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Database: PDB
Entry: 1NZW
LinkDB: 1NZW
Original site: 1NZW 
HEADER    OXIDOREDUCTASE                          20-FEB-03   1NZW              
TITLE     CYS302SER MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE        
TITLE    2 COMPLEXED WITH NADH AND MG2+                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDEHYDE DEHYDROGENASE;                                    
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: COMPLETE MATURE SEQUENCE (DOES NOT CONTAIN MITOCHONDRIAL   
COMPND   5 LEADER SEQUENCE).;                                                   
COMPND   6 SYNONYM: ALDH CLASS 2, ALDHI, ALDH-E2;                               
COMPND   7 EC: 1.2.1.3;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ALDH2 OR ALDM;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET7-7                                    
KEYWDS    ALDH, NAD, NADH, ISOMERIZATION, OXIDOREDUCTASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.J.PEREZ-MILLER,T.D.HURLEY                                           
REVDAT   4   04-APR-18 1NZW    1       REMARK                                   
REVDAT   3   30-OCT-13 1NZW    1       HETATM HETNAM VERSN                      
REVDAT   2   24-FEB-09 1NZW    1       VERSN                                    
REVDAT   1   24-JUN-03 1NZW    0                                                
JRNL        AUTH   S.J.PEREZ-MILLER,T.D.HURLEY                                  
JRNL        TITL   COENZYME ISOMERIZATION IS INTEGRAL TO CATALYSIS IN ALDEHYDE  
JRNL        TITL 2 DEHYDROGENASE                                                
JRNL        REF    BIOCHEMISTRY                  V.  42  7100 2003              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   12795606                                                     
JRNL        DOI    10.1021/BI034182W                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 4700324.580                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 100409                         
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) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4997                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.74                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7222                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3260                       
REMARK   3   BIN FREE R VALUE                    : 0.3730                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 348                          
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            : 30384                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 368                                     
REMARK   3   SOLVENT ATOMS            : 820                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 19.73000                                             
REMARK   3    B22 (A**2) : -8.40000                                             
REMARK   3    B33 (A**2) : -11.33000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.44                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.39                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.54                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.030                           
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) : 1.060 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.710 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.620 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.460 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.29                                                 
REMARK   3   BSOL        : 10.00                                                
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.PARAM                                  
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : PARAMETER.NAD                                  
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : TOPOLOGY.NAD                                   
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD TARGET USING           
REMARK   3  AMPLITUDES                                                          
REMARK   4                                                                      
REMARK   4 1NZW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000018400.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-AUG-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 6.4                                
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC CONFOCAL                     
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   : 100497                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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: 1CW3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: ACES, PEG 6000, GUANIDINE HCL, MGCL2,    
REMARK 280  DTT. CRYSTAL SOAKED WITH NADH AT PH 7.0 PRIOR TO DATA               
REMARK 280  COLLECTION., PH 6.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE     
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       70.68050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.46150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.24700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.46150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       70.68050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.24700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 26360 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -177.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 26500 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 57360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -181.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     SER B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     SER C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     GLN C     6                                                      
REMARK 465     SER D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     GLN D     6                                                      
REMARK 465     SER E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     ALA E     4                                                      
REMARK 465     THR E     5                                                      
REMARK 465     GLN E     6                                                      
REMARK 465     SER F     1                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     ALA F     3                                                      
REMARK 465     ALA F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     GLN F     6                                                      
REMARK 465     SER G     1                                                      
REMARK 465     ALA G     2                                                      
REMARK 465     ALA G     3                                                      
REMARK 465     ALA G     4                                                      
REMARK 465     THR G     5                                                      
REMARK 465     GLN G     6                                                      
REMARK 465     SER H     1                                                      
REMARK 465     ALA H     2                                                      
REMARK 465     ALA H     3                                                      
REMARK 465     ALA H     4                                                      
REMARK 465     THR H     5                                                      
REMARK 465     GLN H     6                                                      
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    ASN A  20       27.44   -151.71                                   
REMARK 500    VAL A 120      -72.38   -111.12                                   
REMARK 500    THR A 227      -83.74    -93.81                                   
REMARK 500    SER A 260     -112.97    -97.30                                   
REMARK 500    LEU A 269       67.62   -116.96                                   
REMARK 500    LYS A 272       54.13   -144.85                                   
REMARK 500    TYR A 379       63.60   -111.09                                   
REMARK 500    LYS A 411      -64.93   -105.44                                   
REMARK 500    LYS A 469     -127.98     48.80                                   
REMARK 500    LEU A 477      156.66     72.51                                   
REMARK 500    GLN B  14       57.88   -142.66                                   
REMARK 500    ASN B  20       27.78   -152.02                                   
REMARK 500    VAL B 120      -70.43   -110.95                                   
REMARK 500    THR B 227      -85.14    -90.66                                   
REMARK 500    SER B 260     -107.67    -97.07                                   
REMARK 500    LEU B 269       67.83   -119.52                                   
REMARK 500    GLN B 300       59.22    -91.57                                   
REMARK 500    TYR B 379       62.26   -110.91                                   
REMARK 500    LYS B 411      -66.49   -105.16                                   
REMARK 500    LYS B 469     -128.73     48.49                                   
REMARK 500    LEU B 477      159.46     70.95                                   
REMARK 500    ASN C  20       27.34   -148.93                                   
REMARK 500    THR C 227      -84.53    -93.35                                   
REMARK 500    SER C 260     -108.36    -98.20                                   
REMARK 500    LEU C 269       55.41   -117.16                                   
REMARK 500    GLN C 300       57.60    -94.01                                   
