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LongText Report for: 6b1e-pdb

Name Class
6b1e-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           18-SEP-17   6B1E              
TITLE     THE STRUCTURE OF DPP4 IN COMPLEX WITH VILDAGLIPTIN                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ADABP,ADENOSINE DEAMINASE COMPLEXING PROTEIN 2,ADCP-2,      
COMPND   5 DIPEPTIDYL PEPTIDASE IV,DPP IV,T-CELL ACTIVATION ANTIGEN CD26,TP103; 
COMPND   6 EC: 3.4.14.5;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DPP4, ADCP2, CD26;                                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    DIABETES, DPP4 INHIBITORS, COVALENT INHIBITORS, HYDROLASE, HYDROLASE- 
KEYWDS   2 HYDROLASE INHIBITOR COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.SCAPIN                                                              
REVDAT   1   27-SEP-17 6B1E    0                                                
JRNL        AUTH   J.P.BERGER,R.SINHAROY,A.POCAI,T.M.KELLY,G.SCAPIN,Y.-D.GAO,   
JRNL        AUTH 2 K.A.D.PRYOR,J.WU,G.J.EIERMANN,S.XU,X.ZHANG,D.A.TATOSIAN,     
JRNL        AUTH 3 A.E.WEBER,N.A.THORNBERRY,R.D.CARR                            
JRNL        TITL   A COMPARATIVE STUDY OF THE BINDING PROPERTIES, DIPEPTIDYL    
JRNL        TITL 2 PEPTIDASE-4 (DPP-4) INHIBITORY ACTIVITY AND GLUCOSE LOWERING 
JRNL        TITL 3 EFFICACY OF THE DPP-4 INHIBITORS ALOGLIPTIN, LINAGLIPTIN,    
JRNL        TITL 4 SAXAGLIPTIN, SITAGLIPTIN AND VILDAGLIPTIN IN MICE            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.77 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 187696                         
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) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.186                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9939                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.77                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.82                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 13685                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 720                          
REMARK   3   BIN FREE R VALUE                    : 0.2630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11930                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 311                                     
REMARK   3   SOLVENT ATOMS            : 1877                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.82000                                             
REMARK   3    B22 (A**2) : 0.30000                                              
REMARK   3    B33 (A**2) : 0.52000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.096         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.092         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.057         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.944         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12781 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17452 ; 1.268 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1484 ; 5.941 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   624 ;33.787 ;23.958       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2029 ;12.260 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    62 ;16.507 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1898 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9817 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    39        A   766                          
REMARK   3    RESIDUE RANGE :   L     1        L     1                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.2100  54.7980  39.4020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0545 T22:   0.0680                                     
REMARK   3      T33:   0.0618 T12:  -0.0117                                     
REMARK   3      T13:   0.0060 T23:   0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5974 L22:   0.1228                                     
REMARK   3      L33:   0.2977 L12:  -0.0020                                     
REMARK   3      L13:  -0.0224 L23:  -0.0539                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0146 S12:   0.0109 S13:   0.0179                       
REMARK   3      S21:  -0.0008 S22:  -0.0077 S23:  -0.0098                       
REMARK   3      S31:   0.0018 S32:   0.0180 S33:  -0.0069                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    39        B   766                          
REMARK   3    RESIDUE RANGE :   L     2        L     2                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.5990  60.2290  31.7840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0403 T22:   0.0992                                     
REMARK   3      T33:   0.0750 T12:  -0.0037                                     
REMARK   3      T13:   0.0107 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5016 L22:   0.1000                                     
