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LongText Report for: 1N1M-pdb

Name Class
1N1M-pdb
HEADER    HYDROLASE                               18-OCT-02   1N1M              
TITLE     HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 IN COMPLEX WITH AN                 
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND   5 SYNONYM: DPP IV, T-CELL ACTIVATION ANTIGEN CD26, TP103,              
COMPND   6 ADENOSINE DEAMINASE COMPLEXING PROTEIN-2, ADABP;                     
COMPND   7 EC: 3.4.14.5;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 EXPRESSION_SYSTEM_CELL_LINE: HI5;                                    
SOURCE   5 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   6 EXPRESSION_SYSTEM_VECTOR: PBLUEBAC4.5                                
KEYWDS    ALPHA/BETA, BETA-PROPELLER, DIMER                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.B.RASMUSSEN,S.BRANNER,F.C.WIBERG,N.R.WAGTMANN                       
REVDAT   2   07-JAN-03 1N1M    1       JRNL                                     
REVDAT   1   27-DEC-02 1N1M    0                                                
JRNL        AUTH   H.B.RASMUSSEN,S.BRANNER,F.C.WIBERG,N.R.WAGTMANN              
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE              
JRNL        TITL 2 IV/CD26 IN COMPLEX WITH A SUBSTRATE ANALOGUE                 
JRNL        REF    NAT.STRUCT.BIOL.              V.  10    19 2003              
JRNL        REFN   ASTM NSBIEW  US ISSN 1072-8368                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.50 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2002                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 294537.50000                   
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 59045                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2987                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7292                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE                    : 0.3750                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 397                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11912                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 427                                     
REMARK   3   SOLVENT ATOMS            : 931                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.39                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.43                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.51                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.80                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.31                                                 
REMARK   3   BSOL        : 25.60                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  5  : MOL3085.PARAM                                  
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1N1M COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-2002.                
REMARK 100 THE RCSB ID CODE IS RCSB017405.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-OCT-1999; 15-FEB-2000; 15-      
REMARK 200                                   FEB-2000                           
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100; 100                      
REMARK 200  PH                             : 8.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y; Y                            
REMARK 200  RADIATION SOURCE               : MAX II ; ESRF ; ESRF               
REMARK 200  BEAMLINE                       : I711; BM14; BM14                   
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M; M                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0266; 1.0085; 0.8265             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL; SI 111             
REMARK 200                                   CHANNEL; SI 111 CHANNEL            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR; AREA DETECTOR;      
REMARK 200                                   AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH; MARRESEARCH;          
REMARK 200                                   MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63399                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY                : 9.200                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, SODIUM ACETATE, TRIS, PH        
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   1/2-X,-Y,1/2+Z                                          
REMARK 290       3555   -X,1/2+Y,1/2-Z                                          
REMARK 290       4555   1/2+X,1/2-Y,-Z                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       59.61700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.65750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.72400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.65750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.61700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.72400            
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350 J, K, L, M, N, O, P                                                  
