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Database: PDB
Entry: 2OAE
LinkDB: 2OAE
Original site: 2OAE 
HEADER    HYDROLASE                               15-DEC-06   2OAE              
TITLE     CRYSTAL STRUCTURE OF RAT DIPEPTIDYL PEPTIDASE (DPPIV) WITH THIAZOLE-  
TITLE    2 BASED PEPTIDE MIMETIC #31                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SOLUBLE FORM: RESIDUES 37-767;                             
COMPND   5 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN  
COMPND   6 CD26, GP110 GLYCOPROTEIN, BILE CANALICULUS DOMAIN-SPECIFIC MEMBRANE  
COMPND   7 GLYCOPROTEIN;                                                        
COMPND   8 EC: 3.4.14.5                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116                                                
KEYWDS    SERINE-PEPTIDASE, INHIBITOR COMPLEX, HYDROLASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.L.LONGENECKER,Q.SHUAI,J.PATEL,P.WIEDEMAN                            
REVDAT   4   18-OCT-17 2OAE    1       REMARK                                   
REVDAT   3   24-FEB-09 2OAE    1       VERSN                                    
REVDAT   2   01-MAY-07 2OAE    1       JRNL                                     
REVDAT   1   27-FEB-07 2OAE    0                                                
JRNL        AUTH   B.J.BACKES,K.LONGENECKER,G.L.HAMILTON,K.STEWART,C.LAI,       
JRNL        AUTH 2 H.KOPECKA,T.W.VON GELDERN,D.J.MADAR,Z.PEI,T.H.LUBBEN,        
JRNL        AUTH 3 B.A.ZINKER,Z.TIAN,S.J.BALLARON,M.A.STASHKO,A.K.MIKA,         
JRNL        AUTH 4 D.W.BENO,A.J.KEMPF-GROTE,C.BLACK-SCHAEFER,H.L.SHAM,          
JRNL        AUTH 5 J.M.TREVILLYAN                                               
JRNL        TITL   PYRROLIDINE-CONSTRAINED PHENETHYLAMINES: THE DESIGN OF       
JRNL        TITL 2 POTENT, SELECTIVE, AND PHARMACOLOGICALLY EFFICACIOUS         
JRNL        TITL 3 DIPEPTIDYL PEPTIDASE IV (DPP4) INHIBITORS FROM A LEAD-LIKE   
JRNL        TITL 4 SCREENING HIT.                                               
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  17  2005 2007              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   17276063                                                     
JRNL        DOI    10.1016/J.BMCL.2007.01.026                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 59968                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.249                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3039                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 50                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1007                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4090                       
REMARK   3   BIN FREE R VALUE                    : 0.4280                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 49                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11840                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REPADD.PARAM                           
REMARK   3  PARAMETER FILE  2  : LIG.PAR                                        
REMARK   3  PARAMETER FILE  3  : MSI_CNX_TOPPAR:WATER_REP.PARAM                 
REMARK   3  PARAMETER FILE  4  : MSI_CNX_TOPPAR:ION.PARAM                       
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2OAE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000040888.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60215                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53300                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3                           
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       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
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      104.17450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      104.17450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      104.17450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      104.17450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      104.17450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      104.17450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000      104.17450            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000      104.17450            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000      104.17450            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000      104.17450            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000      104.17450            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000      104.17450            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000      104.17450            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000      104.17450            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000      104.17450            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000      104.17450            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000      104.17450            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000      104.17450            
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 300 REMARK: THE DIMER OF THE ASYMMETRIC UNIT IS THOUGHT TO BE            
REMARK 300 BIOLOGICALLY RELEVANT                                                
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: 5120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 56370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 22550 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 161930 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -153.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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  0.000000  0.000000 -1.000000     -104.17450            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  1.000000  0.000000     -104.17450            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  0.000000  1.000000      104.17450            
