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Database: PDB
Entry: 6DQG
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Original site: 6DQG 
HEADER    OXIDOREDUCTASE                          10-JUN-18   6DQG              
TITLE     HUMAN GLUTAMATE DEHYDROGENASE, H454Y MUTANT                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL;                  
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: UNP RESIDUES 63-558;                                       
COMPND   5 SYNONYM: GDH 1;                                                      
COMPND   6 EC: 1.4.1.3;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GLUD1, GLUD;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GLUTAMATE, DEHYDROGENASE, INSULIN, HYPERINSULINISM, OXIDOREDUCTASE    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.J.SMITH                                                             
REVDAT   2   09-JAN-19 6DQG    1       JRNL                                     
REVDAT   1   20-JUN-18 6DQG    0                                                
JRNL        AUTH   O.M.NASSAR,C.LI,C.A.STANLEY,B.M.PETTITT,T.J.SMITH            
JRNL        TITL   GLUTAMATE DEHYDROGENASE: STRUCTURE OF A HYPERINSULINISM      
JRNL        TITL 2 MUTANT, CORRECTIONS TO THE ATOMIC MODEL, AND INSIGHTS INTO A 
JRNL        TITL 3 REGULATORY SITE.                                             
JRNL        REF    PROTEINS                      V.  87    41 2019              
JRNL        REFN                   ESSN 1097-0134                               
JRNL        PMID   30367518                                                     
JRNL        DOI    10.1002/PROT.25620                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.78                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.020                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 90875                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.243                           
REMARK   3   R VALUE            (WORKING SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4607                            
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 29.7767 -  8.3302    0.99     3160   201  0.1764 0.1953        
REMARK   3     2  8.3302 -  6.6360    0.99     3223   151  0.1879 0.1983        
REMARK   3     3  6.6360 -  5.8042    0.99     3181   169  0.2268 0.2301        
REMARK   3     4  5.8042 -  5.2768    0.98     3165   190  0.2303 0.2758        
REMARK   3     5  5.2768 -  4.9003    0.97     3151   177  0.2151 0.2605        
REMARK   3     6  4.9003 -  4.6125    0.97     3134   195  0.2152 0.2484        
REMARK   3     7  4.6125 -  4.3823    0.97     3111   177  0.2140 0.2579        
REMARK   3     8  4.3823 -  4.1921    0.96     3124   179  0.2397 0.2830        
REMARK   3     9  4.1921 -  4.0311    0.96     3085   160  0.2428 0.2710        
REMARK   3    10  4.0311 -  3.8923    0.95     3047   156  0.2465 0.2758        
REMARK   3    11  3.8923 -  3.7708    0.94     3083   163  0.2537 0.2740        
REMARK   3    12  3.7708 -  3.6632    0.94     3022   156  0.2408 0.2865        
REMARK   3    13  3.6632 -  3.5670    0.93     3043   142  0.2576 0.2799        
REMARK   3    14  3.5670 -  3.4801    0.93     3002   163  0.2687 0.3182        
REMARK   3    15  3.4801 -  3.4011    0.92     3001   159  0.2710 0.3029        
REMARK   3    16  3.4011 -  3.3288    0.91     2926   153  0.2730 0.3367        
REMARK   3    17  3.3288 -  3.2623    0.90     2901   147  0.2833 0.3228        
REMARK   3    18  3.2623 -  3.2008    0.88     2834   152  0.2923 0.3536        
REMARK   3    19  3.2008 -  3.1437    0.86     2844   125  0.2809 0.3098        
REMARK   3    20  3.1437 -  3.0905    0.87     2776   158  0.2716 0.3603        
REMARK   3    21  3.0905 -  3.0407    0.85     2753   143  0.2839 0.3821        
REMARK   3    22  3.0407 -  2.9939    0.84     2758   140  0.2847 0.3629        
REMARK   3    23  2.9939 -  2.9499    0.84     2742   127  0.2805 0.3483        
REMARK   3    24  2.9499 -  2.9084    0.82     2638   126  0.2737 0.3050        
REMARK   3    25  2.9084 -  2.8691    0.81     2620   148  0.2677 0.3486        
REMARK   3    26  2.8691 -  2.8319    0.81     2567   153  0.2706 0.3263        
REMARK   3    27  2.8319 -  2.7965    0.78     2563   135  0.2806 0.3291        
REMARK   3    28  2.7965 -  2.7629    0.76     2441   117  0.2933 0.3975        
REMARK   3    29  2.7629 -  2.7308    0.73     2372   111  0.2892 0.3974        
REMARK   3    30  2.7308 -  2.7001    0.62     2001   134  0.2862 0.3325        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.330           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008          23820                                  
REMARK   3   ANGLE     :  0.949          32160                                  
REMARK   3   CHIRALITY :  0.051           3456                                  
REMARK   3   PLANARITY :  0.007           4188                                  
REMARK   3   DIHEDRAL  : 16.175          14250                                  
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 : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 3876                                        
REMARK   3     RMSD               : 0.064                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN C                                     
REMARK   3     ATOM PAIRS NUMBER  : 3876                                        
REMARK   3     RMSD               : 0.071                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 3876                                        
REMARK   3     RMSD               : 0.052                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN E                                     
REMARK   3     ATOM PAIRS NUMBER  : 3876                                        
REMARK   3     RMSD               : 0.058                                       
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN F                                     
REMARK   3     ATOM PAIRS NUMBER  : 3876                                        
REMARK   3     RMSD               : 0.056                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6DQG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000235075.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5406                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 98035                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.775                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 10% W/V PEG8000, 0.1 M        
REMARK 280  SODIUM CHLORIDE, 1.3% W/V OCTYL-B-GLUCOPYRANOSIDE, 7.5% V/V MPD,    
REMARK 280  0.1 M SODIUM PHOSPHATE, PH 6.8, 1 MM SODIUM AZIDE, VAPOR            
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 TOTAL BURIED SURFACE AREA: 36460 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 103420 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -218.0 KCAL/MOL                       
