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LongText Report for: 2RIP-pdb

Name Class
2RIP-pdb
HEADER    HYDROLASE                               12-OCT-07   2RIP              
TITLE     STRUCTURE OF DPPIV IN COMPLEX WITH AN INHIBITOR                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DIPEPTIDYL PEPTIDASE IV; DPP IV; T-CELL                     
COMPND   5 ACTIVATION ANTIGEN CD26; TP103; ADENOSINE DEAMINASE                  
COMPND   6 COMPLEXING PROTEIN 2; ADABP;                                         
COMPND   7 EC: 3.4.14.5;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: DPPIV;                                                         
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS                                
KEYWDS    DPPIV, DIABETES, DRUG DESIGN, AMINOPEPTIDASE, GLYCOPROTEIN,           
KEYWDS   2 HYDROLASE, MEMBRANE, PROTEASE, SECRETED, SERINE PROTEASE,            
KEYWDS   3 SIGNAL-ANCHOR, TRANSMEMBRANE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.QIU                                                                 
REVDAT   1   18-MAR-08 2RIP    0                                                
JRNL        AUTH   J.W.CORBETT,K.DIRICO,W.SONG,B.P.BOSCOE,S.D.DORAN,            
JRNL        AUTH 2 D.BOYER,X.QIU,M.AMMIRATI,M.A.VANVOLKENBURG,                  
JRNL        AUTH 3 R.K.MCPHERSON,J.C.PARKER,E.D.COX                             
JRNL        TITL   DESIGN AND SYNTHESIS OF POTENT AMIDO- AND                    
JRNL        TITL 2 BENZYL-SUBSTITUTED                                           
JRNL        TITL 3 CIS-3-AMINO-4-(2-CYANOPYRROLIDIDE)PYRROLIDINYL               
JRNL        TITL 4 DPP-IV INHIBITORS.                                           
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  17  6707 2007              
JRNL        REFN   ASTM BMCLE8  UK ISSN 0960-894X                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.90 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 20047                          
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) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.293                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1095                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1170                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 75                           
REMARK   3   BIN FREE R VALUE                    : 0.4090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 6158                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 69.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.53000                                              
REMARK   3    B22 (A**2) : 1.53000                                              
REMARK   3    B33 (A**2) : -3.06000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.496         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.372         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.972        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.911                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.845                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6319 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8608 ; 1.399 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   728 ; 6.724 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   926 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4824 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2607 ; 0.229 ; 0.200       
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):   192 ; 0.158 ; 0.200       
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):    48 ; 0.226 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.203 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3632 ; 0.589 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5892 ; 1.129 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2687 ; 1.396 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2716 ; 2.440 ; 4.500       
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 : 0                                 
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 0                                          
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2RIP COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.                               
