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LongText Report for: 4WJL-pdb

Name Class
4WJL-pdb
HEADER    MEMBRANE PROTEIN                        30-SEP-14   4WJL              
TITLE     STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE 10 (DPPY): A MODULATOR OF     
TITLE    2 NEURONAL KV4 CHANNELS                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INACTIVE DIPEPTIDYL PEPTIDASE 10;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 65-783;                                       
COMPND   5 SYNONYM: DIPEPTIDYL PEPTIDASE IV-RELATED PROTEIN 3,DPRP-3,DIPEPTIDYL 
COMPND   6 PEPTIDASE X,DPP X,DIPEPTIDYL PEPTIDASE-LIKE PROTEIN 2,DPL2;          
COMPND   7 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: DPP10, DPRP3, KIAA1492;                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: SF9                                       
KEYWDS    INACTIVE DIPEPTIDYL PEPTIDASE 10, DPP4 STRUCTURE HOMOLOGUE,           
KEYWDS   2 ALPHA/BETA HYDROLASE, BETA-PROPELLER, MEMBRANE PROTEIN               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.A.BEZERRA,E.DOBROVETSKY,A.SEITOVA,S.FEDOSYUK,S.DHE-PAGANON,K.GRUBER 
REVDAT   1   18-MAR-15 4WJL    0                                                
JRNL        AUTH   G.A.BEZERRA,E.DOBROVETSKY,A.SEITOVA,S.FEDOSYUK,              
JRNL        AUTH 2 S.DHE-PAGANON,K.GRUBER                                       
JRNL        TITL   STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE 10 (DPPY): A         
JRNL        TITL 2 MODULATOR OF NEURONAL KV4 CHANNELS.                          
JRNL        REF    SCI REP                       V.   5  8769 2015              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   25740212                                                     
JRNL        DOI    10.1038/SREP08769                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 66.55                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 28967                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1476                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 66.5585 -  7.5582    1.00     2666   140  0.2176 0.2363        
REMARK   3     2  7.5582 -  6.0004    1.00     2560   126  0.2241 0.2279        
REMARK   3     3  6.0004 -  5.2423    1.00     2512   150  0.1942 0.2499        
REMARK   3     4  5.2423 -  4.7631    1.00     2479   137  0.1654 0.2169        
REMARK   3     5  4.7631 -  4.4218    1.00     2489   146  0.1630 0.1792        
REMARK   3     6  4.4218 -  4.1611    1.00     2480   129  0.1801 0.2401        
REMARK   3     7  4.1611 -  3.9528    1.00     2490   136  0.2074 0.2442        
REMARK   3     8  3.9528 -  3.7807    1.00     2458   132  0.2179 0.2602        
REMARK   3     9  3.7807 -  3.6352    1.00     2470   133  0.2500 0.3078        
REMARK   3    10  3.6352 -  3.5098    1.00     2425   131  0.2552 0.2922        
REMARK   3    11  3.5098 -  3.4000    1.00     2462   116  0.2804 0.3134        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 71.01                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.470           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 74.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.27940                                             
REMARK   3    B22 (A**2) : 9.61090                                              
REMARK   3    B33 (A**2) : -5.33150                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008          12146                                  
REMARK   3   ANGLE     :  1.362          16474                                  
REMARK   3   CHIRALITY :  0.102           1856                                  
REMARK   3   PLANARITY :  0.007           2053                                  
REMARK   3   DIHEDRAL  : 20.860           4530                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 67:407 OR RESSEQ        
REMARK   3                          412:782 )                                   
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 67:407 OR RESSEQ        
REMARK   3                          412:782 )                                   
REMARK   3     ATOM PAIRS NUMBER  : 5752                                        
REMARK   3     RMSD               : 0.052                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4WJL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203920.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97943                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.9                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29019                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 111.388                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.22600                            
