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Database: PDB
Entry: 4PZD
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Original site: 4PZD 
HEADER    OXIDOREDUCTASE                          29-MAR-14   4PZD              
TITLE     CRYSTAL STRUCTURE OF (S)-3-HYDROXYBUTYRYL-COA DEHYDROGENASE PAAH1 IN  
TITLE    2 COMPLEX WITH NAD+                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3-HYDROXYACYL-COA DEHYDROGENASE;                           
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I;                                    
COMPND   4 EC: 1.1.1.35;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RALSTONIA EUTROPHA H16;                         
SOURCE   3 ORGANISM_TAXID: 381666;                                              
SOURCE   4 STRAIN: ATCC 17699 / H16 / DSM 428 / STANIER 337;                    
SOURCE   5 GENE: PAAH1, H16_A0282;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ROSSMANN FOLD, OXIDOREDUCTASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.KIM,J.H.CHANG,K.J.KIM                                               
REVDAT   2   18-FEB-15 4PZD    1                                                
REVDAT   1   11-FEB-15 4PZD    0                                                
JRNL        AUTH   J.KIM,J.H.CHANG,K.J.KIM                                      
JRNL        TITL   CRYSTAL STRUCTURE AND BIOCHEMICAL PROPERTIES OF THE          
JRNL        TITL 2 (S)-3-HYDROXYBUTYRYL-COA DEHYDROGENASE PAAH1 FROM RALSTONIA  
JRNL        TITL 3 EUTROPHA                                                     
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 448   163 2014              
JRNL        REFN                   ISSN 0006-291X                               
JRNL        PMID   24792376                                                     
JRNL        DOI    10.1016/J.BBRC.2014.04.101                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 86885                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4557                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.61                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.68                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6195                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 313                          
REMARK   3   BIN FREE R VALUE                    : 0.3450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18918                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 396                                     
REMARK   3   SOLVENT ATOMS            : 101                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.76000                                              
REMARK   3    B22 (A**2) : 3.56000                                              
REMARK   3    B33 (A**2) : -7.32000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.06000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.770         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.339         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.254         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.043        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.904                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 19584 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 19521 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 26568 ; 1.686 ; 2.012       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 44955 ; 0.846 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2538 ; 6.779 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   657 ;41.016 ;24.658       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3465 ;18.682 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    99 ;16.622 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3240 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 21600 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  3906 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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): 10179 ; 4.704 ; 6.585       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 10178 ; 4.704 ; 6.584       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12708 ; 6.908 ; 9.862       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 12709 ; 6.908 ; 9.862       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  9405 ; 5.090 ; 7.169       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  9406 ; 5.089 ; 7.169       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 13861 ; 7.674 ;10.585       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 22235 ;10.792 ;53.151       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 22236 ;10.792 ;53.152       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4PZD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-APR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085409.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-SEP-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 7A (6B, 6C1)                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 91442                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
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     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M (NH4)2SO4, 0.1M CACODYLATE PH 6.5,    
REMARK 280  0.2M SODIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  295K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      117.53800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.79300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      117.53800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       67.79300            
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, 3, 4, 5                                           
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.15307            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -97.44488            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, G                                  
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: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I                                  
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     MET A     1                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET D     1                                                      