REMARK   3      L33:   0.1994 L12:  -0.0404                                     
REMARK   3      L13:   0.1011 L23:  -0.0677                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0013 S12:  -0.0649 S13:  -0.0449                       
REMARK   3      S21:  -0.0063 S22:   0.0033 S23:   0.0040                       
REMARK   3      S31:  -0.0070 S32:  -0.0407 S33:  -0.0046                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS       
REMARK   3  HAVE BEEN ADDED IN THE RIDING POSITIONS                             
REMARK   4                                                                      
REMARK   4 6B1E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000230131.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
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) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.15                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 197793                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.770                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 136.865                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200   FOR THE DATA SET  : 19.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.49600                            
REMARK 200   FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM ACETATE, TRIS, PH       
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       59.15700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.43250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       62.87550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.43250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.15700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       62.87550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: 9570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 59900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 45.0 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   630     C20  LF7 A   801              1.57            
REMARK 500   O    HOH A  1380     O    HOH A  1623              1.94            
REMARK 500   O    HOH B  1422     O    HOH B  1486              2.01            
REMARK 500   O    HOH A  1207     O    HOH A  1632              2.05            
REMARK 500   O    HOH A  1630     O    HOH A  1685              2.13            
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  64     -169.54   -165.88                                   
REMARK 500    GLN A 123     -101.93   -107.59                                   
REMARK 500    TRP A 124     -143.67    -94.29                                   
REMARK 500    HIS A 162       32.79   -153.60                                   
REMARK 500    ILE A 193      -61.57   -131.76                                   
REMARK 500    ILE A 193      -62.36   -131.30                                   
REMARK 500    SER A 242     -165.10     66.35                                   
REMARK 500    GLN A 320       38.19    -86.03                                   
REMARK 500    LYS A 423       17.02     55.84                                   
REMARK 500    ASN A 450       81.41   -156.72                                   
REMARK 500    GLU A 521       -0.26     73.44                                   
REMARK 500    TYR A 547      -72.13   -122.93                                   
REMARK 500    ARG A 597       47.21   -143.65                                   
REMARK 500    THR A 600      -94.47   -118.97                                   
REMARK 500    SER A 630     -116.01     63.61                                   
REMARK 500    ASP A 678      -95.97   -109.01                                   
REMARK 500    ASN A 710      -71.91   -101.27                                   
REMARK 500    ASP A 739     -156.87    -98.88                                   
REMARK 500    ILE A 742       58.58     35.97                                   
REMARK 500    ASN B  74       -3.58     61.69                                   
REMARK 500    GLN B 123     -101.05   -112.19                                   
REMARK 500    TRP B 124     -146.36    -94.63                                   
REMARK 500    HIS B 162       30.94   -153.30                                   
REMARK 500    ILE B 193      -61.61   -130.83                                   
REMARK 500    SER B 242     -165.68     65.68                                   
REMARK 500    ASN B 281       87.17   -151.10                                   
REMARK 500    GLN B 320       39.20    -87.09                                   
REMARK 500    LYS B 423       17.79     58.50                                   
REMARK 500    ASP B 438       94.93   -160.04                                   
REMARK 500    ASN B 450       82.71   -151.36                                   
REMARK 500    TYR B 547      -71.98   -124.14                                   