REMARK 200   FOR THE DATA SET  : 6.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.77500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.77500                            
REMARK 200   FOR SHELL         : 0.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.1.4                                          
REMARK 200 STARTING MODEL: 1XFD                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS FORMED WITHIN 2-4 WEEKS USING   
REMARK 280  100 MICROMETERS OF RESERVOIR SOLUTION CONSISTING OF 20%(W/V) PEG    
REMARK 280  1500, 0.2 M MGCL2, 0.1 M SODIUM CACODYLATE PH 5.5., VAPOR           
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       40.45500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.12500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       71.86500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.12500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.45500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       71.86500            
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: 7230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 60840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 27.0 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     SER A    65                                                      
REMARK 465     GLU A   783                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  97    CG   CD   CE   NZ                                   
REMARK 470     ILE A 413    CB   CG1  CG2  CD1                                  
REMARK 470     LYS A 553    CG   CD   CE   NZ                                   
REMARK 470     LYS B  97    CG   CD   CE   NZ                                   
REMARK 470     ILE B 413    CB   CG1  CG2  CD1                                  
REMARK 470     LYS B 553    CG   CD   CE   NZ                                   
REMARK 470     LYS B 669    CD   CE   NZ                                        
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   119     C2   NAG A   802              1.61            
REMARK 500   ND2  ASN A   119     N2   NAG A   802              1.78            
REMARK 500   O    ASN B   710     N    HIS B   712              2.01            
REMARK 500   ND2  ASN B   119     C2   NAG B   802              2.07            
REMARK 500   O    TYR B   477     O    CYS B   493              2.08            
REMARK 500   O    TYR A   477     O    CYS A   493              2.11            
REMARK 500   O    GLN B   407     O    LYS B   409              2.16            
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    PRO A 533   C   -  N   -  CA  ANGL. DEV. =  10.4 DEGREES          
REMARK 500    PRO A 695   C   -  N   -  CA  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    PRO B 533   C   -  N   -  CA  ANGL. DEV. =  10.5 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    PHE A  79     -157.86    -79.57                                   
REMARK 500    VAL A  80       86.22     70.61                                   
REMARK 500    ILE A  89      -72.12   -131.24                                   
REMARK 500    SER A  98       73.88     59.68                                   
REMARK 500    GLU A  99      -62.92   -101.01                                   
REMARK 500    ASN A 111       -4.30     74.80                                   
REMARK 500    GLU A 118     -164.45   -126.10                                   
REMARK 500    ASN A 119       37.09    -73.17                                   
REMARK 500    PHE A 122      -61.19   -159.68                                   
REMARK 500    PHE A 125       64.10     30.00                                   
REMARK 500    LYS A 126       69.17     39.34                                   
REMARK 500    ILE A 148      -65.02   -131.02                                   
REMARK 500    PHE A 149      -79.17   -120.86                                   
REMARK 500    HIS A 150      -66.09   -132.96                                   
REMARK 500    ARG A 165      -38.75    -34.20                                   
REMARK 500    GLU A 174      -13.72     75.07                                   
REMARK 500    ALA A 183      -73.47   -132.48                                   
REMARK 500    ALA A 184     -144.87     47.04                                   
REMARK 500    ILE A 221      -61.93   -132.33                                   
REMARK 500    ALA A 272     -165.73    -73.18                                   
