Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 3SX4-pdb

Name Class
3SX4-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           14-JUL-11   3SX4              
TITLE     CRYSTAL STRUCTURE OF HUMAN DPP-IV IN COMPLEX WITH SA-(+)-3-           
TITLE    2 (AMINOMETHYL)-4-(2,4-DICHLOROPHENYL)-6-(2-METHOXYPHENYL)- 2-METHYL-  
TITLE    3 5H-PYRROLO[3,4-B]PYRIDIN-7(6H)-ONE                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 39-766;                                       
COMPND   5 SYNONYM: ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,    
COMPND   6 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,     
COMPND   7 TP103, DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE IV 
COMPND   8 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM, DIPEPTIDYL       
COMPND   9 PEPTIDASE IV SOLUBLE FORM;                                           
COMPND  10 EC: 3.4.14.5;                                                        
COMPND  11 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 DPP4, DIMER, PROTEIN:INHIBITOR COMPLEX, AMINOPEPTIDASE,              
KEYWDS   3 GLYCOPROTEIN, MEMBRANE, PROTEASE, SECRETED, SERINE PROTEASE, SIGNAL- 
KEYWDS   4 ANCHOR, TRANSMEMBRANE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.E.KLEI                                                              
REVDAT   1   26-OCT-11 3SX4    0                                                
JRNL        AUTH   W.WANG,P.DEVASTHALE,A.WANG,T.HARRITY,D.EGAN,N.MORGAN,M.CAP,  
JRNL        AUTH 2 A.FURA,H.E.KLEI,K.KISH,C.WEIGELT,L.SUN,P.LEVESQUE,Y.X.LI,    
JRNL        AUTH 3 R.ZAHLER,M.S.KIRBY,L.G.HAMANN                                
JRNL        TITL   7-OXOPYRROLOPYRIDINE-DERIVED DPP4 INHIBITORS-MITIGATION OF   
JRNL        TITL 2 CYP AND HERG LIABILITIES VIA INTRODUCTION OF POLAR           
JRNL        TITL 3 FUNCTIONALITIES IN THE ACTIVE SITE.                          
JRNL        REF    BIOORG.MED.CHEM.LETT.                      2011              
JRNL        REFN                   ESSN 1464-3405                               
JRNL        PMID   21996520                                                     
JRNL        DOI    10.1016/J.BMCL.2011.09.074                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_780)                      
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.10                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.440                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 57656                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2329                            
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 48.1045 -  6.6716    0.99     3640   151  0.1957 0.2865        
REMARK   3     2  6.6716 -  5.2976    1.00     3476   161  0.1810 0.2483        
REMARK   3     3  5.2976 -  4.6286    1.00     3431   157  0.1444 0.2021        
REMARK   3     4  4.6286 -  4.2056    1.00     3420   133  0.1368 0.1958        
REMARK   3     5  4.2056 -  3.9043    1.00     3409   119  0.1639 0.2123        
REMARK   3     6  3.9043 -  3.6742    1.00     3361   141  0.1845 0.2732        
REMARK   3     7  3.6742 -  3.4903    1.00     3370   145  0.2155 0.2931        
REMARK   3     8  3.4903 -  3.3384    1.00     3381   148  0.2325 0.3169        
REMARK   3     9  3.3384 -  3.2099    1.00     3327   152  0.2376 0.3018        
REMARK   3    10  3.2099 -  3.0992    1.00     3349   128  0.2416 0.3086        
REMARK   3    11  3.0992 -  3.0023    1.00     3334   142  0.2544 0.3594        
REMARK   3    12  3.0023 -  2.9165    1.00     3362   153  0.2614 0.2909        
REMARK   3    13  2.9165 -  2.8397    1.00     3297   140  0.2831 0.3744        
REMARK   3    14  2.8397 -  2.7704    0.96     3198   146  0.3049 0.3698        
REMARK   3    15  2.7704 -  2.7074    0.91     2998   127  0.3252 0.4333        
REMARK   3    16  2.7074 -  2.6498    0.81     2745   104  0.3216 0.4199        
REMARK   3    17  2.6498 -  2.5968    0.67     2229    82  0.3233 0.3892        
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              : 0.31                                          
REMARK   3   B_SOL              : 30.12                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.820            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.660           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.47                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.51630                                              
REMARK   3    B22 (A**2) : 7.51390                                              
REMARK   3    B33 (A**2) : -14.03020                                            
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          12464                                  
REMARK   3   ANGLE     :  1.189          16993                                  
REMARK   3   CHIRALITY :  0.076           1813                                  
REMARK   3   PLANARITY :  0.004           2129                                  
REMARK   3   DIHEDRAL  : 17.297           4419                                  
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 3SX4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066761.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