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU B   315     O    HOH B   701              1.84            
REMARK 500   O    ILE B   227     O    HOH B   702              1.85            
REMARK 500   O    PRO E    58     O    HOH E   701              1.85            
REMARK 500   OE1  GLN B    88     O    HOH B   703              1.88            
REMARK 500   OE1  GLU B   177     O    HOH B   704              1.91            
REMARK 500   OD2  ASP D    72     O    HOH D   701              1.92            
REMARK 500   OE1  GLN D    88     O    HOH D   702              1.92            
REMARK 500   O    HOH F  2120     O    HOH F  2130              1.93            
REMARK 500   OE2  GLU D   462     O    HOH D   703              1.95            
REMARK 500   O    HOH C   741     O    HOH C   742              1.98            
REMARK 500   O    GLN A   467     O    HOH A  1101              1.99            
REMARK 500   N    GLY F   478     O    HOH F  2101              2.00            
REMARK 500   O4   PO4 F  2003     O    HOH F  2102              2.01            
REMARK 500   SD   MET C   370     O    HOH C   746              2.01            
REMARK 500   ND2  ASN C   286     O    HOH C   701              2.02            
REMARK 500   O    HOH C   739     O    HOH C   742              2.02            
REMARK 500   NE   ARG E   221     O    HOH E   702              2.02            
REMARK 500   OH   TYR D   386     O    HOH D   704              2.03            
REMARK 500   OD2  ASP C   408     O    HOH C   702              2.04            
REMARK 500   OE1  GLU D    80     O    HOH D   705              2.06            
REMARK 500   N    GLY C   478     O    HOH C   703              2.07            
REMARK 500   OE1  GLU E    77     O    HOH E   703              2.08            
REMARK 500   OD2  ASP E   291     O    HOH E   704              2.09            
REMARK 500   O    ASN F   229     O    HOH F  2103              2.09            
REMARK 500   N    GLY C   220     O    HOH C   704              2.09            
REMARK 500   O    ARG C   269     O    HOH C   705              2.09            
REMARK 500   O    ASN C   392     O    HOH C   706              2.09            
REMARK 500   O2   PO4 A  1001     O    HOH A  1102              2.10            
REMARK 500   O3   PO4 A  1001     O    HOH A  1103              2.11            
REMARK 500   O    THR E   175     O    HOH E   705              2.11            
REMARK 500   O    HOH B   705     O    HOH B   735              2.12            
REMARK 500   N    ASP D    10     O    HOH D   706              2.12            
REMARK 500   O    ILE B    55     O    HOH B   705              2.13            
REMARK 500   O    HOH A  1127     O    HOH B   749              2.13            
REMARK 500   NH2  ARG D    54     O    HOH D   707              2.14            
REMARK 500   SG   CYS F    59     O    HOH F  2130              2.14            
REMARK 500   O2   PO4 D   603     O    HOH D   708              2.14            
REMARK 500   OE1  GLU B   491     O    HOH B   706              2.15            
REMARK 500   OH   TYR E   266     O4   PO4 E   602              2.15            
REMARK 500   SG   CYS B    59     O    HOH B   744              2.15            
REMARK 500   O    HOH E   735     O    HOH E   745              2.16            
REMARK 500   OD1  ASP F   442     O    HOH F  2104              2.16            
REMARK 500   OE1  GLU E   296     O    HOH E   706              2.16            
REMARK 500   NH2  ARG D    23     O    HOH D   709              2.17            
REMARK 500   O    HOH A  1131     O    HOH C   744              2.17            
REMARK 500   SG   CYS A    59     O    HOH A  1126              2.17            
REMARK 500   SG   CYS C    59     O    HOH C   735              2.18            
REMARK 500   OE1  GLU C   320     NH2  ARG C   342              2.18            
REMARK 500   OH   TYR F   486     O    HOH F  2105              2.18            
REMARK 500   OE1  GLU D   179     O    HOH D   710              2.18            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      53 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 221   CD  -  NE  -  CZ  ANGL. DEV. =  13.5 DEGREES          
REMARK 500    ARG A 221   NE  -  CZ  -  NH1 ANGL. DEV. = -10.4 DEGREES          
REMARK 500    ARG A 221   NE  -  CZ  -  NH2 ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG B 367   CD  -  NE  -  CZ  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ARG B 367   NE  -  CZ  -  NH1 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ARG B 367   NE  -  CZ  -  NH2 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ARG C  46   CD  -  NE  -  CZ  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ARG C  46   NE  -  CZ  -  NH1 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ARG C  46   NE  -  CZ  -  NH2 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG C 443   CD  -  NE  -  CZ  ANGL. DEV. =  13.3 DEGREES          
REMARK 500    ARG C 443   NE  -  CZ  -  NH1 ANGL. DEV. = -10.1 DEGREES          
REMARK 500    ARG C 443   NE  -  CZ  -  NH2 ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG D 221   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG D 221   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG F 443   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  13       23.20    -60.99                                   
REMARK 500    ASP A  35      -18.30    179.03                                   
REMARK 500    THR A  38      109.61   -174.85                                   
REMARK 500    GLU A  40      -70.26      7.20                                   
REMARK 500    ASP A 172       66.34   -169.70                                   
REMARK 500    MET A 173      -66.08     70.74                                   
REMARK 500    THR A 190      -97.35   -122.29                                   
REMARK 500    ILE A 239       -7.07    -57.03                                   
REMARK 500    PRO A 244      179.01    -57.96                                   
REMARK 500    ARG A 269       -8.88    -59.36                                   
REMARK 500    GLU A 279     -168.37   -164.53                                   
REMARK 500    ASP A 281     -126.39    -91.66                                   
REMARK 500    ASN A 286      106.71   -160.96                                   
REMARK 500    PRO A 309       34.90    -68.81                                   
REMARK 500    LYS A 310       21.45   -154.22                                   
REMARK 500    ALA A 330      138.09   -178.20                                   
REMARK 500    SER A 331      126.00     64.52                                   
REMARK 500    ALA A 379        3.90    -68.74                                   
REMARK 500    PHE A 425     -121.69   -109.19                                   