REMARK 350   BIOMT3   3 -1.000000  0.000000  0.000000     -104.17450            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  39    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A  40    OG1  CG2                                            
REMARK 470     THR A  42    OG1  CG2                                            
REMARK 470     LEU A  43    CG   CD1  CD2                                       
REMARK 470     PHE A  96    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN A 442    CG   OD1  ND2                                       
REMARK 470     LYS A 503    CG   CD   CE   NZ                                   
REMARK 470     ARG B  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  39    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B  40    OG1  CG2                                            
REMARK 470     THR B  42    OG1  CG2                                            
REMARK 470     LEU B  43    CG   CD1  CD2                                       
REMARK 470     PHE B  96    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN B 442    CG   OD1  ND2                                       
REMARK 470     LYS B 503    CG   CD   CE   NZ                                   
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    CYS A 383   CA  -  CB  -  SG  ANGL. DEV. =   7.2 DEGREES          
REMARK 500    HIS A 713   N   -  CA  -  C   ANGL. DEV. =  19.0 DEGREES          
REMARK 500    CYS B 383   CA  -  CB  -  SG  ANGL. DEV. =   7.8 DEGREES          
REMARK 500    HIS B 713   N   -  CA  -  C   ANGL. DEV. =  18.5 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    SER A  62     -159.57   -147.40                                   
REMARK 500    SER A  64       -1.03   -143.10                                   
REMARK 500    GLU A  80      -56.97    123.09                                   
REMARK 500    ASN A  83      112.45    -23.25                                   
REMARK 500    SER A  84     -150.77   -113.22                                   
REMARK 500    SER A  85      136.53    154.39                                   
REMARK 500    SER A  91     -136.94    -63.49                                   
REMARK 500    THR A  92      -71.91     30.94                                   
REMARK 500    PHE A  96       41.94    -82.55                                   
REMARK 500    ILE A 100       93.35    -69.48                                   
REMARK 500    GLN A 121       98.61   -169.17                                   
REMARK 500    TRP A 122     -179.55     74.96                                   
REMARK 500    TYR A 126      155.97    177.15                                   
REMARK 500    GLN A 139      163.10    174.02                                   
REMARK 500    GLU A 143      -97.08    -67.62                                   
REMARK 500    PRO A 147      138.16    -25.38                                   
REMARK 500    ASN A 148       32.98    -81.28                                   
REMARK 500    ASN A 149       28.81   -163.13                                   
REMARK 500    GLU A 158     -100.69   -105.24                                   
REMARK 500    SER A 185       -4.35   -145.43                                   
REMARK 500    VAL A 191      -63.24   -136.94                                   
REMARK 500    ILE A 205      -75.61    -97.62                                   
REMARK 500    SER A 240     -163.00     53.45                                   
REMARK 500    LEU A 274      -43.26    -29.20                                   
REMARK 500    ALA A 287      154.17    -49.90                                   
REMARK 500    SER A 290       11.93    -64.57                                   
REMARK 500    GLN A 318       31.65    -60.51                                   
REMARK 500    HIS A 343      107.30     71.55                                   
REMARK 500    ASP A 365        4.33    -68.12                                   
REMARK 500    PRO A 391       96.75    -41.04                                   
REMARK 500    GLN A 393       19.07   -171.81                                   
REMARK 500    ALA A 410      147.22   -170.44                                   
REMARK 500    ASN A 442       54.54    -67.49                                   
REMARK 500    LEU A 450      -71.95     -3.29                                   
REMARK 500    SER A 461       93.01    172.41                                   
REMARK 500    LYS A 464      -36.95    -35.29                                   
REMARK 500    PRO A 476      -50.94    -24.57                                   
REMARK 500    GLN A 489       -0.50     74.30                                   
REMARK 500    GLU A 496      116.46   -169.60                                   
REMARK 500    ASP A 516     -163.45   -126.20                                   
REMARK 500    ASN A 521       40.90     31.82                                   
REMARK 500    PRO A 533     -116.87    -13.40                                   
REMARK 500    HIS A 534       43.82    -61.71                                   
REMARK 500    LYS A 537      -16.24    -44.88                                   
REMARK 500    TYR A 548      -80.08   -153.15                                   
REMARK 500    ALA A 558       34.63    -87.24                                   
REMARK 500    ASN A 563     -156.82   -116.60                                   
REMARK 500    TYR A 586       71.09   -117.45                                   
REMARK 500    ASN A 596      133.66    -34.50                                   
REMARK 500    ARG A 598       67.35   -156.75                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     135 RAMACHANDRAN OUTLIERS.                        
