  ARG D 463                                          
SITE     1 AC2  6 ARG A 221  TYR A 266  ARG A 269  LYS A 450                    
SITE     2 AC2  6 HOH A 725  HOH A 754                                          
SITE     1 AC3  3 ASN A 394  ASN B 394  ASN D 394                               
SITE     1 AC4  3 HIS A 213  GLY A 214  LYS A 450                               
SITE     1 AC5  1 GLY A 478                                                     
SITE     1 AC6  1 HOH A 859                                                     
SITE     1 AC7  2 ARG A 247  LYS C 424                                          
SITE     1 AC8  2 GLY B 501  HOH B 704                                          
SITE     1 AC9  2 GLU A  42  ARG A  46                                          
SITE     1 AD1  7 ARG A 463  HOH A 723  SER B 397  ARG B 400                    
SITE     2 AD1  7 HOH B 702  HOH B 708  HOH B 710                               
SITE     1 AD2  6 ARG B 265  TYR B 266  ARG B 269  HIS B 454                    
SITE     2 AD2  6 HOH B 738  HOH B 760                                          
SITE     1 AD3  4 THR A 431  ARG B 423  LYS B 424  ARG E 247                    
SITE     1 AD4  2 TYR B 194  TYR D 194                                          
SITE     1 AD5  2 HIS B 213  GLY B 214                                          
SITE     1 AD6  1 ASN B 197                                                     
SITE     1 AD7  5 ASP C 123  ARG C 463  HOH C 734  SER F 397                    
SITE     2 AD7  5 ARG F 400                                                     
SITE     1 AD8  6 ARG C 221  ARG C 265  TYR C 266  ARG C 269                    
SITE     2 AD8  6 LYS C 450  HOH C 711                                          
SITE     1 AD9  6 SER C 397  ARG C 400  HOH C 703  HOH C 720                    
SITE     2 AD9  6 HOH C 727  ARG E 463                                          
SITE     1 AE1  4  NA C 606  HOH C 719  HOH C 740  ALA E 438                    
SITE     1 AE2  1 LYS C 293                                                     
SITE     1 AE3  2 ARG C 423  PO4 C 604                                          
SITE     1 AE4  2 HOH C 845  HOH C 857                                          
SITE     1 AE5  2 HIS C 213  HOH C 909                                          
SITE     1 AE6  3 ARG B 463  SER D 397  ARG D 400                               
SITE     1 AE7  4 ARG D 221  TYR D 266  ARG D 269  HOH D 758                    
SITE     1 AE8  5 ILE D  55  ILE D  56  PRO D  58  ASN D  60                    
SITE     2 AE8  5 HIS D  86                                                     
SITE     1 AE9  1 HOH D 838                                                     
SITE     1 AF1  1 LYS D 344                                                     
SITE     1 AF2  1  CL D 618                                                     
SITE     1 AF3  1 HOH D 884                                                     
SITE     1 AF4  4 HOH B 853  HOH B 862  HOH D 802  HOH D 982                    
SITE     1 AF5  4 ASP D 172  THR D 175  HOH D 937  HOH D1001                    
SITE     1 AF6  1 ASP D 281                                                     
SITE     1 AF7  1  NA D 606                                                     
SITE     1 AF8  6 HIS E 213  GLY E 214  LYS E 450  HOH E 721                    
SITE     2 AF8  6 HOH E 729  HOH E 749                                          
SITE     1 AF9  4 ARG E 221  TYR E 266  ARG E 269  LYS E 450                    
SITE     1 AG1  2 THR E 357  GLU E 359                                          
SITE     1 AG2  2 ASP E  10  HOH E 790                                          
SITE     1 AG3  4 GLY E 429  HOH E 723  HOH E 887  HOH E 931                    
SITE     1 AG4  1 LEU C 393                                                     
SITE     1 AG5  6 HIS F 213  GLY F 214  LYS F 450  HOH F 710                    
SITE     2 AG5  6 HOH F 722  HOH F 761                                          
SITE     1 AG6  6 ARG F 221  ARG F 265  TYR F 266  ARG F 269                    
SITE     2 AG6  6 LYS F 450  HOH F 759                                          
SITE     1 AG7  5 SER E 397  ARG E 400  ASP F 123  ARG F 463                    
SITE     2 AG7  5 HOH F 704                                                     
SITE     1 AG8  4 ASN C 394  ASN E 394  ASN F 394  HOH F 701                    
SITE     1 AG9  1 TYR F 194                                                     
SITE     1 AH1  1 HOH C 884                                                     
SITE     1 AH2  2 GLU F 146  HOH F 834                                          
SITE     1 AH3  4 HOH C 725  HIS F 193  ASP F 195  HOH F 788                    
SITE     1 AH4  1 ARG F  23                                                     
CRYST1  121.795  149.304  433.315  90.00  90.00  90.00 C 2 2 21     48          
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      0.008211  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006698  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002308        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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