Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 4A5S-pdb

Name Class
4A5S-pdb
HEADER    HYDROLASE                               28-OCT-11   4A5S              
TITLE     CRYSTAL STRUCTURE OF HUMAN DPP4 IN COMPLEX WITH A NOVAL HETEROCYCLIC  
TITLE    2 DPP4 INHIBITOR                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM, DIPEPTIDYL PEPTIDASE  
COMPND   5  4, ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,         
COMPND   6  DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,    
COMPND   7  TP103, CD_ANTIGEN=CD26;                                             
COMPND   8 EC: 3.4.14.5;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    HYDROLASE, TYPE 2 DIABETES, NOVARTIS COMPOUND NVP-BIV988              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.OSTERMANN,M.KROEMER,F.ZINK,B.GERHARTZ,J.M.SUTTON,D.E.CLARK,         
AUTHOR   2 S.J.DUNSDON,G.FENTON,A.FILLMORE,N.V.HARRIS,C.HIGGS,C.A.HURLEY,       
AUTHOR   3 S.L.KRINTEL,R.E.MACKENZIE,A.DUTTAROY,E.GANGL,W.MANIARA,R.SEDRANI,    
AUTHOR   4 K.NAMOTO,F.SIROCKIN,J.TRAPPE,U.HASSIEPEN,D.K.BAESCHLIN               
REVDAT   1   08-FEB-12 4A5S    0                                                
JRNL        AUTH   J.M.SUTTON,D.E.CLARK,S.J.DUNSDON,G.FENTON,A.FILLMORE,        
JRNL        AUTH 2 N.V.HARRIS,C.HIGGS,C.A.HURLEY,S.L.KRINTEL,R.E.MACKENZIE,     
JRNL        AUTH 3 A.DUTTAROY,E.GANGL,W.MANIARA,R.SEDRANI,K.NAMOTO,N.OSTERMANN, 
JRNL        AUTH 4 B.GERHARTZ,F.SIROCKIN,J.TRAPPE,U.HASSIEPEN,D.K.BAESCHLIN     
JRNL        TITL   NOVEL HETEROCYCLIC DPP-4 INHIBITORS FOR THE TREATMENT OF     
JRNL        TITL 2 TYPE 2 DIABETES.                                             
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  22  1464 2012              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   22177783                                                     
JRNL        DOI    10.1016/J.BMCL.2011.11.054                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.62 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 68.06                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.74                          
REMARK   3   NUMBER OF REFLECTIONS             : 284274                         
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)  : 0.1641                         
REMARK   3   R VALUE            (WORKING SET)  : 0.1638                         
REMARK   3   FREE R VALUE                      : 0.1789                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 1.80                           
REMARK   3   FREE R VALUE TEST SET COUNT       : 5116                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.62                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.66                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.74                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 20777                    
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1925                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 20403                    
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1924                   
REMARK   3   BIN FREE R VALUE                        : 0.1959                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 1.80                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 374                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12058                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 333                                     
REMARK   3   SOLVENT ATOMS            : 1590                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.73                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.1534                                              
REMARK   3    B22 (A**2) : 0.2328                                               
REMARK   3    B33 (A**2) : -0.0794                                              
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.155               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.068               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.066               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.066               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.064               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.9644                        
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.9596                        
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 12792  ; 2.00   ; HARMONIC            
REMARK   3    BOND ANGLES               : 17481  ; 2.00   ; HARMONIC            
REMARK   3    TORSION ANGLES            : 4368   ; 2.00   ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 311    ; 2.00   ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1868   ; 5.00   ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 12792  ; 20.00  ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1677   ; 5.00   ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 16099  ; 4.00   ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.05                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.30                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.91                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.    
REMARK   3   ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY.                        