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 SO4 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AIL A 901                 
DBREF  2OAE A   38   767  UNP    P14740   DPP4_RAT        38    767             
DBREF  2OAE B   38   767  UNP    P14740   DPP4_RAT        38    767             
SEQRES   1 A  730  ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS ASN THR          
SEQRES   2 A  730  PHE ARG VAL LYS SER TYR SER LEU ARG TRP VAL SER ASP          
SEQRES   3 A  730  SER GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU LEU          
SEQRES   4 A  730  PHE ASN ALA GLU HIS GLY ASN SER SER ILE PHE LEU GLU          
SEQRES   5 A  730  ASN SER THR PHE GLU ILE PHE GLY ASP SER ILE SER ASP          
SEQRES   6 A  730  TYR SER VAL SER PRO ASP ARG LEU PHE VAL LEU LEU GLU          
SEQRES   7 A  730  TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA          
SEQRES   8 A  730  SER TYR SER ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE          
SEQRES   9 A  730  THR GLU GLU LYS ILE PRO ASN ASN THR GLN TRP ILE THR          
SEQRES  10 A  730  TRP SER GLN GLU GLY HIS LYS LEU ALA TYR VAL TRP LYS          
SEQRES  11 A  730  ASN ASP ILE TYR VAL LYS ILE GLU PRO HIS LEU PRO SER          
SEQRES  12 A  730  HIS ARG ILE THR SER THR GLY LYS GLU ASN VAL ILE PHE          
SEQRES  13 A  730  ASN GLY ILE ASN ASP TRP VAL TYR GLU GLU GLU ILE PHE          
SEQRES  14 A  730  GLY ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR          
SEQRES  15 A  730  PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLY VAL PRO          
SEQRES  16 A  730  LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN          
SEQRES  17 A  730  TYR PRO LYS THR VAL TRP ILE PRO TYR PRO LYS ALA GLY          
SEQRES  18 A  730  ALA VAL ASN PRO THR VAL LYS PHE PHE ILE VAL ASN THR          
SEQRES  19 A  730  ASP SER LEU SER SER THR THR THR THR ILE PRO MET GLN          
SEQRES  20 A  730  ILE THR ALA PRO ALA SER VAL THR THR GLY ASP HIS TYR          
SEQRES  21 A  730  LEU CYS ASP VAL ALA TRP VAL SER GLU ASP ARG ILE SER          
SEQRES  22 A  730  LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET          
SEQRES  23 A  730  ALA ILE CYS ASP TYR ASP LYS THR THR LEU VAL TRP ASN          
SEQRES  24 A  730  CYS PRO THR THR GLN GLU HIS ILE GLU THR SER ALA THR          
SEQRES  25 A  730  GLY TRP CYS GLY ARG PHE ARG PRO ALA GLU PRO HIS PHE          
SEQRES  26 A  730  THR SER ASP GLY SER SER PHE TYR LYS ILE VAL SER ASP          
SEQRES  27 A  730  LYS ASP GLY TYR LYS HIS ILE CYS GLN PHE GLN LYS ASP          
SEQRES  28 A  730  ARG LYS PRO GLU GLN VAL CYS THR PHE ILE THR LYS GLY          
SEQRES  29 A  730  ALA TRP GLU VAL ILE SER ILE GLU ALA LEU THR SER ASP          
SEQRES  30 A  730  TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLU MET PRO          
SEQRES  31 A  730  GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU THR ASP HIS          
SEQRES  32 A  730  THR ASN LYS LYS CYS LEU SER CYS ASP LEU ASN PRO GLU          
SEQRES  33 A  730  ARG CYS GLN TYR TYR SER VAL SER LEU SER LYS GLU ALA          
SEQRES  34 A  730  LYS TYR TYR GLN LEU GLY CYS ARG GLY PRO GLY LEU PRO          
SEQRES  35 A  730  LEU TYR THR LEU HIS ARG SER THR ASP GLN LYS GLU LEU          
SEQRES  36 A  730  ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU          
SEQRES  37 A  730  GLN ASP VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE          
SEQRES  38 A  730  VAL LEU ASN GLU THR ARG PHE TRP TYR GLN MET ILE LEU          
SEQRES  39 A  730  PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU          
SEQRES  40 A  730  ILE ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP          
SEQRES  41 A  730  ALA ALA PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER          
SEQRES  42 A  730  THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY          