REMARK 500    TYR C 379       64.38   -111.94                                   
REMARK 500    LYS C 411      -65.86   -104.94                                   
REMARK 500    LYS C 469     -128.56     51.01                                   
REMARK 500    LEU C 477      160.21     73.11                                   
REMARK 500    GLN D  13      -15.78    -34.51                                   
REMARK 500    GLN D  14       78.82   -161.04                                   
REMARK 500    ASN D  20       27.95   -155.10                                   
REMARK 500    ARG D  34       -1.41     70.58                                   
REMARK 500    VAL D 120      -72.42   -110.77                                   
REMARK 500    THR D 227      -80.38    -95.38                                   
REMARK 500    SER D 260     -108.57    -98.39                                   
REMARK 500    LEU D 269       63.54   -116.83                                   
REMARK 500    LYS D 272       56.30   -142.01                                   
REMARK 500    GLN D 300       56.39    -91.99                                   
REMARK 500    TYR D 379       64.18   -110.69                                   
REMARK 500    LYS D 469     -126.59     48.47                                   
REMARK 500    LEU D 477      160.16     72.89                                   
REMARK 500    ASN E  20       26.64   -151.81                                   
REMARK 500    THR E 227      -82.63    -97.17                                   
REMARK 500    SER E 260     -109.93    -95.76                                   
REMARK 500    LEU E 269       66.71   -116.08                                   
REMARK 500    LYS E 272       55.53   -140.78                                   
REMARK 500    TYR E 379       61.58   -110.35                                   
REMARK 500    LYS E 411      -64.57   -109.55                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      81 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1601  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 196   O                                                      
REMARK 620 2 VAL A  40   O   165.8                                              
REMARK 620 3 ASP A 109   OD1  85.5  95.4                                        
REMARK 620 4 ASP A 109   O   101.4  92.4  72.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAI A1502   O2A                                                    
REMARK 620 2 NAI A1502   O1N  89.4                                              
REMARK 620 3 HOH A1756   O   104.8  81.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B1602  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2582   O                                                      
REMARK 620 2 ASP B 109   OD1 139.4                                              
REMARK 620 3 VAL B  40   O    68.3 107.6                                        
REMARK 620 4 GLN B 196   O   101.2  80.3 169.5                                  
REMARK 620 5 THR B  39   OG1 150.9  69.6 106.0  83.1                            
REMARK 620 6 ASP B 109   O    78.0  61.4  85.1  92.9 130.8                      
REMARK 620 7 HOH B2571   O    65.3 153.7  89.0  86.2  86.5 142.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1702  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAI B2502   O1N                                                    
REMARK 620 2 NAI B2502   O2A  76.5                                              
REMARK 620 3 HOH B2563   O    79.0  80.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C1603  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 196   O                                                      
REMARK 620 2 VAL C  40   O   166.6                                              
REMARK 620 3 ASP C 109   OD1  74.9 100.0                                        
REMARK 620 4 HOH C3549   O    83.6 107.9 135.5                                  
REMARK 620 5 ASP C 109   O    94.9  93.9  64.6  79.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1703  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAI C3502   O1N                                                    
REMARK 620 2 NAI C3502   O2A  84.1                                              
REMARK 620 3 HOH C3611   O   101.0  94.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D1604  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 109   O                                                      
REMARK 620 2 VAL D  40   O   100.7                                              
REMARK 620 3 ASP D 109   OD1  70.3 109.4                                        
REMARK 620 4 GLN D 196   O   101.1 157.3  72.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1704  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAI D4502   O1N                                                    
REMARK 620 2 NAI D4502   O2A  71.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA E1605  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN E 196   O                                                      
REMARK 620 2 ASP E 109   OD1  77.3                                              
REMARK 620 3 ASP E 109   O   110.3  72.1                                        
REMARK 620 4 VAL E  40   O   144.9  93.2  98.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E1705  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAI E5502   O2A                                                    
REMARK 620 2 HOH E5538   O    77.2                                              
REMARK 620 3 HOH E5584   O    88.1  72.4                                        
REMARK 620 4 NAI E5502   O1N  76.1 128.5  63.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA F1606  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 109   OD1                                                    
REMARK 620 2 VAL F  40   O    93.8                                              
REMARK 620 3 GLN F 196   O    74.5 155.5                                        
REMARK 620 4 ASP F 109   O    67.5  94.5 100.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F1706  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAI F6502   O2A                                                    
REMARK 620 2 HOH F6525   O    71.4                                              
REMARK 620 3 NAI F6502   O1N  79.3  72.0                                        
REMARK 620 4 HOH F6621   O    82.4  84.5 153.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA G1607  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 109   O                                                      
REMARK 620 2 VAL G  40   O   101.5                                              
REMARK 620 3 GLN G 196   O    99.2 159.1                                        
REMARK 620 4 ASP G 109   OD1  73.3 108.6  79.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G1707  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAI G7502   O2A                                                    
REMARK 620 2 NAI G7502   O1N  77.3                                              
REMARK 620 3 HOH G7536   O    73.9  65.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA H1608  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN H 196   O                                                      
REMARK 620 2 ASP H 109   OD1  73.0                                              
REMARK 620 3 VAL H  40   O   155.1  97.4                                        
REMARK 620 4 ASP H 109   O   102.4  66.8  94.2                                  
REMARK 620 5 HOH H8543   O    79.4 121.2  86.8 171.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H1708  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAI H8502   O1N                                                    
REMARK 620 2 HOH H8542   O    87.6                                              
REMARK 620 3 NAI H8502   O2A  84.6  79.4                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 1603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 1604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 1605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 1606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 1607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 1608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 1705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 1706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 1707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 1708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI A 1502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B 2502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI C 3502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI D 4502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI E 5502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI F 6502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI G 7502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI H 8502                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CW3   RELATED DB: PDB                                   
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NAD+ AND   
REMARK 900 MN2+                                                                 
REMARK 900 RELATED ID: 1AG8   RELATED DB: PDB                                   
REMARK 900 ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA (APO)                
REMARK 900 RELATED ID: 1A4Z   RELATED DB: PDB                                   
REMARK 900 ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA COMPLEXED WITH NAD   
REMARK 900 AND SM3+                                                             
REMARK 900 RELATED ID: 1NZX   RELATED DB: PDB                                   
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NAD+ IN    