REMARK 500    LYS A 427     -122.61   -114.75                                   
REMARK 500    ILE A 432       66.25   -111.14                                   
REMARK 500    ILE A 434     -129.71    -75.68                                   
REMARK 500    VAL A 435       98.12     36.31                                   
REMARK 500    PRO A 436      151.51    -49.53                                   
REMARK 500    VAL A 502      -63.41   -156.65                                   
REMARK 500    THR A 503     -114.41    -98.22                                   
REMARK 500    PHE B  13       24.13    -60.17                                   
REMARK 500    ASP B  35      -18.18    179.90                                   
REMARK 500    THR B  38      109.12   -175.73                                   
REMARK 500    GLU B  40      -70.94      7.75                                   
REMARK 500    ASP B 167      122.91   -171.08                                   
REMARK 500    ASP B 172       69.76   -169.57                                   
REMARK 500    MET B 173      -64.88     66.99                                   
REMARK 500    THR B 190     -101.27   -124.91                                   
REMARK 500    ILE B 239       -6.72    -56.84                                   
REMARK 500    PRO B 244     -179.02    -58.70                                   
REMARK 500    GLU B 279     -167.50   -165.88                                   
REMARK 500    ASP B 281     -125.73    -90.45                                   
REMARK 500    ASN B 286      106.76   -161.10                                   
REMARK 500    PRO B 309       33.81    -67.62                                   
REMARK 500    LYS B 310       21.38   -154.35                                   
REMARK 500    ALA B 330      138.19   -179.81                                   
REMARK 500    SER B 331      126.25     64.42                                   
REMARK 500    ALA B 379        6.27    -67.50                                   
REMARK 500    PHE B 425     -121.68   -109.14                                   
REMARK 500    LYS B 427     -122.48   -115.67                                   
REMARK 500    ILE B 432       65.55   -110.84                                   
REMARK 500    PRO B 433       30.97    -90.96                                   
REMARK 500    ILE B 434     -126.40    -78.80                                   
REMARK 500    VAL B 435       99.94     33.56                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     153 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A   91     PRO A   92                   45.00                    
REMARK 500 PRO A  433     ILE A  434                  145.04                    
REMARK 500 PRO B  433     ILE B  434                  147.78                    
REMARK 500 PRO C  433     ILE C  434                  147.68                    
REMARK 500 PRO D  433     ILE D  434                  146.65                    
REMARK 500 PRO E  433     ILE E  434                  147.19                    
REMARK 500 THR F   91     PRO F   92                  -47.85                    
REMARK 500 PRO F  433     ILE F  434                  146.66                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    THR A  91         11.05                                           
REMARK 500    THR F  91        -12.23                                           
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 D 749        DISTANCE =  5.91 ANGSTROMS                       
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 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 E 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 F 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 F 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 F 2003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 F 2004                
DBREF  6DQG A   10   505  UNP    P00367   DHE3_HUMAN      63    558             
DBREF  6DQG B   10   505  UNP    P00367   DHE3_HUMAN      63    558             
DBREF  6DQG C   10   505  UNP    P00367   DHE3_HUMAN      63    558             
DBREF  6DQG D   10   505  UNP    P00367   DHE3_HUMAN      63    558             
DBREF  6DQG E   10   505  UNP    P00367   DHE3_HUMAN      63    558             
DBREF  6DQG F   10   505  UNP    P00367   DHE3_HUMAN      63    558             
SEQADV 6DQG TYR A  454  UNP  P00367    HIS   507 ENGINEERED MUTATION            
SEQADV 6DQG TYR B  454  UNP  P00367    HIS   507 ENGINEERED MUTATION            
SEQADV 6DQG TYR C  454  UNP  P00367    HIS   507 ENGINEERED MUTATION            
SEQADV 6DQG TYR D  454  UNP  P00367    HIS   507 ENGINEERED MUTATION            
SEQADV 6DQG TYR E  454  UNP  P00367    HIS   507 ENGINEERED MUTATION            
SEQADV 6DQG TYR F  454  UNP  P00367    HIS   507 ENGINEERED MUTATION            
SEQRES   1 A  496  ASP PRO ASN PHE PHE LYS MET VAL GLU GLY PHE PHE ASP          
SEQRES   2 A  496  ARG GLY ALA SER ILE VAL GLU ASP LYS LEU VAL GLU ASP          
SEQRES   3 A  496  LEU ARG THR ARG GLU SER GLU GLU GLN LYS ARG ASN ARG          
SEQRES   4 A  496  VAL ARG GLY ILE LEU ARG ILE ILE LYS PRO CYS ASN HIS          
SEQRES   5 A  496  VAL LEU SER LEU SER PHE PRO ILE ARG ARG ASP ASP GLY          
SEQRES   6 A  496  SER TRP GLU VAL ILE GLU GLY TYR ARG ALA GLN HIS SER          
SEQRES   7 A  496  GLN HIS ARG THR PRO CYS LYS GLY GLY ILE ARG TYR SER          
SEQRES   8 A  496  THR ASP VAL SER VAL ASP GLU VAL LYS ALA LEU ALA SER          
SEQRES   9 A  496  LEU MET THR TYR LYS CYS ALA VAL VAL ASP VAL PRO PHE          
SEQRES  10 A  496  GLY GLY ALA LYS ALA GLY VAL LYS ILE ASN PRO LYS ASN          
SEQRES  11 A  496  TYR THR ASP ASN GLU LEU GLU LYS ILE THR ARG ARG PHE          
SEQRES  12 A  496  THR MET GLU LEU ALA LYS LYS GLY PHE ILE GLY PRO GLY          
SEQRES  13 A  496  ILE ASP VAL PRO ALA PRO ASP MET SER THR GLY GLU ARG          
SEQRES  14 A  496  GLU MET SER TRP ILE ALA ASP THR TYR ALA SER THR ILE          
SEQRES  15 A  496  GLY HIS TYR ASP ILE ASN ALA HIS ALA CYS VAL THR GLY          
SEQRES  16 A  496  LYS PRO ILE SER GLN GLY GLY ILE HIS GLY ARG ILE SER          
SEQRES  17 A  496  ALA THR GLY ARG GLY VAL PHE HIS GLY ILE GLU ASN PHE          
SEQRES  18 A  496  ILE ASN GLU ALA SER TYR MET SER ILE LEU GLY MET THR          
SEQRES  19 A  496  PRO GLY PHE GLY ASP LYS THR PHE VAL VAL GLN GLY PHE          
SEQRES  20 A  496  GLY ASN VAL GLY LEU HIS SER MET ARG TYR LEU HIS ARG          
SEQRES  21 A  496  PHE GLY ALA LYS CYS ILE ALA VAL GLY GLU SER ASP GLY          
SEQRES  22 A  496  SER ILE TRP ASN PRO ASP GLY ILE ASP PRO LYS GLU LEU          
SEQRES  23 A  496  GLU ASP PHE LYS LEU GLN HIS GLY SER ILE LEU GLY PHE          
SEQRES  24 A  496  PRO LYS ALA LYS PRO TYR GLU GLY SER ILE LEU GLU ALA          
SEQRES  25 A  496  ASP CYS ASP ILE LEU ILE PRO ALA ALA SER GLU LYS GLN          
SEQRES  26 A  496  LEU THR LYS SER ASN ALA PRO ARG VAL LYS ALA LYS ILE          
