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LongText Report for: 1NU6-pdb

Name Class
1NU6-pdb
HEADER    HYDROLASE                               31-JAN-03   1NU6              
TITLE     CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (DPP-IV)           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DPP IV;                                                     
COMPND   5 EC: 3.4.14.5;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   5 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PCHDP1-23                                 
KEYWDS    EXOPEPTIDASE, BETA BARREL, ALPHA/BETA HYDROLASE FOLD, DPP-IV          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.HENNIG,M.STIHLE,R.THOMA,A.RUF                                       
REVDAT   1   26-AUG-03 1NU6    0                                                
JRNL        AUTH   R.THOMA,B.LOEFFLER,M.STIHLE,W.HUBER,A.RUF,M.HENNIG           
JRNL        TITL   STRUCTURAL BASIS OF PROLINE-SPECIFIC EXOPEPTIDASE            
JRNL        TITL 2 ACTIVITY AS OBSERVED IN HUMAN DIPEPTIDYL                     
JRNL        TITL 3 PEPTIDASE-IV.                                                
JRNL        REF    STRUCTURE                     V.  11   947 2003              
JRNL        REFN   ASTM STRUE6  UK ISSN 0969-2126                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.10 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 83.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 87113                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4619                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2014                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 91                           
REMARK   3   BIN FREE R VALUE                    : 0.2780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 12366                                   
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.63                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.30000                                             
REMARK   3    B22 (A**2) : 4.24000                                              
REMARK   3    B33 (A**2) : -1.93000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.280         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.228         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.244         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.427         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12400 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A): 10588 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16876 ; 1.867 ; 1.936       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 24632 ; 0.889 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1454 ; 5.183 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2075 ;19.350 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1790 ; 0.135 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 13738 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2674 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2592 ; 0.240 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 10721 ; 0.223 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):    17 ; 0.494 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   820 ; 0.155 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     7 ; 0.115 ; 0.500       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     9 ; 0.235 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    38 ; 0.277 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.397 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7252 ; 0.874 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11766 ; 1.603 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5148 ; 2.300 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5110 ; 3.638 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 0                                 
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 0                                          
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1NU6 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-FEB-2003.                
REMARK 100 THE RCSB ID CODE IS RCSB018208.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-2001                        
REMARK 200  TEMPERATURE           (KELVIN) : 90.0                               
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9765                             
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87113                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 12.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
