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Database: PDB
Entry: 1NR1
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Original site: 1NR1 
HEADER    OXIDOREDUCTASE                          23-JAN-03   1NR1              
TITLE     CRYSTAL STRUCTURE OF THE R463A MUTANT OF HUMAN GLUTAMATE DEHYDROGENASE
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE DEHYDROGENASE 1;                                 
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 EC: 1.4.1.3;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: 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    GLUTAMATE DEHYDROGENASE, HEXAMER, REGULATION, OXIDOREDUCTASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BANERJEE,T.SCHMIDT,J.FANG,C.A.STANLEY,T.J.SMITH                     
REVDAT   4   11-OCT-17 1NR1    1       REMARK                                   
REVDAT   3   08-FEB-17 1NR1    1       AUTHOR VERSN                             
REVDAT   2   24-FEB-09 1NR1    1       VERSN                                    
REVDAT   1   06-MAY-03 1NR1    0                                                
JRNL        AUTH   S.BANERJEE,T.SCHMIDT,J.FANG,C.A.STANLEY,T.J.SMITH            
JRNL        TITL   STRUCTURAL STUDIES ON ADP ACTIVATION OF MAMMALIAN GLUTAMATE  
JRNL        TITL 2 DEHYDROGENASE AND THE EVOLUTION OF REGULATION                
JRNL        REF    BIOCHEMISTRY                  V.  42  3446 2003              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   12653548                                                     
JRNL        DOI    10.1021/BI0206917                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 50903                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5072                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.51                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7555                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE                    : 0.3500                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 314                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 23208                                   
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) : 46.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.63000                                             
REMARK   3    B22 (A**2) : -6.27000                                             
REMARK   3    B33 (A**2) : -4.37000                                             
REMARK   3    B12 (A**2) : 2.27000                                              
REMARK   3    B13 (A**2) : -16.05000                                            
REMARK   3    B23 (A**2) : -1.50000                                             
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) : 0.51                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.53                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.800                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.240                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 5.180 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 7.830 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 7.550 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 10.010; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.26                                                 
REMARK   3   BSOL        : 33.61                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ADP.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ADP.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1NR1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000018131.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUN-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) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50903                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
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     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
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) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.0                               
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: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM PHOSPHATE, PEG 8000, BOG,         