REMARK   4                                                                      
REMARK   4 4A5S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-OCT-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-50100.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00054                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 284276                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.62                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 87.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.89                               
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.22                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.09                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.20                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.2                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 UL PROTEIN, 0.4 UL RESERVOIR,          
REMARK 280  0.25 UL WATER; PROTEIN SOLUTION: 5.2 MG/ML DPP4, 25 MM              
REMARK 280  TRIS PH 8, 25 MM NACL, 2 MM NVP-BIV988-AA-1, 2% DMSO;               
REMARK 280  RESERVOIR SOLUTION: 40% PEG 1000, 200 MM TRIS PH 9.0, 200           
REMARK 280  MM AMMONIUM SULFATE, 5% GLYCEROL                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       48.59150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       95.34950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.71200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       95.34950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.59150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.71200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10090 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 60290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    39                                                      
REMARK 465     ALA A   768                                                      
REMARK 465     ALA A   769                                                      
REMARK 465     SER A   770                                                      
REMARK 465     TRP A   771                                                      
REMARK 465     SER A   772                                                      
REMARK 465     HIS A   773                                                      
REMARK 465     PRO A   774                                                      
REMARK 465     GLN A   775                                                      
REMARK 465     PHE A   776                                                      
REMARK 465     GLU A   777                                                      
REMARK 465     LYS A   778                                                      
REMARK 465     SER B    39                                                      
REMARK 465     PRO B   774                                                      
REMARK 465     GLN B   775                                                      
REMARK 465     PHE B   776                                                      
REMARK 465     GLU B   777                                                      
REMARK 465     LYS B   778                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ALA A 767    CA   C    O    CB                                   
REMARK 470     HIS B 773    CA   C    O    CB   CG   ND1  CD2  CE1  NE2         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  74       -5.68     64.71                                   
REMARK 500    GLN A 123     -101.46   -111.60                                   
REMARK 500    TRP A 124     -144.44    -95.83                                   
REMARK 500    HIS A 162       35.67   -151.42                                   
REMARK 500    ILE A 193      -56.78   -128.05                                   
REMARK 500    SER A 242     -165.31     64.32                                   
REMARK 500    GLN A 320       37.64    -74.86                                   
REMARK 500    LYS A 423       16.17     59.41                                   
REMARK 500    ASN A 450       70.55   -151.64                                   
REMARK 500    ASN A 487       26.78   -140.40                                   
REMARK 500    TYR A 547      -75.68   -117.44                                   
REMARK 500    ARG A 597       47.54   -143.09                                   
REMARK 500    THR A 600      -96.58   -119.12                                   
REMARK 500    SER A 630     -124.30     64.27                                   
REMARK 500    ASP A 678     -101.30   -109.35                                   
REMARK 500    ASN A 710      -66.54   -101.77                                   
REMARK 500    ASP A 739     -159.43   -102.43                                   
REMARK 500    ILE A 742       52.99     38.76                                   
REMARK 500    ASN B  74       -0.85     66.78                                   
REMARK 500    GLN B 123      -99.05   -110.60                                   
REMARK 500    TRP B 124     -143.42    -97.47                                   
REMARK 500    HIS B 162       32.97   -152.17                                   
REMARK 500    ILE B 193      -60.23   -130.22                                   
REMARK 500    SER B 242     -163.63     62.43                                   
REMARK 500    GLN B 320       38.28    -77.11                                   
REMARK 500    LYS B 423       16.35     57.11                                   
REMARK 500    ASN B 450       77.22   -159.86                                   
REMARK 500    TYR B 547      -76.25   -118.57                                   
REMARK 500    ARG B 597       50.02   -141.66                                   
REMARK 500    THR B 600      -95.35   -119.74                                   
REMARK 500    SER B 630     -121.54     64.36                                   
REMARK 500    ASP B 678      -95.92   -109.20                                   
REMARK 500    ASN B 710      -69.79    -98.95                                   
REMARK 500    ASP B 739     -156.61   -104.18                                   
REMARK 500    ILE B 742       52.83     38.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ILE B 389        25.0      L          L   OUTSIDE RANGE           
