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Database: PDB
Entry: 1O02
LinkDB: 1O02
Original site: 1O02 
HEADER    OXIDOREDUCTASE                          20-FEB-03   1O02              
TITLE     HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NADH IN THE 
TITLE    2 PRESENCE OF 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                                                      
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   27-FEB-19 1O02    1       REMARK                                   
REVDAT   3   30-OCT-13 1O02    1       HETATM REMARK VERSN                      
REVDAT   2   24-FEB-09 1O02    1       VERSN                                    
REVDAT   1   24-JUN-03 1O02    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.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 5708381.720                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 291570                         
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) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 14729                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.97                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 24697                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE                    : 0.3000                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1288                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.008                        
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          : 464                                     
REMARK   3   SOLVENT ATOMS            : 3584                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.16000                                             
REMARK   3    B22 (A**2) : -4.89000                                             
REMARK   3    B33 (A**2) : -7.27000                                             
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) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
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) : 0.23                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.27                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.230                           
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) : 1.080 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.480 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.010 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.900 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.30                                                 
REMARK   3   BSOL        : 18.21                                                
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  : GND-EGY.PAR                                    
REMARK   3  PARAMETER FILE  6  : 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   : GND-EGY.TOP                                    
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD TARGET USING           
REMARK   3  AMPLITUDES                                                          
REMARK   4                                                                      
REMARK   4 1O02 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_1000018405.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97881                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 291666                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
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     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
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   (%): 36.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
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       70.74600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.59750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.43650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.59750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       70.74600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.43650            
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: 29690 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.0 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: 29680 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -155.0 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       25.15   -149.32                                   
REMARK 500    GLN A  21     -168.73   -119.73                                   
REMARK 500    VAL A 120      -69.96   -103.62                                   
REMARK 500    THR A 227      -83.08    -99.27                                   
REMARK 500    SER A 260     -105.12   -100.01                                   
REMARK 500    LEU A 269     -160.64   -106.93                                   
REMARK 500    TYR A 379       54.95   -111.04                                   
REMARK 500    LYS A 469     -131.51     51.42                                   
REMARK 500    LEU A 477      163.06     74.16                                   
REMARK 500    ASN B  20       29.05   -152.17                                   
REMARK 500    VAL B 120      -69.03   -106.33                                   
REMARK 500    THR B 227      -83.38    -98.84                                   
REMARK 500    SER B 260     -100.44   -104.75                                   
REMARK 500    LEU B 269     -164.62   -107.54                                   
REMARK 500    TYR B 379       55.70    -94.68                                   
REMARK 500    LYS B 469     -131.95     49.97                                   
REMARK 500    LEU B 477      162.75     72.35                                   
REMARK 500    ASN C  20       29.30   -151.49                                   
REMARK 500    VAL C 120      -73.40   -104.27                                   
REMARK 500    THR C 227      -83.00    -97.62                                   
REMARK 500    SER C 260     -100.06   -100.41                                   
REMARK 500    LEU C 269     -165.84   -108.52                                   
REMARK 500    LYS C 469     -131.31     48.92                                   
REMARK 500    LEU C 477      161.38     72.39                                   