REMARK 900 THE PRESENCE OF LOW MG2+                                             
REMARK 900 RELATED ID: 1NZZ   RELATED DB: PDB                                   
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NADH IN    
REMARK 900 THE PRESENCE OF LOW MG2+                                             
REMARK 900 RELATED ID: 1O00   RELATED DB: PDB                                   
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NAD+ AND   
REMARK 900 MG2+ SHOWING DUAL NAD CONFORMATIONS                                  
REMARK 900 RELATED ID: 1O01   RELATED DB: PDB                                   
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH            
REMARK 900 CROTONALDEHYDE, NAD(H) AND MG2+                                      
REMARK 900 RELATED ID: 1O02   RELATED DB: PDB                                   
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NADH IN    
REMARK 900 THE PRESENCE OF MG2+                                                 
REMARK 900 RELATED ID: 1O04   RELATED DB: PDB                                   
REMARK 900 CYS302SER MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE       
REMARK 900 COMPLEXED WITH NAD+ AND MG2+                                         
REMARK 900 RELATED ID: 1O05   RELATED DB: PDB                                   
REMARK 900 APO FORM OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE               
DBREF  1NZW A    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1NZW B    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1NZW C    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1NZW D    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1NZW E    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1NZW F    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1NZW G    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1NZW H    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
SEQADV 1NZW SER A  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 1NZW SER B  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 1NZW SER C  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 1NZW SER D  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 1NZW SER E  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 1NZW SER F  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 1NZW SER G  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 1NZW SER H  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQRES   1 A  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 A  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 A  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 A  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 A  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 A  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 A  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 A  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 A  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 A  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 A  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 A  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 A  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 A  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 A  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 A  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 A  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 A  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 A  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 A  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 A  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 A  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 A  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 A  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 A  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 A  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 A  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 A  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 A  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 A  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 A  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 A  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 A  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 A  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 A  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 A  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 A  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 A  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 A  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 B  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 B  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 B  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 B  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 B  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 B  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 B  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 B  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 B  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 B  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 B  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 B  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 B  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 B  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 B  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 B  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 B  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 B  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 B  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 B  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 B  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 B  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 B  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 B  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 B  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 B  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 B  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 B  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 B  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 B  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 B  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 B  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 B  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 B  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 B  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 B  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 B  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 B  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 B  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 C  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 C  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 C  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 C  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 C  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 C  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 C  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 C  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 C  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 C  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 C  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 C  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 C  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 C  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 C  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 C  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 C  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 C  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 C  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 C  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 C  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 C  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 C  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 C  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 C  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 C  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 C  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 C  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 C  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 C  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 C  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 C  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 C  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 C  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 C  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 C  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 C  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 C  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 C  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 D  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 D  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 D  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 D  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 D  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 D  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 D  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 D  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 D  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 D  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 D  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 D  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 D  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 D  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 