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     LEU A   765                                                      
REMARK 465     PRO A   766                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)                  
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET A 293   CE    MET A 293   SD    -0.037                        
REMARK 500    MET A 325   CE    MET A 325   SD    -0.042                        
REMARK 500    MET A 689   SD    MET A 689   CG     0.038                        
REMARK 500    MET A 755   CE    MET A 755   SD    -0.047                        
REMARK 500    MET B 348   SD    MET B 348   CG     0.047                        
REMARK 500    MET B 425   SD    MET B 425   CG     0.043                        
REMARK 500    MET B 528   CE    MET B 528   SD    -0.061                        
REMARK 500    MET B 733   CE    MET B 733   SD    -0.054                        
REMARK 500    MET B 755   CE    MET B 755   SD    -0.071                        
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: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER A 158   N   -  CA  -  C   ANGL. DEV. = -8.9 DEGREES           
REMARK 500    ALA A 165   N   -  CA  -  C   ANGL. DEV. = -9.5 DEGREES           
REMARK 500    ASP A 200   N   -  CA  -  C   ANGL. DEV. = -8.4 DEGREES           
REMARK 500    GLU A 206   N   -  CA  -  C   ANGL. DEV. = 10.7 DEGREES           
REMARK 500    PHE A 240   N   -  CA  -  C   ANGL. DEV. = -9.2 DEGREES           
REMARK 500    ILE A 287   N   -  CA  -  C   ANGL. DEV. = -9.2 DEGREES           
REMARK 500    LEU A 300   N   -  CA  -  C   ANGL. DEV. =-11.2 DEGREES           
REMARK 500    ILE A 319   N   -  CA  -  C   ANGL. DEV. =-11.4 DEGREES           
REMARK 500    GLU A 378   N   -  CA  -  C   ANGL. DEV. = -8.5 DEGREES           
REMARK 500    GLN A 388   N   -  CA  -  C   ANGL. DEV. =-10.1 DEGREES           
REMARK 500    TRP A 402   N   -  CA  -  C   ANGL. DEV. = -9.6 DEGREES           
REMARK 500    GLU A 408   N   -  CA  -  C   ANGL. DEV. =  8.3 DEGREES           
REMARK 500    LEU A 415   N   -  CA  -  C   ANGL. DEV. =-10.2 DEGREES           
REMARK 500    GLU A 448   N   -  CA  -  C   ANGL. DEV. =  9.5 DEGREES           
REMARK 500    SER A 458   N   -  CA  -  C   ANGL. DEV. =-12.1 DEGREES           
REMARK 500    TYR A 547   N   -  CA  -  C   ANGL. DEV. = -9.5 DEGREES           
REMARK 500    LEU A 561   N   -  CA  -  C   ANGL. DEV. = -9.9 DEGREES           
REMARK 500    VAL A 656   N   -  CA  -  C   ANGL. DEV. =-10.4 DEGREES           
REMARK 500    MET A 671   N   -  CA  -  C   ANGL. DEV. =  8.5 DEGREES           
REMARK 500    VAL A 711   N   -  CA  -  C   ANGL. DEV. = -8.6 DEGREES           
REMARK 500    LEU B  90   N   -  CA  -  C   ANGL. DEV. = -8.3 DEGREES           
REMARK 500    GLU B  91   N   -  CA  -  C   ANGL. DEV. =  9.0 DEGREES           
REMARK 500    SER B 158   N   -  CA  -  C   ANGL. DEV. = -9.1 DEGREES           
REMARK 500    ASP B 200   N   -  CA  -  C   ANGL. DEV. = -8.8 DEGREES           
REMARK 500    GLU B 206   N   -  CA  -  C   ANGL. DEV. =  8.4 DEGREES           
REMARK 500    ILE B 236   N   -  CA  -  C   ANGL. DEV. =-11.9 DEGREES           
REMARK 500    PRO B 255   N   -  CA  -  C   ANGL. DEV. = -8.7 DEGREES           
REMARK 500    ILE B 287   N   -  CA  -  C   ANGL. DEV. = -9.0 DEGREES           
REMARK 500    PRO B 290   C   -  N   -  CA  ANGL. DEV. =  8.7 DEGREES           
REMARK 500    LEU B 300   N   -  CA  -  C   ANGL. DEV. =-11.1 DEGREES           
REMARK 500    ILE B 319   N   -  CA  -  C   ANGL. DEV. =-11.8 DEGREES           
REMARK 500    GLN B 320   N   -  CA  -  C   ANGL. DEV. =  8.6 DEGREES           
REMARK 500    GLN B 388   N   -  CA  -  C   ANGL. DEV. =-10.8 DEGREES           
REMARK 500    LYS B 392   N   -  CA  -  C   ANGL. DEV. =  8.3 DEGREES           
REMARK 500    LYS B 399   N   -  CA  -  C   ANGL. DEV. = 13.8 DEGREES           
REMARK 500    GLY B 400   N   -  CA  -  C   ANGL. DEV. = 12.1 DEGREES           
REMARK 500    THR B 401   N   -  CA  -  C   ANGL. DEV. =  9.8 DEGREES           
REMARK 500    TRP B 402   N   -  CA  -  C   ANGL. DEV. =-10.4 DEGREES           
REMARK 500    SER B 458   N   -  CA  -  C   ANGL. DEV. =-13.6 DEGREES           
REMARK 500    ALA B 548   N   -  CA  -  C   ANGL. DEV. =  8.9 DEGREES           
REMARK 500    GLY B 617   N   -  CA  -  C   ANGL. DEV. = 10.5 DEGREES           
REMARK 500    VAL B 656   N   -  CA  -  C   ANGL. DEV. =-11.1 DEGREES           
REMARK 500    VAL B 711   N   -  CA  -  C   ANGL. DEV. = -8.6 DEGREES           
REMARK 500    PRO B 766   C   -  N   -  CA  ANGL. DEV. = 14.9 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 521      -69.50     88.82                                   
REMARK 500    THR B 280      -47.64    133.45                                   
REMARK 500    LYS B 399     -137.82    -37.77                                   
DBREF  1N1M A   39   766  SWS    P27487   DPP4_HUMAN      39    766             
DBREF  1N1M B   39   766  SWS    P27487   DPP4_HUMAN      39    766             
