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LongText Report for: 3Q0T-pdb

Name Class
3Q0T-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           16-DEC-10   3Q0T              
TITLE     CRYSTAL STRUCTURE OF HUMAN DPP-IV IN COMPLEX WITHSA-(+)- METHYL2-(3-  
TITLE    2 (AMINOMETHYL)-4-(2,4-DICHLOROPHENYL)-2-METHYL- 7-OXO-5H-PYRROLO[3,4- 
TITLE    3 B]PYRIDIN-6(7H)-YL)ACETATE                                           
CAVEAT     3Q0T    INCORRECT CHIRALITY AT C1 ATOM OF NAG1501B                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,    
COMPND   5 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,     
COMPND   6 TP103, DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE IV 
COMPND   7 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM, DIPEPTIDYL       
COMPND   8 PEPTIDASE IV SOLUBLE FORM;                                           
COMPND   9 EC: 3.4.14.5;                                                        
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DPP4, ADCP2, CD26;                                             
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPICZALPHA                                
KEYWDS    EXOPEPTIDASE, ALPHA/BETA HYDROLASE FOLD, BETA BARREL, BETA PROPELLER, 
KEYWDS   2 AMINOPEPTIDASE, GLYCOPROTEIN, MEMBRANE, SERINE PROTEASE, SIGNAL-     
KEYWDS   3 ANCHOR, TRANSMEMBRANE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.E.KLEI                                                              
REVDAT   1   29-FEB-12 3Q0T    0                                                
JRNL        AUTH   W.WANG,P.DEVASTHALE,A.WANG,D.EGAN,N.MORGAN,M.CAP,A.FURA,     
JRNL        AUTH 2 H.E.KLEI,K.KISH,L.SUN,P.LEVESQUE,R.ZAHLER,M.KIRBY,L.G.HAMANN 
JRNL        TITL   DISCOVERY OF 7-OXO-PYRROLOPYRIDINES AS POTENT AND SELECTIVE  
JRNL        TITL 2 INHIBITORS OF DPP4                                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_606)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.95                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.440                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 71776                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2935                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.9612 -  6.6194    0.99     3663   168  0.1985 0.2219        
REMARK   3     2  6.6194 -  5.2561    1.00     3527   146  0.1914 0.2409        
REMARK   3     3  5.2561 -  4.5923    1.00     3495   142  0.1445 0.1940        
REMARK   3     4  4.5923 -  4.1727    1.00     3436   144  0.1493 0.1863        
REMARK   3     5  4.1727 -  3.8738    1.00     3419   150  0.1665 0.2321        
REMARK   3     6  3.8738 -  3.6455    1.00     3423   151  0.1925 0.2501        
REMARK   3     7  3.6455 -  3.4630    1.00     3388   160  0.1984 0.2463        
REMARK   3     8  3.4630 -  3.3123    1.00     3433   128  0.2099 0.3026        
REMARK   3     9  3.3123 -  3.1848    1.00     3374   152  0.2105 0.2515        
REMARK   3    10  3.1848 -  3.0749    1.00     3366   131  0.2216 0.2823        
REMARK   3    11  3.0749 -  2.9788    1.00     3386   145  0.2292 0.2899        
REMARK   3    12  2.9788 -  2.8936    1.00     3390   133  0.2222 0.3267        
REMARK   3    13  2.8936 -  2.8175    0.99     3330   150  0.2278 0.3084        
REMARK   3    14  2.8175 -  2.7487    0.99     3336   163  0.2502 0.3424        
REMARK   3    15  2.7487 -  2.6862    0.99     3361   125  0.2540 0.3330        
REMARK   3    16  2.6862 -  2.6291    0.98     3259   133  0.2627 0.3794        
REMARK   3    17  2.6291 -  2.5765    0.95     3259   127  0.2720 0.3619        
REMARK   3    18  2.5765 -  2.5279    0.91     3027   122  0.3004 0.3878        
REMARK   3    19  2.5279 -  2.4827    0.88     2933   142  0.2915 0.3764        
REMARK   3    20  2.4827 -  2.4406    0.79     2657   118  0.2932 0.3815        
REMARK   3    21  2.4406 -  2.4013    0.71     2379   105  0.2856 0.3378        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.32                                          
REMARK   3   B_SOL              : 42.70                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.01230                                              
REMARK   3    B22 (A**2) : 13.25540                                             
REMARK   3    B33 (A**2) : -16.26770                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008          12407                                  
REMARK   3   ANGLE     :  1.114          16901                                  
REMARK   3   CHIRALITY :  0.075           1811                                  
REMARK   3   PLANARITY :  0.004           2126                                  
REMARK   3   DIHEDRAL  : 17.052           4447                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3Q0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB063051.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71882                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 3NOX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS GROWN IN 2 UL EQUIVOLUME        
REMARK 280  MIXTURE OF PROTEIN SOLUTION (0.1 M NACL, 20 MM TRIS-HCL BUFFER PH   
REMARK 280  7.8, 9.8 MG/ML PROTEIN) AND CRYSTALLIZATION SOLUTION (17% W/V PEG   
REMARK 280  3350, 15% W/V GLYCEROL, 200 MM MGCL2, 100 MM TRIS-HCL BUFFER PH     
REMARK 280  8.5). SUFFICIENT. 100 MM LIGAND STOCK SOLUTION (NEAT DMSO) ADDED    
REMARK 280  TO ACHIEVE 1 MM LIGAND CONCENTRATION. SOAKED OVERNIGHT. HARVESTED   
REMARK 280  DIRECTLY AND CRYO-STORED IN LN2. 2. TEMPERATURE 298K, VAPOR         
REMARK 280  DIFFUSION, HANGING DROP                                             
