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LongText Report for: 3Q8W-pdb

Name Class
3Q8W-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           07-JAN-11   3Q8W              
TITLE     A B-AMINOACYL CONTAINING THIAZOLIDINE DERIVATIVE AND DPPIV COMPLEX    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN (UNP RESIDUES 39-764);                
COMPND   5 SYNONYM: ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,    
COMPND   6 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,     
COMPND   7 TP103, DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE IV 
COMPND   8 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM, DIPEPTIDYL       
COMPND   9 PEPTIDASE IV SOLUBLE FORM;                                           
COMPND  10 EC: 3.4.14.5;                                                        
COMPND  11 ENGINEERED: 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: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HIGH-FIVE;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACGP67A                                  
KEYWDS    ROSSMANN FOLD, HYDROLASE, MEMBRANE, HYDROLASE-HYDROLASE INHIBITOR     
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.O.LEE,D.H.SONG                                                      
REVDAT   1   16-MAR-11 3Q8W    0                                                
JRNL        AUTH   W.S.PARK,S.K.KANG,M.A.JUN,M.S.SHIN,K.Y.KIM,S.D.RHEE,M.A.BAE, 
JRNL        AUTH 2 M.S.KIM,K.R.KIM,N.S.KANG,S.E.YOO,J.O.LEE,D.H.SONG,           
JRNL        AUTH 3 P.SILINSKI,S.E.SCHNEIDER,J.H.AHN,S.S.KIM                     
JRNL        TITL   DISCOVERY OF B-AMINOACYL CONTAINING THIAZOLIDINE DERIVATIVES 
JRNL        TITL 2 AS POTENT AND SELECTIVE DIPEPTIDYL PEPTIDASE IV INHIBITORS   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.64 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.47                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 65144.690                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 20002                          
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 SET) : 0.282                           
REMARK   3   FREE R VALUE                     : 0.324                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1972                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.83                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 66.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2319                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3690                       
REMARK   3   BIN FREE R VALUE                    : 0.4010                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 220                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.027                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11896                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 76                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 69.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -27.56000                                            
REMARK   3    B22 (A**2) : -11.14000                                            
REMARK   3    B33 (A**2) : 38.70000                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.59                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.87                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.71                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.97                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.30                                                 
REMARK   3   BSOL        : 13.25                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  5  : 66223.PARAM                                    
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  5   : 66223.TOP                                      
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3Q8W COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063341.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-JAN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 103                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 4A                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
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          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20014                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
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     (%) : 89.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.23600                            
REMARK 200   FOR SHELL         : 11.000                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.0, 22 % (W/V) PEG        
REMARK 280  4000, 0.3M NAACETATE , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE   
REMARK 280  295K                                                                
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       59.20600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.55950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       62.25050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.55950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.20600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       62.25050            
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: 4350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 57150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A   765                                                      
REMARK 465     HIS A   766                                                      
REMARK 465     HIS A   767                                                      
REMARK 465     HIS A   768                                                      
REMARK 465     HIS A   769                                                      
REMARK 465     HIS A   770                                                      
REMARK 465     HIS B   765                                                      
REMARK 465     HIS B   766                                                      
REMARK 465     HIS B   767                                                      
REMARK 465     HIS B   768                                                      
REMARK 465     HIS B   769                                                      