REMARK 500    ARG B 597       46.04   -144.44                                   
REMARK 500    THR B 600      -95.87   -120.89                                   
REMARK 500    SER B 630     -112.67     64.00                                   
REMARK 500    ASP B 678      -95.47   -110.81                                   
REMARK 500    ASN B 710      -70.50   -102.68                                   
REMARK 500    ASP B 739     -157.56    -99.03                                   
REMARK 500    ILE B 742       58.23     33.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1864        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH A1865        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH A1866        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH A1867        DISTANCE =  6.63 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 811  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 490   O                                                      
REMARK 620 2 LEU A 491   O    82.2                                              
REMARK 620 3 LEU B 276   O    65.5  60.5                                        
REMARK 620 4 VAL B 279   O    65.3  58.8   1.7                                  
REMARK 620 5 HOH B1179   O   125.3  94.4  65.7  66.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LF7 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 811                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 802 bound   
REMARK 800  to ASN A 85                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  803 through NAG A 804 bound to ASN A 150                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  805 through NAG A 806 bound to ASN A 219                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 807 bound   
REMARK 800  to ASN A 229                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 808 bound   
REMARK 800  to ASN A 281                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  809 through NAG A 810 bound to ASN A 321                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  802 through NAG B 803 bound to ASN B 85                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 804 bound   
REMARK 800  to ASN B 150                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  805 through NAG B 806 bound to ASN B 219                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  807 through NAG B 808 bound to ASN B 229                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  809 through NAG B 810 bound to ASN B 281                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 811 bound   
REMARK 800  to ASN B 321                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide LF7 B 801 and SER B    
REMARK 800  630                                                                 
DBREF  6B1E A   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  6B1E B   39   766  UNP    P27487   DPP4_HUMAN      39    766             
SEQADV 6B1E THR A   39  UNP  P27487    SER    39 ENGINEERED MUTATION            
SEQADV 6B1E THR B   39  UNP  P27487    SER    39 ENGINEERED MUTATION            
SEQRES   1 A  728  THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 A  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 A  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 A  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 A  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 A  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 A  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 A  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 A  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 A  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 A  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 A  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 A  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 A  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 A  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 A  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 A  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 A  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 A  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 A  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 A  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 A  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 A  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 A  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 A  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 A  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 A  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 A  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 A  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 A  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 A  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 