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       32.84300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      210.48900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.78450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      210.48900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.84300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.78450            
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: 8240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 58450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 42.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A    37                                                      
REMARK 465     PHE A    38                                                      
REMARK 465     SER A    39                                                      
REMARK 465     PRO A   767                                                      
REMARK 465     LEU A   768                                                      
REMARK 465     GLU A   769                                                      
REMARK 465     GLN A   770                                                      
REMARK 465     LYS A   771                                                      
REMARK 465     LEU A   772                                                      
REMARK 465     ILE A   773                                                      
REMARK 465     SER A   774                                                      
REMARK 465     GLU A   775                                                      
REMARK 465     GLU A   776                                                      
REMARK 465     ASP A   777                                                      
REMARK 465     LEU A   778                                                      
REMARK 465     ASN A   779                                                      
REMARK 465     SER A   780                                                      
REMARK 465     ALA A   781                                                      
REMARK 465     VAL A   782                                                      
REMARK 465     ASP A   783                                                      
REMARK 465     HIS A   784                                                      
REMARK 465     HIS A   785                                                      
REMARK 465     HIS A   786                                                      
REMARK 465     HIS A   787                                                      
REMARK 465     HIS A   788                                                      
REMARK 465     HIS A   789                                                      
REMARK 465     GLU B    37                                                      
REMARK 465     PHE B    38                                                      
REMARK 465     SER B    39                                                      
REMARK 465     PRO B   767                                                      
REMARK 465     LEU B   768                                                      
REMARK 465     GLU B   769                                                      
REMARK 465     GLN B   770                                                      
REMARK 465     LYS B   771                                                      
REMARK 465     LEU B   772                                                      
REMARK 465     ILE B   773                                                      
REMARK 465     SER B   774                                                      
REMARK 465     GLU B   775                                                      
REMARK 465     GLU B   776                                                      
REMARK 465     ASP B   777                                                      
REMARK 465     LEU B   778                                                      
REMARK 465     ASN B   779                                                      
REMARK 465     SER B   780                                                      
REMARK 465     ALA B   781                                                      
REMARK 465     VAL B   782                                                      
REMARK 465     ASP B   783                                                      
REMARK 465     HIS B   784                                                      
REMARK 465     HIS B   785                                                      
REMARK 465     HIS B   786                                                      
REMARK 465     HIS B   787                                                      
REMARK 465     HIS B   788                                                      
REMARK 465     HIS B   789                                                      
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     ARG A  40    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A  54    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  71    CD   CE   NZ                                        
REMARK 470     GLU A  91    CD   OE1  OE2                                       
REMARK 470     LYS A 139    CE   NZ                                             
REMARK 470     ARG A 140    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 175    CE   NZ                                             
REMARK 470     ASN A 179    O                                                   
REMARK 470     ASP A 243    OD1  OD2                                            
REMARK 470     LYS A 250    CE   NZ                                             
REMARK 470     GLU A 332    CD   OE1  OE2                                       
REMARK 470     GLU A 378    CD   OE1  OE2                                       
REMARK 470     LYS A 391    NZ                                                  
REMARK 470     LYS A 392    CE   NZ                                             
REMARK 470     LYS A 441    CE   NZ                                             
