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LongText Report for: 3C45-pdb

Name Class
3C45-pdb
HEADER    HYDROLASE                               29-JAN-08   3C45              
TITLE     HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 IN COMPLEX WITH A                  
TITLE    2 FLUOROOLEFIN INHIBITOR                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND   5 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL                     
COMPND   6 ACTIVATION ANTIGEN CD26, TP103, ADENOSINE DEAMINASE                  
COMPND   7 COMPLEXING PROTEIN 2, ADABP;                                         
COMPND   8 EC: 3.4.14.5;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: DPP4, ADCP2, CD26;                                             
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: HI5;                                       
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PBLUEBAC4.5                               
KEYWDS    ALPHA/BETA, BETA-PROPELLER, DIMER, AMINOPEPTIDASE,                    
KEYWDS   2 GLYCOPROTEIN, HYDROLASE, MEMBRANE, PROTEASE, SECRETED,               
KEYWDS   3 SERINE PROTEASE, SIGNAL-ANCHOR, TRANSMEMBRANE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.SCAPIN,S.D.EDMONDSON,A.E.WEBER                                      
REVDAT   1   22-APR-08 3C45    0                                                
JRNL        AUTH   S.D.EDMONDSON,L.WEI,J.XU,J.SHANG,S.XU,J.PANG,                
JRNL        AUTH 2 A.CHAUDHARY,D.C.DEAN,H.HE,B.LEITING,K.A.LYONS,               
JRNL        AUTH 3 R.A.PATEL,S.B.PATEL,G.SCAPIN,J.K.WU,M.G.BECONI,              
JRNL        AUTH 4 N.A.THORNBERRY,A.E.WEBER                                     
JRNL        TITL   FLUOROOLEFINS AS AMIDE BOND MIMICS IN DIPEPTIDYL             
JRNL        TITL 2 PEPTIDASE IV INHIBITORS                                      
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  18  2409 2008              
JRNL        REFN   ASTM BMCLE8  UK ISSN 0960-894X                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.05 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX                                                  
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  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 127430                         
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6422                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 127768               
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.12                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610                       
REMARK   3   BIN FREE R VALUE                    : 0.2810                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 635                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11930                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 397                                     
REMARK   3   SOLVENT ATOMS            : 1015                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.22500                                              
REMARK   3    B22 (A**2) : -0.34200                                             
REMARK   3    B33 (A**2) : -5.88300                                             
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) : 0.23                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.18                            
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) : 0.26                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.22                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.43                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ANISOTROPIC                               
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) : 0.820 ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3C45 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 RCSB046317.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-2003                        
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                       : 32-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 128988                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.740                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.56                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNX                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1X70                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, SODIUM ACETATE, TRIS, PH        
REMARK 280  8.00, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   1/2-X,-Y,1/2+Z                                          
REMARK 290       3555   -X,1/2+Y,1/2-Z                                          
REMARK 290       4555   1/2+X,1/2-Y,-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       58.94400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.37500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       62.95450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.37500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       58.94400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       62.95450            
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: 10790 ANGSTROM**2                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: 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    TYR A  58       81.31   -150.14                                   
REMARK 500    SER A  64     -166.04   -165.20                                   
REMARK 500    GLN A 123     -104.43   -112.96                                   
REMARK 500    TRP A 124     -144.97    -88.64                                   
REMARK 500    HIS A 162       30.65   -150.86                                   
REMARK 500    ASP A 192       12.25     59.16                                   
REMARK 500    ILE A 193      -62.05   -130.91                                   
REMARK 500    SER A 242     -163.93     65.40                                   
REMARK 500    GLN A 320       38.59    -67.32                                   
REMARK 500    ARG A 358      164.24    179.34                                   
REMARK 500    ASN A 450       77.54   -169.31                                   
