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LongText Report for: 5zid-pdb

Name Class
5zid-pdb
HEADER    HYDROLASE                               14-MAR-18   5ZID              
TITLE     CRYSTAL STRUCTURE OF HUMAN DPP-IV IN COMPLEX WITH HL2                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM;                       
COMPND   5 SYNONYM: ADABP,ADENOSINE DEAMINASE COMPLEXING PROTEIN 2,ADCP-2,      
COMPND   6 DIPEPTIDYL PEPTIDASE IV,DPP IV,T-CELL ACTIVATION ANTIGEN CD26,TP103; 
COMPND   7 EC: 3.4.14.5;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DPP4, ADCP2, CD26;                                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    INHIBITOR COMPLEX, DPP-4, HYDROLASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.ZHU,H.LI,F.WU                                                       
REVDAT   1   20-MAR-19 5ZID    0                                                
JRNL        AUTH   L.ZHU,H.LI,F.WU                                              
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN DPP-IV IN COMPLEX WITH HL2        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 85.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 33338                          
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                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1786                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2196                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.45                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 125                          
REMARK   3   BIN FREE R VALUE                    : 0.3510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11914                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 131                                     
REMARK   3   SOLVENT ATOMS            : 43                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.06000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.480         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.317         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.669        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.908                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.858                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12423 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 11162 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16919 ; 1.885 ; 1.944       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 25653 ; 0.988 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1452 ; 8.408 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   616 ;36.600 ;23.961       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1992 ;19.873 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;20.703 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1792 ; 0.158 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14040 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  3076 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5814 ; 2.003 ; 3.027       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5813 ; 2.002 ; 3.027       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7264 ; 3.363 ; 4.535       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  7265 ; 3.363 ; 4.536       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6609 ; 1.943 ; 3.199       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  6609 ; 1.943 ; 3.199       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  9656 ; 3.208 ; 4.728       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 14319 ; 5.288 ;24.278       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 14320 ; 5.288 ;24.277       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3   POSITIONS                                                          
REMARK   4                                                                      
REMARK   4 5ZID COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300007131.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97852                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35139                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 85.820                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.14900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 5J3J                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS PH 8, 18% PEG 3350, 200MM     
REMARK 280  NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       63.09500            
REMARK 290   SMTRY3   2  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: 5610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 60130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 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     GLY A   767                                                      
REMARK 465     HIS A   768                                                      
REMARK 465     HIS A   769                                                      
REMARK 465     HIS A   770                                                      
REMARK 465     HIS A   771                                                      
REMARK 465     HIS A   772                                                      
