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Database: PDB
Entry: 3N83
LinkDB: 3N83
Original site: 3N83 
HEADER    OXIDOREDUCTASE                          27-MAY-10   3N83              
TITLE     T244A MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE, NAD       
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   4   31-JAN-18 3N83    1       JRNL                                     
REVDAT   3   08-NOV-17 3N83    1       REMARK                                   
REVDAT   2   12-MAR-14 3N83    1       SOURCE VERSN                             
REVDAT   1   13-APR-11 3N83    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.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.06                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 303379                         
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) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 15253                           
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 20941                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1111                         
REMARK   3   BIN FREE R VALUE                    : 0.4040                       
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          : 380                                     
REMARK   3   SOLVENT ATOMS            : 2933                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.88000                                              
REMARK   3    B22 (A**2) : -1.23000                                             
REMARK   3    B33 (A**2) : -0.64000                                             
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): 0.154         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.122         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.261         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 31816 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 43239 ; 1.260 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4028 ; 6.077 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1423 ;35.338 ;24.603       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5120 ;13.147 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   168 ;16.675 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4700 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 24432 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 16445 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 21806 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  3007 ; 0.129 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    17 ; 0.081 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    80 ; 0.180 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    53 ; 0.184 ; 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): 19851 ; 0.496 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31865 ; 0.886 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 12413 ; 1.727 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11363 ; 2.748 ; 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 : 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 3N83 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_1000059498.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUL-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) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-3000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 305300                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
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   (%): 44.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
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       72.56450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.84750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.49650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.84750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       72.56450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.49650            
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: 28030 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 57240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 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: 29060 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 57500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 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: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP C 346   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  20       23.76   -151.13                                   
REMARK 500    ASP A  55     -169.95   -129.55                                   
REMARK 500    VAL A 120      -72.74   -103.08                                   
REMARK 500    THR A 227      -76.28    -95.68                                   
REMARK 500    SER A 260      -97.33   -105.09                                   
REMARK 500    LEU A 269     -157.36   -114.68                                   
REMARK 500    GLU A 312      -39.33    -38.88                                   
REMARK 500    TYR A 379       62.45   -101.27                                   
REMARK 500    LYS A 469     -132.20     51.30                                   
REMARK 500    LEU A 477      166.29     70.86                                   
REMARK 500    ASN B  20       21.81   -153.38                                   
REMARK 500    VAL B 120      -72.57   -105.41                                   
REMARK 500    THR B 227      -74.05   -100.47                                   
REMARK 500    SER B 260      -95.91   -104.38                                   
REMARK 500    LEU B 269     -158.94   -112.22                                   
REMARK 500    GLN B 300       59.43    -91.45                                   
REMARK 500    GLN B 300       57.67    -91.45                                   
REMARK 500    TYR B 379       58.32    -98.36                                   
REMARK 500    LYS B 411      -62.87   -102.25                                   
REMARK 500    LYS B 469     -133.01     55.12                                   
REMARK 500    LEU B 477      164.54     65.56                                   
REMARK 500    ASN C  20       33.31   -145.97                                   
REMARK 500    VAL C 120      -74.42   -103.01                                   
REMARK 500    THR C 227      -83.14   -102.90                                   
REMARK 500    SER C 260     -105.76   -106.94                                   
REMARK 500    LEU C 269     -160.51   -117.52                                   
REMARK 500    LYS C 469     -127.75     53.15                                   
REMARK 500    LEU C 477      161.16     72.99                                   
REMARK 500    GLN C 497      112.63   -160.37                                   
REMARK 500    ASN D  20       27.16   -149.64                                   
REMARK 500    THR D 227      -81.80   -101.74                                   