D  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 D  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 D  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 D  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 D  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 D  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 D  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 D  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 D  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 D  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 D  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 D  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 D  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 D  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 D  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 D  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 D  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 D  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 D  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 D  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 D  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 D  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 D  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 D  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 D  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 E  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 E  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 E  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 E  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 E  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 E  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 E  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 E  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 E  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 E  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 E  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 E  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 E  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 E  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 E  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 E  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 E  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 E  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 E  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 E  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 E  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 E  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 E  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 E  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 E  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 E  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 E  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 E  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 E  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 E  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 E  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 E  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 E  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 E  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 E  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 E  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 E  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 E  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 E  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 F  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 F  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 F  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 F  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 F  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 F  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 F  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 F  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 F  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 F  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 F  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 F  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 F  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 F  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 F  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 F  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 F  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 F  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 F  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 F  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 F  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 F  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 F  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 F  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 F  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 F  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 F  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 F  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 F  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 F  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 F  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 F  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 F  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 F  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 F  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 F  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 F  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 F  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 F  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 G  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 G  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 G  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 G  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 G  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 G  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 G  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 G  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 G  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 G  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 G  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 G  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 G  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 G  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 G  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 G  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 G  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 G  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 G  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 G  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 G  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 G  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 G  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 G  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 G  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 G  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 G  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 G  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 G  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 G  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 G  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 G  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 G  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 G  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 G  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 G  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 G  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 G  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 G  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 H  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 H  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 H  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 H  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 H  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 H  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 H  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 H  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 H  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 H  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 H  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 H  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 H  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 H  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 H  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 H  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 H  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 H  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 H  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 H  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 H  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 H  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 H  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 H  500  GLN CYS SER CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 H  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 H  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 H  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 H  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 H  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 H  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 H  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 H  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 H  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 H  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 H  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 H  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 H  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 H  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 H  500  VAL PRO GLN LYS ASN SER                                      