REMARK 500    ASN D  20       24.14   -150.43                                   
REMARK 500    VAL D 120      -67.01   -107.51                                   
REMARK 500    THR D 227      -84.67    -97.85                                   
REMARK 500    SER D 260      -98.03    -98.33                                   
REMARK 500    LEU D 269     -169.70   -107.45                                   
REMARK 500    TYR D 379       59.09   -105.89                                   
REMARK 500    LYS D 469     -133.17     48.91                                   
REMARK 500    LEU D 477      161.88     72.13                                   
REMARK 500    GLN D 497      109.67   -160.25                                   
REMARK 500    ASN E  20       27.47   -149.52                                   
REMARK 500    VAL E 120      -66.70   -106.25                                   
REMARK 500    THR E 227      -79.58   -104.67                                   
REMARK 500    SER E 260     -102.47   -100.25                                   
REMARK 500    LEU E 269     -163.83   -106.69                                   
REMARK 500    TYR E 379       58.64   -113.05                                   
REMARK 500    LYS E 469     -131.92     48.16                                   
REMARK 500    LEU E 477      161.00     71.67                                   
REMARK 500    ASN F  20       26.57   -148.56                                   
REMARK 500    VAL F 120      -71.98   -103.71                                   
REMARK 500    THR F 227      -82.00   -101.21                                   
REMARK 500    SER F 260     -100.21   -101.94                                   
REMARK 500    LEU F 269     -165.24   -110.73                                   
REMARK 500    LYS F 469     -134.41     48.58                                   
REMARK 500    LEU F 477      158.89     75.31                                   
REMARK 500    ASN G  20       26.29   -150.33                                   
REMARK 500    VAL G 120      -69.35   -106.18                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      67 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A4941        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH B 778        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH B 884        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH B1116        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH D1053        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH E1049        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH E1094        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH E1120        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH E1165        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH E1166        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH F 829        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH F 849        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH F1134        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH G 762        DISTANCE =  7.13 ANGSTROMS                       
REMARK 525    HOH G 843        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH G 947        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH G1120        DISTANCE =  6.78 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH F 784   O                                                      
REMARK 620 2 NAI F 607   O2A  95.5                                              
REMARK 620 3 HOH F 783   O    89.2 102.5                                        
REMARK 620 4 NAI F 607   O1N  87.5  84.9 172.1                                  
REMARK 620 5 HOH F 817   O    87.1 169.4  87.7  85.0                            
REMARK 620 6 HOH F 816   O   173.2  88.9  84.7  98.1  89.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAI G 606   O2A                                                    
REMARK 620 2 NAI G 606   O1N  90.4                                              
REMARK 620 3 HOH G 706   O   101.1 167.7                                        
REMARK 620 4 HOH G 707   O    89.9 104.7  80.0                                  
REMARK 620 5 HOH G 709   O   107.5  82.5  89.7 161.3                            
REMARK 620 6 HOH G 708   O   163.8  80.9  88.9  79.3  85.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH E 921   O                                                      
REMARK 620 2 NAI E 606   O2A 103.9                                              
REMARK 620 3 NAI E 606   O1N  91.5  84.3                                        
REMARK 620 4 HOH E 920   O    92.5 163.0  90.8                                  
REMARK 620 5 HOH E 788   O    93.6 101.0 171.5  82.2                            
REMARK 620 6 HOH E 787   O   171.0  82.7  95.3  81.6  79.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 788   O                                                      
REMARK 620 2 NAI B 606   O1N  92.4                                              
REMARK 620 3 HOH B 787   O    94.8 172.6                                        
REMARK 620 4 HOH B 786   O   179.2  87.0  85.9                                  
REMARK 620 5 HOH B 785   O    95.5  91.2  86.0  84.8                            
REMARK 620 6 NAI B 606   O2A  97.9  86.8  94.4  81.7 166.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH H 763   O                                                      
REMARK 620 2 NAI H 605   O2A  94.3                                              
REMARK 620 3 NAI H 605   O1N  88.5  89.3                                        
REMARK 620 4 HOH H 768   O    93.2 100.0 170.4                                  
REMARK 620 5 HOH H 770   O    99.0 166.4  88.8  81.6                            
REMARK 620 6 HOH H 769   O   173.2  88.7  97.5  80.3  78.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 720   O                                                      
REMARK 620 2 NAI D 606   O2A 100.1                                              
REMARK 620 3 HOH D 717   O    98.3 105.0                                        
REMARK 620 4 NAI D 606   O1N 179.6  79.5  81.9                                  
REMARK 620 5 HOH D 719   O    78.1  90.2 164.7 101.7                            