REMARK 470     LYS A 463    CG   CD   CE   NZ                                   
REMARK 470     LYS A 466    CG   CD   CE   NZ                                   
REMARK 470     LYS A 502    CG   CD   CE   NZ                                   
REMARK 470     LYS A 513    CE   NZ                                             
REMARK 470     LYS A 589    CE   NZ                                             
REMARK 470     LYS A 696    CD   CE   NZ                                        
REMARK 470     GLN A 761    CD   OE1  NE2                                       
REMARK 470     ARG B  40    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B  41    CD   CE   NZ                                        
REMARK 470     ARG B  54    NH1  NH2                                            
REMARK 470     LEU B  90    CD1  CD2                                            
REMARK 470     GLU B  97    CD   OE1  OE2                                       
REMARK 470     LYS B 139    CD   CE   NZ                                        
REMARK 470     ARG B 140    CD   NE   CZ   NH1  NH2                             
REMARK 470     ILE B 143    CD1                                                 
REMARK 470     ARG B 147    NH1  NH2                                            
REMARK 470     LYS B 190    CE   NZ                                             
REMARK 470     LYS B 250    CE   NZ                                             
REMARK 470     SER B 278    OG                                                  
REMARK 470     VAL B 279    CG1  CG2                                            
REMARK 470     GLU B 332    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 340    CD1  CD2                                            
REMARK 470     LYS B 391    CE   NZ                                             
REMARK 470     LYS B 392    CD   CE   NZ                                        
REMARK 470     LYS B 441    NZ                                                  
REMARK 470     GLU B 452    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 463    CE   NZ                                             
REMARK 470     ARG B 471    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 489    NZ                                                  
REMARK 470     LYS B 536    CG   CD   CE   NZ                                   
REMARK 470     LYS B 589    CE   NZ                                             
REMARK 470     GLN B 761    CD   OE1  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  51       43.28     73.97                                   
REMARK 500    SER A  64     -169.52   -176.05                                   
REMARK 500    HIS A  66        8.25   -152.08                                   
REMARK 500    ASN A  74       11.13     57.02                                   
REMARK 500    GLN A 123     -100.82   -103.49                                   
REMARK 500    TRP A 124     -153.26    -92.95                                   
REMARK 500    HIS A 162       31.75   -140.70                                   
REMARK 500    ASP A 192       -8.40     60.74                                   
REMARK 500    ALA A 213       38.40   -142.29                                   
REMARK 500    SER A 242     -155.39     64.73                                   
REMARK 500    SER A 275       48.65    -99.91                                   
REMARK 500    VAL A 279      -60.65    -92.23                                   
REMARK 500    GLN A 320       35.22    -83.44                                   
REMARK 500    ASP A 393     -173.68     62.51                                   
REMARK 500    TRP A 402      174.39    179.58                                   
REMARK 500    LYS A 423       18.94     48.09                                   
REMARK 500    ASP A 438       91.02   -165.59                                   
REMARK 500    ASN A 450       85.66   -159.75                                   
REMARK 500    GLU A 464      -11.54     70.64                                   
REMARK 500    ALA A 465       30.75     70.46                                   
REMARK 500    LYS A 536        1.24    -66.51                                   
REMARK 500    TYR A 547      -64.61   -124.45                                   
REMARK 500    ARG A 597       48.10   -145.80                                   
REMARK 500    THR A 600      -94.04   -123.86                                   
REMARK 500    SER A 630     -125.18     51.14                                   
REMARK 500    ASP A 678     -116.47   -114.76                                   
REMARK 500    GLN A 714      -47.47    -29.76                                   
REMARK 500    ILE A 742       60.47     33.98                                   
REMARK 500    HIS B  66       -1.84   -148.81                                   
REMARK 500    GLN B 123     -104.44   -104.52                                   
REMARK 500    TRP B 124     -141.99    -88.58                                   
REMARK 500    ASN B 138      -82.43    -48.78                                   
REMARK 500    HIS B 162       34.19   -153.80                                   
REMARK 500    ASP B 192       -5.09     70.46                                   
REMARK 500    ILE B 193      -65.28   -121.20                                   
REMARK 500    VAL B 207      -62.97   -108.75                                   
REMARK 500    SER B 242     -162.76     67.98                                   
REMARK 500    GLN B 320       49.43    -79.60                                   
REMARK 500    ARG B 358      151.89    177.27                                   
REMARK 500    ASP B 393     -164.28     61.76                                   
REMARK 500    GLU B 464       16.98     59.62                                   