SEQRES  43 A  730  SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN          
SEQRES  44 A  730  LYS ARG LEU GLY THR LEU GLU VAL GLU ASP GLN ILE GLU          
SEQRES  45 A  730  ALA ALA ARG GLN PHE LEU LYS MET GLY PHE VAL ASP SER          
SEQRES  46 A  730  LYS ARG VAL ALA ILE TRP GLY TRP SER TYR GLY GLY TYR          
SEQRES  47 A  730  VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE          
SEQRES  48 A  730  LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU          
SEQRES  49 A  730  TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU          
SEQRES  50 A  730  PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER          
SEQRES  51 A  730  THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU          
SEQRES  52 A  730  TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS          
SEQRES  53 A  730  PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP          
SEQRES  54 A  730  ALA GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU          
SEQRES  55 A  730  ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE          
SEQRES  56 A  730  TYR SER HIS MET SER HIS PHE LEU GLN GLN CYS PHE SER          
SEQRES  57 A  730  LEU ARG                                                      
SEQRES   1 B  730  ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS ASN THR          
SEQRES   2 B  730  PHE ARG VAL LYS SER TYR SER LEU ARG TRP VAL SER ASP          
SEQRES   3 B  730  SER GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU LEU          
SEQRES   4 B  730  PHE ASN ALA GLU HIS GLY ASN SER SER ILE PHE LEU GLU          
SEQRES   5 B  730  ASN SER THR PHE GLU ILE PHE GLY ASP SER ILE SER ASP          
SEQRES   6 B  730  TYR SER VAL SER PRO ASP ARG LEU PHE VAL LEU LEU GLU          
SEQRES   7 B  730  TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA          
SEQRES   8 B  730  SER TYR SER ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE          
SEQRES   9 B  730  THR GLU GLU LYS ILE PRO ASN ASN THR GLN TRP ILE THR          
SEQRES  10 B  730  TRP SER GLN GLU GLY HIS LYS LEU ALA TYR VAL TRP LYS          
SEQRES  11 B  730  ASN ASP ILE TYR VAL LYS ILE GLU PRO HIS LEU PRO SER          
SEQRES  12 B  730  HIS ARG ILE THR SER THR GLY LYS GLU ASN VAL ILE PHE          
SEQRES  13 B  730  ASN GLY ILE ASN ASP TRP VAL TYR GLU GLU GLU ILE PHE          
SEQRES  14 B  730  GLY ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR          
SEQRES  15 B  730  PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLY VAL PRO          
SEQRES  16 B  730  LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN          
SEQRES  17 B  730  TYR PRO LYS THR VAL TRP ILE PRO TYR PRO LYS ALA GLY          
SEQRES  18 B  730  ALA VAL ASN PRO THR VAL LYS PHE PHE ILE VAL ASN THR          
SEQRES  19 B  730  ASP SER LEU SER SER THR THR THR THR ILE PRO MET GLN          
SEQRES  20 B  730  ILE THR ALA PRO ALA SER VAL THR THR GLY ASP HIS TYR          
SEQRES  21 B  730  LEU CYS ASP VAL ALA TRP VAL SER GLU ASP ARG ILE SER          
SEQRES  22 B  730  LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET          
SEQRES  23 B  730  ALA ILE CYS ASP TYR ASP LYS THR THR LEU VAL TRP ASN          
SEQRES  24 B  730  CYS PRO THR THR GLN GLU HIS ILE GLU THR SER ALA THR          
SEQRES  25 B  730  GLY TRP CYS GLY ARG PHE ARG PRO ALA GLU PRO HIS PHE          
SEQRES  26 B  730  THR SER ASP GLY SER SER PHE TYR LYS ILE VAL SER ASP          
SEQRES  27 B  730  LYS ASP GLY TYR LYS HIS ILE CYS GLN PHE GLN LYS ASP          
SEQRES  28 B  730  ARG LYS PRO GLU GLN VAL CYS THR PHE ILE THR LYS GLY          
SEQRES  29 B  730  ALA TRP GLU VAL ILE SER ILE GLU ALA LEU THR SER ASP          
SEQRES  30 B  730  TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLU MET PRO          