REMARK 620 6 HOH D 718   O    98.4 158.4  83.0  82.0  82.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C1039   O                                                      
REMARK 620 2 HOH C1066   O    96.3                                              
REMARK 620 3 NAI C 606   O2A  95.2  93.4                                        
REMARK 620 4 NAI C 606   O1N  83.4 176.2  82.9                                  
REMARK 620 5 HOH C1040   O    91.7  92.0 170.7  91.8                            
REMARK 620 6 HOH C1067   O   173.0  76.8  86.5 103.6  87.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A4601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAI A4606   O2A                                                    
REMARK 620 2 HOH A4866   O    96.4                                              
REMARK 620 3 HOH A4731   O   168.5  90.6                                        
REMARK 620 4 HOH A4733   O    98.4  92.2  90.4                                  
REMARK 620 5 HOH A4867   O    86.4 177.1  86.7  86.8                            
REMARK 620 6 NAI A4606   O1N  88.0  82.3  83.9 172.0  98.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A4602  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 109   OD1                                                    
REMARK 620 2 GLN A 196   O    86.9                                              
REMARK 620 3 VAL A  40   O   109.5 156.4                                        
REMARK 620 4 HOH A4919   O   161.8  84.3  84.1                                  
REMARK 620 5 ASP A 109   O    81.2  99.8  99.5  84.7                            
REMARK 620 6 THR A  39   OG1  56.4  71.5 102.8 134.1 136.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 602  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C1056   O                                                      
REMARK 620 2 GLN C 196   O    89.3                                              
REMARK 620 3 VAL C  40   O    83.1 155.7                                        
REMARK 620 4 ASP C 109   O    78.9 100.9 100.2                                  
REMARK 620 5 ASP C 109   OD1 161.8  89.9 104.4  83.3                            
REMARK 620 6 THR C  39   OG1 138.2  71.6  99.2 140.0  58.0                      
REMARK 620 7 HOH C1165   O    71.2  73.6  82.1 149.5 125.9  67.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 602  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 109   OD1                                                    
REMARK 620 2 HOH B 797   O   166.1                                              
REMARK 620 3 GLN B 196   O    87.6  81.6                                        
REMARK 620 4 ASP B 109   O    82.9  90.7 102.4                                  
REMARK 620 5 VAL B  40   O   107.2  85.7 157.7  96.0                            
REMARK 620 6 THR B  39   OG1  59.3 123.7  69.2 141.0 103.7                      
REMARK 620 7 HOH B 796   O   129.5  56.5  77.1 147.2  80.6  70.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA F 602  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL F  40   O                                                      
REMARK 620 2 ASP F 109   OD1 110.1                                              
REMARK 620 3 ASP F 109   O   103.2  84.1                                        
REMARK 620 4 HOH F1017   O    86.9 161.8  85.6                                  
REMARK 620 5 GLN F 196   O   154.6  86.9  97.1  79.4                            
REMARK 620 6 THR F  39   OG1 102.2  57.3 139.2 127.2  70.5                      
REMARK 620 7 HOH F 792   O    81.7 125.2 147.2  62.1  73.0  67.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 602  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 109   OD1                                                    
REMARK 620 2 ASP D 109   O    84.5                                              
REMARK 620 3 VAL D  40   O   107.4  99.9                                        
REMARK 620 4 GLN D 196   O    86.3  99.0 157.6                                  
REMARK 620 5 HOH D1118   O   160.2  84.2  90.5  79.5                            
REMARK 620 6 HOH D1119   O   125.6 148.4  81.3  76.3  64.2                      
REMARK 620 7 THR D  39   OG1  56.1 139.2 101.7  70.8 129.4  69.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA E 602  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 109   O                                                      
REMARK 620 2 VAL E  40   O   102.8                                              
REMARK 620 3 ASP E 109   OD1  86.1 107.1                                        
REMARK 620 4 HOH E1084   O    93.1  89.6 163.1                                  
REMARK 620 5 GLN E 196   O    99.0 154.0  88.2  75.2                            
REMARK 620 6 THR E  39   OG1 138.7 101.5  54.8 120.1  69.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA G 602  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL G  40   O                                                      
REMARK 620 2 ASP G 109   OD1 105.3                                              
REMARK 620 3 HOH G 718   O    88.3 157.8                                        
REMARK 620 4 GLN G 196   O   161.8  87.4  84.0                                  
REMARK 620 5 ASP G 109   O    97.3  78.8  82.2  98.0                            
REMARK 620 6 HOH G 717   O    82.9 133.5  64.5  78.9 146.7                      
REMARK 620 7 THR G  39   OG1 104.7  56.3 137.7  71.2 133.7  77.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA H 602  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN H 196   O                                                      
REMARK 620 2 ASP H 109   OD1  91.7                                              
REMARK 620 3 VAL H  40   O   159.8 103.7                                        
REMARK 620 4 HOH H 753   O    83.8 165.6  84.1                                  
REMARK 620 5 ASP H 109   O    99.9  82.2  95.1  85.1                            
