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Database: PDB
Entry: 1L1F
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Original site: 1L1F 
HEADER    OXIDOREDUCTASE                          15-FEB-02   1L1F              
TITLE     STRUCTURE OF HUMAN GLUTAMATE DEHYDROGENASE-APO FORM                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE DEHYDROGENASE 1;                                 
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: GDH;                                                        
COMPND   5 EC: 1.4.1.3;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALLOSTERY, NEGATIVE COOPERATIVITY, OXIDOREDUCTASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.J.SMITH,T.SCHMIDT,J.FANG,J.WU,G.SIUZDAK,C.A.STANLEY                 
REVDAT   3   24-FEB-09 1L1F    1       VERSN                                    
REVDAT   2   15-MAY-02 1L1F    1       JRNL   AUTHOR                            
REVDAT   1   06-MAR-02 1L1F    0                                                
JRNL        AUTH   T.J.SMITH,T.SCHMIDT,J.FANG,J.WU,G.SIUZDAK,                   
JRNL        AUTH 2 C.A.STANLEY                                                  
JRNL        TITL   THE STRUCTURE OF APO HUMAN GLUTAMATE DEHYDROGENASE           
JRNL        TITL 2 DETAILS SUBUNIT COMMUNICATION AND ALLOSTERY.                 
JRNL        REF    J.MOL.BIOL.                   V. 318   765 2002              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12054821                                                     
JRNL        DOI    10.1016/S0022-2836(02)00161-4                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : O                                                    
REMARK   3   AUTHORS     : JONES,ZOU,COWAN,KJELDGAARD                           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 78217                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : 5%, X-PLOR                      
REMARK   3   R VALUE            (WORKING SET) : 0.262                           
REMARK   3   FREE R VALUE                     : 0.302                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 30                              
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 23244                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1L1F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB015553.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-FEB-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 7                                  
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 RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 91356                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, NACL, SODIUM PHOSPHATE,        
REMARK 280  SODIUM AZIDE, OCTYL-B-GLUCOPYRANOSIDE, METHYL PENTANEDIOL, PH       
REMARK 280  7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                  
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: 30360 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 103940 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 NAD binding domain orientation differs among                         
REMARK 400 the six chains.                                                      
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     ALA A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     ALA 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     SER C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     ALA 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     SER D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     VAL D     4                                                      
REMARK 465     ALA D     5                                                      
REMARK 465     ASP D     6                                                      
REMARK 465     ARG D     7                                                      
REMARK 465     GLU D     8                                                      
REMARK 465     ASP D     9                                                      
REMARK 465     SER E     1                                                      
REMARK 465     GLU E     2                                                      
REMARK 465     ALA 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     SER F     1                                                      
REMARK 465     GLU F     2                                                      
REMARK 465     ALA F     3                                                      
REMARK 465     VAL F     4                                                      
REMARK 465     ALA F     5                                                      
REMARK 465     ASP F     6                                                      
REMARK 465     ARG F     7                                                      
REMARK 465     GLU F     8                                                      
REMARK 465     ASP F     9                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A  59   CB    CYS A  59   SG      0.133                       
REMARK 500    CYS B  59   CB    CYS B  59   SG      0.127                       
REMARK 500    CYS C  59   CB    CYS C  59   SG      0.142                       
REMARK 500    CYS C 201   CB    CYS C 201   SG     -0.098                       
REMARK 500    CYS D  59   CB    CYS D  59   SG      0.151                       
REMARK 500    CYS E  59   CB    CYS E  59   SG      0.105                       
REMARK 500    CYS F 201   CB    CYS F 201   SG     -0.115                       
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    LEU A 326   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    PHE A 504   N   -  CA  -  C   ANGL. DEV. = -19.4 DEGREES          
REMARK 500    THR B  91   N   -  CA  -  C   ANGL. DEV. =  16.3 DEGREES          
REMARK 500    LEU B 326   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    PHE B 504   N   -  CA  -  C   ANGL. DEV. = -19.6 DEGREES          
REMARK 500    THR C  91   N   -  CA  -  C   ANGL. DEV. =  16.3 DEGREES          