REMARK 500    SER A 316       -7.04     84.55                                   
REMARK 500    THR A 330      -58.44   -128.47                                   
REMARK 500    LYS A 359      -63.68   -121.33                                   
REMARK 500    THR A 366      -79.32   -117.29                                   
REMARK 500    SER A 369     -167.17    -73.49                                   
REMARK 500    ARG A 379      -19.75     74.53                                   
REMARK 500    GLN A 392       -5.57     63.13                                   
REMARK 500    ARG A 395       -3.22     88.73                                   
REMARK 500    LYS A 409     -140.94     53.56                                   
REMARK 500    GLU A 411     -144.54     52.00                                   
REMARK 500    GLN A 412     -162.90     36.69                                   
REMARK 500    ILE A 413       87.70     98.80                                   
REMARK 500    TRP A 423      167.65    171.89                                   
REMARK 500    SER A 446      141.25   -179.64                                   
REMARK 500    THR A 457      -73.37    -56.04                                   
REMARK 500    ILE A 466      -60.54    -98.64                                   
REMARK 500    PHE A 470      -68.11   -132.52                                   
REMARK 500    LYS A 472     -110.33     60.33                                   
REMARK 500    CYS A 493      -72.48    -73.81                                   
REMARK 500    GLU A 494       -1.78     65.05                                   
REMARK 500    THR A 506      -73.75    -56.26                                   
REMARK 500    PRO A 509       75.14    -64.61                                   
REMARK 500    LYS A 511      -14.02     68.66                                   
REMARK 500    TYR A 512     -119.88     42.50                                   
REMARK 500    LYS A 529      -73.21    -48.84                                   
REMARK 500    ILE A 530       74.63     58.82                                   
REMARK 500    ASP A 541     -126.81     50.46                                   
REMARK 500    ASP A 592       -4.97     90.04                                   
REMARK 500    ARG A 617      -13.18     69.49                                   
REMARK 500    SER A 663      -28.53     40.28                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     120 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A  412     ILE A  413                 -147.25                    
REMARK 500 GLN B  407     SER B  408                  139.24                    
REMARK 500 ASN B  710     VAL B  711                  139.37                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLN A 412        -15.05                                           
REMARK 500    GLN B 412         16.21                                           
REMARK 500    PRO B 695        -10.68                                           
REMARK 500    ASN B 710         10.29                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 801 bound   
REMARK 800  to ASN A 111                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 802 bound   
REMARK 800  to ASN A 119                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  803 through MAN A 806 bound to ASN A 257                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  807 through NAG A 808 bound to ASN A 342                            
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 111                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  802 through NAG B 803 bound to ASN B 119                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  804 through BMA B 806 bound to ASN B 257                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  807 through NAG B 808 bound to ASN B 342                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 809 bound   
REMARK 800  to ASN B 748                                                        
DBREF  4WJL A   65   783  UNP    Q8N608   DPP10_HUMAN     15    733             
DBREF  4WJL B   65   783  UNP    Q8N608   DPP10_HUMAN     15    733             
SEQADV 4WJL MET A  288  UNP  Q8N608    VAL   238 VARIANT                        
SEQADV 4WJL ILE A  401  UNP  Q8N608    VAL   351 VARIANT                        
SEQADV 4WJL MET B  288  UNP  Q8N608    VAL   238 VARIANT                        
SEQADV 4WJL ILE B  401  UNP  Q8N608    VAL   351 VARIANT                        