REMARK 620 6 THR H  39   OG1  72.7  60.1 103.6 130.4 140.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 4601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 4602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 4603                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 4604                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4605                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI A 4606                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI C 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI D 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI E 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI F 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI G 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI H 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI H 605                 
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: 1NZW   RELATED DB: PDB                                   
REMARK 900 CYS302SER MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE       
REMARK 900 COMPLEXED WITH NADH AND MG2+                                         
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: 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  1O02 A    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1O02 B    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1O02 C    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1O02 D    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1O02 E    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1O02 F    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1O02 G    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  1O02 H    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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     MG  A4601       1                                                       
HET     NA  A4602       1                                                       
HET    GAI  A4603       4                                                       
HET    GAI  A4604       4                                                       
HET    EDO  A4605       4                                                       
HET    NAI  A4606      44                                                       
HET     MG  B 601       1                                                       
HET     NA  B 602       1                                                       
HET    GAI  B 603       4                                                       
HET    GAI  B 604       4                                                       
HET    EDO  B 605       4                                                       
HET    NAI  B 606      44                                                       
HET     MG  C 601       1                                                       
HET     NA  C 602       1                                                       
HET    GAI  C 603       4                                                       
HET    GAI  C 604       4                                                       
HET    EDO  C 605       4                                                       
HET    NAI  C 606      44                                                       
HET     MG  D 601       1                                                       
HET     NA  D 602       1                                                       
HET    GAI  D 603       4                                                       
HET    GAI  D 604       4                                                       
HET    EDO  D 605       4                                                       
HET    NAI  D 606      44                                                       
HET     MG  E 601       1                                                       
HET     NA  E 602       1                                                       
HET    GAI  E 603       4                                                       
HET    GAI  E 604       4                                                       
HET    EDO  E 605       4                                                       
HET    NAI  E 606      44                                                       
HET     MG  F 601       1                                                       
HET     NA  F 602       1                                                       
HET    GAI  F 603       4                                                       
HET    GAI  F 604       4                                                       
HET    EDO  F 605       4                                                       
HET    EDO  F 606       4                                                       
HET    NAI  F 607      44                                                       
HET     MG  G 601       1                                                       
HET     NA  G 602       1                                                       
HET    GAI  G 603       4                                                       
HET    GAI  G 604       4                                                       
HET    GAI  G 605       4                                                       
HET    NAI  G 606      44                                                       
HET     MG  H 601       1                                                       
HET     NA  H 602       1                                                       
HET    GAI  H 603       4                                                       
HET    EDO  H 604       4                                                       
HET    NAI  H 605      44                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM     GAI GUANIDINE                                                        
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     NAI NADH                                                             
FORMUL   9   MG    8(MG 2+)                                                     
FORMUL  10   NA    8(NA 1+)                                                     
FORMUL  11  GAI    16(C H5 N3)                                                  
FORMUL  13  EDO    8(C2 H6 O2)                                                  
FORMUL  14  NAI    8(C21 H29 N7 O14 P2)                                         
FORMUL  57  HOH   *3584(H2 O)                                                   
HELIX    1   1 ASP A   55  PHE A   70  1                                  16    
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 ILE A  314  ARG A  329  1                                  16    