SEQRES  27 A  496  ILE ALA GLU GLY ALA ASN GLY PRO THR THR PRO GLU ALA          
SEQRES  28 A  496  ASP LYS ILE PHE LEU GLU ARG ASN ILE MET VAL ILE PRO          
SEQRES  29 A  496  ASP LEU TYR LEU ASN ALA GLY GLY VAL THR VAL SER TYR          
SEQRES  30 A  496  PHE GLU TRP LEU LYS ASN LEU ASN HIS VAL SER TYR GLY          
SEQRES  31 A  496  ARG LEU THR PHE LYS TYR GLU ARG ASP SER ASN TYR HIS          
SEQRES  32 A  496  LEU LEU MET SER VAL GLN GLU SER LEU GLU ARG LYS PHE          
SEQRES  33 A  496  GLY LYS HIS GLY GLY THR ILE PRO ILE VAL PRO THR ALA          
SEQRES  34 A  496  GLU PHE GLN ASP ARG ILE SER GLY ALA SER GLU LYS ASP          
SEQRES  35 A  496  ILE VAL TYR SER GLY LEU ALA TYR THR MET GLU ARG SER          
SEQRES  36 A  496  ALA ARG GLN ILE MET ARG THR ALA MET LYS TYR ASN LEU          
SEQRES  37 A  496  GLY LEU ASP LEU ARG THR ALA ALA TYR VAL ASN ALA ILE          
SEQRES  38 A  496  GLU LYS VAL PHE LYS VAL TYR ASN GLU ALA GLY VAL THR          
SEQRES  39 A  496  PHE THR                                                      
SEQRES   1 B  496  ASP PRO ASN PHE PHE LYS MET VAL GLU GLY PHE PHE ASP          
SEQRES   2 B  496  ARG GLY ALA SER ILE VAL GLU ASP LYS LEU VAL GLU ASP          
SEQRES   3 B  496  LEU ARG THR ARG GLU SER GLU GLU GLN LYS ARG ASN ARG          
SEQRES   4 B  496  VAL ARG GLY ILE LEU ARG ILE ILE LYS PRO CYS ASN HIS          
SEQRES   5 B  496  VAL LEU SER LEU SER PHE PRO ILE ARG ARG ASP ASP GLY          
SEQRES   6 B  496  SER TRP GLU VAL ILE GLU GLY TYR ARG ALA GLN HIS SER          
SEQRES   7 B  496  GLN HIS ARG THR PRO CYS LYS GLY GLY ILE ARG TYR SER          
SEQRES   8 B  496  THR ASP VAL SER VAL ASP GLU VAL LYS ALA LEU ALA SER          
SEQRES   9 B  496  LEU MET THR TYR LYS CYS ALA VAL VAL ASP VAL PRO PHE          
SEQRES  10 B  496  GLY GLY ALA LYS ALA GLY VAL LYS ILE ASN PRO LYS ASN          
SEQRES  11 B  496  TYR THR ASP ASN GLU LEU GLU LYS ILE THR ARG ARG PHE          
SEQRES  12 B  496  THR MET GLU LEU ALA LYS LYS GLY PHE ILE GLY PRO GLY          
SEQRES  13 B  496  ILE ASP VAL PRO ALA PRO ASP MET SER THR GLY GLU ARG          
SEQRES  14 B  496  GLU MET SER TRP ILE ALA ASP THR TYR ALA SER THR ILE          
SEQRES  15 B  496  GLY HIS TYR ASP ILE ASN ALA HIS ALA CYS VAL THR GLY          
SEQRES  16 B  496  LYS PRO ILE SER GLN GLY GLY ILE HIS GLY ARG ILE SER          
SEQRES  17 B  496  ALA THR GLY ARG GLY VAL PHE HIS GLY ILE GLU ASN PHE          
SEQRES  18 B  496  ILE ASN GLU ALA SER TYR MET SER ILE LEU GLY MET THR          
SEQRES  19 B  496  PRO GLY PHE GLY ASP LYS THR PHE VAL VAL GLN GLY PHE          
SEQRES  20 B  496  GLY ASN VAL GLY LEU HIS SER MET ARG TYR LEU HIS ARG          
SEQRES  21 B  496  PHE GLY ALA LYS CYS ILE ALA VAL GLY GLU SER ASP GLY          
SEQRES  22 B  496  SER ILE TRP ASN PRO ASP GLY ILE ASP PRO LYS GLU LEU          
SEQRES  23 B  496  GLU ASP PHE LYS LEU GLN HIS GLY SER ILE LEU GLY PHE          
SEQRES  24 B  496  PRO LYS ALA LYS PRO TYR GLU GLY SER ILE LEU GLU ALA          
SEQRES  25 B  496  ASP CYS ASP ILE LEU ILE PRO ALA ALA SER GLU LYS GLN          
SEQRES  26 B  496  LEU THR LYS SER ASN ALA PRO ARG VAL LYS ALA LYS ILE          
SEQRES  27 B  496  ILE ALA GLU GLY ALA ASN GLY PRO THR THR PRO GLU ALA          
SEQRES  28 B  496  ASP LYS ILE PHE LEU GLU ARG ASN ILE MET VAL ILE PRO          
SEQRES  29 B  496  ASP LEU TYR LEU ASN ALA GLY GLY VAL THR VAL SER TYR          
SEQRES  30 B  496  PHE GLU TRP LEU LYS ASN LEU ASN HIS VAL SER TYR GLY          
SEQRES  31 B  496  ARG LEU THR PHE LYS TYR GLU ARG ASP SER ASN TYR HIS          
SEQRES  32 B  496  LEU LEU MET SER VAL GLN GLU SER LEU GLU ARG LYS PHE          
SEQRES  33 B  496  GLY LYS HIS GLY GLY THR ILE PRO ILE VAL PRO THR ALA          
SEQRES  34 B  496  GLU PHE GLN ASP ARG ILE SER GLY ALA SER GLU LYS ASP          
SEQRES  35 B  496  ILE VAL TYR SER GLY LEU ALA TYR THR MET GLU ARG SER          
SEQRES  36 B  496  ALA ARG GLN ILE MET ARG THR ALA MET LYS TYR ASN LEU          
SEQRES  37 B  496  GLY LEU ASP LEU ARG THR ALA ALA TYR VAL ASN ALA ILE          
SEQRES  38 B  496  GLU LYS VAL PHE LYS VAL TYR ASN GLU ALA GLY VAL THR          
SEQRES  39 B  496  PHE THR                                                      
SEQRES   1 C  496  ASP PRO ASN PHE PHE LYS MET VAL GLU GLY PHE PHE ASP          
SEQRES   2 C  496  ARG GLY ALA SER ILE VAL GLU ASP LYS LEU VAL GLU ASP          
SEQRES   3 C  496  LEU ARG THR ARG GLU SER GLU GLU GLN LYS ARG ASN ARG          
SEQRES   4 C  496  VAL ARG GLY ILE LEU ARG ILE ILE LYS PRO CYS ASN HIS          
SEQRES   5 C  496  VAL LEU SER LEU SER PHE PRO ILE ARG ARG ASP ASP GLY          
SEQRES   6 C  496  SER TRP GLU VAL ILE GLU GLY TYR ARG ALA GLN HIS SER          
SEQRES   7 C  496  GLN HIS ARG THR PRO CYS LYS GLY GLY ILE ARG TYR SER          
SEQRES   8 C  496  THR ASP VAL SER VAL ASP GLU VAL LYS ALA LEU ALA SER          
SEQRES   9 C  496  LEU MET THR TYR LYS CYS ALA VAL VAL ASP VAL PRO PHE          
SEQRES  10 C  496  GLY GLY ALA LYS ALA GLY VAL LYS ILE ASN PRO LYS ASN          
SEQRES  11 C  496  TYR THR ASP ASN GLU LEU GLU LYS ILE THR ARG ARG PHE          
SEQRES  12 C  496  THR MET GLU LEU ALA LYS LYS GLY PHE ILE GLY PRO GLY          
SEQRES  13 C  496  ILE ASP VAL PRO ALA PRO ASP MET SER THR GLY GLU ARG          
SEQRES  14 C  496  GLU MET SER TRP ILE ALA ASP THR TYR ALA SER THR ILE          
SEQRES  15 C  496  GLY HIS TYR ASP ILE ASN ALA HIS ALA CYS VAL THR GLY          
SEQRES  16 C  496  LYS PRO ILE SER GLN GLY GLY ILE HIS GLY ARG ILE SER          
SEQRES  17 C  496  ALA THR GLY ARG GLY VAL PHE HIS GLY ILE GLU ASN PHE          
SEQRES  18 C  496  ILE ASN GLU ALA SER TYR MET SER ILE LEU GLY MET THR          
SEQRES  19 C  496  PRO GLY PHE GLY ASP LYS THR PHE VAL VAL GLN GLY PHE          
SEQRES  20 C  496  GLY ASN VAL GLY LEU HIS SER MET ARG TYR LEU HIS ARG          
SEQRES  21 C  496  PHE GLY ALA LYS CYS ILE ALA VAL GLY GLU SER ASP GLY          
SEQRES  22 C  496  SER ILE TRP ASN PRO ASP GLY ILE ASP PRO LYS GLU LEU          
SEQRES  23 C  496  GLU ASP PHE LYS LEU GLN HIS GLY SER ILE LEU GLY PHE          
SEQRES  24 C  496  PRO LYS ALA LYS PRO TYR GLU GLY SER ILE LEU GLU ALA          
SEQRES  25 C  496  ASP CYS ASP ILE LEU ILE PRO ALA ALA SER GLU LYS GLN          
SEQRES  26 C  496  LEU THR LYS SER ASN ALA PRO ARG VAL LYS ALA LYS ILE          
SEQRES  27 C  496  ILE ALA GLU GLY ALA ASN GLY PRO THR THR PRO GLU ALA          
SEQRES  28 C  496  ASP LYS ILE PHE LEU GLU ARG ASN ILE MET VAL ILE PRO          
SEQRES  29 C  496  ASP LEU TYR LEU ASN ALA GLY GLY VAL THR VAL SER TYR          
SEQRES  30 C  496  PHE GLU TRP LEU LYS ASN LEU ASN HIS VAL SER TYR GLY          
SEQRES  31 C  496  ARG LEU THR PHE LYS TYR GLU ARG ASP SER ASN TYR HIS          
SEQRES  32 C  496  LEU LEU MET SER VAL GLN GLU SER LEU GLU ARG LYS PHE          
SEQRES  33 C  496  GLY LYS HIS GLY GLY THR ILE PRO ILE VAL PRO THR ALA          