REMARK 500    ASP B 515     -164.09   -128.26                                   
REMARK 500    TYR B 547      -71.66   -115.94                                   
REMARK 500    ARG B 597       45.96   -147.47                                   
REMARK 500    THR B 600      -96.45   -126.60                                   
REMARK 500    SER B 630     -121.83     55.24                                   
REMARK 500    ALA B 654       65.45     23.33                                   
REMARK 500    ASP B 678     -106.72    -96.73                                   
REMARK 500    ASP B 708      105.36    -59.66                                   
REMARK 500    ASN B 710      -66.83   -103.67                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A 2811                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 851                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2191                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2291                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2292                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2811                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LGE A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 851                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 921                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2191                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2291                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2292                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 5201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LGE B 2                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3NOX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3BJM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3SWW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3SX4   RELATED DB: PDB                                   
DBREF  3Q0T A   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  3Q0T B   39   766  UNP    P27487   DPP4_HUMAN      39    766             
SEQADV 3Q0T GLU A   37  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T PHE A   38  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T PRO A  767  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T LEU A  768  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T GLU A  769  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T GLN A  770  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T LYS A  771  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T LEU A  772  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T ILE A  773  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T SER A  774  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T GLU A  775  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T GLU A  776  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T ASP A  777  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T LEU A  778  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T ASN A  779  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T SER A  780  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T ALA A  781  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T VAL A  782  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T ASP A  783  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T HIS A  784  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T HIS A  785  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T HIS A  786  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T HIS A  787  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T HIS A  788  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T HIS A  789  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T GLU B   37  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T PHE B   38  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T PRO B  767  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T LEU B  768  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T GLU B  769  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T GLN B  770  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T LYS B  771  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T LEU B  772  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T ILE B  773  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T SER B  774  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T GLU B  775  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T GLU B  776  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T ASP B  777  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T LEU B  778  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T ASN B  779  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T SER B  780  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T ALA B  781  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T VAL B  782  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T ASP B  783  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T HIS B  784  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T HIS B  785  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T HIS B  786  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T HIS B  787  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T HIS B  788  UNP  P27487              EXPRESSION TAG                 
SEQADV 3Q0T HIS B  789  UNP  P27487              EXPRESSION TAG                 
SEQRES   1 A  753  GLU PHE SER ARG LYS THR TYR THR LEU THR ASP TYR LEU          
SEQRES   2 A  753  LYS ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP          
SEQRES   3 A  753  ILE SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN          
SEQRES   4 A  753  ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL          