REMARK 500    SER D 260     -103.17   -104.67                                   
REMARK 500    LEU D 269     -159.98   -116.96                                   
REMARK 500    GLN D 300       59.90    -99.96                                   
REMARK 500    GLN D 300       57.48    -99.96                                   
REMARK 500    LYS D 469     -131.31     55.01                                   
REMARK 500    LEU D 477      167.78     71.95                                   
REMARK 500    ASN E  20       21.79   -149.38                                   
REMARK 500    VAL E 120      -67.27   -108.41                                   
REMARK 500    THR E 227      -75.85   -103.30                                   
REMARK 500    SER E 260     -103.28   -103.86                                   
REMARK 500    LEU E 269     -154.72   -115.57                                   
REMARK 500    TYR E 379       57.76   -101.81                                   
REMARK 500    LYS E 469     -129.05     49.82                                   
REMARK 500    LEU E 477      165.99     69.48                                   
REMARK 500    GLN E 497      108.38   -160.17                                   
REMARK 500    ASN F  20       25.67   -149.90                                   
REMARK 500    VAL F 120      -69.48   -106.10                                   
REMARK 500    THR F 197       59.68   -142.21                                   
REMARK 500    THR F 227      -84.59   -105.12                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      76 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 701  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 196   O                                                      
REMARK 620 2 VAL A  40   O   162.6                                              
REMARK 620 3 ASP A 109   O    98.4  97.8                                        
REMARK 620 4 ASP A 109   OD1  85.0  91.1  80.8                                  
REMARK 620 N                    1     2     3                                   
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 HOH B1336   O                                                      
REMARK 620 2 GLN B 196   O    82.6                                              
REMARK 620 3 ASP B 109   O    88.2 101.3                                        
REMARK 620 4 VAL B  40   O    93.3 159.7  98.3                                  
REMARK 620 5 ASP B 109   OD1 163.5  83.9  85.2 102.6                            
REMARK 620 6 THR B  39   OG1 127.2  69.2 139.4  98.5  55.2                      
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 ASP G 109   O                                                      
REMARK 620 2 GLN G 196   O   107.0                                              
REMARK 620 3 HOH G1840   O    97.7  85.5                                        
REMARK 620 4 VAL G  40   O    98.9 152.8  99.4                                  
REMARK 620 5 ASP G 109   OD1  80.7  81.9 166.3  94.3                            
REMARK 620 6 HOH G2538   O   163.6  74.9  66.0  82.7 115.5                      
REMARK 620 N                    1     2     3     4     5                       
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 C 526   O                                                      
REMARK 620 2 GLN C 196   O    82.4                                              
REMARK 620 3 VAL C  40   O    94.1 161.8                                        
REMARK 620 4 ASP C 109   O    84.1  99.6  97.8                                  
REMARK 620 5 ASP C 109   OD1 164.4  89.2  97.9  84.3                            
REMARK 620 6 THR C  39   OG1 132.6  72.4  97.8 138.4  55.4                      
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 VAL H  40   O                                                      
REMARK 620 2 ASP H 109   O   102.7                                              
REMARK 620 3 ASP H 109   OD1 106.5  83.8                                        
REMARK 620 4 GLN H 196   O   158.9  95.2  86.2                                  
REMARK 620 5 THR H  39   OG1 102.6 139.0  58.3  69.4                            
REMARK 620 N                    1     2     3     4                             
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 VAL D  40   O                                                      
REMARK 620 2 HOH D1571   O    92.1                                              
REMARK 620 3 GLN D 196   O   167.0  89.5                                        
REMARK 620 4 ASP D 109   O    98.9  94.7  93.8                                  
REMARK 620 5 ASP D 109   OD1  94.6 170.6  85.5  77.7                            
REMARK 620 6 HOH D1523   O    87.8  60.9  81.7 155.0 126.0                      
REMARK 620 7 THR D  39   OG1  98.7 129.9  70.6 130.9  55.4  70.9                
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 GLN E 196   O                                                      
REMARK 620 2 HOH E1520   O    81.9                                              
REMARK 620 3 ASP E 109   O    99.0  87.2                                        
REMARK 620 4 VAL E  40   O   159.3  87.9  98.4                                  
REMARK 620 5 ASP E 109   OD1  90.0 165.4  82.2 103.5                            
REMARK 620 6 THR E  39   OG1  71.6 126.8 141.0 101.2  60.6                      
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 VAL F  40   O                                                      
REMARK 620 2 HOH F2178   O    92.5                                              
REMARK 620 3 GLN F 196   O   162.0  80.7                                        
REMARK 620 4 ASP F 109   O   102.0  82.4  93.7                                  
REMARK 620 5 ASP F 109   OD1 104.8 159.4  85.6  83.2                            
REMARK 620 6 THR F  39   OG1 100.5 131.6  72.7 137.9  56.7                      
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 NA A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 911                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 921                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 812                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 912                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 913                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 923                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 963                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 814                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 833                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 944                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 705                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 815                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 915                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 706                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 