REMARK 500    LYS B 463        24.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N7F A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1767                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1768                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1769                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N7F B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1773                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1774                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1775                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A  85 RESIDUES 1085 TO 1089                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 150 RESIDUES 1150 TO 1150                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 219 RESIDUES 1219 TO 1219                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 229 RESIDUES 1229 TO 1229                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 281 RESIDUES 1281 TO 1281                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 321 RESIDUES 1321 TO 1321                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 520 RESIDUES 1520 TO 1520                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO         
REMARK 800   ASN B  85 RESIDUES 2085 TO 2085                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO         
REMARK 800   ASN B 150 RESIDUES 2150 TO 2150                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO         
REMARK 800   ASN B 219 RESIDUES 2219 TO 2219                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO         
REMARK 800   ASN B 229 RESIDUES 2229 TO 2229                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO         
REMARK 800   ASN B 281 RESIDUES 2281 TO 2281                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG B2321 BOUND TO ASN B 321                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1W1I   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPPIV OR              
REMARK 900  CD26) IN COMPLEX WITH ADENOSINE DEAMINASE                           
REMARK 900 RELATED ID: 1RWQ   RELATED DB: PDB                                   
REMARK 900  HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH 5-                    
REMARK 900  AMINOMETHYL-6-(2,4-DICHLORO-PHENYL)-2-(3,5-DIMETHOXY                
REMARK 900  -PHENYL)-PYRIMIDIN-4-YLAMINE                                        
REMARK 900 RELATED ID: 1TK3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN APO DIPEPTIDYL PEPTIDASE IV/             
REMARK 900  CD26                                                                
REMARK 900 RELATED ID: 2BGR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HIV-1 TAT DERIVED NONAPEPTIDES                 
REMARK 900  TAT(1-9) BOUND TO THE ACTIVE SITE OF DIPEPTIDYL                     
REMARK 900  PEPTIDASE IV (CD26)                                                 
REMARK 900 RELATED ID: 1N1M   RELATED DB: PDB                                   
REMARK 900  HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 IN COMPLEX WITH                  
REMARK 900  ANINHIBITOR                                                         
REMARK 900 RELATED ID: 2G5T   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (                
REMARK 900  DPPIV)COMPLEXED WITH CYANOPYRROLIDINE (C5-PRO-PRO)                  
REMARK 900  INHIBITOR 21AG                                                      
REMARK 900 RELATED ID: 1NU6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (DPP             
REMARK 900  -IV)                                                                
REMARK 900 RELATED ID: 1PFQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN APO DIPEPTIDYL PEPTIDASE IV              
REMARK 900   /CD26                                                              
REMARK 900 RELATED ID: 1TKR   RELATED DB: PDB                                   
REMARK 900  HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 INHIBITED                        
REMARK 900  WITHDIISOPROPYL FLUOROPHOSPHATE                                     
REMARK 900 RELATED ID: 2G5P   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (                
REMARK 900  DPPIV)COMPLEXED WITH CYANOPYRROLIDINE (C5-PRO-PRO)                  
REMARK 900  INHIBITOR 21AC                                                      
REMARK 900 RELATED ID: 1X70   RELATED DB: PDB                                   
REMARK 900  HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH A BETA                
REMARK 900  AMINOACID INHIBITOR                                                 
REMARK 900 RELATED ID: 1WCY   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (                
REMARK 900  DPPIV)COMPLEX WITH DIPROTIN A                                       
REMARK 900 RELATED ID: 1R9M   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV AT               
REMARK 900  2.1ANG. RESOLUTION.                                                 
REMARK 900 RELATED ID: 1NU8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (DPP             
REMARK 900  -IV)IN COMPLEX WITH DIPROTIN A (ILI)                                
REMARK 900 RELATED ID: 1J2E   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV                  
REMARK 900 RELATED ID: 2JID   RELATED DB: PDB                                   
REMARK 900  HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH 1-(3,4                
REMARK 900  -DIMETHOXY-PHENYL)-3-M-TOLYL-PIPERIDINE-4-YLAMINE                   
REMARK 900 RELATED ID: 1U8E   RELATED DB: PDB                                   
REMARK 900  HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 MUTANT Y547F                     
REMARK 900 RELATED ID: 2G63   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (                
REMARK 900  DPPIV)COMPLEXED WITH CYANOPYRROLIDINE (C5-PRO-PRO)                  
REMARK 900  INHIBITOR 24B                                                       
REMARK 900 RELATED ID: 2BUB   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPDIDASE IV (CD26            
REMARK 900  ) IN COMPLEX WITH A REVERSED AMIDE INHIBITOR                        
REMARK 900 RELATED ID: 2AJL   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF NOVEL BIARYL-BASED DIPEPTIDYL                    
REMARK 900  PEPTIDASEIV INHIBITOR                                               
REMARK 900 RELATED ID: 2BGN   RELATED DB: PDB                                   
REMARK 900  HIV-1 TAT PROTEIN DERIVED N-TERMINAL NONAPEPTIDE TRP2               
REMARK 900  -TAT(1-9) BOUND TO THE ACTIVE SITE OF DIPEPTIDYL                    
REMARK 900  PEPTIDASE IV (CD26)                                                 
REMARK 900 RELATED ID: 1R9N   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV                  
REMARK 900  INCOMPLEX WITH A DECAPEPTIDE (TNPY) AT 2.3 ANG.                     
REMARK 900  RESOLUTION                                                          
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 S437I SEQUENCE CONFLICT KNOWN IN UNIPROT.                            