SEQRES  31 B  730  GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU THR ASP HIS          
SEQRES  32 B  730  THR ASN LYS LYS CYS LEU SER CYS ASP LEU ASN PRO GLU          
SEQRES  33 B  730  ARG CYS GLN TYR TYR SER VAL SER LEU SER LYS GLU ALA          
SEQRES  34 B  730  LYS TYR TYR GLN LEU GLY CYS ARG GLY PRO GLY LEU PRO          
SEQRES  35 B  730  LEU TYR THR LEU HIS ARG SER THR ASP GLN LYS GLU LEU          
SEQRES  36 B  730  ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU          
SEQRES  37 B  730  GLN ASP VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE          
SEQRES  38 B  730  VAL LEU ASN GLU THR ARG PHE TRP TYR GLN MET ILE LEU          
SEQRES  39 B  730  PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU          
SEQRES  40 B  730  ILE ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP          
SEQRES  41 B  730  ALA ALA PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER          
SEQRES  42 B  730  THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY          
SEQRES  43 B  730  SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN          
SEQRES  44 B  730  LYS ARG LEU GLY THR LEU GLU VAL GLU ASP GLN ILE GLU          
SEQRES  45 B  730  ALA ALA ARG GLN PHE LEU LYS MET GLY PHE VAL ASP SER          
SEQRES  46 B  730  LYS ARG VAL ALA ILE TRP GLY TRP SER TYR GLY GLY TYR          
SEQRES  47 B  730  VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE          
SEQRES  48 B  730  LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU          
SEQRES  49 B  730  TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU          
SEQRES  50 B  730  PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER          
SEQRES  51 B  730  THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU          
SEQRES  52 B  730  TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS          
SEQRES  53 B  730  PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP          
SEQRES  54 B  730  ALA GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU          
SEQRES  55 B  730  ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE          
SEQRES  56 B  730  TYR SER HIS MET SER HIS PHE LEU GLN GLN CYS PHE SER          
SEQRES  57 B  730  LEU ARG                                                      
HET    SO4  A 801       5                                                       
HET    AIL  A 901      21                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     AIL N-{[(3S,5S)-5-(1,3-THIAZOLIDIN-3-YLCARBONYL)PYRROLIDIN-          
HETNAM   2 AIL  3-YL]METHYL}-1,3-THIAZOLE-4-CARBOXAMIDE                         
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  AIL    C13 H18 N4 O2 S2                                             
HELIX    1   1 THR A   42  LYS A   48  1                                   7    
HELIX    2   2 SER A   91  ILE A   95  5                                   5    
HELIX    3   3 ASP A  198  ILE A  205  1                                   8    
HELIX    4   4 PRO A  216  GLY A  218  5                                   3    
HELIX    5   5 ASP A  272  THR A  277  5                                   6    
HELIX    6   6 PRO A  288  THR A  293  1                                   6    
HELIX    7   7 PRO A  338  GLU A  342  5                                   5    
HELIX    8   8 GLU A  422  MET A  426  5                                   5    
HELIX    9   9 ASN A  498  GLN A  506  1                                   9    
HELIX   10  10 ASN A  563  THR A  571  1                                   9    
HELIX   11  11 GLY A  588  HIS A  593  1                                   6    
HELIX   12  12 ALA A  594  ASN A  596  5                                   3    
HELIX   13  13 THR A  601  MET A  617  1                                  17    
HELIX   14  14 SER A  631  GLY A  642  1                                  12    