HELIX   14  14 ASP A  346  GLU A  363  1                                  18    
HELIX   15  15 MET A  393  GLU A  398  1                                   6    
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  PHE B   70  1                                  16    
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  ARG B  329  1                                  18    
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 GLY B  478  ALA B  484  5                                   7    
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  GLU C  398  1                                   6    
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  GLY D  134  1                                  15    
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 GLY D  478  ALA D  484  5                                   7    
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 ILE E  314  ARG E  329  1                                  16    
HELIX   90  90 ASP E  346  GLU E  363  1                                  18    
HELIX   91  91 MET E  393  GLU E  398  1                                   6    
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 GLU E  479  ALA E  484  5                                   6    
HELIX   96  96 ASP F   55  PHE F   70  1                                  16    
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  SER F  234  1                                   8    
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  GLU F  398  1                                   6    
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  ARG G  329  1                                  18    
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  PHE H   70  1                                  16    
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  ARG H  329  1                                  18    
HELIX  147 147 ASP H  346  GLU H  363  1                                  18    
HELIX  148 148 MET H  393  GLU H  398  1                                   6    
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  ILE B 277   O  PHE B 309           
SHEET    6   C20 ALA B 428  PHE B 432  1  O  ALA B 430   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  PHE A 151   O  VAL A 493           
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  VAL D 493   N  PHE D 151           
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  ALA C 430           
SHEET   17   C20 ARG C 307  GLN C 311  1  O  PHE C 309   N  ILE C 277           
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  GLN A 164   O  LYS A 192           
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  VAL A 310   O  LEU A 408           
SHEET    5   E20 PRO A 274  ILE A 277  1  N  ILE A 277   O  PHE A 309           
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  PHE B 151   O  VAL B 493           
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  GLY C 141   N  THR B 143           
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  VAL C 493   N  PHE C 151           
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  PHE D 309   N  ILE D 277           
SHEET   18   E20 VAL D 404  PHE D 410  1  O  LEU D 408   N  VAL D 310           
SHEET   19   E20 THR D 384  GLY D 387  1  N  THR D 384   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  GLN B 164   O  LYS B 192           
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  CYS C 162   O  VAL C 188           
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  GLN D 164   O  LYS D 192           
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  ILE F 277   O  PHE F 309           
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  PHE E 151   O  VAL E 493           
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  GLY H 141   N  THR E 143           
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 493   N  PHE H 151           
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  ALA G 430           
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  THR G 308           
SHEET   19   Q20 THR G 384  GLY G 387  1  N  THR G 384   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  GLN E 164   O  LYS E 192           
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  THR E 384           
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  ILE E 277   O  PHE E 309           
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  PHE F 151   O  VAL F 493           
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 493   N  PHE G 151           
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  VAL H 310           
SHEET   19   S20 THR H 384  GLY H 387  1  N  THR H 384   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  GLN F 164   O  LYS F 192           
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  GLN G 164   O  LYS G 192           
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  GLN H 164   O  LYS H 192           
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           
LINK        MG    MG F 601                 O   HOH F 784     1555   1555  1.92  
LINK        MG    MG G 601                 O2A NAI G 606     1555   1555  1.93  
LINK        MG    MG E 601                 O   HOH E 921     1555   1555  1.95  
LINK        MG    MG B 601                 O   HOH B 788     1555   1555  1.99  
LINK        MG    MG H 601                 O   HOH H 763     1555   1555  2.00  
LINK        MG    MG B 601                 O1N NAI B 606     1555   1555  2.00  
LINK        MG    MG F 601                 O2A NAI F 607     1555   1555  2.01  
LINK        MG    MG D 601                 O   HOH D 720     1555   1555  2.01  
LINK        MG    MG C 601                 O   HOH C1039     1555   1555  2.04  
LINK        MG    MG H 601                 O2A NAI H 605     1555   1555  2.05  
LINK        MG    MG G 601                 O1N NAI G 606     1555   1555  2.07  
LINK        MG    MG E 601                 O2A NAI E 606     1555   1555  2.07  
LINK        MG    MG F 601                 O   HOH F 783     1555   1555  2.09  
LINK        MG    MG D 601                 O2A NAI D 606     1555   1555  2.10  
LINK        MG    MG E 601                 O1N NAI E 606     1555   1555  2.10  