SEQRES  34 C  496  GLU PHE GLN ASP ARG ILE SER GLY ALA SER GLU LYS ASP          
SEQRES  35 C  496  ILE VAL TYR SER GLY LEU ALA TYR THR MET GLU ARG SER          
SEQRES  36 C  496  ALA ARG GLN ILE MET ARG THR ALA MET LYS TYR ASN LEU          
SEQRES  37 C  496  GLY LEU ASP LEU ARG THR ALA ALA TYR VAL ASN ALA ILE          
SEQRES  38 C  496  GLU LYS VAL PHE LYS VAL TYR ASN GLU ALA GLY VAL THR          
SEQRES  39 C  496  PHE THR                                                      
SEQRES   1 D  496  ASP PRO ASN PHE PHE LYS MET VAL GLU GLY PHE PHE ASP          
SEQRES   2 D  496  ARG GLY ALA SER ILE VAL GLU ASP LYS LEU VAL GLU ASP          
SEQRES   3 D  496  LEU ARG THR ARG GLU SER GLU GLU GLN LYS ARG ASN ARG          
SEQRES   4 D  496  VAL ARG GLY ILE LEU ARG ILE ILE LYS PRO CYS ASN HIS          
SEQRES   5 D  496  VAL LEU SER LEU SER PHE PRO ILE ARG ARG ASP ASP GLY          
SEQRES   6 D  496  SER TRP GLU VAL ILE GLU GLY TYR ARG ALA GLN HIS SER          
SEQRES   7 D  496  GLN HIS ARG THR PRO CYS LYS GLY GLY ILE ARG TYR SER          
SEQRES   8 D  496  THR ASP VAL SER VAL ASP GLU VAL LYS ALA LEU ALA SER          
SEQRES   9 D  496  LEU MET THR TYR LYS CYS ALA VAL VAL ASP VAL PRO PHE          
SEQRES  10 D  496  GLY GLY ALA LYS ALA GLY VAL LYS ILE ASN PRO LYS ASN          
SEQRES  11 D  496  TYR THR ASP ASN GLU LEU GLU LYS ILE THR ARG ARG PHE          
SEQRES  12 D  496  THR MET GLU LEU ALA LYS LYS GLY PHE ILE GLY PRO GLY          
SEQRES  13 D  496  ILE ASP VAL PRO ALA PRO ASP MET SER THR GLY GLU ARG          
SEQRES  14 D  496  GLU MET SER TRP ILE ALA ASP THR TYR ALA SER THR ILE          
SEQRES  15 D  496  GLY HIS TYR ASP ILE ASN ALA HIS ALA CYS VAL THR GLY          
SEQRES  16 D  496  LYS PRO ILE SER GLN GLY GLY ILE HIS GLY ARG ILE SER          
SEQRES  17 D  496  ALA THR GLY ARG GLY VAL PHE HIS GLY ILE GLU ASN PHE          
SEQRES  18 D  496  ILE ASN GLU ALA SER TYR MET SER ILE LEU GLY MET THR          
SEQRES  19 D  496  PRO GLY PHE GLY ASP LYS THR PHE VAL VAL GLN GLY PHE          
SEQRES  20 D  496  GLY ASN VAL GLY LEU HIS SER MET ARG TYR LEU HIS ARG          
SEQRES  21 D  496  PHE GLY ALA LYS CYS ILE ALA VAL GLY GLU SER ASP GLY          
SEQRES  22 D  496  SER ILE TRP ASN PRO ASP GLY ILE ASP PRO LYS GLU LEU          
SEQRES  23 D  496  GLU ASP PHE LYS LEU GLN HIS GLY SER ILE LEU GLY PHE          
SEQRES  24 D  496  PRO LYS ALA LYS PRO TYR GLU GLY SER ILE LEU GLU ALA          
SEQRES  25 D  496  ASP CYS ASP ILE LEU ILE PRO ALA ALA SER GLU LYS GLN          
SEQRES  26 D  496  LEU THR LYS SER ASN ALA PRO ARG VAL LYS ALA LYS ILE          
SEQRES  27 D  496  ILE ALA GLU GLY ALA ASN GLY PRO THR THR PRO GLU ALA          
SEQRES  28 D  496  ASP LYS ILE PHE LEU GLU ARG ASN ILE MET VAL ILE PRO          
SEQRES  29 D  496  ASP LEU TYR LEU ASN ALA GLY GLY VAL THR VAL SER TYR          
SEQRES  30 D  496  PHE GLU TRP LEU LYS ASN LEU ASN HIS VAL SER TYR GLY          
SEQRES  31 D  496  ARG LEU THR PHE LYS TYR GLU ARG ASP SER ASN TYR HIS          
SEQRES  32 D  496  LEU LEU MET SER VAL GLN GLU SER LEU GLU ARG LYS PHE          
SEQRES  33 D  496  GLY LYS HIS GLY GLY THR ILE PRO ILE VAL PRO THR ALA          
SEQRES  34 D  496  GLU PHE GLN ASP ARG ILE SER GLY ALA SER GLU LYS ASP          
SEQRES  35 D  496  ILE VAL TYR SER GLY LEU ALA TYR THR MET GLU ARG SER          
SEQRES  36 D  496  ALA ARG GLN ILE MET ARG THR ALA MET LYS TYR ASN LEU          
SEQRES  37 D  496  GLY LEU ASP LEU ARG THR ALA ALA TYR VAL ASN ALA ILE          
SEQRES  38 D  496  GLU LYS VAL PHE LYS VAL TYR ASN GLU ALA GLY VAL THR          
SEQRES  39 D  496  PHE THR                                                      
SEQRES   1 E  496  ASP PRO ASN PHE PHE LYS MET VAL GLU GLY PHE PHE ASP          
SEQRES   2 E  496  ARG GLY ALA SER ILE VAL GLU ASP LYS LEU VAL GLU ASP          
SEQRES   3 E  496  LEU ARG THR ARG GLU SER GLU GLU GLN LYS ARG ASN ARG          
SEQRES   4 E  496  VAL ARG GLY ILE LEU ARG ILE ILE LYS PRO CYS ASN HIS          
SEQRES   5 E  496  VAL LEU SER LEU SER PHE PRO ILE ARG ARG ASP ASP GLY          
SEQRES   6 E  496  SER TRP GLU VAL ILE GLU GLY TYR ARG ALA GLN HIS SER          
SEQRES   7 E  496  GLN HIS ARG THR PRO CYS LYS GLY GLY ILE ARG TYR SER          
SEQRES   8 E  496  THR ASP VAL SER VAL ASP GLU VAL LYS ALA LEU ALA SER          
SEQRES   9 E  496  LEU MET THR TYR LYS CYS ALA VAL VAL ASP VAL PRO PHE          
SEQRES  10 E  496  GLY GLY ALA LYS ALA GLY VAL LYS ILE ASN PRO LYS ASN          
SEQRES  11 E  496  TYR THR ASP ASN GLU LEU GLU LYS ILE THR ARG ARG PHE          
SEQRES  12 E  496  THR MET GLU LEU ALA LYS LYS GLY PHE ILE GLY PRO GLY          
SEQRES  13 E  496  ILE ASP VAL PRO ALA PRO ASP MET SER THR GLY GLU ARG          
SEQRES  14 E  496  GLU MET SER TRP ILE ALA ASP THR TYR ALA SER THR ILE          
SEQRES  15 E  496  GLY HIS TYR ASP ILE ASN ALA HIS ALA CYS VAL THR GLY          
SEQRES  16 E  496  LYS PRO ILE SER GLN GLY GLY ILE HIS GLY ARG ILE SER          
SEQRES  17 E  496  ALA THR GLY ARG GLY VAL PHE HIS GLY ILE GLU ASN PHE          
SEQRES  18 E  496  ILE ASN GLU ALA SER TYR MET SER ILE LEU GLY MET THR          
SEQRES  19 E  496  PRO GLY PHE GLY ASP LYS THR PHE VAL VAL GLN GLY PHE          
SEQRES  20 E  496  GLY ASN VAL GLY LEU HIS SER MET ARG TYR LEU HIS ARG          
SEQRES  21 E  496  PHE GLY ALA LYS CYS ILE ALA VAL GLY GLU SER ASP GLY          
SEQRES  22 E  496  SER ILE TRP ASN PRO ASP GLY ILE ASP PRO LYS GLU LEU          
SEQRES  23 E  496  GLU ASP PHE LYS LEU GLN HIS GLY SER ILE LEU GLY PHE          
SEQRES  24 E  496  PRO LYS ALA LYS PRO TYR GLU GLY SER ILE LEU GLU ALA          
SEQRES  25 E  496  ASP CYS ASP ILE LEU ILE PRO ALA ALA SER GLU LYS GLN          
SEQRES  26 E  496  LEU THR LYS SER ASN ALA PRO ARG VAL LYS ALA LYS ILE          
SEQRES  27 E  496  ILE ALA GLU GLY ALA ASN GLY PRO THR THR PRO GLU ALA          
SEQRES  28 E  496  ASP LYS ILE PHE LEU GLU ARG ASN ILE MET VAL ILE PRO          
SEQRES  29 E  496  ASP LEU TYR LEU ASN ALA GLY GLY VAL THR VAL SER TYR          
SEQRES  30 E  496  PHE GLU TRP LEU LYS ASN LEU ASN HIS VAL SER TYR GLY          
SEQRES  31 E  496  ARG LEU THR PHE LYS TYR GLU ARG ASP SER ASN TYR HIS          
SEQRES  32 E  496  LEU LEU MET SER VAL GLN GLU SER LEU GLU ARG LYS PHE          
SEQRES  33 E  496  GLY LYS HIS GLY GLY THR ILE PRO ILE VAL PRO THR ALA          
SEQRES  34 E  496  GLU PHE GLN ASP ARG ILE SER GLY ALA SER GLU LYS ASP          
SEQRES  35 E  496  ILE VAL TYR SER GLY LEU ALA TYR THR MET GLU ARG SER          
SEQRES  36 E  496  ALA ARG GLN ILE MET ARG THR ALA MET LYS TYR ASN LEU          
SEQRES  37 E  496  GLY LEU ASP LEU ARG THR ALA ALA TYR VAL ASN ALA ILE          
SEQRES  38 E  496  GLU LYS VAL PHE LYS VAL TYR ASN GLU ALA GLY VAL THR          
SEQRES  39 E  496  PHE THR                                                      
SEQRES   1 F  496  ASP PRO ASN PHE PHE LYS MET VAL GLU GLY PHE PHE ASP          
SEQRES   2 F  496  ARG GLY ALA SER ILE VAL GLU ASP LYS LEU VAL GLU ASP          