816                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 826                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 916                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 926                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 946                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 966                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP F 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 707                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 817                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 838                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 917                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 927                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 708                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI H 808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 908                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 928                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP 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: 3N82   RELATED DB: PDB                                   
REMARK 900 T244A MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE, NADH     
REMARK 900 COMPLEX                                                              
DBREF  3N83 A    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N83 B    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N83 C    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N83 D    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N83 E    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N83 F    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N83 G    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3N83 H    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
SEQADV 3N83 ALA A  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N83 ALA B  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N83 ALA C  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N83 ALA D  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N83 ALA E  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N83 ALA F  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N83 ALA G  244  UNP  P05091    THR   261 ENGINEERED MUTATION            
SEQADV 3N83 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     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    ADP  A 501      35                                                       
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    ADP  B 502      35                                                       
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    ADP  C 503      35                                                       
HET     NA  D 704       1                                                       
HET    GAI  D 804       4                                                       
HET    GAI  D 814       4                                                       
HET    GAI  D 833       4                                                       
HET    EDO  D 904       4                                                       
HET    EDO  D 944       4                                                       
HET    ADP  D 504      35                                                       
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    ADP  E 505      35                                                       
HET     NA  F 706       1                                                       
HET    GAI  F 806       4                                                       
HET    GAI  F 816       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    ADP  F 506      35                                                       
HET     NA  G 707       1                                                       
HET    GAI  G 807       4                                                       
HET    GAI  G 817       4                                                       
HET    GAI  G 838       4                                                       
HET    EDO  G 907       4                                                       
HET    EDO  G 917       4                                                       
HET    EDO  G 927       4                                                       
HET    ADP  G 507      35                                                       
HET     NA  H 708       1                                                       
HET    GAI  H 808       4                                                       
HET    EDO  H 908       4                                                       
HET    EDO  H 928       4                                                       
HET    ADP  H 508      35                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     GAI GUANIDINE                                                        
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   9   NA    8(NA 1+)                                                     
FORMUL  10  GAI    16(C H5 N3)                                                  
FORMUL  11  EDO    23(C2 H6 O2)                                                 
FORMUL  14  ADP    8(C10 H15 N5 O10 P2)                                         
FORMUL  64  HOH   *2933(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  SER A  234  1                                   8    
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 GLY A  478  ALA A  484  5                                   7    
HELIX   19  19 ASP B   55  PHE B   70  1                                  16    
HELIX   20  20 SER B   74  MET B   79  1                                   6    
HELIX   21  21 ASP B   80  ASP B   98  1                                  19    
HELIX   22  22 ASP B   98  GLY B  111  1                                  14    
HELIX   23  23 PRO B  113  VAL B  120  1                                   8    
HELIX   24  24 VAL B  120  ALA B  136  1                                  17    
HELIX   25  25 PHE B  170  THR B  185  1                                  16    
HELIX   26  26 PRO B  198  GLY B  212  1                                  15    
HELIX   27  27 THR B  227  SER B  234  1                                   8    
HELIX   28  28 SER B  246  SER B  260  1                                  15    
HELIX   29  29 ASP B  282  PHE B  296  1                                  15    
HELIX   30  30 ASN B  297  GLN B  300  5                                   4    
HELIX   31  31 GLU B  312  SER B  328  1                                  17    
HELIX   32  32 ASP B  346  GLU B  363  1                                  18    
HELIX   33  33 MET B  393  GLU B  398  1                                   6    
HELIX   34  34 THR B  412  ASN B  422  1                                  11    
HELIX   35  35 ASP B  435  LEU B  446  1                                  12    