REMARK 465     MET E     1                                                      
REMARK 465     MET F     1                                                      
REMARK 465     MET G     1                                                      
REMARK 465     MET H     1                                                      
REMARK 465     MET I     1                                                      
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 A 253   CB  -  CG  -  OD1 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    THR B  75   CB  -  CA  -  C   ANGL. DEV. =  24.2 DEGREES          
REMARK 500    ARG D 191   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP D 253   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    SER F 184   CB  -  CA  -  C   ANGL. DEV. =  14.9 DEGREES          
REMARK 500    ARG F 191   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG F 191   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG G 191   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP G 253   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    PHE H 187   N   -  CA  -  C   ANGL. DEV. = -16.4 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    ALA A  89       39.64   -162.55                                   
REMARK 500    GLU A 110      -33.94    -39.04                                   
REMARK 500    THR A 118      143.09   -173.45                                   
REMARK 500    SER A 122      109.99    -52.81                                   
REMARK 500    ALA A 149       34.69    -97.75                                   
REMARK 500    LEU A 174       -4.82    -50.75                                   
REMARK 500    PHE A 187     -115.46     40.55                                   
REMARK 500    ALA B  11       22.99   -151.30                                   
REMARK 500    SER B  35     -160.65   -103.30                                   
REMARK 500    LYS B  56        0.53    -62.28                                   
REMARK 500    GLU B  57        8.48     80.27                                   
REMARK 500    SER B  74     -164.74   -176.78                                   
REMARK 500    THR B  75      -52.08   -133.70                                   
REMARK 500    LEU B  80      -34.77    -32.22                                   
REMARK 500    LYS B  81       -0.33    -55.29                                   
REMARK 500    ALA B  89       29.82   -160.03                                   
REMARK 500    GLU B  92       72.50   -101.35                                   
REMARK 500    SER B 120       74.69   -158.74                                   
REMARK 500    THR B 159      124.30    -38.72                                   
REMARK 500    SER B 184      144.29   -170.86                                   
REMARK 500    PHE B 187     -112.14     47.98                                   
REMARK 500    ALA B 209      164.97    177.63                                   
REMARK 500    ALA C  82       37.72    -89.83                                   
REMARK 500    ALA C  89       49.15   -147.66                                   
REMARK 500    SER C 120      -24.94   -174.84                                   
REMARK 500    ASN C 143      111.24    -25.01                                   
REMARK 500    PHE C 187     -118.85     52.21                                   
REMARK 500    PRO C 254       -8.54    -58.76                                   
REMARK 500    LYS C 274      -10.70    -34.86                                   
REMARK 500    ARG C 277      134.87   -170.34                                   
REMARK 500    TYR C 282     -165.96   -126.43                                   
REMARK 500    THR D  60     -114.42   -146.83                                   
REMARK 500    THR D  75       -0.09   -140.11                                   
REMARK 500    ALA D  82        1.48    -66.59                                   
REMARK 500    ALA D  89       37.28   -153.86                                   
REMARK 500    THR D 118      146.91   -171.06                                   
REMARK 500    SER D 120      -34.86   -134.53                                   
REMARK 500    ALA D 149       43.50    -93.71                                   
REMARK 500    PHE D 187     -129.67     43.33                                   
REMARK 500    SER D 283      -75.28    -59.94                                   
REMARK 500    ALA E  11       22.18   -156.16                                   
REMARK 500    SER E  35     -158.97   -112.03                                   
REMARK 500    GLU E  57        7.43     84.99                                   
REMARK 500    SER E  74     -173.75   -178.98                                   
REMARK 500    THR E  75       11.73   -154.85                                   
REMARK 500    ALA E  89       24.25   -154.12                                   
REMARK 500    SER E 120       47.30   -161.25                                   
REMARK 500    ASP E 134       -6.75    -57.95                                   
REMARK 500    SER E 184      146.20   -171.15                                   
REMARK 500    PHE E 187     -118.55     50.97                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      85 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE A  142     ASN A  143                 -132.55                    
REMARK 500 THR B   75     SER B   76                 -145.49                    
REMARK 500 PHE D  142     ASN D  143                 -131.70                    
REMARK 500 PHE G  142     ASN G  143                 -141.17                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG C 191         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ILE A 192        24.6      L          L   OUTSIDE RANGE           
REMARK 500    THR B  75        19.1      L          L   OUTSIDE RANGE           
REMARK 500    ILE G 192        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD E 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD F 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD G 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD H 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD I 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4PZC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PZE   RELATED DB: PDB                                   