SEQRES   1 A  728  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 A  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 A  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 A  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 A  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 A  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 A  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 A  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 A  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 A  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 A  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 A  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 A  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 A  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 A  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 A  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 A  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 A  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 A  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 A  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 A  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 A  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 A  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 A  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 A  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 A  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 A  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 A  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 A  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 A  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 A  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 A  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 A  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 A  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 A  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 A  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 A  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 A  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 A  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 A  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 A  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 A  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 A  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 A  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 A  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 A  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 A  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 A  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 A  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 A  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 A  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 A  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 A  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 A  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 A  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 A  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
SEQRES   1 B  728  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 B  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 B  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 B  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 B  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 B  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 B  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 B  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 B  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 B  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 B  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 B  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 B  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 B  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 B  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 B  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 B  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 B  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 B  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 B  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 B  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 B  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 B  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 B  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 B  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 B  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 B  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 B  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 B  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 B  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 B  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 B  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 B  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 B  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 B  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 B  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 B  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 B  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 B  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 B  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 B  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 B  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 B  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 B  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 B  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 B  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 B  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 B  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 B  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 B  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 B  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 B  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 B  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 B  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 B  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 B  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
MODRES 1N1M ASN A   85  ASN  GLYCOSYLATION SITE                                 
MODRES 1N1M ASN A  150  ASN  GLYCOSYLATION SITE                                 
MODRES 1N1M ASN A  219  ASN  GLYCOSYLATION SITE                                 
MODRES 1N1M ASN A  229  ASN  GLYCOSYLATION SITE                                 
MODRES 1N1M ASN A  281  ASN  GLYCOSYLATION SITE                                 
MODRES 1N1M ASN A  321  ASN  GLYCOSYLATION SITE                                 
MODRES 1N1M ASN A  520  ASN  GLYCOSYLATION SITE                                 
MODRES 1N1M ASN B   85  ASN  GLYCOSYLATION SITE                                 
MODRES 1N1M ASN B  150  ASN  GLYCOSYLATION SITE                                 
MODRES 1N1M ASN B  219  ASN  GLYCOSYLATION SITE                                 
MODRES 1N1M ASN B  229  ASN  GLYCOSYLATION SITE                                 
MODRES 1N1M ASN B  281  ASN  GLYCOSYLATION SITE                                 
MODRES 1N1M ASN B  321  ASN  GLYCOSYLATION SITE                                 
MODRES 1N1M ASN B  520  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C  85      14                                                       
HET    NAG  C2085      14                                                       
HET    FUC  C1085      10                                                       
HET    NAG  D 150      14                                                       
HET    NAG  D2150      14                                                       
HET    FUC  D1150      10                                                       
HET    NAG  E 219      14                                                       
HET    NAG  E2219      14                                                       
HET    NAG  F 229      14                                                       
HET    NAG  F2229      14                                                       
HET    MAN  F3229      11                                                       
HET    NAG  G 281      14                                                       
HET    NAG  G2281      14                                                       
HET    NAG  H 321      14                                                       
HET    NAG  H2321      14                                                       
HET    NAG  I 520      14                                                       
HET    NAG  J  85      14                                                       
HET    FUC  J1085      10                                                       
HET    NAG  K 150      14                                                       
HET    NAG  L 219      14                                                       
HET    NAG  L2219      14                                                       
HET    NAG  M 229      14                                                       
HET    NAG  M2229      14                                                       
HET    MAN  M3229      11                                                       
HET    NAG  N 281      14                                                       
HET    NAG  N2281      14                                                       
HET    MAN  N3281      11                                                       
HET    NAG  O 321      14                                                       
HET    NAG  O2321      14                                                       
HET    NAG  P 520      14                                                       
HET     HG    950       1                                                       
HET     HG    951       1                                                       
HET     HG    952       1                                                       
HET     HG    953       1                                                       
HET    A3M    954      12                                                       
HET    A3M    955      12                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC FUCOSE                                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      HG MERCURY (II) ION                                                 
HETNAM     A3M 2-AMINO-3-METHYL-1-PYRROLIDIN-1-YL-BUTAN-1-ONE                   