REMARK 280  SODIUM CHLORIDE, MPD, SODIUM AZIDE, PH 6.8, VAPOR DIFFUSION,        
REMARK 280  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: 31560 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 106250 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -140.0 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   O    PRO C   433     N    VAL C   435              2.09            
REMARK 500   O    PRO E   433     N    VAL E   435              2.09            
REMARK 500   O    PRO F   433     N    VAL F   435              2.12            
REMARK 500   O    ASP B   172     N    SER B   174              2.14            
REMARK 500   O    ASP D   172     N    SER D   174              2.15            
REMARK 500   OXT  THR B   505     NH2  ARG F   150              2.18            
REMARK 500   O    ASP E   172     N    SER E   174              2.19            
REMARK 500   O    SER B   104     N    GLU B   107              2.19            
REMARK 500   O    THR C   505     OD1  ASP D   185              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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      0.161                       
REMARK 500    CYS C  59   CB    CYS C  59   SG      0.148                       
REMARK 500    CYS C  93   CB    CYS C  93   SG     -0.097                       
REMARK 500    CYS D  59   CB    CYS D  59   SG      0.130                       
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    PHE A 504   N   -  CA  -  C   ANGL. DEV. = -16.5 DEGREES          
REMARK 500    PRO B  58   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    PRO B  92   C   -  N   -  CA  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    PRO B 137   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    CYS C  59   CB  -  CA  -  C   ANGL. DEV. =   7.6 DEGREES          
REMARK 500    SER C  66   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500    PRO C  92   C   -  N   -  CA  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    PRO C 125   C   -  N   -  CA  ANGL. DEV. =  12.6 DEGREES          
REMARK 500    PRO C 137   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    PRO C 244   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    PRO C 292   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    GLY C 316   N   -  CA  -  C   ANGL. DEV. = -15.8 DEGREES          
REMARK 500    PRO C 373   C   -  N   -  CA  ANGL. DEV. =  11.6 DEGREES          
REMARK 500    THR C 503   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500    PRO D 169   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    LEU D 240   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    LEU D 326   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    PHE D 504   N   -  CA  -  C   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    PRO E 244   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    PRO F  58   C   -  N   -  CA  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    PRO F 164   C   -  N   -  CA  ANGL. DEV. =  11.0 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    PRO A  11      174.71    -57.01                                   
REMARK 500    VAL A  33      -77.58    -62.13                                   
REMARK 500    GLU A  34     -131.91    -47.46                                   
REMARK 500    ASP A  35       26.44    -44.78                                   
REMARK 500    ARG A  37       13.21   -157.98                                   
REMARK 500    SER A  41       60.75    -66.35                                   
REMARK 500    LYS A  45       46.51    -87.76                                   
REMARK 500    VAL A  49       16.59    -69.20                                   
REMARK 500    ILE A  52      -56.06    -26.43                                   
REMARK 500    SER A  66       77.71   -166.22                                   
REMARK 500    THR A  91      -70.09    -48.14                                   
REMARK 500    ASP A 123       74.74     35.31                                   
REMARK 500    PRO A 125       66.66    -69.93                                   
REMARK 500    LYS A 130      146.78   -172.23                                   
REMARK 500    LYS A 134       62.23    -16.25                                   
