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Database: PDB
Entry: 3N82
LinkDB: 3N82
Original site: 3N82 
HEADER    OXIDOREDUCTASE                          27-MAY-10   3N82              
TITLE     T244A MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE, NADH      
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDEHYDE DEHYDROGENASE, MITOCHONDRIAL;                     
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: MATURE SEQUENCE, RESIDUES 18-517;                          
COMPND   5 EC: 1.2.1.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ALDH2, ALDM;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT-7-7                                    
KEYWDS    OXIDOREDUCTASE, ALDH, ROSSMANN FOLD                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.GONZALEZ-SEGURA,T.D.HURLEY                                          
REVDAT   3   31-JAN-18 3N82    1       JRNL                                     
REVDAT   2   08-NOV-17 3N82    1       REMARK                                   
REVDAT   1   13-APR-11 3N82    0                                                
JRNL        AUTH   K.-K.HO,L.GONZALEZ-SEGURA,S.PEREZ-MILLER,H.WEINER,T.D.HURLEY 
JRNL        TITL   CONFORMATIONAL SELECTION DURING CATALYSIS: THE ROLE OF       
JRNL        TITL 2 THREONINE 244 IN ALDH2                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.-K.HO,T.D.HURLEY,H.WEINER                                  
REMARK   1  TITL   SELECTIVE ALTERATION OF THE RATE-LIMITING STEP IN CYTOSOLIC  
REMARK   1  TITL 2 ALDEHYDE DEHYDROGENASE THROUGH RANDOM MUTAGENESIS            
REMARK   1  REF    BIOCHEMISTRY                  V.  45  9445 2006              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   H.N.LARSON,J.ZHOU,Z.CHEN,J.S.STAMLER,H.WEINER,T.D.HURLEY     
REMARK   1  TITL   STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF COENZYME BINDING   
REMARK   1  TITL 2 TO THE INACTIVE ASIAN VARIANT OF MITOCHONDRIAL ALDEHYDE      
REMARK   1  TITL 3 DEHYDROGENASE (ROLES OF RESIDUES 475 AND 487)                
REMARK   1  REF    J. BIOL. CHEM.                V. 282 12940 2007              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0037                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 179564                         
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 + TEST SET) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8995                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12119                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.95                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1890                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 656                          
REMARK   3   BIN FREE R VALUE                    : 0.2590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 30368                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 516                                     
REMARK   3   SOLVENT ATOMS            : 2676                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.36000                                              
REMARK   3    B22 (A**2) : -2.02000                                             
REMARK   3    B33 (A**2) : -1.34000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.224         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.935         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 31813 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 43217 ; 1.073 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4008 ; 5.713 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1414 ;35.462 ;24.682       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5096 ;12.893 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   160 ;15.726 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4720 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 24420 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 16358 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 21980 ; 0.300 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  3078 ; 0.121 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    11 ; 0.050 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    71 ; 0.162 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    42 ; 0.117 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 19809 ; 0.313 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31798 ; 0.616 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 12510 ; 1.139 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11417 ; 1.896 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3N82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059497.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC BLUE                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 179717                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIRECT REFINEMENT            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1O05                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM ACES (N-[2-ACETAMIDO]-2           
REMARK 280  -AMINOETHANE SULFONIC ACID), 1-10MM MGCL2, 100-200 MM GUANIDINE     
REMARK 280  HCL, 16-17% W/V PEG 6000, PH 6.4, VAPOR DIFFUSION, TEMPERATURE      
REMARK 280  292K                                                                
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       71.10800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.64950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.36200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.64950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       71.10800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.36200            
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: 30150 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -144.0 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: 30910 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.0 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       26.37   -146.83                                   
REMARK 500    VAL A 120      -73.15   -106.78                                   
REMARK 500    THR A 227      -83.16    -97.34                                   
REMARK 500    SER A 260     -104.98   -108.07                                   
REMARK 500    LEU A 269     -151.92   -113.29                                   
REMARK 500    TYR A 379       57.25    -95.88                                   
REMARK 500    LYS A 411      -60.60   -101.60                                   
REMARK 500    LYS A 469     -132.65     52.44                                   
REMARK 500    LEU A 477      162.94     78.19                                   
REMARK 500    GLN A 497      103.55   -160.71                                   
REMARK 500    ASN B  20       25.24   -151.31                                   
REMARK 500    VAL B 120      -71.41   -107.49                                   
REMARK 500    THR B 227      -81.51    -98.23                                   
REMARK 500    SER B 260      -96.27   -103.17                                   
REMARK 500    LEU B 269     -159.50   -117.55                                   
REMARK 500    GLN B 300       59.69    -92.72                                   
REMARK 500    TYR B 379       54.13    -90.99                                   
REMARK 500    LYS B 411      -63.87   -102.88                                   
REMARK 500    LYS B 469     -132.71     50.12                                   
REMARK 500    LEU B 477      163.32     71.03                                   
REMARK 500    ASN C  20       28.55   -149.39                                   
REMARK 500    VAL C 120      -76.89   -110.00                                   
REMARK 500    THR C 227      -83.53    -99.85                                   