DBREF  4PZD A    1   284  UNP    Q0KEY8   Q0KEY8_CUPNH     1    284             
DBREF  4PZD B    1   284  UNP    Q0KEY8   Q0KEY8_CUPNH     1    284             
DBREF  4PZD C    1   284  UNP    Q0KEY8   Q0KEY8_CUPNH     1    284             
DBREF  4PZD D    1   284  UNP    Q0KEY8   Q0KEY8_CUPNH     1    284             
DBREF  4PZD E    1   284  UNP    Q0KEY8   Q0KEY8_CUPNH     1    284             
DBREF  4PZD F    1   284  UNP    Q0KEY8   Q0KEY8_CUPNH     1    284             
DBREF  4PZD G    1   284  UNP    Q0KEY8   Q0KEY8_CUPNH     1    284             
DBREF  4PZD H    1   284  UNP    Q0KEY8   Q0KEY8_CUPNH     1    284             
DBREF  4PZD I    1   284  UNP    Q0KEY8   Q0KEY8_CUPNH     1    284             
SEQRES   1 A  284  MET SER ILE ARG THR VAL GLY ILE VAL GLY ALA GLY THR          
SEQRES   2 A  284  MET GLY ASN GLY ILE ALA GLN ALA CYS ALA VAL VAL GLY          
SEQRES   3 A  284  LEU ASN VAL VAL MET VAL ASP ILE SER ASP ALA ALA VAL          
SEQRES   4 A  284  GLN LYS GLY VAL ALA THR VAL ALA SER SER LEU ASP ARG          
SEQRES   5 A  284  LEU ILE LYS LYS GLU LYS LEU THR GLU ALA ASP LYS ALA          
SEQRES   6 A  284  SER ALA LEU ALA ARG ILE LYS GLY SER THR SER TYR ASP          
SEQRES   7 A  284  ASP LEU LYS ALA THR ASP ILE VAL ILE GLU ALA ALA THR          
SEQRES   8 A  284  GLU ASN TYR ASP LEU LYS VAL LYS ILE LEU LYS GLN ILE          
SEQRES   9 A  284  ASP GLY ILE VAL GLY GLU ASN VAL ILE ILE ALA SER ASN          
SEQRES  10 A  284  THR SER SER ILE SER ILE THR LYS LEU ALA ALA VAL THR          
SEQRES  11 A  284  SER ARG ALA ASP ARG PHE ILE GLY MET HIS PHE PHE ASN          
SEQRES  12 A  284  PRO VAL PRO VAL MET ALA LEU VAL GLU LEU ILE ARG GLY          
SEQRES  13 A  284  LEU GLN THR SER ASP THR THR HIS ALA ALA VAL GLU ALA          
SEQRES  14 A  284  LEU SER LYS GLN LEU GLY LYS TYR PRO ILE THR VAL LYS          
SEQRES  15 A  284  ASN SER PRO GLY PHE VAL VAL ASN ARG ILE LEU CYS PRO          
SEQRES  16 A  284  MET ILE ASN GLU ALA PHE CYS VAL LEU GLY GLU GLY LEU          
SEQRES  17 A  284  ALA SER PRO GLU GLU ILE ASP GLU GLY MET LYS LEU GLY          
SEQRES  18 A  284  CYS ASN HIS PRO ILE GLY PRO LEU ALA LEU ALA ASP MET          
SEQRES  19 A  284  ILE GLY LEU ASP THR MET LEU ALA VAL MET GLU VAL LEU          
SEQRES  20 A  284  TYR THR GLU PHE ALA ASP PRO LYS TYR ARG PRO ALA MET          
SEQRES  21 A  284  LEU MET ARG GLU MET VAL ALA ALA GLY TYR LEU GLY ARG          
SEQRES  22 A  284  LYS THR GLY ARG GLY VAL TYR VAL TYR SER LYS                  
SEQRES   1 B  284  MET SER ILE ARG THR VAL GLY ILE VAL GLY ALA GLY THR          
SEQRES   2 B  284  MET GLY ASN GLY ILE ALA GLN ALA CYS ALA VAL VAL GLY          
SEQRES   3 B  284  LEU ASN VAL VAL MET VAL ASP ILE SER ASP ALA ALA VAL          
SEQRES   4 B  284  GLN LYS GLY VAL ALA THR VAL ALA SER SER LEU ASP ARG          
SEQRES   5 B  284  LEU ILE LYS LYS GLU LYS LEU THR GLU ALA ASP LYS ALA          
SEQRES   6 B  284  SER ALA LEU ALA ARG ILE LYS GLY SER THR SER TYR ASP          
SEQRES   7 B  284  ASP LEU LYS ALA THR ASP ILE VAL ILE GLU ALA ALA THR          
SEQRES   8 B  284  GLU ASN TYR ASP LEU LYS VAL LYS ILE LEU LYS GLN ILE          
SEQRES   9 B  284  ASP GLY ILE VAL GLY GLU ASN VAL ILE ILE ALA SER ASN          
SEQRES  10 B  284  THR SER SER ILE SER ILE THR LYS LEU ALA ALA VAL THR          
SEQRES  11 B  284  SER ARG ALA ASP ARG PHE ILE GLY MET HIS PHE PHE ASN          
SEQRES  12 B  284  PRO VAL PRO VAL MET ALA LEU VAL GLU LEU ILE ARG GLY          
SEQRES  13 B  284  LEU GLN THR SER ASP THR THR HIS ALA ALA VAL GLU ALA          
SEQRES  14 B  284  LEU SER LYS GLN LEU GLY LYS TYR PRO ILE THR VAL LYS          
SEQRES  15 B  284  ASN SER PRO GLY PHE VAL VAL ASN ARG ILE LEU CYS PRO          
SEQRES  16 B  284  MET ILE ASN GLU ALA PHE CYS VAL LEU GLY GLU GLY LEU          
SEQRES  17 B  284  ALA SER PRO GLU GLU ILE ASP GLU GLY MET LYS LEU GLY          
SEQRES  18 B  284  CYS ASN HIS PRO ILE GLY PRO LEU ALA LEU ALA ASP MET          
SEQRES  19 B  284  ILE GLY LEU ASP THR MET LEU ALA VAL MET GLU VAL LEU          
SEQRES  20 B  284  TYR THR GLU PHE ALA ASP PRO LYS TYR ARG PRO ALA MET          
SEQRES  21 B  284  LEU MET ARG GLU MET VAL ALA ALA GLY TYR LEU GLY ARG          
SEQRES  22 B  284  LYS THR GLY ARG GLY VAL TYR VAL TYR SER LYS                  
SEQRES   1 C  284  MET SER ILE ARG THR VAL GLY ILE VAL GLY ALA GLY THR          
SEQRES   2 C  284  MET GLY ASN GLY ILE ALA GLN ALA CYS ALA VAL VAL GLY          
SEQRES   3 C  284  LEU ASN VAL VAL MET VAL ASP ILE SER ASP ALA ALA VAL          
SEQRES   4 C  284  GLN LYS GLY VAL ALA THR VAL ALA SER SER LEU ASP ARG          
SEQRES   5 C  284  LEU ILE LYS LYS GLU LYS LEU THR GLU ALA ASP LYS ALA          
SEQRES   6 C  284  SER ALA LEU ALA ARG ILE LYS GLY SER THR SER TYR ASP          
SEQRES   7 C  284  ASP LEU LYS ALA THR ASP ILE VAL ILE GLU ALA ALA THR          
SEQRES   8 C  284  GLU ASN TYR ASP LEU LYS VAL LYS ILE LEU LYS GLN ILE          
SEQRES   9 C  284  ASP GLY ILE VAL GLY GLU ASN VAL ILE ILE ALA SER ASN          
SEQRES  10 C  284  THR SER SER ILE SER ILE THR LYS LEU ALA ALA VAL THR          
SEQRES  11 C  284  SER ARG ALA ASP ARG PHE ILE GLY MET HIS PHE PHE ASN          
SEQRES  12 C  284  PRO VAL PRO VAL MET ALA LEU VAL GLU LEU ILE ARG GLY          
SEQRES  13 C  284  LEU GLN THR SER ASP THR THR HIS ALA ALA VAL GLU ALA          
SEQRES  14 C  284  LEU SER LYS GLN LEU GLY LYS TYR PRO ILE THR VAL LYS          
SEQRES  15 C  284  ASN SER PRO GLY PHE VAL VAL ASN ARG ILE LEU CYS PRO          
SEQRES  16 C  284  MET ILE ASN GLU ALA PHE CYS VAL LEU GLY GLU GLY LEU          
SEQRES  17 C  284  ALA SER PRO GLU GLU ILE ASP GLU GLY MET LYS LEU GLY          
SEQRES  18 C  284  CYS ASN HIS PRO ILE GLY PRO LEU ALA LEU ALA ASP MET          
SEQRES  19 C  284  ILE GLY LEU ASP THR MET LEU ALA VAL MET GLU VAL LEU          
SEQRES  20 C  284  TYR THR GLU PHE ALA ASP PRO LYS TYR ARG PRO ALA MET          
SEQRES  21 C  284  LEU MET ARG GLU MET VAL ALA ALA GLY TYR LEU GLY ARG          
SEQRES  22 C  284  LYS THR GLY ARG GLY VAL TYR VAL TYR SER LYS                  
SEQRES   1 D  284  MET SER ILE ARG THR VAL GLY ILE VAL GLY ALA GLY THR          
SEQRES   2 D  284  MET GLY ASN GLY ILE ALA GLN ALA CYS ALA VAL VAL GLY          
SEQRES   3 D  284  LEU ASN VAL VAL MET VAL ASP ILE SER ASP ALA ALA VAL          