REMARK 500    PRO A 137      -39.91    -37.03                                   
REMARK 500    LYS A 147      -72.14    -38.38                                   
REMARK 500    ILE A 162      106.15   -172.98                                   
REMARK 500    ILE A 166      -60.20   -102.61                                   
REMARK 500    ASP A 172       98.18   -172.58                                   
REMARK 500    MET A 173      -80.82     36.72                                   
REMARK 500    GLU A 177       -2.77    -53.32                                   
REMARK 500    THR A 190     -107.37   -120.87                                   
REMARK 500    ASP A 195       99.33    -64.20                                   
REMARK 500    ILE A 196       -9.38    -53.75                                   
REMARK 500    HIS A 199       -7.33    -56.70                                   
REMARK 500    ALA A 218      -75.81    -26.42                                   
REMARK 500    ALA A 234      -77.78    -67.79                                   
REMARK 500    SER A 235      -41.19    -27.01                                   
REMARK 500    MET A 242     -154.69    -90.75                                   
REMARK 500    PRO A 244     -165.33    -66.27                                   
REMARK 500    PHE A 246      -17.09   -142.77                                   
REMARK 500    ASP A 248      -88.32      3.08                                   
REMARK 500    LEU A 261      -79.00    -57.49                                   
REMARK 500    HIS A 268      -72.89    -52.98                                   
REMARK 500    ARG A 269      -30.53    -34.94                                   
REMARK 500    PHE A 270       59.02   -109.66                                   
REMARK 500    ASP A 281     -123.04    -99.88                                   
REMARK 500    ASN A 286       97.74    165.12                                   
REMARK 500    PRO A 287       -8.69    -59.75                                   
REMARK 500    GLN A 301      -36.88    -34.67                                   
REMARK 500    SER A 304     -158.83   -122.56                                   
REMARK 500    LYS A 310       26.45    110.35                                   
REMARK 500    PRO A 313      104.34    -45.68                                   
REMARK 500    SER A 317       99.24     30.07                                   
REMARK 500    ALA A 321      138.80    -16.51                                   
REMARK 500    ALA A 329       55.63   -101.57                                   
REMARK 500    ALA A 330      172.20    168.42                                   
REMARK 500    SER A 331      115.47     43.78                                   
REMARK 500    LYS A 333       81.06     20.51                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     377 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR D 266         0.07    SIDE CHAIN                              
REMARK 500    TYR D 459         0.08    SIDE CHAIN                              
REMARK 500    TYR E 187         0.09    SIDE CHAIN                              
REMARK 500    TYR E 398         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1L1F   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF APO-HUMAN GLUTAMATE DEHYDROGENASE                       
REMARK 900 RELATED ID: 1NQT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1NR7   RELATED DB: PDB                                   
DBREF  1NR1 A   10   505  UNP    P00367   DHE3_HUMAN      63    558             
DBREF  1NR1 B   10   505  UNP    P00367   DHE3_HUMAN      63    558             
DBREF  1NR1 C   10   505  UNP    P00367   DHE3_HUMAN      63    558             
DBREF  1NR1 D   10   505  UNP    P00367   DHE3_HUMAN      63    558             
DBREF  1NR1 E   10   505  UNP    P00367   DHE3_HUMAN      63    558             
DBREF  1NR1 F   10   505  UNP    P00367   DHE3_HUMAN      63    558             
SEQADV 1NR1 GLN A   88  UNP  P00367    HIS   141 CONFLICT                       
SEQADV 1NR1 HIS A   89  UNP  P00367    GLN   142 CONFLICT                       
SEQADV 1NR1 ALA A  463  UNP  P00367    ARG   516 ENGINEERED                     
SEQADV 1NR1 GLN B   88  UNP  P00367    HIS   141 CONFLICT                       