SEQRES   3 F  496  LEU ARG THR ARG GLU SER GLU GLU GLN LYS ARG ASN ARG          
SEQRES   4 F  496  VAL ARG GLY ILE LEU ARG ILE ILE LYS PRO CYS ASN HIS          
SEQRES   5 F  496  VAL LEU SER LEU SER PHE PRO ILE ARG ARG ASP ASP GLY          
SEQRES   6 F  496  SER TRP GLU VAL ILE GLU GLY TYR ARG ALA GLN HIS SER          
SEQRES   7 F  496  GLN HIS ARG THR PRO CYS LYS GLY GLY ILE ARG TYR SER          
SEQRES   8 F  496  THR ASP VAL SER VAL ASP GLU VAL LYS ALA LEU ALA SER          
SEQRES   9 F  496  LEU MET THR TYR LYS CYS ALA VAL VAL ASP VAL PRO PHE          
SEQRES  10 F  496  GLY GLY ALA LYS ALA GLY VAL LYS ILE ASN PRO LYS ASN          
SEQRES  11 F  496  TYR THR ASP ASN GLU LEU GLU LYS ILE THR ARG ARG PHE          
SEQRES  12 F  496  THR MET GLU LEU ALA LYS LYS GLY PHE ILE GLY PRO GLY          
SEQRES  13 F  496  ILE ASP VAL PRO ALA PRO ASP MET SER THR GLY GLU ARG          
SEQRES  14 F  496  GLU MET SER TRP ILE ALA ASP THR TYR ALA SER THR ILE          
SEQRES  15 F  496  GLY HIS TYR ASP ILE ASN ALA HIS ALA CYS VAL THR GLY          
SEQRES  16 F  496  LYS PRO ILE SER GLN GLY GLY ILE HIS GLY ARG ILE SER          
SEQRES  17 F  496  ALA THR GLY ARG GLY VAL PHE HIS GLY ILE GLU ASN PHE          
SEQRES  18 F  496  ILE ASN GLU ALA SER TYR MET SER ILE LEU GLY MET THR          
SEQRES  19 F  496  PRO GLY PHE GLY ASP LYS THR PHE VAL VAL GLN GLY PHE          
SEQRES  20 F  496  GLY ASN VAL GLY LEU HIS SER MET ARG TYR LEU HIS ARG          
SEQRES  21 F  496  PHE GLY ALA LYS CYS ILE ALA VAL GLY GLU SER ASP GLY          
SEQRES  22 F  496  SER ILE TRP ASN PRO ASP GLY ILE ASP PRO LYS GLU LEU          
SEQRES  23 F  496  GLU ASP PHE LYS LEU GLN HIS GLY SER ILE LEU GLY PHE          
SEQRES  24 F  496  PRO LYS ALA LYS PRO TYR GLU GLY SER ILE LEU GLU ALA          
SEQRES  25 F  496  ASP CYS ASP ILE LEU ILE PRO ALA ALA SER GLU LYS GLN          
SEQRES  26 F  496  LEU THR LYS SER ASN ALA PRO ARG VAL LYS ALA LYS ILE          
SEQRES  27 F  496  ILE ALA GLU GLY ALA ASN GLY PRO THR THR PRO GLU ALA          
SEQRES  28 F  496  ASP LYS ILE PHE LEU GLU ARG ASN ILE MET VAL ILE PRO          
SEQRES  29 F  496  ASP LEU TYR LEU ASN ALA GLY GLY VAL THR VAL SER TYR          
SEQRES  30 F  496  PHE GLU TRP LEU LYS ASN LEU ASN HIS VAL SER TYR GLY          
SEQRES  31 F  496  ARG LEU THR PHE LYS TYR GLU ARG ASP SER ASN TYR HIS          
SEQRES  32 F  496  LEU LEU MET SER VAL GLN GLU SER LEU GLU ARG LYS PHE          
SEQRES  33 F  496  GLY LYS HIS GLY GLY THR ILE PRO ILE VAL PRO THR ALA          
SEQRES  34 F  496  GLU PHE GLN ASP ARG ILE SER GLY ALA SER GLU LYS ASP          
SEQRES  35 F  496  ILE VAL TYR SER GLY LEU ALA TYR THR MET GLU ARG SER          
SEQRES  36 F  496  ALA ARG GLN ILE MET ARG THR ALA MET LYS TYR ASN LEU          
SEQRES  37 F  496  GLY LEU ASP LEU ARG THR ALA ALA TYR VAL ASN ALA ILE          
SEQRES  38 F  496  GLU LYS VAL PHE LYS VAL TYR ASN GLU ALA GLY VAL THR          
SEQRES  39 F  496  PHE THR                                                      
HET    PO4  A1001       5                                                       
HET    PO4  B 601       5                                                       
HET    PO4  B 602       5                                                       
HET    PO4  C 601       5                                                       
HET    PO4  C 602       5                                                       
HET    PO4  D 601       5                                                       
HET    PO4  D 602       5                                                       
HET    PO4  D 603       5                                                       
HET    PO4  E 601       5                                                       
HET    PO4  E 602       5                                                       
HET    PO4  E 603       5                                                       
HET    PO4  F2001       5                                                       
HET    PO4  F2002       5                                                       
HET    PO4  F2003       5                                                       
HET    PO4  F2004       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   7  PO4    15(O4 P 3-)                                                  
FORMUL  22  HOH   *260(H2 O)                                                    
HELIX    1 AA1 PHE A   14  GLU A   34  1                                  21    
HELIX    2 AA2 LYS A   45  LYS A   57  1                                  13    
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  ILE A  239  1                                   7    
HELIX   11 AB2 GLY A  257  ARG A  269  1                                  13    
HELIX   12 AB3 ASP A  291  HIS A  302  1                                  12    
HELIX   13 AB4 SER A  317  ALA 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  GLY A  446  1                                  10    
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 PHE B   14  GLU B   34  1                                  21    
HELIX   23 AC5 LYS B   45  LYS B   57  1                                  13    
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  ILE B  239  1                                   7    
HELIX   32 AD5 GLY B  257  ARG B  269  1                                  13    
HELIX   33 AD6 ASP B  291  HIS B  302  1                                  12    
HELIX   34 AD7 SER B  317  ALA B  321  5                                   5    
HELIX   35 AD8 ASN B  339  VAL B  343  5                                   5    
HELIX   36 AD9 THR B  357  ARG B  367  1                                  11    
HELIX   37 AE1 PRO B  373  ASN B  378  1                                   6    
HELIX   38 AE2 ALA B  379  HIS B  395  1                                  17    
HELIX   39 AE3 THR B  402  PHE B  425  1                                  24    
HELIX   40 AE4 THR B  437  GLY B  446  1                                  10    
HELIX   41 AE5 SER B  448  TYR B  475  1                                  28    
HELIX   42 AE6 ASP B  480  GLU B  499  1                                  20    
HELIX   43 AE7 PHE C   14  GLU C   34  1                                  21    
HELIX   44 AE8 LYS C   45  LYS C   57  1                                  13    
HELIX   45 AE9 SER C  104  VAL C  122  1                                  19    
HELIX   46 AF1 ASN C  136  TYR C  140  5                                   5    
HELIX   47 AF2 THR C  141  LYS C  159  1                                  19    
HELIX   48 AF3 GLY C  176  THR C  190  1                                  15    
HELIX   49 AF4 ASN C  197  VAL C  202  5                                   6    
HELIX   50 AF5 PRO C  206  GLY C  210  5                                   5    
HELIX   51 AF6 SER C  217  ASN C  232  1                                  16    
HELIX   52 AF7 GLU C  233  ILE C  239  1                                   7    