SEQRES   4 D  284  GLN LYS GLY VAL ALA THR VAL ALA SER SER LEU ASP ARG          
SEQRES   5 D  284  LEU ILE LYS LYS GLU LYS LEU THR GLU ALA ASP LYS ALA          
SEQRES   6 D  284  SER ALA LEU ALA ARG ILE LYS GLY SER THR SER TYR ASP          
SEQRES   7 D  284  ASP LEU LYS ALA THR ASP ILE VAL ILE GLU ALA ALA THR          
SEQRES   8 D  284  GLU ASN TYR ASP LEU LYS VAL LYS ILE LEU LYS GLN ILE          
SEQRES   9 D  284  ASP GLY ILE VAL GLY GLU ASN VAL ILE ILE ALA SER ASN          
SEQRES  10 D  284  THR SER SER ILE SER ILE THR LYS LEU ALA ALA VAL THR          
SEQRES  11 D  284  SER ARG ALA ASP ARG PHE ILE GLY MET HIS PHE PHE ASN          
SEQRES  12 D  284  PRO VAL PRO VAL MET ALA LEU VAL GLU LEU ILE ARG GLY          
SEQRES  13 D  284  LEU GLN THR SER ASP THR THR HIS ALA ALA VAL GLU ALA          
SEQRES  14 D  284  LEU SER LYS GLN LEU GLY LYS TYR PRO ILE THR VAL LYS          
SEQRES  15 D  284  ASN SER PRO GLY PHE VAL VAL ASN ARG ILE LEU CYS PRO          
SEQRES  16 D  284  MET ILE ASN GLU ALA PHE CYS VAL LEU GLY GLU GLY LEU          
SEQRES  17 D  284  ALA SER PRO GLU GLU ILE ASP GLU GLY MET LYS LEU GLY          
SEQRES  18 D  284  CYS ASN HIS PRO ILE GLY PRO LEU ALA LEU ALA ASP MET          
SEQRES  19 D  284  ILE GLY LEU ASP THR MET LEU ALA VAL MET GLU VAL LEU          
SEQRES  20 D  284  TYR THR GLU PHE ALA ASP PRO LYS TYR ARG PRO ALA MET          
SEQRES  21 D  284  LEU MET ARG GLU MET VAL ALA ALA GLY TYR LEU GLY ARG          
SEQRES  22 D  284  LYS THR GLY ARG GLY VAL TYR VAL TYR SER LYS                  
SEQRES   1 E  284  MET SER ILE ARG THR VAL GLY ILE VAL GLY ALA GLY THR          
SEQRES   2 E  284  MET GLY ASN GLY ILE ALA GLN ALA CYS ALA VAL VAL GLY          
SEQRES   3 E  284  LEU ASN VAL VAL MET VAL ASP ILE SER ASP ALA ALA VAL          
SEQRES   4 E  284  GLN LYS GLY VAL ALA THR VAL ALA SER SER LEU ASP ARG          
SEQRES   5 E  284  LEU ILE LYS LYS GLU LYS LEU THR GLU ALA ASP LYS ALA          
SEQRES   6 E  284  SER ALA LEU ALA ARG ILE LYS GLY SER THR SER TYR ASP          
SEQRES   7 E  284  ASP LEU LYS ALA THR ASP ILE VAL ILE GLU ALA ALA THR          
SEQRES   8 E  284  GLU ASN TYR ASP LEU LYS VAL LYS ILE LEU LYS GLN ILE          
SEQRES   9 E  284  ASP GLY ILE VAL GLY GLU ASN VAL ILE ILE ALA SER ASN          
SEQRES  10 E  284  THR SER SER ILE SER ILE THR LYS LEU ALA ALA VAL THR          
SEQRES  11 E  284  SER ARG ALA ASP ARG PHE ILE GLY MET HIS PHE PHE ASN          
SEQRES  12 E  284  PRO VAL PRO VAL MET ALA LEU VAL GLU LEU ILE ARG GLY          
SEQRES  13 E  284  LEU GLN THR SER ASP THR THR HIS ALA ALA VAL GLU ALA          
SEQRES  14 E  284  LEU SER LYS GLN LEU GLY LYS TYR PRO ILE THR VAL LYS          
SEQRES  15 E  284  ASN SER PRO GLY PHE VAL VAL ASN ARG ILE LEU CYS PRO          
SEQRES  16 E  284  MET ILE ASN GLU ALA PHE CYS VAL LEU GLY GLU GLY LEU          
SEQRES  17 E  284  ALA SER PRO GLU GLU ILE ASP GLU GLY MET LYS LEU GLY          
SEQRES  18 E  284  CYS ASN HIS PRO ILE GLY PRO LEU ALA LEU ALA ASP MET          
SEQRES  19 E  284  ILE GLY LEU ASP THR MET LEU ALA VAL MET GLU VAL LEU          
SEQRES  20 E  284  TYR THR GLU PHE ALA ASP PRO LYS TYR ARG PRO ALA MET          
SEQRES  21 E  284  LEU MET ARG GLU MET VAL ALA ALA GLY TYR LEU GLY ARG          
SEQRES  22 E  284  LYS THR GLY ARG GLY VAL TYR VAL TYR SER LYS                  
SEQRES   1 F  284  MET SER ILE ARG THR VAL GLY ILE VAL GLY ALA GLY THR          
SEQRES   2 F  284  MET GLY ASN GLY ILE ALA GLN ALA CYS ALA VAL VAL GLY          
SEQRES   3 F  284  LEU ASN VAL VAL MET VAL ASP ILE SER ASP ALA ALA VAL          
SEQRES   4 F  284  GLN LYS GLY VAL ALA THR VAL ALA SER SER LEU ASP ARG          
SEQRES   5 F  284  LEU ILE LYS LYS GLU LYS LEU THR GLU ALA ASP LYS ALA          
SEQRES   6 F  284  SER ALA LEU ALA ARG ILE LYS GLY SER THR SER TYR ASP          
SEQRES   7 F  284  ASP LEU LYS ALA THR ASP ILE VAL ILE GLU ALA ALA THR          
SEQRES   8 F  284  GLU ASN TYR ASP LEU LYS VAL LYS ILE LEU LYS GLN ILE          
SEQRES   9 F  284  ASP GLY ILE VAL GLY GLU ASN VAL ILE ILE ALA SER ASN          
SEQRES  10 F  284  THR SER SER ILE SER ILE THR LYS LEU ALA ALA VAL THR          
SEQRES  11 F  284  SER ARG ALA ASP ARG PHE ILE GLY MET HIS PHE PHE ASN          
SEQRES  12 F  284  PRO VAL PRO VAL MET ALA LEU VAL GLU LEU ILE ARG GLY          
SEQRES  13 F  284  LEU GLN THR SER ASP THR THR HIS ALA ALA VAL GLU ALA          
SEQRES  14 F  284  LEU SER LYS GLN LEU GLY LYS TYR PRO ILE THR VAL LYS          
SEQRES  15 F  284  ASN SER PRO GLY PHE VAL VAL ASN ARG ILE LEU CYS PRO          
SEQRES  16 F  284  MET ILE ASN GLU ALA PHE CYS VAL LEU GLY GLU GLY LEU          
SEQRES  17 F  284  ALA SER PRO GLU GLU ILE ASP GLU GLY MET LYS LEU GLY          
SEQRES  18 F  284  CYS ASN HIS PRO ILE GLY PRO LEU ALA LEU ALA ASP MET          
SEQRES  19 F  284  ILE GLY LEU ASP THR MET LEU ALA VAL MET GLU VAL LEU          
SEQRES  20 F  284  TYR THR GLU PHE ALA ASP PRO LYS TYR ARG PRO ALA MET          
SEQRES  21 F  284  LEU MET ARG GLU MET VAL ALA ALA GLY TYR LEU GLY ARG          
SEQRES  22 F  284  LYS THR GLY ARG GLY VAL TYR VAL TYR SER LYS                  
SEQRES   1 G  284  MET SER ILE ARG THR VAL GLY ILE VAL GLY ALA GLY THR          
SEQRES   2 G  284  MET GLY ASN GLY ILE ALA GLN ALA CYS ALA VAL VAL GLY          
SEQRES   3 G  284  LEU ASN VAL VAL MET VAL ASP ILE SER ASP ALA ALA VAL          
SEQRES   4 G  284  GLN LYS GLY VAL ALA THR VAL ALA SER SER LEU ASP ARG          
SEQRES   5 G  284  LEU ILE LYS LYS GLU LYS LEU THR GLU ALA ASP LYS ALA          
SEQRES   6 G  284  SER ALA LEU ALA ARG ILE LYS GLY SER THR SER TYR ASP          
SEQRES   7 G  284  ASP LEU LYS ALA THR ASP ILE VAL ILE GLU ALA ALA THR          
SEQRES   8 G  284  GLU ASN TYR ASP LEU LYS VAL LYS ILE LEU LYS GLN ILE          
SEQRES   9 G  284  ASP GLY ILE VAL GLY GLU ASN VAL ILE ILE ALA SER ASN          
SEQRES  10 G  284  THR SER SER ILE SER ILE THR LYS LEU ALA ALA VAL THR          
SEQRES  11 G  284  SER ARG ALA ASP ARG PHE ILE GLY MET HIS PHE PHE ASN          
SEQRES  12 G  284  PRO VAL PRO VAL MET ALA LEU VAL GLU LEU ILE ARG GLY          
SEQRES  13 G  284  LEU GLN THR SER ASP THR THR HIS ALA ALA VAL GLU ALA          
SEQRES  14 G  284  LEU SER LYS GLN LEU GLY LYS TYR PRO ILE THR VAL LYS          
SEQRES  15 G  284  ASN SER PRO GLY PHE VAL VAL ASN ARG ILE LEU CYS PRO          
SEQRES  16 G  284  MET ILE ASN GLU ALA PHE CYS VAL LEU GLY GLU GLY LEU          