SEQADV 1NR1 HIS B   89  UNP  P00367    GLN   142 CONFLICT                       
SEQADV 1NR1 ALA B  463  UNP  P00367    ARG   516 ENGINEERED                     
SEQADV 1NR1 GLN C   88  UNP  P00367    HIS   141 CONFLICT                       
SEQADV 1NR1 HIS C   89  UNP  P00367    GLN   142 CONFLICT                       
SEQADV 1NR1 ALA C  463  UNP  P00367    ARG   516 ENGINEERED                     
SEQADV 1NR1 GLN D   88  UNP  P00367    HIS   141 CONFLICT                       
SEQADV 1NR1 HIS D   89  UNP  P00367    GLN   142 CONFLICT                       
SEQADV 1NR1 ALA D  463  UNP  P00367    ARG   516 ENGINEERED                     
SEQADV 1NR1 GLN E   88  UNP  P00367    HIS   141 CONFLICT                       
SEQADV 1NR1 HIS E   89  UNP  P00367    GLN   142 CONFLICT                       
SEQADV 1NR1 ALA E  463  UNP  P00367    ARG   516 ENGINEERED                     
SEQADV 1NR1 GLN F   88  UNP  P00367    HIS   141 CONFLICT                       
SEQADV 1NR1 HIS F   89  UNP  P00367    GLN   142 CONFLICT                       
SEQADV 1NR1 ALA F  463  UNP  P00367    ARG   516 ENGINEERED                     
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 HIS SER GLY LEU ALA TYR THR MET GLU ALA 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 HIS SER GLY LEU ALA TYR THR MET GLU ALA 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 HIS SER GLY LEU ALA TYR THR MET GLU ALA 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 HIS SER GLY LEU ALA TYR THR MET GLU ALA 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 HIS SER GLY LEU ALA TYR THR MET GLU ALA 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 HIS SER GLY LEU ALA TYR THR MET GLU ALA 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                                                      
HELIX    1   1 ASN A   12  THR A   38  1                                  27    
HELIX    2   2 ARG A   39  LYS A   45  5                                   7    
HELIX    3   3 ASN A   47  VAL A   49  5                                   3    
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  158  1                                  18    
HELIX    8   8 GLY A  176  THR A  190  1                                  15    
HELIX    9   9 ILE A  191  TYR A  194  5                                   4    
HELIX   10  10 ASN A  197  CYS A  201  5                                   5    
HELIX   11  11 PRO A  206  GLY A  210  5                                   5    
HELIX   12  12 GLY A  214  ASN A  232  1                                  19    
HELIX   13  13 GLU A  233  SER A  238  1                                   6    
HELIX   14  14 GLY A  257  PHE A  270  1                                  14    
HELIX   15  15 ASP A  291  HIS A  302  1                                  12    
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  GLU A  422  1                                  21    
HELIX   20  20 THR A  437  GLY A  446  1                                  10    
HELIX   21  21 SER A  448  ASN A  476  1                                  29    
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 ASN B   47  VAL B   49  5                                   3    
HELIX   25  25 ARG B   50  LYS B   57  1                                   8    
HELIX   26  26 VAL B  105  VAL B  122  1                                  18    
HELIX   27  27 ASN B  136  TYR B  140  5                                   5    
HELIX   28  28 THR B  141  LYS B  159  1                                  19    
HELIX   29  29 GLY B  176  THR B  190  1                                  15    
HELIX   30  30 ASN B  197  CYS B  201  5                                   5    
HELIX   31  31 PRO B  206  GLY B  210  5                                   5    
HELIX   32  32 SER B  217  ASN B  232  1                                  16    
HELIX   33  33 GLU B  233  GLY B  241  1                                   9    
HELIX   34  34 GLY B  257  PHE B  270  1                                  14    
HELIX   35  35 ASP B  291  HIS B  302  1                                  12    
HELIX   36  36 SER B  317  ALA B  321  5                                   5    
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  GLU B  422  1                                  21    
HELIX   42  42 THR B  437  ALA B  447  1                                  11    