DBREF  4A5S A   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  4A5S B   39   766  UNP    P27487   DPP4_HUMAN      39    766             
SEQADV 4A5S ALA A  767  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S ALA A  768  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S ALA A  769  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S SER A  770  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S TRP A  771  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S SER A  772  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S HIS A  773  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S PRO A  774  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S GLN A  775  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S PHE A  776  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S GLU A  777  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S LYS A  778  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S ILE A  437  UNP  P27487    SER   437 CONFLICT                       
SEQADV 4A5S ALA B  767  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S ALA B  768  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S ALA B  769  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S SER B  770  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S TRP B  771  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S SER B  772  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S HIS B  773  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S PRO B  774  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S GLN B  775  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S PHE B  776  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S GLU B  777  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S LYS B  778  UNP  P27487              EXPRESSION TAG                 
SEQADV 4A5S ILE B  437  UNP  P27487    SER   437 CONFLICT                       
SEQRES   1 A  740  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 A  740  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 A  740  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 A  740  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 A  740  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 A  740  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 A  740  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 A  740  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 A  740  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 A  740  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 A  740  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 A  740  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 A  740  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 A  740  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 A  740  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 A  740  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 A  740  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 A  740  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 A  740  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 A  740  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 A  740  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 A  740  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 A  740  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 A  740  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 A  740  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 A  740  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 A  740  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 A  740  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 A  740  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 A  740  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 A  740  ARG ASN LEU TYR LYS ILE GLN LEU ILE ASP TYR THR LYS          
SEQRES  32 A  740  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 A  740  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 A  740  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 A  740  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 A  740  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 A  740  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 A  740  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 A  740  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 A  740  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 A  740  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 A  740  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 A  740  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 A  740  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 A  740  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 A  740  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 A  740  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 A  740  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 A  740  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 A  740  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 A  740  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 A  740  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 A  740  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 A  740  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 A  740  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 A  740  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
SEQRES  57 A  740  ALA ALA ALA SER TRP SER HIS PRO GLN PHE GLU LYS              