REMARK 465     HIS B   770                                                      
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    ARG A  40      155.20     62.93                                   
REMARK 500    LYS A  41     -167.39   -115.63                                   
REMARK 500    TYR A  48      -71.63    -94.10                                   
REMARK 500    ASN A  51       80.23     51.77                                   
REMARK 500    LEU A  57     -146.00   -103.57                                   
REMARK 500    TYR A  58       66.55    173.82                                   
REMARK 500    SER A  64     -145.40   -154.38                                   
REMARK 500    HIS A  66       43.09   -152.83                                   
REMARK 500    GLN A  72       36.59   -145.21                                   
REMARK 500    GLU A  73      -66.98     68.13                                   
REMARK 500    ASN A  74      -86.27    -74.89                                   
REMARK 500    ALA A  81      -42.31    -28.96                                   
REMARK 500    GLU A  82     -114.66    -78.71                                   
REMARK 500    SER A  86      102.91    -55.35                                   
REMARK 500    GLU A  97       76.19    -68.48                                   
REMARK 500    ASN A 119       30.13     73.91                                   
REMARK 500    GLN A 123      -75.26   -120.70                                   
REMARK 500    TRP A 124     -146.30   -111.72                                   
REMARK 500    ARG A 140       49.90     38.46                                   
REMARK 500    THR A 144      -50.81   -131.43                                   
REMARK 500    TRP A 154      141.66   -172.24                                   
REMARK 500    ASN A 170       36.28     70.65                                   
REMARK 500    PRO A 181     -124.97    -61.59                                   
REMARK 500    TRP A 187      -11.50   -142.20                                   
REMARK 500    ASP A 192       29.25     43.16                                   
REMARK 500    ILE A 193      -68.39   -149.67                                   
REMARK 500    ASP A 200     -157.92    -68.58                                   
REMARK 500    GLU A 204      -65.18    -91.19                                   
REMARK 500    SER A 212       90.06    -56.28                                   
REMARK 500    PRO A 218      -56.96    -27.62                                   
REMARK 500    SER A 242     -158.10     48.87                                   
REMARK 500    GLU A 244      -18.96    -42.71                                   
REMARK 500    PRO A 249      162.03    -49.36                                   
REMARK 500    TYR A 256      101.73   -165.23                                   
REMARK 500    ALA A 259      125.78    -30.76                                   
REMARK 500    ALA A 261     -164.28    -78.78                                   
REMARK 500    THR A 273       -3.87    -59.33                                   
REMARK 500    VAL A 279      -32.19   -144.94                                   
REMARK 500    THR A 280      -96.92    108.64                                   
REMARK 500    THR A 288     -151.47   -119.48                                   
REMARK 500    ALA A 289     -169.45     51.34                                   
REMARK 500    CYS A 301      -79.49    -55.45                                   
REMARK 500    ALA A 306      -47.39   -135.63                                   
REMARK 500    GLN A 320       23.21    -68.43                                   
REMARK 500    ALA A 342       25.36    -70.40                                   
REMARK 500    ARG A 358      147.96    161.98                                   
REMARK 500    ASN A 377     -162.55   -101.91                                   
REMARK 500    GLU A 378      -70.65    -56.80                                   
REMARK 500    GLU A 379       -4.71    -56.21                                   
REMARK 500    ILE A 384       84.74    -52.73                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     193 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZV A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZV B 1                   
DBREF  3Q8W A   39   764  UNP    P27487   DPP4_HUMAN      39    764             
DBREF  3Q8W B   39   764  UNP    P27487   DPP4_HUMAN      39    764             
SEQADV 3Q8W HIS A  765  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q8W HIS A  766  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q8W HIS A  767  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q8W HIS A  768  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q8W HIS A  769  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q8W HIS A  770  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q8W HIS B  765  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q8W HIS B  766  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q8W HIS B  767  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q8W HIS B  768  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q8W HIS B  769  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q8W HIS B  770  UNP  P27487              EXPRESSION TAG                 
SEQRES   1 A  732  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 A  732  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 A  732  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 A  732  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 A  732  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 A  732  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 A  732  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 A  732  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 A  732  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 A  732  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 A  732  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 A  732  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 A  732  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 A  732  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 A  732  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 A  732  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 