HETSYN     NAG NAG                                                              
FORMUL   3  NAG    24(C8 H15 N1 O6)                                             
FORMUL   3  FUC    3(C6 H12 O5)                                                 
FORMUL   6  MAN    3(C6 H12 O6)                                                 
FORMUL  17   HG    4(HG1 2+)                                                    
FORMUL  21  A3M    2(C9 H18 N2 O1)                                              
FORMUL  23  HOH   *931(H2 O1)                                                   
HELIX    1   1 THR A   44  LYS A   50  1                                   7    
HELIX    2   2 ASN A   92  GLY A   99  5                                   8    
HELIX    3   3 ASP A  200  GLU A  206  1                                   7    
HELIX    4   4 PRO A  290  ILE A  295  1                                   6    
HELIX    5   5 GLU A  332  GLY A  335  5                                   4    
HELIX    6   6 GLU A  421  MET A  425  5                                   5    
HELIX    7   7 ASN A  497  GLN A  505  1                                   9    
HELIX    8   8 ASN A  562  THR A  570  1                                   9    
HELIX    9   9 GLY A  587  HIS A  592  1                                   6    
HELIX   10  10 ALA A  593  ASN A  595  5                                   3    
HELIX   11  11 THR A  600  LYS A  615  1                                  16    
HELIX   12  12 SER A  630  GLY A  641  1                                  12    
HELIX   13  13 ARG A  658  TYR A  662  5                                   5    
HELIX   14  14 ASP A  663  GLY A  672  1                                  10    
HELIX   15  15 ASN A  679  SER A  686  1                                   8    
HELIX   16  16 VAL A  688  VAL A  698  5                                  11    
HELIX   17  17 HIS A  712  GLY A  727  1                                  16    
HELIX   18  18 SER A  744  SER A  764  1                                  21    
HELIX   19  19 THR B   44  ASN B   51  1                                   8    
HELIX   20  20 ASP B  200  GLU B  206  1                                   7    
HELIX   21  21 PRO B  290  ILE B  295  1                                   6    
HELIX   22  22 LEU B  340  GLN B  344  5                                   5    
HELIX   23  23 GLU B  421  MET B  425  5                                   5    
HELIX   24  24 ASN B  497  GLN B  505  1                                   9    
HELIX   25  25 ASN B  562  THR B  570  1                                   9    
HELIX   26  26 GLY B  587  HIS B  592  1                                   6    
HELIX   27  27 ALA B  593  ASN B  595  5                                   3    
HELIX   28  28 THR B  600  MET B  616  1                                  17    
HELIX   29  29 SER B  630  GLY B  641  1                                  12    
HELIX   30  30 ARG B  658  TYR B  662  5                                   5    
HELIX   31  31 ASP B  663  GLY B  672  1                                  10    
HELIX   32  32 ASN B  679  SER B  686  1                                   8    
HELIX   33  33 VAL B  688  VAL B  698  5                                  11    
HELIX   34  34 PHE B  713  VAL B  726  1                                  14    
HELIX   35  35 SER B  744  SER B  764  1                                  21    
SHEET    1   A 2 LYS A  41  THR A  42  0                                        
SHEET    2   A 2 VAL A 507  GLN A 508  1  O  GLN A 508   N  LYS A  41           
SHEET    1   B 4 ARG A  61  TRP A  62  0                                        
SHEET    2   B 4 GLU A  67  LYS A  71 -1  O  LEU A  69   N  ARG A  61           
SHEET    3   B 4 ILE A  76  ASN A  80 -1  O  LEU A  77   N  TYR A  70           
SHEET    4   B 4 SER A  86  LEU A  90 -1  O  PHE A  89   N  ILE A  76           
SHEET    1   C 4 ILE A 102  ILE A 107  0                                        
SHEET    2   C 4 PHE A 113  LYS A 122 -1  O  LEU A 115   N  SER A 106           
SHEET    3   C 4 TYR A 128  ASP A 136 -1  O  SER A 131   N  TYR A 118           
SHEET    4   C 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1   D 4 TRP A 154  TRP A 157  0                                        
SHEET    2   D 4 LEU A 164  TRP A 168 -1  O  ALA A 165   N  THR A 156           
SHEET    3   D 4 ASP A 171  LYS A 175 -1  O  LYS A 175   N  LEU A 164           
SHEET    4   D 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174           
SHEET    1   E 4 SER A 284  ILE A 287  0                                        
SHEET    2   E 4 THR A 265  ASN A 272 -1  N  VAL A 270   O  ILE A 285           
SHEET    3   E 4 PHE A 222  ASN A 229 -1  N  TYR A 225   O  PHE A 269           
SHEET    4   E 4 ILE A 194  ASN A 196 -1  N  TYR A 195   O  PHE A 228           
SHEET    1   F 4 SER A 284  ILE A 287  0                                        
SHEET    2   F 4 THR A 265  ASN A 272 -1  N  VAL A 270   O  ILE A 285           
SHEET    3   F 4 PHE A 222  ASN A 229 -1  N  TYR A 225   O  PHE A 269           
SHEET    4   F 4 LEU A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224           
SHEET    1   G 2 LEU A 235  PHE A 240  0                                        