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) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC Q315                          
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000 (DENZO)                    
REMARK 200  DATA SCALING SOFTWARE          : HKL2000 (SCALEPACK)                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57759                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 19.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 3NOX.PDB                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
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. FOR CRYSTAL 2:  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       32.95250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      211.04750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.92700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      211.04750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.95250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.92700            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 57040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 139    CD   CE   NZ                                        
REMARK 470     ARG A 140    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 145    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 175    CE   NZ                                             
REMARK 470     ASN A 179    O                                                   
REMARK 470     ASP A 243    OD1  OD2                                            
REMARK 470     GLU A 244    CA                                                  
REMARK 470     LYS A 250    CD   CE   NZ                                        
REMARK 470     ILE A 319    CD1                                                 
REMARK 470     GLU A 332    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 378    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 391    CE   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     VAL A 486    CG1  CG2                                            
REMARK 470     ASN A 487    OD1  ND2                                            
REMARK 470     LYS A 489    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    CZ   NH1  NH2                                       
REMARK 470     LEU B  90    CG   CD1  CD2                                       
REMARK 470     GLU B  97    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 138    CG   OD1  ND2                                       
REMARK 470     LYS B 139    CD   CE   NZ                                        
REMARK 470     ARG B 140    CG   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    CD   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    CG   CD1  CD2                                       
REMARK 470     LYS B 391    CD   CE   NZ                                        
REMARK 470     LYS B 392    CG   CD   CE   NZ                                   
REMARK 470     ASP B 393    CG   OD1  OD2                                       
REMARK 470     LYS B 441    CE   NZ                                             
REMARK 470     GLU B 452    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 463    CE   NZ                                             
REMARK 470     LYS B 489    NZ                                                  
REMARK 470     LYS B 536    CG   CD   CE   NZ                                   
REMARK 470     LYS B 589    CD   CE   NZ                                        
REMARK 470     LYS B 622    CD   CE   NZ                                        
REMARK 470     GLN B 761    CD   OE1  NE2                                       
REMARK 470     LEU B 765    CD1  CD2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A   520     C2   NAG A  5201              2.05            
REMARK 500   ND2  ASN A   150     C2   NAG A  1501              2.10            
REMARK 500   NH2  ARG B   596     OD1  ASP B   678              2.14            
REMARK 500   ND2  ASN B    85     C2   NAG B   851              2.18            
REMARK 500   NH2  ARG A   596     OD1  ASP A   678              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 362   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO A 451   C   -  N   -  CA  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    PRO B 178   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  64     -149.81   -165.97                                   
REMARK 500    HIS A  66        2.79   -159.83                                   
REMARK 500    ASN A  92       13.61    -64.98                                   
REMARK 500    GLN A 123     -101.59   -108.45                                   
REMARK 500    TRP A 124     -147.84    -90.49                                   
REMARK 500    TYR A 128     -178.18   -174.73                                   
REMARK 500    HIS A 162       31.79   -147.24                                   
REMARK 500    PRO A 178      -52.06    -29.85                                   
REMARK 500    ASP A 192       14.52     56.77                                   
REMARK 500    ILE A 193      -57.53   -135.68                                   