SEQRES   5 A  753  PHE LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER          
SEQRES   6 A  753  ILE ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE          
SEQRES   7 A  753  LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER          
SEQRES   8 A  753  TYR THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG          
SEQRES   9 A  753  GLN LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN          
SEQRES  10 A  753  TRP VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR          
SEQRES  11 A  753  VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN          
SEQRES  12 A  753  LEU PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP          
SEQRES  13 A  753  ILE ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU          
SEQRES  14 A  753  GLU VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO          
SEQRES  15 A  753  ASN GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR          
SEQRES  16 A  753  GLU VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU          
SEQRES  17 A  753  SER LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO          
SEQRES  18 A  753  LYS ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL          
SEQRES  19 A  753  VAL ASN THR ASP SER LEU SER SER VAL THR ASN ALA THR          
SEQRES  20 A  753  SER ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY          
SEQRES  21 A  753  ASP HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU          
SEQRES  22 A  753  ARG ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR          
SEQRES  23 A  753  SER VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY          
SEQRES  24 A  753  ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET          
SEQRES  25 A  753  SER THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU          
SEQRES  26 A  753  PRO HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE          
SEQRES  27 A  753  ILE SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE          
SEQRES  28 A  753  GLN ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY          
SEQRES  29 A  753  THR TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP          
SEQRES  30 A  753  TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO          
SEQRES  31 A  753  GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR          
SEQRES  32 A  753  THR LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU          
SEQRES  33 A  753  ARG CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA          
SEQRES  34 A  753  LYS TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO          
SEQRES  35 A  753  LEU TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU          
SEQRES  36 A  753  ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU          
SEQRES  37 A  753  GLN ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE          
SEQRES  38 A  753  ILE LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU          
SEQRES  39 A  753  PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU          
SEQRES  40 A  753  LEU ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP          
SEQRES  41 A  753  THR VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER          
SEQRES  42 A  753  THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY          
SEQRES  43 A  753  SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN          
SEQRES  44 A  753  ARG ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU          
SEQRES  45 A  753  ALA ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN          
SEQRES  46 A  753  LYS ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR          
SEQRES  47 A  753  VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE          
SEQRES  48 A  753  LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU          
SEQRES  49 A  753  TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU          
SEQRES  50 A  753  PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER          
SEQRES  51 A  753  THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU          
SEQRES  52 A  753  TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS          
SEQRES  53 A  753  PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP          
SEQRES  54 A  753  VAL GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU          
SEQRES  55 A  753  ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE          
SEQRES  56 A  753  TYR THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER          
SEQRES  57 A  753  LEU PRO PRO LEU GLU GLN LYS LEU ILE SER GLU GLU ASP          
SEQRES  58 A  753  LEU ASN SER ALA VAL ASP HIS HIS HIS HIS HIS HIS              
SEQRES   1 B  753  GLU PHE SER ARG LYS THR TYR THR LEU THR ASP TYR LEU          
SEQRES   2 B  753  LYS ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP          
SEQRES   3 B  753  ILE SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN          
SEQRES   4 B  753  ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL          
SEQRES   5 B  753  PHE LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER          
SEQRES   6 B  753  ILE ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE          
SEQRES   7 B  753  LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER          
SEQRES   8 B  753  TYR THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG          
SEQRES   9 B  753  GLN LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN          
SEQRES  10 B  753  TRP VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR          
SEQRES  11 B  753  VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN          
SEQRES  12 B  753  LEU PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP          
SEQRES  13 B  753  ILE ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU          