SHEET    2   G 2 LYS A 250  PRO A 255 -1  O  LYS A 250   N  PHE A 240           
SHEET    1   H 4 HIS A 298  TRP A 305  0                                        
SHEET    2   H 4 ARG A 310  ARG A 317 -1  O  SER A 312   N  THR A 304           
SHEET    3   H 4 TYR A 322  TYR A 330 -1  O  ASP A 326   N  LEU A 313           
SHEET    4   H 4 TRP A 337  ASN A 338 -1  O  ASN A 338   N  ASP A 329           
SHEET    1   I 4 HIS A 298  TRP A 305  0                                        
SHEET    2   I 4 ARG A 310  ARG A 317 -1  O  SER A 312   N  THR A 304           
SHEET    3   I 4 TYR A 322  TYR A 330 -1  O  ASP A 326   N  LEU A 313           
SHEET    4   I 4 HIS A 345  MET A 348 -1  O  GLU A 347   N  SER A 323           
SHEET    1   J 4 HIS A 363  PHE A 364  0                                        
SHEET    2   J 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363           
SHEET    3   J 4 ARG A 382  GLN A 388 -1  O  PHE A 387   N  PHE A 371           
SHEET    4   J 4 LYS A 391  PHE A 396 -1  O  LYS A 391   N  GLN A 388           
SHEET    1   K 4 VAL A 404  LEU A 410  0                                        
SHEET    2   K 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  ALA A 409           
SHEET    3   K 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417           
SHEET    4   K 4 VAL A 442  CYS A 444 -1  O  THR A 443   N  LYS A 433           
SHEET    1   L 4 TYR A 457  PHE A 461  0                                        
SHEET    2   L 4 TYR A 467  CYS A 472 -1  O  GLN A 469   N  SER A 460           
SHEET    3   L 4 LEU A 479  SER A 484 -1  O  THR A 481   N  LEU A 470           
SHEET    4   L 4 LYS A 489  GLU A 495 -1  O  LEU A 494   N  TYR A 480           
SHEET    1   M 8 SER A 511  LEU A 519  0                                        
SHEET    2   M 8 THR A 522  LEU A 530 -1  O  TYR A 526   N  ASP A 515           
SHEET    3   M 8 ILE A 574  PHE A 578 -1  O  VAL A 575   N  ILE A 529           
SHEET    4   M 8 TYR A 540  VAL A 546  1  N  LEU A 543   O  ILE A 574           
SHEET    5   M 8 VAL A 619  TRP A 629  1  O  ALA A 625   N  LEU A 542           
SHEET    6   M 8 CYS A 649  VAL A 653  1  O  VAL A 653   N  GLY A 628           
SHEET    7   M 8 GLU A 699  GLY A 705  1  O  LEU A 701   N  ALA A 652           
SHEET    8   M 8 GLN A 731  TYR A 735  1  O  GLN A 731   N  LEU A 702           
SHEET    1   N 2 LYS B  41  THR B  42  0                                        
SHEET    2   N 2 VAL B 507  GLN B 508  1  O  GLN B 508   N  LYS B  41           
SHEET    1   O 4 ARG B  61  TRP B  62  0                                        
SHEET    2   O 4 GLU B  67  LYS B  71 -1  O  LEU B  69   N  ARG B  61           
SHEET    3   O 4 ILE B  76  ASN B  80 -1  O  PHE B  79   N  TYR B  68           
SHEET    4   O 4 VAL B  88  LEU B  90 -1  O  LEU B  90   N  ILE B  76           
SHEET    1   P 3 ILE B 102  ASP B 104  0                                        
SHEET    2   P 3 PHE B 113  LYS B 122 -1  O  GLU B 117   N  ASP B 104           
SHEET    3   P 3 TYR B 128  ASP B 136 -1  O  SER B 131   N  TYR B 118           
SHEET    1   Q 4 TRP B 154  TRP B 157  0                                        
SHEET    2   Q 4 LEU B 164  TRP B 168 -1  O  VAL B 167   N  TRP B 154           
SHEET    3   Q 4 ASP B 171  LYS B 175 -1  O  TYR B 173   N  TYR B 166           
SHEET    4   Q 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1   R 4 SER B 284  ILE B 287  0                                        
SHEET    2   R 4 THR B 265  ASN B 272 -1  N  VAL B 270   O  ILE B 285           
SHEET    3   R 4 PHE B 222  ASN B 229 -1  N  TYR B 225   O  PHE B 269           
SHEET    4   R 4 ILE B 194  ASN B 196 -1  N  TYR B 195   O  PHE B 228           
SHEET    1   S 4 SER B 284  ILE B 287  0                                        
SHEET    2   S 4 THR B 265  ASN B 272 -1  N  VAL B 270   O  ILE B 285           
SHEET    3   S 4 PHE B 222  ASN B 229 -1  N  TYR B 225   O  PHE B 269           
SHEET    4   S 4 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224           
SHEET    1   T 2 LEU B 235  PHE B 240  0                                        
SHEET    2   T 2 LYS B 250  PRO B 255 -1  O  LYS B 250   N  PHE B 240           
SHEET    1   U 4 HIS B 298  THR B 307  0                                        
SHEET    2   U 4 ARG B 310  ARG B 317 -1  O  LEU B 316   N  TYR B 299           
SHEET    3   U 4 TYR B 322  TYR B 330 -1  O  ASP B 326   N  LEU B 313           
SHEET    4   U 4 TRP B 337  ASN B 338 -1  O  ASN B 338   N  ASP B 329           
SHEET    1   V 4 HIS B 298  THR B 307  0                                        
SHEET    2   V 4 ARG B 310  ARG B 317 -1  O  LEU B 316   N  TYR B 299           
SHEET    3   V 4 TYR B 322  TYR B 330 -1  O  ASP B 326   N  LEU B 313           
SHEET    4   V 4 HIS B 345  MET B 348 -1  O  HIS B 345   N  MET B 325           
SHEET    1   W 4 HIS B 363  PHE B 364  0                                        
SHEET    2   W 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3   W 4 ARG B 382  GLN B 388 -1  O  PHE B 387   N  PHE B 371           
SHEET    4   W 4 LYS B 391  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1   X 4 VAL B 404  LEU B 410  0                                        