A  732  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 A  732  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 A  732  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 A  732  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 A  732  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 A  732  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 A  732  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 A  732  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 A  732  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 A  732  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 A  732  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 A  732  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 A  732  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 A  732  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 A  732  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 A  732  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 A  732  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 A  732  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 A  732  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 A  732  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 A  732  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 A  732  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 A  732  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 A  732  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 A  732  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 A  732  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 A  732  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 A  732  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 A  732  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 A  732  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 A  732  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 A  732  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 A  732  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 A  732  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 A  732  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 A  732  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 A  732  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 A  732  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 A  732  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 A  732  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER HIS HIS          
SEQRES  57 A  732  HIS HIS HIS HIS                                              
SEQRES   1 B  732  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 B  732  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 B  732  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 B  732  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 B  732  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 B  732  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 B  732  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 B  732  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 B  732  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 B  732  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 B  732  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 B  732  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 B  732  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 B  732  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 B  732  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 B  732  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 B  732  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 B  732  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 B  732  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 B  732  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 B  732  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 B  732  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 B  732  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 B  732  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 B  732  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 B  732  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 B  732  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 B  732  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 B  732  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 B  732  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 B  732  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 B  732  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 B  732  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 B  732  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 B  732  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 B  732  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 B  732  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 B  732  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 B  732  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 B  732  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 B  732  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 B  732  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 B  732  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 B  732  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 B  732  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 B  732  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 B  732  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 B  732  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 B  732  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 B  732  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 B  732  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 B  732  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 B  732  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 B  732  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 B  732  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 B  732  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER HIS HIS          
SEQRES  57 B  732  HIS HIS HIS HIS                                              
HET    AZV  A   1      38                                                       
HET    AZV  B   1      38                                                       