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  GLU C   34  1                                  23    
HELIX   46  46 ARG C   37  SER C   41  5                                   5    
HELIX   47  47 ARG C   50  LYS C   57  1                                   8    
HELIX   48  48 SER C  104  VAL C  122  1                                  19    
HELIX   49  49 ASN C  136  TYR C  140  5                                   5    
HELIX   50  50 THR C  141  LYS C  158  1                                  18    
HELIX   51  51 GLY C  176  THR C  190  1                                  15    
HELIX   52  52 ASN C  197  VAL C  202  5                                   6    
HELIX   53  53 PRO C  206  GLY C  210  5                                   5    
HELIX   54  54 GLY C  214  ASN C  232  1                                  19    
HELIX   55  55 GLU C  233  LEU C  240  1                                   8    
HELIX   56  56 GLY C  257  PHE C  270  1                                  14    
HELIX   57  57 ASP C  291  HIS C  302  1                                  12    
HELIX   58  58 SER C  317  ALA C  321  5                                   5    
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  GLU C  422  1                                  21    
HELIX   64  64 THR C  437  GLY C  446  1                                  10    
HELIX   65  65 SER C  448  ASN C  476  1                                  29    
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  SER D   41  5                                   3    
HELIX   69  69 ARG D   50  LYS D   57  1                                   8    
HELIX   70  70 SER D  104  ALA D  120  1                                  17    
HELIX   71  71 THR D  141  GLY D  160  1                                  20    
HELIX   72  72 GLY D  176  THR D  190  1                                  15    
HELIX   73  73 ASN D  197  VAL D  202  5                                   6    
HELIX   74  74 SER D  217  ASN D  232  1                                  16    
HELIX   75  75 GLY D  257  PHE D  270  1                                  14    
HELIX   76  76 ASP D  291  GLN D  301  1                                  11    
HELIX   77  77 ASN D  339  VAL D  343  5                                   5    
HELIX   78  78 THR D  357  ARG D  367  1                                  11    
HELIX   79  79 PRO D  373  ASN D  378  1                                   6    
HELIX   80  80 GLY D  380  HIS D  395  1                                  16    
HELIX   81  81 THR D  402  ARG D  423  1                                  22    
HELIX   82  82 THR D  437  SER D  445  1                                   9    
HELIX   83  83 GLU D  449  TYR D  475  1                                  27    
HELIX   84  84 ASP D  480  GLU D  499  1                                  20    
HELIX   85  85 ASN E   12  THR E   38  1                                  27    
HELIX   86  86 ASN E   47  ARG E   50  5                                   4    
HELIX   87  87 GLY E   51  LYS E   57  1                                   7    
HELIX   88  88 SER E  104  VAL E  122  1                                  19    
HELIX   89  89 THR E  141  LYS E  159  1                                  19    
HELIX   90  90 GLY E  176  THR E  190  1                                  15    
HELIX   91  91 ASN E  197  CYS E  201  5                                   5    
HELIX   92  92 PRO E  206  GLY E  210  5                                   5    
HELIX   93  93 GLY E  214  ASN E  232  1                                  19    
HELIX   94  94 GLU E  233  LEU E  240  1                                   8    
HELIX   95  95 GLY E  257  PHE E  270  1                                  14    
HELIX   96  96 ASP E  291  HIS E  302  1                                  12    
HELIX   97  97 SER E  317  ALA E  321  5                                   5    
HELIX   98  98 ASN E  339  VAL E  343  5                                   5    
HELIX   99  99 THR E  357  ARG E  367  1                                  11    
HELIX  100 100 PRO E  373  ASN E  378  1                                   6    
HELIX  101 101 ALA E  379  HIS E  395  1                                  17    
HELIX  102 102 THR E  402  GLU E  422  1                                  21    