SHEET    2   X 4 TYR B 414  SER B 419 -1  O  TYR B 416   N  ALA B 409           
SHEET    3   X 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4   X 4 VAL B 442  CYS B 444 -1  O  THR B 443   N  LYS B 433           
SHEET    1   Y 4 TYR B 457  PHE B 461  0                                        
SHEET    2   Y 4 TYR B 467  CYS B 472 -1  O  ARG B 471   N  SER B 458           
SHEET    3   Y 4 LEU B 479  SER B 484 -1  O  THR B 481   N  LEU B 470           
SHEET    4   Y 4 LYS B 489  GLU B 495 -1  O  LEU B 491   N  LEU B 482           
SHEET    1   Z 8 SER B 511  ILE B 518  0                                        
SHEET    2   Z 8 LYS B 523  LEU B 530 -1  O  MET B 528   N  LYS B 513           
SHEET    3   Z 8 ILE B 574  PHE B 578 -1  O  SER B 577   N  GLN B 527           
SHEET    4   Z 8 TYR B 540  VAL B 546  1  N  LEU B 543   O  ILE B 574           
SHEET    5   Z 8 VAL B 619  TRP B 629  1  O  ALA B 625   N  LEU B 544           
SHEET    6   Z 8 CYS B 649  VAL B 653  1  O  VAL B 653   N  GLY B 628           
SHEET    7   Z 8 GLU B 699  GLY B 705  1  O  ILE B 703   N  ALA B 652           
SHEET    8   Z 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  LEU B 702           
SSBOND   1 CYS A  328    CYS A  339                                             
SSBOND   2 CYS A  385    CYS A  394                                             
SSBOND   3 CYS A  444    CYS A  447                                             
SSBOND   4 CYS A  454    CYS A  472                                             
SSBOND   5 CYS A  649    CYS A  762                                             
SSBOND   6 CYS B  328    CYS B  339                                             
SSBOND   7 CYS B  385    CYS B  394                                             
SSBOND   8 CYS B  444    CYS B  447                                             
SSBOND   9 CYS B  454    CYS B  472                                             
SSBOND  10 CYS B  649    CYS B  762                                             
LINK         ND2 ASN A  85                 C1  NAG C  85                        
LINK         ND2 ASN A 150                 C1  NAG D 150                        
LINK         ND2 ASN A 219                 C1  NAG E 219                        
LINK         ND2 ASN A 229                 C1  NAG F 229                        
LINK         ND2 ASN A 281                 C1  NAG G 281                        
LINK         ND2 ASN A 321                 C1  NAG H 321                        
LINK         ND2 ASN B  85                 C1  NAG J  85                        
LINK         ND2 ASN B 219                 C1  NAG L 219                        
LINK         ND2 ASN B 229                 C1  NAG M 229                        
LINK         ND2 ASN B 281                 C1  NAG N 281                        
LINK         ND2 ASN B 321                 C1  NAG O 321                        
LINK         O4  NAG C  85                 C1  NAG C2085                        
LINK         O6  NAG C  85                 C1  FUC C1085                        
LINK         O4  NAG D 150                 C1  NAG D2150                        
LINK         O6  NAG D 150                 C1  FUC D1150                        
LINK         O4  NAG E 219                 C1  NAG E2219                        
LINK         O4  NAG F 229                 C1  NAG F2229                        
LINK         O4  NAG F2229                 C1  MAN F3229                        
LINK         O4  NAG G 281                 C1  NAG G2281                        
LINK         O4  NAG H 321                 C1  NAG H2321                        
LINK         O6  NAG J  85                 C1  FUC J1085                        
LINK         O4  NAG L 219                 C1  NAG L2219                        
LINK         O4  NAG M 229                 C1  NAG M2229                        
LINK         O4  NAG M2229                 C1  MAN M3229                        
LINK         O4  NAG N 281                 C1  NAG N2281                        
LINK         O4  NAG N2281                 C1  MAN N3281                        
LINK         O4  NAG O 321                 C1  NAG O2321                        
LINK         ND2 ASN A 520                 C1  NAG I 520                        
LINK         ND2 ASN B 150                 C1  NAG K 150                        
LINK         ND2 ASN B 520                 C1  NAG P 520                        
CISPEP   1 ALA A  289    PRO A  290          0        -0.50                     
CISPEP   2 GLY A  474    PRO A  475          0         0.48                     
CISPEP   3 ALA B  289    PRO B  290          0         1.87                     
CISPEP   4 GLY B  474    PRO B  475          0         0.14                     
CISPEP   5 LEU B  765    PRO B  766          0         0.51                     
CRYST1  119.234  123.448  131.315  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008387  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008101  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007615        0.00000                               
END                                                                             

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