HELIX   15  15 ARG A  659  TYR A  663  5                                   5    
HELIX   16  16 ASP A  664  GLY A  673  1                                  10    
HELIX   17  17 ASN A  680  SER A  687  1                                   8    
HELIX   18  18 VAL A  689  VAL A  699  5                                  11    
HELIX   19  19 PHE A  714  GLY A  728  1                                  15    
HELIX   20  20 SER A  745  PHE A  764  1                                  20    
HELIX   21  21 THR B   42  LYS B   48  1                                   7    
HELIX   22  22 SER B   91  ILE B   95  5                                   5    
HELIX   23  23 ASP B  198  ILE B  205  1                                   8    
HELIX   24  24 PRO B  216  GLY B  218  5                                   3    
HELIX   25  25 ASP B  272  THR B  277  5                                   6    
HELIX   26  26 PRO B  288  THR B  293  1                                   6    
HELIX   27  27 PRO B  338  GLU B  342  5                                   5    
HELIX   28  28 GLU B  422  MET B  426  5                                   5    
HELIX   29  29 ASN B  498  GLN B  506  1                                   9    
HELIX   30  30 ASN B  563  THR B  571  1                                   9    
HELIX   31  31 GLY B  588  HIS B  593  1                                   6    
HELIX   32  32 ALA B  594  ASN B  596  5                                   3    
HELIX   33  33 THR B  601  MET B  617  1                                  17    
HELIX   34  34 SER B  631  GLY B  642  1                                  12    
HELIX   35  35 ARG B  659  TYR B  663  5                                   5    
HELIX   36  36 ASP B  664  GLY B  673  1                                  10    
HELIX   37  37 ASN B  680  SER B  687  1                                   8    
HELIX   38  38 VAL B  689  VAL B  699  5                                  11    
HELIX   39  39 PHE B  714  GLY B  728  1                                  15    
HELIX   40  40 SER B  745  PHE B  764  1                                  20    
SHEET    1   A 4 ARG A  59  TRP A  60  0                                        
SHEET    2   A 4 GLU A  65  LYS A  69 -1  O  LEU A  67   N  ARG A  59           
SHEET    3   A 4 ILE A  74  ASN A  78 -1  O  LEU A  75   N  TYR A  68           
SHEET    4   A 4 ILE A  86  LEU A  88 -1  O  PHE A  87   N  ILE A  74           
SHEET    1   B 4 ILE A 100  VAL A 105  0                                        
SHEET    2   B 4 PHE A 111  LYS A 120 -1  O  LEU A 113   N  SER A 104           
SHEET    3   B 4 TYR A 126  ASP A 134 -1  O  SER A 129   N  TYR A 116           
SHEET    4   B 4 GLN A 139  LEU A 140 -1  O  GLN A 139   N  ASP A 134           
SHEET    1   C 4 TRP A 152  TRP A 155  0                                        
SHEET    2   C 4 LEU A 162  TRP A 166 -1  O  VAL A 165   N  TRP A 152           
SHEET    3   C 4 ASP A 169  LYS A 173 -1  O  TYR A 171   N  TYR A 164           
SHEET    4   C 4 HIS A 181  ARG A 182 -1  O  HIS A 181   N  VAL A 172           
SHEET    1   D 3 ILE A 192  ASN A 194  0                                        
SHEET    2   D 3 PHE A 220  ASN A 227 -1  O  PHE A 226   N  PHE A 193           
SHEET    3   D 3 LEU A 212  TRP A 214 -1  N  TRP A 213   O  ALA A 222           
SHEET    1   E 4 ILE A 192  ASN A 194  0                                        
SHEET    2   E 4 PHE A 220  ASN A 227 -1  O  PHE A 226   N  PHE A 193           
SHEET    3   E 4 THR A 263  ASN A 270 -1  O  PHE A 267   N  TYR A 223           
SHEET    4   E 4 MET A 283  ILE A 285 -1  O  MET A 283   N  ILE A 268           
SHEET    1   F 2 LEU A 233  PHE A 238  0                                        
SHEET    2   F 2 LYS A 248  PRO A 253 -1  O  VAL A 250   N  TYR A 236           