HELIX   53 AF8 GLY C  257  ARG C  269  1                                  13    
HELIX   54 AF9 ASP C  291  HIS C  302  1                                  12    
HELIX   55 AG1 SER C  317  ALA C  321  5                                   5    
HELIX   56 AG2 ASN C  339  VAL C  343  5                                   5    
HELIX   57 AG3 THR C  357  ARG C  367  1                                  11    
HELIX   58 AG4 PRO C  373  ASN C  378  1                                   6    
HELIX   59 AG5 ALA C  379  HIS C  395  1                                  17    
HELIX   60 AG6 THR C  402  PHE C  425  1                                  24    
HELIX   61 AG7 THR C  437  GLY C  446  1                                  10    
HELIX   62 AG8 SER C  448  TYR C  475  1                                  28    
HELIX   63 AG9 ASP C  480  GLU C  499  1                                  20    
HELIX   64 AH1 PHE D   14  GLU D   34  1                                  21    
HELIX   65 AH2 LYS D   45  LYS D   57  1                                  13    
HELIX   66 AH3 SER D  104  VAL D  122  1                                  19    
HELIX   67 AH4 ASN D  136  TYR D  140  5                                   5    
HELIX   68 AH5 THR D  141  LYS D  159  1                                  19    
HELIX   69 AH6 GLY D  176  THR D  190  1                                  15    
HELIX   70 AH7 ASN D  197  VAL D  202  5                                   6    
HELIX   71 AH8 PRO D  206  GLY D  210  5                                   5    
HELIX   72 AH9 SER D  217  ASN D  232  1                                  16    
HELIX   73 AI1 GLU D  233  ILE D  239  1                                   7    
HELIX   74 AI2 GLY D  257  ARG D  269  1                                  13    
HELIX   75 AI3 ASP D  291  HIS D  302  1                                  12    
HELIX   76 AI4 SER D  317  ALA D  321  5                                   5    
HELIX   77 AI5 ASN D  339  VAL D  343  5                                   5    
HELIX   78 AI6 THR D  357  ARG D  367  1                                  11    
HELIX   79 AI7 PRO D  373  ASN D  378  1                                   6    
HELIX   80 AI8 ALA D  379  HIS D  395  1                                  17    
HELIX   81 AI9 THR D  402  PHE D  425  1                                  24    
HELIX   82 AJ1 THR D  437  GLY D  446  1                                  10    
HELIX   83 AJ2 SER D  448  TYR D  475  1                                  28    
HELIX   84 AJ3 ASP D  480  GLU D  499  1                                  20    
HELIX   85 AJ4 PHE E   14  GLU E   34  1                                  21    
HELIX   86 AJ5 LYS E   45  LYS E   57  1                                  13    
HELIX   87 AJ6 SER E  104  VAL E  122  1                                  19    
HELIX   88 AJ7 ASN E  136  TYR E  140  5                                   5    
HELIX   89 AJ8 THR E  141  LYS E  159  1                                  19    
HELIX   90 AJ9 GLY E  176  THR E  190  1                                  15    
HELIX   91 AK1 ASN E  197  VAL E  202  5                                   6    
HELIX   92 AK2 PRO E  206  GLY E  210  5                                   5    
HELIX   93 AK3 SER E  217  ASN E  232  1                                  16    
HELIX   94 AK4 GLU E  233  ILE E  239  1                                   7    
HELIX   95 AK5 GLY E  257  PHE E  270  1                                  14    
HELIX   96 AK6 ASP E  291  HIS E  302  1                                  12    
HELIX   97 AK7 SER E  317  ALA E  321  5                                   5    
HELIX   98 AK8 ASN E  339  VAL E  343  5                                   5    
HELIX   99 AK9 THR E  357  ARG E  367  1                                  11    
HELIX  100 AL1 PRO E  373  ASN E  378  1                                   6    
HELIX  101 AL2 ALA E  379  HIS E  395  1                                  17    
HELIX  102 AL3 THR E  402  PHE E  425  1                                  24    
HELIX  103 AL4 THR E  437  GLY E  446  1                                  10    
HELIX  104 AL5 SER E  448  TYR E  475  1                                  28    
HELIX  105 AL6 ASP E  480  GLU E  499  1                                  20    
HELIX  106 AL7 PHE F   14  GLU F   34  1                                  21    
HELIX  107 AL8 LYS F   45  LYS F   57  1                                  13    
HELIX  108 AL9 SER F  104  VAL F  122  1                                  19    
HELIX  109 AM1 ASN F  136  TYR F  140  5                                   5    
HELIX  110 AM2 THR F  141  LYS F  159  1                                  19    
HELIX  111 AM3 GLY F  176  THR F  190  1                                  15    
HELIX  112 AM4 ASN F  197  VAL F  202  5                                   6    
HELIX  113 AM5 PRO F  206  GLY F  210  5                                   5    
HELIX  114 AM6 SER F  217  ASN F  232  1                                  16    
HELIX  115 AM7 GLU F  233  ILE F  239  1                                   7    
HELIX  116 AM8 GLY F  257  ARG F  269  1                                  13    
HELIX  117 AM9 ASP F  291  HIS F  302  1                                  12    
HELIX  118 AN1 SER F  317  ALA F  321  5                                   5    
HELIX  119 AN2 ASN F  339  VAL F  343  5                                   5    
HELIX  120 AN3 THR F  357  ARG F  367  1                                  11    
HELIX  121 AN4 PRO F  373  ASN F  378  1                                   6    
HELIX  122 AN5 ALA F  379  HIS F  395  1                                  17    
HELIX  123 AN6 THR F  402  PHE F  425  1                                  24    
HELIX  124 AN7 THR F  437  GLY F  446  1                                  10    
HELIX  125 AN8 SER F  448  TYR F  475  1                                  28    
HELIX  126 AN9 ASP F  480  GLU F  499  1                                  20    
SHEET    1 AA110 ASP A 167  ALA A 170  0                                        
SHEET    2 AA110 CYS A  93  TYR A  99  1  N  CYS A  93   O  VAL A 168           
SHEET    3 AA110 GLY A 127  VAL A 133  1  O  VAL A 133   N  ARG A  98           
SHEET    4 AA110 TRP A  76  GLN A  85 -1  N  TYR A  82   O  GLY A 132           
SHEET    5 AA110 HIS A  61  ARG A  70 -1  N  LEU A  65   O  GLY A  81           
SHEET    6 AA110 HIS E  61  ARG E  70 -1  O  SER E  64   N  VAL A  62           
SHEET    7 AA110 TRP E  76  GLN E  85 -1  O  GLY E  81   N  LEU E  65           
SHEET    8 AA110 GLY E 127  VAL E 133 -1  O  LYS E 130   N  ALA E  84           
SHEET    9 AA110 CYS E  93  TYR E  99  1  N  ARG E  98   O  VAL E 133           
SHEET   10 AA110 ASP E 167  ALA E 170  1  O  VAL E 168   N  CYS E  93           
SHEET    1 AA2 7 LYS A 312  PRO A 313  0                                        
SHEET    2 AA2 7 SER A 283  TRP A 285 -1  N  TRP A 285   O  LYS A 312           