REMARK 465     HIS A   773                                                      
REMARK 465     GLY B   767                                                      
REMARK 465     HIS B   768                                                      
REMARK 465     HIS B   769                                                      
REMARK 465     HIS B   770                                                      
REMARK 465     HIS B   771                                                      
REMARK 465     HIS B   772                                                      
REMARK 465     HIS B   773                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A   229     O5   NAG A   801              1.91            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 328   CA  -  CB  -  SG  ANGL. DEV. =   6.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  53       75.23   -118.92                                   
REMARK 500    ILE A  63       13.40   -154.27                                   
REMARK 500    SER A  64      167.46    170.57                                   
REMARK 500    TYR A  70      102.88   -163.60                                   
REMARK 500    TYR A  83     -128.64   -109.68                                   
REMARK 500    ASN A  85       43.34    -38.29                                   
REMARK 500    SER A  93     -111.66    -71.45                                   
REMARK 500    THR A  94     -107.62     56.34                                   
REMARK 500    PHE A  95       -3.14    -44.73                                   
REMARK 500    GLU A  97       32.90    -96.74                                   
REMARK 500    GLN A 123      -95.09   -112.43                                   
REMARK 500    TRP A 124     -126.67   -106.05                                   
REMARK 500    TYR A 128      145.61    175.07                                   
REMARK 500    ARG A 140       56.20     25.09                                   
REMARK 500    GLU A 146       24.52     40.97                                   
REMARK 500    ARG A 147      171.09    -52.96                                   
REMARK 500    ASN A 150      152.47    -47.72                                   
REMARK 500    HIS A 162       36.77   -161.03                                   
REMARK 500    ASN A 170       -0.24     80.78                                   
REMARK 500    GLU A 191      120.40    -21.37                                   
REMARK 500    ILE A 193      -71.52   -135.82                                   
REMARK 500    ASP A 200     -166.61    -79.94                                   
REMARK 500    VAL A 207      -78.32   -138.00                                   
REMARK 500    ALA A 213       55.38   -140.97                                   
REMARK 500    THR A 231      -60.39    -23.36                                   
REMARK 500    SER A 242     -149.24     84.82                                   
REMARK 500    SER A 275       76.89   -150.02                                   
REMARK 500    VAL A 279      -76.15    -89.56                                   
REMARK 500    ASN A 281     -171.85    -54.66                                   
REMARK 500    GLU A 309       36.81   -140.25                                   
REMARK 500    GLN A 320       48.37    -89.07                                   
REMARK 500    GLU A 332        7.58    -64.08                                   
REMARK 500    ARG A 336     -167.99   -101.77                                   
REMARK 500    LEU A 366      -36.73    -38.25                                   
REMARK 500    ASN A 377     -161.05    -77.06                                   
REMARK 500    TRP A 402      161.83    178.22                                   
REMARK 500    LYS A 423       27.13     48.05                                   
REMARK 500    ASP A 438       93.01   -173.02                                   
REMARK 500    TYR A 439        3.29    -66.04                                   
REMARK 500    ASN A 450       74.39    167.93                                   
REMARK 500    ASP A 515     -177.60   -171.45                                   
REMARK 500    ASN A 520       32.98     31.99                                   
REMARK 500    GLU A 521       17.19     82.01                                   
REMARK 500    HIS A 533       47.62     35.29                                   
REMARK 500    TYR A 547      -71.50   -137.94                                   
REMARK 500    CYS A 551       34.86     75.11                                   
REMARK 500    ARG A 596       -0.20     64.09                                   
REMARK 500    THR A 600      -81.16   -134.43                                   
REMARK 500    ASN A 621       16.01    -67.93                                   
REMARK 500    ARG A 623       64.89   -118.01                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     124 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 926        DISTANCE =  9.21 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9EL A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9EL B 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 801 bound   
REMARK 800  to ASN A 229                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  802 through MAN B 805 bound to ASN B 229                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 801 bound   