A  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 A  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 A  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 A  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 A  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 A  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 A  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 A  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 A  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 A  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 A  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 A  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 A  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 A  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 A  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 A  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 A  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 A  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 A  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 A  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 A  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 A  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 A  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 A  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 A  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
SEQRES   1 B  728  THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 B  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 B  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 B  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 B  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 B  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 B  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 B  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 B  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 B  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 B  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 B  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 B  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 B  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 B  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 B  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 B  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 B  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 B  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 B  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 B  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 B  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 B  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 B  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 B  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 B  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 B  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 B  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 B  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 B  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 B  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 B  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 B  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 B  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 B  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 B  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 B  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 B  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 B  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 B  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 B  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 B  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 B  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 B  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 B  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 B  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 B  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 B  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 B  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 B  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 B  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 B  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 B  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 B  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 B  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 B  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
HET    LF7  A 801      22                                                       
HET    NAG  A 802      14                                                       
HET    NAG  A 803      14                                                       
HET    NAG  A 804      14                                                       
HET    NAG  A 805      14                                                       
HET    NAG  A 806      14                                                       
HET    NAG  A 807      14                                                       
HET    NAG  A 808      14                                                       
HET    NAG  A 809      14                                                       
HET    NAG  A 810      14                                                       
HET     NA  A 811       1                                                       
HET    LF7  B 801      22                                                       
HET    NAG  B 802      14                                                       
HET    NAG  B 803      14                                                       
HET    NAG  B 804      14                                                       
HET    NAG  B 805      14                                                       
HET    NAG  B 806      14                                                       
HET    NAG  B 807      14                                                       
HET    NAG  B 808      14                                                       
HET    NAG  B 809      14                                                       
HET    NAG  B 810      14                                                       
HET    NAG  B 811      14                                                       
HETNAM     LF7 (2S)-1-{N-[(1R,3S,5R,7S)-3-HYDROXYTRICYCLO[3.3.1.1~3,            
HETNAM   2 LF7  7~]DEC-1-YL]GLYCYL}PYRROLIDINE-2-CARBONITRILE                   
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      NA SODIUM ION                                                       
HETSYN     LF7 VILDAGLIPTIN                                                     
FORMUL   3  LF7    2(C17 H25 N3 O2)                                             
FORMUL   4  NAG    19(C8 H15 N O6)                                              
FORMUL  10   NA    NA 1+                                                        
FORMUL  18  HOH   *1877(H2 O)                                                   
HELIX    1 AA1 THR A   44  ASN A   51  1                                   8    
HELIX    2 AA2 GLU A   91  ASP A   96  5                                   6    
HELIX    3 AA3 ASP A  200  VAL A  207  1                                   8    
HELIX    4 AA4 ASP A  274  LEU A  276  5                                   3    
HELIX    5 AA5 PRO A  290  ILE A  295  1                                   6    
HELIX    6 AA6 VAL A  341  GLN A  344  5                                   4    
HELIX    7 AA7 GLU A  421  MET A  425  5                                   5    
HELIX    8 AA8 ASN A  497  GLN A  505  1                                   9    
HELIX    9 AA9 ASN A  562  THR A  570  1                                   9    
HELIX   10 AB1 GLY A  587  HIS A  592  1                                   6    
HELIX   11 AB2 ALA A  593  ASN A  595  5                                   3    
HELIX   12 AB3 THR A  600  LYS A  615  1                                  16    
HELIX   13 AB4 SER A  630  GLY A  641  1                                  12    
HELIX   14 AB5 ARG A  658  TYR A  662  5                                   5    
HELIX   15 AB6 ASP A  663  GLY A  672  1                                  10    
HELIX   16 AB7 ASN A  679  SER A  686  1                                   8    
HELIX   17 AB8 VAL A  688  VAL A  698  5                                  11    
HELIX   18 AB9 HIS A  712  VAL A  726  1                                  15    
HELIX   19 AC1 SER A  744  PHE A  763  1                                  20    
HELIX   20 AC2 THR B   44  ASN B   51  1                                   8    
HELIX   21 AC3 ASP B  200  VAL B  207  1                                   8    
HELIX   22 AC4 ASP B  274  LEU B  276  5                                   3    
HELIX   23 AC5 PRO B  290  ILE B  295  1                                   6    
HELIX   24 AC6 VAL B  341  GLN B  344  5                                   4    
HELIX   25 AC7 GLU B  421  MET B  425  5                                   5    
HELIX   26 AC8 ASN B  497  GLN B  505  1                                   9    
HELIX   27 AC9 ASN B  562  THR B  570  1                                   9    
HELIX   28 AD1 GLY B  587  HIS B  592  1                                   6    
HELIX   29 AD2 ALA B  593  ASN B  595  5                                   3    
HELIX   30 AD3 THR B  600  MET B  616  1                                  17    
HELIX   31 AD4 SER B  630  GLY B  641  1                                  12    
HELIX   32 AD5 ARG B  658  TYR B  662  5                                   5    
HELIX   33 AD6 ASP B  663  GLY B  672  1                                  10    
HELIX   34 AD7 ASN B  679  SER B  686  1                                   8    