LINK        MG    MG G 601                 O   HOH G 706     1555   1555  2.11  
LINK        MG    MG A4601                 O2A NAI A4606     1555   1555  2.11  
LINK        MG    MG C 601                 O   HOH C1066     1555   1555  2.12  
LINK        MG    MG A4601                 O   HOH A4866     1555   1555  2.12  
LINK        MG    MG B 601                 O   HOH B 787     1555   1555  2.13  
LINK        MG    MG C 601                 O2A NAI C 606     1555   1555  2.13  
LINK        MG    MG B 601                 O   HOH B 786     1555   1555  2.15  
LINK        MG    MG B 601                 O   HOH B 785     1555   1555  2.16  
LINK        MG    MG D 601                 O   HOH D 717     1555   1555  2.16  
LINK        MG    MG B 601                 O2A NAI B 606     1555   1555  2.16  
LINK        MG    MG C 601                 O1N NAI C 606     1555   1555  2.16  
LINK        MG    MG H 601                 O1N NAI H 605     1555   1555  2.16  
LINK        MG    MG E 601                 O   HOH E 920     1555   1555  2.17  
LINK        MG    MG A4601                 O   HOH A4731     1555   1555  2.18  
LINK        MG    MG G 601                 O   HOH G 707     1555   1555  2.18  
LINK        MG    MG A4601                 O   HOH A4733     1555   1555  2.18  
LINK        MG    MG G 601                 O   HOH G 709     1555   1555  2.19  
LINK        MG    MG F 601                 O1N NAI F 607     1555   1555  2.19  
LINK        MG    MG A4601                 O   HOH A4867     1555   1555  2.21  
LINK         OD1 ASP A 109                NA    NA A4602     1555   1555  2.22  
LINK        MG    MG H 601                 O   HOH H 768     1555   1555  2.24  
LINK        MG    MG A4601                 O1N NAI A4606     1555   1555  2.25  
LINK        MG    MG C 601                 O   HOH C1040     1555   1555  2.25  
LINK        MG    MG D 601                 O1N NAI D 606     1555   1555  2.25  
LINK        NA    NA C 602                 O   HOH C1056     1555   1555  2.26  
LINK         OD1 ASP B 109                NA    NA B 602     1555   1555  2.27  
LINK        MG    MG F 601                 O   HOH F 817     1555   1555  2.28  
LINK         O   VAL F  40                NA    NA F 602     1555   1555  2.28  
LINK        MG    MG E 601                 O   HOH E 788     1555   1555  2.28  
LINK        MG    MG D 601                 O   HOH D 719     1555   1555  2.28  
LINK         OD1 ASP D 109                NA    NA D 602     1555   1555  2.29  
LINK         OD1 ASP F 109                NA    NA F 602     1555   1555  2.29  
LINK        NA    NA B 602                 O   HOH B 797     1555   1555  2.30  
LINK         O   ASP E 109                NA    NA E 602     1555   1555  2.30  
LINK        MG    MG F 601                 O   HOH F 816     1555   1555  2.31  
LINK         O   VAL G  40                NA    NA G 602     1555   1555  2.31  
LINK         O   GLN H 196                NA    NA H 602     1555   1555  2.31  
LINK        MG    MG C 601                 O   HOH C1067     1555   1555  2.36  
LINK         O   GLN A 196                NA    NA A4602     1555   1555  2.36  
LINK         O   ASP D 109                NA    NA D 602     1555   1555  2.36  
LINK         O   VAL A  40                NA    NA A4602     1555   1555  2.36  
LINK        MG    MG H 601                 O   HOH H 770     1555   1555  2.37  
LINK         O   GLN C 196                NA    NA C 602     1555   1555  2.37  
LINK         O   VAL E  40                NA    NA E 602     1555   1555  2.37  
LINK        MG    MG G 601                 O   HOH G 708     1555   1555  2.37  
LINK        MG    MG H 601                 O   HOH H 769     1555   1555  2.38  
LINK         OD1 ASP H 109                NA    NA H 602     1555   1555  2.38  
LINK         O   VAL C  40                NA    NA C 602     1555   1555  2.38  
LINK         O   GLN B 196                NA    NA B 602     1555   1555  2.38  
LINK         O   VAL D  40                NA    NA D 602     1555   1555  2.38  
LINK         OD1 ASP G 109                NA    NA G 602     1555   1555  2.39  
LINK         O   ASP B 109                NA    NA B 602     1555   1555  2.39  
LINK         O   ASP F 109                NA    NA F 602     1555   1555  2.40  
LINK        NA    NA G 602                 O   HOH G 718     1555   1555  2.40  
LINK        NA    NA A4602                 O   HOH A4919     1555   1555  2.40  
LINK         O   GLN D 196                NA    NA D 602     1555   1555  2.40  
LINK         OD1 ASP E 109                NA    NA E 602     1555   1555  2.40  
LINK        MG    MG E 601                 O   HOH E 787     1555   1555  2.41  
LINK         O   GLN G 196                NA    NA G 602     1555   1555  2.42  
LINK         O   VAL H  40                NA    NA H 602     1555   1555  2.42  
LINK        NA    NA E 602                 O   HOH E1084     1555   1555  2.43  
LINK         O   ASP C 109                NA    NA C 602     1555   1555  2.43  
LINK        NA    NA H 602                 O   HOH H 753     1555   1555  2.43  
LINK         O   VAL B  40                NA    NA B 602     1555   1555  2.43  
LINK         O   ASP A 109                NA    NA A4602     1555   1555  2.46  
LINK        NA    NA D 602                 O   HOH D1118     1555   1555  2.46  
LINK        MG    MG D 601                 O   HOH D 718     1555   1555  2.46  
LINK        NA    NA F 602                 O   HOH F1017     1555   1555  2.47  
LINK         OD1 ASP C 109                NA    NA C 602     1555   1555  2.48  
LINK         O   ASP H 109                NA    NA H 602     1555   1555  2.50  
LINK         O   GLN E 196                NA    NA E 602     1555   1555  2.50  
LINK         O   GLN F 196                NA    NA F 602     1555   1555  2.52  
LINK         O   ASP G 109                NA    NA G 602     1555   1555  2.54  
LINK        NA    NA D 602                 O   HOH D1119     1555   1555  2.93  
LINK         OG1 THR H  39                NA    NA H 602     1555   1555  2.93  
LINK         OG1 THR C  39                NA    NA C 602     1555   1555  3.03  
LINK         OG1 THR B  39                NA    NA B 602     1555   1555  3.06  