REMARK 500    LEU C 326   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    PHE C 504   N   -  CA  -  C   ANGL. DEV. = -19.7 DEGREES          
REMARK 500    LEU D 326   CA  -  CB  -  CG  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    PHE D 504   N   -  CA  -  C   ANGL. DEV. = -19.4 DEGREES          
REMARK 500    LEU E 326   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    PHE E 504   N   -  CA  -  C   ANGL. DEV. = -19.7 DEGREES          
REMARK 500    LEU F 326   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    PHE F 504   N   -  CA  -  C   ANGL. DEV. = -19.6 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      -39.01    -39.13                                   
REMARK 500    GLU A  34     -124.03    -45.94                                   
REMARK 500    ASP A  35      -29.31    -38.43                                   
REMARK 500    GLU A  40       47.80   -109.88                                   
REMARK 500    SER A  41       69.48    -53.70                                   
REMARK 500    GLU A  43       -0.34     65.72                                   
REMARK 500    GLN A  44       18.70     53.70                                   
REMARK 500    LYS A  45       37.35    -85.14                                   
REMARK 500    CYS A  59      109.30    -56.97                                   
REMARK 500    ASP A  72      -34.46    -38.31                                   
REMARK 500    THR A  91      -94.41    -33.70                                   
REMARK 500    ASP A 102       -1.93    173.35                                   
REMARK 500    PRO A 125       60.97    -65.30                                   
REMARK 500    LYS A 134       80.57    -64.32                                   
REMARK 500    ILE A 162       -7.42   -152.39                                   
REMARK 500    ILE A 166      -55.17   -125.33                                   
REMARK 500    PRO A 169     -177.40    -60.26                                   
REMARK 500    THR A 190      -95.76   -121.10                                   
REMARK 500    ALA A 234      -75.28    -49.38                                   
REMARK 500    ASP A 248     -102.80     49.91                                   
REMARK 500    ASN A 258      -61.67    -10.30                                   
REMARK 500    GLU A 279     -154.11   -145.77                                   
REMARK 500    ASP A 281     -119.49    -86.99                                   
REMARK 500    ASN A 286      102.33    168.28                                   
REMARK 500    HIS A 302      116.16   -173.21                                   
REMARK 500    LYS A 310       33.45     75.36                                   
REMARK 500    PRO A 313       89.66    -55.98                                   
REMARK 500    ALA A 329       50.98   -101.41                                   
REMARK 500    SER A 331      135.87     -2.98                                   
REMARK 500    LYS A 333       81.40     21.75                                   
REMARK 500    HIS A 395       31.09     70.09                                   
REMARK 500    LYS A 424       54.21   -114.90                                   
REMARK 500    PHE A 425      163.74    164.14                                   
REMARK 500    HIS A 428       73.55   -161.51                                   
REMARK 500    ILE A 432       79.82   -110.64                                   
REMARK 500    ILE A 434      -22.60    -35.62                                   
REMARK 500    GLU A 499       44.43    -88.73                                   
REMARK 500    ALA A 500      -87.62   -166.31                                   
REMARK 500    VAL A 502      -68.21   -148.46                                   
REMARK 500    PHE A 504       60.93   -100.67                                   
REMARK 500    PHE B  13      -38.64    -39.04                                   
REMARK 500    GLU B  34     -124.43    -45.96                                   
REMARK 500    ASP B  35      -29.59    -38.19                                   
REMARK 500    GLU B  40       47.65   -109.61                                   
REMARK 500    SER B  41       69.91    -53.87                                   
REMARK 500    GLU B  43       -0.43     65.59                                   
REMARK 500    GLN B  44       18.38     53.91                                   
REMARK 500    LYS B  45       37.25    -84.98                                   
REMARK 500    ASP B  72      -34.65    -37.79                                   
REMARK 500    THR B  91      -94.55    -33.76                                   
REMARK 500    ASP B 102       -1.98    173.62                                   
REMARK 500    PRO B 125       61.45    -64.60                                   
REMARK 500    LYS B 134       79.86    -64.02                                   
REMARK 500    ILE B 162       -6.15   -153.05                                   
REMARK 500    ILE B 166      -53.84   -124.06                                   
REMARK 500    PRO B 169     -177.88    -60.19                                   
REMARK 500    GLU B 177      -18.75    -49.52                                   
REMARK 500    THR B 190      -96.38   -123.16                                   
REMARK 500    ALA B 234      -75.98    -48.79                                   
REMARK 500    ASP B 248     -102.69     49.90                                   
REMARK 500    ASN B 258      -61.56    -10.56                                   
REMARK 500    GLU B 279     -153.97   -146.22                                   
REMARK 500    ASP B 281     -119.37    -87.16                                   
REMARK 500    ASN B 286      102.25    168.71                                   
REMARK 500    HIS B 302      115.99   -173.41                                   
REMARK 500    LYS B 310       33.22     75.27                                   
REMARK 500    PRO B 313       89.05    -56.08                                   
REMARK 500    ALA B 329       51.56   -101.25                                   