SEQRES  17 G  284  ALA SER PRO GLU GLU ILE ASP GLU GLY MET LYS LEU GLY          
SEQRES  18 G  284  CYS ASN HIS PRO ILE GLY PRO LEU ALA LEU ALA ASP MET          
SEQRES  19 G  284  ILE GLY LEU ASP THR MET LEU ALA VAL MET GLU VAL LEU          
SEQRES  20 G  284  TYR THR GLU PHE ALA ASP PRO LYS TYR ARG PRO ALA MET          
SEQRES  21 G  284  LEU MET ARG GLU MET VAL ALA ALA GLY TYR LEU GLY ARG          
SEQRES  22 G  284  LYS THR GLY ARG GLY VAL TYR VAL TYR SER LYS                  
SEQRES   1 H  284  MET SER ILE ARG THR VAL GLY ILE VAL GLY ALA GLY THR          
SEQRES   2 H  284  MET GLY ASN GLY ILE ALA GLN ALA CYS ALA VAL VAL GLY          
SEQRES   3 H  284  LEU ASN VAL VAL MET VAL ASP ILE SER ASP ALA ALA VAL          
SEQRES   4 H  284  GLN LYS GLY VAL ALA THR VAL ALA SER SER LEU ASP ARG          
SEQRES   5 H  284  LEU ILE LYS LYS GLU LYS LEU THR GLU ALA ASP LYS ALA          
SEQRES   6 H  284  SER ALA LEU ALA ARG ILE LYS GLY SER THR SER TYR ASP          
SEQRES   7 H  284  ASP LEU LYS ALA THR ASP ILE VAL ILE GLU ALA ALA THR          
SEQRES   8 H  284  GLU ASN TYR ASP LEU LYS VAL LYS ILE LEU LYS GLN ILE          
SEQRES   9 H  284  ASP GLY ILE VAL GLY GLU ASN VAL ILE ILE ALA SER ASN          
SEQRES  10 H  284  THR SER SER ILE SER ILE THR LYS LEU ALA ALA VAL THR          
SEQRES  11 H  284  SER ARG ALA ASP ARG PHE ILE GLY MET HIS PHE PHE ASN          
SEQRES  12 H  284  PRO VAL PRO VAL MET ALA LEU VAL GLU LEU ILE ARG GLY          
SEQRES  13 H  284  LEU GLN THR SER ASP THR THR HIS ALA ALA VAL GLU ALA          
SEQRES  14 H  284  LEU SER LYS GLN LEU GLY LYS TYR PRO ILE THR VAL LYS          
SEQRES  15 H  284  ASN SER PRO GLY PHE VAL VAL ASN ARG ILE LEU CYS PRO          
SEQRES  16 H  284  MET ILE ASN GLU ALA PHE CYS VAL LEU GLY GLU GLY LEU          
SEQRES  17 H  284  ALA SER PRO GLU GLU ILE ASP GLU GLY MET LYS LEU GLY          
SEQRES  18 H  284  CYS ASN HIS PRO ILE GLY PRO LEU ALA LEU ALA ASP MET          
SEQRES  19 H  284  ILE GLY LEU ASP THR MET LEU ALA VAL MET GLU VAL LEU          
SEQRES  20 H  284  TYR THR GLU PHE ALA ASP PRO LYS TYR ARG PRO ALA MET          
SEQRES  21 H  284  LEU MET ARG GLU MET VAL ALA ALA GLY TYR LEU GLY ARG          
SEQRES  22 H  284  LYS THR GLY ARG GLY VAL TYR VAL TYR SER LYS                  
SEQRES   1 I  284  MET SER ILE ARG THR VAL GLY ILE VAL GLY ALA GLY THR          
SEQRES   2 I  284  MET GLY ASN GLY ILE ALA GLN ALA CYS ALA VAL VAL GLY          
SEQRES   3 I  284  LEU ASN VAL VAL MET VAL ASP ILE SER ASP ALA ALA VAL          
SEQRES   4 I  284  GLN LYS GLY VAL ALA THR VAL ALA SER SER LEU ASP ARG          
SEQRES   5 I  284  LEU ILE LYS LYS GLU LYS LEU THR GLU ALA ASP LYS ALA          
SEQRES   6 I  284  SER ALA LEU ALA ARG ILE LYS GLY SER THR SER TYR ASP          
SEQRES   7 I  284  ASP LEU LYS ALA THR ASP ILE VAL ILE GLU ALA ALA THR          
SEQRES   8 I  284  GLU ASN TYR ASP LEU LYS VAL LYS ILE LEU LYS GLN ILE          
SEQRES   9 I  284  ASP GLY ILE VAL GLY GLU ASN VAL ILE ILE ALA SER ASN          
SEQRES  10 I  284  THR SER SER ILE SER ILE THR LYS LEU ALA ALA VAL THR          
SEQRES  11 I  284  SER ARG ALA ASP ARG PHE ILE GLY MET HIS PHE PHE ASN          
SEQRES  12 I  284  PRO VAL PRO VAL MET ALA LEU VAL GLU LEU ILE ARG GLY          
SEQRES  13 I  284  LEU GLN THR SER ASP THR THR HIS ALA ALA VAL GLU ALA          
SEQRES  14 I  284  LEU SER LYS GLN LEU GLY LYS TYR PRO ILE THR VAL LYS          
SEQRES  15 I  284  ASN SER PRO GLY PHE VAL VAL ASN ARG ILE LEU CYS PRO          
SEQRES  16 I  284  MET ILE ASN GLU ALA PHE CYS VAL LEU GLY GLU GLY LEU          
SEQRES  17 I  284  ALA SER PRO GLU GLU ILE ASP GLU GLY MET LYS LEU GLY          
SEQRES  18 I  284  CYS ASN HIS PRO ILE GLY PRO LEU ALA LEU ALA ASP MET          
SEQRES  19 I  284  ILE GLY LEU ASP THR MET LEU ALA VAL MET GLU VAL LEU          
SEQRES  20 I  284  TYR THR GLU PHE ALA ASP PRO LYS TYR ARG PRO ALA MET          
SEQRES  21 I  284  LEU MET ARG GLU MET VAL ALA ALA GLY TYR LEU GLY ARG          
SEQRES  22 I  284  LYS THR GLY ARG GLY VAL TYR VAL TYR SER LYS                  
HET    NAD  A 301      44                                                       
HET    NAD  B 301      44                                                       
HET    NAD  C 301      44                                                       
HET    NAD  D 301      44                                                       
HET    NAD  E 301      44                                                       
HET    NAD  F 301      44                                                       
HET    NAD  G 301      44                                                       
HET    NAD  H 301      44                                                       
HET    NAD  I 301      44                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL  10  NAD    9(C21 H27 N7 O14 P2)                                         
FORMUL  19  HOH   *101(H2 O)                                                    
HELIX    1   1 GLY A   12  VAL A   24  1                                  13    
HELIX    2   2 ASP A   36  LYS A   55  1                                  20    
HELIX    3   3 THR A   60  ARG A   70  1                                  11    
HELIX    4   4 TYR A   77  ALA A   82  5                                   6    
HELIX    5   5 ASN A   93  VAL A  108  1                                  16    
HELIX    6   6 SER A  122  ALA A  128  1                                   7    
HELIX    7   7 ARG A  132  ASP A  134  5                                   3    
HELIX    8   8 SER A  160  LEU A  174  1                                  15    
HELIX    9   9 VAL A  188  GLU A  206  1                                  19    
HELIX   10  10 SER A  210  ASN A  223  1                                  14    
HELIX   11  11 GLY A  227  GLY A  236  1                                  10    
HELIX   12  12 GLY A  236  ALA A  252  1                                  17    
HELIX   13  13 ASP A  253  ARG A  257  5                                   5    
HELIX   14  14 ALA A  259  GLY A  269  1                                  11    
HELIX   15  15 GLY B   12  VAL B   24  1                                  13    
HELIX   16  16 ASP B   36  LYS B   56  1                                  21    
HELIX   17  17 THR B   60  ILE B   71  1                                  12    
HELIX   18  18 ASP B   78  THR B   83  5                                   6    