REMARK 500    SER C 260     -107.94   -105.10                                   
REMARK 500    LEU C 269     -160.26   -118.26                                   
REMARK 500    LYS C 469     -131.19     53.43                                   
REMARK 500    LEU C 477      166.56     68.87                                   
REMARK 500    ASN D  20       25.31   -147.06                                   
REMARK 500    VAL D 120      -71.60   -112.46                                   
REMARK 500    THR D 227      -78.90    -98.70                                   
REMARK 500    SER D 260     -103.17   -105.58                                   
REMARK 500    LEU D 269     -164.44   -118.76                                   
REMARK 500    GLN D 300       61.63   -101.19                                   
REMARK 500    GLN D 300       57.52   -101.19                                   
REMARK 500    TYR D 379       55.43   -103.79                                   
REMARK 500    LYS D 469     -132.65     49.76                                   
REMARK 500    LEU D 477      168.21     68.91                                   
REMARK 500    ASN E  20       22.54   -148.51                                   
REMARK 500    VAL E 120      -69.10   -105.08                                   
REMARK 500    THR E 227      -81.42   -101.14                                   
REMARK 500    SER E 260     -106.15    -99.47                                   
REMARK 500    LEU E 269     -162.68   -115.53                                   
REMARK 500    GLN E 300       58.72    -92.29                                   
REMARK 500    TYR E 379       58.23   -111.79                                   
REMARK 500    LYS E 469     -131.11     48.08                                   
REMARK 500    LEU E 477      164.45     68.72                                   
REMARK 500    ASN F  20       28.92   -145.18                                   
REMARK 500    VAL F 120      -73.54   -100.29                                   
REMARK 500    THR F 227      -84.26    -98.84                                   
REMARK 500    SER F 260      -98.57   -106.17                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      72 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 605  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAD E 505   O1N                                                    
REMARK 620 2 NAD E 505   O2A  73.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 607  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAD G 507   O2A                                                    
REMARK 620 2 NAD G 507   O1N  76.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 608  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAD H 508   O2A                                                    
REMARK 620 2 NAD H 508   O1N  71.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAD A 501   O1N                                                    
REMARK 620 2 NAD A 501   O2A  70.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAD B 502   O1N                                                    
REMARK 620 2 NAD B 502   O2A  70.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 606  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAD F 506   O1N                                                    
REMARK 620 2 NAD F 506   O2A  71.7                                              
REMARK 620 3 HOH F2345   O    90.9  81.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 604  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAD D 504   O2A                                                    
REMARK 620 2 NAD D 504   O1N  69.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 603  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NAD C 503   O2A                                                    
REMARK 620 2 HOH C1286   O    85.1                                              
REMARK 620 3 HOH C1222   O    81.8 166.8                                        
REMARK 620 4 NAD C 503   O1N  68.5  85.6  89.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 701  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 196   O                                                      
REMARK 620 2 VAL A  40   O   164.1                                              
REMARK 620 3 ASP A 109   OD1  87.5 104.4                                        
REMARK 620 4 ASP A 109   O    94.9  97.9  77.1                                  
REMARK 620 5 THR A  39   OG1  76.0 101.5  56.9 133.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 703  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C1718   O                                                      
REMARK 620 2 GLN C 196   O    86.1                                              
REMARK 620 3 VAL C  40   O    89.0 165.1                                        
REMARK 620 4 ASP C 109   O    78.7  96.8  96.0                                  
REMARK 620 5 ASP C 109   OD1 154.0  86.0 104.2  77.7                            
REMARK 620 6 THR C  39   OG1 143.6  73.6 102.8 132.6  55.7                      
REMARK 620 7 HOH C1342   O    74.9  77.6  87.5 153.3 127.1  71.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA E 705  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH E1984   O                                                      
REMARK 620 2 VAL E  40   O    89.9                                              
REMARK 620 3 GLN E 196   O    87.7 164.3                                        
REMARK 620 4 ASP E 109   O    98.3 100.6  95.1                                  
REMARK 620 5 ASP E 109   OD1 166.8 102.3  81.8  74.9                            
REMARK 620 6 THR E  39   OG1 127.5  97.1  72.3 130.7  56.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA G 707  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL G  40   O                                                      
REMARK 620 2 ASP G 109   OD1 108.3                                              
REMARK 620 3 GLN G 196   O   166.5  83.1                                        
REMARK 620 4 ASP G 109   O    96.3  76.6  93.4                                  
REMARK 620 5 THR G  39   OG1 110.9  62.6  67.2 136.0                            
REMARK 620 6 HOH G2465   O    84.8 134.3  81.9 147.1  71.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 704  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN D 196   O                                                      
REMARK 620 2 VAL D  40   O   171.5                                              
REMARK 620 3 ASP D 109   OD1  85.3  93.2                                        
REMARK 620 4 ASP D 109   O    97.2  90.6  76.0                                  
REMARK 620 5 HOH D2424   O    79.0  95.6 128.5 154.1                            
REMARK 620 6 THR D  39   OG1  72.5  99.8  55.0 130.2  73.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 702  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN B 196   O                                                      
REMARK 620 2 ASP B 109   OD1  83.9                                              
REMARK 620 3 HOH B1956   O    81.5 157.4                                        
REMARK 620 4 ASP B 109   O   100.8  80.8  85.1                                  
REMARK 620 5 VAL B  40   O   160.2 107.5  91.6  97.0                            
REMARK 620 6 THR B  39   OG1  68.6  58.1 130.1 137.9 103.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA H 708  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN H 196   O                                                      
REMARK 620 2 VAL H  40   O   169.0                                              
REMARK 620 3 ASP H 109   OD1  90.3 100.5                                        
REMARK 620 4 ASP H 109   O    92.9  91.8  76.8                                  