REMARK 500    SER B 331      136.11     -3.19                                   
REMARK 500    LYS B 333       80.66     21.58                                   
REMARK 500    LYS B 424       54.45   -114.50                                   
REMARK 500    PHE B 425      163.37    163.99                                   
REMARK 500    HIS B 428       73.29   -161.68                                   
REMARK 500    ILE B 432       78.98   -109.67                                   
REMARK 500    ILE B 434      -22.83    -35.93                                   
REMARK 500    ASN B 476       29.84     47.95                                   
REMARK 500    GLU B 499       44.31    -88.75                                   
REMARK 500    ALA B 500      -87.52   -166.71                                   
REMARK 500    VAL B 502      -68.14   -148.43                                   
REMARK 500    PHE B 504       61.15   -100.97                                   
REMARK 500    PHE C  13      -38.75    -38.98                                   
REMARK 500    GLU C  34     -124.50    -45.81                                   
REMARK 500    ASP C  35      -29.57    -38.14                                   
REMARK 500    GLU C  40       47.33   -109.64                                   
REMARK 500    SER C  41       69.65    -53.41                                   
REMARK 500    GLU C  43       -0.47     65.83                                   
REMARK 500    GLN C  44       18.49     53.81                                   
REMARK 500    LYS C  45       37.40    -84.94                                   
REMARK 500    CYS C  59      108.85    -56.30                                   
REMARK 500    ASP C  72      -34.36    -38.25                                   
REMARK 500    THR C  91      -94.10    -34.07                                   
REMARK 500    ASP C 102       -2.02    173.82                                   
REMARK 500    PRO C 125       61.22    -64.37                                   
REMARK 500    LYS C 134       80.27    -64.23                                   
REMARK 500    ILE C 162       -7.03   -152.91                                   
REMARK 500    ILE C 166      -56.20   -123.86                                   
REMARK 500    PRO C 169     -177.97    -60.38                                   
REMARK 500    GLU C 177      -18.19    -49.24                                   
REMARK 500    THR C 190      -96.26   -121.94                                   
REMARK 500    ALA C 234      -75.20    -49.72                                   
REMARK 500    ASP C 248     -102.96     49.97                                   
REMARK 500    ASN C 258      -61.50    -10.40                                   
REMARK 500    GLU C 279     -154.17   -145.58                                   
REMARK 500    ASP C 281     -119.46    -87.17                                   
REMARK 500    ASN C 286      102.18    168.25                                   
REMARK 500    HIS C 302      116.45   -173.22                                   
REMARK 500    LYS C 310       33.29     75.36                                   
REMARK 500    PRO C 313       89.63    -55.89                                   
REMARK 500    ALA C 329       51.27   -101.61                                   
REMARK 500    SER C 331      135.89     -2.72                                   
REMARK 500    LYS C 333       81.55     21.79                                   
REMARK 500    LYS C 424       54.29   -114.95                                   
REMARK 500    PHE C 425      163.29    164.07                                   
REMARK 500    HIS C 428       73.53   -161.77                                   
REMARK 500    ILE C 432       79.08   -109.42                                   
REMARK 500    ILE C 434      -22.16    -36.61                                   
REMARK 500    ASN C 476       29.86     47.91                                   
REMARK 500    GLU C 499       44.52    -89.08                                   
REMARK 500    ALA C 500      -87.63   -166.20                                   
REMARK 500    VAL C 502      -68.19   -148.62                                   
REMARK 500    PHE C 504       61.03   -100.94                                   
REMARK 500    PHE D  13      -38.89    -38.75                                   
REMARK 500    GLU D  34     -124.28    -45.73                                   
REMARK 500    ASP D  35      -29.61    -38.23                                   
REMARK 500    GLU D  40       47.69   -109.75                                   
REMARK 500    SER D  41       69.71    -53.64                                   
REMARK 500    GLU D  43       -0.29     65.40                                   
REMARK 500    GLN D  44       18.42     53.57                                   
REMARK 500    LYS D  45       37.23    -84.97                                   
REMARK 500    CYS D  59      109.15    -56.35                                   
REMARK 500    ASP D  72      -34.71    -38.42                                   
REMARK 500    THR D  91      -94.52    -33.40                                   
REMARK 500    ASP D 102       -2.03    174.20                                   
REMARK 500    PRO D 125       60.20    -64.73                                   
REMARK 500    LYS D 134       80.39    -64.62                                   
REMARK 500    ILE D 162       -7.40   -152.55                                   
REMARK 500    ILE D 166      -54.93   -124.98                                   
REMARK 500    PRO D 169     -177.28    -59.81                                   
REMARK 500    THR D 190      -94.92   -123.05                                   
REMARK 500    ALA D 234      -74.83    -49.96                                   
REMARK 500    ASP D 248     -102.91     50.17                                   
REMARK 500    ASN D 258      -61.49    -10.56                                   
REMARK 500    GLU D 279     -153.97   -146.01                                   
REMARK 500    ASP D 281     -119.44    -87.03                                   
REMARK 500    ASN D 286      102.30    168.73                                   
REMARK 500    HIS D 302      115.90   -173.09                                   
REMARK 500    LYS D 310       33.39     75.75                                   
REMARK 500    PRO D 313       89.31    -56.28                                   
REMARK 500    ALA D 329       51.84   -102.62                                   
REMARK 500    SER D 331      135.97     -3.41                                   
REMARK 500    LYS D 333       81.31     21.63                                   
REMARK 500    LYS D 424       54.15   -114.84                                   
REMARK 500    PHE D 425      163.68    164.13                                   
REMARK 500    HIS D 428       73.47   -161.58                                   
REMARK 500    ILE D 432       78.77   -109.72                                   
REMARK 500    ILE D 434      -22.81    -35.99                                   
REMARK 500    ASN D 476       29.67     48.05                                   
REMARK 500    GLU D 499       44.04    -88.59                                   
REMARK 500    ALA D 500      -87.59   -166.08                                   
REMARK 500    VAL D 502      -68.24   -148.59                                   
REMARK 500    PHE D 504       60.91   -100.82                                   
REMARK 500    PHE E  13      -38.91    -39.14                                   
REMARK 500    GLU E  34     -124.52    -45.85                                   
REMARK 500    ASP E  35      -29.37    -38.21                                   
REMARK 500    GLU E  40       47.74   -109.63                                   
REMARK 500    SER E  41       69.53    -53.70                                   
REMARK 500    GLU E  43       -0.23     65.68                                   
REMARK 500    GLN E  44       18.69     53.50                                   
REMARK 500    LYS E  45       37.21    -84.84                                   
REMARK 500    CYS E  59      109.34    -57.47                                   
REMARK 500    ASP E  72      -34.49    -38.29                                   
REMARK 500    THR E  91      -93.70    -34.15                                   
REMARK 500    ASP E 102       -1.97    174.10                                   
REMARK 500    PRO E 125       60.47    -64.45                                   
REMARK 500    LYS E 134       80.07    -64.30                                   
REMARK 500    ILE E 162       -7.17   -153.89                                   
REMARK 500    ILE E 166      -54.10   -126.02                                   
REMARK 500    PRO E 169     -177.78    -59.58                                   
REMARK 500    GLU E 177      -18.84    -49.75                                   
REMARK 500    THR E 190      -96.10   -121.60                                   
REMARK 500    ALA E 234      -74.87    -49.23                                   
REMARK 500    ASP E 248     -102.84     49.87                                   
REMARK 500    ASN E 258      -61.57    -10.34                                   
REMARK 500    GLU E 279     -153.99   -146.04                                   
REMARK 500    ASP E 281     -119.14    -87.33                                   
REMARK 500    ASN E 286      102.33    168.84                                   
REMARK 500    HIS E 302      115.88   -173.30                                   
REMARK 500    LYS E 310       33.48     75.96                                   
REMARK 500    PRO E 313       89.31    -56.03                                   
REMARK 500    ALA E 329       51.31   -101.26                                   
REMARK 500    SER E 331      136.10     -3.12                                   
REMARK 500    LYS E 333       81.12     21.75                                   
REMARK 500    LYS E 424       54.33   -114.47                                   
REMARK 500    PHE E 425      163.33    163.93                                   
REMARK 500    HIS E 428       73.41   -161.67                                   
REMARK 500    ILE E 432       78.77   -110.13                                   
REMARK 500    ILE E 434      -22.83    -35.37                                   
REMARK 500    GLU E 499       44.22    -88.82                                   
REMARK 500    ALA E 500      -87.73   -166.32                                   
REMARK 500    VAL E 502      -68.17   -147.57                                   
REMARK 500    PHE E 504       61.09   -100.93                                   
REMARK 500    PHE F  13      -39.34    -38.83                                   
REMARK 500    GLU F  34     -124.46    -45.72                                   
REMARK 500    ASP F  35      -29.47    -38.28                                   
REMARK 500    GLU F  40       47.66   -109.78                                   
REMARK 500    SER F  41       69.58    -53.50                                   
REMARK 500    GLU F  43       -0.28     65.58                                   
REMARK 500    GLN F  44       18.67     53.70                                   
REMARK 500    LYS F  45       37.21    -85.04                                   
REMARK 500    CYS F  59      108.64    -56.70                                   
REMARK 500    ASP F  72      -34.56    -38.60                                   
REMARK 500    THR F  91      -93.96    -33.90                                   
REMARK 500    ASP F 102       -1.61    173.41                                   
REMARK 500    PRO F 125       60.27    -64.01                                   
REMARK 500    LYS F 134       80.91    -64.82                                   
REMARK 500    ILE F 162       -7.59   -152.45                                   
REMARK 500    ILE F 166      -55.76   -124.77                                   
REMARK 500    PRO F 169     -178.03    -60.27                                   
REMARK 500    GLU F 177      -19.43    -49.92                                   