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: PEG, PH 8.5, VAPOR DIFFUSION,            
REMARK 280  HANGING DROP, TEMPERATURE 90K                                       
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       32.74800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      209.64450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.12000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      209.64450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.74800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.12000            
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                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: 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                             
REMARK 500   NZ   LYS B   175     O    PRO B   178              2.11            
REMARK 500   O    HOH     259     O    HOH     260              2.13            
REMARK 500   O4   NAG B   796     O    HOH     340              2.15            
REMARK 500   NZ   LYS A   175     O    PRO A   178              2.16            
REMARK 500   OE2  GLU A   602     OH   TYR A   631              2.16            
REMARK 500   OH   TYR B   422     OE2  GLU B   448              2.16            
REMARK 500   O    ASN A   487     N    LYS A   489              2.17            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS A    41     O    VAL A   341     1655     2.12            
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    CYS A 301   CA    CYS A 301   CB     0.129                        
REMARK 500    CYS A 301   CB    CYS A 301   SG     0.153                        
REMARK 500    MET A 528   SD    MET A 528   CE    -0.236                        
REMARK 500    MET A 755   SD    MET A 755   CE    -0.140                        
REMARK 500    CYS B 301   CB    CYS B 301   SG     0.145                        
REMARK 500    MET B 325   SD    MET B 325   CE    -0.135                        
REMARK 500    PRO B 362   CB    PRO B 362   CG     0.114                        
REMARK 500    VAL B 558   CB    VAL B 558   CG1   -0.120                        
REMARK 500    LYS B 721   CG    LYS B 721   CD     0.128                        
REMARK 500    LYS B 721   CD    LYS B 721   CE     0.118                        
REMARK 500    LYS B 721   CE    LYS B 721   NZ     0.115                        
REMARK 500    MET B 733   SD    MET B 733   CE    -0.189                        
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    ARG A  40   N   -  CA  -  C   ANGL. DEV. = 15.5 DEGREES           
REMARK 500    LEU A  60   CA  -  CB  -  CG  ANGL. DEV. = 13.8 DEGREES           
REMARK 500    LEU A 316   CA  -  CB  -  CG  ANGL. DEV. = 12.7 DEGREES           
REMARK 500    ILE A 389   N   -  CA  -  C   ANGL. DEV. = 12.2 DEGREES           
REMARK 500    LEU A 482   CA  -  CB  -  CG  ANGL. DEV. = 12.3 DEGREES           
REMARK 500    ASN A 487   N   -  CA  -  C   ANGL. DEV. =-11.7 DEGREES           
REMARK 500    LEU A 544   CA  -  CB  -  CG  ANGL. DEV. = 11.7 DEGREES           
REMARK 500    LEU B  60   CA  -  CB  -  CG  ANGL. DEV. = 11.6 DEGREES           
REMARK 500    ASP B 110   N   -  CA  -  C   ANGL. DEV. =-13.5 DEGREES           
REMARK 500    GLY B 111   N   -  CA  -  C   ANGL. DEV. = 18.7 DEGREES           
REMARK 500    LYS B 721   CD  -  CE  -  NZ  ANGL. DEV. = 13.1 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    ARG A  40     -105.28     60.56                                   
REMARK 500    SER A 630     -119.66     63.38                                   
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED            
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE                 
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL                 
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH    18        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH   131        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH   145        DISTANCE =  7.93 ANGSTROMS                       
REMARK 525    HOH   259        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH   381        DISTANCE =  5.67 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NU8   RELATED DB: PDB                                   
REMARK 900 1NU8 CONTAINS THE SAME PROTEIN COMPLEXED WITH NAG AND                
REMARK 900 DIPROTIN A                                                           
DBREF  1NU6 A   39   766  SWS    P27487   DPP4_HUMAN      39    766             