SHEET    1   G 4 HIS A 296  TRP A 303  0                                        
SHEET    2   G 4 ARG A 308  ARG A 315 -1  O  LEU A 314   N  TYR A 297           
SHEET    3   G 4 TYR A 320  ASP A 329 -1  O  VAL A 322   N  TRP A 313           
SHEET    4   G 4 VAL A 334  ASN A 336 -1  O  VAL A 334   N  ASP A 329           
SHEET    1   H 4 HIS A 296  TRP A 303  0                                        
SHEET    2   H 4 ARG A 308  ARG A 315 -1  O  LEU A 314   N  TYR A 297           
SHEET    3   H 4 TYR A 320  ASP A 329 -1  O  VAL A 322   N  TRP A 313           
SHEET    4   H 4 ILE A 344  THR A 346 -1  O  GLU A 345   N  SER A 321           
SHEET    1   I 3 HIS A 361  PHE A 362  0                                        
SHEET    2   I 3 SER A 368  SER A 374 -1  O  TYR A 370   N  HIS A 361           
SHEET    3   I 3 LYS A 380  GLN A 386 -1  O  HIS A 381   N  VAL A 373           
SHEET    1   J 4 VAL A 405  LEU A 411  0                                        
SHEET    2   J 4 TYR A 415  SER A 420 -1  O  TYR A 417   N  GLU A 409           
SHEET    3   J 4 ASN A 431  GLN A 436 -1  O  ILE A 435   N  LEU A 416           
SHEET    4   J 4 LYS A 444  CYS A 445 -1  O  LYS A 444   N  LYS A 434           
SHEET    1   K 4 TYR A 458  SER A 459  0                                        
SHEET    2   K 4 TYR A 468  CYS A 473 -1  O  GLY A 472   N  SER A 459           
SHEET    3   K 4 LEU A 480  ARG A 485 -1  O  THR A 482   N  LEU A 471           
SHEET    4   K 4 GLU A 491  ASP A 497 -1  O  GLU A 496   N  TYR A 481           
SHEET    1   L 8 SER A 512  LEU A 520  0                                        
SHEET    2   L 8 THR A 523  LEU A 531 -1  O  THR A 523   N  LEU A 520           
SHEET    3   L 8 ILE A 575  PHE A 579 -1  O  VAL A 576   N  ILE A 530           
SHEET    4   L 8 TYR A 541  VAL A 547  1  N  LEU A 544   O  ILE A 575           
SHEET    5   L 8 VAL A 620  TRP A 630  1  O  ALA A 626   N  LEU A 543           
SHEET    6   L 8 CYS A 650  VAL A 654  1  O  VAL A 654   N  GLY A 629           
SHEET    7   L 8 GLU A 700  GLY A 706  1  O  ILE A 704   N  ALA A 653           
SHEET    8   L 8 GLN A 732  TYR A 736  1  O  GLN A 732   N  LEU A 703           
SHEET    1   M 4 ARG B  59  TRP B  60  0                                        
SHEET    2   M 4 GLU B  65  LYS B  69 -1  O  LEU B  67   N  ARG B  59           
SHEET    3   M 4 ILE B  74  ASN B  78 -1  O  LEU B  75   N  TYR B  68           
SHEET    4   M 4 ILE B  86  LEU B  88 -1  O  PHE B  87   N  ILE B  74           
SHEET    1   N 4 ILE B 100  VAL B 105  0                                        
SHEET    2   N 4 PHE B 111  LYS B 120 -1  O  LEU B 113   N  SER B 104           
SHEET    3   N 4 TYR B 126  ASP B 134 -1  O  SER B 129   N  TYR B 116           
SHEET    4   N 4 GLN B 139  LEU B 140 -1  O  GLN B 139   N  ASP B 134           
SHEET    1   O 4 TRP B 152  TRP B 155  0                                        
SHEET    2   O 4 LEU B 162  TRP B 166 -1  O  VAL B 165   N  TRP B 152           
SHEET    3   O 4 ASP B 169  LYS B 173 -1  O  TYR B 171   N  TYR B 164           
SHEET    4   O 4 HIS B 181  ARG B 182 -1  O  HIS B 181   N  VAL B 172           
SHEET    1   P 3 ILE B 192  ASN B 194  0                                        
SHEET    2   P 3 PHE B 220  ASN B 227 -1  O  PHE B 226   N  PHE B 193           
SHEET    3   P 3 LEU B 212  TRP B 214 -1  N  TRP B 213   O  ALA B 222           
SHEET    1   Q 4 ILE B 192  ASN B 194  0                                        
SHEET    2   Q 4 PHE B 220  ASN B 227 -1  O  PHE B 226   N  PHE B 193           
SHEET    3   Q 4 THR B 263  ASN B 270 -1  O  PHE B 267   N  TYR B 223           
SHEET    4   Q 4 MET B 283  ILE B 285 -1  O  MET B 283   N  ILE B 268           
SHEET    1   R 2 LEU B 233  PHE B 238  0                                        