SEQRES  14 B  753  GLU VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO          
SEQRES  15 B  753  ASN GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR          
SEQRES  16 B  753  GLU VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU          
SEQRES  17 B  753  SER LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO          
SEQRES  18 B  753  LYS ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL          
SEQRES  19 B  753  VAL ASN THR ASP SER LEU SER SER VAL THR ASN ALA THR          
SEQRES  20 B  753  SER ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY          
SEQRES  21 B  753  ASP HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU          
SEQRES  22 B  753  ARG ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR          
SEQRES  23 B  753  SER VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY          
SEQRES  24 B  753  ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET          
SEQRES  25 B  753  SER THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU          
SEQRES  26 B  753  PRO HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE          
SEQRES  27 B  753  ILE SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE          
SEQRES  28 B  753  GLN ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY          
SEQRES  29 B  753  THR TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP          
SEQRES  30 B  753  TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO          
SEQRES  31 B  753  GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR          
SEQRES  32 B  753  THR LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU          
SEQRES  33 B  753  ARG CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA          
SEQRES  34 B  753  LYS TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO          
SEQRES  35 B  753  LEU TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU          
SEQRES  36 B  753  ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU          
SEQRES  37 B  753  GLN ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE          
SEQRES  38 B  753  ILE LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU          
SEQRES  39 B  753  PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU          
SEQRES  40 B  753  LEU ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP          
SEQRES  41 B  753  THR VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER          
SEQRES  42 B  753  THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY          
SEQRES  43 B  753  SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN          
SEQRES  44 B  753  ARG ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU          
SEQRES  45 B  753  ALA ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN          
SEQRES  46 B  753  LYS ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR          
SEQRES  47 B  753  VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE          
SEQRES  48 B  753  LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU          
SEQRES  49 B  753  TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU          
SEQRES  50 B  753  PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER          
SEQRES  51 B  753  THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU          
SEQRES  52 B  753  TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS          
SEQRES  53 B  753  PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP          
SEQRES  54 B  753  VAL GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU          
SEQRES  55 B  753  ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE          
SEQRES  56 B  753  TYR THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER          
SEQRES  57 B  753  LEU PRO PRO LEU GLU GLN LYS LEU ILE SER GLU GLU ASP          
SEQRES  58 B  753  LEU ASN SER ALA VAL ASP HIS HIS HIS HIS HIS HIS              
MODRES 3Q0T ASN B  520  ASN  GLYCOSYLATION SITE                                 
MODRES 3Q0T ASN B   85  ASN  GLYCOSYLATION SITE                                 
MODRES 3Q0T ASN A  150  ASN  GLYCOSYLATION SITE                                 
MODRES 3Q0T ASN A   85  ASN  GLYCOSYLATION SITE                                 
MODRES 3Q0T ASN A  520  ASN  GLYCOSYLATION SITE                                 
MODRES 3Q0T ASN B  219  ASN  GLYCOSYLATION SITE                                 
MODRES 3Q0T ASN B  150  ASN  GLYCOSYLATION SITE                                 
MODRES 3Q0T ASN B   92  ASN  GLYCOSYLATION SITE                                 
MODRES 3Q0T ASN A  229  ASN  GLYCOSYLATION SITE                                 
MODRES 3Q0T ASN B  229  ASN  GLYCOSYLATION SITE                                 
MODRES 3Q0T ASN A  219  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 851      14                                                       
HET    NAG  A1501      14                                                       
HET    NAG  A2191      14                                                       
HET    NAG  A2291      14                                                       
HET    NAG  A2292      14                                                       
HET    NAG  A2811      14                                                       
HET    NAG  A5201      14                                                       
HET    LGE  A   1      26                                                       
HET    NAG  B 851      14                                                       
HET    NAG  B 921      14                                                       
HET    NAG  B1501      14                                                       
HET    NAG  B2191      14                                                       
HET    NAG  B2291      14                                                       