HETNAM     AZV N-(4-{[({(2R)-3-[(3R)-3-AMINO-4-(2,4,5-                          
HETNAM   2 AZV  TRIFLUOROPHENYL)BUTANOYL]-1,3-THIAZOLIDIN-2-                    
HETNAM   3 AZV  YL}CARBONYL)AMINO]METHYL}PHENYL)-D-VALINE                       
FORMUL   3  AZV    2(C26 H31 F3 N4 O4 S)                                        
HELIX    1   1 THR A   44  LYS A   50  1                                   7    
HELIX    2   2 ASN A   92  ASP A   96  5                                   5    
HELIX    3   3 TRP A  201  GLU A  206  1                                   6    
HELIX    4   4 ASP A  274  VAL A  279  5                                   6    
HELIX    5   5 PRO A  290  ILE A  295  1                                   6    
HELIX    6   6 LEU A  340  GLN A  344  5                                   5    
HELIX    7   7 GLU A  421  MET A  425  5                                   5    
HELIX    8   8 ASN A  497  MET A  503  1                                   7    
HELIX    9   9 ASN A  562  THR A  570  1                                   9    
HELIX   10  10 GLY A  587  HIS A  592  1                                   6    
HELIX   11  11 ALA A  593  ASN A  595  5                                   3    
HELIX   12  12 THR A  600  LYS A  615  1                                  16    
HELIX   13  13 SER A  630  GLY A  641  1                                  12    
HELIX   14  14 ARG A  658  TYR A  662  5                                   5    
HELIX   15  15 ASP A  663  GLY A  672  1                                  10    
HELIX   16  16 ASN A  679  ARG A  684  1                                   6    
HELIX   17  17 ARG A  691  LYS A  696  5                                   6    
HELIX   18  18 HIS A  712  GLY A  727  1                                  16    
HELIX   19  19 SER A  744  LYS A  760  1                                  17    
HELIX   20  20 THR B   44  LYS B   50  1                                   7    
HELIX   21  21 ASN B   92  ASP B   96  5                                   5    
HELIX   22  22 TRP B  201  GLU B  206  1                                   6    
HELIX   23  23 ASP B  274  VAL B  279  5                                   6    
HELIX   24  24 PRO B  290  ILE B  295  1                                   6    
HELIX   25  25 LEU B  340  GLN B  344  5                                   5    
HELIX   26  26 GLU B  421  MET B  425  5                                   5    
HELIX   27  27 ASN B  497  MET B  503  1                                   7    
HELIX   28  28 ASN B  562  THR B  570  1                                   9    
HELIX   29  29 GLY B  587  HIS B  592  1                                   6    
HELIX   30  30 ALA B  593  ASN B  595  5                                   3    
HELIX   31  31 THR B  600  LYS B  615  1                                  16    
HELIX   32  32 SER B  630  GLY B  641  1                                  12    
HELIX   33  33 ARG B  658  TYR B  662  5                                   5    
HELIX   34  34 ASP B  663  GLY B  672  1                                  10    
HELIX   35  35 ASN B  679  ARG B  684  1                                   6    
HELIX   36  36 ARG B  691  LYS B  696  5                                   6    
HELIX   37  37 HIS B  712  GLY B  727  1                                  16    
HELIX   38  38 SER B  744  LYS B  760  1                                  17    
SHEET    1   A 4 ARG A  61  TRP A  62  0                                        
SHEET    2   A 4 TYR A  68  LYS A  71 -1  O  LEU A  69   N  ARG A  61           
SHEET    3   A 4 ILE A  76  PHE A  79 -1  O  LEU A  77   N  TYR A  70           
SHEET    4   A 4 SER A  87  LEU A  90 -1  O  SER A  87   N  VAL A  78           
SHEET    1   B 4 ASP A 104  ILE A 107  0                                        
SHEET    2   B 4 PHE A 113  LYS A 122 -1  O  GLU A 117   N  ASP A 104           
SHEET    3   B 4 TYR A 128  ASP A 136 -1  O  TYR A 135   N  ILE A 114           
SHEET    4   B 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1   C 4 TRP A 154  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  LYS A 267   N  GLN A 227           
SHEET    4   E 4 SER A 284  ILE A 287 -1  O  ILE A 287   N  PHE A 268           
SHEET    1   F 2 SER A 239  PHE A 240  0                                        
SHEET    2   F 2 LYS A 250  THR A 251 -1  O  LYS A 250   N  PHE A 240           
SHEET    1   G 4 VAL A 303  THR A 307  0                                        
SHEET    2   G 4 ARG A 310  LEU A 316 -1  O  SER A 312   N  THR A 304           
SHEET    3   G 4 TYR A 322  TYR A 330 -1  O  ASP A 326   N  LEU A 313           
SHEET    4   G 4 TRP A 337  ASN A 338 -1  O  ASN A 338   N  ASP A 329           
SHEET    1   H 4 VAL A 303  THR A 307  0                                        
SHEET    2   H 4 ARG A 310  LEU A 316 -1  O  SER A 312   N  THR A 304           
SHEET    3   H 4 TYR A 322  TYR A 330 -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 3 SER A 370  SER A 376  0                                        
SHEET    2   I 3 ARG A 382  GLN A 388 -1  O  CYS A 385   N  LYS A 373           
SHEET    3   I 3 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  ILE A 418   N  ILE A 405           
SHEET    3   J 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417           
SHEET    4   J 4 VAL A 442  CYS A 444 -1  O  THR A 443   N  LYS A 433           
SHEET    1   K 2 CYS A 454  TYR A 456  0                                        
SHEET    2   K 2 GLY A 474  PRO A 475 -1  O  GLY A 474   N  GLN A 455           
SHEET    1   L 4 VAL A 459  PHE A 461  0                                        
SHEET    2   L 4 TYR A 467  CYS A 472 -1  O  GLN A 469   N  SER A 460           
SHEET    3   L 4 LEU A 479  SER A 484 -1  O  LEU A 479   N  CYS A 472           
SHEET    4   L 4 VAL A 493  GLU A 495 -1  O  GLU A 495   N  TYR A 480           
SHEET    1   M 8 SER A 511  LEU A 519  0                                        
SHEET    2   M 8 THR A 522  LEU A 530 -1  O  THR A 522   N  LEU A 519           
SHEET    3   M 8 ILE A 574  PHE A 578 -1  O  VAL A 575   N  ILE A 529           
SHEET    4   M 8 TYR A 540  ASP A 545  1  N  ASP A 545   O  ALA A 576           
SHEET    5   M 8 VAL A 619  TRP A 629  1  O  TRP A 627   N  LEU A 544           
SHEET    6   M 8 ILE A 651  VAL A 653  1  O  ILE A 651   N  GLY A 628           