REMARK 800  to ASN B 281                                                        
DBREF  5ZID A   40   766  UNP    P27487   DPP4_HUMAN      40    766             
DBREF  5ZID B   40   766  UNP    P27487   DPP4_HUMAN      40    766             
SEQADV 5ZID GLY A  767  UNP  P27487              EXPRESSION TAG                 
SEQADV 5ZID HIS A  768  UNP  P27487              EXPRESSION TAG                 
SEQADV 5ZID HIS A  769  UNP  P27487              EXPRESSION TAG                 
SEQADV 5ZID HIS A  770  UNP  P27487              EXPRESSION TAG                 
SEQADV 5ZID HIS A  771  UNP  P27487              EXPRESSION TAG                 
SEQADV 5ZID HIS A  772  UNP  P27487              EXPRESSION TAG                 
SEQADV 5ZID HIS A  773  UNP  P27487              EXPRESSION TAG                 
SEQADV 5ZID GLY B  767  UNP  P27487              EXPRESSION TAG                 
SEQADV 5ZID HIS B  768  UNP  P27487              EXPRESSION TAG                 
SEQADV 5ZID HIS B  769  UNP  P27487              EXPRESSION TAG                 
SEQADV 5ZID HIS B  770  UNP  P27487              EXPRESSION TAG                 
SEQADV 5ZID HIS B  771  UNP  P27487              EXPRESSION TAG                 
SEQADV 5ZID HIS B  772  UNP  P27487              EXPRESSION TAG                 
SEQADV 5ZID HIS B  773  UNP  P27487              EXPRESSION TAG                 
SEQRES   1 A  734  ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR          
SEQRES   2 A  734  TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP          
SEQRES   3 A  734  HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL          
SEQRES   4 A  734  PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU          
SEQRES   5 A  734  ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP          
SEQRES   6 A  734  TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU          
SEQRES   7 A  734  TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA          
SEQRES   8 A  734  SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE          
SEQRES   9 A  734  THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR          
SEQRES  10 A  734  TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN          
SEQRES  11 A  734  ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER          
SEQRES  12 A  734  TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR          
SEQRES  13 A  734  ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE          
SEQRES  14 A  734  SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR          
SEQRES  15 A  734  PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO          
SEQRES  16 A  734  LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN          
SEQRES  17 A  734  TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY          
SEQRES  18 A  734  ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR          
SEQRES  19 A  734  ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN          
SEQRES  20 A  734  ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR          
SEQRES  21 A  734  LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER          
SEQRES  22 A  734  LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET          
SEQRES  23 A  734  ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN          
SEQRES  24 A  734  CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR          
SEQRES  25 A  734  GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE          
SEQRES  26 A  734  THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN          
SEQRES  27 A  734  GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP          
SEQRES  28 A  734  LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU          
SEQRES  29 A  734  VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR          
SEQRES  30 A  734  TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG          
SEQRES  31 A  734  ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL          
SEQRES  32 A  734  THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN          
SEQRES  33 A  734  TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR          
SEQRES  34 A  734  GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR          
SEQRES  35 A  734  LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU          
SEQRES  36 A  734  GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL          
SEQRES  37 A  734  GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN          
SEQRES  38 A  734  GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS          
SEQRES  39 A  734  PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL          
SEQRES  40 A  734  TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE          
SEQRES  41 A  734  ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN          
SEQRES  42 A  734  ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR          
SEQRES  43 A  734  GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU          
SEQRES  44 A  734  GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG          
SEQRES  45 A  734  GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE          
SEQRES  46 A  734  ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER          