SEQRES   1 A  719  SER GLU THR ARG LEU SER LEU GLU ASP LEU PHE ARG LYS          
SEQRES   2 A  719  ASP PHE VAL LEU HIS ASP PRO GLU ALA ARG TRP ILE ASN          
SEQRES   3 A  719  ASP THR ASP VAL VAL TYR LYS SER GLU ASN GLY HIS VAL          
SEQRES   4 A  719  ILE LYS LEU ASN ILE GLU THR ASN ALA THR THR LEU LEU          
SEQRES   5 A  719  LEU GLU ASN THR THR PHE VAL THR PHE LYS ALA SER ARG          
SEQRES   6 A  719  HIS SER VAL SER PRO ASP LEU LYS TYR VAL LEU LEU ALA          
SEQRES   7 A  719  TYR ASP VAL LYS GLN ILE PHE HIS TYR SER TYR THR ALA          
SEQRES   8 A  719  SER TYR VAL ILE TYR ASN ILE HIS THR ARG GLU VAL TRP          
SEQRES   9 A  719  GLU LEU ASN PRO PRO GLU VAL GLU ASP SER VAL LEU GLN          
SEQRES  10 A  719  TYR ALA ALA TRP GLY VAL GLN GLY GLN GLN LEU ILE TYR          
SEQRES  11 A  719  ILE PHE GLU ASN ASN ILE TYR TYR GLN PRO ASP ILE LYS          
SEQRES  12 A  719  SER SER SER LEU ARG LEU THR SER SER GLY LYS GLU GLU          
SEQRES  13 A  719  ILE ILE PHE ASN GLY ILE ALA ASP TRP LEU TYR GLU GLU          
SEQRES  14 A  719  GLU LEU LEU HIS SER HIS ILE ALA HIS TRP TRP SER PRO          
SEQRES  15 A  719  ASP GLY GLU ARG LEU ALA PHE LEU MET ILE ASN ASP SER          
SEQRES  16 A  719  LEU VAL PRO THR MET VAL ILE PRO ARG PHE THR GLY ALA          
SEQRES  17 A  719  LEU TYR PRO LYS GLY LYS GLN TYR PRO TYR PRO LYS ALA          
SEQRES  18 A  719  GLY GLN MET ASN PRO THR ILE LYS LEU TYR VAL VAL ASN          
SEQRES  19 A  719  LEU TYR GLY PRO THR HIS THR LEU GLU LEU MET PRO PRO          
SEQRES  20 A  719  ASP SER PHE LYS SER ARG GLU TYR TYR ILE THR MET VAL          
SEQRES  21 A  719  LYS TRP VAL SER ASN THR LYS THR VAL VAL ARG TRP LEU          
SEQRES  22 A  719  ASN ARG ALA GLN ASN ILE SER ILE LEU THR VAL CYS GLU          
SEQRES  23 A  719  THR THR THR GLY ALA CYS SER LYS LYS TYR GLU MET THR          
SEQRES  24 A  719  SER ASP THR TRP LEU SER GLN GLN ASN GLU GLU PRO VAL          
SEQRES  25 A  719  PHE SER ARG ASP GLY SER LYS PHE PHE MET THR VAL PRO          
SEQRES  26 A  719  VAL LYS GLN GLY GLY ARG GLY GLU PHE HIS HIS ILE ALA          
SEQRES  27 A  719  MET PHE LEU ILE GLN SER LYS SER GLU GLN ILE THR VAL          
SEQRES  28 A  719  ARG HIS LEU THR SER GLY ASN TRP GLU VAL ILE LYS ILE          
SEQRES  29 A  719  LEU ALA TYR ASP GLU THR THR GLN LYS ILE TYR PHE LEU          
SEQRES  30 A  719  SER THR GLU SER SER PRO ARG GLY ARG GLN LEU TYR SER          
SEQRES  31 A  719  ALA SER THR GLU GLY LEU LEU ASN ARG GLN CYS ILE SER          
SEQRES  32 A  719  CYS ASN PHE MET LYS GLU GLN CYS THR TYR PHE ASP ALA          
SEQRES  33 A  719  SER PHE SER PRO MET ASN GLN HIS PHE LEU LEU PHE CYS          
SEQRES  34 A  719  GLU GLY PRO ARG VAL PRO VAL VAL SER LEU HIS SER THR          
SEQRES  35 A  719  ASP ASN PRO ALA LYS TYR PHE ILE LEU GLU SER ASN SER          
SEQRES  36 A  719  MET LEU LYS GLU ALA ILE LEU LYS LYS LYS ILE GLY LYS          
SEQRES  37 A  719  PRO GLU ILE LYS ILE LEU HIS ILE ASP ASP TYR GLU LEU          
SEQRES  38 A  719  PRO LEU GLN LEU SER LEU PRO LYS ASP PHE MET ASP ARG          
SEQRES  39 A  719  ASN GLN TYR ALA LEU LEU LEU ILE MET ASP GLU GLU PRO          
SEQRES  40 A  719  GLY GLY GLN LEU VAL THR ASP LYS PHE HIS ILE ASP TRP          
SEQRES  41 A  719  ASP SER VAL LEU ILE ASP MET ASP ASN VAL ILE VAL ALA          
SEQRES  42 A  719  ARG PHE ASP GLY ARG GLY SER GLY PHE GLN GLY LEU LYS          
SEQRES  43 A  719  ILE LEU GLN GLU ILE HIS ARG ARG LEU GLY SER VAL GLU          
SEQRES  44 A  719  VAL LYS ASP GLN ILE THR ALA VAL LYS PHE LEU LEU LYS          
SEQRES  45 A  719  LEU PRO TYR ILE ASP SER LYS ARG LEU SER ILE PHE GLY          
SEQRES  46 A  719  LYS GLY TYR GLY GLY TYR ILE ALA SER MET ILE LEU LYS          
SEQRES  47 A  719  SER ASP GLU LYS LEU PHE LYS CYS GLY SER VAL VAL ALA          
SEQRES  48 A  719  PRO ILE THR ASP LEU LYS LEU TYR ALA SER ALA PHE SER          
SEQRES  49 A  719  GLU ARG TYR LEU GLY MET PRO SER LYS GLU GLU SER THR          
SEQRES  50 A  719  TYR GLN ALA ALA SER VAL LEU HIS ASN VAL HIS GLY LEU          
SEQRES  51 A  719  LYS GLU GLU ASN ILE LEU ILE ILE HIS GLY THR ALA ASP          
SEQRES  52 A  719  THR LYS VAL HIS PHE GLN HIS SER ALA GLU LEU ILE LYS          
SEQRES  53 A  719  HIS LEU ILE LYS ALA GLY VAL ASN TYR THR MET GLN VAL          
SEQRES  54 A  719  TYR PRO ASP GLU GLY HIS ASN VAL SER GLU LYS SER LYS          
SEQRES  55 A  719  TYR HIS LEU TYR SER THR ILE LEU LYS PHE PHE SER ASP          
SEQRES  56 A  719  CYS LEU LYS GLU                                              
SEQRES   1 B  719  SER GLU THR ARG LEU SER LEU GLU ASP LEU PHE ARG LYS          
SEQRES   2 B  719  ASP PHE VAL LEU HIS ASP PRO GLU ALA ARG TRP ILE ASN          