REMARK 500    THR F 190      -95.62   -121.94                                   
REMARK 500    ALA F 234      -75.25    -49.99                                   
REMARK 500    ASP F 248     -103.16     49.92                                   
REMARK 500    ASN F 258      -61.33    -10.43                                   
REMARK 500    GLU F 279     -154.15   -146.05                                   
REMARK 500    ASP F 281     -119.33    -87.35                                   
REMARK 500    ASN F 286      102.10    168.31                                   
REMARK 500    HIS F 302      116.41   -173.22                                   
REMARK 500    LYS F 310       33.44     75.70                                   
REMARK 500    PRO F 313       89.28    -55.85                                   
REMARK 500    ALA F 329       51.69   -101.99                                   
REMARK 500    SER F 331      136.21     -3.28                                   
REMARK 500    LYS F 333       81.54     21.68                                   
REMARK 500    LYS F 424       53.82   -114.74                                   
REMARK 500    PHE F 425      163.19    164.34                                   
REMARK 500    HIS F 428       73.15   -161.68                                   
REMARK 500    ILE F 432       78.79   -109.18                                   
REMARK 500    ILE F 434      -21.99    -36.04                                   
REMARK 500    GLU F 499       44.41    -89.07                                   
REMARK 500    ALA F 500      -87.71   -166.00                                   
REMARK 500    VAL F 502      -68.18   -148.52                                   
REMARK 500    PHE F 504       61.19   -100.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HWX   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BOVINE LIVER GLUTAMATE DEHYDROGENASE            
REMARK 900 COMPLEXED WITH GTP, NADH, AND L-GLUTAMIC ACID                        
REMARK 900 RELATED ID: 1HWY   RELATED DB: PDB                                   
REMARK 900 BOVINE GLUTAMATE DEHYDROGENASE COMPLEXED WITH NAD AND 2-             
REMARK 900 OXOGLUTARATE                                                         
REMARK 900 RELATED ID: 1HWZ   RELATED DB: PDB                                   
REMARK 900 BOVINE GLUTAMATE DEHYDROGENASE COMPLEXED WITH NADPH,                 
REMARK 900 GLUTAMATE, AND GTP                                                   
DBREF  1L1F A    1   505  UNP    P00367   DHE3_HUMAN      54    558             
DBREF  1L1F B    1   505  UNP    P00367   DHE3_HUMAN      54    558             
DBREF  1L1F C    1   505  UNP    P00367   DHE3_HUMAN      54    558             
DBREF  1L1F D    1   505  UNP    P00367   DHE3_HUMAN      54    558             
DBREF  1L1F E    1   505  UNP    P00367   DHE3_HUMAN      54    558             
DBREF  1L1F F    1   505  UNP    P00367   DHE3_HUMAN      54    558             
SEQRES   1 A  505  SER GLU ALA 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 GLU ASP LEU ARG THR ARG          
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 ASP 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 ILE ASP VAL PRO          
SEQRES  14 A  505  ALA PRO ASP MET SER 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 GLY          
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 ALA ASP CYS ASP ILE          
SEQRES  26 A  505  LEU ILE PRO ALA ALA SER 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 MET 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 MET 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  ARG ILE SER GLY ALA SER GLU LYS ASP ILE VAL HIS SER          
SEQRES  36 A  505  GLY LEU ALA TYR THR MET GLU ARG SER ALA ARG GLN ILE          
SEQRES  37 A  505  MET ARG 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 ASN GLU ALA GLY VAL THR PHE THR                  
SEQRES   1 B  505  SER GLU ALA 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 GLU ASP LEU ARG THR ARG          
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 ASP 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 ILE ASP VAL PRO          
SEQRES  14 B  505  ALA PRO ASP MET SER 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 GLY          
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 ALA ASP CYS ASP ILE          
SEQRES  26 B  505  LEU ILE PRO ALA ALA SER 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 MET 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 MET 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  ARG ILE SER GLY ALA SER GLU LYS ASP ILE VAL HIS SER          
SEQRES  36 B  505  GLY LEU ALA TYR THR MET GLU ARG SER ALA ARG GLN ILE          
SEQRES  37 B  505  MET ARG 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 ASN GLU ALA GLY VAL THR PHE THR                  
SEQRES   1 C  505  SER GLU ALA 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 GLU ASP LEU ARG THR ARG          
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 ASP 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 ILE ASP VAL PRO          
SEQRES  14 C  505  ALA PRO ASP MET SER 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 GLY          
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 ALA ASP CYS ASP ILE          
SEQRES  26 C  505  LEU ILE PRO ALA ALA SER 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 MET 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 MET 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  ARG ILE SER GLY ALA SER GLU LYS ASP ILE VAL HIS SER          
SEQRES  36 C  505  GLY LEU ALA TYR THR MET GLU ARG SER ALA ARG GLN ILE          
SEQRES  37 C  505  MET ARG 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 ASN GLU ALA GLY VAL THR PHE THR                  
SEQRES   1 D  505  SER GLU ALA 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 GLU ASP LEU ARG THR ARG          
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 ASP 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 ILE ASP VAL PRO          
SEQRES  14 D  505  ALA PRO ASP MET SER 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 GLY          