SEQRES  47 A  734  MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY          
SEQRES  48 A  734  ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP          
SEQRES  49 A  734  SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO          
SEQRES  50 A  734  GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET          
SEQRES  51 A  734  SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU          
SEQRES  52 A  734  ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN          
SEQRES  53 A  734  SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL          
SEQRES  54 A  734  ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY          
SEQRES  55 A  734  ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS          
SEQRES  56 A  734  MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO GLY          
SEQRES  57 A  734  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 B  734  ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR          
SEQRES   2 B  734  TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP          
SEQRES   3 B  734  HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL          
SEQRES   4 B  734  PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU          
SEQRES   5 B  734  ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP          
SEQRES   6 B  734  TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU          
SEQRES   7 B  734  TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA          
SEQRES   8 B  734  SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE          
SEQRES   9 B  734  THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR          
SEQRES  10 B  734  TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN          
SEQRES  11 B  734  ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER          
SEQRES  12 B  734  TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR          
SEQRES  13 B  734  ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE          
SEQRES  14 B  734  SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR          
SEQRES  15 B  734  PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO          
SEQRES  16 B  734  LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN          
SEQRES  17 B  734  TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY          
SEQRES  18 B  734  ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR          
SEQRES  19 B  734  ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN          
SEQRES  20 B  734  ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR          
SEQRES  21 B  734  LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER          
SEQRES  22 B  734  LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET          
SEQRES  23 B  734  ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN          
SEQRES  24 B  734  CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR          
SEQRES  25 B  734  GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE          
SEQRES  26 B  734  THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN          
SEQRES  27 B  734  GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP          
SEQRES  28 B  734  LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU          
SEQRES  29 B  734  VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR          
SEQRES  30 B  734  TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG          
SEQRES  31 B  734  ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL          
SEQRES  32 B  734  THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN          
SEQRES  33 B  734  TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR          
SEQRES  34 B  734  GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR          
SEQRES  35 B  734  LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU          
SEQRES  36 B  734  GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL          
SEQRES  37 B  734  GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN          
SEQRES  38 B  734  GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS          
SEQRES  39 B  734  PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL          
SEQRES  40 B  734  TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE          
SEQRES  41 B  734  ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN          
SEQRES  42 B  734  ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR          
SEQRES  43 B  734  GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU          
SEQRES  44 B  734  GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG          
SEQRES  45 B  734  GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE          
SEQRES  46 B  734  ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER          
SEQRES  47 B  734  MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY          
SEQRES  48 B  734  ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP          
SEQRES  49 B  734  SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO          
SEQRES  50 B  734  GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET          
SEQRES  51 B  734  SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU          
SEQRES  52 B  734  ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN          
SEQRES  53 B  734  SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL          
SEQRES  54 B  734  ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY          
SEQRES  55 B  734  ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS          
SEQRES  56 B  734  MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO GLY          
SEQRES  57 B  734  HIS HIS HIS HIS HIS HIS                                      
MODRES 5ZID NAG A  801  NAG  -D                                                 
MODRES 5ZID NAG B  801  NAG  -D                                                 
MODRES 5ZID MAN B  803  MAN  -D                                                 
MODRES 5ZID MAN B  804  MAN  -D                                                 
HET    NAG  A 801      14                                                       
HET    9EL  A 802      28                                                       
HET    NAG  B 801      14                                                       
HET    NAG  B 802      14                                                       
HET    MAN  B 803      11                                                       
HET    MAN  B 804      11                                                       
HET    MAN  B 805      11                                                       
HET    9EL  B 806      28                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     9EL (2S,3R)-2-AMINO-9-METHOXY-3-(2,4,5-TRIFLUOROPHENYL)-2,           
HETNAM   2 9EL  3-DIHYDRO-1H-NAPHTHO[2,1-B]PYRAN-8-CARBONITRILE                 
HETNAM     MAN ALPHA-D-MANNOSE                                                  
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   4  9EL    2(C21 H15 F3 N2 O2)                                          
FORMUL   6  MAN    3(C6 H12 O6)                                                 
FORMUL   8  HOH   *43(H2 O)                                                     
HELIX    1 AA1 THR A   44  LYS A   50  1                                   7    
HELIX    2 AA2 THR A   94  GLY A   99  5                                   6    
HELIX    3 AA3 ASP A  200  VAL A  207  1                                   8    
HELIX    4 AA4 PRO A  290  ILE A  295  1                                   6    
HELIX    5 AA5 VAL A  341  GLN A  344  5                                   4    
HELIX    6 AA6 GLU A  421  MET A  425  5                                   5    
HELIX    7 AA7 ASN A  497  GLN A  505  1                                   9    
HELIX    8 AA8 ASN A  562  ASN A  572  1                                  11    
HELIX    9 AA9 GLY A  587  HIS A  592  1                                   6    
HELIX   10 AB1 ALA A  593  ASN A  595  5                                   3    
HELIX   11 AB2 THR A  600  MET A  616  1                                  17    
HELIX   12 AB3 SER A  630  SER A  642  1                                  13    
HELIX   13 AB4 ARG A  658  TYR A  662  5                                   5    
HELIX   14 AB5 ASP A  663  GLY A  672  1                                  10    
HELIX   15 AB6 ASN A  679  SER A  686  1                                   8    
HELIX   16 AB7 VAL A  688  VAL A  698  5                                  11    
HELIX   17 AB8 PHE A  713  VAL A  726  1                                  14    
HELIX   18 AB9 SER A  744  PHE A  763  1                                  20    
HELIX   19 AC1 THR B   44  LYS B   50  1                                   7    
HELIX   20 AC2 PHE B   95  GLY B   99  5                                   5    
HELIX   21 AC3 ASP B  200  VAL B  207  1                                   8    
HELIX   22 AC4 PRO B  290  ILE B  295  1                                   6    
HELIX   23 AC5 VAL B  341  GLN B  344  5                                   4    
HELIX   24 AC6 GLU B  421  MET B  425  5                                   5    
HELIX   25 AC7 ASN B  497  LEU B  504  1                                   8    
HELIX   26 AC8 GLN B  505  VAL B  507  5                                   3    
HELIX   27 AC9 ASN B  562  THR B  570  1                                   9    
HELIX   28 AD1 GLY B  587  HIS B  592  1                                   6    
HELIX   29 AD2 ALA B  593  ASN B  595  5                                   3    
HELIX   30 AD3 THR B  600  LYS B  615  1                                  16    
HELIX   31 AD4 TRP B  629  SER B  642  1                                  14    
HELIX   32 AD5 ARG B  658  TYR B  662  5                                   5    
HELIX   33 AD6 ASP B  663  GLY B  672  1                                  10    
HELIX   34 AD7 ASN B  679  SER B  686  1                                   8    
HELIX   35 AD8 VAL B  688  VAL B  698  5                                  11    
HELIX   36 AD9 PHE B  713  VAL B  726  1                                  14    
HELIX   37 AE1 SER B  744  SER B  764  1                                  21    
SHEET    1 AA1 2 LYS A  41  THR A  42  0                                        
SHEET    2 AA1 2 VAL A 507  GLN A 508  1  O  GLN A 508   N  LYS A  41           
SHEET    1 AA2 4 ARG A  61  TRP A  62  0                                        
SHEET    2 AA2 4 GLU A  67  GLN A  72 -1  O  LEU A  69   N  ARG A  61           
SHEET    3 AA2 4 ASN A  75  ASN A  80 -1  O  PHE A  79   N  TYR A  68           