HET     NA  A1601       1                                                       
HET     MG  A1701       1                                                       
HET    NAI  A1502      44                                                       
HET     NA  B1602       1                                                       
HET     MG  B1702       1                                                       
HET    NAI  B2502      44                                                       
HET     NA  C1603       1                                                       
HET     MG  C1703       1                                                       
HET    NAI  C3502      44                                                       
HET     NA  D1604       1                                                       
HET     MG  D1704       1                                                       
HET    NAI  D4502      44                                                       
HET     NA  E1605       1                                                       
HET     MG  E1705       1                                                       
HET    NAI  E5502      44                                                       
HET     NA  F1606       1                                                       
HET     MG  F1706       1                                                       
HET    NAI  F6502      44                                                       
HET     NA  G1607       1                                                       
HET     MG  G1707       1                                                       
HET    NAI  G7502      44                                                       
HET     NA  H1608       1                                                       
HET     MG  H1708       1                                                       
HET    NAI  H8502      44                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETSYN     NAI NADH                                                             
FORMUL   9   NA    8(NA 1+)                                                     
FORMUL  10   MG    8(MG 2+)                                                     
FORMUL  11  NAI    8(C21 H29 N7 O14 P2)                                         
FORMUL  33  HOH   *820(H2 O)                                                    
HELIX    1   1 ASP A   55  GLN A   71  1                                  17    
HELIX    2   2 SER A   74  MET A   79  1                                   6    
HELIX    3   3 ASP A   80  ASP A   98  1                                  19    
HELIX    4   4 ASP A   98  GLY A  111  1                                  14    
HELIX    5   5 PRO A  113  VAL A  120  1                                   8    
HELIX    6   6 VAL A  120  ALA A  136  1                                  17    
HELIX    7   7 PHE A  170  THR A  185  1                                  16    
HELIX    8   8 PRO A  198  GLY A  212  1                                  15    
HELIX    9   9 THR A  227  HIS A  235  1                                   9    
HELIX   10  10 SER A  246  SER A  260  1                                  15    
HELIX   11  11 ASP A  282  PHE A  296  1                                  15    
HELIX   12  12 ASN A  297  GLN A  300  5                                   4    
HELIX   13  13 GLU A  312  SER A  328  1                                  17    
HELIX   14  14 ASP A  346  GLU A  363  1                                  18    
HELIX   15  15 MET A  393  LYS A  397  5                                   5    
HELIX   16  16 THR A  412  ASN A  422  1                                  11    
HELIX   17  17 ASP A  435  LEU A  446  1                                  12    
HELIX   18  18 TYR A  468  MET A  470  5                                   3    
HELIX   19  19 GLU A  479  ALA A  484  5                                   6    
HELIX   20  20 ASP B   55  GLN B   71  1                                  17    
HELIX   21  21 SER B   74  MET B   79  1                                   6    
HELIX   22  22 ASP B   80  ASP B   98  1                                  19    
HELIX   23  23 ASP B   98  GLY B  111  1                                  14    
HELIX   24  24 PRO B  113  VAL B  120  1                                   8    
HELIX   25  25 VAL B  120  ALA B  136  1                                  17    
HELIX   26  26 PHE B  170  THR B  185  1                                  16    
HELIX   27  27 PRO B  198  GLY B  212  1                                  15    
HELIX   28  28 THR B  227  HIS B  235  1                                   9    
HELIX   29  29 SER B  246  SER B  260  1                                  15    
HELIX   30  30 ASP B  282  PHE B  296  1                                  15    
HELIX   31  31 ASN B  297  GLN B  300  5                                   4    
HELIX   32  32 GLU B  312  SER B  328  1                                  17    
HELIX   33  33 ASP B  346  GLU B  363  1                                  18    
HELIX   34  34 MET B  393  GLU B  398  1                                   6    
HELIX   35  35 THR B  412  ASN B  422  1                                  11    
HELIX   36  36 ASP B  435  LEU B  446  1                                  12    
HELIX   37  37 TYR B  468  MET B  470  5                                   3    
HELIX   38  38 GLU B  479  ALA B  484  5                                   6    
HELIX   39  39 ASP C   55  PHE C   70  1                                  16    
HELIX   40  40 SER C   74  MET C   79  1                                   6    
HELIX   41  41 ASP C   80  ASP C   98  1                                  19    
HELIX   42  42 ASP C   98  GLY C  111  1                                  14    
HELIX   43  43 PRO C  113  VAL C  120  1                                   8    
HELIX   44  44 VAL C  120  ALA C  136  1                                  17    
HELIX   45  45 PHE C  170  THR C  185  1                                  16    
HELIX   46  46 PRO C  198  GLY C  212  1                                  15    
HELIX   47  47 THR C  227  HIS C  235  1                                   9    
HELIX   48  48 SER C  246  SER C  260  1                                  15    
HELIX   49  49 ASP C  282  PHE C  296  1                                  15    
HELIX   50  50 ASN C  297  GLN C  300  5                                   4    
HELIX   51  51 GLU C  312  ARG C  329  1                                  18    
HELIX   52  52 ASP C  346  GLU C  363  1                                  18    
HELIX   53  53 MET C  393  LYS C  397  5                                   5    
HELIX   54  54 THR C  412  ASN C  422  1                                  11    
HELIX   55  55 ASP C  435  LEU C  446  1                                  12    
HELIX   56  56 TYR C  468  MET C  470  5                                   3    
HELIX   57  57 GLY C  478  ALA C  484  5                                   7    
HELIX   58  58 ASP D   55  PHE D   70  1                                  16    
HELIX   59  59 SER D   74  MET D   79  1                                   6    
HELIX   60  60 ASP D   80  ASP D   98  1                                  19    
HELIX   61  61 ASP D   98  GLY D  111  1                                  14    
HELIX   62  62 PRO D  113  VAL D  120  1                                   8    
HELIX   63  63 VAL D  120  ALA D  136  1                                  17    
HELIX   64  64 PHE D  170  THR D  185  1                                  16    
HELIX   65  65 PRO D  198  GLY D  212  1                                  15    
HELIX   66  66 THR D  227  SER D  234  1                                   8    
HELIX   67  67 SER D  246  SER D  260  1                                  15    
HELIX   68  68 ASP D  282  PHE D  296  1                                  15    
HELIX   69  69 ASN D  297  GLN D  300  5                                   4    
HELIX   70  70 GLU D  312  ARG D  329  1                                  18    
HELIX   71  71 ASP D  346  GLU D  363  1                                  18    
HELIX   72  72 MET D  393  GLU D  398  1                                   6    
HELIX   73  73 THR D  412  ASN D  422  1                                  11    
HELIX   74  74 ASP D  435  LEU D  446  1                                  12    
HELIX   75  75 TYR D  468  MET D  470  5                                   3    
HELIX   76  76 GLU D  479  ALA D  484  5                                   6    
HELIX   77  77 ASP E   55  PHE E   70  1                                  16    
HELIX   78  78 SER E   74  MET E   79  1                                   6    
HELIX   79  79 ASP E   80  ASP E   98  1                                  19    
HELIX   80  80 ASP E   98  GLY E  111  1                                  14    
HELIX   81  81 PRO E  113  VAL E  120  1                                   8    
HELIX   82  82 VAL E  120  ALA E  136  1                                  17    
HELIX   83  83 PHE E  170  THR E  185  1                                  16    
HELIX   84  84 PRO E  198  GLY E  212  1                                  15    
HELIX   85  85 THR E  227  SER E  234  1                                   8    
HELIX   86  86 SER E  246  SER E  260  1                                  15    
HELIX   87  87 ASP E  282  PHE E  296  1                                  15    