HELIX  103 103 THR E  437  ALA E  447  1                                  11    
HELIX  104 104 SER E  448  TYR E  475  1                                  28    
HELIX  105 105 ASP E  480  GLU E  499  1                                  20    
HELIX  106 106 ASN F   12  THR F   38  1                                  27    
HELIX  107 107 ARG F   39  LYS F   45  5                                   7    
HELIX  108 108 GLY F   51  LYS F   57  1                                   7    
HELIX  109 109 SER F  104  VAL F  122  1                                  19    
HELIX  110 110 ASN F  136  TYR F  140  5                                   5    
HELIX  111 111 THR F  141  LYS F  159  1                                  19    
HELIX  112 112 GLY F  176  SER F  189  1                                  14    
HELIX  113 113 ASN F  197  VAL F  202  5                                   6    
HELIX  114 114 PRO F  206  GLY F  210  5                                   5    
HELIX  115 115 SER F  217  ASN F  232  1                                  16    
HELIX  116 116 GLU F  233  ILE F  239  1                                   7    
HELIX  117 117 GLY F  257  PHE F  270  1                                  14    
HELIX  118 118 ASP F  291  HIS F  302  1                                  12    
HELIX  119 119 SER F  317  ALA F  321  5                                   5    
HELIX  120 120 ASN F  339  VAL F  343  5                                   5    
HELIX  121 121 THR F  357  ARG F  367  1                                  11    
HELIX  122 122 PRO F  373  ASN F  378  1                                   6    
HELIX  123 123 ALA F  379  HIS F  395  1                                  17    
HELIX  124 124 THR F  402  GLU F  422  1                                  21    
HELIX  125 125 THR F  437  GLY F  446  1                                  10    
HELIX  126 126 SER F  448  TYR F  475  1                                  28    
HELIX  127 127 ASP F  480  GLU F  499  1                                  20    
SHEET    1   A10 ASP A 167  ALA A 170  0                                        
SHEET    2   A10 CYS A  93  ARG A  98  1  N  CYS A  93   O  VAL A 168           
SHEET    3   A10 GLY A 127  GLY A 132  1  O  GLY A 127   N  LYS A  94           
SHEET    4   A10 TRP A  76  GLN A  85 -1  N  ALA A  84   O  LYS A 130           
SHEET    5   A10 HIS A  61  ARG A  70 -1  N  LEU A  65   O  GLY A  81           
SHEET    6   A10 HIS E  61  LEU E  65 -1  O  VAL E  62   N  SER A  64           
SHEET    7   A10 GLY E  81  GLN E  85 -1  O  GLN E  85   N  HIS E  61           
SHEET    8   A10 GLY E 127  VAL E 133 -1  O  LYS E 130   N  ALA E  84           
SHEET    9   A10 CYS E  93  TYR E  99  1  N  ARG E  98   O  ALA E 131           
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  VAL A 253  1  N  PHE A 251   O  LYS A 273           
SHEET    3   B 5 ILE A 325  ILE A 327  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 D 167  ALA D 170  0                                        
SHEET    2   C10 CYS D  93  ARG D  98  1  N  CYS D  93   O  VAL D 168           
SHEET    3   C10 ALA D 129  GLY D 132  1  O  ALA D 131   N  ARG D  98           
SHEET    4   C10 TRP D  76  GLN D  85 -1  N  ALA D  84   O  LYS D 130           
SHEET    5   C10 HIS D  61  ARG D  70 -1  N  PHE D  67   O  ILE D  79           
SHEET    6   C10 HIS B  61  ARG B  70 -1  N  SER B  64   O  VAL D  62           
SHEET    7   C10 TRP B  76  GLN B  85 -1  O  ILE B  79   N  PHE B  67           
SHEET    8   C10 GLY B 127  VAL B 133 -1  O  LYS B 130   N  ALA B  84           
SHEET    9   C10 CYS B  93  LYS B  94  1  N  LYS B  94   O  GLY B 127           
SHEET   10   C10 ASP B 167  VAL B 168  1  O  VAL B 168   N  CYS B  93           
SHEET    1   D 9 ASP D 167  ALA D 170  0                                        
SHEET    2   D 9 CYS D  93  ARG D  98  1  N  CYS D  93   O  VAL D 168           
SHEET    3   D 9 ALA D 129  GLY D 132  1  O  ALA D 131   N  ARG D  98           
SHEET    4   D 9 TRP D  76  GLN D  85 -1  N  ALA D  84   O  LYS D 130           
SHEET    5   D 9 HIS D  61  ARG D  70 -1  N  PHE D  67   O  ILE D  79           
SHEET    6   D 9 HIS B  61  ARG B  70 -1  N  SER B  64   O  VAL D  62           
SHEET    7   D 9 TRP B  76  GLN B  85 -1  O  ILE B  79   N  PHE B  67           