LINK         OG1 THR F  39                NA    NA F 602     1555   1555  3.09  
LINK        NA    NA G 602                 O   HOH G 717     1555   1555  3.11  
LINK        NA    NA C 602                 O   HOH C1165     1555   1555  3.12  
LINK         OG1 THR D  39                NA    NA D 602     1555   1555  3.13  
LINK         OG1 THR E  39                NA    NA E 602     1555   1555  3.15  
LINK         OG1 THR A  39                NA    NA A4602     1555   1555  3.15  
LINK         OG1 THR G  39                NA    NA G 602     1555   1555  3.18  
LINK        NA    NA F 602                 O   HOH F 792     1555   1555  3.19  
LINK        NA    NA B 602                 O   HOH B 796     1555   1555  3.20  
SITE     1 AC1  5 NAI A4606  HOH A4731  HOH A4733  HOH A4866                    
SITE     2 AC1  5 HOH A4867                                                     
SITE     1 AC2  5 THR A  39  VAL A  40  ASP A 109  GLN A 196                    
SITE     2 AC2  5 HOH A4919                                                     
SITE     1 AC3  7 PHE A  70  GLU A 157  PRO A 158  VAL A 159                    
SITE     2 AC3  7 HOH A5100  HOH A5101  TYR B 468                               
SITE     1 AC4  6 ILE A 146  ASP A 147  PHE A 150  HOH A4753                    
SITE     2 AC4  6 HOH A4758  PHE B 459                                          
SITE     1 AC5  5 TYR A 153  ARG A 155  HOH A5072  SER B 443                    
SITE     2 AC5  5 PHE D 151                                                     
SITE     1 AC6 32 ILE A 165  ILE A 166  PRO A 167  TRP A 168                    
SITE     2 AC6 32 ASN A 169  LYS A 192  GLU A 195  GLY A 225                    
SITE     3 AC6 32 GLY A 229  ALA A 230  PHE A 243  GLY A 245                    
SITE     4 AC6 32 SER A 246  ILE A 249  ILE A 253  GLU A 268                    
SITE     5 AC6 32 LEU A 269  CYS A 302  GLN A 349  GLU A 399                    
SITE     6 AC6 32 PHE A 401   MG A4601  HOH A4728  HOH A4729                    
SITE     7 AC6 32 HOH A4731  HOH A4734  HOH A4735  HOH A4738                    
SITE     8 AC6 32 HOH A4851  HOH A4866  HOH A4867  HOH A5114                    
SITE     1 AC7  5 NAI B 606  HOH B 785  HOH B 786  HOH B 787                    
SITE     2 AC7  5 HOH B 788                                                     
SITE     1 AC8  5 THR B  39  VAL B  40  ASP B 109  GLN B 196                    
SITE     2 AC8  5 HOH B 797                                                     
SITE     1 AC9  7 TYR A 468  GLU B 157  PRO B 158  VAL B 159                    
SITE     2 AC9  7 HOH B 751  HOH B 996  HOH B 998                               
SITE     1 BC1  6 PHE A 459  HOH A4898  ILE B 146  ASP B 147                    
SITE     2 BC1  6 PHE B 150  HOH B1043                                          
SITE     1 BC2  4 SER A 443  TYR B 153  ARG B 155  PHE C 151                    
SITE     1 BC3 33 ILE B 165  ILE B 166  PRO B 167  TRP B 168                    
SITE     2 BC3 33 ASN B 169  LYS B 192  GLU B 195  GLY B 225                    
SITE     3 BC3 33 PRO B 226  GLY B 229  ALA B 230  PHE B 243                    
SITE     4 BC3 33 GLY B 245  SER B 246  ILE B 249  ILE B 253                    
SITE     5 BC3 33 GLU B 268  LEU B 269  CYS B 302  GLN B 349                    
SITE     6 BC3 33 GLU B 399  PHE B 401   MG B 601  HOH B 713                    
SITE     7 BC3 33 HOH B 775  HOH B 776  HOH B 785  HOH B 786                    
SITE     8 BC3 33 HOH B 788  HOH B 790  HOH B1099  HOH B1100                    
SITE     9 BC3 33 HOH B1196                                                     
SITE     1 BC4  5 NAI C 606  HOH C1039  HOH C1040  HOH C1066                    
SITE     2 BC4  5 HOH C1067                                                     
SITE     1 BC5  5 THR C  39  VAL C  40  ASP C 109  GLN C 196                    
SITE     2 BC5  5 HOH C1056                                                     
SITE     1 BC6  5 GLU C 157  PRO C 158  VAL C 159  HOH C 721                    
SITE     2 BC6  5 TYR D 468                                                     
SITE     1 BC7  6 ASP C 147  PHE C 150  HOH C 865  HOH C 870                    
SITE     2 BC7  6 PHE D 459  HOH D1006                                          
SITE     1 BC8  4 PHE B 151  TYR C 153  ARG C 155  SER D 443                    
SITE     1 BC9 34 ILE C 165  ILE C 166  PRO C 167  TRP C 168                    
SITE     2 BC9 34 ASN C 169  LYS C 192  ALA C 194  GLU C 195                    
SITE     3 BC9 34 GLN C 196  GLY C 225  GLY C 229  ALA C 230                    
SITE     4 BC9 34 PHE C 243  GLY C 245  SER C 246  ILE C 249                    
SITE     5 BC9 34 ILE C 253  GLU C 268  LEU C 269  CYS C 302                    
SITE     6 BC9 34 GLN C 349  LYS C 352  GLU C 399  PHE C 401                    
SITE     7 BC9 34  MG C 601  HOH C 969  HOH C 971  HOH C1038                    
SITE     8 BC9 34 HOH C1039  HOH C1051  HOH C1052  HOH C1066                    
SITE     9 BC9 34 HOH C1067  HOH C1068                                          
SITE     1 CC1  5 NAI D 606  HOH D 717  HOH D 718  HOH D 719                    
SITE     2 CC1  5 HOH D 720                                                     
SITE     1 CC2  6 THR D  39  VAL D  40  ASP D 109  GLN D 196                    
SITE     2 CC2  6 HOH D1118  HOH D1119                                          
SITE     1 CC3  4 TYR C 468  GLU D 157  PRO D 158  VAL D 159                    
SITE     1 CC4  5 PHE C 459  HOH C 754  ILE D 146  ASP D 147                    
SITE     2 CC4  5 PHE D 150                                                     
SITE     1 CC5  4 PHE A 151  SER C 443  TYR D 153  ARG D 155                    
SITE     1 CC6 31 ILE D 165  ILE D 166  PRO D 167  TRP D 168                    
SITE     2 CC6 31 ASN D 169  LYS D 192  GLU D 195  GLY D 225                    
SITE     3 CC6 31 GLY D 229  ALA D 230  PHE D 243  GLY D 245                    
SITE     4 CC6 31 SER D 246  ILE D 249  ILE D 253  GLU D 268                    
SITE     5 CC6 31 LEU D 269  CYS D 302  GLN D 349  LYS D 352                    
SITE     6 CC6 31 GLU D 399  PHE D 401   MG D 601  HOH D 715                    
SITE     7 CC6 31 HOH D 717  HOH D 718  HOH D 721  HOH D 722                    