HELIX   88  88 ASN E  297  GLN E  300  5                                   4    
HELIX   89  89 GLU E  312  SER E  328  1                                  17    
HELIX   90  90 ASP E  346  GLU E  363  1                                  18    
HELIX   91  91 MET E  393  LYS E  397  5                                   5    
HELIX   92  92 THR E  412  ASN E  422  1                                  11    
HELIX   93  93 ASP E  435  LEU E  446  1                                  12    
HELIX   94  94 TYR E  468  MET E  470  5                                   3    
HELIX   95  95 GLY E  478  ALA E  484  5                                   7    
HELIX   96  96 ASP F   55  GLN F   71  1                                  17    
HELIX   97  97 SER F   74  MET F   79  1                                   6    
HELIX   98  98 ASP F   80  ASP F   98  1                                  19    
HELIX   99  99 ASP F   98  GLY F  111  1                                  14    
HELIX  100 100 PRO F  113  VAL F  120  1                                   8    
HELIX  101 101 VAL F  120  ALA F  136  1                                  17    
HELIX  102 102 PHE F  170  THR F  185  1                                  16    
HELIX  103 103 PRO F  198  GLY F  212  1                                  15    
HELIX  104 104 THR F  227  HIS F  235  1                                   9    
HELIX  105 105 SER F  246  SER F  260  1                                  15    
HELIX  106 106 ASP F  282  PHE F  296  1                                  15    
HELIX  107 107 ASN F  297  GLN F  300  5                                   4    
HELIX  108 108 GLU F  312  ARG F  329  1                                  18    
HELIX  109 109 ASP F  346  GLU F  363  1                                  18    
HELIX  110 110 MET F  393  LYS F  397  5                                   5    
HELIX  111 111 THR F  412  ASN F  422  1                                  11    
HELIX  112 112 ASP F  435  LEU F  446  1                                  12    
HELIX  113 113 TYR F  468  MET F  470  5                                   3    
HELIX  114 114 GLY F  478  ALA F  484  5                                   7    
HELIX  115 115 ASP G   55  PHE G   70  1                                  16    
HELIX  116 116 SER G   74  MET G   79  1                                   6    
HELIX  117 117 ASP G   80  ASP G   98  1                                  19    
HELIX  118 118 ASP G   98  GLY G  111  1                                  14    
HELIX  119 119 PRO G  113  VAL G  120  1                                   8    
HELIX  120 120 VAL G  120  ALA G  136  1                                  17    
HELIX  121 121 PHE G  170  THR G  185  1                                  16    
HELIX  122 122 PRO G  198  GLY G  212  1                                  15    
HELIX  123 123 THR G  227  HIS G  235  1                                   9    
HELIX  124 124 SER G  246  SER G  260  1                                  15    
HELIX  125 125 ASP G  282  PHE G  296  1                                  15    
HELIX  126 126 ASN G  297  GLN G  300  5                                   4    
HELIX  127 127 GLU G  312  SER G  328  1                                  17    
HELIX  128 128 ASP G  346  GLU G  363  1                                  18    
HELIX  129 129 MET G  393  GLU G  398  1                                   6    
HELIX  130 130 THR G  412  ASN G  422  1                                  11    
HELIX  131 131 ASP G  435  LEU G  446  1                                  12    
HELIX  132 132 TYR G  468  MET G  470  5                                   3    
HELIX  133 133 GLU G  479  ALA G  484  5                                   6    
HELIX  134 134 ASP H   55  GLN H   71  1                                  17    
HELIX  135 135 SER H   74  MET H   79  1                                   6    
HELIX  136 136 ASP H   80  ASP H   98  1                                  19    
HELIX  137 137 ASP H   98  GLY H  111  1                                  14    
HELIX  138 138 PRO H  113  VAL H  120  1                                   8    
HELIX  139 139 VAL H  120  ALA H  136  1                                  17    
HELIX  140 140 PHE H  170  THR H  185  1                                  16    
HELIX  141 141 PRO H  198  GLY H  212  1                                  15    
HELIX  142 142 THR H  227  HIS H  235  1                                   9    
HELIX  143 143 SER H  246  SER H  260  1                                  15    
HELIX  144 144 ASP H  282  PHE H  296  1                                  15    
HELIX  145 145 ASN H  297  GLN H  300  5                                   4    
HELIX  146 146 GLU H  312  SER H  328  1                                  17    
HELIX  147 147 ASP H  346  GLU H  363  1                                  18    
HELIX  148 148 MET H  393  LYS H  397  5                                   5    
HELIX  149 149 THR H  412  ASN H  422  1                                  11    
HELIX  150 150 ASP H  435  LEU H  446  1                                  12    
HELIX  151 151 TYR H  468  MET H  470  5                                   3    
HELIX  152 152 GLU H  479  ALA H  484  5                                   6    
SHEET    1   A 2 ILE A  22  ILE A  24  0                                        
SHEET    2   A 2 GLU A  27  HIS A  29 -1  O  HIS A  29   N  ILE A  22           
SHEET    1   B 2 THR A  36  VAL A  40  0                                        
SHEET    2   B 2 VAL A  47  ALA A  52 -1  O  ILE A  48   N  THR A  39           
SHEET    1   C20 LYS B 366  CYS B 369  0                                        
SHEET    2   C20 THR B 384  GLY B 387 -1  O  GLY B 387   N  LYS B 366           
SHEET    3   C20 VAL B 404  PHE B 410  1  O  MET B 405   N  PHE B 386           
SHEET    4   C20 ARG B 307  GLN B 311  1  N  VAL B 310   O  LEU B 408           
SHEET    5   C20 PRO B 274  ILE B 277  1  N  ASN B 275   O  ARG B 307           
SHEET    6   C20 ALA B 428  PHE B 432  1  O  PHE B 432   N  ILE B 276           
SHEET    7   C20 THR B 450  VAL B 453  1  O  TRP B 452   N  ALA B 429           
SHEET    8   C20 THR A 486  LYS A 494  1  N  THR A 490   O  VAL B 451           
SHEET    9   C20 PHE A 150  PRO A 158 -1  N  TYR A 153   O  VAL A 491           
SHEET   10   C20 GLY A 141  ILE A 144 -1  N  ILE A 144   O  SER A 152           
SHEET   11   C20 GLY D 141  ILE D 144 -1  O  THR D 143   N  GLY A 141           
SHEET   12   C20 PHE D 150  PRO D 158 -1  O  SER D 152   N  ILE D 144           
SHEET   13   C20 THR D 486  LYS D 494 -1  O  GLU D 487   N  GLU D 157           
SHEET   14   C20 THR C 450  VAL C 453  1  N  VAL C 451   O  THR D 490           
SHEET   15   C20 ALA C 428  PHE C 432  1  N  ALA C 429   O  TRP C 452           
SHEET   16   C20 PRO C 274  ILE C 277  1  N  ILE C 276   O  PHE C 432           
SHEET   17   C20 ARG C 307  GLN C 311  1  O  ARG C 307   N  ASN C 275           
SHEET   18   C20 VAL C 404  PHE C 410  1  O  LEU C 408   N  THR C 308           
SHEET   19   C20 THR C 384  GLY C 387  1  N  PHE C 386   O  MET C 405           
SHEET   20   C20 LYS C 366  CYS C 369 -1  N  LYS C 366   O  GLY C 387           
SHEET    1   D 6 VAL A 218  ILE A 220  0                                        
SHEET    2   D 6 VAL A 188  LYS A 192  1  N  MET A 191   O  ASN A 219           
SHEET    3   D 6 VAL A 161  ILE A 165  1  N  CYS A 162   O  VAL A 188           
SHEET    4   D 6 LYS A 240  THR A 244  1  O  LYS A 240   N  GLY A 163           
SHEET    5   D 6 ARG A 264  GLU A 268  1  O  ARG A 264   N  VAL A 241           
SHEET    6   D 6 GLY A 472  SER A 473 -1  O  SER A 473   N  LEU A 267           
SHEET    1   E20 LYS A 366  CYS A 369  0                                        
SHEET    2   E20 THR A 384  GLY A 387 -1  O  GLY A 387   N  LYS A 366           
SHEET    3   E20 VAL A 404  PHE A 410  1  O  MET A 405   N  THR A 384           
SHEET    4   E20 ARG A 307  GLN A 311  1  N  THR A 308   O  LEU A 408           
SHEET    5   E20 PRO A 274  ILE A 277  1  N  ASN A 275   O  ARG A 307           
SHEET    6   E20 ALA A 428  PHE A 432  1  O  ALA A 430   N  ILE A 276           
SHEET    7   E20 THR A 450  VAL A 453  1  O  TRP A 452   N  ALA A 429           
SHEET    8   E20 THR B 486  LYS B 494  1  O  THR B 490   N  VAL A 451           
SHEET    9   E20 PHE B 150  PRO B 158 -1  N  TYR B 153   O  VAL B 491           
SHEET   10   E20 GLY B 141  ILE B 144 -1  N  ILE B 144   O  SER B 152           
SHEET   11   E20 GLY C 141  ILE C 144 -1  O  THR C 143   N  GLY B 141           
SHEET   12   E20 PHE C 150  PRO C 158 -1  O  SER C 152   N  ILE C 144           
SHEET   13   E20 THR C 486  LYS C 494 -1  O  GLU C 487   N  GLU C 157           
SHEET   14   E20 THR D 450  VAL D 453  1  O  VAL D 451   N  THR C 490           
SHEET   15   E20 ALA D 428  PHE D 432  1  N  ALA D 429   O  TRP D 452           
SHEET   16   E20 PRO D 274  ILE D 277  1  N  ILE D 276   O  ALA D 430           
SHEET   17   E20 ARG D 307  GLN D 311  1  O  ARG D 307   N  ASN D 275           
SHEET   18   E20 VAL D 404  PHE D 410  1  O  LEU D 408   N  THR D 308           
SHEET   19   E20 THR D 384  GLY D 387  1  N  PHE D 386   O  MET D 405           
SHEET   20   E20 LYS D 366  CYS D 369 -1  N  LYS D 366   O  GLY D 387           
SHEET    1   F 2 ILE B  22  ILE B  24  0                                        
SHEET    2   F 2 GLU B  27  HIS B  29 -1  O  HIS B  29   N  ILE B  22           
SHEET    1   G 2 THR B  36  VAL B  40  0                                        
SHEET    2   G 2 VAL B  47  ALA B  52 -1  O  ILE B  48   N  THR B  39           
SHEET    1   H 6 VAL B 218  ILE B 220  0                                        
SHEET    2   H 6 VAL B 188  LYS B 192  1  N  MET B 191   O  ASN B 219           
SHEET    3   H 6 VAL B 161  ILE B 165  1  N  CYS B 162   O  VAL B 188           