REMARK 500    SER A 242     -151.71     64.18                                   
REMARK 500    SER A 275       60.34   -102.76                                   
REMARK 500    ASN A 281     -160.74    -69.44                                   
REMARK 500    THR A 307     -156.84   -137.31                                   
REMARK 500    GLN A 320       38.08    -75.66                                   
REMARK 500    ASP A 390        3.84     96.08                                   
REMARK 500    ASP A 393      179.20     62.61                                   
REMARK 500    TRP A 402     -176.21   -177.33                                   
REMARK 500    LYS A 423       15.04     58.45                                   
REMARK 500    ASP A 438       85.52   -160.91                                   
REMARK 500    ASN A 450       68.87   -164.79                                   
REMARK 500    GLU A 464      -23.50     82.46                                   
REMARK 500    ALA A 465       38.18     76.42                                   
REMARK 500    ASN A 487       48.98   -140.86                                   
REMARK 500    TYR A 547      -75.26   -128.21                                   
REMARK 500    ARG A 596        7.62     58.44                                   
REMARK 500    THR A 600      -89.00   -115.42                                   
REMARK 500    SER A 630     -130.20     55.67                                   
REMARK 500    ASP A 678     -108.52   -118.74                                   
REMARK 500    LYS A 696        7.18    -67.99                                   
REMARK 500    ASP A 708       98.61    -59.47                                   
REMARK 500    ASN A 710      -69.55   -101.25                                   
REMARK 500    GLN A 714      -51.88    -21.98                                   
REMARK 500    ILE A 742       58.43     38.90                                   
REMARK 500    SER B  64     -168.14   -167.08                                   
REMARK 500    HIS B  66       -2.27   -150.24                                   
REMARK 500    GLN B 123     -105.42    -97.24                                   
REMARK 500    TRP B 124     -140.76    -88.56                                   
REMARK 500    LEU B 137      -72.14    -67.35                                   
REMARK 500    ASN B 138       55.88    -64.28                                   
REMARK 500    LYS B 139      -16.32   -175.50                                   
REMARK 500    HIS B 162       36.97   -151.74                                   
REMARK 500    PRO B 178      -27.47    -39.93                                   
REMARK 500    ILE B 193      -64.47   -121.34                                   
REMARK 500    SER B 242     -170.35     65.87                                   
REMARK 500    GLU B 244      -33.59    -37.00                                   
REMARK 500    THR B 307     -156.88   -119.29                                   
REMARK 500    GLU B 309       12.06   -141.57                                   
REMARK 500    CYS B 339       78.79   -105.09                                   
REMARK 500    PHE B 371      165.74    179.64                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      71 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 KXA 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 2811                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 5201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KXA B 2                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3BJM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DPP-IV IN COMPLEX WITH (1S,3S,            
REMARK 900 5S)-2-[(2S)-2-AMINO-2-(3-HYDROXYTRICYCLO[3.3.1.13,7]DEC-1-           
REMARK 900 YL)ACETYL]-2-AZABICYCLO[3.1.0]HEXANE-3-CARBONITRILE (CAS),           
REMARK 900 (1S,3S,5S)-2-((2S)-2-AMINO-2-(3-HYDROXYADAMANTAN-1- YL)              
REMARK 900 ACETYL)-2-AZABICYCLO[3.1.0]HEXANE-3-CARBONITRILE (IUPAC),            
REMARK 900 OR BMS-477118                                                        
REMARK 900 RELATED ID: 3NOX   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DPP-IV IN COMPLEX WITH SA-(+)-            
REMARK 900 (6-(AMINOMETHYL)-5-(2,4-DICHLOROPHENYL)-7-METHYLIMIDAZO[1,           
REMARK 900 2-A]PYRIMIDIN-2-YL)(MORPHOLINO)METHANONE                             
REMARK 900 RELATED ID: 3SWW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3Q0T   RELATED DB: PDB                                   
DBREF  3SX4 A   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  3SX4 B   39   766  UNP    P27487   DPP4_HUMAN      39    766             