SHEET    8   D 9 GLY B 127  VAL B 133 -1  O  LYS B 130   N  ALA B  84           
SHEET    9   D 9 ILE B  97  ARG B  98  1  N  ARG B  98   O  ALA B 131           
SHEET    1   E 5 LYS B 273  GLY B 278  0                                        
SHEET    2   E 5 THR B 250  GLN B 254  1  N  PHE B 251   O  LYS B 273           
SHEET    3   E 5 ILE B 325  PRO B 328  1  O  ILE B 327   N  VAL B 252           
SHEET    4   E 5 ILE B 347  ALA B 349  1  O  ILE B 347   N  LEU B 326           
SHEET    5   E 5 MET B 370  ILE B 372  1  O  ILE B 372   N  ILE B 348           
SHEET    1   F10 ASP C 167  ALA C 170  0                                        
SHEET    2   F10 CYS C  93  ARG C  98  1  N  CYS C  93   O  VAL C 168           
SHEET    3   F10 GLY C 127  VAL C 133  1  O  ALA C 131   N  ARG C  98           
SHEET    4   F10 TRP C  76  GLN C  85 -1  N  ALA C  84   O  LYS C 130           
SHEET    5   F10 HIS C  61  ARG C  70 -1  N  LEU C  65   O  GLY C  81           
SHEET    6   F10 HIS F  61  ARG F  70 -1  O  SER F  64   N  VAL C  62           
SHEET    7   F10 TRP F  76  GLN F  85 -1  O  ILE F  79   N  PHE F  67           
SHEET    8   F10 GLY F 127  LYS F 134 -1  O  LYS F 130   N  ALA F  84           
SHEET    9   F10 CYS F  93  LYS F  94  1  N  LYS F  94   O  GLY F 127           
SHEET   10   F10 ASP F 167  VAL F 168  1  O  VAL F 168   N  CYS F  93           
SHEET    1   G 9 ASP C 167  ALA C 170  0                                        
SHEET    2   G 9 CYS C  93  ARG C  98  1  N  CYS C  93   O  VAL C 168           
SHEET    3   G 9 GLY C 127  VAL C 133  1  O  ALA C 131   N  ARG C  98           
SHEET    4   G 9 TRP C  76  GLN C  85 -1  N  ALA C  84   O  LYS C 130           
SHEET    5   G 9 HIS C  61  ARG C  70 -1  N  LEU C  65   O  GLY C  81           
SHEET    6   G 9 HIS F  61  ARG F  70 -1  O  SER F  64   N  VAL C  62           
SHEET    7   G 9 TRP F  76  GLN F  85 -1  O  ILE F  79   N  PHE F  67           
SHEET    8   G 9 GLY F 127  LYS F 134 -1  O  LYS F 130   N  ALA F  84           
SHEET    9   G 9 ILE F  97  SER F 100  1  N  ARG F  98   O  ALA F 131           
SHEET    1   H 5 LYS C 273  GLY C 278  0                                        
SHEET    2   H 5 THR C 250  GLN C 254  1  N  PHE C 251   O  LYS C 273           
SHEET    3   H 5 ILE C 325  PRO C 328  1  O  ILE C 327   N  VAL C 252           
SHEET    4   H 5 ILE C 347  ALA C 349  1  O  ALA C 349   N  LEU C 326           
SHEET    5   H 5 MET C 370  ILE C 372  1  O  MET C 370   N  ILE C 348           
SHEET    1   I 5 LYS D 273  VAL D 277  0                                        
SHEET    2   I 5 THR D 250  GLN D 254  1  N  PHE D 251   O  LYS D 273           
SHEET    3   I 5 ILE D 325  PRO D 328  1  O  ILE D 327   N  VAL D 252           
SHEET    4   I 5 ILE D 347  ALA D 349  1  O  ILE D 347   N  LEU D 326           
SHEET    5   I 5 MET D 370  ILE D 372  1  O  ILE D 372   N  ILE D 348           
SHEET    1   J 2 PHE E  67  ILE E  69  0                                        
SHEET    2   J 2 GLU E  77  ILE E  79 -1  O  ILE E  79   N  PHE E  67           
SHEET    1   K 5 LYS E 273  GLY E 278  0                                        
SHEET    2   K 5 THR E 250  GLN E 254  1  N  PHE E 251   O  ILE E 275           
SHEET    3   K 5 ILE E 325  PRO E 328  1  O  ILE E 325   N  VAL E 252           
SHEET    4   K 5 ILE E 347  ALA E 349  1  O  ALA E 349   N  LEU E 326           
SHEET    5   K 5 MET E 370  ILE E 372  1  O  MET E 370   N  ILE E 348           
SHEET    1   L 5 LYS F 273  GLY F 278  0                                        
SHEET    2   L 5 THR F 250  GLN F 254  1  N  PHE F 251   O  LYS F 273           
SHEET    3   L 5 ILE F 325  PRO F 328  1  O  ILE F 327   N  VAL F 252           
SHEET    4   L 5 ILE F 347  ALA F 349  1  O  ILE F 347   N  LEU F 326           
SHEET    5   L 5 MET F 370  ILE F 372  1  O  ILE F 372   N  ILE F 348           
CRYST1   96.920   98.640  124.260  86.48  69.69  60.87 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      0.010318 -0.005750 -0.004614        0.00000                         
SCALE2      0.000000  0.011606  0.001537        0.00000                         
SCALE3      0.000000  0.000000  0.008656        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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