DBREF  1NU6 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 1NU6 ASN A  150  ASN  GLYCOSYLATION SITE                                 
MODRES 1NU6 ASN A   85  ASN  GLYCOSYLATION SITE                                 
MODRES 1NU6 ASN A  281  ASN  GLYCOSYLATION SITE                                 
MODRES 1NU6 ASN A  229  ASN  GLYCOSYLATION SITE                                 
MODRES 1NU6 ASN B  150  ASN  GLYCOSYLATION SITE                                 
MODRES 1NU6 ASN B   85  ASN  GLYCOSYLATION SITE                                 
MODRES 1NU6 ASN B  229  ASN  GLYCOSYLATION SITE                                 
MODRES 1NU6 ASN B   92  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 793      14                                                       
HET    NAG  A 794      14                                                       
HET    NAG  A 795      14                                                       
HET    NAG  A 796      14                                                       
HET    NAG  B 793      14                                                       
HET    NAG  B 794      14                                                       
HET    NAG  B 796      14                                                       
HET    NAG  B 797      14                                                       
HET     HG   1301       1                                                       
HET     HG   1302       1                                                       
HET     HG   1303       1                                                       
HET     HG   2301       1                                                       
HET     HG   2302       1                                                       
HET     HG   2303       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      HG MERCURY (II) ION                                                 
HETSYN     NAG NAG                                                              
FORMUL   3  NAG    8(C8 H15 N1 O6)                                              
FORMUL  11   HG    6(HG1 2+)                                                    
FORMUL  17  HOH   *322(H2 O1)                                                   
HELIX    1   1 THR A   44  ASN A   51  1                                   8    
HELIX    2   2 PHE A   95  GLY A   99  5                                   5    
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  421  MET A  425  5                                   5    
HELIX    6   6 LYS A  463  ALA A  465  5                                   3    
HELIX    7   7 ASN A  497  ASN A  506  1                                  10    
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  MET A  616  1                                  17    
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  VAL A  726  1                                  15    
HELIX   18  18 SER A  744  PHE A  763  1                                  20    
HELIX   19  19 THR B   44  LYS B   50  1                                   7    
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 VAL B  341  GLN B  344  5                                   4    
HELIX   23  23 GLU B  421  MET B  425  5                                   5    
HELIX   24  24 LYS B  463  ALA B  465  5                                   3    
HELIX   25  25 ASN B  497  GLN B  505  1                                   9    
HELIX   26  26 ASN B  562  THR B  570  1                                   9    
HELIX   27  27 GLY B  587  HIS B  592  1                                   6    
HELIX   28  28 ALA B  593  ASN B  595  5                                   3    
HELIX   29  29 THR B  600  LYS B  615  1                                  16    
HELIX   30  30 SER B  630  GLY B  641  1                                  12    
HELIX   31  31 ARG B  658  TYR B  662  5                                   5    
HELIX   32  32 ASP B  663  GLY B  672  1                                  10    
HELIX   33  33 ASN B  679  SER B  686  1                                   8    
HELIX   34  34 THR B  687  THR B  687  5                                   1    
HELIX   35  35 VAL B  688  VAL B  698  5                                  11    
HELIX   36  36 HIS B  712  VAL B  726  1                                  15    
HELIX   37  37 SER B  744  PHE B  763  1                                  20    
SHEET    1   A 4 ARG A  61  TRP A  62  0                                        
SHEET    2   A 4 GLU A  67  GLN A  72 -1  O  LEU A  69   N  ARG A  61           