REMARK 100 THE RCSB ID CODE IS RCSB044905.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JAN-2004                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.00                               
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                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39722                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.12500                            
REMARK 200  R SYM                      (I) : 0.12500                            
REMARK 200   FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.00580                            
REMARK 200  R SYM FOR SHELL            (I) : 0.00580                            
REMARK 200   FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1WCY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%PEG, PH 8, VAPOR DIFFUSION,           
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,1/2+Z                                             
REMARK 290       3555   1/2-Y,1/2+X,3/4+Z                                       
REMARK 290       4555   1/2+Y,1/2-X,1/4+Z                                       
REMARK 290       5555   1/2-X,1/2+Y,3/4-Z                                       
REMARK 290       6555   1/2+X,1/2-Y,1/4-Z                                       
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,1/2-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      204.61000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       34.61000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       34.61000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      306.91500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       34.61000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       34.61000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      102.30500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       34.61000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       34.61000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      306.91500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       34.61000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       34.61000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      102.30500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      204.61000            
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: 9010 ANGSTROM**2                          
REMARK 350 TOTAL SURFACE AREA FOR THE COMPLEX: 61780 ANGSTROM**2                
REMARK 350 GAIN IN SOLVENT FREE ENERGY: 49 KCAL/MOL                             
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000      138.44000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      138.44000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      204.61000            
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 NUCELIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  96   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 171   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 243   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP A 302   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  51       51.08     76.38                                   
REMARK 500    SER A  64     -153.51   -157.37                                   
REMARK 500    GLU A  73      -93.35     63.01                                   
REMARK 500    ASN A  74       -2.69   -140.48                                   
REMARK 500    ASN A  92       26.12    -79.27                                   
REMARK 500    PHE A  98      -22.54   -151.20                                   
REMARK 500    TYR A 105      147.90   -172.70                                   
REMARK 500    PRO A 109       38.30    -68.41                                   
REMARK 500    ASP A 110       20.48   -159.34                                   
REMARK 500    GLN A 123     -100.35   -111.10                                   
REMARK 500    TRP A 124     -149.89    -88.31                                   
REMARK 500    PRO A 178       -1.04    -50.79                                   
REMARK 500    ASN A 179       20.86   -149.39                                   
REMARK 500    ASP A 192       -3.30     65.05                                   
REMARK 500    VAL A 207      -56.80   -126.98                                   
REMARK 500    SER A 242     -165.29     70.40                                   
REMARK 500    VAL A 279      -47.65   -132.10                                   
REMARK 500    ALA A 306      -62.69    -95.02                                   
REMARK 500    GLN A 320       32.67    -75.27                                   
REMARK 500    GLU A 332      -74.64    -52.86                                   
REMARK 500    LYS A 423       16.20     53.51                                   
REMARK 500    ASN A 450       34.62   -152.07                                   
REMARK 500    PRO A 451      -34.82    -30.99                                   
REMARK 500    ALA A 465       33.10     73.22                                   
REMARK 500    PRO A 478      130.11    -32.60                                   
REMARK 500    LEU A 491      -66.32    -94.44                                   
REMARK 500    ASN A 520       44.99     35.74                                   
REMARK 500    TYR A 547      -69.04   -132.82                                   
REMARK 500    CYS A 551       32.08     73.22                                   
REMARK 500    ARG A 596       10.49     46.46                                   