SITE     8 CC6 31 HOH D 729  HOH D1024  HOH D1079                               
SITE     1 CC7  5 NAI E 606  HOH E 787  HOH E 788  HOH E 920                    
SITE     2 CC7  5 HOH E 921                                                     
SITE     1 CC8  5 THR E  39  VAL E  40  ASP E 109  GLN E 196                    
SITE     2 CC8  5 HOH E1084                                                     
SITE     1 CC9  4 GLU E 157  PRO E 158  VAL E 159  TYR F 468                    
SITE     1 DC1  4 ASP E 147  PHE E 150  PHE F 459  HOH F1132                    
SITE     1 DC2  5 TYR E 153  ARG E 155  HOH E1008  SER F 443                    
SITE     2 DC2  5 PHE H 151                                                     
SITE     1 DC3 33 ILE E 165  ILE E 166  PRO E 167  TRP E 168                    
SITE     2 DC3 33 ASN E 169  LYS E 192  GLU E 195  GLN E 196                    
SITE     3 DC3 33 GLY E 225  GLY E 229  ALA E 230  PHE E 243                    
SITE     4 DC3 33 GLY E 245  SER E 246  ILE E 249  ILE E 253                    
SITE     5 DC3 33 GLU E 268  LEU E 269  CYS E 302  GLN E 349                    
SITE     6 DC3 33 GLU E 399  PHE E 401   MG E 601  HOH E 782                    
SITE     7 DC3 33 HOH E 783  HOH E 787  HOH E 789  HOH E 790                    
SITE     8 DC3 33 HOH E 792  HOH E 920  HOH E 921  HOH E 923                    
SITE     9 DC3 33 HOH E1107                                                     
SITE     1 DC4  5 NAI F 607  HOH F 783  HOH F 784  HOH F 816                    
SITE     2 DC4  5 HOH F 817                                                     
SITE     1 DC5  5 THR F  39  VAL F  40  ASP F 109  GLN F 196                    
SITE     2 DC5  5 HOH F1017                                                     
SITE     1 DC6  6 TYR E 468  GLU F 157  PRO F 158  VAL F 159                    
SITE     2 DC6  6 HOH F 739  HOH F 740                                          
SITE     1 DC7  5 PHE E 459  HOH E1048  ILE F 146  ASP F 147                    
SITE     2 DC7  5 PHE F 150                                                     
SITE     1 DC8  4 SER E 443  TYR F 153  ARG F 155  PHE G 151                    
SITE     1 DC9  5 PHE F 151  HOH F 907  TYR G 153  ARG G 155                    
SITE     2 DC9  5 SER H 443                                                     
SITE     1 EC1 35 ILE F 165  ILE F 166  PRO F 167  TRP F 168                    
SITE     2 EC1 35 ASN F 169  LYS F 192  GLU F 195  GLN F 196                    
SITE     3 EC1 35 GLY F 225  PRO F 226  GLY F 229  ALA F 230                    
SITE     4 EC1 35 PHE F 243  GLY F 245  SER F 246  ILE F 249                    
SITE     5 EC1 35 ILE F 253  GLU F 268  LEU F 269  CYS F 302                    
SITE     6 EC1 35 GLN F 349  LYS F 352  GLU F 399  PHE F 401                    
SITE     7 EC1 35  MG F 601  HOH F 777  HOH F 781  HOH F 782                    
SITE     8 EC1 35 HOH F 784  HOH F 786  HOH F 804  HOH F 805                    
SITE     9 EC1 35 HOH F 816  HOH F 817  HOH F 980                               
SITE     1 EC2  5 NAI G 606  HOH G 706  HOH G 707  HOH G 708                    
SITE     2 EC2  5 HOH G 709                                                     
SITE     1 EC3  5 THR G  39  VAL G  40  ASP G 109  GLN G 196                    
SITE     2 EC3  5 HOH G 718                                                     
SITE     1 EC4  6 GLU G 157  PRO G 158  VAL G 159  HOH G1103                    
SITE     2 EC4  6 HOH G1104  TYR H 468                                          
SITE     1 EC5  6 ILE G 146  ASP G 147  PHE G 150  HOH G1056                    
SITE     2 EC5  6 PHE H 459  HOH H 935                                          
SITE     1 EC6  5 PHE G 459  HOH G1012  ILE H 146  ASP H 147                    
SITE     2 EC6  5 PHE H 150                                                     
SITE     1 EC7 35 ILE G 165  ILE G 166  PRO G 167  TRP G 168                    
SITE     2 EC7 35 ASN G 169  LYS G 192  ALA G 194  GLU G 195                    
SITE     3 EC7 35 GLY G 225  GLY G 229  ALA G 230  PHE G 243                    
SITE     4 EC7 35 GLY G 245  SER G 246  ILE G 249  ILE G 253                    
SITE     5 EC7 35 GLU G 268  LEU G 269  CYS G 302  GLN G 349                    
SITE     6 EC7 35 LYS G 352  GLU G 399  PHE G 401   MG G 601                    
SITE     7 EC7 35 HOH G 704  HOH G 705  HOH G 707  HOH G 708                    
SITE     8 EC7 35 HOH G 709  HOH G 710  HOH G 711  HOH G 736                    
SITE     9 EC7 35 HOH G 737  HOH G 845  HOH G1097                               
SITE     1 EC8  5 NAI H 605  HOH H 763  HOH H 768  HOH H 769                    
SITE     2 EC8  5 HOH H 770                                                     
SITE     1 EC9  5 THR H  39  VAL H  40  ASP H 109  GLN H 196                    
SITE     2 EC9  5 HOH H 753                                                     
SITE     1 FC1  6 TYR G 468  GLU H 157  PRO H 158  VAL H 159                    
SITE     2 FC1  6 HOH H 850  HOH H 851                                          
SITE     1 FC2  4 PHE E 151  SER G 443  TYR H 153  ARG H 155                    
SITE     1 FC3 33 ILE H 165  ILE H 166  PRO H 167  TRP H 168                    
SITE     2 FC3 33 ASN H 169  LYS H 192  ALA H 194  GLU H 195                    
SITE     3 FC3 33 GLN H 196  GLY H 225  GLY H 229  ALA H 230                    
SITE     4 FC3 33 PHE H 243  GLY H 245  SER H 246  ILE H 249                    
SITE     5 FC3 33 ILE H 253  GLU H 268  LEU H 269  CYS H 302                    
SITE     6 FC3 33 GLN H 349  GLU H 399  PHE H 401   MG H 601                    
SITE     7 FC3 33 HOH H 724  HOH H 725  HOH H 762  HOH H 763                    
SITE     8 FC3 33 HOH H 765  HOH H 767  HOH H 771  HOH H 773                    
SITE     9 FC3 33 HOH H 793                                                     
CRYST1  141.492  150.873  177.195  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      0.007068  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006628  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005644        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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