SHEET    3   A 4 ASN A  75  ASN A  80 -1  O  LEU A  77   N  TYR A  70           
SHEET    4   A 4 SER A  86  LEU A  90 -1  O  SER A  87   N  VAL A  78           
SHEET    1   B 4 ILE A 102  ILE A 107  0                                        
SHEET    2   B 4 PHE A 113  LYS A 122 -1  O  LEU A 115   N  SER A 106           
SHEET    3   B 4 TYR A 128  ASP A 136 -1  O  SER A 131   N  TYR A 118           
SHEET    4   B 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1   C 4 TRP A 154  TRP A 157  0                                        
SHEET    2   C 4 LEU A 164  TRP A 168 -1  O  VAL A 167   N  TRP A 154           
SHEET    3   C 4 ASP A 171  LYS A 175 -1  O  TYR A 173   N  TYR A 166           
SHEET    4   C 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174           
SHEET    1   D 4 SER A 284  ILE A 287  0                                        
SHEET    2   D 4 THR A 265  ASN A 272 -1  N  PHE A 268   O  ILE A 287           
SHEET    3   D 4 PHE A 222  ASN A 229 -1  N  TYR A 225   O  PHE A 269           
SHEET    4   D 4 ILE A 194  ASN A 196 -1  N  TYR A 195   O  PHE A 228           
SHEET    1   E 4 SER A 284  ILE A 287  0                                        
SHEET    2   E 4 THR A 265  ASN A 272 -1  N  PHE A 268   O  ILE A 287           
SHEET    3   E 4 PHE A 222  ASN A 229 -1  N  TYR A 225   O  PHE A 269           
SHEET    4   E 4 LEU A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224           
SHEET    1   F 2 LEU A 235  PHE A 240  0                                        
SHEET    2   F 2 LYS A 250  PRO A 255 -1  O  VAL A 252   N  TYR A 238           
SHEET    1   G 4 HIS A 298  THR A 307  0                                        
SHEET    2   G 4 ARG A 310  ARG A 317 -1  O  SER A 312   N  THR A 304           
SHEET    3   G 4 TYR A 322  TYR A 330 -1  O  CYS A 328   N  ILE A 311           
SHEET    4   G 4 TRP A 337  CYS A 339 -1  O  ASN A 338   N  ASP A 329           
SHEET    1   H 4 HIS A 298  THR A 307  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  CYS A 328   N  ILE A 311           
SHEET    4   H 4 HIS A 345  MET A 348 -1  O  HIS A 345   N  MET A 325           
SHEET    1   I 4 HIS A 363  PHE A 364  0                                        
SHEET    2   I 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363           
SHEET    3   I 4 ARG A 382  GLN A 388 -1  O  CYS A 385   N  LYS A 373           
SHEET    4   I 4 THR A 395  PHE A 396 -1  O  THR A 395   N  TYR A 386           
SHEET    1   J 4 VAL A 404  LEU A 410  0                                        
SHEET    2   J 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  ALA A 409           
SHEET    3   J 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417           
SHEET    4   J 4 VAL A 442  CYS A 444 -1  O  THR A 443   N  LYS A 433           
SHEET    1   K 4 TYR A 457  PHE A 461  0                                        
SHEET    2   K 4 TYR A 467  CYS A 472 -1  O  GLN A 469   N  SER A 460           
SHEET    3   K 4 LEU A 479  SER A 484 -1  O  LEU A 479   N  CYS A 472           
SHEET    4   K 4 LYS A 489  GLU A 495 -1  O  LEU A 491   N  LEU A 482           
SHEET    1   L 8 SER A 511  ILE A 518  0                                        
SHEET    2   L 8 LYS A 523  LEU A 530 -1  O  TYR A 526   N  ASP A 515           
SHEET    3   L 8 ILE A 574  PHE A 578 -1  O  VAL A 575   N  ILE A 529           
SHEET    4   L 8 TYR A 540  VAL A 546  1  N  LEU A 543   O  ILE A 574           
SHEET    5   L 8 VAL A 619  TRP A 629  1  O  ASP A 620   N  TYR A 540           
SHEET    6   L 8 CYS A 649  VAL A 653  1  O  VAL A 653   N  GLY A 628           
SHEET    7   L 8 GLU A 699  GLY A 705  1  O  LEU A 701   N  ALA A 652           
SHEET    8   L 8 GLN A 731  TYR A 735  1  O  TYR A 735   N  HIS A 704           
SHEET    1   M 2 LYS B  41  THR B  42  0                                        
SHEET    2   M 2 VAL B 507  GLN B 508  1  O  GLN B 508   N  LYS B  41           
SHEET    1   N 4 ARG B  61  TRP B  62  0                                        
SHEET    2   N 4 GLU B  67  GLN B  72 -1  O  LEU B  69   N  ARG B  61           
SHEET    3   N 4 ASN B  75  ASN B  80 -1  O  LEU B  77   N  TYR B  70           
SHEET    4   N 4 SER B  86  LEU B  90 -1  O  PHE B  89   N  ILE B  76           
SHEET    1   O 4 ILE B 102  ILE B 107  0                                        
SHEET    2   O 4 PHE B 113  LYS B 122 -1  O  LEU B 115   N  SER B 106           
SHEET    3   O 4 TYR B 128  ASP B 136 -1  O  THR B 129   N  VAL B 121           
SHEET    4   O 4 GLN B 141  LEU B 142 -1  O  GLN B 141   N  ASP B 136           