SHEET    4 AA2 4 SER A  87  LEU A  90 -1  O  SER A  87   N  VAL A  78           
SHEET    1 AA3 4 ASP A 104  ILE A 107  0                                        
SHEET    2 AA3 4 PHE A 113  LYS A 122 -1  O  LEU A 115   N  SER A 106           
SHEET    3 AA3 4 TYR A 128  ASP A 136 -1  O  SER A 131   N  TYR A 118           
SHEET    4 AA3 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1 AA4 4 TRP A 154  TRP A 157  0                                        
SHEET    2 AA4 4 LEU A 164  TRP A 168 -1  O  ALA A 165   N  THR A 156           
SHEET    3 AA4 4 ASP A 171  LYS A 175 -1  O  TYR A 173   N  TYR A 166           
SHEET    4 AA4 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174           
SHEET    1 AA5 3 ILE A 194  ASN A 196  0                                        
SHEET    2 AA5 3 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3 AA5 3 LEU A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224           
SHEET    1 AA6 4 ILE A 194  ASN A 196  0                                        
SHEET    2 AA6 4 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3 AA6 4 THR A 265  ASN A 272 -1  O  LYS A 267   N  GLN A 227           
SHEET    4 AA6 4 ILE A 285  GLN A 286 -1  O  ILE A 285   N  VAL A 270           
SHEET    1 AA7 2 LEU A 235  PHE A 240  0                                        
SHEET    2 AA7 2 LYS A 250  PRO A 255 -1  O  VAL A 252   N  TYR A 238           
SHEET    1 AA8 4 HIS A 298  THR A 307  0                                        
SHEET    2 AA8 4 ARG A 310  ARG A 317 -1  O  ARG A 310   N  ALA A 306           
SHEET    3 AA8 4 TYR A 322  TYR A 330 -1  O  VAL A 324   N  TRP A 315           
SHEET    4 AA8 4 TRP A 337  CYS A 339 -1  O  ASN A 338   N  ASP A 329           
SHEET    1 AA9 4 HIS A 298  THR A 307  0                                        
SHEET    2 AA9 4 ARG A 310  ARG A 317 -1  O  ARG A 310   N  ALA A 306           
SHEET    3 AA9 4 TYR A 322  TYR A 330 -1  O  VAL A 324   N  TRP A 315           
SHEET    4 AA9 4 HIS A 345  MET A 348 -1  O  GLU A 347   N  SER A 323           
SHEET    1 AB1 4 HIS A 363  PHE A 364  0                                        
SHEET    2 AB1 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363           
SHEET    3 AB1 4 ARG A 382  GLN A 388 -1  O  PHE A 387   N  PHE A 371           
SHEET    4 AB1 4 LYS A 391  PHE A 396 -1  O  THR A 395   N  TYR A 386           
SHEET    1 AB2 4 VAL A 404  LEU A 410  0                                        
SHEET    2 AB2 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  ALA A 409           
SHEET    3 AB2 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417           
SHEET    4 AB2 4 VAL A 442  CYS A 444 -1  O  THR A 443   N  LYS A 433           
SHEET    1 AB3 4 TYR A 457  PHE A 461  0                                        
SHEET    2 AB3 4 TYR A 467  CYS A 472 -1  O  GLN A 469   N  SER A 460           
SHEET    3 AB3 4 TYR A 480  SER A 484 -1  O  THR A 481   N  LEU A 470           
SHEET    4 AB3 4 GLY A 490  GLU A 495 -1  O  LEU A 494   N  TYR A 480           
SHEET    1 AB4 8 SER A 511  LEU A 519  0                                        
SHEET    2 AB4 8 THR A 522  LEU A 530 -1  O  THR A 522   N  LEU A 519           
SHEET    3 AB4 8 ILE A 574  ASP A 579 -1  O  VAL A 575   N  ILE A 529           
SHEET    4 AB4 8 TYR A 540  VAL A 546  1  N  ASP A 545   O  ALA A 576           
SHEET    5 AB4 8 VAL A 619  TRP A 629  1  O  ARG A 623   N  LEU A 542           
SHEET    6 AB4 8 CYS A 649  VAL A 653  1  O  VAL A 653   N  GLY A 628           
SHEET    7 AB4 8 GLU A 699  GLY A 705  1  O  LEU A 701   N  ALA A 652           
SHEET    8 AB4 8 GLN A 731  TYR A 735  1  O  TYR A 735   N  HIS A 704           
SHEET    1 AB5 3 ARG B  61  TRP B  62  0                                        
SHEET    2 AB5 3 GLU B  67  LYS B  71 -1  O  LEU B  69   N  ARG B  61           
SHEET    3 AB5 3 ILE B  76  ASN B  80 -1  O  PHE B  79   N  TYR B  68           
SHEET    1 AB6 4 TYR B 105  ILE B 107  0                                        
SHEET    2 AB6 4 PHE B 113  LYS B 122 -1  O  LEU B 115   N  SER B 106           
SHEET    3 AB6 4 TYR B 128  ASP B 136 -1  O  SER B 131   N  TYR B 118           
SHEET    4 AB6 4 LEU B 142  THR B 152 -1  O  ILE B 143   N  ILE B 134           
SHEET    1 AB7 4 TRP B 154  TRP B 157  0                                        
SHEET    2 AB7 4 LEU B 164  VAL B 167 -1  O  ALA B 165   N  THR B 156           
SHEET    3 AB7 4 ILE B 172  LYS B 175 -1  O  LYS B 175   N  LEU B 164           
SHEET    4 AB7 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1 AB8 3 ILE B 194  ASN B 196  0                                        
SHEET    2 AB8 3 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3 AB8 3 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224           
SHEET    1 AB9 4 ILE B 194  ASN B 196  0                                        
SHEET    2 AB9 4 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3 AB9 4 VAL B 266  ASN B 272 -1  O  LYS B 267   N  GLN B 227           
SHEET    4 AB9 4 ILE B 285  GLN B 286 -1  O  ILE B 285   N  VAL B 270           
SHEET    1 AC1 2 LEU B 235  PHE B 240  0                                        
SHEET    2 AC1 2 LYS B 250  PRO B 255 -1  O  VAL B 252   N  TYR B 238           
SHEET    1 AC2 4 HIS B 298  TRP B 305  0                                        