SEQADV 3SX4 GLU A   37  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 PHE A   38  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 PRO A  767  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 LEU A  768  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 GLU A  769  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 GLN A  770  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 LYS A  771  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 LEU A  772  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 ILE A  773  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 SER A  774  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 GLU A  775  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 GLU A  776  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 ASP A  777  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 LEU A  778  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 ASN A  779  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 SER A  780  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 ALA A  781  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 VAL A  782  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 ASP A  783  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 HIS A  784  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 HIS A  785  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 HIS A  786  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 HIS A  787  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 HIS A  788  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 HIS A  789  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 GLU B   37  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 PHE B   38  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 PRO B  767  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 LEU B  768  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 GLU B  769  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 GLN B  770  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 LYS B  771  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 LEU B  772  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 ILE B  773  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 SER B  774  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 GLU B  775  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 GLU B  776  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 ASP B  777  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 LEU B  778  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 ASN B  779  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 SER B  780  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 ALA B  781  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 VAL B  782  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 ASP B  783  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 HIS B  784  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 HIS B  785  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 HIS B  786  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 HIS B  787  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 HIS B  788  UNP  P27487              EXPRESSION TAG                 
SEQADV 3SX4 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 3SX4 ASN B  520  ASN  GLYCOSYLATION SITE                                 
MODRES 3SX4 ASN B  229  ASN  GLYCOSYLATION SITE                                 
MODRES 3SX4 ASN A   85  ASN  GLYCOSYLATION SITE                                 
MODRES 3SX4 ASN A  150  ASN  GLYCOSYLATION SITE                                 
MODRES 3SX4 ASN B  281  ASN  GLYCOSYLATION SITE                                 
MODRES 3SX4 ASN B   92  ASN  GLYCOSYLATION SITE                                 
MODRES 3SX4 ASN A  520  ASN  GLYCOSYLATION SITE                                 
MODRES 3SX4 ASN B  150  ASN  GLYCOSYLATION SITE                                 
MODRES 3SX4 ASN A  219  ASN  GLYCOSYLATION SITE                                 
MODRES 3SX4 ASN B   85  ASN  GLYCOSYLATION SITE                                 
MODRES 3SX4 ASN B  219  ASN  GLYCOSYLATION SITE                                 
MODRES 3SX4 ASN A  229  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    KXA  A   1      58                                                       
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  B2811      14                                                       
HET    NAG  B5201      14                                                       
HET    KXA  B   2      58                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     KXA 3-(AMINOMETHYL)-4-(2,4-DICHLOROPHENYL)-6-(2-                     
HETNAM   2 KXA  METHOXYPHENYL)-2-METHYL-5,6-DIHYDRO-7H-PYRROLO[3,4-             
HETNAM   3 KXA  B]PYRIDIN-7-ONE                                                 
FORMUL   3  NAG    15(C8 H15 N O6)                                              
FORMUL   9  KXA    2(C22 H19 CL2 N3 O2)                                         
FORMUL  18  HOH   *23(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 ASP A  274  LEU A  276  5                                   3    
HELIX    4   4 PRO A  290  ILE A  295  1                                   6    
HELIX    5   5 VAL A  341  GLN A  344  5                                   4    
HELIX    6   6 GLU A  421  MET A  425  5                                   5    
HELIX    7   7 LYS A  463  ALA A  465  5                                   3    
HELIX    8   8 ASN A  497  GLN A  505  1                                   9    
HELIX    9   9 ASN A  562  THR A  570  1                                   9    
HELIX   10  10 GLY A  587  HIS A  592  1                                   6    