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 ALA ASP CYS ASP ILE          
SEQRES  26 D  505  LEU ILE PRO ALA ALA SER 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 MET 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 MET 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  ARG ILE SER GLY ALA SER GLU LYS ASP ILE VAL HIS SER          
SEQRES  36 D  505  GLY LEU ALA TYR THR MET GLU ARG SER ALA ARG GLN ILE          
SEQRES  37 D  505  MET ARG 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 ASN GLU ALA GLY VAL THR PHE THR                  
SEQRES   1 E  505  SER GLU ALA 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 GLU ASP LEU ARG THR ARG          
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 ASP 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 ILE ASP VAL PRO          
SEQRES  14 E  505  ALA PRO ASP MET SER 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 GLY          
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 ALA ASP CYS ASP ILE          
SEQRES  26 E  505  LEU ILE PRO ALA ALA SER 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 MET 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 MET 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  ARG ILE SER GLY ALA SER GLU LYS ASP ILE VAL HIS SER          
SEQRES  36 E  505  GLY LEU ALA TYR THR MET GLU ARG SER ALA ARG GLN ILE          
SEQRES  37 E  505  MET ARG 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 ASN GLU ALA GLY VAL THR PHE THR                  
SEQRES   1 F  505  SER GLU ALA 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 GLU ASP LEU ARG THR ARG          
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 ASP 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 ILE ASP VAL PRO          
SEQRES  14 F  505  ALA PRO ASP MET SER 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 GLY          
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 ALA ASP CYS ASP ILE          
SEQRES  26 F  505  LEU ILE PRO ALA ALA SER 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 MET 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 MET 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  ARG ILE SER GLY ALA SER GLU LYS ASP ILE VAL HIS SER          
SEQRES  36 F  505  GLY LEU ALA TYR THR MET GLU ARG SER ALA ARG GLN ILE          
SEQRES  37 F  505  MET ARG 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 ASN GLU ALA GLY VAL THR PHE THR                  
HELIX    1   1 ASN A   12  THR A   38  1                                  27    
HELIX    2   2 ARG A   39  GLN A   44  5                                   6    
HELIX    3   3 LYS A   45  ARG A   50  1                                   6    
HELIX    4   4 ARG A   50  LYS A   57  1                                   8    
HELIX    5   5 SER A  104  VAL A  122  1                                  19    
HELIX    6   6 ASN A  136  TYR A  140  5                                   5    
HELIX    7   7 THR A  141  LYS A  159  1                                  19    
HELIX    8   8 GLY A  176  THR A  190  1                                  15    
HELIX    9   9 ASN A  197  CYS A  201  5                                   5    
HELIX   10  10 PRO A  206  GLY A  210  5                                   5    
HELIX   11  11 SER A  217  ASN A  232  1                                  16    
HELIX   12  12 GLU A  233  GLY A  241  1                                   9    
HELIX   13  13 GLY A  257  PHE A  270  1                                  14    
HELIX   14  14 ASP A  291  HIS A  302  1                                  12    
HELIX   15  15 ASN A  339  VAL A  343  5                                   5    
HELIX   16  16 THR A  357  ARG A  367  1                                  11    
HELIX   17  17 PRO A  373  ASN A  378  1                                   6    
HELIX   18  18 ALA A  379  HIS A  395  1                                  17    
HELIX   19  19 THR A  402  ARG A  423  1                                  22    
HELIX   20  20 THR A  437  GLY A  446  1                                  10    
HELIX   21  21 SER A  448  TYR A  475  1                                  28    
HELIX   22  22 ASP A  480  GLU A  499  1                                  20    
HELIX   23  23 ASN B   12  THR B   38  1                                  27    
HELIX   24  24 ARG B   39  GLN B   44  5                                   6    
HELIX   25  25 LYS B   45  ARG B   50  1                                   6    
HELIX   26  26 ARG B   50  LYS B   57  1                                   8    
HELIX   27  27 SER B  104  VAL B  122  1                                  19    
HELIX   28  28 ASN B  136  TYR B  140  5                                   5    
HELIX   29  29 THR B  141  LYS B  159  1                                  19    
HELIX   30  30 GLY B  176  THR B  190  1                                  15    
HELIX   31  31 ASN B  197  CYS B  201  5                                   5    
HELIX   32  32 PRO B  206  GLY B  210  5                                   5    
HELIX   33  33 SER B  217  ASN B  232  1                                  16    
HELIX   34  34 GLU B  233  GLY B  241  1                                   9    
HELIX   35  35 GLY B  257  PHE B  270  1                                  14    
HELIX   36  36 ASP B  291  HIS B  302  1                                  12    
HELIX   37  37 ASN B  339  VAL B  343  5                                   5    
HELIX   38  38 THR B  357  ARG B  367  1                                  11    
HELIX   39  39 PRO B  373  ASN B  378  1                                   6    
HELIX   40  40 ALA B  379  HIS B  395  1                                  17    
HELIX   41  41 THR B  402  ARG B  423  1                                  22    
HELIX   42  42 THR B  437  GLY B  446  1                                  10    
HELIX   43  43 SER B  448  TYR B  475  1                                  28    
HELIX   44  44 ASP B  480  GLU B  499  1                                  20    
HELIX   45  45 ASN C   12  THR C   38  1                                  27    
HELIX   46  46 ARG C   39  GLN C   44  5                                   6    