REMARK 500    GLU A 521       -1.54     64.86                                   
REMARK 500    LYS A 536       -9.78    -57.52                                   
REMARK 500    TYR A 547      -72.44   -127.49                                   
REMARK 500    ARG A 596       12.91     59.04                                   
REMARK 500    THR A 600      -88.74   -121.18                                   
REMARK 500    SER A 630     -122.02     63.06                                   
REMARK 500    ASP A 678      -95.85   -109.78                                   
REMARK 500    ASN A 710      -70.59    -90.40                                   
REMARK 500    ASP A 739     -157.00   -102.76                                   
REMARK 500    ILE A 742       48.95     36.89                                   
REMARK 500    SER B  64     -164.41   -167.51                                   
REMARK 500    ASN B  74      -20.04     70.66                                   
REMARK 500    GLN B 123     -103.62   -117.44                                   
REMARK 500    TRP B 124     -142.17    -91.35                                   
REMARK 500    HIS B 162       33.01   -149.60                                   
REMARK 500    ILE B 193      -60.24   -126.12                                   
REMARK 500    SER B 242     -164.93     64.58                                   
REMARK 500    GLN B 320       37.21    -65.88                                   
REMARK 500    ARG B 358      162.74    178.25                                   
REMARK 500    ASP B 438       92.09   -164.65                                   
REMARK 500    ASN B 450       76.58   -160.51                                   
REMARK 500    ARG B 492      168.20    175.37                                   
REMARK 500    TYR B 547      -71.57   -131.82                                   
REMARK 500    THR B 600      -94.71   -123.07                                   
REMARK 500    SER B 630     -120.99     64.67                                   
REMARK 500    ASP B 678      -97.74   -115.37                                   
REMARK 500    ASN B 710      -73.83    -90.40                                   
REMARK 500    ASP B 739     -158.70   -103.10                                   
REMARK 500    ILE B 742       51.23     34.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 700         0.08    SIDE_CHAIN                              
REMARK 500    TYR B 700         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A   1  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 490   O                                                      
REMARK 620 2 LEU A 491   O    82.5                                              
REMARK 620 N                    1                                               
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 1092                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1150                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1219                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1220                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1229                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1281                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1321                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1322                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1520                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2085                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2086                
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2092                
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2150                
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2219                
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2220                
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2229                
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2281                
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2282                
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2321                
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 SITE_DESCRIPTION: NA BINDING SITE FOR RESIDUE A 1                    
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 SITE_DESCRIPTION: 317 BINDING SITE FOR RESIDUE A 1521                
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 SITE_DESCRIPTION: 317 BINDING SITE FOR RESIDUE B 2                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1X70   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3C43   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2HHA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2IIT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2IIV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2OPH   RELATED DB: PDB                                   
DBREF  3C45 A   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  3C45 B   39   766  UNP    P27487   DPP4_HUMAN      39    766             
SEQADV 3C45 THR A   39  UNP  P27487    SER    39 ENGINEERED                     
SEQADV 3C45 THR B   39  UNP  P27487    SER    39 ENGINEERED                     
SEQRES   1 A  728  THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 A  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 A  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 A  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 A  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 A  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 A  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 A  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 A  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 A  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 A  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 A  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 A  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 A  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 A  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 A  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 A  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 A  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 A  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 A  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 A  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 A  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 A  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 A  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 A  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 A  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 A  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 A  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 A  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 A  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 A  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 A  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 A  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 A  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 A  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 A  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 A  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 A  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 A  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 A  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 A  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 A  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 A  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 A  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 A  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 A  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 A  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 A  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 A  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 A  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 A  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 A  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 A  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 A  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 A  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 A  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
SEQRES   1 B  728  THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 B  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 B  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 B  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 B  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 B  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 B  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 B  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 B  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 B  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 B  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 B  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 B  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 B  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 B  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 B  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 B  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 B  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 B  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 B  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 B  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 B  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 B  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 B  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 B  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 B  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 B  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 B  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 B  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 B  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 B  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 B  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 B  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 B  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 B  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 B  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 B  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 B  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 B  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 B  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 B  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 B  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 B  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 B  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 B  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 B  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 B  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 B  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 B  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 B  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 B  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 B  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 B  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 B  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 B  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 B  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
MODRES 3C45 ASN A   85  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN A   92  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN A  150  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN A  219  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN A  229  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN A  281  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN A  321  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN A  520  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN B   85  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN B   92  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN B  150  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN B  219  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN B  229  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN B  281  ASN  GLYCOSYLATION SITE                                 
MODRES 3C45 ASN B  321  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1085      14                                                       
HET    NDG  A1086      14                                                       
HET    NAG  A1092      14                                                       
HET    NAG  A1150      14                                                       
HET    NAG  A1151      14                                                       
HET    NAG  A1219      14                                                       
HET    NAG  A1220      14                                                       
HET    NAG  A1229      14                                                       
HET    NDG  A1230      14                                                       
HET    NAG  A1281      14                                                       
HET    NAG  A1321      14                                                       
HET    NAG  A1322      14                                                       
HET    NAG  A1520      14                                                       
HET    NAG  B2085      14                                                       
HET    NAG  B2086      14                                                       
HET    NAG  B2092      14                                                       
HET    NAG  B2150      14                                                       
HET    NAG  B2219      14                                                       
HET    NAG  B2220      14                                                       
HET    NAG  B2229      14                                                       
HET    NAG  B2230      14                                                       
HET    NAG  B2281      14                                                       
HET    NAG  B2282      14                                                       
HET    NAG  B2321      14                                                       
HET     NA  A   1       1                                                       
HET    317  A1521      30                                                       
HET    317  B   2      30                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM      NA SODIUM ION                                                       
HETNAM     317 (2S,3S)-3-{3-[2-CHLORO-4-(METHYLSULFONYL)PHENYL]-1,2,            
HETNAM   2 317  4-OXADIAZOL-5-YL}-1-CYCLOPENTYLIDENE-4-CYCLOPROPYL-1-           
HETNAM   3 317  FLUOROBUTAN-2-AMINE                                             
HETSYN     NAG NAG                                                              
FORMUL   3  NAG    22(C8 H15 N O6)                                              
FORMUL   3  NDG    2(C8 H15 N O6)                                               
FORMUL  18   NA    NA 1+                                                        
FORMUL  19  317    2(C21 H25 CL F N3 O3 S)                                      
FORMUL  21  HOH   *1015(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 LEU A  340  GLN A  344  5                                   5    
HELIX    5   5 GLU A  421  MET A  425  5                                   5    
HELIX    6   6 ASN A  497  GLN A  505  1                                   9    
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  LYS A  615  1                                  16    
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  VAL A  726  1                                  15    
HELIX   17  17 SER A  744  SER A  764  1                                  21    
HELIX   18  18 THR B   44  ASN B   51  1                                   8    
HELIX   19  19 ASP B  200  VAL B  207  1                                   8    
HELIX   20  20 ASP B  274  LEU B  276  5                                   3    
HELIX   21  21 PRO B  290  ILE B  295  1                                   6    
HELIX   22  22 VAL B  341  GLN B  344  5                                   4    
HELIX   23  23 GLU B  421  MET B  425  5                                   5    
HELIX   24  24 ASN B  497  ASN B  506  1                                  10    
HELIX   25  25 ASN B  562  THR B  570  1                                   9    
HELIX   26  26 GLY B  587  HIS B  592  1                                   6    
HELIX   27  27 ALA B  593  ASN B  595  5                                   3    
HELIX   28  28 THR B  600  LYS B  615  1                                  16    
HELIX   29  29 SER B  630  GLY B  641  1                                  12    
HELIX   30  30 ARG B  658  TYR B  662  5                                   5    
HELIX   31  31 ASP B  663  GLY B  672  1                                  10    
HELIX   32  32 ASN B  679  SER B  686  1                                   8    
HELIX   33  33 VAL B  688  VAL B  698  5                                  11    
HELIX   34  34 HIS B  712  VAL B  726  1                                  15    
HELIX   35  35 SER B  744  PHE B  763  1                                  20    
SHEET    1   A 2 LYS A  41  THR A  42  0                                        
SHEET    2   A 2 VAL A 507  GLN A 508  1  O  GLN A 508   N  LYS A  41           
SHEET    1   B 4 ARG A  61  TRP A  62  0                                        
SHEET    2   B 4 GLU A  67  GLN A  72 -1  O  LEU A  69   N  ARG A  61           
SHEET    3   B 4 ASN A  75  ASN A  80 -1  O  ASN A  75   N  GLN A  72           
SHEET    4   B 4 SER A  86  LEU A  90 -1  O  PHE A  89   N  ILE A  76           
SHEET    1   C 4 ILE A 102  ILE A 107  0                                        
SHEET    2   C 4 PHE A 113  LYS A 122 -1  O  GLU A 117   N  ASN A 103           
SHEET    3   C 4 TYR A 128  ASP A 136 -1  O  ASP A 133   N  LEU A 116           
SHEET    4   C 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1   D 4 TRP A 154  TRP A 157  0                                        
SHEET    2   D 4 LEU A 164  TRP A 168 -1  O  VAL A 167   N  TRP A 154           
SHEET    3   D 4 ASP A 171  LYS A 175 -1  O  LYS A 175   N  LEU A 164           
SHEET    4   D 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174           
SHEET    1   E 3 ILE A 194  ASN A 196  0                                        
SHEET    2   E 3 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   E 3 LEU A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224           
SHEET    1   F 4 ILE A 194  ASN A 196  0                                        
SHEET    2   F 4 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   F 4 THR A 265  ASN A 272 -1  O  PHE A 269   N  TYR A 225           
SHEET    4   F 4 SER A 284  ILE A 287 -1  O  ILE A 285   N  VAL A 270           
SHEET    1   G 2 LEU A 235  PHE A 240  0                                        
SHEET    2   G 2 LYS A 250  PRO A 255 -1  O  VAL A 252   N  TYR A 238           
SHEET    1   H 4 HIS A 298  THR A 307  0                                        
SHEET    2   H 4 ARG A 310  ARG A 317 -1  O  ARG A 310   N  ALA A 306           
SHEET    3   H 4 TYR A 322  TYR A 330 -1  O  CYS A 328   N  ILE A 311           
SHEET    4   H 4 TRP A 337  ASN A 338 -1  O  ASN A 338   N  ASP A 329           
SHEET    1   I 4 HIS A 298  THR A 307  0                                        
SHEET    2   I 4 ARG A 310  ARG A 317 -1  O  ARG A 310   N  ALA A 306           
SHEET    3   I 4 TYR A 322  TYR A 330 -1  O  CYS A 328   N  ILE A 311           
SHEET    4   I 4 HIS A 345  MET A 348 -1  O  GLU A 347   N  SER A 323           
SHEET    1   J 4 HIS A 363  PHE A 364  0                                        
SHEET    2   J 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363           
SHEET    3   J 4 ARG A 382  GLN A 388 -1  O  PHE A 387   N  PHE A 371           
SHEET    4   J 4 THR A 395  PHE A 396 -1  O  THR A 395   N  TYR A 386           
SHEET    1   K 4 VAL A 404  LEU A 410  0                                        
SHEET    2   K 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  ALA A 409           
SHEET    3   K 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417           
SHEET    4   K 4 VAL A 442  CYS A 444 -1  O  THR A 443   N  LYS A 433           
SHEET    1   L 4 TYR A 457  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 LYS A 489  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  PHE A 524   N  ILE A 517           
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  VAL A 546  1  N  ASP A 545   O  ALA A 576           
SHEET    5   M 8 VAL A 619  TRP A 629  1  O  ALA A 625   N  LEU A 542           
SHEET    6   M 8 CYS A 649  VAL A 653  1  O  VAL A 653   N  GLY A 628           
SHEET    7   M 8 GLU A 699  GLY A 705  1  O  ILE A 703   N  ALA A 652           
SHEET    8   M 8 GLN A 731  TYR A 735  1  O  GLN A 731   N  TYR A 700           
SHEET    1   N 2 LYS B  41  THR B  42  0                                        
SHEET    2   N 2 VAL B 507  GLN B 508  1  O  GLN B 508   N  LYS B  41           
SHEET    1   O 4 ARG B  61  TRP B  62  0                                        
SHEET    2   O 4 GLU B  67  GLN B  72 -1  O  LEU B  69   N  ARG B  61           
SHEET    3   O 4 ASN B  75  ASN B  80 -1  O  PHE B  79   N  TYR B  68           
SHEET    4   O 4 SER B  86  LEU B  90 -1  O  PHE B  89   N  ILE B  76           
SHEET    1   P 4 ASP B 104  ILE B 107  0                                        
SHEET    2   P 4 PHE B 113  LYS B 122 -1  O  LEU B 115   N  SER B 106           
SHEET    3   P 4 TYR B 128  ASP B 136 -1  O  SER B 131   N  TYR B 118           
SHEET    4   P 4 GLN B 141  LEU B 142 -1  O  GLN B 141   N  ASP B 136           
SHEET    1   Q 4 TRP B 154  TRP B 157  0                                        
SHEET    2   Q 4 LEU B 164  TRP B 168 -1  O  VAL B 167   N  TRP B 154           
SHEET    3   Q 4 ASP B 171  LYS B 175 -1  O  LYS B 175   N  LEU B 164           
SHEET    4   Q 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1   R 3 ILE B 194  ASN B 196  0                                        
SHEET    2   R 3 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   R 3 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224           
SHEET    1   S 4 ILE B 194  ASN B 196  0                                        
SHEET    2   S 4 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   S 4 THR B 265  ASN B 272 -1  O  VAL B 271   N  LEU B 223           
SHEET    4   S 4 SER B 284  GLN B 286 -1  O  ILE B 285   N  VAL B 270           
SHEET    1   T 2 LEU B 235  PHE B 240  0                                        
SHEET    2   T 2 LYS B 250  PRO B 255 -1  O  VAL B 252   N  TYR B 238           
SHEET    1   U 4 HIS B 298  THR B 307  0                                        
SHEET    2   U 4 ARG B 310  ARG B 317 -1  O  ARG B 310   N  ALA B 306           
SHEET    3   U 4 TYR B 322  TYR B 330 -1  O  CYS B 328   N  ILE B 311           
SHEET    4   U 4 TRP B 337  CYS B 339 -1  O  ASN B 338   N  ASP B 329           
SHEET    1   V 4 HIS B 298  THR B 307  0                                        
SHEET    2   V 4 ARG B 310  ARG B 317 -1  O  ARG B 310   N  ALA B 306           
SHEET    3   V 4 TYR B 322  TYR B 330 -1  O  CYS B 328   N  ILE B 311           
SHEET    4   V 4 HIS B 345  MET B 348 -1  O  HIS B 345   N  MET B 325           
SHEET    1   W 4 HIS B 363  PHE B 364  0                                        
SHEET    2   W 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3   W 4 ARG B 382  GLN B 388 -1  O  PHE B 387   N  PHE B 371           
SHEET    4   W 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1   X 4 VAL B 404  LEU B 410  0                                        
SHEET    2   X 4 TYR B 414  SER B 419 -1  O  TYR B 416   N  ALA B 409           
SHEET    3   X 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4   X 4 ASP B 438  CYS B 444 -1  O  THR B 443   N  LYS B 433           
SHEET    1   Y 4 TYR B 457  PHE B 461  0                                        
SHEET    2   Y 4 TYR B 467  CYS B 472 -1  O  ARG B 471   N  SER B 458           
SHEET    3   Y 4 LEU B 479  SER B 484 -1  O  THR B 481   N  LEU B 470           
SHEET    4   Y 4 LYS B 489  GLU B 495 -1  O  LEU B 491   N  LEU B 482           
SHEET    1   Z 8 SER B 511  LEU B 519  0                                        
SHEET    2   Z 8 THR B 522  LEU B 530 -1  O  LEU B 530   N  SER B 511           
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  VAL B 546  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  VAL B 546           
SHEET    6   Z 8 CYS B 649  VAL B 653  1  O  VAL B 653   N  GLY B 628           
SHEET    7   Z 8 GLU B 699  GLY B 705  1  O  LEU B 701   N  ALA B 652           
SHEET    8   Z 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  TYR B 700           
SSBOND   1 CYS A  328    CYS A  339                        1555   1555    2.05  
SSBOND   2 CYS A  385    CYS A  394                        1555   1555    2.05  
SSBOND   3 CYS A  444    CYS A  447                        1555   1555    2.04  
SSBOND   4 CYS A  454    CYS A  472                        1555   1555    2.05  
SSBOND   5 CYS A  649    CYS A  762                        1555   1555    2.05  
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    2.06  
SSBOND  10 CYS B  649    CYS B  762                        1555   1555    2.05  
LINK         ND2 ASN A  85                 C1  NAG A1085   1555   1555    1.54  
LINK         ND2 ASN A  92                 C1  NAG A1092   1555   1555    1.45  
LINK         ND2 ASN A 150                 C1  NAG A1150   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    1.44  
LINK         O   GLY A 490                NA    NA A   1   1555   1555    2.38  
LINK         O   LEU A 491                NA    NA A   1   1555   1555    2.53  
LINK         ND2 ASN A 520                 C1  NAG A1520   1555   1555    1.45  
LINK         ND2 ASN B  85                 C1  NAG B2085   1555   1555    1.45  
LINK         ND2 ASN B  92                 C1  NAG B2092   1555   1555    1.45  
LINK         ND2 ASN B 150                 C1  NAG B2150   1555   1555    1.45  
LINK         ND2 ASN B 219                 C1  NAG B2219   1555   1555    1.45  
LINK         ND2 ASN B 229                 C1  NAG B2229   1555   1555    1.45  
LINK         ND2 ASN B 281                 C1  NAG B2281   1555   1555    1.45  
LINK         ND2 ASN B 321                 C1  NAG B2321   1555   1555    1.44  
LINK         O4  NAG A1085                 C1  NDG A1086   1555   1555    1.32  
LINK         O4  NAG A1150                 C1  NAG A1151   1555   1555    1.39  
LINK         O4  NAG A1219                 C1  NAG A1220   1555   1555    1.39  
LINK         O4  NAG A1229                 C1  NDG A1230   1555   1555    1.39  
LINK         O4  NAG A1321                 C1  NAG A1322   1555   1555    1.38  
LINK         O4  NAG B2085                 C1  NAG B2086   1555   1555    1.41  
LINK         O4  NAG B2219                 C1  NAG B2220   1555   1555    1.38  
LINK         O4  NAG B2229                 C1  NAG B2230   1555   1555    1.38  
LINK         O4  NAG B2281                 C1  NAG B2282   1555   1555    1.38  
CISPEP   1 GLY A  474    PRO A  475          0         0.33                     
CISPEP   2 GLY B  474    PRO B  475          0         0.43                     
SITE     1 AC1  5 GLU A  67  ASN A  85  SER A  86  SER A  87                    
SITE     2 AC1  5 HOH A1971                                                     
SITE     1 AC2  4 GLU A  73  ASN A  74  ASN A  75  ASN A  92                    
SITE     1 AC3  2 PRO A 149  ASN A 150                                          
SITE     1 AC4  4 ASN A 219  THR A 221  GLN A 308  GLU A 309                    
SITE     1 AC5  2 TYR A 330  GLU A 332                                          
SITE     1 AC6  6 ILE A 194  ASN A 229  THR A 231  GLU A 232                    
SITE     2 AC6  6 HOH A1579  HOH A2013                                          
SITE     1 AC7  1 ASN A 281                                                     
SITE     1 AC8  4 ASN A 321  SER A 349  THR A 350  ARG A 596                    
SITE     1 AC9  1 ASP A 678                                                     
SITE     1 BC1  2 ASN A 520  ARG A 581                                          
SITE     1 BC2  4 GLU B  67  ASN B  85  SER B  86  SER B  87                    
SITE     1 BC3  1 HOH B2603                                                     
SITE     1 BC4  4 GLU B  73  ASN B  74  ASN B  75  ASN B  92                    
SITE     1 BC5  4 ARG B 147  ILE B 148  ASN B 150  HOH B2797                    
SITE     1 BC6  5 ASN B 219  THR B 221  GLN B 308  GLU B 309                    
SITE     2 BC6  5 HOH B2817                                                     
SITE     1 BC7  5 PHE B 222  ASN B 272  TYR B 330  HOH B2732                    
SITE     2 BC7  5 HOH B2738                                                     
SITE     1 BC8  6 ILE B 194  ASN B 229  THR B 231  GLU B 232                    
SITE     2 BC8  6 HOH B2366  HOH B2598                                          
SITE     1 BC9  5 HOH A1674  TRP B 187  ASN B 281  HOH B2467                    
SITE     2 BC9  5 HOH B2825                                                     
SITE     1 CC1  3 THR B 188  HOH B2467  HOH B2473                               
SITE     1 CC2  6 ILE B 319  ASN B 321  MET B 348  SER B 349                    
SITE     2 CC2  6 THR B 350  HOH B2815                                          
SITE     1 CC3  4 GLY A 490  LEU A 491  LEU B 276  HOH B2486                    
SITE     1 CC4 13 ARG A 125  GLU A 205  GLU A 206  PHE A 357                    
SITE     2 CC4 13 TYR A 547  SER A 552  GLN A 553  LYS A 554                    
SITE     3 CC4 13 SER A 630  TYR A 662  TYR A 666  ASN A 710                    
SITE     4 CC4 13 HOH A2018                                                     
SITE     1 CC5 14 ARG B 125  GLU B 205  GLU B 206  SER B 209                    
SITE     2 CC5 14 PHE B 357  TYR B 547  SER B 552  LYS B 554                    
SITE     3 CC5 14 SER B 630  TYR B 662  TYR B 666  ASN B 710                    
SITE     4 CC5 14 HOH B2606  HOH B2832                                          
CRYST1  117.888  125.909  136.750  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      0.008483  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007942  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007313        0.00000                         
TER    5966      PRO A 766                                                      
TER   11932      PRO B 766                                                      
MASTER      355    0   27   35  102    0   36    613342    2  434  112          
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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