REMARK 500    THR A 600      -79.63   -130.89                                   
REMARK 500    SER A 630     -131.86     55.78                                   
REMARK 500    GLU A 660        0.59    -66.86                                   
REMARK 500    ARG A 669      -34.80    -37.93                                   
REMARK 500    ASP A 678     -105.25    -92.72                                   
REMARK 500    ASN A 685        0.26    -63.62                                   
REMARK 500    ASN A 710      -71.50    -75.32                                   
REMARK 500    ASP A 737       -6.22     72.25                                   
REMARK 500    ASP A 739     -153.75    -99.60                                   
REMARK 500    ILE A 742       60.46     33.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1085                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 2085                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR RESIDUE A 3085                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR RESIDUE A 4085                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 4086                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 4087                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1219                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1229                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1281                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1321                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 SITE_DESCRIPTION: 34Q BINDING SITE FOR RESIDUE A 800                 
DBREF  2RIP A   38   766  UNP    P27487   DPP4_HUMAN      38    766             
SEQRES   1 A  729  ASP SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS          
SEQRES   2 A  729  ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE          
SEQRES   3 A  729  SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE          
SEQRES   4 A  729  LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE          
SEQRES   5 A  729  LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE          
SEQRES   6 A  729  ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU          
SEQRES   7 A  729  LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR          
SEQRES   8 A  729  THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN          
SEQRES   9 A  729  LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP          
SEQRES  10 A  729  VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL          
SEQRES  11 A  729  TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU          
SEQRES  12 A  729  PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE          
SEQRES  13 A  729  ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU          
SEQRES  14 A  729  VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN          
SEQRES  15 A  729  GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU          
SEQRES  16 A  729  VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER          
SEQRES  17 A  729  LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS          
SEQRES  18 A  729  ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL          
SEQRES  19 A  729  ASN THR ASP SER LEU SER SER VAL THR ASN ALA THR SER          
SEQRES  20 A  729  ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP          
SEQRES  21 A  729  HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG          
SEQRES  22 A  729  ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER          
SEQRES  23 A  729  VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG          
SEQRES  24 A  729  TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER          
SEQRES  25 A  729  THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO          
SEQRES  26 A  729  HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE          
SEQRES  27 A  729  SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN          
SEQRES  28 A  729  ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR          
SEQRES  29 A  729  TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR          
SEQRES  30 A  729  LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY          
SEQRES  31 A  729  GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR          
SEQRES  32 A  729  LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG          
SEQRES  33 A  729  CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS          
SEQRES  34 A  729  TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU          
SEQRES  35 A  729  TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG          
SEQRES  36 A  729  VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN          
SEQRES  37 A  729  ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE          
SEQRES  38 A  729  LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO          
SEQRES  39 A  729  PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU          
SEQRES  40 A  729  ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR          
SEQRES  41 A  729  VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR          
SEQRES  42 A  729  GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER          
SEQRES  43 A  729  GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG          
SEQRES  44 A  729  ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA          
SEQRES  45 A  729  ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS          
SEQRES  46 A  729  ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL          
SEQRES  47 A  729  THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS          
SEQRES  48 A  729  CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR          
SEQRES  49 A  729  TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO          
SEQRES  50 A  729  THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR          
SEQRES  51 A  729  VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR          
SEQRES  52 A  729  LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE          
SEQRES  53 A  729  GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL          
SEQRES  54 A  729  GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP          
SEQRES  55 A  729  HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR          
SEQRES  56 A  729  THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU          
SEQRES  57 A  729  PRO                                                          
MODRES 2RIP ASN A   85  ASN  GLYCOSYLATION SITE                                 
MODRES 2RIP ASN A  150  ASN  GLYCOSYLATION SITE                                 
MODRES 2RIP ASN A  219  ASN  GLYCOSYLATION SITE                                 
MODRES 2RIP ASN A  229  ASN  GLYCOSYLATION SITE                                 
MODRES 2RIP ASN A  281  ASN  GLYCOSYLATION SITE                                 
MODRES 2RIP ASN A  321  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1085      14                                                       
HET    NAG  A2085      14                                                       
HET    MAN  A3085      11                                                       
HET    MAN  A4085      11                                                       
HET    NAG  A4086      14                                                       
HET    NAG  A4087      14                                                       
HET    NAG  A1219      14                                                       
HET    NAG  A1229      14                                                       
HET    NAG  A1281      14                                                       
HET    NAG  A1321      14                                                       
HET    34Q  A 800      25                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     34Q (3R,4R)-4-(PYRROLIDIN-1-YLCARBONYL)-1-(QUINOXALIN-2-             
HETNAM   2 34Q  YLCARBONYL)PYRROLIDIN-3-AMINE                                   
HETSYN     NAG NAG                                                              
FORMUL   2  NAG    8(C8 H15 N O6)                                               
FORMUL   2  MAN    2(C6 H12 O6)                                                 
FORMUL   8  34Q    C18 H21 N5 O2                                                
FORMUL   9  HOH   *27(H2 O)                                                     
HELIX    1   1 THR A   44  ASN A   51  1                                   8    
HELIX    2   2 ASP A  200  VAL A  207  1                                   8    
HELIX    3   3 PRO A  290  ILE A  295  1                                   6    
HELIX    4   4 VAL A  341  GLN A  344  5                                   4    
HELIX    5   5 GLU A  421  MET A  425  5                                   5    
HELIX    6   6 ASN A  497  ASN A  506  1                                  10    
HELIX    7   7 ASN A  562  THR A  570  1                                   9    
HELIX    8   8 GLY A  587  HIS A  592  1                                   6    
HELIX    9   9 ALA A  593  ASN A  595  5                                   3    
HELIX   10  10 THR A  600  MET A  616  1                                  17    
HELIX   11  11 SER A  630  GLY A  641  1                                  12    
HELIX   12  12 ARG A  658  TYR A  662  5                                   5    
HELIX   13  13 ASP A  663  GLY A  672  1                                  10    
HELIX   14  14 ASN A  679  SER A  686  1                                   8    
HELIX   15  15 VAL A  688  VAL A  698  5                                  11    
HELIX   16  16 HIS A  712  ASP A  725  1                                  14    
HELIX   17  17 SER A  744  SER A  764  1                                  21    
SHEET    1   A 4 LEU A  60  TRP A  62  0                                        
SHEET    2   A 4 GLU A  67  GLN A  72 -1  O  LEU A  69   N  ARG A  61           
SHEET    3   A 4 ASN A  75  ASN A  80 -1  O  LEU A  77   N  TYR A  70           
SHEET    4   A 4 SER A  86  LEU A  90 -1  O  LEU A  90   N  ILE A  76           
SHEET    1   B 4 ILE A 102  ILE A 107  0                                        
SHEET    2   B 4 PHE A 113  LYS A 122 -1  O  LEU A 115   N  SER A 106           
SHEET    3   B 4 TYR A 128  ASP A 136 -1  O  SER A 131   N  TYR A 118           
SHEET    4   B 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1   C 4 THR A 152  TRP A 157  0                                        
SHEET    2   C 4 LEU A 164  TRP A 168 -1  O  VAL A 167   N  TRP A 154           
SHEET    3   C 4 ASP A 171  LYS A 175 -1  O  LYS A 175   N  LEU A 164           
SHEET    4   C 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174           
SHEET    1   D 3 ILE A 194  ASN A 196  0                                        
SHEET    2   D 3 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   D 3 LEU A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224           
SHEET    1   E 4 ILE A 194  ASN A 196  0                                        