HELIX   47  47 LYS C   45  ARG C   50  1                                   6    
HELIX   48  48 ARG C   50  LYS C   57  1                                   8    
HELIX   49  49 SER C  104  VAL C  122  1                                  19    
HELIX   50  50 ASN C  136  TYR C  140  5                                   5    
HELIX   51  51 THR C  141  LYS C  159  1                                  19    
HELIX   52  52 GLY C  176  THR C  190  1                                  15    
HELIX   53  53 ASN C  197  CYS C  201  5                                   5    
HELIX   54  54 PRO C  206  GLY C  210  5                                   5    
HELIX   55  55 SER C  217  ASN C  232  1                                  16    
HELIX   56  56 GLU C  233  GLY C  241  1                                   9    
HELIX   57  57 GLY C  257  PHE C  270  1                                  14    
HELIX   58  58 ASP C  291  HIS C  302  1                                  12    
HELIX   59  59 ASN C  339  VAL C  343  5                                   5    
HELIX   60  60 THR C  357  ARG C  367  1                                  11    
HELIX   61  61 PRO C  373  ASN C  378  1                                   6    
HELIX   62  62 ALA C  379  HIS C  395  1                                  17    
HELIX   63  63 THR C  402  ARG C  423  1                                  22    
HELIX   64  64 THR C  437  GLY C  446  1                                  10    
HELIX   65  65 SER C  448  TYR C  475  1                                  28    
HELIX   66  66 ASP C  480  GLU C  499  1                                  20    
HELIX   67  67 ASN D   12  THR D   38  1                                  27    
HELIX   68  68 ARG D   39  GLN D   44  5                                   6    
HELIX   69  69 LYS D   45  ARG D   50  1                                   6    
HELIX   70  70 ARG D   50  LYS D   57  1                                   8    
HELIX   71  71 SER D  104  VAL D  122  1                                  19    
HELIX   72  72 ASN D  136  TYR D  140  5                                   5    
HELIX   73  73 THR D  141  LYS D  159  1                                  19    
HELIX   74  74 GLY D  176  THR D  190  1                                  15    
HELIX   75  75 ASN D  197  CYS D  201  5                                   5    
HELIX   76  76 PRO D  206  GLY D  210  5                                   5    
HELIX   77  77 SER D  217  ASN D  232  1                                  16    
HELIX   78  78 GLU D  233  GLY D  241  1                                   9    
HELIX   79  79 GLY D  257  PHE D  270  1                                  14    
HELIX   80  80 ASP D  291  HIS D  302  1                                  12    
HELIX   81  81 ASN D  339  VAL D  343  5                                   5    
HELIX   82  82 THR D  357  ARG D  367  1                                  11    
HELIX   83  83 PRO D  373  ASN D  378  1                                   6    
HELIX   84  84 ALA D  379  HIS D  395  1                                  17    
HELIX   85  85 THR D  402  ARG D  423  1                                  22    
HELIX   86  86 THR D  437  GLY D  446  1                                  10    
HELIX   87  87 SER D  448  TYR D  475  1                                  28    
HELIX   88  88 ASP D  480  GLU D  499  1                                  20    
HELIX   89  89 ASN E   12  THR E   38  1                                  27    
HELIX   90  90 ARG E   39  GLN E   44  5                                   6    
HELIX   91  91 LYS E   45  ARG E   50  1                                   6    
HELIX   92  92 ARG E   50  LYS E   57  1                                   8    
HELIX   93  93 SER E  104  VAL E  122  1                                  19    
HELIX   94  94 ASN E  136  TYR E  140  5                                   5    
HELIX   95  95 THR E  141  LYS E  159  1                                  19    
HELIX   96  96 GLY E  176  THR E  190  1                                  15    
HELIX   97  97 ASN E  197  CYS E  201  5                                   5    
HELIX   98  98 PRO E  206  GLY E  210  5                                   5    
HELIX   99  99 SER E  217  ASN E  232  1                                  16    
HELIX  100 100 GLU E  233  GLY E  241  1                                   9    
HELIX  101 101 GLY E  257  PHE E  270  1                                  14    
HELIX  102 102 ASP E  291  HIS E  302  1                                  12    
HELIX  103 103 ASN E  339  VAL E  343  5                                   5    
HELIX  104 104 THR E  357  ARG E  367  1                                  11    
HELIX  105 105 PRO E  373  ASN E  378  1                                   6    
HELIX  106 106 ALA E  379  HIS E  395  1                                  17    
HELIX  107 107 THR E  402  ARG E  423  1                                  22    
HELIX  108 108 THR E  437  GLY E  446  1                                  10    
HELIX  109 109 SER E  448  TYR E  475  1                                  28    
HELIX  110 110 ASP E  480  GLU E  499  1                                  20    
HELIX  111 111 ASN F   12  THR F   38  1                                  27    
HELIX  112 112 ARG F   39  GLN F   44  5                                   6    
HELIX  113 113 LYS F   45  ARG F   50  1                                   6    
HELIX  114 114 ARG F   50  LYS F   57  1                                   8    
HELIX  115 115 SER F  104  VAL F  122  1                                  19    
HELIX  116 116 ASN F  136  TYR F  140  5                                   5    
HELIX  117 117 THR F  141  LYS F  159  1                                  19    
HELIX  118 118 GLY F  176  THR F  190  1                                  15    
HELIX  119 119 ASN F  197  CYS F  201  5                                   5    
HELIX  120 120 PRO F  206  GLY F  210  5                                   5    
HELIX  121 121 SER F  217  ASN F  232  1                                  16    
HELIX  122 122 GLU F  233  GLY F  241  1                                   9    
HELIX  123 123 GLY F  257  PHE F  270  1                                  14    
HELIX  124 124 ASP F  291  HIS F  302  1                                  12    
HELIX  125 125 ASN F  339  VAL F  343  5                                   5    
HELIX  126 126 THR F  357  ARG F  367  1                                  11    
HELIX  127 127 PRO F  373  ASN F  378  1                                   6    
HELIX  128 128 ALA F  379  HIS F  395  1                                  17    
HELIX  129 129 THR F  402  ARG F  423  1                                  22    
HELIX  130 130 THR F  437  GLY F  446  1                                  10    
HELIX  131 131 SER F  448  TYR F  475  1                                  28    
HELIX  132 132 ASP F  480  GLU F  499  1                                  20    
SHEET    1   A10 ASP A 167  ALA A 170  0                                        
SHEET    2   A10 CYS A  93  TYR A  99  1  N  CYS A  93   O  VAL A 168           
SHEET    3   A10 GLY A 127  VAL A 133  1  O  GLY A 127   N  LYS A  94           
SHEET    4   A10 TRP A  76  GLN A  85 -1  N  TYR A  82   O  GLY A 132           
SHEET    5   A10 HIS A  61  ARG A  70 -1  N  LEU A  63   O  ARG A  83           
SHEET    6   A10 HIS E  61  ARG E  70 -1  O  SER E  64   N  VAL A  62           
SHEET    7   A10 TRP E  76  GLN E  85 -1  O  ARG E  83   N  LEU E  63           
SHEET    8   A10 GLY E 127  VAL E 133 -1  O  GLY E 132   N  TYR E  82           
SHEET    9   A10 CYS E  93  TYR E  99  1  N  ARG E  98   O  VAL E 133           
SHEET   10   A10 ASP E 167  ALA E 170  1  O  VAL E 168   N  CYS E  93           
SHEET    1   B 5 LYS A 273  VAL A 277  0                                        
SHEET    2   B 5 THR A 250  GLN A 254  1  N  PHE A 251   O  LYS A 273           
SHEET    3   B 5 ILE A 325  PRO A 328  1  O  ILE A 327   N  VAL A 252           
SHEET    4   B 5 ILE A 347  ALA A 349  1  O  ILE A 347   N  LEU A 326           
SHEET    5   B 5 MET A 370  ILE A 372  1  O  MET A 370   N  ILE A 348           
SHEET    1   C10 ASP B 167  ALA B 170  0                                        
SHEET    2   C10 CYS B  93  TYR B  99  1  N  CYS B  93   O  VAL B 168           
SHEET    3   C10 GLY B 127  VAL B 133  1  O  VAL B 133   N  ARG B  98           
SHEET    4   C10 TRP B  76  GLN B  85 -1  N  TYR B  82   O  GLY B 132           
SHEET    5   C10 HIS B  61  ARG B  70 -1  N  LEU B  63   O  ARG B  83           
SHEET    6   C10 HIS D  61  ARG D  70 -1  O  VAL D  62   N  SER B  64           
SHEET    7   C10 TRP D  76  GLN D  85 -1  O  ARG D  83   N  LEU D  63           
SHEET    8   C10 GLY D 127  VAL D 133 -1  O  GLY D 132   N  TYR D  82           
SHEET    9   C10 CYS D  93  TYR D  99  1  N  LYS D  94   O  GLY D 127           
SHEET   10   C10 ASP D 167  ALA D 170  1  O  VAL D 168   N  CYS D  93           
SHEET    1   D 5 LYS B 273  VAL B 277  0                                        
SHEET    2   D 5 THR B 250  GLN B 254  1  N  PHE B 251   O  LYS B 273           
SHEET    3   D 5 ILE B 325  PRO B 328  1  O  ILE B 327   N  VAL B 252           
SHEET    4   D 5 ILE B 347  ALA B 349  1  O  ILE B 347   N  LEU B 326           
SHEET    5   D 5 MET B 370  ILE B 372  1  O  MET B 370   N  ILE B 348           
SHEET    1   E10 ASP C 167  ALA C 170  0                                        
SHEET    2   E10 CYS C  93  TYR C  99  1  N  CYS C  93   O  VAL C 168           
SHEET    3   E10 GLY C 127  VAL C 133  1  O  GLY C 127   N  LYS C  94           
SHEET    4   E10 TRP C  76  GLN C  85 -1  N  TYR C  82   O  GLY C 132           
SHEET    5   E10 HIS C  61  ARG C  70 -1  N  LEU C  63   O  ARG C  83           
SHEET    6   E10 HIS F  61  ARG F  70 -1  O  VAL F  62   N  SER C  64           
SHEET    7   E10 TRP F  76  GLN F  85 -1  O  ARG F  83   N  LEU F  63           
SHEET    8   E10 GLY F 127  VAL F 133 -1  O  GLY F 132   N  TYR F  82           
SHEET    9   E10 CYS F  93  TYR F  99  1  N  ARG F  98   O  VAL F 133           
SHEET   10   E10 ASP F 167  ALA F 170  1  O  VAL F 168   N  CYS F  93           
SHEET    1   F 5 LYS C 273  VAL C 277  0                                        
SHEET    2   F 5 THR C 250  GLN C 254  1  N  PHE C 251   O  LYS C 273           
SHEET    3   F 5 ILE C 325  PRO C 328  1  O  ILE C 327   N  VAL C 252           
SHEET    4   F 5 ILE C 347  ALA C 349  1  O  ILE C 347   N  LEU C 326           
SHEET    5   F 5 MET C 370  ILE C 372  1  O  MET C 370   N  ILE C 348           
SHEET    1   G 5 LYS D 273  VAL D 277  0                                        
SHEET    2   G 5 THR D 250  GLN D 254  1  N  PHE D 251   O  LYS D 273           
SHEET    3   G 5 ILE D 325  PRO D 328  1  O  ILE D 327   N  VAL D 252           
SHEET    4   G 5 ILE D 347  ALA D 349  1  O  ILE D 347   N  LEU D 326           
SHEET    5   G 5 MET D 370  ILE D 372  1  O  MET D 370   N  ILE D 348           
SHEET    1   H 5 LYS E 273  VAL E 277  0                                        
SHEET    2   H 5 THR E 250  GLN E 254  1  N  PHE E 251   O  LYS E 273           
SHEET    3   H 5 ILE E 325  PRO E 328  1  O  ILE E 327   N  VAL E 252           
SHEET    4   H 5 ILE E 347  ALA E 349  1  O  ILE E 347   N  LEU E 326           
SHEET    5   H 5 MET E 370  ILE E 372  1  O  MET E 370   N  ILE E 348           
SHEET    1   I 5 LYS F 273  VAL F 277  0                                        
SHEET    2   I 5 THR F 250  GLN F 254  1  N  PHE F 251   O  LYS F 273           
SHEET    3   I 5 ILE F 325  PRO F 328  1  O  ILE F 327   N  VAL F 252           
SHEET    4   I 5 ILE F 347  ALA F 349  1  O  ILE F 347   N  LEU F 326           
SHEET    5   I 5 MET F 370  ILE F 372  1  O  MET F 370   N  ILE F 348           
CRYST1   97.800   98.800  124.200  86.26  70.28  60.34 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      0.010225 -0.005823 -0.004424        0.00000                         
SCALE2      0.000000  0.011648  0.001460        0.00000                         
SCALE3      0.000000  0.000000  0.008620        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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