HELIX   19  19 ASN B   93  VAL B  108  1                                  16    
HELIX   20  20 SER B  122  ALA B  128  1                                   7    
HELIX   21  21 ARG B  132  ASP B  134  5                                   3    
HELIX   22  22 SER B  160  LEU B  174  1                                  15    
HELIX   23  23 VAL B  188  GLU B  206  1                                  19    
HELIX   24  24 SER B  210  ASN B  223  1                                  14    
HELIX   25  25 GLY B  227  GLY B  236  1                                  10    
HELIX   26  26 GLY B  236  ALA B  252  1                                  17    
HELIX   27  27 ASP B  253  ARG B  257  5                                   5    
HELIX   28  28 ALA B  259  ALA B  268  1                                  10    
HELIX   29  29 GLY B  272  GLY B  276  5                                   5    
HELIX   30  30 GLY C   12  VAL C   24  1                                  13    
HELIX   31  31 SER C   35  LYS C   56  1                                  22    
HELIX   32  32 THR C   60  ALA C   69  1                                  10    
HELIX   33  33 SER C   76  THR C   83  5                                   8    
HELIX   34  34 ASN C   93  VAL C  108  1                                  16    
HELIX   35  35 SER C  122  VAL C  129  1                                   8    
HELIX   36  36 ARG C  132  ASP C  134  5                                   3    
HELIX   37  37 SER C  160  LEU C  174  1                                  15    
HELIX   38  38 VAL C  188  GLU C  206  1                                  19    
HELIX   39  39 SER C  210  ASN C  223  1                                  14    
HELIX   40  40 GLY C  227  GLY C  236  1                                  10    
HELIX   41  41 GLY C  236  ALA C  252  1                                  17    
HELIX   42  42 ASP C  253  ARG C  257  5                                   5    
HELIX   43  43 ALA C  259  ALA C  268  1                                  10    
HELIX   44  44 GLY C  272  GLY C  276  5                                   5    
HELIX   45  45 GLY D   12  VAL D   24  1                                  13    
HELIX   46  46 ASP D   36  LYS D   55  1                                  20    
HELIX   47  47 GLU D   61  ILE D   71  1                                  11    
HELIX   48  48 SER D   76  ALA D   82  5                                   7    
HELIX   49  49 ASN D   93  VAL D  108  1                                  16    
HELIX   50  50 SER D  122  ALA D  128  1                                   7    
HELIX   51  51 ARG D  132  ASP D  134  5                                   3    
HELIX   52  52 SER D  160  LEU D  174  1                                  15    
HELIX   53  53 VAL D  188  GLU D  206  1                                  19    
HELIX   54  54 SER D  210  ASN D  223  1                                  14    
HELIX   55  55 GLY D  227  GLY D  236  1                                  10    
HELIX   56  56 GLY D  236  ALA D  252  1                                  17    
HELIX   57  57 ASP D  253  ARG D  257  5                                   5    
HELIX   58  58 ALA D  259  GLY D  269  1                                  11    
HELIX   59  59 GLY D  272  GLY D  276  5                                   5    
HELIX   60  60 MET E   14  VAL E   25  1                                  12    
HELIX   61  61 ASP E   36  LYS E   56  1                                  21    
HELIX   62  62 THR E   60  ILE E   71  1                                  12    
HELIX   63  63 ASP E   78  THR E   83  5                                   6    
HELIX   64  64 ASN E   93  VAL E  108  1                                  16    
HELIX   65  65 SER E  122  ALA E  128  1                                   7    
HELIX   66  66 ARG E  132  ASP E  134  5                                   3    
HELIX   67  67 SER E  160  LEU E  174  1                                  15    
HELIX   68  68 VAL E  188  GLU E  206  1                                  19    
HELIX   69  69 SER E  210  ASN E  223  1                                  14    
HELIX   70  70 GLY E  227  GLY E  236  1                                  10    
HELIX   71  71 GLY E  236  ALA E  252  1                                  17    
HELIX   72  72 ASP E  253  ARG E  257  5                                   5    
HELIX   73  73 ALA E  259  ALA E  268  1                                  10    
HELIX   74  74 GLY E  272  GLY E  276  5                                   5    
HELIX   75  75 GLY F   12  VAL F   24  1                                  13    
HELIX   76  76 SER F   35  LYS F   56  1                                  22    
HELIX   77  77 THR F   60  ALA F   69  1                                  10    
HELIX   78  78 SER F   76  THR F   83  5                                   8    
HELIX   79  79 ASN F   93  VAL F  108  1                                  16    
HELIX   80  80 SER F  122  VAL F  129  1                                   8    
HELIX   81  81 ARG F  132  ASP F  134  5                                   3    
HELIX   82  82 SER F  160  LEU F  174  1                                  15    
HELIX   83  83 VAL F  188  GLU F  206  1                                  19    
HELIX   84  84 SER F  210  ASN F  223  1                                  14    
HELIX   85  85 GLY F  227  GLY F  236  1                                  10    
HELIX   86  86 GLY F  236  ALA F  252  1                                  17    
HELIX   87  87 ASP F  253  ARG F  257  5                                   5    
HELIX   88  88 ALA F  259  GLY F  269  1                                  11    
HELIX   89  89 GLY F  272  GLY F  276  5                                   5    
HELIX   90  90 GLY G   12  VAL G   24  1                                  13    
HELIX   91  91 ASP G   36  LYS G   56  1                                  21    
HELIX   92  92 THR G   60  ILE G   71  1                                  12    
HELIX   93  93 SER G   76  ALA G   82  5                                   7    
HELIX   94  94 ASN G   93  VAL G  108  1                                  16    
HELIX   95  95 SER G  122  ALA G  128  1                                   7    
HELIX   96  96 ARG G  132  ASP G  134  5                                   3    
HELIX   97  97 SER G  160  LEU G  174  1                                  15    