SEQRES   1 B  740  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 B  740  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 B  740  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 B  740  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 B  740  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 B  740  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 B  740  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 B  740  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 B  740  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 B  740  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 B  740  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 B  740  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 B  740  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 B  740  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 B  740  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 B  740  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 B  740  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 B  740  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 B  740  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 B  740  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 B  740  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 B  740  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 B  740  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 B  740  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 B  740  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 B  740  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 B  740  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 B  740  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 B  740  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 B  740  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 B  740  ARG ASN LEU TYR LYS ILE GLN LEU ILE ASP TYR THR LYS          
SEQRES  32 B  740  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 B  740  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 B  740  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 B  740  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 B  740  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 B  740  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 B  740  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 B  740  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 B  740  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 B  740  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 B  740  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 B  740  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 B  740  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 B  740  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 B  740  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 B  740  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 B  740  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 B  740  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 B  740  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 B  740  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 B  740  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 B  740  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 B  740  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 B  740  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 B  740  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
SEQRES  57 B  740  ALA ALA ALA SER TRP SER HIS PRO GLN PHE GLU LYS              
HET    N7F  A 901      37                                                       
HET    NAG  A1085      14                                                       
HET    NAG  A1086      14                                                       
HET    MAN  A1087      11                                                       
HET    MAN  A1088      11                                                       
HET    MAN  A1089      11                                                       
HET    NAG  A1150      14                                                       
HET    NAG  A1219      14                                                       
HET    NAG  A1229      14                                                       
HET    NAG  A1281      14                                                       
HET    NAG  A1321      14                                                       
HET    NAG  A1520      14                                                       
HET    SO4  A1767       5                                                       
HET    SO4  A1768       5                                                       
HET    SO4  A1769       5                                                       
HET    N7F  B 901      37                                                       
HET    SO4  B1773       5                                                       
HET    SO4  B1774       5                                                       
HET    SO4  B1775       5                                                       
HET    NAG  B2085      14                                                       
HET    NAG  B2150      14                                                       
HET    NAG  B2219      14                                                       
HET    NAG  B2229      14                                                       
HET    NAG  B2281      14                                                       
HET    NAG  B2321      14                                                       
HETNAM     N7F 6-[(3S)-3-AMINOPIPERIDIN-1-YL]-5-BENZYL-4-                       
HETNAM   2 N7F  OXO-3-(QUINOLIN-4-YLMETHYL)-4,5-DIHYDRO-3H-                     
HETNAM   3 N7F  PYRROLO[3,2-D]PYRIMIDINE-7-CARBONITRILE                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  N7F    2(C29 H27 N7 O)                                              
FORMUL   4  NAG    14(C8 H15 N O6)                                              
FORMUL   5  MAN    3(C6 H12 O6)                                                 
FORMUL   6  SO4    6(O4 S 2-)                                                   
FORMUL   7  HOH   *1590(H2 O)                                                   
HELIX    1   1 THR A   44  ASN A   51  1                                   8    