SHEET    2   R 2 LYS B 248  PRO B 253 -1  O  VAL B 250   N  TYR B 236           
SHEET    1   S 4 HIS B 296  TRP B 303  0                                        
SHEET    2   S 4 ARG B 308  ARG B 315 -1  O  GLN B 312   N  CYS B 299           
SHEET    3   S 4 TYR B 320  ASP B 329 -1  O  VAL B 322   N  TRP B 313           
SHEET    4   S 4 VAL B 334  ASN B 336 -1  O  VAL B 334   N  ASP B 329           
SHEET    1   T 4 HIS B 296  TRP B 303  0                                        
SHEET    2   T 4 ARG B 308  ARG B 315 -1  O  GLN B 312   N  CYS B 299           
SHEET    3   T 4 TYR B 320  ASP B 329 -1  O  VAL B 322   N  TRP B 313           
SHEET    4   T 4 ILE B 344  THR B 346 -1  O  GLU B 345   N  SER B 321           
SHEET    1   U 3 HIS B 361  PHE B 362  0                                        
SHEET    2   U 3 SER B 368  SER B 374 -1  O  TYR B 370   N  HIS B 361           
SHEET    3   U 3 LYS B 380  GLN B 386 -1  O  HIS B 381   N  VAL B 373           
SHEET    1   V 4 VAL B 405  LEU B 411  0                                        
SHEET    2   V 4 TYR B 415  SER B 420 -1  O  TYR B 417   N  GLU B 409           
SHEET    3   V 4 ASN B 431  GLN B 436 -1  O  ILE B 435   N  LEU B 416           
SHEET    4   V 4 LYS B 444  CYS B 445 -1  O  LYS B 444   N  LYS B 434           
SHEET    1   W 4 TYR B 458  SER B 459  0                                        
SHEET    2   W 4 TYR B 468  CYS B 473 -1  O  GLY B 472   N  SER B 459           
SHEET    3   W 4 LEU B 480  ARG B 485 -1  O  THR B 482   N  LEU B 471           
SHEET    4   W 4 GLU B 491  GLU B 496 -1  O  GLU B 496   N  TYR B 481           
SHEET    1   X 8 SER B 512  LEU B 520  0                                        
SHEET    2   X 8 THR B 523  LEU B 531 -1  O  TYR B 527   N  ASP B 516           
SHEET    3   X 8 ILE B 575  PHE B 579 -1  O  VAL B 576   N  ILE B 530           
SHEET    4   X 8 TYR B 541  VAL B 547  1  N  LEU B 544   O  ILE B 575           
SHEET    5   X 8 VAL B 620  TRP B 630  1  O  ASP B 621   N  TYR B 541           
SHEET    6   X 8 CYS B 650  VAL B 654  1  O  VAL B 654   N  GLY B 629           
SHEET    7   X 8 GLU B 700  GLY B 706  1  O  ILE B 704   N  ALA B 653           
SHEET    8   X 8 GLN B 732  TYR B 736  1  O  GLN B 732   N  LEU B 703           
SSBOND   1 CYS A  326    CYS A  337                          1555   1555  2.03  
SSBOND   2 CYS A  383    CYS A  395                          1555   1555  2.04  
SSBOND   3 CYS A  445    CYS A  448                          1555   1555  2.03  
SSBOND   4 CYS A  455    CYS A  473                          1555   1555  2.04  
SSBOND   5 CYS A  650    CYS A  763                          1555   1555  2.05  
SSBOND   6 CYS B  326    CYS B  337                          1555   1555  2.04  
SSBOND   7 CYS B  383    CYS B  395                          1555   1555  2.05  
SSBOND   8 CYS B  445    CYS B  448                          1555   1555  2.05  
SSBOND   9 CYS B  455    CYS B  473                          1555   1555  2.04  
SSBOND  10 CYS B  650    CYS B  763                          1555   1555  2.05  
SITE     1 AC1  5 ARG A 123  TYR A 548  SER A 631  HIS A 741                    
SITE     2 AC1  5 AIL A 901                                                     
SITE     1 AC2 11 ARG A 123  GLU A 203  GLU A 204  ILE A 205                    
SITE     2 AC2 11 PHE A 355  SER A 631  TYR A 663  TYR A 667                    
SITE     3 AC2 11 ASN A 711  VAL A 712  SO4 A 801                               
CRYST1  208.349  208.349  208.349  90.00  90.00  90.00 P 21 3       24          
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      0.004800  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004800  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004800        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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