HELIX   35 AD8 VAL B  688  VAL B  698  5                                  11    
HELIX   36 AD9 HIS B  712  VAL B  726  1                                  15    
HELIX   37 AE1 SER B  744  PHE B  763  1                                  20    
SHEET    1 AA1 2 LYS A  41  THR A  42  0                                        
SHEET    2 AA1 2 VAL A 507  GLN A 508  1  O  GLN A 508   N  LYS A  41           
SHEET    1 AA2 4 ARG A  61  TRP A  62  0                                        
SHEET    2 AA2 4 GLU A  67  GLN A  72 -1  O  LEU A  69   N  ARG A  61           
SHEET    3 AA2 4 ASN A  75  ASN A  80 -1  O  ASN A  75   N  GLN A  72           
SHEET    4 AA2 4 SER A  86  LEU A  90 -1  O  PHE A  89   N  ILE A  76           
SHEET    1 AA3 4 ILE A 102  ILE A 107  0                                        
SHEET    2 AA3 4 PHE A 113  LYS A 122 -1  O  LEU A 115   N  SER A 106           
SHEET    3 AA3 4 TYR A 128  ASP A 136 -1  O  ASP A 133   N  LEU A 116           
SHEET    4 AA3 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1 AA4 4 THR A 152  TRP A 157  0                                        
SHEET    2 AA4 4 LEU A 164  TRP A 168 -1  O  VAL A 167   N  GLN A 153           
SHEET    3 AA4 4 ASP A 171  LYS A 175 -1  O  TYR A 173   N  TYR A 166           
SHEET    4 AA4 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174           
SHEET    1 AA5 3 ILE A 194  ASN A 196  0                                        
SHEET    2 AA5 3 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3 AA5 3 LEU A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224           
SHEET    1 AA6 4 ILE A 194  ASN A 196  0                                        
SHEET    2 AA6 4 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3 AA6 4 THR A 265  ASN A 272 -1  O  PHE A 269   N  TYR A 225           
SHEET    4 AA6 4 SER A 284  GLN A 286 -1  O  ILE A 285   N  VAL A 270           
SHEET    1 AA7 2 LEU A 235  PHE A 240  0                                        
SHEET    2 AA7 2 LYS A 250  PRO A 255 -1  O  VAL A 252   N  TYR A 238           
SHEET    1 AA8 4 HIS A 298  THR A 307  0                                        
SHEET    2 AA8 4 ARG A 310  ARG A 317 -1  O  ARG A 310   N  ALA A 306           
SHEET    3 AA8 4 TYR A 322  TYR A 330 -1  O  CYS A 328   N  ILE A 311           
SHEET    4 AA8 4 TRP A 337  CYS A 339 -1  O  ASN A 338   N  ASP A 329           
SHEET    1 AA9 4 HIS A 298  THR A 307  0                                        
SHEET    2 AA9 4 ARG A 310  ARG A 317 -1  O  ARG A 310   N  ALA A 306           
SHEET    3 AA9 4 TYR A 322  TYR A 330 -1  O  CYS A 328   N  ILE A 311           
SHEET    4 AA9 4 HIS A 345  MET A 348 -1  O  GLU A 347   N  SER A 323           
SHEET    1 AB1 4 HIS A 363  PHE A 364  0                                        
SHEET    2 AB1 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363           
SHEET    3 AB1 4 ARG A 382  GLN A 388 -1  O  PHE A 387   N  PHE A 371           
SHEET    4 AB1 4 THR A 395  PHE A 396 -1  O  THR A 395   N  TYR A 386           
SHEET    1 AB2 4 VAL A 404  LEU A 410  0                                        
SHEET    2 AB2 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  ALA A 409           
SHEET    3 AB2 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417           
SHEET    4 AB2 4 VAL A 442  CYS A 444 -1  O  THR A 443   N  LYS A 433           
SHEET    1 AB3 4 TYR A 457  PHE A 461  0                                        
SHEET    2 AB3 4 TYR A 467  CYS A 472 -1  O  GLN A 469   N  SER A 460           
SHEET    3 AB3 4 LEU A 479  SER A 484 -1  O  LEU A 479   N  CYS A 472           
SHEET    4 AB3 4 LYS A 489  GLU A 495 -1  O  GLU A 495   N  TYR A 480           
SHEET    1 AB4 8 SER A 511  LEU A 519  0                                        
SHEET    2 AB4 8 THR A 522  LEU A 530 -1  O  LEU A 530   N  SER A 511           
SHEET    3 AB4 8 ILE A 574  PHE A 578 -1  O  VAL A 575   N  ILE A 529           
SHEET    4 AB4 8 TYR A 540  ASP A 545  1  N  ASP A 545   O  ALA A 576           
SHEET    5 AB4 8 VAL A 619  TRP A 629  1  O  ALA A 625   N  LEU A 544           
SHEET    6 AB4 8 CYS A 649  VAL A 653  1  O  VAL A 653   N  GLY A 628           
SHEET    7 AB4 8 GLU A 699  GLY A 705  1  O  ILE A 703   N  ALA A 652           
SHEET    8 AB4 8 GLN A 731  TYR A 735  1  O  GLN A 731   N  TYR A 700           
SHEET    1 AB5 2 LYS B  41  THR B  42  0                                        
SHEET    2 AB5 2 VAL B 507  GLN B 508  1  O  GLN B 508   N  LYS B  41           
SHEET    1 AB6 4 ARG B  61  TRP B  62  0                                        
SHEET    2 AB6 4 GLU B  67  GLN B  72 -1  O  LEU B  69   N  ARG B  61           
SHEET    3 AB6 4 ASN B  75  ASN B  80 -1  O  LEU B  77   N  TYR B  70           
SHEET    4 AB6 4 SER B  86  LEU B  90 -1  O  SER B  87   N  VAL B  78           
SHEET    1 AB7 4 ILE B 102  ILE B 107  0                                        
SHEET    2 AB7 4 PHE B 113  LYS B 122 -1  O  LEU B 115   N  SER B 106           
SHEET    3 AB7 4 TYR B 128  ASP B 136 -1  O  ASP B 133   N  LEU B 116           
SHEET    4 AB7 4 GLN B 141  LEU B 142 -1  O  GLN B 141   N  ASP B 136           
SHEET    1 AB8 4 THR B 152  TRP B 157  0                                        
SHEET    2 AB8 4 LEU B 164  TRP B 168 -1  O  VAL B 167   N  GLN B 153           
SHEET    3 AB8 4 ASP B 171  LYS B 175 -1  O  TYR B 173   N  TYR B 166           
SHEET    4 AB8 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1 AB9 3 ILE B 194  ASN B 196  0                                        
SHEET    2 AB9 3 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3 AB9 3 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224           
SHEET    1 AC1 4 ILE B 194  ASN B 196  0                                        
SHEET    2 AC1 4 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3 AC1 4 THR B 265  ASN B 272 -1  O  PHE B 269   N  TYR B 225           
SHEET    4 AC1 4 ILE B 285  GLN B 286 -1  O  ILE B 285   N  VAL B 270           
SHEET    1 AC2 2 LEU B 235  PHE B 240  0                                        
SHEET    2 AC2 2 LYS B 250  PRO B 255 -1  O  VAL B 252   N  TYR B 238           
SHEET    1 AC3 4 HIS B 298  THR B 307  0                                        
SHEET    2 AC3 4 ARG B 310  ARG B 317 -1  O  ARG B 310   N  ALA B 306           
SHEET    3 AC3 4 TYR B 322  ASP B 331 -1  O  CYS B 328   N  ILE B 311           
SHEET    4 AC3 4 ARG B 336  CYS B 339 -1  O  ARG B 336   N  ASP B 331           
SHEET    1 AC4 4 HIS B 298  THR B 307  0                                        
SHEET    2 AC4 4 ARG B 310  ARG B 317 -1  O  ARG B 310   N  ALA B 306           
SHEET    3 AC4 4 TYR B 322  ASP B 331 -1  O  CYS B 328   N  ILE B 311           
SHEET    4 AC4 4 HIS B 345  MET B 348 -1  O  HIS B 345   N  MET B 325           
SHEET    1 AC5 4 HIS B 363  PHE B 364  0                                        
SHEET    2 AC5 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3 AC5 4 ARG B 382  GLN B 388 -1  O  PHE B 387   N  PHE B 371           
SHEET    4 AC5 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1 AC6 4 VAL B 404  LEU B 410  0                                        
SHEET    2 AC6 4 TYR B 414  SER B 419 -1  O  TYR B 416   N  ALA B 409           
SHEET    3 AC6 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4 AC6 4 ASP B 438  CYS B 444 -1  O  THR B 443   N  LYS B 433           
SHEET    1 AC7 4 TYR B 457  PHE B 461  0                                        
SHEET    2 AC7 4 TYR B 467  CYS B 472 -1  O  GLN B 469   N  SER B 460           
SHEET    3 AC7 4 LEU B 479  SER B 484 -1  O  LEU B 479   N  CYS B 472           
SHEET    4 AC7 4 LYS B 489  GLU B 495 -1  O  GLU B 495   N  TYR B 480           
SHEET    1 AC8 8 SER B 511  LEU B 519  0                                        
SHEET    2 AC8 8 THR B 522  LEU B 530 -1  O  THR B 522   N  LEU B 519           
SHEET    3 AC8 8 ILE B 574  PHE B 578 -1  O  VAL B 575   N  ILE B 529           
SHEET    4 AC8 8 TYR B 540  VAL B 546  1  N  LEU B 543   O  ILE B 574           
SHEET    5 AC8 8 VAL B 619  TRP B 629  1  O  TRP B 627   N  VAL B 546           
SHEET    6 AC8 8 CYS B 649  VAL B 653  1  O  VAL B 653   N  GLY B 628           
SHEET    7 AC8 8 GLU B 699  GLY B 705  1  O  LEU B 701   N  ALA B 652           
SHEET    8 AC8 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  TYR B 700           
SSBOND   1 CYS A  328    CYS A  339                          1555   1555  2.06  
SSBOND   2 CYS A  385    CYS A  394                          1555   1555  2.06  
SSBOND   3 CYS A  444    CYS A  447                          1555   1555  2.01  
SSBOND   4 CYS A  454    CYS A  472                          1555   1555  2.09  
SSBOND   5 CYS A  649    CYS A  762                          1555   1555  2.07  
SSBOND   6 CYS B  328    CYS B  339                          1555   1555  2.06  
SSBOND   7 CYS B  385    CYS B  394                          1555   1555  2.05  
SSBOND   8 CYS B  444    CYS B  447                          1555   1555  2.04  
SSBOND   9 CYS B  454    CYS B  472                          1555   1555  2.08  
SSBOND  10 CYS B  649    CYS B  762                          1555   1555  2.07  
LINK         ND2 ASN A  85                 C1  NAG A 802     1555   1555  1.44  
LINK         ND2 ASN A 150                 C1  NAG A 803     1555   1555  1.44  
LINK         ND2 ASN A 219                 C1  NAG A 805     1555   1555  1.44  
LINK         ND2 ASN A 229                 C1  NAG A 807     1555   1555  1.43  
LINK         ND2 ASN A 281                 C1  NAG A 808     1555   1555  1.45  
LINK         ND2 ASN A 321                 C1  NAG A 809     1555   1555  1.44  
LINK         O   GLY A 490                NA    NA A 811     1555   1555  2.42  
LINK         O   LEU A 491                NA    NA A 811     1555   1555  2.48  
LINK         ND2 ASN B  85                 C1  NAG B 802     1555   1555  1.44  
LINK         ND2 ASN B 150                 C1  NAG B 804     1555   1555  1.45  
LINK         ND2 ASN B 219                 C1  NAG B 805     1555   1555  1.43  
LINK         ND2 ASN B 229                 C1  NAG B 807     1555   1555  1.44  
LINK         ND2 ASN B 281                 C1  NAG B 809     1555   1555  1.45  
LINK         ND2 ASN B 321                 C1  NAG B 811     1555   1555  1.44  
LINK         OG  SER B 630                 C20 LF7 B 801     1555   1555  1.42  
LINK         O4  NAG A 803                 C1  NAG A 804     1555   1555  1.46  
LINK         O4  NAG A 805                 C1  NAG A 806     1555   1555  1.44  
LINK         O4  NAG A 809                 C1  NAG A 810     1555   1555  1.44  
LINK         O4  NAG B 802                 C1  NAG B 803     1555   1555  1.46  
LINK         O4  NAG B 805                 C1  NAG B 806     1555   1555  1.44  
LINK         O4  NAG B 807                 C1  NAG B 808     1555   1555  1.44  
LINK         O4  NAG B 809                 C1  NAG B 810     1555   1555  1.44  
LINK         O   LEU B 276                NA    NA A 811     1555   2564  2.25  
LINK         O   VAL B 279                NA    NA A 811     1555   2564  2.33  
LINK        NA    NA A 811                 O   HOH B1179     1555   2565  2.37  
CISPEP   1 GLY A  474    PRO A  475          0         8.91                     
CISPEP   2 GLY B  474    PRO B  475          0         6.96                     
SITE     1 AC1 13 ARG A 125  GLU A 205  GLU A 206  TYR A 547                    
SITE     2 AC1 13 SER A 630  TYR A 631  VAL A 656  TYR A 662                    
SITE     3 AC1 13 TYR A 666  ASN A 710  VAL A 711  HOH A1133                    
SITE     4 AC1 13 HOH A1226                                                     
SITE     1 AC2  5 GLY A 490  LEU A 491  LEU B 276  VAL B 279                    
SITE     2 AC2  5 HOH B1179                                                     
SITE     1 AC3  8 GLU A  67  VAL A  78  ASN A  85  SER A  86                    
SITE     2 AC3  8 SER A  87  HOH A 909  HOH A 920  HOH A1268                    
SITE     1 AC4  3 ILE A 148  ASN A 150  HOH A1300                               
SITE     1 AC5 12 ASN A 219  THR A 221  GLN A 308  GLU A 309                    
SITE     2 AC5 12 TYR A 330  GLU A 332  HOH A 901  HOH A 915                    
SITE     3 AC5 12 HOH A 935  HOH A1078  HOH A1235  HOH A1439                    
SITE     1 AC6  7 ILE A 194  ASN A 229  THR A 231  GLU A 232                    
SITE     2 AC6  7 HOH A 972  HOH A1302  HOH A1331                               
SITE     1 AC7  8 TRP A 187  VAL A 279  ASN A 281  HOH A 934                    
SITE     2 AC7  8 HOH A 961  HOH A1405  HOH A1585  HOH A1596                    
SITE     1 AC8  2 ASN A 321  SER A 349                                          
SITE     1 AC9  6 VAL B  78  ASN B  85  SER B  86  SER B  87                    
SITE     2 AC9  6 HOH B 905  HOH B1257                                          
SITE     1 AD1  3 ARG B 147  ILE B 148  ASN B 150                               
SITE     1 AD2 11 ASN B 219  THR B 221  PHE B 222  ASN B 272                    
SITE     2 AD2 11 GLN B 308  GLU B 309  TYR B 330  HOH B 911                    
SITE     3 AD2 11 HOH B 975  HOH B1256  HOH B1414                               
SITE     1 AD3  9 ILE B 194  ASN B 229  THR B 231  GLU B 232                    
SITE     2 AD3  9 HOH B1013  HOH B1018  HOH B1048  HOH B1381                    
SITE     3 AD3  9 HOH B1527                                                     
SITE     1 AD4 11 ASN A 450  TRP B 187  THR B 188  ASN B 281                    
SITE     2 AD4 11 HOH B 901  HOH B 904  HOH B 926  HOH B 965                    
SITE     3 AD4 11 HOH B1150  HOH B1178  HOH B1504                               
SITE     1 AD5  7 ILE B 319  ASN B 321  SER B 349  THR B 350                    
SITE     2 AD5  7 HOH B 970  HOH B1297  HOH B1473                               
SITE     1 AD6 20 ARG B 125  GLU B 205  GLU B 206  TYR B 547                    
SITE     2 AD6 20 TRP B 629  TYR B 631  GLY B 632  GLY B 633                    
SITE     3 AD6 20 TYR B 634  VAL B 653  ALA B 654  PRO B 655                    
SITE     4 AD6 20 VAL B 656  TYR B 662  TYR B 666  ASN B 710                    
SITE     5 AD6 20 VAL B 711  HIS B 740  HOH B 978  HOH B1253                    
CRYST1  118.314  125.751  136.865  90.00  90.00  90.00 P 21 21 21    8          
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      0.008452  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007952  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007306        0.00000                         
TER    6029      PRO A 766                                                      
TER   12033      PRO B 766                                                      
MASTER      449    0   22   37  102    0   36    614118    2  346  112          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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