REMARK 620 5 THR H  39   OG1  81.8 102.4  55.6 131.8                            
REMARK 620 6 HOH H1571   O    85.8  85.6 130.3 152.9  74.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA F 706  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 109   O                                                      
REMARK 620 2 ASP F 109   OD1  83.4                                              
REMARK 620 3 GLN F 196   O   101.9  88.6                                        
REMARK 620 4 HOH F1585   O    85.0 164.5  83.8                                  
REMARK 620 5 VAL F  40   O   100.0 108.0 153.8  84.1                            
REMARK 620 6 THR F  39   OG1 141.1  59.1  69.8 129.5 101.0                      
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 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 911                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 921                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 812                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 912                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 913                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 923                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 963                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 814                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 944                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 705                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 815                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 915                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 925                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD E 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 706                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 826                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 916                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 926                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 946                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 966                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD F 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 607                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 707                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 817                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 917                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 927                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD G 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 608                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 708                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI H 808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 908                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 928                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD H 508                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3N80   RELATED DB: PDB                                   
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE, APO FORM                 
REMARK 900 RELATED ID: 3N81   RELATED DB: PDB                                   
REMARK 900 T244A MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE, APO FORM 
REMARK 900 RELATED ID: 3N83   RELATED DB: PDB                                   
REMARK 900 T244A MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE, NAD      
REMARK 900 COMPLEX                                                              
DBREF  3N82 A    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N82 B    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N82 C    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N82 D    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N82 E    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N82 F    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N82 G    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N82 H    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
SEQADV 3N82 ALA A  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N82 ALA B  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N82 ALA C  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N82 ALA D  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N82 ALA E  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N82 ALA F  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N82 ALA G  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N82 ALA H  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
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 ALA 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 ALA 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 ALA 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 ALA 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 ALA 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 ALA 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 ALA 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 ALA 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  A 601       1                                                       
HET     NA  A 701       1                                                       
HET    GAI  A 801       4                                                       
HET    EDO  A 901       4                                                       
HET    EDO  A 911       4                                                       
HET    EDO  A 921       4                                                       
HET    NAD  A 501      44                                                       
HET     MG  B 602       1                                                       
HET     NA  B 702       1                                                       
HET    GAI  B 802       4                                                       
HET    GAI  B 812       4                                                       
HET    EDO  B 902       4                                                       
HET    EDO  B 912       4                                                       
HET    NAD  B 502      44                                                       
HET     MG  C 603       1                                                       
HET     NA  C 703       1                                                       
HET    GAI  C 803       4                                                       
HET    EDO  C 903       4                                                       
HET    EDO  C 913       4                                                       
HET    EDO  C 923       4                                                       
HET    EDO  C 963       4                                                       
HET    NAD  C 503      44                                                       
HET     MG  D 604       1                                                       
HET     NA  D 704       1                                                       
HET    GAI  D 804       4                                                       
HET    GAI  D 814       4                                                       
HET    EDO  D 904       4                                                       
HET    EDO  D 944       4                                                       
HET    NAD  D 504      44                                                       
HET     MG  E 605       1                                                       
HET     NA  E 705       1                                                       
HET    GAI  E 805       4                                                       