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 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 HIS A  712  GLY A  727  1                                  16    
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  ASP B   96  5                                   6    
HELIX   20  20 ASN B  138  ARG B  140  5                                   3    
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 LEU B  340  GLN B  344  5                                   5    
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  LEU B  504  1                                   8    
HELIX   27  27 GLN B  505  VAL B  507  5                                   3    
HELIX   28  28 ASN B  562  THR B  570  1                                   9    
HELIX   29  29 GLY B  587  ALA B  593  1                                   7    
HELIX   30  30 THR B  600  LYS B  615  1                                  16    
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 VAL B  688  VAL B  698  5                                  11    
HELIX   36  36 HIS B  712  ASP B  725  1                                  14    
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  ASN A 103           
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  ILE A 143 -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  ALA A 165   N  THR A 156           
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 SER A 284  GLN A 286 -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  SER A 312   N  THR A 304           
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  CYS A 339 -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  SER A 312   N  THR A 304           
SHEET    3   H 4 TYR A 322  TYR A 330 -1  O  ASP A 326   N  LEU A 313           
SHEET    4   H 4 HIS A 345  MET A 348 -1  O  HIS A 345   N  MET A 325           
SHEET    1   I 4 PRO A 362  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  ILE A 418   N  ILE A 405           
SHEET    3   J 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417           
SHEET    4   J 4 VAL A 442  CYS A 444 -1  O  THR A 443   N  LYS A 433           
SHEET    1   K 4 TYR A 457  PHE A 461  0                                        
SHEET    2   K 4 TYR A 467  CYS A 472 -1  O  GLN A 469   N  SER A 460           
SHEET    3   K 4 LEU A 479  SER A 484 -1  O  THR A 481   N  LEU A 470           
SHEET    4   K 4 GLY A 490  GLU A 495 -1  O  GLU A 495   N  TYR A 480           
SHEET    1   L 8 SER A 511  LEU A 519  0                                        
SHEET    2   L 8 THR A 522  LEU A 530 -1  O  TYR A 526   N  ASP A 515           
SHEET    3   L 8 ILE A 574  PHE A 578 -1  O  VAL A 575   N  ILE A 529           
SHEET    4   L 8 TYR A 540  VAL A 546  1  N  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  ILE A 703   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 4 ARG B  61  TRP B  62  0                                        
SHEET    2   M 4 GLU B  67  GLN B  72 -1  O  LEU B  69   N  ARG B  61           
SHEET    3   M 4 ASN B  75  ASN B  80 -1  O  LEU B  77   N  TYR B  70           
SHEET    4   M 4 SER B  86  LEU B  90 -1  O  LEU B  90   N  ILE B  76           
SHEET    1   N 4 ILE B 102  ILE B 107  0                                        
SHEET    2   N 4 PHE B 113  LYS B 122 -1  O  LEU B 115   N  SER B 106           
SHEET    3   N 4 TYR B 128  ASP B 136 -1  O  ASP B 133   N  LEU B 116           
SHEET    4   N 4 GLN B 141  LEU B 142 -1  O  GLN B 141   N  ASP B 136           
SHEET    1   O 4 TRP B 154  TRP B 157  0                                        
SHEET    2   O 4 LEU B 164  TRP B 168 -1  O  VAL B 167   N  TRP B 154           
SHEET    3   O 4 ASP B 171  LYS B 175 -1  O  ASP B 171   N  TRP B 168           
SHEET    4   O 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1   P 3 ILE B 194  ASN B 196  0                                        
SHEET    2   P 3 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   P 3 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224           
SHEET    1   Q 4 ILE B 194  ASN B 196  0                                        
SHEET    2   Q 4 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   Q 4 THR B 265  ASN B 272 -1  O  PHE B 269   N  TYR B 225           
SHEET    4   Q 4 ILE B 285  GLN B 286 -1  O  ILE B 285   N  VAL B 270           
SHEET    1   R 2 LEU B 235  PHE B 240  0                                        
SHEET    2   R 2 LYS B 250  PRO B 255 -1  O  VAL B 252   N  TYR B 238           
SHEET    1   S 4 HIS B 298  TRP B 305  0                                        
SHEET    2   S 4 ARG B 310  ARG B 317 -1  O  LEU B 316   N  TYR B 299           
SHEET    3   S 4 TYR B 322  TYR B 330 -1  O  ASP B 326   N  LEU B 313           
SHEET    4   S 4 TRP B 337  ASN B 338 -1  O  ASN B 338   N  ASP B 329           
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 HIS B 345  MET B 348 -1  O  GLU B 347   N  SER B 323           
SHEET    1   U 4 PRO B 362  PHE B 364  0                                        
SHEET    2   U 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3   U 4 ARG B 382  GLN B 388 -1  O  HIS B 383   N  ILE B 375           
SHEET    4   U 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1   V 4 VAL B 404  LEU B 410  0                                        