HELIX    2   2 ASP A  200  VAL A  207  1                                   8    
HELIX    3   3 PRO A  290  ILE A  295  1                                   6    
HELIX    4   4 VAL A  341  GLN A  344  5                                   4    
HELIX    5   5 GLU A  421  MET A  425  5                                   5    
HELIX    6   6 ASN A  497  GLN A  505  1                                   9    
HELIX    7   7 ASN A  562  THR A  570  1                                   9    
HELIX    8   8 GLY A  587  HIS A  592  1                                   6    
HELIX    9   9 ALA A  593  ASN A  595  5                                   3    
HELIX   10  10 THR A  600  LYS A  615  1                                  16    
HELIX   11  11 SER A  630  GLY A  641  1                                  12    
HELIX   12  12 ARG A  658  TYR A  662  5                                   5    
HELIX   13  13 ASP A  663  GLY A  672  1                                  10    
HELIX   14  14 ASN A  679  SER A  686  1                                   8    
HELIX   15  15 VAL A  688  VAL A  698  5                                  11    
HELIX   16  16 PHE A  713  VAL A  726  1                                  14    
HELIX   17  17 SER A  744  PHE A  763  1                                  20    
HELIX   18  18 THR B   44  ASN B   51  1                                   8    
HELIX   19  19 GLU B   91  GLU B   97  5                                   7    
HELIX   20  20 ASP B  200  VAL B  207  1                                   8    
HELIX   21  21 PRO B  290  ILE B  295  1                                   6    
HELIX   22  22 VAL B  341  GLN B  344  5                                   4    
HELIX   23  23 GLU B  421  MET B  425  5                                   5    
HELIX   24  24 ASN B  497  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 HIS B  712  VAL B  726  1                                  15    
HELIX   35  35 SER B  744  PHE B  763  1                                  20    
SHEET    1  AA 2 LYS A  41  THR A  42  0                                        
SHEET    2  AA 2 VAL A 507  GLN A 508  1  N  GLN A 508   O  LYS A  41           
SHEET    1  AB 4 LEU A  60  TRP A  62  0                                        
SHEET    2  AB 4 GLU A  67  GLN A  72 -1  O  LEU A  69   N  ARG A  61           
SHEET    3  AB 4 ASN A  75  ASN A  80 -1  O  ASN A  75   N  GLN A  72           
SHEET    4  AB 4 SER A  86  LEU A  90 -1  O  SER A  87   N  VAL A  78           
SHEET    1  AC 4 ASP A 104  ILE A 107  0                                        
SHEET    2  AC 4 PHE A 113  LYS A 122 -1  O  LEU A 115   N  SER A 106           
SHEET    3  AC 4 TYR A 128  ASP A 136 -1  O  THR A 129   N  VAL A 121           
SHEET    4  AC 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1  AD 4 THR A 152  TRP A 157  0                                        
SHEET    2  AD 4 LEU A 164  TRP A 168 -1  O  ALA A 165   N  THR A 156           
SHEET    3  AD 4 ASP A 171  LYS A 175 -1  O  ASP A 171   N  TRP A 168           
SHEET    4  AD 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174           
SHEET    1  AE 2 ILE A 194  ASN A 196  0                                        
SHEET    2  AE 2 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    1  AF 2 LEU A 214  TRP A 216  0                                        
SHEET    2  AF 2 PHE A 222  ASN A 229 -1  O  ALA A 224   N  TRP A 215           
SHEET    1  AG 4 SER A 284  ILE A 287  0                                        
SHEET    2  AG 4 THR A 265  ASN A 272 -1  O  PHE A 268   N  ILE A 287           
SHEET    3  AG 4 PHE A 222  ASN A 229 -1  O  LEU A 223   N  VAL A 271           
SHEET    4  AG 4 LEU A 214  TRP A 216 -1  O  TRP A 215   N  ALA A 224           
SHEET    1  AH 4 SER A 284  ILE A 287  0                                        
SHEET    2  AH 4 THR A 265  ASN A 272 -1  O  PHE A 268   N  ILE A 287           
SHEET    3  AH 4 PHE A 222  ASN A 229 -1  O  LEU A 223   N  VAL A 271           
SHEET    4  AH 4 ILE A 194  ASN A 196 -1  O  TYR A 195   N  PHE A 228           
SHEET    1  AI 2 LEU A 235  PHE A 240  0                                        
SHEET    2  AI 2 LYS A 250  PRO A 255 -1  O  LYS A 250   N  PHE A 240           
SHEET    1  AJ 4 HIS A 298  THR A 307  0                                        
SHEET    2  AJ 4 ARG A 310  ARG A 317 -1  O  ARG A 310   N  ALA A 306           
SHEET    3  AJ 4 TYR A 322  TYR A 330 -1  O  TYR A 322   N  ARG A 317           
SHEET    4  AJ 4 TRP A 337  CYS A 339  1  O  ASN A 338   N  ASP A 329           
SHEET    1  AK 4 HIS A 298  THR A 307  0                                        
SHEET    2  AK 4 ARG A 310  ARG A 317 -1  O  ARG A 310   N  ALA A 306           
SHEET    3  AK 4 TYR A 322  TYR A 330 -1  O  TYR A 322   N  ARG A 317           
SHEET    4  AK 4 HIS A 345  MET A 348 -1  O  HIS A 345   N  MET A 325           
SHEET    1  AL 2 TRP A 337  CYS A 339  0                                        
SHEET    2  AL 2 TYR A 322  TYR A 330  1  O  ASP A 329   N  ASN A 338           
SHEET    1  AM 4 HIS A 363  PHE A 364  0                                        
SHEET    2  AM 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363           
SHEET    3  AM 4 ARG A 382  GLN A 388 -1  O  HIS A 383   N  ILE A 375           
SHEET    4  AM 4 THR A 395  PHE A 396 -1  O  THR A 395   N  TYR A 386           
SHEET    1  AN 4 VAL A 404  LEU A 410  0                                        
SHEET    2  AN 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  GLU A 408           
SHEET    3  AN 4 ASN A 430  GLN A 435 -1  O  ASN A 430   N  SER A 419           
SHEET    4  AN 4 ASP A 438  CYS A 444 -1  N  ASP A 438   O  GLN A 435           
SHEET    1  AO 4 TYR A 457  PHE A 461  0                                        
SHEET    2  AO 4 TYR A 467  CYS A 472 -1  O  GLN A 469   N  SER A 460           
SHEET    3  AO 4 LEU A 479  SER A 484 -1  O  LEU A 479   N  CYS A 472           
SHEET    4  AO 4 LYS A 489  GLU A 495 -1  O  LYS A 489   N  SER A 484           