HET    NAG  B2292      14                                                       
HET    NAG  B5201      14                                                       
HET    LGE  B   2      26                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     LGE METHYL [3-(AMINOMETHYL)-4-(2,4-DIMETHYLPHENYL)-2-                
HETNAM   2 LGE  METHYL-7-OXO-5,7-DIHYDRO-6H-PYRROLO[3,4-B]PYRIDIN-6-            
HETNAM   3 LGE  YL]ACETATE                                                      
FORMUL   3  NAG    14(C8 H15 N O6)                                              
FORMUL   9  LGE    2(C20 H23 N3 O3)                                             
FORMUL  17  HOH   *431(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 LEU A  340  GLN A  344  5                                   5    
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 THR A  687  VAL A  698  5                                  12    
HELIX   17  17 HIS A  712  VAL A  726  1                                  15    
HELIX   18  18 SER A  744  SER A  764  1                                  21    
HELIX   19  19 THR B   44  ASN B   51  1                                   8    
HELIX   20  20 GLU B   91  ASP B   96  5                                   6    
HELIX   21  21 ASP B  200  VAL B  207  1                                   8    
HELIX   22  22 PRO B  290  ILE B  295  1                                   6    
HELIX   23  23 VAL B  341  GLN B  344  5                                   4    
HELIX   24  24 GLU B  421  MET B  425  5                                   5    
HELIX   25  25 LYS B  463  ALA B  465  5                                   3    
HELIX   26  26 ASN B  497  ASN B  506  1                                  10    
HELIX   27  27 ASN B  562  ASN B  572  1                                  11    
HELIX   28  28 GLY B  587  HIS B  592  1                                   6    
HELIX   29  29 ALA B  593  ASN B  595  5                                   3    
HELIX   30  30 THR B  600  MET B  616  1                                  17    
HELIX   31  31 SER B  630  GLY B  641  1                                  12    
HELIX   32  32 ARG B  658  TYR B  662  5                                   5    
HELIX   33  33 ASP B  663  GLY B  672  1                                  10    
HELIX   34  34 ASN B  679  SER B  686  1                                   8    
HELIX   35  35 THR B  687  VAL B  698  5                                  12    
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  LEU A  90   N  ILE A  76           
SHEET    1   B 4 ILE A 102  ILE A 107  0                                        
SHEET    2   B 4 PHE A 113  LYS A 122 -1  O  GLU A 117   N  ASP A 104           
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 3 ILE A 194  ASN A 196  0                                        
SHEET    2   D 3 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   D 3 LEU A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224           
SHEET    1   E 4 ILE A 194  ASN A 196  0                                        
SHEET    2   E 4 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   E 4 THR A 265  ASN A 272 -1  O  PHE A 269   N  TYR A 225           
SHEET    4   E 4 ILE A 285  ILE A 287 -1  O  ILE A 285   N  VAL A 270           
SHEET    1   F 2 LEU A 235  PHE A 240  0                                        
SHEET    2   F 2 LYS A 250  PRO A 255 -1  O  LYS A 250   N  PHE A 240           
SHEET    1   G 4 HIS A 298  TRP A 305  0                                        
SHEET    2   G 4 ARG A 310  ARG A 317 -1  O  LEU A 316   N  TYR A 299           
SHEET    3   G 4 TYR A 322  TYR A 330 -1  O  ASP A 326   N  LEU A 313           
SHEET    4   G 4 TRP A 337  ASN A 338 -1  O  ASN A 338   N  ASP A 329           
SHEET    1   H 4 HIS A 298  TRP A 305  0                                        
SHEET    2   H 4 ARG A 310  ARG A 317 -1  O  LEU A 316   N  TYR A 299           
SHEET    3   H 4 TYR A 322  TYR A 330 -1  O  ASP A 326   N  LEU A 313           
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  PHE A 387   N  PHE A 371           
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  ARG A 471   N  SER A 458           
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  GLU A 495   N  TYR A 480           
SHEET    1   L 8 SER A 511  ILE A 518  0                                        
SHEET    2   L 8 LYS A 523  LEU A 530 -1  O  LEU A 530   N  SER A 511           
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  ASP A 545   O  ALA A 576           
SHEET    5   L 8 VAL A 619  TRP A 629  1  O  TRP A 627   N  VAL A 546           
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  GLN A 731   N  TYR A 700           
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 LEU B  60  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  SER B  87   N  VAL B  78           
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  SER B 131   N  TYR B 118           
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  VAL B 167   N  TRP B 154           
SHEET    3   P 4 ASP B 171  LYS B 175 -1  O  TYR B 173   N  TYR B 166           
SHEET    4   P 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1   Q 3 ILE B 194  ASN B 196  0                                        
SHEET    2   Q 3 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   Q 3 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224           
SHEET    1   R 4 ILE B 194  ASN B 196  0                                        
SHEET    2   R 4 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   R 4 THR B 265  ASN B 272 -1  O  PHE B 269   N  TYR B 225           
SHEET    4   R 4 ILE B 285  GLN B 286 -1  O  ILE B 285   N  VAL B 270           
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  TRP B 305  0                                        
SHEET    2   T 4 ARG B 310  ARG B 317 -1  O  LEU B 316   N  TYR B 299           