HELIX   98  98 VAL G  188  GLU G  206  1                                  19    
HELIX   99  99 SER G  210  ASN G  223  1                                  14    
HELIX  100 100 GLY G  227  GLY G  236  1                                  10    
HELIX  101 101 GLY G  236  ALA G  252  1                                  17    
HELIX  102 102 ASP G  253  ARG G  257  5                                   5    
HELIX  103 103 ALA G  259  GLY G  269  1                                  11    
HELIX  104 104 GLY G  272  GLY G  276  5                                   5    
HELIX  105 105 GLY H   12  VAL H   24  1                                  13    
HELIX  106 106 ASP H   36  LYS H   56  1                                  21    
HELIX  107 107 THR H   60  ILE H   71  1                                  12    
HELIX  108 108 SER H   76  THR H   83  5                                   8    
HELIX  109 109 ASN H   93  VAL H  108  1                                  16    
HELIX  110 110 SER H  122  VAL H  129  1                                   8    
HELIX  111 111 ARG H  132  ASP H  134  5                                   3    
HELIX  112 112 SER H  160  LEU H  174  1                                  15    
HELIX  113 113 VAL H  188  GLU H  206  1                                  19    
HELIX  114 114 SER H  210  ASN H  223  1                                  14    
HELIX  115 115 GLY H  227  GLY H  236  1                                  10    
HELIX  116 116 GLY H  236  ALA H  252  1                                  17    
HELIX  117 117 ASP H  253  ARG H  257  5                                   5    
HELIX  118 118 ALA H  259  ALA H  268  1                                  10    
HELIX  119 119 GLY H  272  GLY H  276  5                                   5    
HELIX  120 120 GLY I   12  VAL I   24  1                                  13    
HELIX  121 121 SER I   35  LYS I   56  1                                  22    
HELIX  122 122 THR I   60  ALA I   69  1                                  10    
HELIX  123 123 SER I   76  THR I   83  5                                   8    
HELIX  124 124 ASN I   93  VAL I  108  1                                  16    
HELIX  125 125 SER I  122  VAL I  129  1                                   8    
HELIX  126 126 ARG I  132  ASP I  134  5                                   3    
HELIX  127 127 SER I  160  LEU I  174  1                                  15    
HELIX  128 128 VAL I  188  GLU I  206  1                                  19    
HELIX  129 129 SER I  210  ASN I  223  1                                  14    
HELIX  130 130 GLY I  227  GLY I  236  1                                  10    
HELIX  131 131 GLY I  236  ALA I  252  1                                  17    
HELIX  132 132 ASP I  253  ARG I  257  5                                   5    
HELIX  133 133 ALA I  259  ALA I  268  1                                  10    
HELIX  134 134 GLY I  272  GLY I  276  5                                   5    
SHEET    1   A 8 ILE A  71  SER A  74  0                                        
SHEET    2   A 8 ASN A  28  VAL A  32  1  N  VAL A  29   O  LYS A  72           
SHEET    3   A 8 THR A   5  VAL A   9  1  N  ILE A   8   O  VAL A  32           
SHEET    4   A 8 ILE A  85  GLU A  88  1  O  ILE A  85   N  GLY A   7           
SHEET    5   A 8 ILE A 113  ASN A 117  1  O  ALA A 115   N  VAL A  86           
SHEET    6   A 8 PHE A 136  PHE A 141  1  O  MET A 139   N  SER A 116           
SHEET    7   A 8 LEU A 150  ARG A 155 -1  O  ILE A 154   N  GLY A 138           
SHEET    8   A 8 TYR A 177  LYS A 182  1  O  ILE A 179   N  LEU A 153           
SHEET    1   B 5 ASN B  28  VAL B  30  0                                        
SHEET    2   B 5 THR B   5  GLY B   7  1  N  VAL B   6   O  ASN B  28           
SHEET    3   B 5 ILE B  85  GLU B  88  1  O  ILE B  85   N  GLY B   7           
SHEET    4   B 5 ILE B 113  ASN B 117  1  O  ALA B 115   N  VAL B  86           
SHEET    5   B 5 PHE B 136  MET B 139  1  O  MET B 139   N  SER B 116           
SHEET    1   C 2 LEU B 150  ARG B 155  0                                        
SHEET    2   C 2 TYR B 177  LYS B 182  1  O  ILE B 179   N  LEU B 153           
SHEET    1   D 8 ILE C  71  SER C  74  0                                        
SHEET    2   D 8 ASN C  28  VAL C  32  1  N  VAL C  29   O  LYS C  72           
SHEET    3   D 8 THR C   5  VAL C   9  1  N  VAL C   6   O  VAL C  30           
SHEET    4   D 8 ILE C  85  GLU C  88  1  O  ILE C  85   N  GLY C   7           
SHEET    5   D 8 ILE C 113  SER C 116  1  O  ALA C 115   N  VAL C  86           
SHEET    6   D 8 PHE C 136  HIS C 140  1  O  MET C 139   N  SER C 116           
SHEET    7   D 8 LEU C 150  ARG C 155 -1  O  GLU C 152   N  HIS C 140           
SHEET    8   D 8 TYR C 177  LYS C 182  1  O  VAL C 181   N  LEU C 153           
SHEET    1   E 7 ASN D  28  VAL D  32  0                                        
SHEET    2   E 7 THR D   5  VAL D   9  1  N  ILE D   8   O  VAL D  30           
SHEET    3   E 7 ILE D  85  GLU D  88  1  O  ILE D  85   N  GLY D   7           
SHEET    4   E 7 ILE D 113  ASN D 117  1  O  ALA D 115   N  VAL D  86           
SHEET    5   E 7 PHE D 136  PHE D 141  1  O  MET D 139   N  SER D 116           
SHEET    6   E 7 LEU D 150  ARG D 155 -1  O  GLU D 152   N  HIS D 140           
SHEET    7   E 7 TYR D 177  LYS D 182  1  O  ILE D 179   N  LEU D 153           
SHEET    1   F 7 ASN E  28  VAL E  32  0                                        
SHEET    2   F 7 THR E   5  VAL E   9  1  N  VAL E   6   O  ASN E  28           
SHEET    3   F 7 ILE E  85  GLU E  88  1  O  ILE E  85   N  GLY E   7           
SHEET    4   F 7 ILE E 113  ASN E 117  1  O  ALA E 115   N  GLU E  88           
SHEET    5   F 7 PHE E 136  PHE E 141  1  O  MET E 139   N  SER E 116           
SHEET    6   F 7 LEU E 150  ARG E 155 -1  O  GLU E 152   N  HIS E 140           
SHEET    7   F 7 TYR E 177  LYS E 182  1  O  ILE E 179   N  LEU E 153           
SHEET    1   G 8 ILE F  71  SER F  74  0                                        
SHEET    2   G 8 ASN F  28  VAL F  32  1  N  MET F  31   O  LYS F  72           
SHEET    3   G 8 THR F   5  VAL F   9  1  N  VAL F   6   O  ASN F  28           
SHEET    4   G 8 ILE F  85  GLU F  88  1  O  ILE F  85   N  GLY F   7           