SEQRES   3 B  719  ASP THR ASP VAL VAL TYR LYS SER GLU ASN GLY HIS VAL          
SEQRES   4 B  719  ILE LYS LEU ASN ILE GLU THR ASN ALA THR THR LEU LEU          
SEQRES   5 B  719  LEU GLU ASN THR THR PHE VAL THR PHE LYS ALA SER ARG          
SEQRES   6 B  719  HIS SER VAL SER PRO ASP LEU LYS TYR VAL LEU LEU ALA          
SEQRES   7 B  719  TYR ASP VAL LYS GLN ILE PHE HIS TYR SER TYR THR ALA          
SEQRES   8 B  719  SER TYR VAL ILE TYR ASN ILE HIS THR ARG GLU VAL TRP          
SEQRES   9 B  719  GLU LEU ASN PRO PRO GLU VAL GLU ASP SER VAL LEU GLN          
SEQRES  10 B  719  TYR ALA ALA TRP GLY VAL GLN GLY GLN GLN LEU ILE TYR          
SEQRES  11 B  719  ILE PHE GLU ASN ASN ILE TYR TYR GLN PRO ASP ILE LYS          
SEQRES  12 B  719  SER SER SER LEU ARG LEU THR SER SER GLY LYS GLU GLU          
SEQRES  13 B  719  ILE ILE PHE ASN GLY ILE ALA ASP TRP LEU TYR GLU GLU          
SEQRES  14 B  719  GLU LEU LEU HIS SER HIS ILE ALA HIS TRP TRP SER PRO          
SEQRES  15 B  719  ASP GLY GLU ARG LEU ALA PHE LEU MET ILE ASN ASP SER          
SEQRES  16 B  719  LEU VAL PRO THR MET VAL ILE PRO ARG PHE THR GLY ALA          
SEQRES  17 B  719  LEU TYR PRO LYS GLY LYS GLN TYR PRO TYR PRO LYS ALA          
SEQRES  18 B  719  GLY GLN MET ASN PRO THR ILE LYS LEU TYR VAL VAL ASN          
SEQRES  19 B  719  LEU TYR GLY PRO THR HIS THR LEU GLU LEU MET PRO PRO          
SEQRES  20 B  719  ASP SER PHE LYS SER ARG GLU TYR TYR ILE THR MET VAL          
SEQRES  21 B  719  LYS TRP VAL SER ASN THR LYS THR VAL VAL ARG TRP LEU          
SEQRES  22 B  719  ASN ARG ALA GLN ASN ILE SER ILE LEU THR VAL CYS GLU          
SEQRES  23 B  719  THR THR THR GLY ALA CYS SER LYS LYS TYR GLU MET THR          
SEQRES  24 B  719  SER ASP THR TRP LEU SER GLN GLN ASN GLU GLU PRO VAL          
SEQRES  25 B  719  PHE SER ARG ASP GLY SER LYS PHE PHE MET THR VAL PRO          
SEQRES  26 B  719  VAL LYS GLN GLY GLY ARG GLY GLU PHE HIS HIS ILE ALA          
SEQRES  27 B  719  MET PHE LEU ILE GLN SER LYS SER GLU GLN ILE THR VAL          
SEQRES  28 B  719  ARG HIS LEU THR SER GLY ASN TRP GLU VAL ILE LYS ILE          
SEQRES  29 B  719  LEU ALA TYR ASP GLU THR THR GLN LYS ILE TYR PHE LEU          
SEQRES  30 B  719  SER THR GLU SER SER PRO ARG GLY ARG GLN LEU TYR SER          
SEQRES  31 B  719  ALA SER THR GLU GLY LEU LEU ASN ARG GLN CYS ILE SER          
SEQRES  32 B  719  CYS ASN PHE MET LYS GLU GLN CYS THR TYR PHE ASP ALA          
SEQRES  33 B  719  SER PHE SER PRO MET ASN GLN HIS PHE LEU LEU PHE CYS          
SEQRES  34 B  719  GLU GLY PRO ARG VAL PRO VAL VAL SER LEU HIS SER THR          
SEQRES  35 B  719  ASP ASN PRO ALA LYS TYR PHE ILE LEU GLU SER ASN SER          
SEQRES  36 B  719  MET LEU LYS GLU ALA ILE LEU LYS LYS LYS ILE GLY LYS          
SEQRES  37 B  719  PRO GLU ILE LYS ILE LEU HIS ILE ASP ASP TYR GLU LEU          
SEQRES  38 B  719  PRO LEU GLN LEU SER LEU PRO LYS ASP PHE MET ASP ARG          
SEQRES  39 B  719  ASN GLN TYR ALA LEU LEU LEU ILE MET ASP GLU GLU PRO          
SEQRES  40 B  719  GLY GLY GLN LEU VAL THR ASP LYS PHE HIS ILE ASP TRP          
SEQRES  41 B  719  ASP SER VAL LEU ILE ASP MET ASP ASN VAL ILE VAL ALA          
SEQRES  42 B  719  ARG PHE ASP GLY ARG GLY SER GLY PHE GLN GLY LEU LYS          
SEQRES  43 B  719  ILE LEU GLN GLU ILE HIS ARG ARG LEU GLY SER VAL GLU          
SEQRES  44 B  719  VAL LYS ASP GLN ILE THR ALA VAL LYS PHE LEU LEU LYS          
SEQRES  45 B  719  LEU PRO TYR ILE ASP SER LYS ARG LEU SER ILE PHE GLY          
SEQRES  46 B  719  LYS GLY TYR GLY GLY TYR ILE ALA SER MET ILE LEU LYS          
SEQRES  47 B  719  SER ASP GLU LYS LEU PHE LYS CYS GLY SER VAL VAL ALA          
SEQRES  48 B  719  PRO ILE THR ASP LEU LYS LEU TYR ALA SER ALA PHE SER          
SEQRES  49 B  719  GLU ARG TYR LEU GLY MET PRO SER LYS GLU GLU SER THR          
SEQRES  50 B  719  TYR GLN ALA ALA SER VAL LEU HIS ASN VAL HIS GLY LEU          
SEQRES  51 B  719  LYS GLU GLU ASN ILE LEU ILE ILE HIS GLY THR ALA ASP          
SEQRES  52 B  719  THR LYS VAL HIS PHE GLN HIS SER ALA GLU LEU ILE LYS          
SEQRES  53 B  719  HIS LEU ILE LYS ALA GLY VAL ASN TYR THR MET GLN VAL          
SEQRES  54 B  719  TYR PRO ASP GLU GLY HIS ASN VAL SER GLU LYS SER LYS          
SEQRES  55 B  719  TYR HIS LEU TYR SER THR ILE LEU LYS PHE PHE SER ASP          
SEQRES  56 B  719  CYS LEU LYS GLU                                              
HET    NAG  A 801      14                                                       
HET    NAG  A 802      14                                                       
HET    NAG  A 803      14                                                       