SHEET    4   H 6 LYS B 240  THR B 244  1  O  LYS B 240   N  GLY B 163           
SHEET    5   H 6 ARG B 264  GLU B 268  1  O  ARG B 264   N  VAL B 241           
SHEET    6   H 6 GLY B 472  SER B 473 -1  O  SER B 473   N  LEU B 267           
SHEET    1   I 2 ILE C  22  ILE C  24  0                                        
SHEET    2   I 2 GLU C  27  HIS C  29 -1  O  HIS C  29   N  ILE C  22           
SHEET    1   J 2 THR C  36  VAL C  40  0                                        
SHEET    2   J 2 VAL C  47  ALA C  52 -1  O  ILE C  48   N  THR C  39           
SHEET    1   K 6 VAL C 218  ILE C 220  0                                        
SHEET    2   K 6 VAL C 188  LYS C 192  1  N  MET C 191   O  ASN C 219           
SHEET    3   K 6 VAL C 161  ILE C 165  1  N  GLN C 164   O  LYS C 192           
SHEET    4   K 6 LYS C 240  THR C 244  1  O  LYS C 240   N  GLY C 163           
SHEET    5   K 6 ARG C 264  GLU C 268  1  O  ARG C 264   N  VAL C 241           
SHEET    6   K 6 GLY C 472  SER C 473 -1  O  SER C 473   N  LEU C 267           
SHEET    1   L 2 ILE D  22  ILE D  24  0                                        
SHEET    2   L 2 GLU D  27  HIS D  29 -1  O  HIS D  29   N  ILE D  22           
SHEET    1   M 2 THR D  36  VAL D  40  0                                        
SHEET    2   M 2 VAL D  47  ALA D  52 -1  O  ILE D  48   N  THR D  39           
SHEET    1   N 6 VAL D 218  ILE D 220  0                                        
SHEET    2   N 6 VAL D 188  LYS D 192  1  N  MET D 191   O  ASN D 219           
SHEET    3   N 6 VAL D 161  ILE D 165  1  N  CYS D 162   O  VAL D 188           
SHEET    4   N 6 LYS D 240  THR D 244  1  O  LYS D 240   N  GLY D 163           
SHEET    5   N 6 ARG D 264  GLU D 268  1  O  ARG D 264   N  VAL D 241           
SHEET    6   N 6 GLY D 472  SER D 473 -1  O  SER D 473   N  LEU D 267           
SHEET    1   O 2 ILE E  22  ILE E  24  0                                        
SHEET    2   O 2 GLU E  27  HIS E  29 -1  O  HIS E  29   N  ILE E  22           
SHEET    1   P 2 THR E  36  VAL E  40  0                                        
SHEET    2   P 2 VAL E  47  ALA E  52 -1  O  ILE E  48   N  THR E  39           
SHEET    1   Q20 LYS F 366  CYS F 369  0                                        
SHEET    2   Q20 THR F 384  GLY F 387 -1  O  GLY F 387   N  LYS F 366           
SHEET    3   Q20 VAL F 404  PHE F 410  1  O  MET F 405   N  PHE F 386           
SHEET    4   Q20 ARG F 307  GLN F 311  1  N  VAL F 310   O  LEU F 408           
SHEET    5   Q20 PRO F 274  ILE F 277  1  N  ASN F 275   O  ARG F 307           
SHEET    6   Q20 ALA F 428  PHE F 432  1  O  ALA F 430   N  ILE F 276           
SHEET    7   Q20 THR F 450  VAL F 453  1  O  TRP F 452   N  ALA F 429           
SHEET    8   Q20 THR E 486  LYS E 494  1  N  THR E 490   O  VAL F 451           
SHEET    9   Q20 PHE E 150  PRO E 158 -1  N  GLU E 157   O  GLU E 487           
SHEET   10   Q20 GLY E 141  ILE E 144 -1  N  ILE E 144   O  SER E 152           
SHEET   11   Q20 GLY H 141  ILE H 144 -1  O  THR H 143   N  GLY E 141           
SHEET   12   Q20 PHE H 150  PRO H 158 -1  O  SER H 152   N  ILE H 144           
SHEET   13   Q20 THR H 486  LYS H 494 -1  O  VAL H 491   N  TYR H 153           
SHEET   14   Q20 THR G 450  VAL G 453  1  N  VAL G 451   O  THR H 490           
SHEET   15   Q20 ALA G 428  PHE G 432  1  N  ALA G 429   O  TRP G 452           
SHEET   16   Q20 PRO G 274  ILE G 277  1  N  ILE G 276   O  PHE G 432           
SHEET   17   Q20 ARG G 307  GLN G 311  1  O  PHE G 309   N  ILE G 277           
SHEET   18   Q20 VAL G 404  PHE G 410  1  O  LEU G 408   N  VAL G 310           
SHEET   19   Q20 THR G 384  GLY G 387  1  N  PHE G 386   O  MET G 405           
SHEET   20   Q20 LYS G 366  CYS G 369 -1  N  LYS G 366   O  GLY G 387           
SHEET    1   R 6 VAL E 218  ILE E 220  0                                        
SHEET    2   R 6 VAL E 188  LYS E 192  1  N  MET E 191   O  ASN E 219           
SHEET    3   R 6 VAL E 161  ILE E 165  1  N  CYS E 162   O  VAL E 188           
SHEET    4   R 6 LYS E 240  THR E 244  1  O  LYS E 240   N  GLY E 163           
SHEET    5   R 6 ARG E 264  GLU E 268  1  O  ARG E 264   N  VAL E 241           
SHEET    6   R 6 GLY E 472  SER E 473 -1  O  SER E 473   N  LEU E 267           
SHEET    1   S20 LYS E 366  CYS E 369  0                                        
SHEET    2   S20 THR E 384  GLY E 387 -1  O  GLY E 387   N  LYS E 366           
SHEET    3   S20 VAL E 404  PHE E 410  1  O  MET E 405   N  PHE E 386           
SHEET    4   S20 ARG E 307  GLN E 311  1  N  VAL E 310   O  LEU E 408           
SHEET    5   S20 PRO E 274  ILE E 277  1  N  ASN E 275   O  ARG E 307           
SHEET    6   S20 ALA E 428  PHE E 432  1  O  ALA E 430   N  ILE E 276           
SHEET    7   S20 THR E 450  VAL E 453  1  O  TRP E 452   N  ALA E 429           
SHEET    8   S20 THR F 486  LYS F 494  1  O  THR F 490   N  VAL E 451           
SHEET    9   S20 PHE F 150  PRO F 158 -1  N  TYR F 153   O  VAL F 491           
SHEET   10   S20 GLY F 141  ILE F 144 -1  N  ILE F 144   O  SER F 152           
SHEET   11   S20 GLY G 141  ILE G 144 -1  O  THR G 143   N  GLY F 141           
SHEET   12   S20 PHE G 150  PRO G 158 -1  O  SER G 152   N  ILE G 144           
SHEET   13   S20 THR G 486  LYS G 494 -1  O  VAL G 491   N  TYR G 153           
SHEET   14   S20 THR H 450  VAL H 453  1  O  VAL H 451   N  THR G 490           
SHEET   15   S20 ALA H 428  PHE H 432  1  N  ALA H 429   O  TRP H 452           
SHEET   16   S20 PRO H 274  ILE H 277  1  N  ILE H 276   O  ALA H 430           
SHEET   17   S20 ARG H 307  GLN H 311  1  O  ARG H 307   N  ASN H 275           
SHEET   18   S20 VAL H 404  PHE H 410  1  O  LEU H 408   N  THR H 308           
SHEET   19   S20 THR H 384  GLY H 387  1  N  PHE H 386   O  MET H 405           
SHEET   20   S20 LYS H 366  CYS H 369 -1  N  LYS H 366   O  GLY H 387           
SHEET    1   T 2 ILE F  22  ILE F  24  0                                        
SHEET    2   T 2 GLU F  27  HIS F  29 -1  O  HIS F  29   N  ILE F  22           
SHEET    1   U 2 THR F  36  VAL F  40  0                                        
SHEET    2   U 2 VAL F  47  ALA F  52 -1  O  ILE F  48   N  THR F  39           
SHEET    1   V 6 VAL F 218  ILE F 220  0                                        
SHEET    2   V 6 VAL F 188  LYS F 192  1  N  MET F 191   O  ASN F 219           
SHEET    3   V 6 VAL F 161  ILE F 165  1  N  CYS F 162   O  VAL F 188           
SHEET    4   V 6 LYS F 240  THR F 244  1  O  LYS F 240   N  GLY F 163           
SHEET    5   V 6 ARG F 264  GLU F 268  1  O  ARG F 264   N  VAL F 241           
SHEET    6   V 6 GLY F 472  SER F 473 -1  O  SER F 473   N  LEU F 267           
SHEET    1   W 2 ILE G  22  ILE G  24  0                                        
SHEET    2   W 2 GLU G  27  HIS G  29 -1  O  HIS G  29   N  ILE G  22           
SHEET    1   X 2 THR G  36  VAL G  40  0                                        
SHEET    2   X 2 VAL G  47  ALA G  52 -1  O  ILE G  48   N  THR G  39           
SHEET    1   Y 6 VAL G 218  ILE G 220  0                                        
SHEET    2   Y 6 VAL G 188  LYS G 192  1  N  MET G 191   O  ASN G 219           
SHEET    3   Y 6 VAL G 161  ILE G 165  1  N  CYS G 162   O  VAL G 188           
SHEET    4   Y 6 LYS G 240  THR G 244  1  O  LYS G 240   N  GLY G 163           
SHEET    5   Y 6 ARG G 264  GLU G 268  1  O  ARG G 264   N  VAL G 241           
SHEET    6   Y 6 GLY G 472  SER G 473 -1  O  SER G 473   N  LEU G 267           
SHEET    1   Z 2 ILE H  22  ILE H  24  0                                        
SHEET    2   Z 2 GLU H  27  HIS H  29 -1  O  HIS H  29   N  ILE H  22           
SHEET    1  AA 2 THR H  36  VAL H  40  0                                        
SHEET    2  AA 2 VAL H  47  ALA H  52 -1  O  ILE H  48   N  THR H  39           
SHEET    1  AB 6 VAL H 218  ILE H 220  0                                        
SHEET    2  AB 6 VAL H 188  LYS H 192  1  N  MET H 191   O  ASN H 219           
SHEET    3  AB 6 VAL H 161  ILE H 165  1  N  CYS H 162   O  VAL H 188           
SHEET    4  AB 6 LYS H 240  THR H 244  1  O  LYS H 240   N  GLY H 163           
SHEET    5  AB 6 ARG H 264  GLU H 268  1  O  ARG H 264   N  VAL H 241           
SHEET    6  AB 6 GLY H 472  SER H 473 -1  O  SER H 473   N  LEU H 267           
SSBOND   1 CYS A  301    CYS A  303                          1555   1555  2.92  
LINK        NA    NA A1601                 O   GLN A 196     1555   1555  2.27  
LINK        NA    NA A1601                 O   VAL A  40     1555   1555  2.45  
LINK        NA    NA A1601                 OD1 ASP A 109     1555   1555  2.41  
LINK        MG    MG A1701                 O2A NAI A1502     1555   1555  2.28  
LINK        MG    MG A1701                 O1N NAI A1502     1555   1555  2.18  
LINK        MG    MG A1701                 O   HOH A1756     1555   1555  2.20  
LINK        NA    NA B1602                 O   HOH B2582     1555   1555  2.54  
LINK        NA    NA B1602                 OD1 ASP B 109     1555   1555  2.17  
LINK        NA    NA B1602                 O   VAL B  40     1555   1555  2.53  
LINK        NA    NA B1602                 O   GLN B 196     1555   1555  2.20  
LINK        MG    MG B1702                 O1N NAI B2502     1555   1555  2.08  
LINK        MG    MG B1702                 O2A NAI B2502     1555   1555  2.29  
LINK        MG    MG B1702                 O   HOH B2563     1555   1555  2.71  
LINK        NA    NA C1603                 O   GLN C 196     1555   1555  2.39  
LINK        NA    NA C1603                 O   VAL C  40     1555   1555  2.28  
LINK        NA    NA C1603                 OD1 ASP C 109     1555   1555  2.42  
LINK        NA    NA C1603                 O   HOH C3549     1555   1555  2.12  
LINK        MG    MG C1703                 O1N NAI C3502     1555   1555  2.28  