HELIX   36  36 TYR B  468  MET B  470  5                                   3    
HELIX   37  37 GLY B  478  ALA B  484  5                                   7    
HELIX   38  38 ASP C   55  PHE C   70  1                                  16    
HELIX   39  39 SER C   74  MET C   79  1                                   6    
HELIX   40  40 ASP C   80  ASP C   98  1                                  19    
HELIX   41  41 ASP C   98  GLY C  111  1                                  14    
HELIX   42  42 PRO C  113  VAL C  120  1                                   8    
HELIX   43  43 VAL C  120  ALA C  136  1                                  17    
HELIX   44  44 PHE C  170  THR C  185  1                                  16    
HELIX   45  45 PRO C  198  GLY C  212  1                                  15    
HELIX   46  46 THR C  227  SER C  234  1                                   8    
HELIX   47  47 SER C  246  SER C  260  1                                  15    
HELIX   48  48 ASP C  282  PHE C  296  1                                  15    
HELIX   49  49 ASN C  297  GLN C  300  5                                   4    
HELIX   50  50 GLU C  312  SER C  328  1                                  17    
HELIX   51  51 ASP C  346  GLY C  364  1                                  19    
HELIX   52  52 MET C  393  GLU C  398  1                                   6    
HELIX   53  53 THR C  412  ASN C  422  1                                  11    
HELIX   54  54 ASP C  435  LEU C  446  1                                  12    
HELIX   55  55 GLY C  478  ALA C  484  5                                   7    
HELIX   56  56 ASP D   55  GLN D   71  1                                  17    
HELIX   57  57 SER D   74  MET D   79  1                                   6    
HELIX   58  58 ASP D   80  ASP D   98  1                                  19    
HELIX   59  59 ASP D   98  GLY D  111  1                                  14    
HELIX   60  60 PRO D  113  VAL D  120  1                                   8    
HELIX   61  61 VAL D  120  ALA D  136  1                                  17    
HELIX   62  62 PHE D  170  THR D  185  1                                  16    
HELIX   63  63 PRO D  198  GLY D  212  1                                  15    
HELIX   64  64 THR D  227  SER D  234  1                                   8    
HELIX   65  65 SER D  246  SER D  260  1                                  15    
HELIX   66  66 ASP D  282  PHE D  296  1                                  15    
HELIX   67  67 ASN D  297  GLN D  300  5                                   4    
HELIX   68  68 ILE D  314  ARG D  329  1                                  16    
HELIX   69  69 ASP D  346  GLU D  363  1                                  18    
HELIX   70  70 MET D  393  GLU D  398  1                                   6    
HELIX   71  71 THR D  412  ASN D  422  1                                  11    
HELIX   72  72 ASP D  435  LEU D  446  1                                  12    
HELIX   73  73 TYR D  468  MET D  470  5                                   3    
HELIX   74  74 GLU D  479  ALA D  484  5                                   6    
HELIX   75  75 ASP E   55  PHE E   70  1                                  16    
HELIX   76  76 SER E   74  MET E   79  1                                   6    
HELIX   77  77 ASP E   80  ASP E   98  1                                  19    
HELIX   78  78 ASP E   98  GLY E  111  1                                  14    
HELIX   79  79 PRO E  113  VAL E  120  1                                   8    
HELIX   80  80 VAL E  120  ALA E  136  1                                  17    
HELIX   81  81 PHE E  170  THR E  185  1                                  16    
HELIX   82  82 PRO E  198  GLY E  212  1                                  15    
HELIX   83  83 THR E  227  SER E  234  1                                   8    
HELIX   84  84 SER E  246  SER E  260  1                                  15    
HELIX   85  85 ASP E  282  PHE E  296  1                                  15    
HELIX   86  86 ASN E  297  GLN E  300  5                                   4    
HELIX   87  87 ILE E  314  SER E  328  1                                  15    
HELIX   88  88 ASP E  346  GLU E  363  1                                  18    
HELIX   89  89 MET E  393  GLU E  398  1                                   6    
HELIX   90  90 THR E  412  ASN E  422  1                                  11    
HELIX   91  91 ASP E  435  LEU E  446  1                                  12    
HELIX   92  92 TYR E  468  MET E  470  5                                   3    
HELIX   93  93 GLY E  478  ALA E  484  5                                   7    
HELIX   94  94 ASP F   55  PHE F   70  1                                  16    
HELIX   95  95 SER F   74  MET F   79  1                                   6    
HELIX   96  96 ASP F   80  ASP F   98  1                                  19    
HELIX   97  97 ASP F   98  GLY F  111  1                                  14    
HELIX   98  98 PRO F  113  VAL F  120  1                                   8    
HELIX   99  99 VAL F  120  ALA F  136  1                                  17    
HELIX  100 100 PHE F  170  THR F  185  1                                  16    
HELIX  101 101 PRO F  198  GLY F  212  1                                  15    
HELIX  102 102 THR F  227  SER F  234  1                                   8    
HELIX  103 103 SER F  246  SER F  260  1                                  15    
HELIX  104 104 ASP F  282  PHE F  296  1                                  15    
HELIX  105 105 ASN F  297  GLN F  300  5                                   4    
HELIX  106 106 GLU F  312  ARG F  329  1                                  18    
HELIX  107 107 ASP F  346  GLU F  363  1                                  18    
HELIX  108 108 MET F  393  GLU F  398  1                                   6    
HELIX  109 109 THR F  412  ASN F  422  1                                  11    
HELIX  110 110 ASP F  435  LEU F  446  1                                  12    
HELIX  111 111 TYR F  468  MET F  470  5                                   3    
HELIX  112 112 GLY F  478  ALA F  484  5                                   7    
HELIX  113 113 ASP G   55  PHE G   70  1                                  16    
HELIX  114 114 SER G   74  MET G   79  1                                   6    
HELIX  115 115 ASP G   80  ASP G   98  1                                  19    
HELIX  116 116 ASP G   98  GLY G  111  1                                  14    
HELIX  117 117 PRO G  113  VAL G  120  1                                   8    
HELIX  118 118 VAL G  120  ALA G  136  1                                  17    
HELIX  119 119 PHE G  170  THR G  185  1                                  16    
HELIX  120 120 PRO G  198  GLY G  212  1                                  15    
HELIX  121 121 THR G  227  SER G  234  1                                   8    
HELIX  122 122 SER G  246  SER G  260  1                                  15    