SHEET    5   G 8 ILE F 113  SER F 116  1  O  ALA F 115   N  VAL F  86           
SHEET    6   G 8 PHE F 136  HIS F 140  1  O  MET F 139   N  SER F 116           
SHEET    7   G 8 LEU F 150  ARG F 155 -1  O  GLU F 152   N  HIS F 140           
SHEET    8   G 8 TYR F 177  LYS F 182  1  O  ILE F 179   N  VAL F 151           
SHEET    1   H 7 ASN G  28  VAL G  32  0                                        
SHEET    2   H 7 THR G   5  VAL G   9  1  N  VAL G   6   O  VAL G  30           
SHEET    3   H 7 ILE G  85  GLU G  88  1  O  ILE G  85   N  GLY G   7           
SHEET    4   H 7 ILE G 113  ASN G 117  1  O  ALA G 115   N  VAL G  86           
SHEET    5   H 7 PHE G 136  PHE G 141  1  O  MET G 139   N  SER G 116           
SHEET    6   H 7 LEU G 150  ARG G 155 -1  O  ILE G 154   N  GLY G 138           
SHEET    7   H 7 TYR G 177  LYS G 182  1  O  ILE G 179   N  LEU G 153           
SHEET    1   I 7 ASN H  28  VAL H  30  0                                        
SHEET    2   I 7 THR H   5  GLY H   7  1  N  VAL H   6   O  ASN H  28           
SHEET    3   I 7 ILE H  85  GLU H  88  1  O  ILE H  85   N  GLY H   7           
SHEET    4   I 7 ILE H 113  ASN H 117  1  O  ALA H 115   N  VAL H  86           
SHEET    5   I 7 PHE H 136  PHE H 141  1  O  MET H 139   N  SER H 116           
SHEET    6   I 7 LEU H 150  ARG H 155 -1  O  GLU H 152   N  HIS H 140           
SHEET    7   I 7 TYR H 177  LYS H 182  1  O  ILE H 179   N  LEU H 153           
SHEET    1   J 8 ILE I  71  SER I  74  0                                        
SHEET    2   J 8 ASN I  28  VAL I  32  1  N  VAL I  29   O  LYS I  72           
SHEET    3   J 8 THR I   5  VAL I   9  1  N  VAL I   6   O  VAL I  30           
SHEET    4   J 8 ILE I  85  GLU I  88  1  O  ILE I  85   N  GLY I   7           
SHEET    5   J 8 ILE I 113  SER I 116  1  O  ALA I 115   N  GLU I  88           
SHEET    6   J 8 PHE I 136  HIS I 140  1  O  MET I 139   N  SER I 116           
SHEET    7   J 8 LEU I 150  ARG I 155 -1  O  GLU I 152   N  HIS I 140           
SHEET    8   J 8 TYR I 177  LYS I 182  1  O  VAL I 181   N  LEU I 153           
CISPEP   1 LEU A   59    THR A   60          0       -20.95                     
CISPEP   2 ASN B  143    PRO B  144          0       -10.81                     
CISPEP   3 SER B  283    LYS B  284          0       -16.46                     
CISPEP   4 ASN C  143    PRO C  144          0       -15.20                     
CISPEP   5 LEU D   59    THR D   60          0       -17.20                     
CISPEP   6 ASN E  143    PRO E  144          0       -10.12                     
CISPEP   7 SER E  283    LYS E  284          0       -12.51                     
CISPEP   8 ASN F  143    PRO F  144          0       -11.60                     
CISPEP   9 LEU G   59    THR G   60          0       -21.50                     
CISPEP  10 ASN H  143    PRO H  144          0        -3.10                     
CISPEP  11 SER H  283    LYS H  284          0       -15.20                     
CISPEP  12 ASN I  143    PRO I  144          0       -12.14                     
SITE     1 AC1 15 VAL A   9  GLY A  12  THR A  13  MET A  14                    
SITE     2 AC1 15 ASP A  33  ALA A  89  ALA A  90  THR A  91                    
SITE     3 AC1 15 GLU A  92  LYS A  97  ILE A 100  ASN A 117                    
SITE     4 AC1 15 SER A 119  HIS A 140  ASN A 143                               
SITE     1 AC2 15 VAL B   9  GLY B  12  THR B  13  MET B  14                    
SITE     2 AC2 15 ASP B  33  TYR B  77  ALA B  89  ALA B  90                    
SITE     3 AC2 15 THR B  91  GLU B  92  ASN B 117  THR B 118                    
SITE     4 AC2 15 SER B 119  HIS B 140  PHE B 141                               
SITE     1 AC3 15 GLY C  10  GLY C  12  THR C  13  MET C  14                    
SITE     2 AC3 15 ASP C  33  ILE C  34  TYR C  77  ALA C  89                    
SITE     3 AC3 15 ALA C  90  THR C  91  GLU C  92  ILE C 100                    
SITE     4 AC3 15 ASN C 117  HIS C 140  ASN C 143                               
SITE     1 AC4 17 GLY D  12  THR D  13  MET D  14  ASP D  33                    
SITE     2 AC4 17 ILE D  34  TYR D  77  ALA D  89  ALA D  90                    
SITE     3 AC4 17 THR D  91  GLU D  92  LYS D  97  ASN D 117                    
SITE     4 AC4 17 SER D 119  HIS D 140  PHE D 141  ASN D 143                    
SITE     5 AC4 17 SER F 283                                                     
SITE     1 AC5 14 GLY E  12  THR E  13  MET E  14  ASP E  33                    
SITE     2 AC5 14 TYR E  77  ALA E  89  ALA E  90  THR E  91                    
SITE     3 AC5 14 GLU E  92  LYS E  97  ASN E 117  HIS E 140                    
SITE     4 AC5 14 PHE E 141  ASN E 143                                          
SITE     1 AC6 14 GLY F  10  GLY F  12  THR F  13  MET F  14                    
SITE     2 AC6 14 ASP F  33  ILE F  34  TYR F  77  ALA F  89                    
SITE     3 AC6 14 ALA F  90  THR F  91  GLU F  92  ILE F 100                    
SITE     4 AC6 14 ASN F 117  HOH F 411                                          
SITE     1 AC7 15 GLY G  12  THR G  13  MET G  14  ASP G  33                    
SITE     2 AC7 15 ILE G  34  TYR G  77  ALA G  89  ALA G  90                    
SITE     3 AC7 15 THR G  91  GLU G  92  ASN G 117  SER G 119                    
SITE     4 AC7 15 HIS G 140  ASN G 143  SER I 283                               
SITE     1 AC8 12 GLY H  12  THR H  13  MET H  14  ASP H  33                    
SITE     2 AC8 12 TYR H  77  ALA H  89  ALA H  90  THR H  91                    
SITE     3 AC8 12 GLU H  92  ASN H 117  HIS H 140  HOH H 408                    
SITE     1 AC9 15 GLY I  10  GLY I  12  THR I  13  MET I  14                    
SITE     2 AC9 15 ASP I  33  ILE I  34  TYR I  77  ALA I  89                    
SITE     3 AC9 15 ALA I  90  THR I  91  GLU I  92  LYS I  97                    
SITE     4 AC9 15 ILE I 100  ASN I 117  THR I 239                               
CRYST1  235.076  135.586   97.445  90.00  90.09  90.00 C 1 2 1      36          
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      0.004254  0.000000  0.000006        0.00000                         
SCALE2      0.000000  0.007375  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010262        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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