SHEET    2   E 4 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   E 4 THR A 265  ASN A 272 -1  O  PHE A 269   N  TYR A 225           
SHEET    4   E 4 ILE A 285  GLN A 286 -1  O  ILE A 285   N  VAL A 270           
SHEET    1   F 2 LEU A 235  PHE A 240  0                                        
SHEET    2   F 2 LYS A 250  PRO A 255 -1  O  VAL A 252   N  TYR A 238           
SHEET    1   G 4 HIS A 298  THR A 307  0                                        
SHEET    2   G 4 ARG A 310  ARG A 317 -1  O  SER A 312   N  THR A 304           
SHEET    3   G 4 TYR A 322  ASP A 331 -1  O  ASP A 326   N  LEU A 313           
SHEET    4   G 4 ARG A 336  CYS A 339 -1  O  ASN A 338   N  ASP A 329           
SHEET    1   H 4 HIS A 298  THR A 307  0                                        
SHEET    2   H 4 ARG A 310  ARG A 317 -1  O  SER A 312   N  THR A 304           
SHEET    3   H 4 TYR A 322  ASP A 331 -1  O  ASP A 326   N  LEU A 313           
SHEET    4   H 4 HIS A 345  MET A 348 -1  O  GLU A 347   N  SER A 323           
SHEET    1   I 4 PRO A 362  PHE A 364  0                                        
SHEET    2   I 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363           
SHEET    3   I 4 ARG A 382  GLN A 388 -1  O  PHE A 387   N  PHE A 371           
SHEET    4   I 4 THR A 395  PHE A 396 -1  O  THR A 395   N  TYR A 386           
SHEET    1   J 4 VAL A 404  LEU A 410  0                                        
SHEET    2   J 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  GLU A 408           
SHEET    3   J 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417           
SHEET    4   J 4 ASP A 438  CYS A 444 -1  O  ASP A 438   N  GLN A 435           
SHEET    1   K 4 TYR A 457  PHE A 461  0                                        
SHEET    2   K 4 TYR A 467  CYS A 472 -1  O  ARG A 471   N  SER A 458           
SHEET    3   K 4 LEU A 479  SER A 484 -1  O  LEU A 479   N  CYS A 472           
SHEET    4   K 4 LYS A 489  GLU A 495 -1  O  LEU A 494   N  TYR A 480           
SHEET    1   L 8 SER A 511  LEU A 519  0                                        
SHEET    2   L 8 THR A 522  LEU A 530 -1  O  THR A 522   N  LEU A 519           
SHEET    3   L 8 ILE A 574  PHE A 578 -1  O  SER A 577   N  GLN A 527           
SHEET    4   L 8 TYR A 540  VAL A 546  1  N  LEU A 543   O  ILE A 574           
SHEET    5   L 8 VAL A 619  TRP A 629  1  O  ASP A 620   N  TYR A 540           
SHEET    6   L 8 CYS A 649  VAL A 653  1  O  VAL A 653   N  GLY A 628           
SHEET    7   L 8 GLU A 699  GLY A 705  1  O  GLU A 699   N  GLY A 650           
SHEET    8   L 8 GLN A 731  TYR A 735  1  O  GLN A 731   N  TYR A 700           
SSBOND   1 CYS A  328    CYS A  339                        1555   1555    2.04  
SSBOND   2 CYS A  385    CYS A  394                        1555   1555    2.07  
SSBOND   3 CYS A  444    CYS A  447                        1555   1555    2.02  
LINK         ND2 ASN A  85                 C1  NAG A1085   1555   1555    1.43  
LINK         ND2 ASN A 150                 C1  NAG A4086   1555   1555    1.45  
LINK         ND2 ASN A 219                 C1  NAG A1219   1555   1555    1.45  
LINK         ND2 ASN A 229                 C1  NAG A1229   1555   1555    1.45  
LINK         ND2 ASN A 281                 C1  NAG A1281   1555   1555    1.45  
LINK         ND2 ASN A 321                 C1  NAG A1321   1555   1555    1.45  
LINK         O4  NAG A1085                 C1  NAG A2085   1555   1555    1.45  
LINK         O4  NAG A2085                 C1  MAN A3085   1555   1555    1.44  
LINK         O6  MAN A3085                 C1  MAN A4085   1555   1555    1.44  
LINK         O4  NAG A4086                 C1  NAG A4087   1555   1555    1.44  
CISPEP   1 GLY A  474    PRO A  475          0        -1.99                     
SITE     1 AC1  7 PHE A  79  ASN A  80  ASN A  85  SER A  86                    
SITE     2 AC1  7 SER A  87  GLN A 388  THR A 395                               
SITE     1 AC3  1 HOH A  11                                                     
SITE     1 AC4  2 ASP A  38  SER A  39                                          
SITE     1 AC5  3 ARG A 147  ILE A 148  ASN A 150                               
SITE     1 AC6  1 HOH A  27                                                     
SITE     1 AC7  3 ASN A 219  GLN A 308  GLU A 309                               
SITE     1 AC8  2 ILE A 194  ASN A 229                                          
SITE     1 AC9  2 TRP A 187  ASN A 281                                          
SITE     1 BC1  2 ILE A 319  ASN A 321                                          
SITE     1 BC2  9 ARG A 125  GLU A 205  GLU A 206  SER A 209                    
SITE     2 BC2  9 PHE A 357  SER A 630  TYR A 662  TYR A 666                    
SITE     3 BC2  9 ASN A 710                                                     
CRYST1   69.220   69.220  409.220  90.00  90.00  90.00 P 43 21 2     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      0.014447  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014447  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002444        0.00000                         
TER    5973      PRO A 766                                                      
MASTER      352    0   11   17   49    0   13    6 6158    1  171   57          
END                                                                             

Send your questions or comments to :
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:
ESTHER Home Page and ACEDB Home Page
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