HELIX  123 123 ASP G  282  PHE G  296  1                                  15    
HELIX  124 124 ASN G  297  GLN G  300  5                                   4    
HELIX  125 125 ILE G  314  ARG G  329  1                                  16    
HELIX  126 126 ASP G  346  GLU G  363  1                                  18    
HELIX  127 127 MET G  393  GLU G  398  1                                   6    
HELIX  128 128 THR G  412  ASN G  422  1                                  11    
HELIX  129 129 ASP G  435  LEU G  446  1                                  12    
HELIX  130 130 TYR G  468  MET G  470  5                                   3    
HELIX  131 131 GLY G  478  ALA G  484  5                                   7    
HELIX  132 132 ASP H   55  PHE H   70  1                                  16    
HELIX  133 133 SER H   74  MET H   79  1                                   6    
HELIX  134 134 ASP H   80  ASP H   98  1                                  19    
HELIX  135 135 ASP H   98  GLY H  111  1                                  14    
HELIX  136 136 PRO H  113  VAL H  120  1                                   8    
HELIX  137 137 VAL H  120  ALA H  136  1                                  17    
HELIX  138 138 PHE H  170  THR H  185  1                                  16    
HELIX  139 139 PRO H  198  GLY H  212  1                                  15    
HELIX  140 140 THR H  227  SER H  234  1                                   8    
HELIX  141 141 SER H  246  SER H  260  1                                  15    
HELIX  142 142 ASP H  282  PHE H  296  1                                  15    
HELIX  143 143 ASN H  297  GLN H  300  5                                   4    
HELIX  144 144 GLU H  312  SER H  328  1                                  17    
HELIX  145 145 ASP H  346  GLU H  363  1                                  18    
HELIX  146 146 MET H  393  GLU H  398  1                                   6    
HELIX  147 147 THR H  412  ASN H  422  1                                  11    
HELIX  148 148 ASP H  435  LEU H  446  1                                  12    
HELIX  149 149 TYR H  468  MET H  470  5                                   3    
HELIX  150 150 GLY H  478  ALA H  484  5                                   7    
SHEET    1   A 2 ILE A  22  ILE A  24  0                                        
SHEET    2   A 2 GLU A  27  HIS A  29 -1  O  HIS A  29   N  ILE A  22           
SHEET    1   B 2 THR A  36  VAL A  40  0                                        
SHEET    2   B 2 VAL A  47  ALA A  52 -1  O  ILE A  48   N  THR A  39           
SHEET    1   C20 LYS B 366  CYS B 369  0                                        
SHEET    2   C20 THR B 384  GLY B 387 -1  O  GLY B 387   N  LYS B 366           
SHEET    3   C20 VAL B 404  PHE B 410  1  O  MET B 405   N  PHE B 386           
SHEET    4   C20 ARG B 307  GLN B 311  1  N  VAL B 310   O  LEU B 408           
SHEET    5   C20 PRO B 274  ILE B 277  1  N  ILE B 277   O  PHE B 309           
SHEET    6   C20 ALA B 428  PHE B 432  1  O  ALA B 430   N  ILE B 276           
SHEET    7   C20 THR B 450  VAL B 453  1  O  TRP B 452   N  ALA B 429           
SHEET    8   C20 THR A 486  LYS A 494  1  N  THR A 490   O  VAL B 451           
SHEET    9   C20 PHE A 150  PRO A 158 -1  N  TYR A 153   O  VAL A 491           
SHEET   10   C20 GLY A 141  ILE A 144 -1  N  ILE A 144   O  SER A 152           
SHEET   11   C20 GLY D 141  ILE D 144 -1  O  THR D 143   N  GLY A 141           
SHEET   12   C20 PHE D 150  PRO D 158 -1  O  SER D 152   N  ILE D 144           
SHEET   13   C20 THR D 486  LYS D 494 -1  O  GLU D 487   N  GLU D 157           
SHEET   14   C20 THR C 450  VAL C 453  1  N  VAL C 451   O  THR D 490           
SHEET   15   C20 ALA C 428  PHE C 432  1  N  ALA C 429   O  TRP C 452           
SHEET   16   C20 PRO C 274  ILE C 277  1  N  ILE C 276   O  ALA C 430           
SHEET   17   C20 ARG C 307  GLN C 311  1  O  PHE C 309   N  ILE C 277           
SHEET   18   C20 VAL C 404  PHE C 410  1  O  LEU C 408   N  THR C 308           
SHEET   19   C20 THR C 384  GLY C 387  1  N  PHE C 386   O  MET C 405           
SHEET   20   C20 LYS C 366  CYS C 369 -1  N  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  CYS A 162   O  VAL A 188           
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  ALA A 430   N  ILE A 276           
SHEET    7   E20 THR A 450  VAL A 453  1  O  TRP A 452   N  ALA A 429           
SHEET    8   E20 THR B 486  LYS B 494  1  O  THR B 490   N  VAL A 451           
SHEET    9   E20 PHE B 150  PRO B 158 -1  N  TYR B 153   O  VAL B 491           
SHEET   10   E20 GLY B 141  ILE B 144 -1  N  ILE B 144   O  SER B 152           
SHEET   11   E20 GLY C 141  ILE C 144 -1  O  GLY C 141   N  THR B 143           
SHEET   12   E20 PHE C 150  PRO C 158 -1  O  SER C 152   N  ILE C 144           
SHEET   13   E20 THR C 486  LYS C 494 -1  O  VAL C 493   N  PHE C 151           
SHEET   14   E20 THR D 450  VAL D 453  1  O  VAL D 453   N  THR C 492           
SHEET   15   E20 ALA D 428  PHE D 432  1  N  ALA D 429   O  TRP D 452           
SHEET   16   E20 SER D 273  ILE D 277  1  N  ILE D 276   O  PHE D 432           
SHEET   17   E20 GLY D 305  GLN D 311  1  O  PHE D 309   N  ILE D 277           
SHEET   18   E20 VAL D 404  PHE D 410  1  O  LEU D 408   N  VAL D 310           
SHEET   19   E20 THR D 384  GLY D 387  1  N  THR D 384   O  MET D 405           
SHEET   20   E20 LYS D 366  CYS D 369 -1  N  LYS D 366   O  GLY D 387           
SHEET    1   F 2 TYR A 425  GLY A 426  0                                        
SHEET    2   F 2 TYR A 468  LYS A 469 -1  O  TYR A 468   N  GLY A 426           
SHEET    1   G 2 ILE B  22  ILE B  24  0                                        
SHEET    2   G 2 GLU B  27  HIS B  29 -1  O  HIS B  29   N  ILE B  22           
SHEET    1   H 2 THR B  36  VAL B  40  0                                        
SHEET    2   H 2 VAL B  47  ALA B  52 -1  O  ILE B  48   N  THR B  39           
SHEET    1   I 6 VAL B 218  ILE B 220  0                                        
SHEET    2   I 6 VAL B 188  LYS B 192  1  N  MET B 191   O  ASN B 219           
SHEET    3   I 6 VAL B 161  ILE B 165  1  N  GLN B 164   O  LYS B 192           
SHEET    4   I 6 LYS B 240  ALA B 244  1  O  LYS B 240   N  GLY B 163           
SHEET    5   I 6 ARG B 264  GLU B 268  1  O  ARG B 264   N  VAL B 241           
SHEET    6   I 6 GLY B 472  SER B 473 -1  O  SER B 473   N  LEU B 267           
SHEET    1   J 2 ILE C  22  ILE C  24  0                                        
SHEET    2   J 2 GLU C  27  HIS C  29 -1  O  HIS C  29   N  ILE C  22           
SHEET    1   K 2 THR C  36  VAL C  40  0                                        
SHEET    2   K 2 VAL C  47  ALA C  52 -1  O  ILE C  48   N  THR C  39           
SHEET    1   L 6 VAL C 218  ILE C 220  0                                        
SHEET    2   L 6 VAL C 188  LYS C 192  1  N  MET C 191   O  ASN C 219           
SHEET    3   L 6 VAL C 161  ILE C 165  1  N  CYS C 162   O  VAL C 188           
SHEET    4   L 6 LYS C 240  ALA C 244  1  O  LYS C 240   N  GLY C 163           
SHEET    5   L 6 ARG C 264  GLU C 268  1  O  ARG C 264   N  VAL C 241           
SHEET    6   L 6 GLY C 472  SER C 473 -1  O  SER C 473   N  LEU C 267           
SHEET    1   M 2 TYR C 425  GLY C 426  0                                        
SHEET    2   M 2 TYR C 468  LYS C 469 -1  O  TYR C 468   N  GLY C 426           
SHEET    1   N 2 ILE D  22  ILE D  24  0                                        
SHEET    2   N 2 GLU D  27  HIS D  29 -1  O  HIS D  29   N  ILE D  22           
SHEET    1   O 2 THR D  36  VAL D  40  0                                        
SHEET    2   O 2 VAL D  47  ALA D  52 -1  O  ILE D  48   N  THR D  39           
SHEET    1   P 6 VAL D 218  ILE D 220  0                                        
SHEET    2   P 6 VAL D 188  LYS D 192  1  N  MET D 191   O  ASN D 219           
SHEET    3   P 6 VAL D 161  ILE D 165  1  N  CYS D 162   O  VAL D 188           
SHEET    4   P 6 LYS D 240  ALA D 244  1  O  LYS D 240   N  GLY D 163           
SHEET    5   P 6 ARG D 264  GLU D 268  1  O  ARG D 264   N  VAL D 241           
SHEET    6   P 6 GLY D 472  SER D 473 -1  O  SER D 473   N  LEU D 267           
SHEET    1   Q 2 ILE E  22  ILE E  24  0                                        
SHEET    2   Q 2 GLU E  27  HIS E  29 -1  O  HIS E  29   N  ILE E  22           
SHEET    1   R 2 THR E  36  VAL E  40  0                                        
SHEET    2   R 2 VAL E  47  ALA E  52 -1  O  ILE E  48   N  THR E  39           
SHEET    1   S20 LYS F 366  CYS F 369  0                                        
SHEET    2   S20 THR F 384  GLY F 387 -1  O  VAL F 385   N  LEU F 368           
SHEET    3   S20 VAL F 404  PHE F 410  1  O  MET F 405   N  PHE F 386           
SHEET    4   S20 ARG F 307  GLN F 311  1  N  VAL F 310   O  LEU F 408           
SHEET    5   S20 PRO F 274  ILE F 277  1  N  ILE F 277   O  PHE F 309           
SHEET    6   S20 ALA F 428  PHE F 432  1  O  ALA F 430   N  ILE F 276           
SHEET    7   S20 THR F 450  VAL F 453  1  O  TRP F 452   N  ALA F 429           
SHEET    8   S20 THR E 486  LYS E 494  1  N  THR E 490   O  VAL F 451           
SHEET    9   S20 PHE E 150  PRO E 158 -1  N  TYR E 153   O  VAL E 491           
SHEET   10   S20 GLY E 141  ILE E 144 -1  N  ILE E 144   O  SER E 152           
SHEET   11   S20 GLY H 141  ILE H 144 -1  O  THR H 143   N  GLY E 141           
SHEET   12   S20 PHE H 150  PRO H 158 -1  O  SER H 152   N  ILE H 144           
SHEET   13   S20 THR H 486  LYS H 494 -1  O  VAL H 491   N  TYR H 153           
SHEET   14   S20 THR G 450  VAL G 453  1  N  VAL G 451   O  THR H 490           
SHEET   15   S20 ALA G 428  PHE G 432  1  N  VAL G 431   O  TRP G 452           
SHEET   16   S20 PRO G 274  ILE G 277  1  N  ILE G 276   O  PHE G 432           
SHEET   17   S20 ARG G 307  GLN G 311  1  O  PHE G 309   N  ILE G 277           
SHEET   18   S20 VAL G 404  PHE G 410  1  O  LEU G 408   N  VAL G 310           
SHEET   19   S20 THR G 384  GLY G 387  1  N  THR G 384   O  MET G 405           
SHEET   20   S20 LYS G 366  CYS G 369 -1  N  LEU G 368   O  VAL G 385           
SHEET    1   T 6 VAL E 218  ILE E 220  0                                        
SHEET    2   T 6 VAL E 188  LYS E 192  1  N  MET E 191   O  ASN E 219           
SHEET    3   T 6 VAL E 161  ILE E 165  1  N  CYS E 162   O  VAL E 188           
SHEET    4   T 6 LYS E 240  ALA E 244  1  O  LYS E 240   N  GLY E 163           
SHEET    5   T 6 ARG E 264  GLU E 268  1  O  ARG E 264   N  VAL E 241           
SHEET    6   T 6 GLY E 472  SER E 473 -1  O  SER E 473   N  LEU E 267           
SHEET    1   U20 LYS E 366  CYS E 369  0                                        
SHEET    2   U20 THR E 384  GLY E 387 -1  O  GLY E 387   N  LYS E 366           
SHEET    3   U20 VAL E 404  PHE E 410  1  O  MET E 405   N  THR E 384           
SHEET    4   U20 ARG E 307  GLN E 311  1  N  THR E 308   O  LEU E 408           
SHEET    5   U20 PRO E 274  ILE E 277  1  N  ILE E 277   O  PHE E 309           
SHEET    6   U20 ALA E 428  PHE E 432  1  O  ALA E 430   N  ILE E 276           
SHEET    7   U20 THR E 450  VAL E 453  1  O  TRP E 452   N  VAL E 431           
SHEET    8   U20 THR F 486  LYS F 494  1  O  THR F 490   N  VAL E 451           
SHEET    9   U20 PHE F 150  PRO F 158 -1  N  PHE F 151   O  VAL F 493           
SHEET   10   U20 GLY F 141  ILE F 144 -1  N  ILE F 144   O  SER F 152           
SHEET   11   U20 GLY G 141  ILE G 144 -1  O  THR G 143   N  GLY F 141           
SHEET   12   U20 PHE G 150  PRO G 158 -1  O  SER G 152   N  ILE G 144           
SHEET   13   U20 THR G 486  LYS G 494 -1  O  VAL G 491   N  TYR G 153           
SHEET   14   U20 THR H 450  VAL H 453  1  O  VAL H 453   N  THR G 492           
SHEET   15   U20 ALA H 428  PHE H 432  1  N  ALA H 429   O  TRP H 452           
SHEET   16   U20 PRO H 274  ILE H 277  1  N  ILE H 276   O  ALA H 430           
SHEET   17   U20 ARG H 307  GLN H 311  1  O  PHE H 309   N  ILE H 277           
SHEET   18   U20 VAL H 404  PHE H 410  1  O  LEU H 408   N  THR H 308           
SHEET   19   U20 THR H 384  GLY H 387  1  N  PHE H 386   O  MET H 405           
SHEET   20   U20 LYS H 366  CYS H 369 -1  N  LEU H 368   O  VAL H 385           
SHEET    1   V 2 ILE F  22  ILE F  24  0                                        
SHEET    2   V 2 GLU F  27  HIS F  29 -1  O  HIS F  29   N  ILE F  22           
SHEET    1   W 2 THR F  36  VAL F  40  0                                        
SHEET    2   W 2 VAL F  47  ALA F  52 -1  O  ILE F  48   N  THR F  39           
SHEET    1   X 6 VAL F 218  ILE F 220  0                                        
SHEET    2   X 6 VAL F 188  LYS F 192  1  N  MET F 191   O  ASN F 219           
SHEET    3   X 6 VAL F 161  ILE F 165  1  N  CYS F 162   O  VAL F 188           
SHEET    4   X 6 LYS F 240  ALA F 244  1  O  LYS F 240   N  GLY F 163           
SHEET    5   X 6 ARG F 264  GLU F 268  1  O  ARG F 264   N  VAL F 241           
SHEET    6   X 6 GLY F 472  SER F 473 -1  O  SER F 473   N  LEU F 267           
SHEET    1   Y 2 ILE G  22  ILE G  24  0                                        
SHEET    2   Y 2 GLU G  27  HIS G  29 -1  O  HIS G  29   N  ILE G  22           
SHEET    1   Z 2 THR G  36  VAL G  40  0                                        
SHEET    2   Z 2 VAL G  47  ALA G  52 -1  O  ILE G  48   N  THR G  39           
SHEET    1  AA 6 VAL G 218  ILE G 220  0                                        
SHEET    2  AA 6 VAL G 188  LYS G 192  1  N  MET G 191   O  ASN G 219           
SHEET    3  AA 6 VAL G 161  ILE G 165  1  N  GLN G 164   O  LYS G 192           
SHEET    4  AA 6 LYS G 240  ALA G 244  1  O  LYS G 240   N  GLY G 163           
SHEET    5  AA 6 ARG G 264  GLU G 268  1  O  ARG G 264   N  VAL G 241           
SHEET    6  AA 6 GLY G 472  SER G 473 -1  O  SER G 473   N  LEU G 267           
SHEET    1  AB 2 ILE H  22  ILE H  24  0                                        
SHEET    2  AB 2 GLU H  27  HIS H  29 -1  O  HIS H  29   N  ILE H  22           
SHEET    1  AC 2 THR H  36  VAL H  40  0                                        
SHEET    2  AC 2 VAL H  47  ALA H  52 -1  O  ILE H  48   N  THR H  39           
SHEET    1  AD 6 VAL H 218  ILE H 220  0                                        
SHEET    2  AD 6 VAL H 188  LYS H 192  1  N  MET H 191   O  ASN H 219           
SHEET    3  AD 6 VAL H 161  ILE H 165  1  N  CYS H 162   O  VAL H 190           
SHEET    4  AD 6 LYS H 240  ALA H 244  1  O  LYS H 240   N  GLY H 163           
SHEET    5  AD 6 ARG H 264  GLU H 268  1  O  ARG H 264   N  VAL H 241           
SHEET    6  AD 6 GLY H 472  SER H 473 -1  O  SER H 473   N  LEU H 267           
LINK         O   GLN A 196                NA    NA A 701     1555   1555  2.22  
LINK        NA    NA B 702                 O   HOH B1336     1555   1555  2.29  
LINK         O   ASP G 109                NA    NA G 707     1555   1555  2.30  
LINK        NA    NA C 703                 O   HOH C 526     1555   1555  2.30  
LINK         O   VAL H  40                NA    NA H 708     1555   1555  2.32  
LINK         O   GLN G 196                NA    NA G 707     1555   1555  2.34  
LINK        NA    NA G 707                 O   HOH G1840     1555   1555  2.34  
LINK         O   GLN B 196                NA    NA B 702     1555   1555  2.35  
LINK         O   VAL D  40                NA    NA D 704     1555   1555  2.35  
LINK         O   GLN E 196                NA    NA E 705     1555   1555  2.35  
LINK        NA    NA D 704                 O   HOH D1571     1555   1555  2.36  
LINK         O   VAL F  40                NA    NA F 706     1555   1555  2.36  
LINK         O   GLN D 196                NA    NA D 704     1555   1555  2.37  
LINK         O   GLN C 196                NA    NA C 703     1555   1555  2.38  
LINK         O   ASP H 109                NA    NA H 708     1555   1555  2.38  
LINK        NA    NA E 705                 O   HOH E1520     1555   1555  2.40  
LINK        NA    NA F 706                 O   HOH F2178     1555   1555  2.41  
LINK         O   ASP B 109                NA    NA B 702     1555   1555  2.42  
LINK         O   VAL B  40                NA    NA B 702     1555   1555  2.44  
LINK         O   VAL A  40                NA    NA A 701     1555   1555  2.44  
LINK         O   ASP E 109                NA    NA E 705     1555   1555  2.44  
LINK         O   VAL G  40                NA    NA G 707     1555   1555  2.44  
LINK         O   GLN F 196                NA    NA F 706     1555   1555  2.44  
LINK         OD1 ASP H 109                NA    NA H 708     1555   1555  2.45  
LINK         O   VAL C  40                NA    NA C 703     1555   1555  2.45  
LINK         O   VAL E  40                NA    NA E 705     1555   1555  2.46  
LINK         OD1 ASP E 109                NA    NA E 705     1555   1555  2.47  
LINK         O   ASP F 109                NA    NA F 706     1555   1555  2.48  
LINK         O   ASP A 109                NA    NA A 701     1555   1555  2.48  
LINK         O   ASP D 109                NA    NA D 704     1555   1555  2.51  
LINK         OD1 ASP B 109                NA    NA B 702     1555   1555  2.52  
LINK         O   GLN H 196                NA    NA H 708     1555   1555  2.54  
LINK         OD1 ASP F 109                NA    NA F 706     1555   1555  2.54  
LINK         O   ASP C 109                NA    NA C 703     1555   1555  2.57  
LINK         OD1 ASP G 109                NA    NA G 707     1555   1555  2.66  
LINK         OD1 ASP D 109                NA    NA D 704     1555   1555  2.66  
LINK         OD1 ASP C 109                NA    NA C 703     1555   1555  2.68  
LINK         OD1 ASP A 109                NA    NA A 701     1555   1555  2.82  
LINK         OG1 THR F  39                NA    NA F 706     1555   1555  2.99  
LINK         OG1 THR C  39                NA    NA C 703     1555   1555  3.10  
LINK         OG1 THR E  39                NA    NA E 705     1555   1555  3.10  
LINK         OG1 THR H  39                NA    NA H 708     1555   1555  3.10  
LINK        NA    NA D 704                 O   HOH D1523     1555   1555  3.11  
LINK        NA    NA G 707                 O   HOH G2538     1555   1555  3.15  
LINK         OG1 THR D  39                NA    NA D 704     1555   1555  3.15  
LINK         OG1 THR B  39                NA    NA B 702     1555   1555  3.18  
SITE     1 AC1  4 THR A  39  VAL A  40  ASP A 109  GLN A 196                    
SITE     1 AC2  7 PHE A  70  GLU A 157  PRO A 158  VAL A 159                    
SITE     2 AC2  7 HOH A 991  HOH A1322  TYR B 468                               
SITE     1 AC3  5 TYR A 153  ARG A 155  HOH A2135  SER B 443                    
SITE     2 AC3  5 PHE D 151                                                     
SITE     1 AC4  6 GLN A  14  ASN A  41  THR A  44  GLU A  46                    
SITE     2 AC4  6 ILE A  48  LEU A 108                                          
SITE     1 AC5  4 PHE A  18  TYR A 101  TYR A 203  HOH A1400                    
SITE     1 AC6 16 ILE A 165  ILE A 166  PRO A 167  TRP A 168                    
SITE     2 AC6 16 LYS A 192  ALA A 194  GLU A 195  GLY A 225                    
SITE     3 AC6 16 GLY A 229  ALA A 230  PHE A 243  ALA A 244                    
SITE     4 AC6 16 GLY A 245  SER A 246  ILE A 249  ILE A 253                    
SITE     1 AC7  5 THR B  39  VAL B  40  ASP B 109  GLN B 196                    
SITE     2 AC7  5 HOH B1336                                                     
SITE     1 AC8  4 TYR A 468  GLU B 157  PRO B 158  VAL B 159                    
SITE     1 AC9  7 PHE A 459  HOH A 956  HOH A1058  ILE B 146                    
SITE     2 AC9  7 ASP B 147  PHE B 150  HOH B2548                               
SITE     1 BC1  4 SER A 443  TYR B 153  ARG B 155  PHE C 151                    
SITE     1 BC2  3 GLN B  14  ASN B  41  THR B  44                               
SITE     1 BC3 16 ILE B 165  ILE B 166  PRO B 167  TRP B 168                    
SITE     2 BC3 16 LYS B 192  GLU B 195  GLY B 225  GLY B 229                    
SITE     3 BC3 16 ALA B 230  PHE B 243  ALA B 244  GLY B 245                    
SITE     4 BC3 16 SER B 246  ILE B 249  ILE B 253  HOH B2638                    
SITE     1 BC4  5 THR C  39  VAL C  40  ASP C 109  GLN C 196                    
SITE     2 BC4  5 HOH C 526                                                     
SITE     1 BC5  6 PHE C  70  GLU C 157  PRO C 158  VAL C 159                    
SITE     2 BC5  6 HOH C 610  TYR D 468                                          
SITE     1 BC6  4 PHE B 151  TYR C 153  ARG C 155  SER D 443                    
SITE     1 BC7  4 GLN C  14  ASN C  41  THR C  44  GLU C  46                    
SITE     1 BC8  4 PHE C  18  TYR C 101  TYR C 203  HOH C1692                    
SITE     1 BC9  4 GLU C 347  PHE C 350  GLY F  45  VAL F  47                    
SITE     1 CC1 21 ILE C 165  ILE C 166  PRO C 167  TRP C 168                    
SITE     2 CC1 21 LYS C 192  ALA C 194  GLU C 195  GLN C 196                    
SITE     3 CC1 21 GLY C 225  GLY C 229  ALA C 230  PHE C 243                    
SITE     4 CC1 21 ALA C 244  GLY C 245  SER C 246  ILE C 249                    
SITE     5 CC1 21 ILE C 253  GLN C 349  HOH C 543  HOH C1399                    
SITE     6 CC1 21 HOH C2287                                                     
SITE     1 CC2  5 THR D  39  VAL D  40  ASP D 109  GLN D 196                    
SITE     2 CC2  5 HOH D1571                                                     
SITE     1 CC3  4 TYR C 468  GLU D 157  PRO D 158  VAL D 159                    
SITE     1 CC4  5 PHE C 459  ILE D 146  ASP D 147  PHE D 150                    
SITE     2 CC4  5 HOH D1444                                                     
SITE     1 CC5  6 ALA D 326  LYS D 327  ARG D 329  VAL D 331                    
SITE     2 CC5  6 PRO D 383  HOH D1753                                          
SITE     1 CC6  5 PHE A 151  SER C 443  TYR D 153  ARG D 155                    
SITE     2 CC6  5 HOH D2262                                                     
SITE     1 CC7  4 GLU D 414  TYR D 441  HOH D1236  LYS G 361                    
SITE     1 CC8 18 ILE D 165  ILE D 166  PRO D 167  TRP D 168                    
SITE     2 CC8 18 LYS D 192  ALA D 194  GLY D 225  GLY D 229                    
SITE     3 CC8 18 ALA D 230  PHE D 243  ALA D 244  GLY D 245                    
SITE     4 CC8 18 SER D 246  ILE D 249  ILE D 253  HOH D1357                    
SITE     5 CC8 18 HOH D1698  HOH D2234                                          
SITE     1 CC9  5 THR E  39  VAL E  40  ASP E 109  GLN E 196                    
SITE     2 CC9  5 HOH E1520                                                     
SITE     1 DC1  6 PHE E  70  GLU E 157  PRO E 158  VAL E 159                    
SITE     2 DC1  6 HOH E 978  TYR F 468                                          
SITE     1 DC2  6 ILE E 146  ASP E 147  PHE E 150  HOH E1524                    
SITE     2 DC2  6 VAL F 458  PHE F 459                                          
SITE     1 DC3  5 TYR E 153  ARG E 155  HOH E2688  SER F 443                    
SITE     2 DC3  5 PHE H 151                                                     
SITE     1 DC4  3 ASN E  41  THR E  44  VAL E  47                               
SITE     1 DC5 21 ILE E 165  ILE E 166  PRO E 167  TRP E 168                    
SITE     2 DC5 21 LYS E 192  ALA E 194  GLU E 195  GLN E 196                    
SITE     3 DC5 21 GLY E 225  GLY E 229  ALA E 230  PHE E 243                    
SITE     4 DC5 21 ALA E 244  GLY E 245  SER E 246  ILE E 249                    
SITE     5 DC5 21 ILE E 253  HOH E 777  HOH E 849  HOH E1771                    
SITE     6 DC5 21 HOH E2183                                                     
SITE     1 DC6  5 THR F  39  VAL F  40  ASP F 109  GLN F 196                    
SITE     2 DC6  5 HOH F2178                                                     
SITE     1 DC7  5 TYR E 468  GLU F 157  PRO F 158  VAL F 159                    
SITE     2 DC7  5 HOH F 521                                                     
SITE     1 DC8  6 PHE E 459  ILE F 146  ASP F 147  PHE F 150                    
SITE     2 DC8  6 HOH F2283  HOH F2585                                          
SITE     1 DC9  6 PHE F 350  ALA F 375  ASP F 376  GLY F 378                    
SITE     2 DC9  6 EDO F 966  HOH F1775                                          
SITE     1 EC1  4 SER E 443  TYR F 153  ARG F 155  PHE G 151                    
SITE     1 EC2  6 ASN F  41  THR F  44  GLU F  46  LEU F 108                    
SITE     2 EC2  6 HOH F 942  HOH F1529                                          
SITE     1 EC3  5 ARG E 321  PHE F  18  TYR F 101  TYR F 203                    
SITE     2 EC3  5 HOH F2455                                                     
SITE     1 EC4  7 LEU E  72  TYR F 441  GLN F 444  ALA F 445                    
SITE     2 EC4  7 HOH F 703  HOH F1385  GLN H 497                               
SITE     1 EC5  3 GLY C  45  GLU F 347  GAI F 826                               
SITE     1 EC6 19 ILE F 165  ILE F 166  PRO F 167  TRP F 168                    
SITE     2 EC6 19 LYS F 192  ALA F 194  GLU F 195  GLY F 225                    
SITE     3 EC6 19 GLY F 229  ALA F 230  PHE F 243  ALA F 244                    
SITE     4 EC6 19 GLY F 245  SER F 246  ILE F 249  ILE F 253                    
SITE     5 EC6 19 HOH F 624  HOH F1263  HOH F2220                               
SITE     1 EC7  5 THR G  39  VAL G  40  ASP G 109  GLN G 196                    
SITE     2 EC7  5 HOH G1840                                                     
SITE     1 EC8  6 GLU G 157  PRO G 158  VAL G 159  HOH G1429                    
SITE     2 EC8  6 HOH G2513  TYR H 468                                          
SITE     1 EC9  5 ASP G 147  PHE G 150  HOH G2529  VAL H 458                    
SITE     2 EC9  5 PHE H 459                                                     
SITE     1 FC1  6 ALA G 326  LYS G 327  ARG G 329  VAL G 331                    
SITE     2 FC1  6 PRO G 383  HOH G1323                                          
SITE     1 FC2  4 PHE F 151  TYR G 153  ARG G 155  SER H 443                    
SITE     1 FC3  4 ASN G  41  THR G  44  GLU G  46  HOH G2835                    
SITE     1 FC4  4 PHE G  18  TYR G 101  TYR G 203  HOH G1376                    
SITE     1 FC5 21 ILE G 165  ILE G 166  PRO G 167  TRP G 168                    
SITE     2 FC5 21 LYS G 192  ALA G 194  GLU G 195  GLN G 196                    
SITE     3 FC5 21 GLY G 225  GLY G 229  ALA G 230  PHE G 243                    
SITE     4 FC5 21 ALA G 244  GLY G 245  SER G 246  ILE G 249                    
SITE     5 FC5 21 ILE G 253  HOH G1281  HOH G1338  HOH G1973                    
SITE     6 FC5 21 HOH G2740                                                     
SITE     1 FC6  4 THR H  39  VAL H  40  ASP H 109  GLN H 196                    
SITE     1 FC7  6 TYR G 468  GLU H 157  PRO H 158  VAL H 159                    
SITE     2 FC7  6 HOH H2112  HOH H2242                                          
SITE     1 FC8  4 PHE E 151  SER G 443  TYR H 153  ARG H 155                    
SITE     1 FC9  2 TYR H 101  TYR H 203                                          
SITE     1 GC1 20 ILE H 165  ILE H 166  PRO H 167  TRP H 168                    
SITE     2 GC1 20 LYS H 192  GLU H 195  GLN H 196  GLY H 225                    
SITE     3 GC1 20 GLY H 229  ALA H 230  PHE H 243  ALA H 244                    
SITE     4 GC1 20 GLY H 245  SER H 246  ILE H 249  ILE H 253                    
SITE     5 GC1 20 HOH H1289  HOH H1482  HOH H2245  HOH H2279                    
CRYST1  145.129  150.993  177.695  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      0.006890  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006623  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005628        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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