HET    NAG  A 804      14                                                       
HET    BMA  A 805      11                                                       
HET    MAN  A 806      11                                                       
HET    NAG  A 807      14                                                       
HET    NAG  A 808      14                                                       
HET    NAG  B 801      14                                                       
HET    NAG  B 802      14                                                       
HET    NAG  B 803      14                                                       
HET    NAG  B 804      14                                                       
HET    NAG  B 805      14                                                       
HET    BMA  B 806      11                                                       
HET    NAG  B 807      14                                                       
HET    NAG  B 808      14                                                       
HET    NAG  B 809      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
FORMUL   3  NAG    14(C8 H15 N O6)                                              
FORMUL   5  BMA    2(C6 H12 O6)                                                 
FORMUL   5  MAN    C6 H12 O6                                                    
HELIX    1 AA1 SER A   70  PHE A   75  1                                   6    
HELIX    2 AA2 ASP A  228  GLU A  234  1                                   7    
HELIX    3 AA3 ASN A  518  LYS A  528  1                                  11    
HELIX    4 AA4 ASP A  583  MET A  591  1                                   9    
HELIX    5 AA5 ILE A  611  HIS A  616  5                                   6    
HELIX    6 AA6 GLY A  620  LYS A  636  1                                  17    
HELIX    7 AA7 GLY A  651  LEU A  661  1                                  11    
HELIX    8 AA8 ASP A  679  TYR A  683  5                                   5    
HELIX    9 AA9 ALA A  684  GLY A  693  1                                  10    
HELIX   10 AB1 SER A  700  ALA A  705  1                                   6    
HELIX   11 AB2 PHE A  732  ALA A  745  1                                  14    
HELIX   12 AB3 SER A  762  LEU A  781  1                                  20    
HELIX   13 AB4 SER B   70  PHE B   75  1                                   6    
HELIX   14 AB5 ASP B  228  GLU B  234  1                                   7    
HELIX   15 AB6 ASN B  518  LYS B  528  1                                  11    
HELIX   16 AB7 ASP B  583  MET B  591  1                                   9    
HELIX   17 AB8 ILE B  611  HIS B  616  5                                   6    
HELIX   18 AB9 GLY B  620  LYS B  636  1                                  17    
HELIX   19 AC1 GLY B  651  LEU B  661  1                                  11    
HELIX   20 AC2 ASP B  679  TYR B  683  5                                   5    
HELIX   21 AC3 ALA B  684  GLY B  693  1                                  10    
HELIX   22 AC4 SER B  700  ALA B  705  1                                   6    
HELIX   23 AC5 PHE B  732  ALA B  745  1                                  14    
HELIX   24 AC6 SER B  762  LEU B  781  1                                  20    
SHEET    1 AA1 3 ASP A  93  VAL A  94  0                                        
SHEET    2 AA1 3 VAL A 103  ASN A 107 -1  O  LEU A 106   N  VAL A  94           
SHEET    3 AA1 3 THR A 113  LEU A 117 -1  O  THR A 114   N  LYS A 105           
SHEET    1 AA2 4 ARG A 129  VAL A 132  0                                        
SHEET    2 AA2 4 TYR A 138  GLN A 147 -1  O  LEU A 140   N  SER A 131           
SHEET    3 AA2 4 TYR A 153  ASN A 161 -1  O  THR A 154   N  LYS A 146           
SHEET    4 AA2 4 VAL A 167  LEU A 170 -1  O  TRP A 168   N  ILE A 159           
SHEET    1 AA3 3 LEU A 192  PHE A 196  0                                        
SHEET    2 AA3 3 ASN A 199  GLN A 203 -1  O  GLN A 203   N  LEU A 192           
SHEET    3 AA3 3 LEU A 211  ARG A 212 -1  O  LEU A 211   N  TYR A 202           
SHEET    1 AA4 3 ILE A 222  ASN A 224  0                                        
SHEET    2 AA4 3 ARG A 250  ASN A 257 -1  O  ILE A 256   N  PHE A 223           
SHEET    3 AA4 3 HIS A 242  TRP A 244 -1  N  TRP A 243   O  ALA A 252           
SHEET    1 AA5 4 ILE A 222  ASN A 224  0                                        
SHEET    2 AA5 4 ARG A 250  ASN A 257 -1  O  ILE A 256   N  PHE A 223           
SHEET    3 AA5 4 THR A 291  ASN A 298 -1  O  LYS A 293   N  MET A 255           