SHEET    1  AP 8 SER A 511  LEU A 519  0                                        
SHEET    2  AP 8 THR A 522  LEU A 530 -1  O  THR A 522   N  LEU A 519           
SHEET    3  AP 8 ILE A 574  PHE A 578 -1  O  VAL A 575   N  ILE A 529           
SHEET    4  AP 8 TYR A 540  ASP A 545  1  O  PRO A 541   N  ILE A 574           
SHEET    5  AP 8 VAL A 619  TRP A 629  1  N  ASP A 620   O  TYR A 540           
SHEET    6  AP 8 CYS A 649  VAL A 653  1  O  CYS A 649   N  ILE A 626           
SHEET    7  AP 8 GLU A 699  GLY A 705  1  O  GLU A 699   N  GLY A 650           
SHEET    8  AP 8 GLN A 731  TYR A 735  1  O  GLN A 731   N  LEU A 702           
SHEET    1  BA 2 LYS B  41  THR B  42  0                                        
SHEET    2  BA 2 VAL B 507  GLN B 508  1  N  GLN B 508   O  LYS B  41           
SHEET    1  BB 4 LEU B  60  TRP B  62  0                                        
SHEET    2  BB 4 GLU B  67  GLN B  72 -1  O  LEU B  69   N  ARG B  61           
SHEET    3  BB 4 ASN B  75  ASN B  80 -1  O  ASN B  75   N  GLN B  72           
SHEET    4  BB 4 SER B  86  LEU B  90 -1  O  SER B  87   N  VAL B  78           
SHEET    1  BC 4 ASP B 104  ILE B 107  0                                        
SHEET    2  BC 4 PHE B 113  LYS B 122 -1  O  LEU B 115   N  SER B 106           
SHEET    3  BC 4 TYR B 128  ASP B 136 -1  O  THR B 129   N  VAL B 121           
SHEET    4  BC 4 GLN B 141  ILE B 143 -1  O  GLN B 141   N  ASP B 136           
SHEET    1  BD 4 TRP B 154  TRP B 157  0                                        
SHEET    2  BD 4 LEU B 164  TRP B 168 -1  O  ALA B 165   N  THR B 156           
SHEET    3  BD 4 ASP B 171  LYS B 175 -1  O  ASP B 171   N  TRP B 168           
SHEET    4  BD 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1  BE 2 ILE B 194  ASN B 196  0                                        
SHEET    2  BE 2 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    1  BF 2 LEU B 214  TRP B 216  0                                        
SHEET    2  BF 2 PHE B 222  ASN B 229 -1  O  ALA B 224   N  TRP B 215           
SHEET    1  BG 4 ILE B 285  ILE B 287  0                                        
SHEET    2  BG 4 THR B 265  ASN B 272 -1  O  PHE B 268   N  ILE B 287           
SHEET    3  BG 4 PHE B 222  ASN B 229 -1  O  LEU B 223   N  VAL B 271           
SHEET    4  BG 4 LEU B 214  TRP B 216 -1  O  TRP B 215   N  ALA B 224           
SHEET    1  BH 4 ILE B 285  ILE B 287  0                                        
SHEET    2  BH 4 THR B 265  ASN B 272 -1  O  PHE B 268   N  ILE B 287           
SHEET    3  BH 4 PHE B 222  ASN B 229 -1  O  LEU B 223   N  VAL B 271           
SHEET    4  BH 4 ILE B 194  ASN B 196 -1  O  TYR B 195   N  PHE B 228           
SHEET    1  BI 2 LEU B 235  PHE B 240  0                                        
SHEET    2  BI 2 LYS B 250  PRO B 255 -1  O  LYS B 250   N  PHE B 240           
SHEET    1  BJ 4 HIS B 298  THR B 307  0                                        
SHEET    2  BJ 4 ARG B 310  ARG B 317 -1  O  ARG B 310   N  ALA B 306           
SHEET    3  BJ 4 TYR B 322  TYR B 330 -1  O  TYR B 322   N  ARG B 317           
SHEET    4  BJ 4 TRP B 337  CYS B 339  1  O  ASN B 338   N  ASP B 329           
SHEET    1  BK 4 HIS B 298  THR B 307  0                                        
SHEET    2  BK 4 ARG B 310  ARG B 317 -1  O  ARG B 310   N  ALA B 306           
SHEET    3  BK 4 TYR B 322  TYR B 330 -1  O  TYR B 322   N  ARG B 317           
SHEET    4  BK 4 HIS B 345  MET B 348 -1  O  HIS B 345   N  MET B 325           
SHEET    1  BL 2 TRP B 337  CYS B 339  0                                        
SHEET    2  BL 2 TYR B 322  TYR B 330  1  O  ASP B 329   N  ASN B 338           
SHEET    1  BM 4 HIS B 363  PHE B 364  0                                        
SHEET    2  BM 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3  BM 4 ARG B 382  GLN B 388 -1  O  HIS B 383   N  ILE B 375           
SHEET    4  BM 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1  BN 4 VAL B 404  LEU B 410  0                                        
SHEET    2  BN 4 TYR B 414  SER B 419 -1  O  TYR B 416   N  GLU B 408           
SHEET    3  BN 4 ASN B 430  GLN B 435 -1  O  ASN B 430   N  SER B 419           
SHEET    4  BN 4 ASP B 438  CYS B 444 -1  N  ASP B 438   O  GLN B 435           
SHEET    1  BO 4 TYR B 457  PHE B 461  0                                        
SHEET    2  BO 4 TYR B 467  CYS B 472 -1  O  GLN B 469   N  SER B 460           
SHEET    3  BO 4 LEU B 479  SER B 484 -1  O  LEU B 479   N  CYS B 472           
SHEET    4  BO 4 LYS B 489  GLU B 495 -1  O  LYS B 489   N  SER B 484           
SHEET    1  BP 8 SER B 511  LEU B 519  0                                        
SHEET    2  BP 8 THR B 522  LEU B 530 -1  O  THR B 522   N  LEU B 519           
SHEET    3  BP 8 ILE B 574  PHE B 578 -1  O  VAL B 575   N  ILE B 529           
SHEET    4  BP 8 TYR B 540  ASP B 545  1  O  PRO B 541   N  ILE B 574           
SHEET    5  BP 8 VAL B 619  TRP B 629  1  N  ASP B 620   O  TYR B 540           
SHEET    6  BP 8 CYS B 649  VAL B 653  1  O  CYS B 649   N  ILE B 626           
SHEET    7  BP 8 GLU B 699  GLY B 705  1  O  GLU B 699   N  GLY B 650           
SHEET    8  BP 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  LEU B 702           
SSBOND   1 CYS A  328    CYS A  339                          1555   1555  2.07  
SSBOND   2 CYS A  385    CYS A  394                          1555   1555  2.04  
SSBOND   3 CYS A  444    CYS A  447                          1555   1555  2.01  
SSBOND   4 CYS A  454    CYS A  472                          1555   1555  2.10  
SSBOND   5 CYS A  649    CYS A  762                          1555   1555  2.08  
SSBOND   6 CYS B  328    CYS B  339                          1555   1555  2.06  
SSBOND   7 CYS B  385    CYS B  394                          1555   1555  2.05  
SSBOND   8 CYS B  444    CYS B  447                          1555   1555  2.03  