SHEET    2   V 4 TYR B 414  SER B 419 -1  O  ILE B 418   N  GLY B 406           
SHEET    3   V 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4   V 4 ASP B 438  CYS B 444 -1  O  THR B 443   N  LYS B 433           
SHEET    1   W 4 TYR B 457  PHE B 461  0                                        
SHEET    2   W 4 TYR B 467  CYS B 472 -1  O  GLN B 469   N  SER B 460           
SHEET    3   W 4 LEU B 479  SER B 484 -1  O  THR B 481   N  LEU B 470           
SHEET    4   W 4 LYS B 489  GLU B 495 -1  O  LEU B 494   N  TYR B 480           
SHEET    1   X 8 SER B 511  ILE B 518  0                                        
SHEET    2   X 8 LYS B 523  LEU B 530 -1  O  MET B 528   N  LYS B 513           
SHEET    3   X 8 ILE B 574  PHE B 578 -1  O  VAL B 575   N  ILE B 529           
SHEET    4   X 8 TYR B 540  ASP B 545  1  N  ASP B 545   O  ALA B 576           
SHEET    5   X 8 VAL B 619  TRP B 629  1  O  ALA B 625   N  LEU B 544           
SHEET    6   X 8 CYS B 649  VAL B 653  1  O  VAL B 653   N  GLY B 628           
SHEET    7   X 8 GLU B 699  GLY B 705  1  O  ILE B 703   N  ALA B 652           
SHEET    8   X 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  2.04  
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  2.10  
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  2.06  
SSBOND   8 CYS B  444    CYS B  447                          1555   1555  2.04  
SSBOND   9 CYS B  454    CYS B  472                          1555   1555  2.06  
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 229                 C1  NAG B2291     1555   1555  1.43  
LINK         ND2 ASN A  85                 C1  NAG A 851     1555   1555  1.43  
LINK         ND2 ASN A 150                 C1  NAG A1501     1555   1555  1.43  
LINK         ND2 ASN B 281                 C1  NAG B2811     1555   1555  1.43  
LINK         ND2 ASN B  92                 C1  NAG B 921     1555   1555  1.43  
LINK         ND2 ASN A 520                 C1  NAG A5201     1555   1555  1.44  
LINK         ND2 ASN B 150                 C1  NAG B1501     1555   1555  1.44  
LINK         ND2 ASN A 219                 C1  NAG A2191     1555   1555  1.44  
LINK         ND2 ASN B  85                 C1  NAG B 851     1555   1555  1.44  
LINK         ND2 ASN B 219                 C1  NAG B2191     1555   1555  1.44  
LINK         O4  NAG A2291                 C1  NAG A2292     1555   1555  1.44  
LINK         ND2 ASN A 229                 C1  NAG A2291     1555   1555  1.44  
LINK         O4  NAG B2291                 C1  NAG B2292     1555   1555  1.45  
CISPEP   1 GLY A  474    PRO A  475          0         9.74                     
CISPEP   2 GLY B  474    PRO B  475          0         7.37                     
SITE     1 AC1  6 VAL A  78  ASN A  85  SER A  86  SER A  87                    
SITE     2 AC1  6 GLN A 388  THR A 395                                          
SITE     1 AC2  2 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  GLU A 232  LYS A 267  NAG A2292                    
SITE     1 AC5  2 GLU A 232  NAG A2291                                          
SITE     1 AC6  3 TRP A 187  VAL A 279  ASN A 281                               
SITE     1 AC7  4 LEU A 519  ASN A 520  ARG A 581  ASP A 605                    
SITE     1 AC8 11 ARG A 125  GLU A 205  GLU A 206  TYR A 547                    
SITE     2 AC8 11 TRP A 629  SER A 630  TYR A 631  TYR A 662                    
SITE     3 AC8 11 TYR A 666  ASN A 710  HIS A 740                               
SITE     1 AC9  8 VAL B  78  ASN B  80  ASN B  85  SER B  86                    
SITE     2 AC9  8 SER B  87  TYR B 386  GLN B 388  THR B 395                    
SITE     1 BC1  3 GLU B  73  ASN B  75  ASN B  92                               
SITE     1 BC2  3 ARG B 147  ILE B 148  ASN B 150                               
SITE     1 BC3  4 ASN B 219  THR B 221  GLN B 308  GLU B 309                    
SITE     1 BC4  5 ILE B 194  ASN B 229  THR B 231  GLU B 232                    
SITE     2 BC4  5 NAG B2292                                                     
SITE     1 BC5  1 NAG B2291                                                     
SITE     1 BC6  1 ASN B 281                                                     
SITE     1 BC7  5 LEU B 519  ASN B 520  ARG B 581  GLU B 604                    
SITE     2 BC7  5 ASP B 605                                                     
SITE     1 BC8 12 ARG B 125  GLU B 205  GLU B 206  TYR B 547                    
SITE     2 BC8 12 TRP B 629  SER B 630  TYR B 631  TRP B 659                    
SITE     3 BC8 12 TYR B 662  TYR B 666  ASN B 710  HIS B 740                    
CRYST1   65.905   67.854  422.095  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      0.015173  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014738  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002369        0.00000                         
TER    5884      PRO A 766                                                      
TER   11761      PRO B 766                                                      
MASTER      530    0   17   37   98    0   25    612042    2  358  116          
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