SHEET    4 AA5 4 LEU A 306  GLU A 307 -1  O  LEU A 306   N  VAL A 296           
SHEET    1 AA6 2 THR A 263  VAL A 265  0                                        
SHEET    2 AA6 2 GLN A 279  PRO A 281 -1  O  TYR A 280   N  MET A 264           
SHEET    1 AA7 4 TYR A 319  TRP A 326  0                                        
SHEET    2 AA7 4 LYS A 331  ASN A 338 -1  O  LEU A 337   N  TYR A 320           
SHEET    3 AA7 4 ILE A 343  GLU A 350 -1  O  CYS A 349   N  THR A 332           
SHEET    4 AA7 4 ALA A 355  THR A 363 -1  O  TYR A 360   N  LEU A 346           
SHEET    1 AA8 3 VAL A 376  PHE A 377  0                                        
SHEET    2 AA8 3 PHE A 384  VAL A 390 -1  O  PHE A 385   N  VAL A 376           
SHEET    3 AA8 3 PHE A 398  ALA A 402 -1  O  ALA A 402   N  MET A 386           
SHEET    1 AA9 4 VAL A 425  TYR A 431  0                                        
SHEET    2 AA9 4 LYS A 437  SER A 442 -1  O  TYR A 439   N  ALA A 430           
SHEET    3 AA9 4 GLN A 451  SER A 456 -1  O  TYR A 453   N  PHE A 440           
SHEET    4 AA9 4 ARG A 463  CYS A 465 -1  O  GLN A 464   N  SER A 454           
SHEET    1 AB1 4 ASP A 479  PHE A 482  0                                        
SHEET    2 AB1 4 HIS A 488  PHE A 492 -1  O  LEU A 490   N  SER A 481           
SHEET    3 AB1 4 VAL A 501  SER A 505 -1  O  SER A 502   N  LEU A 491           
SHEET    4 AB1 4 PHE A 513  GLU A 516 -1  O  GLU A 516   N  VAL A 501           
SHEET    1 AB2 8 GLU A 534  ILE A 540  0                                        
SHEET    2 AB2 8 TYR A 543  SER A 550 -1  O  LEU A 549   N  GLU A 534           
SHEET    3 AB2 8 VAL A 594  PHE A 599 -1  O  ARG A 598   N  GLN A 548           
SHEET    4 AB2 8 TYR A 561  ILE A 566  1  N  LEU A 564   O  ALA A 597           
SHEET    5 AB2 8 ILE A 640  LYS A 650  1  O  SER A 646   N  LEU A 563           
SHEET    6 AB2 8 CYS A 670  VAL A 674  1  O  SER A 672   N  ILE A 647           
SHEET    7 AB2 8 ASN A 718  GLY A 724  1  O  LEU A 720   N  VAL A 673           
SHEET    8 AB2 8 TYR A 749  TYR A 754  1  O  THR A 750   N  ILE A 719           
SHEET    1 AB3 3 ASP B  93  VAL B  94  0                                        
SHEET    2 AB3 3 VAL B 103  ASN B 107 -1  O  LEU B 106   N  VAL B  94           
SHEET    3 AB3 3 THR B 113  LEU B 117 -1  O  THR B 114   N  LYS B 105           
SHEET    1 AB4 4 ARG B 129  VAL B 132  0                                        
SHEET    2 AB4 4 TYR B 138  GLN B 147 -1  O  LEU B 140   N  SER B 131           
SHEET    3 AB4 4 TYR B 153  ASN B 161 -1  O  THR B 154   N  LYS B 146           
SHEET    4 AB4 4 VAL B 167  LEU B 170 -1  O  TRP B 168   N  ILE B 159           
SHEET    1 AB5 3 LEU B 192  PHE B 196  0                                        
SHEET    2 AB5 3 ASN B 199  GLN B 203 -1  O  GLN B 203   N  LEU B 192           
SHEET    3 AB5 3 LEU B 211  ARG B 212 -1  O  LEU B 211   N  TYR B 202           
SHEET    1 AB6 3 ILE B 222  ASN B 224  0                                        
SHEET    2 AB6 3 ARG B 250  ASN B 257 -1  O  ILE B 256   N  PHE B 223           
SHEET    3 AB6 3 HIS B 242  TRP B 244 -1  N  TRP B 243   O  ALA B 252           
SHEET    1 AB7 4 ILE B 222  ASN B 224  0                                        
SHEET    2 AB7 4 ARG B 250  ASN B 257 -1  O  ILE B 256   N  PHE B 223           
SHEET    3 AB7 4 THR B 291  ASN B 298 -1  O  LYS B 293   N  MET B 255           
SHEET    4 AB7 4 LEU B 306  GLU B 307 -1  O  LEU B 306   N  VAL B 296           
SHEET    1 AB8 2 THR B 263  VAL B 265  0                                        
SHEET    2 AB8 2 GLN B 279  PRO B 281 -1  O  TYR B 280   N  MET B 264           
SHEET    1 AB9 4 TYR B 319  TRP B 326  0                                        
SHEET    2 AB9 4 LYS B 331  ASN B 338 -1  O  LEU B 337   N  TYR B 320           
SHEET    3 AB9 4 ILE B 343  GLU B 350 -1  O  CYS B 349   N  THR B 332           
SHEET    4 AB9 4 ALA B 355  THR B 363 -1  O  TYR B 360   N  LEU B 346           
SHEET    1 AC1 3 VAL B 376  PHE B 377  0                                        
SHEET    2 AC1 3 PHE B 384  VAL B 390 -1  O  PHE B 385   N  VAL B 376           
SHEET    3 AC1 3 PHE B 398  ALA B 402 -1  O  ALA B 402   N  MET B 386           
SHEET    1 AC2 4 VAL B 425  TYR B 431  0                                        
SHEET    2 AC2 4 LYS B 437  SER B 442 -1  O  TYR B 439   N  ALA B 430           
SHEET    3 AC2 4 GLN B 451  SER B 456 -1  O  TYR B 453   N  PHE B 440           
SHEET    4 AC2 4 ARG B 463  CYS B 465 -1  O  GLN B 464   N  SER B 454           
SHEET    1 AC3 4 ASP B 479  PHE B 482  0                                        