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  VAL A 253   O  ALA A 276           
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 MET A 370  ILE A 372  1  O  MET A 370   N  ILE A 348           
SHEET    1 AA310 ASP B 167  ALA B 170  0                                        
SHEET    2 AA310 CYS B  93  TYR B  99  1  N  CYS B  93   O  VAL B 168           
SHEET    3 AA310 GLY B 127  VAL B 133  1  O  VAL B 133   N  ARG B  98           
SHEET    4 AA310 TRP B  76  GLN B  85 -1  N  ALA B  84   O  LYS B 130           
SHEET    5 AA310 HIS B  61  ARG B  70 -1  N  LEU B  65   O  GLY B  81           
SHEET    6 AA310 HIS D  61  ARG D  70 -1  O  VAL D  62   N  SER B  64           
SHEET    7 AA310 TRP D  76  GLN D  85 -1  O  GLY D  81   N  LEU D  65           
SHEET    8 AA310 GLY D 127  VAL D 133 -1  O  LYS D 130   N  ALA D  84           
SHEET    9 AA310 CYS D  93  TYR D  99  1  N  ARG D  98   O  VAL D 133           
SHEET   10 AA310 ASP D 167  ALA D 170  1  O  VAL D 168   N  CYS D  93           
SHEET    1 AA4 7 LYS B 312  PRO B 313  0                                        
SHEET    2 AA4 7 SER B 283  TRP B 285 -1  N  TRP B 285   O  LYS B 312           
SHEET    3 AA4 7 LYS B 273  GLY B 278 -1  N  VAL B 277   O  ILE B 284           
SHEET    4 AA4 7 THR B 250  GLN B 254  1  N  VAL B 253   O  ALA B 276           
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 MET B 370  ILE B 372  1  O  MET B 370   N  ILE B 348           
SHEET    1 AA510 ASP C 167  ALA C 170  0                                        
SHEET    2 AA510 CYS C  93  TYR C  99  1  N  CYS C  93   O  VAL C 168           
SHEET    3 AA510 GLY C 127  VAL C 133  1  O  VAL C 133   N  ARG C  98           
SHEET    4 AA510 TRP C  76  GLN C  85 -1  N  TYR C  82   O  GLY C 132           
SHEET    5 AA510 HIS C  61  ARG C  70 -1  N  HIS C  61   O  GLN C  85           
SHEET    6 AA510 HIS F  61  ARG F  70 -1  O  SER F  64   N  VAL C  62           
SHEET    7 AA510 TRP F  76  GLN F  85 -1  O  GLY F  81   N  LEU F  65           
SHEET    8 AA510 GLY F 127  VAL F 133 -1  O  LYS F 130   N  ALA F  84           
SHEET    9 AA510 CYS F  93  TYR F  99  1  N  ARG F  98   O  VAL F 133           
SHEET   10 AA510 ASP F 167  ALA F 170  1  O  VAL F 168   N  CYS F  93           
SHEET    1 AA6 7 LYS C 312  PRO C 313  0                                        
SHEET    2 AA6 7 SER C 283  TRP C 285 -1  N  TRP C 285   O  LYS C 312           
SHEET    3 AA6 7 LYS C 273  GLY C 278 -1  N  VAL C 277   O  ILE C 284           
SHEET    4 AA6 7 THR C 250  GLN C 254  1  N  VAL C 253   O  ALA C 276           
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 MET C 370  ILE C 372  1  O  MET C 370   N  ILE C 348           
SHEET    1 AA7 7 LYS D 312  PRO D 313  0                                        
SHEET    2 AA7 7 SER D 283  TRP D 285 -1  N  TRP D 285   O  LYS D 312           
SHEET    3 AA7 7 LYS D 273  GLY D 278 -1  N  VAL D 277   O  ILE D 284           
SHEET    4 AA7 7 THR D 250  GLN D 254  1  N  VAL D 253   O  ALA D 276           
SHEET    5 AA7 7 ILE D 325  PRO D 328  1  O  ILE D 327   N  VAL D 252           
SHEET    6 AA7 7 ILE D 347  ALA D 349  1  O  ILE D 347   N  LEU D 326           
SHEET    7 AA7 7 MET D 370  ILE D 372  1  O  MET D 370   N  ILE D 348           
SHEET    1 AA8 7 LYS E 312  PRO E 313  0                                        
SHEET    2 AA8 7 SER E 283  TRP E 285 -1  N  TRP E 285   O  LYS E 312           
SHEET    3 AA8 7 LYS E 273  GLY E 278 -1  N  VAL E 277   O  ILE E 284           
SHEET    4 AA8 7 THR E 250  GLN E 254  1  N  VAL E 253   O  ALA E 276           
SHEET    5 AA8 7 ILE E 325  PRO E 328  1  O  ILE E 327   N  VAL E 252           
SHEET    6 AA8 7 ILE E 347  ALA E 349  1  O  ILE E 347   N  LEU E 326           
SHEET    7 AA8 7 MET E 370  ILE E 372  1  O  MET E 370   N  ILE E 348           
SHEET    1 AA9 7 LYS F 312  PRO F 313  0                                        
SHEET    2 AA9 7 SER F 283  TRP F 285 -1  N  TRP F 285   O  LYS F 312           
SHEET    3 AA9 7 LYS F 273  GLY F 278 -1  N  VAL F 277   O  ILE F 284           
SHEET    4 AA9 7 THR F 250  GLN F 254  1  N  VAL F 253   O  ALA F 276           
SHEET    5 AA9 7 ILE F 325  PRO F 328  1  O  ILE F 327   N  VAL F 252           
SHEET    6 AA9 7 ILE F 347  ALA F 349  1  O  ILE F 347   N  LEU F 326           
SHEET    7 AA9 7 MET F 370  ILE F 372  1  O  MET F 370   N  ILE F 348           
CISPEP   1 THR B   91    PRO B   92          0         0.79                     
CISPEP   2 THR C   91    PRO C   92          0        -1.74                     
CISPEP   3 THR D   91    PRO D   92          0         0.47                     
CISPEP   4 THR E   91    PRO E   92          0         2.28                     
SITE     1 AC1  5 ARG A 463  HOH A1102  HOH A1103  SER B 397                    
SITE     2 AC1  5 HOH B 709                                                     
SITE     1 AC2  2 HIS B 213  LYS B 450                                          
SITE     1 AC3  4 ARG B 265  TYR B 266  ARG B 269  TYR B 454                    
SITE     1 AC4  8 SER C 217  ARG C 221  ARG C 265  TYR C 266                    
SITE     2 AC4  8 ARG C 269  LYS C 450  TYR C 454  HOH C 710                    
SITE     1 AC5  3 HIS C 213  LYS C 391  HOH C 721                               
SITE     1 AC6  3 ILE D 207  HIS D 213  GLY D 214                               
SITE     1 AC7  4 ARG D 221  ARG D 265  TYR D 266  ARG D 269                    
SITE     1 AC8  7 ASP C 123  ARG C 463  HOH C 727  SER D 397                    
SITE     2 AC8  7 ARG D 400  HOH D 708  HOH D 733                               
SITE     1 AC9  2 HIS E 213  GLY E 214                                          
SITE     1 AD1  5 ARG E 221  ARG E 265  TYR E 266  ARG E 269                    
SITE     2 AD1  5 TYR E 454                                                     
SITE     1 AD2  3 ARG D 463  SER E 397  ARG E 400                               
SITE     1 AD3  3 HIS F 213  GLY F 214  LYS F 450                               
SITE     1 AD4  7 SER F 217  ARG F 221  ARG F 265  TYR F 266                    
SITE     2 AD4  7 ARG F 269  LYS F 450  TYR F 454                               
SITE     1 AD5  6 ARG B 463  HIS F 213  LYS F 391  SER F 397                    
SITE     2 AD5  6 HOH F2102  HOH F2119                                          
SITE     1 AD6  6 SER A 397  ARG A 400  ASP F 123  ARG F 463                    
SITE     2 AD6  6 HOH F2123  HOH F2127                                          
CRYST1   96.803   98.380  124.300  85.94  69.35  61.00 P 1           6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010330 -0.005726 -0.004629        0.00000                         
SCALE2      0.000000  0.011622  0.001433        0.00000                         
SCALE3      0.000000  0.000000  0.008663        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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