SHEET    7   M 8 LEU A 701  GLY A 705  1  O  ILE A 703   N  ALA A 652           
SHEET    8   M 8 GLN A 731  TYR A 735  1  O  TYR A 735   N  HIS A 704           
SHEET    1   N 4 ARG B  61  TRP B  62  0                                        
SHEET    2   N 4 GLU B  67  LYS B  71 -1  O  LEU B  69   N  ARG B  61           
SHEET    3   N 4 ILE B  76  ASN B  80 -1  O  LEU B  77   N  TYR B  70           
SHEET    4   N 4 SER B  87  LEU B  90 -1  O  SER B  87   N  VAL B  78           
SHEET    1   O 4 ASP B 104  ILE B 107  0                                        
SHEET    2   O 4 PHE B 113  LYS B 122 -1  O  GLU B 117   N  ASP B 104           
SHEET    3   O 4 TYR B 128  ASP B 136 -1  O  TYR B 135   N  ILE B 114           
SHEET    4   O 4 GLN B 141  LEU B 142 -1  O  GLN B 141   N  ASP B 136           
SHEET    1   P 4 TRP B 154  THR B 156  0                                        
SHEET    2   P 4 LEU B 164  TRP B 168 -1  O  VAL B 167   N  TRP B 154           
SHEET    3   P 4 ASP B 171  LYS B 175 -1  O  LYS B 175   N  LEU B 164           
SHEET    4   P 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1   Q 3 ILE B 194  ASN B 196  0                                        
SHEET    2   Q 3 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   Q 3 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224           
SHEET    1   R 4 ILE B 194  ASN B 196  0                                        
SHEET    2   R 4 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   R 4 THR B 265  ASN B 272 -1  O  LYS B 267   N  GLN B 227           
SHEET    4   R 4 SER B 284  ILE B 287 -1  O  ILE B 287   N  PHE B 268           
SHEET    1   S 2 SER B 239  PHE B 240  0                                        
SHEET    2   S 2 LYS B 250  THR B 251 -1  O  LYS B 250   N  PHE B 240           
SHEET    1   T 4 VAL B 303  THR B 307  0                                        
SHEET    2   T 4 ARG B 310  LEU B 316 -1  O  SER B 312   N  THR B 304           
SHEET    3   T 4 TYR B 322  TYR B 330 -1  O  ASP B 326   N  LEU B 313           
SHEET    4   T 4 TRP B 337  ASN B 338 -1  O  ASN B 338   N  ASP B 329           
SHEET    1   U 4 VAL B 303  THR B 307  0                                        
SHEET    2   U 4 ARG B 310  LEU B 316 -1  O  SER B 312   N  THR B 304           
SHEET    3   U 4 TYR B 322  TYR B 330 -1  O  ASP B 326   N  LEU B 313           
SHEET    4   U 4 HIS B 345  MET B 348 -1  O  GLU B 347   N  SER B 323           
SHEET    1   V 4 HIS B 363  PHE B 364  0                                        
SHEET    2   V 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3   V 4 ARG B 382  GLN B 388 -1  O  CYS B 385   N  LYS B 373           
SHEET    4   V 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1   W 4 VAL B 404  LEU B 410  0                                        
SHEET    2   W 4 TYR B 414  SER B 419 -1  O  ILE B 418   N  ILE B 405           
SHEET    3   W 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4   W 4 VAL B 442  CYS B 444 -1  O  THR B 443   N  LYS B 433           
SHEET    1   X 2 CYS B 454  TYR B 456  0                                        
SHEET    2   X 2 GLY B 474  PRO B 475 -1  O  GLY B 474   N  GLN B 455           
SHEET    1   Y 4 VAL B 459  PHE B 461  0                                        
SHEET    2   Y 4 TYR B 467  CYS B 472 -1  O  GLN B 469   N  SER B 460           
SHEET    3   Y 4 LEU B 479  SER B 484 -1  O  LEU B 479   N  CYS B 472           
SHEET    4   Y 4 LYS B 489  GLU B 495 -1  O  LYS B 489   N  SER B 484           
SHEET    1   Z 8 LYS B 512  LEU B 519  0                                        
SHEET    2   Z 8 THR B 522  ILE B 529 -1  O  THR B 522   N  LEU B 519           
SHEET    3   Z 8 ILE B 574  PHE B 578 -1  O  VAL B 575   N  ILE B 529           
SHEET    4   Z 8 TYR B 540  ASP B 545  1  N  ASP B 545   O  ALA B 576           
SHEET    5   Z 8 VAL B 619  TRP B 629  1  O  TRP B 627   N  LEU B 544           
SHEET    6   Z 8 ILE B 651  VAL B 653  1  O  VAL B 653   N  GLY B 628           
SHEET    7   Z 8 LEU B 701  GLY B 705  1  O  LEU B 701   N  ALA B 652           
SHEET    8   Z 8 GLN B 731  TYR B 735  1  O  TYR B 735   N  HIS B 704           
SSBOND   1 CYS A  328    CYS A  339                          1555   1555  2.04  
SSBOND   2 CYS A  385    CYS A  394                          1555   1555  2.04  
SSBOND   3 CYS A  444    CYS A  447                          1555   1555  2.04  
SSBOND   4 CYS A  454    CYS A  472                          1555   1555  2.03  
SSBOND   5 CYS A  649    CYS A  762                          1555   1555  2.04  
SSBOND   6 CYS B  328    CYS B  339                          1555   1555  2.04  
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  2.03  
SSBOND  10 CYS B  649    CYS B  762                          1555   1555  2.05  
CISPEP   1 ALA A  289    PRO A  290          0        -0.10                     
CISPEP   2 GLY A  474    PRO A  475          0         0.19                     
CISPEP   3 ALA B  289    PRO B  290          0        -0.09                     
CISPEP   4 GLY B  474    PRO B  475          0         0.04                     
SITE     1 AC1 15 ARG A 125  GLU A 205  GLU A 206  SER A 209                    
SITE     2 AC1 15 PHE A 357  TYR A 547  TRP A 629  SER A 630                    
SITE     3 AC1 15 TYR A 631  VAL A 656  TYR A 662  TYR A 666                    
SITE     4 AC1 15 ASN A 710  VAL A 711  HIS A 740                               
SITE     1 AC2 15 ARG B 125  GLU B 205  GLU B 206  SER B 209                    
SITE     2 AC2 15 PHE B 357  TYR B 547  TRP B 629  SER B 630                    
SITE     3 AC2 15 TYR B 631  VAL B 656  TYR B 662  TYR B 666                    
SITE     4 AC2 15 ASN B 710  VAL B 711  HIS B 740                               
CRYST1  118.412  124.501  133.119  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      0.008445  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008032  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007512        0.00000                         
TER    5949      SER A 764                                                      
TER   11898      SER B 764                                                      
MASTER      321    0    2   38  101    0    8    611972    2   96  114          
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.
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