LINK        MG    MG C1703                 O2A NAI C3502     1555   1555  2.26  
LINK        MG    MG C1703                 O   HOH C3611     1555   1555  2.34  
LINK        NA    NA D1604                 O   ASP D 109     1555   1555  2.54  
LINK        NA    NA D1604                 O   VAL D  40     1555   1555  2.34  
LINK        NA    NA D1604                 OD1 ASP D 109     1555   1555  2.40  
LINK        NA    NA D1604                 O   GLN D 196     1555   1555  2.45  
LINK        MG    MG D1704                 O1N NAI D4502     1555   1555  2.49  
LINK        MG    MG D1704                 O2A NAI D4502     1555   1555  2.17  
LINK        NA    NA E1605                 O   GLN E 196     1555   1555  2.28  
LINK        NA    NA E1605                 OD1 ASP E 109     1555   1555  2.42  
LINK        NA    NA E1605                 O   ASP E 109     1555   1555  2.40  
LINK        MG    MG E1705                 O2A NAI E5502     1555   1555  2.24  
LINK        MG    MG E1705                 O   HOH E5538     1555   1555  2.89  
LINK        MG    MG E1705                 O   HOH E5584     1555   1555  2.51  
LINK        MG    MG E1705                 O1N NAI E5502     1555   1555  2.37  
LINK        NA    NA F1606                 OD1 ASP F 109     1555   1555  2.52  
LINK        NA    NA F1606                 O   VAL F  40     1555   1555  2.40  
LINK        NA    NA F1606                 O   GLN F 196     1555   1555  2.34  
LINK        MG    MG F1706                 O2A NAI F6502     1555   1555  2.13  
LINK        MG    MG F1706                 O   HOH F6525     1555   1555  2.48  
LINK        MG    MG F1706                 O1N NAI F6502     1555   1555  2.11  
LINK        MG    MG F1706                 O   HOH F6621     1555   1555  2.27  
LINK        NA    NA G1607                 O   ASP G 109     1555   1555  2.54  
LINK        NA    NA G1607                 O   VAL G  40     1555   1555  2.29  
LINK        NA    NA G1607                 O   GLN G 196     1555   1555  2.44  
LINK        NA    NA G1607                 OD1 ASP G 109     1555   1555  2.40  
LINK        MG    MG G1707                 O2A NAI G7502     1555   1555  2.21  
LINK        MG    MG G1707                 O1N NAI G7502     1555   1555  2.32  
LINK        MG    MG G1707                 O   HOH G7536     1555   1555  2.84  
LINK        NA    NA H1608                 O   GLN H 196     1555   1555  2.33  
LINK        NA    NA H1608                 OD1 ASP H 109     1555   1555  2.42  
LINK        NA    NA H1608                 O   VAL H  40     1555   1555  2.51  
LINK        MG    MG H1708                 O1N NAI H8502     1555   1555  2.18  
LINK        MG    MG H1708                 O   HOH H8542     1555   1555  2.48  
LINK        MG    MG H1708                 O2A NAI H8502     1555   1555  2.46  
LINK         O   ASP A 109                NA    NA A1601     1555   1555  2.72  
LINK         OG1 THR B  39                NA    NA B1602     1555   1555  2.83  
LINK         O   ASP C 109                NA    NA C1603     1555   1555  2.82  
LINK         O   VAL E  40                NA    NA E1605     1555   1555  2.66  
LINK         O   ASP F 109                NA    NA F1606     1555   1555  2.67  
LINK         O   ASP H 109                NA    NA H1608     1555   1555  2.62  
LINK         O   ASP B 109                NA    NA B1602     1555   1555  3.01  
LINK        NA    NA H1608                 O   HOH H8543     1555   1555  3.05  
LINK        NA    NA B1602                 O   HOH B2571     1555   1555  3.09  
SITE     1 AC1  4 THR A  39  VAL A  40  ASP A 109  GLN A 196                    
SITE     1 AC2  6 THR B  39  VAL B  40  ASP B 109  GLN B 196                    
SITE     2 AC2  6 HOH B2571  HOH B2582                                          
SITE     1 AC3  5 THR C  39  VAL C  40  ASP C 109  GLN C 196                    
SITE     2 AC3  5 HOH C3549                                                     
SITE     1 AC4  4 THR D  39  VAL D  40  ASP D 109  GLN D 196                    
SITE     1 AC5  2 NAI A1502  HOH A1756                                          
SITE     1 AC6  2 NAI B2502  HOH B2563                                          
SITE     1 AC7  2 NAI C3502  HOH C3611                                          
SITE     1 AC8  1 NAI D4502                                                     
SITE     1 AC9  4 THR E  39  VAL E  40  ASP E 109  GLN E 196                    
SITE     1 BC1  4 THR F  39  VAL F  40  ASP F 109  GLN F 196                    
SITE     1 BC2  4 THR G  39  VAL G  40  ASP G 109  GLN G 196                    
SITE     1 BC3  5 THR H  39  VAL H  40  ASP H 109  GLN H 196                    
SITE     2 BC3  5 HOH H8543                                                     
SITE     1 BC4  3 NAI E5502  HOH E5538  HOH E5584                               
SITE     1 BC5  3 NAI F6502  HOH F6525  HOH F6621                               
SITE     1 BC6  2 NAI G7502  HOH G7536                                          
SITE     1 BC7  2 NAI H8502  HOH H8542                                          
SITE     1 BC8 23 ILE A 165  ILE A 166  PRO A 167  TRP A 168                    
SITE     2 BC8 23 ASN A 169  LYS A 192  GLU A 195  GLY A 225                    
SITE     3 BC8 23 GLY A 229  ALA A 230  PHE A 243  GLY A 245                    
SITE     4 BC8 23 SER A 246  ILE A 249  GLU A 268  GLY A 270                    
SITE     5 BC8 23 SER A 302  GLN A 349  GLU A 399  PHE A 401                    
SITE     6 BC8 23  MG A1701  HOH A1754  HOH A1756                               
SITE     1 BC9 28 ILE B 165  ILE B 166  PRO B 167  TRP B 168                    
SITE     2 BC9 28 ASN B 169  LYS B 192  ALA B 194  GLU B 195                    
SITE     3 BC9 28 GLY B 225  GLY B 229  ALA B 230  PHE B 243                    
SITE     4 BC9 28 GLY B 245  SER B 246  ILE B 249  ILE B 253                    
SITE     5 BC9 28 GLU B 268  GLY B 270  SER B 302  GLN B 349                    
SITE     6 BC9 28 GLU B 399  PHE B 401   MG B1702  HOH B2514                    
SITE     7 BC9 28 HOH B2529  HOH B2559  HOH B2563  HOH B2564                    
SITE     1 CC1 25 ILE C 165  ILE C 166  PRO C 167  TRP C 168                    
SITE     2 CC1 25 ASN C 169  LYS C 192  ALA C 194  GLU C 195                    
SITE     3 CC1 25 GLY C 225  PRO C 226  GLY C 229  ALA C 230                    
SITE     4 CC1 25 PHE C 243  GLY C 245  SER C 246  ILE C 249                    
SITE     5 CC1 25 ILE C 253  GLU C 268  GLY C 270  SER C 302                    
SITE     6 CC1 25 GLN C 349  GLU C 399  PHE C 401   MG C1703                    
SITE     7 CC1 25 HOH C3505                                                     
SITE     1 CC2 23 ILE D 165  ILE D 166  PRO D 167  TRP D 168                    
SITE     2 CC2 23 ASN D 169  LYS D 192  GLU D 195  GLY D 225                    
SITE     3 CC2 23 GLY D 229  ALA D 230  PHE D 243  THR D 244                    
SITE     4 CC2 23 GLY D 245  SER D 246  ILE D 249  GLU D 268                    
SITE     5 CC2 23 GLY D 270  SER D 302  GLN D 349  GLU D 399                    
SITE     6 CC2 23 PHE D 401   MG D1704  HOH D4575                               
SITE     1 CC3 25 ILE E 165  ILE E 166  PRO E 167  TRP E 168                    
SITE     2 CC3 25 ASN E 169  LYS E 192  GLU E 195  GLY E 225                    
SITE     3 CC3 25 GLY E 229  ALA E 230  PHE E 243  GLY E 245                    
SITE     4 CC3 25 SER E 246  ILE E 249  ILE E 253  GLU E 268                    
SITE     5 CC3 25 GLY E 270  SER E 302  GLN E 349  LYS E 352                    
SITE     6 CC3 25 GLU E 399  PHE E 401   MG E1705  HOH E5567                    
SITE     7 CC3 25 HOH E5584                                                     
SITE     1 CC4 28 ILE F 165  ILE F 166  PRO F 167  TRP F 168                    
SITE     2 CC4 28 ASN F 169  LYS F 192  GLU F 195  GLY F 225                    
SITE     3 CC4 28 GLY F 229  ALA F 230  PHE F 243  GLY F 245                    
SITE     4 CC4 28 SER F 246  ILE F 249  ILE F 253  GLU F 268                    
SITE     5 CC4 28 GLY F 270  SER F 302  GLN F 349  LYS F 352                    
SITE     6 CC4 28 GLU F 399  PHE F 401   MG F1706  HOH F6525                    
SITE     7 CC4 28 HOH F6530  HOH F6562  HOH F6575  HOH F6621                    
SITE     1 CC5 28 ILE G 165  ILE G 166  PRO G 167  TRP G 168                    
SITE     2 CC5 28 ASN G 169  LYS G 192  ALA G 194  GLU G 195                    
SITE     3 CC5 28 GLN G 196  GLY G 225  GLY G 229  ALA G 230                    
SITE     4 CC5 28 PHE G 243  THR G 244  GLY G 245  SER G 246                    
SITE     5 CC5 28 ILE G 249  ILE G 253  GLU G 268  GLY G 270                    
SITE     6 CC5 28 SER G 302  GLN G 349  GLU G 399  PHE G 401                    
SITE     7 CC5 28  MG G1707  HOH G7535  HOH G7536  HOH G7569                    
SITE     1 CC6 27 ILE H 165  ILE H 166  PRO H 167  TRP H 168                    
SITE     2 CC6 27 ASN H 169  LYS H 192  GLU H 195  GLN H 196                    
SITE     3 CC6 27 GLY H 225  PRO H 226  GLY H 229  ALA H 230                    
SITE     4 CC6 27 PHE H 243  THR H 244  GLY H 245  SER H 246                    
SITE     5 CC6 27 ILE H 249  ILE H 253  GLU H 268  GLY H 270                    
SITE     6 CC6 27 SER H 302  GLN H 349  GLU H 399  PHE H 401                    
SITE     7 CC6 27  MG H1708  HOH H8538  HOH H8541                               
CRYST1  141.361  150.494  176.923  90.00  90.00  90.00 P 21 21 21   32          
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      0.007074  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006645  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005652        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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