HET    GAI  E 815       4                                                       
HET    EDO  E 905       4                                                       
HET    EDO  E 915       4                                                       
HET    EDO  E 925       4                                                       
HET    NAD  E 505      44                                                       
HET     MG  F 606       1                                                       
HET     NA  F 706       1                                                       
HET    GAI  F 806       4                                                       
HET    GAI  F 826       4                                                       
HET    EDO  F 906       4                                                       
HET    EDO  F 916       4                                                       
HET    EDO  F 926       4                                                       
HET    EDO  F 946       4                                                       
HET    EDO  F 966       4                                                       
HET    NAD  F 506      44                                                       
HET     MG  G 607       1                                                       
HET     NA  G 707       1                                                       
HET    GAI  G 807       4                                                       
HET    GAI  G 817       4                                                       
HET    EDO  G 907       4                                                       
HET    EDO  G 917       4                                                       
HET    EDO  G 927       4                                                       
HET    NAD  G 507      44                                                       
HET     MG  H 608       1                                                       
HET     NA  H 708       1                                                       
HET    GAI  H 808       4                                                       
HET    EDO  H 908       4                                                       
HET    EDO  H 928       4                                                       
HET    NAD  H 508      44                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM     GAI GUANIDINE                                                        
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   9   MG    8(MG 2+)                                                     
FORMUL  10   NA    8(NA 1+)                                                     
FORMUL  11  GAI    13(C H5 N3)                                                  
FORMUL  12  EDO    24(C2 H6 O2)                                                 
FORMUL  15  NAD    8(C21 H27 N7 O14 P2)                                         
FORMUL  70  HOH   *2676(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 GLU A  312  SER A  328  1                                  17    
HELIX   14  14 ASP A  346  GLU A  363  1                                  18    
HELIX   15  15 MET A  393  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 GLY A  478  ALA A  484  5                                   7    
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  SER B  234  1                                   8    
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 GLU B  479  ALA B  484  5                                   6    
HELIX   39  39 ASP C   55  PHE C   70  1                                  16    
HELIX   40  40 SER C   74  MET C   79  1                                   6    
HELIX   41  41 ASP C   80  ASP C   98  1                                  19    
HELIX   42  42 ASP C   98  GLY C  111  1                                  14    
HELIX   43  43 PRO C  113  VAL C  120  1                                   8    
HELIX   44  44 VAL C  120  ALA C  136  1                                  17    
HELIX   45  45 PHE C  170  THR C  185  1                                  16    
HELIX   46  46 PRO C  198  GLY C  212  1                                  15    
HELIX   47  47 THR C  227  SER C  234  1                                   8    
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 GLY C  478  ALA C  484  5                                   7    
HELIX   57  57 ASP D   55  PHE D   70  1                                  16    
HELIX   58  58 SER D   74  MET D   79  1                                   6    
HELIX   59  59 ASP D   80  ASP D   98  1                                  19    
HELIX   60  60 ASP D   98  GLY D  111  1                                  14    
HELIX   61  61 PRO D  113  VAL D  120  1                                   8    
HELIX   62  62 VAL D  120  ALA D  136  1                                  17    
HELIX   63  63 PHE D  170  THR D  185  1                                  16    
HELIX   64  64 PRO D  198  GLY D  212  1                                  15    
HELIX   65  65 THR D  227  SER D  234  1                                   8    
HELIX   66  66 SER D  246  SER D  260  1                                  15    
HELIX   67  67 ASP D  282  PHE D  296  1                                  15    
HELIX   68  68 ASN D  297  GLN D  300  5                                   4    
HELIX   69  69 ILE D  314  ARG D  329  1                                  16    
HELIX   70  70 ASP D  346  GLU D  363  1                                  18    
HELIX   71  71 MET D  393  GLU D  398  1                                   6    
HELIX   72  72 THR D  412  ASN D  422  1                                  11    
HELIX   73  73 ASP D  435  LEU D  446  1                                  12    
HELIX   74  74 TYR D  468  MET D  470  5                                   3    
HELIX   75  75 GLU D  479  ALA D  484  5                                   6    
HELIX   76  76 ASP E   55  PHE E   70  1                                  16    
HELIX   77  77 SER E   74  MET E   79  1                                   6    
HELIX   78  78 ASP E   80  ASP E   98  1                                  19    
HELIX   79  79 ASP E   98  GLY E  111  1                                  14    
HELIX   80  80 PRO E  113  VAL E  120  1                                   8    
HELIX   81  81 VAL E  120  GLY E  134  1                                  15    
HELIX   82  82 PHE E  170  THR E  185  1                                  16    
HELIX   83  83 PRO E  198  GLY E  212  1                                  15    
HELIX   84  84 THR E  227  SER E  234  1                                   8    
HELIX   85  85 SER E  246  SER E  260  1                                  15    
HELIX   86  86 ASP E  282  PHE E  296  1                                  15    
HELIX   87  87 ASN E  297  GLN E  300  5                                   4    
HELIX   88  88 ILE E  314  ARG E  329  1                                  16    
HELIX   89  89 ASP E  346  GLU E  363  1                                  18    
HELIX   90  90 MET E  393  LYS E  397  5                                   5    
HELIX   91  91 THR E  412  ASN E  422  1                                  11    
HELIX   92  92 ASP E  435  LEU E  446  1                                  12    
HELIX   93  93 TYR E  468  MET E  470  5                                   3    
HELIX   94  94 GLU E  479  ALA E  484  5                                   6    
HELIX   95  95 ASP F   55  PHE F   70  1                                  16    
HELIX   96  96 SER F   74  MET F   79  1                                   6    
HELIX   97  97 ASP F   80  ASP F   98  1                                  19    
HELIX   98  98 ASP F   98  GLY F  111  1                                  14    
HELIX   99  99 PRO F  113  VAL F  120  1                                   8    
HELIX  100 100 VAL F  120  ALA F  136  1                                  17    
HELIX  101 101 PHE F  170  THR F  185  1                                  16    
HELIX  102 102 PRO F  198  GLY F  212  1                                  15    
HELIX  103 103 THR F  227  SER F  234  1                                   8    
HELIX  104 104 SER F  246  SER F  260  1                                  15    
HELIX  105 105 ASP F  282  PHE F  296  1                                  15    
HELIX  106 106 ASN F  297  GLN F  300  5                                   4    
HELIX  107 107 GLU F  312  ARG F  329  1                                  18    
HELIX  108 108 ASP F  346  GLU F  363  1                                  18    
HELIX  109 109 MET F  393  GLU F  398  1                                   6    
HELIX  110 110 THR F  412  ASN F  422  1                                  11    
HELIX  111 111 ASP F  435  LEU F  446  1                                  12    
HELIX  112 112 TYR F  468  MET F  470  5                                   3    
HELIX  113 113 GLY F  478  ALA F  484  5                                   7    
HELIX  114 114 ASP G   55  PHE G   70  1                                  16    
HELIX  115 115 SER G   74  MET G   79  1                                   6    
HELIX  116 116 ASP G   80  ASP G   98  1                                  19    
HELIX  117 117 ASP G   98  GLY G  111  1                                  14    
HELIX  118 118 PRO G  113  VAL G  120  1                                   8    
HELIX  119 119 VAL G  120  ALA G  136  1                                  17    
HELIX  120 120 PHE G  170  THR G  185  1                                  16    
HELIX  121 121 PRO G  198  GLY G  212  1                                  15    
HELIX  122 122 THR G  227  SER G  234  1                                   8    
HELIX  123 123 SER G  246  SER G  260  1                                  15    
HELIX  124 124 ASP G  282  PHE G  296  1                                  15    
HELIX  125 125 ASN G  297  GLN G  300  5                                   4    
HELIX  126 126 GLU G  312  ARG G  329  1                                  18    
HELIX  127 127 ASP G  346  GLU G  363  1                                  18    
HELIX  128 128 MET G  393  GLU G  398  1                                   6    
HELIX  129 129 THR G  412  ASN G  422  1                                  11    
HELIX  130 130 ASP G  435  LEU G  446  1                                  12    
HELIX  131 131 TYR G  468  MET G  470  5                                   3    
HELIX  132 132 GLY G  478  ALA G  484  5                                   7    
HELIX  133 133 ASP H   55  PHE H   70  1                                  16    
HELIX  134 134 SER H   74  MET H   79  1                                   6    
HELIX  135 135 ASP H   80  ASP H   98  1                                  19    
HELIX  136 136 ASP H   98  GLY H  111  1                                  14    
HELIX  137 137 PRO H  113  VAL H  120  1                                   8    
HELIX  138 138 VAL H  120  ALA H  136  1                                  17    
HELIX  139 139 PHE H  170  THR H  185  1                                  16    
HELIX  140 140 PRO H  198  GLY H  212  1                                  15    
HELIX  141 141 THR H  227  SER H  234  1                                   8    
HELIX  142 142 SER H  246  SER H  260  1                                  15    
HELIX  143 143 ASP H  282  PHE H  296  1                                  15    
HELIX  144 144 ASN H  297  GLN H  300  5                                   4    
HELIX  145 145 ILE H  314  ARG H  329  1                                  16    
HELIX  146 146 ASP H  346  GLU H  363  1                                  18    
HELIX  147 147 MET H  393  GLU H  398  1                                   6    
HELIX  148 148 THR H  412  ASN H  422  1                                  11    
HELIX  149 149 ASP H  435  LEU H  446  1                                  12    
HELIX  150 150 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  THR B 308   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  PHE B 432   N  ILE B 276           
SHEET    7   C20 THR B 450  VAL B 453  1  O  TRP B 452   N  ALA B 429           
SHEET    8   C20 THR A 486  LYS A 494  1  N  THR A 490   O  VAL B 451           
SHEET    9   C20 PHE A 150  PRO A 158 -1  N  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  GLY D 141   N  THR A 143           
SHEET   12   C20 PHE D 150  PRO D 158 -1  O  SER D 152   N  ILE D 144           
SHEET   13   C20 THR D 486  LYS D 494 -1  O  GLU D 487   N  GLU D 157           
SHEET   14   C20 THR C 450  VAL C 453  1  N  VAL C 451   O  THR D 490           
SHEET   15   C20 ALA C 428  PHE C 432  1  N  ALA C 429   O  TRP C 452           
SHEET   16   C20 PRO C 274  ILE C 277  1  N  ILE C 276   O  ALA C 430           
SHEET   17   C20 ARG C 307  GLN C 311  1  O  ARG C 307   N  ASN C 275           
SHEET   18   C20 VAL C 404  PHE C 410  1  O  LEU C 408   N  THR C 308           
SHEET   19   C20 THR C 384  GLY C 387  1  N  PHE C 386   O  MET C 405           
SHEET   20   C20 LYS C 366  CYS C 369 -1  N  LEU C 368   O  VAL C 385           
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  ALA 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  PHE A 386           
SHEET    4   E20 ARG A 307  GLN A 311  1  N  THR A 308   O  LEU A 408           
SHEET    5   E20 PRO A 274  ILE A 277  1  N  ASN A 275   O  ARG A 307           
SHEET    6   E20 ALA A 428  PHE A 432  1  O  PHE A 432   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 491   N  TYR C 153           
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  PHE D 386   O  MET D 405           
SHEET   20   E20 LYS D 366  CYS D 369 -1  N  LYS D 366   O  GLY D 387           
SHEET    1   F 2 ILE B  22  ILE B  24  0                                        
SHEET    2   F 2 GLU B  27  HIS B  29 -1  O  HIS B  29   N  ILE B  22           
SHEET    1   G 2 THR B  36  VAL B  40  0                                        
SHEET    2   G 2 VAL B  47  ALA B  52 -1  O  ILE B  48   N  THR B  39           
SHEET    1   H 6 VAL B 218  ILE B 220  0                                        
SHEET    2   H 6 VAL B 188  LYS B 192  1  N  MET B 191   O  ASN B 219           
SHEET    3   H 6 VAL B 161  ILE B 165  1  N  GLN B 164   O  LYS B 192           
SHEET    4   H 6 LYS B 240  ALA B 244  1  O  LYS B 240   N  GLY B 163           
SHEET    5   H 6 ARG B 264  GLU B 268  1  O  ARG B 264   N  VAL B 241           
SHEET    6   H 6 GLY B 472  SER B 473 -1  O  SER B 473   N  LEU B 267           
SHEET    1   I 2 ILE C  22  ILE C  24  0                                        
SHEET    2   I 2 GLU C  27  HIS C  29 -1  O  HIS C  29   N  ILE C  22           
SHEET    1   J 2 THR C  36  VAL C  40  0                                        
SHEET    2   J 2 VAL C  47  ALA C  52 -1  O  ILE C  48   N  THR C  39           
SHEET    1   K 6 VAL C 218  ILE C 220  0                                        
SHEET    2   K 6 VAL C 188  LYS C 192  1  N  MET C 191   O  ASN C 219           
SHEET    3   K 6 VAL C 161  ILE C 165  1  N  GLN C 164   O  LYS C 192           
SHEET    4   K 6 LYS C 240  ALA 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 TYR C 425  GLY C 426  0                                        
SHEET    2   L 2 TYR C 468  LYS C 469 -1  O  TYR C 468   N  GLY C 426           
SHEET    1   M 2 ILE D  22  ILE D  24  0                                        
SHEET    2   M 2 GLU D  27  HIS D  29 -1  O  HIS D  29   N  ILE D  22           
SHEET    1   N 2 THR D  36  VAL D  40  0                                        
SHEET    2   N 2 VAL D  47  ALA D  52 -1  O  ILE D  48   N  THR D  39           
SHEET    1   O 6 VAL D 218  ILE D 220  0                                        
SHEET    2   O 6 VAL D 188  LYS D 192  1  N  MET D 191   O  ASN D 219           
SHEET    3   O 6 VAL D 161  ILE D 165  1  N  GLN D 164   O  LYS D 192           
SHEET    4   O 6 LYS D 240  ALA D 244  1  O  LYS D 240   N  GLY D 163           
SHEET    5   O 6 ARG D 264  GLU D 268  1  O  ARG D 264   N  VAL D 241           
SHEET    6   O 6 GLY D 472  SER D 473 -1  O  SER D 473   N  LEU D 267           
SHEET    1   P 2 ILE E  22  ILE E  24  0                                        
SHEET    2   P 2 GLU E  27  HIS E  29 -1  O  HIS E  29   N  ILE E  22           
SHEET    1   Q 2 THR E  36  VAL E  40  0                                        
SHEET    2   Q 2 VAL E  47  ALA E  52 -1  O  ILE E  48   N  THR E  39           
SHEET    1   R20 LYS F 366  CYS F 369  0                                        
SHEET    2   R20 THR F 384  GLY F 387 -1  O  GLY F 387   N  LYS F 366           
SHEET    3   R20 VAL F 404  PHE F 410  1  O  MET F 405   N  PHE F 386           
SHEET    4   R20 ARG F 307  GLN F 311  1  N  VAL F 310   O  LEU F 408           
SHEET    5   R20 PRO F 274  ILE F 277  1  N  ILE F 277   O  PHE F 309           
SHEET    6   R20 ALA F 428  PHE F 432  1  O  ALA F 430   N  ILE F 276           
SHEET    7   R20 THR F 450  VAL F 453  1  O  TRP F 452   N  VAL F 431           
SHEET    8   R20 THR E 486  LYS E 494  1  N  THR E 490   O  VAL F 451           
SHEET    9   R20 PHE E 150  PRO E 158 -1  N  PHE E 151   O  VAL E 493           
SHEET   10   R20 GLY E 141  ILE E 144 -1  N  ILE E 144   O  SER E 152           
SHEET   11   R20 GLY H 141  ILE H 144 -1  O  GLY H 141   N  THR E 143           
SHEET   12   R20 PHE H 150  PRO H 158 -1  O  SER H 152   N  ILE H 144           
SHEET   13   R20 THR H 486  LYS H 494 -1  O  VAL H 493   N  PHE H 151           
SHEET   14   R20 THR G 450  VAL G 453  1  N  VAL G 451   O  THR H 490           
SHEET   15   R20 ALA G 428  PHE G 432  1  N  VAL G 431   O  TRP G 452           
SHEET   16   R20 PRO G 274  ILE G 277  1  N  ILE G 276   O  ALA G 430           
SHEET   17   R20 ARG G 307  GLN G 311  1  O  PHE G 309   N  ILE G 277           
SHEET   18   R20 VAL G 404  PHE G 410  1  O  LEU G 408   N  VAL G 310           
SHEET   19   R20 THR G 384  GLY G 387  1  N  PHE G 386   O  MET G 405           
SHEET   20   R20 LYS G 366  CYS G 369 -1  N  LEU G 368   O  VAL G 385           
SHEET    1   S 6 VAL E 218  ILE E 220  0                                        
SHEET    2   S 6 VAL E 188  LYS E 192  1  N  MET E 191   O  ASN E 219           
SHEET    3   S 6 VAL E 161  ILE E 165  1  N  CYS E 162   O  VAL E 188           
SHEET    4   S 6 LYS E 240  ALA E 244  1  O  LYS E 240   N  GLY E 163           
SHEET    5   S 6 ARG E 264  GLU E 268  1  O  ARG E 264   N  VAL E 241           
SHEET    6   S 6 GLY E 472  SER E 473 -1  O  SER E 473   N  LEU E 267           
SHEET    1   T20 LYS E 366  CYS E 369  0                                        
SHEET    2   T20 THR E 384  GLY E 387 -1  O  GLY E 387   N  LYS E 366           
SHEET    3   T20 VAL E 404  PHE E 410  1  O  MET E 405   N  THR E 384           
SHEET    4   T20 ARG E 307  GLN E 311  1  N  VAL E 310   O  LEU E 408           
SHEET    5   T20 PRO E 274  ILE E 277  1  N  ILE E 277   O  PHE E 309           
SHEET    6   T20 ALA E 428  PHE E 432  1  O  ALA E 430   N  ILE E 276           
SHEET    7   T20 THR E 450  VAL E 453  1  O  TRP E 452   N  ALA E 429           
SHEET    8   T20 THR F 486  LYS F 494  1  O  THR F 490   N  VAL E 451           
SHEET    9   T20 PHE F 150  PRO F 158 -1  N  PHE F 151   O  VAL F 493           
SHEET   10   T20 GLY F 141  ILE F 144 -1  N  ILE F 144   O  SER F 152           
SHEET   11   T20 GLY G 141  ILE G 144 -1  O  THR G 143   N  GLY F 141           
SHEET   12   T20 PHE G 150  PRO G 158 -1  O  SER G 152   N  ILE G 144           
SHEET   13   T20 THR G 486  LYS G 494 -1  O  VAL G 491   N  TYR G 153           
SHEET   14   T20 THR H 450  VAL H 453  1  O  VAL H 453   N  THR G 492           
SHEET   15   T20 ALA H 428  PHE H 432  1  N  ALA H 429   O  TRP H 452           
SHEET   16   T20 PRO H 274  ILE H 277  1  N  ILE H 276   O  ALA H 430           
SHEET   17   T20 ARG H 307  GLN H 311  1  O  PHE H 309   N  ILE H 277           
SHEET   18   T20 VAL H 404  PHE H 410  1  O  LEU H 408   N  VAL H 310           
SHEET   19   T20 THR H 384  GLY H 387  1  N  PHE H 386   O  MET H 405           
SHEET   20   T20 LYS H 366  CYS H 369 -1  N  LYS H 366   O  GLY H 387           
SHEET    1   U 2 ILE F  22  ILE F  24  0                                        
SHEET    2   U 2 GLU F  27  HIS F  29 -1  O  HIS F  29   N  ILE F  22           
SHEET    1   V 2 THR F  36  VAL F  40  0                                        
SHEET    2   V 2 VAL F  47  ALA F  52 -1  O  ILE F  48   N  THR F  39           
SHEET    1   W 6 VAL F 218  ILE F 220  0                                        
SHEET    2   W 6 VAL F 188  LYS F 192  1  N  MET F 191   O  ASN F 219           
SHEET    3   W 6 VAL F 161  ILE F 165  1  N  CYS F 162   O  VAL F 188           
SHEET    4   W 6 LYS F 240  ALA F 244  1  O  LYS F 240   N  GLY F 163           
SHEET    5   W 6 ARG F 264  GLU F 268  1  O  ARG F 264   N  VAL F 241           
SHEET    6   W 6 GLY F 472  SER F 473 -1  O  SER F 473   N  LEU F 267           
SHEET    1   X 2 ILE G  22  ILE G  24  0                                        
SHEET    2   X 2 GLU G  27  HIS G  29 -1  O  HIS G  29   N  ILE G  22           
SHEET    1   Y 2 THR G  36  VAL G  40  0                                        
SHEET    2   Y 2 VAL G  47  ALA G  52 -1  O  VAL G  51   N  PHE G  37           
SHEET    1   Z 6 VAL G 218  ILE G 220  0                                        
SHEET    2   Z 6 VAL G 188  LYS G 192  1  N  MET G 191   O  ASN G 219           
SHEET    3   Z 6 VAL G 161  ILE G 165  1  N  GLN G 164   O  LYS G 192           
SHEET    4   Z 6 LYS G 240  ALA G 244  1  O  LYS G 240   N  GLY G 163           
SHEET    5   Z 6 ARG G 264  GLU G 268  1  O  ARG G 264   N  VAL G 241           
SHEET    6   Z 6 GLY G 472  SER G 473 -1  O  SER G 473   N  LEU G 267           
SHEET    1  AA 2 ILE H  22  ILE H  24  0                                        
SHEET    2  AA 2 GLU H  27  HIS H  29 -1  O  HIS H  29   N  ILE H  22           
SHEET    1  AB 2 THR H  36  VAL H  40  0                                        
SHEET    2  AB 2 VAL H  47  ALA H  52 -1  O  ILE H  48   N  THR H  39           
SHEET    1  AC 6 VAL H 218  ILE H 220  0                                        
SHEET    2  AC 6 VAL H 188  LYS H 192  1  N  MET H 191   O  ASN H 219           
SHEET    3  AC 6 VAL H 161  ILE H 165  1  N  GLN H 164   O  LYS H 192           
SHEET    4  AC 6 LYS H 240  ALA H 244  1  O  LYS H 240   N  GLY H 163           
SHEET    5  AC 6 ARG H 264  GLU H 268  1  O  ARG H 264   N  VAL H 241           
SHEET    6  AC 6 GLY H 472  SER H 473 -1  O  SER H 473   N  LEU H 267           
SHEET    1  AD 2 TYR H 425  GLY H 426  0                                        
SHEET    2  AD 2 TYR H 468  LYS H 469 -1  N  TYR H 468   O  GLY H 426           
LINK        MG    MG E 605                 O1N NAD E 505     1555   1555  1.99  
LINK        MG    MG G 607                 O2A NAD G 507     1555   1555  2.11  
LINK        MG    MG G 607                 O1N NAD G 507     1555   1555  2.12  
LINK        MG    MG H 608                 O2A NAD H 508     1555   1555  2.18  
LINK        MG    MG A 601                 O1N NAD A 501     1555   1555  2.20  
LINK        MG    MG B 602                 O1N NAD B 502     1555   1555  2.20  
LINK        MG    MG F 606                 O1N NAD F 506     1555   1555  2.23  
LINK        MG    MG D 604                 O2A NAD D 504     1555   1555  2.25  
LINK        MG    MG C 603                 O2A NAD C 503     1555   1555  2.25  
LINK        MG    MG D 604                 O1N NAD D 504     1555   1555  2.27  
LINK        MG    MG F 606                 O2A NAD F 506     1555   1555  2.27  
LINK        MG    MG C 603                 O   HOH C1286     1555   1555  2.31  
LINK        MG    MG H 608                 O1N NAD H 508     1555   1555  2.32  
LINK         O   GLN A 196                NA    NA A 701     1555   1555  2.33  
LINK        NA    NA C 703                 O   HOH C1718     1555   1555  2.34  
LINK        NA    NA E 705                 O   HOH E1984     1555   1555  2.35  
LINK         O   VAL G  40                NA    NA G 707     1555   1555  2.35  
LINK         O   GLN C 196                NA    NA C 703     1555   1555  2.36  
LINK         O   GLN D 196                NA    NA D 704     1555   1555  2.36  
LINK         O   GLN B 196                NA    NA B 702     1555   1555  2.37  
LINK         O   GLN H 196                NA    NA H 708     1555   1555  2.37  
LINK        MG    MG E 605                 O2A NAD E 505     1555   1555  2.38  
LINK        MG    MG B 602                 O2A NAD B 502     1555   1555  2.38  
LINK        MG    MG C 603                 O   HOH C1222     1555   1555  2.38  
LINK        MG    MG A 601                 O2A NAD A 501     1555   1555  2.39  
LINK         O   ASP F 109                NA    NA F 706     1555   1555  2.40  
LINK         OD1 ASP F 109                NA    NA F 706     1555   1555  2.41  
LINK         O   VAL C  40                NA    NA C 703     1555   1555  2.41  
LINK         O   VAL E  40                NA    NA E 705     1555   1555  2.44  
LINK         O   VAL D  40                NA    NA D 704     1555   1555  2.44  
LINK         O   GLN F 196                NA    NA F 706     1555   1555  2.44  
LINK         OD1 ASP B 109                NA    NA B 702     1555   1555  2.45  
LINK         OD1 ASP G 109                NA    NA G 707     1555   1555  2.45  
LINK        NA    NA B 702                 O   HOH B1956     1555   1555  2.45  
LINK         O   ASP B 109                NA    NA B 702     1555   1555  2.46  
LINK        NA    NA F 706                 O   HOH F1585     1555   1555  2.46  
LINK         O   VAL A  40                NA    NA A 701     1555   1555  2.46  
LINK         O   GLN G 196                NA    NA G 707     1555   1555  2.46  
LINK         O   GLN E 196                NA    NA E 705     1555   1555  2.46  
LINK         O   VAL F  40                NA    NA F 706     1555   1555  2.46  
LINK        MG    MG C 603                 O1N NAD C 503     1555   1555  2.46  
LINK         OD1 ASP A 109                NA    NA A 701     1555   1555  2.48  
LINK         O   VAL B  40                NA    NA B 702     1555   1555  2.48  
LINK         O   ASP E 109                NA    NA E 705     1555   1555  2.50  
LINK         O   VAL H  40                NA    NA H 708     1555   1555  2.50  
LINK         OD1 ASP H 109                NA    NA H 708     1555   1555  2.53  
LINK         O   ASP C 109                NA    NA C 703     1555   1555  2.55  
LINK         OD1 ASP D 109                NA    NA D 704     1555   1555  2.57  
LINK         O   ASP A 109                NA    NA A 701     1555   1555  2.58  
LINK        MG    MG F 606                 O   HOH F2345     1555   1555  2.58  
LINK         OD1 ASP E 109                NA    NA E 705     1555   1555  2.59  
LINK         OD1 ASP C 109                NA    NA C 703     1555   1555  2.61  
LINK         O   ASP H 109                NA    NA H 708     1555   1555  2.62  
LINK         O   ASP G 109                NA    NA G 707     1555   1555  2.62  
LINK         O   ASP D 109                NA    NA D 704     1555   1555  2.67  
LINK        NA    NA D 704                 O   HOH D2424     1555   1555  2.72  
LINK         OG1 THR G  39                NA    NA G 707     1555   1555  2.84  
LINK         OG1 THR A  39                NA    NA A 701     1555   1555  2.85  
LINK         OG1 THR H  39                NA    NA H 708     1555   1555  2.91  
LINK         OG1 THR C  39                NA    NA C 703     1555   1555  2.95  
LINK        NA    NA G 707                 O   HOH G2465     1555   1555  2.96  
LINK         OG1 THR F  39                NA    NA F 706     1555   1555  3.01  
LINK         OG1 THR E  39                NA    NA E 705     1555   1555  3.01  
LINK         OG1 THR D  39                NA    NA D 704     1555   1555  3.01  
LINK         OG1 THR B  39                NA    NA B 702     1555   1555  3.02  
LINK        NA    NA H 708                 O   HOH H1571     1555   1555  3.09  
LINK        NA    NA C 703                 O   HOH C1342     1555   1555  3.13  
SITE     1 AC1  1 NAD A 501                                                     
SITE     1 AC2  4 THR A  39  VAL A  40  ASP A 109  GLN A 196                    
SITE     1 AC3  5 GLU A 157  PRO A 158  VAL A 159  HOH A 808                    
SITE     2 AC3  5 TYR B 468                                                     
SITE     1 AC4  4 TYR A 153  ARG A 155  SER B 443  PHE D 151                    
SITE     1 AC5  5 GLN A  14  ASN A  41  THR A  44  GLU A  46                    
SITE     2 AC5  5 ILE A  48                                                     
SITE     1 AC6  5 PHE A  18  ASP A  98  TYR A 101  TYR A 203                    
SITE     2 AC6  5 HOH A 971                                                     
SITE     1 AC7 27 ILE A 165  ILE A 166  PRO A 167  TRP A 168                    
SITE     2 AC7 27 ASN A 169  LYS A 192  ALA A 194  GLU A 195                    
SITE     3 AC7 27 GLY A 225  GLY A 229  ALA A 230  PHE A 243                    
SITE     4 AC7 27 GLY A 245  SER A 246  ILE A 249  ILE A 253                    
SITE     5 AC7 27 GLU A 268  LEU A 269  CYS A 302  GLN A 349                    
SITE     6 AC7 27 GLU A 399  PHE A 401  HOH A 539  HOH A 549                    
SITE     7 AC7 27  MG A 601  HOH A2201  HOH A2394                               
SITE     1 AC8  1 NAD B 502                                                     
SITE     1 AC9  5 THR B  39  VAL B  40  ASP B 109  GLN B 196                    
SITE     2 AC9  5 HOH B1956                                                     
SITE     1 BC1  4 GLU B 157  PRO B 158  VAL B 159  HOH B 525                    
SITE     1 BC2  3 PHE A 459  HOH A 608  ASP B 147                               
SITE     1 BC3  4 SER A 443  TYR B 153  ARG B 155  PHE C 151                    
SITE     1 BC4  4 GLN B  14  ASN B  41  THR B  44  VAL B  47                    
SITE     1 BC5 25 ILE B 165  ILE B 166  PRO B 167  TRP B 168                    
SITE     2 BC5 25 LYS B 192  ALA B 194  GLU B 195  GLN B 196                    
SITE     3 BC5 25 GLY B 225  GLY B 229  ALA B 230  PHE B 243                    
SITE     4 BC5 25 GLY B 245  SER B 246  ILE B 249  ILE B 253                    
SITE     5 BC5 25 GLU B 268  LEU B 269  CYS B 302  GLN B 349                    
SITE     6 BC5 25 GLU B 399  PHE B 401   MG B 602  HOH B 910                    
SITE     7 BC5 25 HOH B1922                                                     
SITE     1 BC6  3 NAD C 503  HOH C1222  HOH C1286                               
SITE     1 BC7  5 THR C  39  VAL C  40  ASP C 109  GLN C 196                    
SITE     2 BC7  5 HOH C1718                                                     
SITE     1 BC8  6 GLU C 157  PRO C 158  VAL C 159  HOH C 678                    
SITE     2 BC8  6 HOH C 846  TYR D 468                                          
SITE     1 BC9  4 PHE B 151  TYR C 153  ARG C 155  SER D 443                    
SITE     1 CC1  5 ASN C  41  THR C  44  GLU C  46  LEU C 108                    
SITE     2 CC1  5 HOH C2127                                                     
SITE     1 CC2  4 PHE C  18  TYR C 101  TYR C 203  HOH C1464                    
SITE     1 CC3  3 GLU C 347  PHE C 350  GLY F  45                               
SITE     1 CC4 30 ILE C 165  ILE C 166  PRO C 167  TRP C 168                    
SITE     2 CC4 30 LYS C 192  ALA C 194  GLU C 195  GLN C 196                    
SITE     3 CC4 30 GLY C 225  GLY C 229  ALA C 230  PHE C 243                    
SITE     4 CC4 30 GLY C 245  SER C 246  ILE C 249  ILE C 253                    
SITE     5 CC4 30 GLU C 268  LEU C 269  CYS C 302  GLN C 349                    
SITE     6 CC4 30 LYS C 352  GLU C 399  PHE C 401   MG C 603                    
SITE     7 CC4 30 HOH C1222  HOH C1279  HOH C1286  HOH C1452                    
SITE     8 CC4 30 HOH C1602  HOH C2005                                          
SITE     1 CC5  1 NAD D 504                                                     
SITE     1 CC6  5 THR D  39  VAL D  40  ASP D 109  GLN D 196                    
SITE     2 CC6  5 HOH D2424                                                     
SITE     1 CC7  4 TYR C 468  GLU D 157  PRO D 158  VAL D 159                    
SITE     1 CC8  4 VAL C 458  PHE C 459  ASP D 147  PHE D 150                    
SITE     1 CC9  5 PHE A 151  SER C 443  TYR D 153  ARG D 155                    
SITE     2 CC9  5 HOH D2650                                                     
SITE     1 DC1  5 GLU D 414  VAL D 417  TYR D 441  LYS G 361                    
SITE     2 DC1  5 HOH G2498                                                     
SITE     1 DC2 30 ILE D 165  ILE D 166  PRO D 167  TRP D 168                    
SITE     2 DC2 30 ASN D 169  LYS D 192  ALA D 194  GLU D 195                    
SITE     3 DC2 30 GLN D 196  GLY D 225  GLY D 229  ALA D 230                    
SITE     4 DC2 30 PHE D 243  GLY D 245  SER D 246  ILE D 249                    
SITE     5 DC2 30 ILE D 253  GLU D 268  LEU D 269  CYS D 302                    
SITE     6 DC2 30 GLN D 349  LYS D 352  GLU D 399  PHE D 401                    
SITE     7 DC2 30 HOH D 540   MG D 604  HOH D 767  HOH D1568                    
SITE     8 DC2 30 HOH D1917  HOH D2380                                          
SITE     1 DC3  1 NAD E 505                                                     
SITE     1 DC4  5 THR E  39  VAL E  40  ASP E 109  GLN E 196                    
SITE     2 DC4  5 HOH E1984                                                     
SITE     1 DC5  6 GLU E 157  PRO E 158  VAL E 159  HOH E 692                    
SITE     2 DC5  6 GLN F 447  TYR F 468                                          
SITE     1 DC6  4 ILE E 146  ASP E 147  PHE E 150  PHE F 459                    
SITE     1 DC7  5 TYR E 153  ARG E 155  HOH E1643  SER F 443                    
SITE     2 DC7  5 PHE H 151                                                     
SITE     1 DC8  4 ASN E  41  THR E  44  GLU E  46  ILE E  48                    
SITE     1 DC9  3 PHE E  18  TYR E 101  TYR E 203                               
SITE     1 EC1 28 ILE E 165  ILE E 166  PRO E 167  TRP E 168                    
SITE     2 EC1 28 ASN E 169  LYS E 192  GLU E 195  GLN E 196                    
SITE     3 EC1 28 GLY E 225  GLY E 229  ALA E 230  PHE E 243                    
SITE     4 EC1 28 GLY E 245  SER E 246  ILE E 249  ILE E 253                    
SITE     5 EC1 28 GLU E 268  LEU E 269  CYS E 302  GLN E 349                    
SITE     6 EC1 28 GLU E 399  PHE E 401   MG E 605  HOH E 867                    
SITE     7 EC1 28 HOH E1014  HOH E1284  HOH E1324  HOH E1763                    
SITE     1 EC2  2 NAD F 506  HOH F2345                                          
SITE     1 EC3  5 THR F  39  VAL F  40  ASP F 109  GLN F 196                    
SITE     2 EC3  5 HOH F1585                                                     
SITE     1 EC4  5 TYR E 468  GLU F 157  PRO F 158  VAL F 159                    
SITE     2 EC4  5 HOH F1990                                                     
SITE     1 EC5  4 ASP F 376  GLY F 378  EDO F 966  HOH F1836                    
SITE     1 EC6  4 SER E 443  TYR F 153  ARG F 155  PHE G 151                    
SITE     1 EC7  5 ASN F  41  THR F  44  GLU F  46  LEU F 108                    
SITE     2 EC7  5 HOH F2533                                                     
SITE     1 EC8  5 ARG E 321  HOH E1754  TYR F 101  TYR F 203                    
SITE     2 EC8  5 HOH F 972                                                     
SITE     1 EC9  7 LEU E  72  TYR F 441  GLN F 444  ALA F 445                    
SITE     2 EC9  7 HOH F 884  GLN H 497  ASN H 499                               
SITE     1 FC1  4 GLY C  45  GLU F 347  PHE F 350  GAI F 826                    
SITE     1 FC2 27 ILE F 165  ILE F 166  PRO F 167  TRP F 168                    
SITE     2 FC2 27 LYS F 192  ALA F 194  GLU F 195  GLN F 196                    
SITE     3 FC2 27 GLY F 225  GLY F 229  ALA F 230  PHE F 243                    
SITE     4 FC2 27 GLY F 245  SER F 246  ILE F 249  ILE F 253                    
SITE     5 FC2 27 GLU F 268  LEU F 269  CYS F 302  GLN F 349                    
SITE     6 FC2 27 LYS F 352  GLU F 399   MG F 606  HOH F1145                    
SITE     7 FC2 27 HOH F1192  HOH F1853  HOH F2445                               
SITE     1 FC3  1 NAD G 507                                                     
SITE     1 FC4  5 THR G  39  VAL G  40  ASP G 109  GLN G 196                    
SITE     2 FC4  5 HOH G2465                                                     
SITE     1 FC5  5 GLU G 157  PRO G 158  VAL G 159  HOH G 738                    
SITE     2 FC5  5 GLN H 447                                                     
SITE     1 FC6  5 ASP G 147  GLY G 148  PHE G 150  VAL H 458                    
SITE     2 FC6  5 PHE H 459                                                     
SITE     1 FC7  4 PHE F 151  TYR G 153  ARG G 155  SER H 443                    
SITE     1 FC8  3 ASN G  41  THR G  44  GLU G  46                               
SITE     1 FC9  2 TYR G 101  TYR G 203                                          
SITE     1 GC1 27 ILE G 165  ILE G 166  PRO G 167  TRP G 168                    
SITE     2 GC1 27 LYS G 192  ALA G 194  GLU G 195  GLN G 196                    
SITE     3 GC1 27 GLY G 225  GLY G 229  ALA G 230  PHE G 243                    
SITE     4 GC1 27 GLY G 245  SER G 246  ILE G 249  ILE G 253                    
SITE     5 GC1 27 GLU G 268  LEU G 269  CYS G 302  GLN G 349                    
SITE     6 GC1 27 GLU G 399  PHE G 401   MG G 607  HOH G 751                    
SITE     7 GC1 27 HOH G1520  HOH G1965  HOH G2225                               
SITE     1 GC2  1 NAD H 508                                                     
SITE     1 GC3  5 THR H  39  VAL H  40  ASP H 109  GLN H 196                    
SITE     2 GC3  5 HOH H1571                                                     
SITE     1 GC4  4 TYR G 468  GLU H 157  PRO H 158  VAL H 159                    
SITE     1 GC5  5 PHE E 151  ASN G 440  SER G 443  TYR H 153                    
SITE     2 GC5  5 ARG H 155                                                     
SITE     1 GC6  3 LYS E 361  TYR H 101  TYR H 203                               
SITE     1 GC7 26 ILE H 165  ILE H 166  PRO H 167  TRP H 168                    
SITE     2 GC7 26 LYS H 192  ALA H 194  GLU H 195  GLN H 196                    
SITE     3 GC7 26 GLY H 225  GLY H 229  ALA H 230  PHE H 243                    
SITE     4 GC7 26 GLY H 245  SER H 246  ILE H 249  ILE H 253                    
SITE     5 GC7 26 GLU H 268  LEU H 269  CYS H 302  GLN H 349                    
SITE     6 GC7 26 LYS H 352  GLU H 399  PHE H 401   MG H 608                    
SITE     7 GC7 26 HOH H1258  HOH H1261                                          
CRYST1  142.216  150.724  177.299  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      0.007032  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006635  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005640        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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