SHEET    1   P 4 TRP B 154  TRP B 157  0                                        
SHEET    2   P 4 LEU B 164  TRP B 168 -1  O  ALA B 165   N  THR B 156           
SHEET    3   P 4 ASP B 171  LYS B 175 -1  O  LYS B 175   N  LEU B 164           
SHEET    4   P 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1   Q 4 ILE B 285  ILE B 287  0                                        
SHEET    2   Q 4 THR B 265  ASN B 272 -1  N  VAL B 270   O  ILE B 285           
SHEET    3   Q 4 PHE B 222  ASN B 229 -1  N  LEU B 223   O  VAL B 271           
SHEET    4   Q 4 ILE B 194  ASN B 196 -1  N  TYR B 195   O  PHE B 228           
SHEET    1   R 4 ILE B 285  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  LEU B 223   O  VAL B 271           
SHEET    4   R 4 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224           
SHEET    1   S 2 LEU B 235  PHE B 240  0                                        
SHEET    2   S 2 LYS B 250  PRO B 255 -1  O  VAL B 252   N  TYR B 238           
SHEET    1   T 4 HIS B 298  THR B 307  0                                        
SHEET    2   T 4 ARG B 310  ARG B 317 -1  O  SER B 312   N  THR B 304           
SHEET    3   T 4 TYR B 322  TYR B 330 -1  O  ASP B 326   N  LEU B 313           
SHEET    4   T 4 TRP B 337  CYS B 339 -1  O  ASN B 338   N  ASP B 329           
SHEET    1   U 4 HIS B 298  THR B 307  0                                        
SHEET    2   U 4 ARG B 310  ARG B 317 -1  O  SER B 312   N  THR B 304           
SHEET    3   U 4 TYR B 322  TYR B 330 -1  O  ASP B 326   N  LEU B 313           
SHEET    4   U 4 HIS B 345  MET B 348 -1  O  HIS B 345   N  MET B 325           
SHEET    1   V 4 HIS B 363  PHE B 364  0                                        
SHEET    2   V 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3   V 4 ARG B 382  GLN B 388 -1  O  CYS B 385   N  LYS B 373           
SHEET    4   V 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1   W 4 VAL B 404  LEU B 410  0                                        
SHEET    2   W 4 TYR B 414  SER B 419 -1  O  TYR B 416   N  ALA B 409           
SHEET    3   W 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4   W 4 VAL B 442  CYS B 444 -1  O  THR B 443   N  LYS B 433           
SHEET    1   X 4 TYR B 457  PHE B 461  0                                        
SHEET    2   X 4 TYR B 467  CYS B 472 -1  O  GLN B 469   N  SER B 460           
SHEET    3   X 4 LEU B 479  SER B 484 -1  O  THR B 481   N  LEU B 470           
SHEET    4   X 4 LYS B 489  GLY B 490 -1  O  LYS B 489   N  SER B 484           
SHEET    1   Y 8 SER B 511  LEU B 519  0                                        
SHEET    2   Y 8 THR B 522  LEU B 530 -1  O  PHE B 524   N  ILE B 517           
SHEET    3   Y 8 ILE B 574  PHE B 578 -1  O  SER B 577   N  GLN B 527           
SHEET    4   Y 8 TYR B 540  ASP B 545  1  N  LEU B 543   O  ILE B 574           
SHEET    5   Y 8 VAL B 619  TRP B 629  1  O  ALA B 625   N  LEU B 544           
SHEET    6   Y 8 CYS B 649  VAL B 653  1  O  VAL B 653   N  GLY B 628           
SHEET    7   Y 8 GLU B 699  GLY B 705  1  O  LEU B 701   N  ALA B 652           
SHEET    8   Y 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 A 794                        
LINK         ND2 ASN A 150                 C1  NAG A 793                        
LINK         ND2 ASN A 229                 C1  NAG A 796                        
LINK         ND2 ASN A 281                 C1  NAG A 795                        
LINK         ND2 ASN B  85                 C1  NAG B 794                        
LINK         ND2 ASN B  92                 C1  NAG B 797                        
LINK         ND2 ASN B 150                 C1  NAG B 793                        
LINK         ND2 ASN B 229                 C1  NAG B 796                        
CISPEP   1 GLY A  474    PRO A  475          0         7.50                     
CISPEP   2 GLY B  474    PRO B  475          0         3.18                     
CRYST1   65.496   68.240  419.289  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      0.015268  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014654  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002385        0.00000                         
TER    5964      PRO A 766                                                      
TER   11928      PRO B 766                                                      
MASTER      336    0   14   37  102    0    0    612366    2  140  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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