SHEET    2 AC3 4 HIS B 488  PHE B 492 -1  O  LEU B 490   N  SER B 481           
SHEET    3 AC3 4 VAL B 501  SER B 505 -1  O  SER B 502   N  LEU B 491           
SHEET    4 AC3 4 PHE B 513  GLU B 516 -1  O  PHE B 513   N  LEU B 503           
SHEET    1 AC4 8 GLU B 534  ILE B 540  0                                        
SHEET    2 AC4 8 TYR B 543  SER B 550 -1  O  LEU B 549   N  GLU B 534           
SHEET    3 AC4 8 VAL B 594  PHE B 599 -1  O  ARG B 598   N  GLN B 548           
SHEET    4 AC4 8 TYR B 561  ILE B 566  1  N  LEU B 564   O  ALA B 597           
SHEET    5 AC4 8 ILE B 640  LYS B 650  1  O  SER B 646   N  LEU B 563           
SHEET    6 AC4 8 CYS B 670  VAL B 674  1  O  SER B 672   N  ILE B 647           
SHEET    7 AC4 8 ASN B 718  GLY B 724  1  O  LEU B 720   N  VAL B 673           
SHEET    8 AC4 8 TYR B 749  TYR B 754  1  O  THR B 750   N  ILE B 719           
SSBOND   1 CYS A  349    CYS A  356                          1555   1555  2.05  
SSBOND   2 CYS A  465    CYS A  468                          1555   1555  2.03  
SSBOND   3 CYS A  475    CYS A  493                          1555   1555  1.97  
SSBOND   4 CYS A  670    CYS A  780                          1555   1555  2.03  
SSBOND   5 CYS B  349    CYS B  356                          1555   1555  2.04  
SSBOND   6 CYS B  465    CYS B  468                          1555   1555  2.03  
SSBOND   7 CYS B  475    CYS B  493                          1555   1555  2.01  
SSBOND   8 CYS B  670    CYS B  780                          1555   1555  2.04  
LINK         ND2 ASN A 111                 C1  NAG A 801     1555   1555  1.45  
LINK         ND2 ASN A 119                 C1  NAG A 802     1555   1555  1.48  
LINK         ND2 ASN A 257                 C1  NAG A 803     1555   1555  1.45  
LINK         ND2 ASN A 342                 C1  NAG A 807     1555   1555  1.44  
LINK         ND2 ASN B 111                 C1  NAG B 801     1555   1555  1.46  
LINK         ND2 ASN B 119                 C1  NAG B 802     1555   1555  1.49  
LINK         ND2 ASN B 257                 C1  NAG B 804     1555   1555  1.43  
LINK         ND2 ASN B 342                 C1  NAG B 807     1555   1555  1.45  
LINK         ND2 ASN B 748                 C1  NAG B 809     1555   1555  1.44  
LINK         O4  NAG A 803                 C1  NAG A 804     1555   1555  1.45  
LINK         O4  NAG A 804                 C1  BMA A 805     1555   1555  1.47  
LINK         O3  BMA A 805                 C1  MAN A 806     1555   1555  1.46  
LINK         O4  NAG A 807                 C1  NAG A 808     1555   1555  1.46  
LINK         O4  NAG B 802                 C1  NAG B 803     1555   1555  1.46  
LINK         O4  NAG B 804                 C1  NAG B 805     1555   1555  1.44  
LINK         O4  NAG B 805                 C1  BMA B 806     1555   1555  1.47  
LINK         O4  NAG B 807                 C1  NAG B 808     1555   1555  1.45  
SITE     1 AC1  4 GLU A 109  ASN A 111  TYR A 512  PHE A 513                    
SITE     1 AC2  3 ASN A 100  HIS A 102  ASN A 119                               
SITE     1 AC3  7 ILE A 222  MET A 255  ASN A 257  SER A 259                    
SITE     2 AC3  7 LEU A 260  GLU B 523  LEU B 526                               
SITE     1 AC4  2 ASN A 342  GLU A 698                                          
SITE     1 AC5  3 ASN B 111  TYR B 512  PHE B 513                               
SITE     1 AC6  3 ASN B 100  HIS B 102  ASN B 119                               
SITE     1 AC7  4 ILE B 222  MET B 255  ASN B 257  SER B 259                    
SITE     1 AC8  4 ASN B 342  THR B 363  SER B 364  GLU B 698                    
SITE     1 AC9  2 LYS A 775  ASN B 748                                          
CRYST1   80.910  143.730  176.250  90.00  90.00  90.00 P 21 21 21    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      0.012359  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006957  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005674        0.00000                         
MTRIX1   1 -0.999919 -0.003172  0.012346      -40.51040    1                    
MTRIX2   1  0.006281  0.720166  0.693774       36.55450    1                    
MTRIX3   1 -0.011091  0.693795 -0.720087      -90.82720    1                    
TER    5795      LYS A 782                                                      
TER   11602      GLU B 783                                                      
MASTER      417    0   17   24   84    0   10    911829    2  254  112          
END                                                                             

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