SHEET    2 AC2 4 ARG B 310  ARG B 317 -1  O  LEU B 316   N  TYR B 299           
SHEET    3 AC2 4 TYR B 322  ASP B 329 -1  O  CYS B 328   N  ILE B 311           
SHEET    4 AC2 4 ASN B 338  CYS B 339 -1  O  ASN B 338   N  ASP B 329           
SHEET    1 AC3 4 HIS B 298  TRP B 305  0                                        
SHEET    2 AC3 4 ARG B 310  ARG B 317 -1  O  LEU B 316   N  TYR B 299           
SHEET    3 AC3 4 TYR B 322  ASP B 329 -1  O  CYS B 328   N  ILE B 311           
SHEET    4 AC3 4 HIS B 345  MET B 348 -1  O  GLU B 347   N  SER B 323           
SHEET    1 AC4 4 HIS B 363  PHE B 364  0                                        
SHEET    2 AC4 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3 AC4 4 ARG B 382  GLN B 388 -1  O  HIS B 383   N  ILE B 375           
SHEET    4 AC4 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1 AC5 4 VAL B 404  LEU B 410  0                                        
SHEET    2 AC5 4 TYR B 414  SER B 419 -1  O  TYR B 416   N  GLU B 408           
SHEET    3 AC5 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4 AC5 4 ASP B 438  CYS B 444 -1  O  THR B 443   N  LYS B 433           
SHEET    1 AC6 4 TYR B 457  PHE B 461  0                                        
SHEET    2 AC6 4 TYR B 467  CYS B 472 -1  O  GLN B 469   N  SER B 460           
SHEET    3 AC6 4 LEU B 479  SER B 484 -1  O  THR B 481   N  LEU B 470           
SHEET    4 AC6 4 LYS B 489  GLU B 495 -1  O  GLU B 495   N  TYR B 480           
SHEET    1 AC7 8 SER B 511  LEU B 519  0                                        
SHEET    2 AC7 8 THR B 522  LEU B 530 -1  O  LEU B 530   N  SER B 511           
SHEET    3 AC7 8 ILE B 574  PHE B 578 -1  O  SER B 577   N  GLN B 527           
SHEET    4 AC7 8 TYR B 540  LEU B 543  1  N  PRO B 541   O  ILE B 574           
SHEET    5 AC7 8 VAL B 619  GLY B 628  1  O  ALA B 625   N  LEU B 542           
SHEET    6 AC7 8 CYS B 649  VAL B 653  1  O  VAL B 653   N  GLY B 628           
SHEET    7 AC7 8 GLU B 699  GLY B 705  1  O  GLU B 699   N  GLY B 650           
SHEET    8 AC7 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  LEU B 702           
SSBOND   1 CYS A  328    CYS A  339                          1555   1555  2.06  
SSBOND   2 CYS A  385    CYS A  394                          1555   1555  2.07  
SSBOND   3 CYS A  444    CYS A  447                          1555   1555  2.02  
SSBOND   4 CYS A  454    CYS A  472                          1555   1555  2.10  
SSBOND   5 CYS A  649    CYS A  762                          1555   1555  2.07  
SSBOND   6 CYS B  328    CYS B  339                          1555   1555  2.06  
SSBOND   7 CYS B  385    CYS B  394                          1555   1555  2.09  
SSBOND   8 CYS B  444    CYS B  447                          1555   1555  2.04  
SSBOND   9 CYS B  454    CYS B  472                          1555   1555  2.13  
SSBOND  10 CYS B  649    CYS B  762                          1555   1555  2.05  
LINK         ND2 ASN A 229                 C1  NAG A 801     1555   1555  1.44  
LINK         ND2 ASN B 229                 C1  NAG B 802     1555   1555  1.33  
LINK         ND2 ASN B 281                 C1  NAG B 801     1555   1555  1.39  
LINK         O4  NAG B 802                 C1  MAN B 803     1555   1555  1.44  
LINK         O3  MAN B 803                 C1  MAN B 804     1555   1555  1.46  
LINK         O3  MAN B 804                 C1  MAN B 805     1555   1555  1.45  
CISPEP   1 GLY A  474    PRO A  475          0        10.82                     
CISPEP   2 GLY B  474    PRO B  475          0         1.82                     
SITE     1 AC1 16 ARG A 125  GLU A 205  GLU A 206  VAL A 207                    
SITE     2 AC1 16 SER A 209  PHE A 357  ARG A 358  TYR A 547                    
SITE     3 AC1 16 SER A 630  TYR A 631  VAL A 656  TYR A 662                    
SITE     4 AC1 16 TYR A 666  ASN A 710  VAL A 711  HIS A 740                    
SITE     1 AC2 15 ARG B 125  GLU B 205  GLU B 206  VAL B 207                    
SITE     2 AC2 15 SER B 209  PHE B 357  ARG B 358  TYR B 547                    
SITE     3 AC2 15 SER B 630  TYR B 631  VAL B 656  TYR B 662                    
SITE     4 AC2 15 TYR B 666  ASN B 710  VAL B 711                               
SITE     1 AC3  4 THR A 188  ASN A 229  THR A 231  LYS A 267                    
SITE     1 AC4  5 SER A 690  GLN B 227  ASN B 229  THR B 231                    
SITE     2 AC4  5 LYS B 267                                                     
SITE     1 AC5  2 TRP B 187  ASN B 281                                          
CRYST1   66.070  126.190  118.620  90.00  99.30  90.00 P 1 21 1      4          
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      0.015135  0.000000  0.002479        0.00000                         
SCALE2      0.000000  0.007925  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008543        0.00000                         
TER    5958      PRO A 766                                                      
TER   11916      PRO B 766                                                      
MASTER      387    0    8   37   99    0   12    612088    2  154  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.
For technical information about these pages see:
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