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  TRP B 305  0                                        
SHEET    2   U 4 ARG B 310  ARG B 317 -1  O  LEU B 316   N  TYR B 299           
SHEET    3   U 4 TYR B 322  TYR B 330 -1  O  ASP B 326   N  LEU B 313           
SHEET    4   U 4 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  HIS B 383   N  ILE B 375           
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  GLU B 495 -1  O  LEU B 494   N  TYR B 480           
SHEET    1   Y 8 SER B 511  LEU B 519  0                                        
SHEET    2   Y 8 THR B 522  LEU B 530 -1  O  LEU B 530   N  SER B 511           
SHEET    3   Y 8 ILE B 574  PHE B 578 -1  O  VAL B 575   N  ILE B 529           
SHEET    4   Y 8 TYR B 540  ASP B 545  1  N  ASP B 545   O  ALA B 576           
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  ILE B 703   N  ALA B 652           
SHEET    8   Y 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  TYR B 700           
SSBOND   1 CYS A  328    CYS A  339                          1555   1555  2.05  
SSBOND   2 CYS A  385    CYS A  394                          1555   1555  2.05  
SSBOND   3 CYS A  444    CYS A  447                          1555   1555  2.04  
SSBOND   4 CYS A  454    CYS A  472                          1555   1555  2.08  
SSBOND   5 CYS A  649    CYS A  762                          1555   1555  2.05  
SSBOND   6 CYS B  328    CYS B  339                          1555   1555  2.05  
SSBOND   7 CYS B  385    CYS B  394                          1555   1555  2.04  
SSBOND   8 CYS B  444    CYS B  447                          1555   1555  2.04  
SSBOND   9 CYS B  454    CYS B  472                          1555   1555  2.07  
SSBOND  10 CYS B  649    CYS B  762                          1555   1555  2.05  
LINK         ND2 ASN B 520                 C1  NAG B5201     1555   1555  1.43  
LINK         ND2 ASN B  85                 C1  NAG B 851     1555   1555  1.43  
LINK         ND2 ASN A 150                 C1  NAG A1501     1555   1555  1.43  
LINK         ND2 ASN A  85                 C1  NAG A 851     1555   1555  1.43  
LINK         ND2 ASN A 520                 C1  NAG A5201     1555   1555  1.43  
LINK         ND2 ASN B 219                 C1  NAG B2191     1555   1555  1.44  
LINK         ND2 ASN B 150                 C1  NAG B1501     1555   1555  1.44  
LINK         ND2 ASN B  92                 C1  NAG B 921     1555   1555  1.44  
LINK         ND2 ASN A 229                 C1  NAG A2291     1555   1555  1.44  
LINK         ND2 ASN B 229                 C1  NAG B2291     1555   1555  1.44  
LINK         ND2 ASN A 219                 C1  NAG A2191     1555   1555  1.44  
LINK         O4  NAG A2291                 C1  NAG A2292     1555   1555  1.45  
LINK         O4  NAG B2291                 C1  NAG B2292     1555   1555  1.45  
CISPEP   1 GLY A  474    PRO A  475          0        10.90                     
CISPEP   2 GLY B  474    PRO B  475          0         7.88                     
SITE     1 AC1  9 VAL A  78  ASN A  85  SER A  86  SER A  87                    
SITE     2 AC1  9 TYR A 386  GLN A 388  THR A 395  HOH A 884                    
SITE     3 AC1  9 HOH A 886                                                     
SITE     1 AC2  3 ARG A 147  ILE A 148  ASN A 150                               
SITE     1 AC3  4 ASN A 219  THR A 221  GLN A 308  GLU A 309                    
SITE     1 AC4  4 ASN A 229  THR A 231  HOH A 969  NAG A2292                    
SITE     1 AC5  2 HOH A 952  NAG A2291                                          
SITE     1 AC6  3 TRP A 187  VAL A 279  ASN A 281                               
SITE     1 AC7  6 LEU A 519  ASN A 520  ARG A 581  GLU A 604                    
SITE     2 AC7  6 ASP A 605  HOH A 945                                          
SITE     1 AC8  9 ARG A 125  GLU A 205  GLU A 206  TYR A 547                    
SITE     2 AC8  9 SER A 630  VAL A 656  TYR A 662  TYR A 666                    
SITE     3 AC8  9 ASN A 710                                                     
SITE     1 AC9  9 VAL B  78  ASN B  85  SER B  86  SER B  87                    
SITE     2 AC9  9 TYR B 386  GLN B 388  THR B 395  HOH B 812                    
SITE     3 AC9  9 HOH B 898                                                     
SITE     1 BC1  3 GLU B  73  ASN B  75  ASN B  92                               
SITE     1 BC2  3 ASN B 150  ASP B 515  PHE B 516                               
SITE     1 BC3  3 ASN B 219  THR B 221  GLU B 309                               
SITE     1 BC4  6 ILE B 194  ASN B 229  THR B 231  GLU B 232                    
SITE     2 BC4  6 HOH B 918  NAG B2292                                          
SITE     1 BC5  1 NAG B2291                                                     
SITE     1 BC6  6 LEU B 519  ASN B 520  ARG B 581  GLU B 604                    
SITE     2 BC6  6 ASP B 605  HOH B 987                                          
SITE     1 BC7 11 ARG B 125  GLU B 205  GLU B 206  TYR B 547                    
SITE     2 BC7 11 SER B 630  VAL B 656  TYR B 662  TYR B 666                    
SITE     3 BC7 11 ASN B 710  HIS B 740  HOH B 995                               
CRYST1   65.686   67.569  420.978  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      0.015224  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014800  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002375        0.00000                         
TER    5897      PRO A 766                                                      
TER   11790      PRO B 766                                                      
MASTER      478    0   16   37  100    0   27    612467    2  279  116          
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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