SSBOND   9 CYS B  454    CYS B  472                          1555   1555  2.08  
SSBOND  10 CYS B  649    CYS B  762                          1555   1555  2.06  
LINK         ND2 ASN A  85                 C1  NAG A1085     1555   1555  1.43  
LINK         ND2 ASN A 150                 C1  NAG A1150     1555   1555  1.43  
LINK         ND2 ASN A 219                 C1  NAG A1219     1555   1555  1.43  
LINK         ND2 ASN A 229                 C1  NAG A1229     1555   1555  1.43  
LINK         ND2 ASN A 281                 C1  NAG A1281     1555   1555  1.43  
LINK         ND2 ASN A 321                 C1  NAG A1321     1555   1555  1.44  
LINK         ND2 ASN A 520                 C1  NAG A1520     1555   1555  1.43  
LINK         O4  NAG A1085                 C1  NAG A1086     1555   1555  1.41  
LINK         O4  NAG A1086                 C1  MAN A1087     1555   1555  1.44  
LINK         O6  MAN A1087                 C1  MAN A1089     1555   1555  1.38  
LINK         O3  MAN A1087                 C1  MAN A1088     1555   1555  1.42  
LINK         ND2 ASN B  85                 C1  NAG B2085     1555   1555  1.43  
LINK         ND2 ASN B 150                 C1  NAG B2150     1555   1555  1.43  
LINK         ND2 ASN B 219                 C1  NAG B2219     1555   1555  1.43  
LINK         ND2 ASN B 229                 C1  NAG B2229     1555   1555  1.43  
LINK         ND2 ASN B 281                 C1  NAG B2281     1555   1555  1.43  
LINK         ND2 ASN B 321                 C1  NAG B2321     1555   1555  1.43  
CISPEP   1 GLY A  474    PRO A  475          0        10.28                     
CISPEP   2 GLY B  474    PRO B  475          0         5.35                     
SITE     1 AC1 15 GLU A 205  GLU A 206  ASP A 545  VAL A 546                    
SITE     2 AC1 15 TYR A 547  TRP A 627  GLY A 628  TRP A 629                    
SITE     3 AC1 15 SER A 630  TYR A 631  TYR A 662  TYR A 666                    
SITE     4 AC1 15 VAL A 711  HOH A3859  HOH A3862                               
SITE     1 AC2  3 ARG A 596  ARG A 597  HOH A3761                               
SITE     1 AC3  3 GLU A 146  ARG A 147  HOH A3186                               
SITE     1 AC4  5 ARG A 658  ARG A 684  HOH A3752  HOH A3771                    
SITE     2 AC4  5 GLU B 244                                                     
SITE     1 AC5 16 GLU B 205  GLU B 206  ASP B 545  VAL B 546                    
SITE     2 AC5 16 TYR B 547  TRP B 627  GLY B 628  TRP B 629                    
SITE     3 AC5 16 SER B 630  TYR B 631  TYR B 662  TYR B 666                    
SITE     4 AC5 16 VAL B 711  HOH B3712  HOH B3714  HOH B3715                    
SITE     1 AC6  4 THR B 144  GLU B 145  GLU B 146  ARG B 147                    
SITE     1 AC7  2 ARG B 596  ARG B 597                                          
SITE     1 AC8  4 GLU A 244  ARG B 658  ARG B 684  HOH B3643                    
SITE     1 AC9 26 GLU A  67  VAL A  78  ASN A  85  SER A  86                    
SITE     2 AC9 26 SER A  87  LEU A 519  ASN A 520  GLU A 608                    
SITE     3 AC9 26 ARG A 611  NAG A1520  HOH A3056  HOH A3081                    
SITE     4 AC9 26 HOH A3082  HOH A3650  HOH A3651  HOH A3863                    
SITE     5 AC9 26 HOH A3864  HOH A3865  HOH A3866  HOH A3867                    
SITE     6 AC9 26 HOH A3868  HOH A3870  HOH A3871  HOH A3872                    
SITE     7 AC9 26 HOH A3873  LYS B 391                                          
SITE     1 BC1  3 ARG A 147  ASN A 150  HOH A3187                               
SITE     1 BC2  5 ASN A 219  THR A 221  GLN A 308  GLU A 309                    
SITE     2 BC2  5 HOH A3288                                                     
SITE     1 BC3  7 ILE A 194  ASN A 229  THR A 231  GLU A 232                    
SITE     2 BC3  7 HOH A3296  HOH A3299  HOH A3300                               
SITE     1 BC4  5 TRP A 187  VAL A 279  ASN A 281  HOH A3380                    
SITE     2 BC4  5 HOH A3877                                                     
SITE     1 BC5  9 ILE A 319  ASN A 321  MET A 348  SER A 349                    
SITE     2 BC5  9 THR A 350  ARG A 596  HOH A3448  ARG B 140                    
SITE     3 BC5  9 HOH B3150                                                     
SITE     1 BC6  6 ASN A 520  ARG A 581  ASP A 605  MAN A1089                    
SITE     2 BC6  6 HOH A3309  HOH A3878                                          
SITE     1 BC7  5 VAL B  78  ASN B  85  SER B  86  SER B  87                    
SITE     2 BC7  5 HOH B3043                                                     
SITE     1 BC8  7 ARG B 147  ILE B 148  ASN B 150  HOH B3093                    
SITE     2 BC8  7 HOH B3161  HOH B3162  HOH B3716                               
SITE     1 BC9  6 ASN B 219  THR B 221  GLN B 308  GLU B 309                    
SITE     2 BC9  6 HOH B3252  HOH B3717                                          
SITE     1 CC1  7 ILE B 194  ASN B 229  THR B 231  GLU B 232                    
SITE     2 CC1  7 HOH B3259  HOH B3262  HOH B3718                               
SITE     1 CC2  4 TRP B 187  VAL B 279  ASN B 281  HOH B3320                    
SITE     1 CC3  5 ASN B 321  MET B 348  SER B 349  THR B 350                    
SITE     2 CC3  5 HOH B3606                                                     
CRYST1   97.183  121.424  190.699  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      0.010290  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008236  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005244        0.00000                         
TER    6009      ALA A 767                                                      
TER   12060      HIS B 773                                                      
MASTER      498    0   25   35  116    0   45    613990    2  366  114          
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
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer