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LongText Report for: 4UPD-pdb

Name Class
4UPD-pdb
HEADER    HYDROLASE                               16-JUN-14   4UPD              
TITLE     OPEN CONFORMATION OF O. PICEAE STEROL ESTERASE MUTANT I544W           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STEROL ESTERASE;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 13-549;                                           
COMPND   5 EC: 3.1.1.13;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: N-ACETYLGLUCOSAMINE GLYCOSYLATIONS IN POSITIONS 362   
COMPND   9  AND 380                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: OPHIOSTOMA PICEAE;                              
SOURCE   3 ORGANISM_TAXID: 61273;                                               
SOURCE   4 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: KM71;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PPIC9                                      
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.GUTIERREZ-FERNANDEZ,M.E.VAQUERO,A.PRIETO,J.BARRIUSO,M.J.GONZALEZ,   
AUTHOR   2 J.A.HERMOSO                                                          
REVDAT   1   24-SEP-14 4UPD    0                                                
JRNL        AUTH   J.GUTIERREZ-FERNANDEZ,M.E.VAQUERO,A.PRIETO,J.BARRIUSO,       
JRNL        AUTH 2 M.J.MARTINEZ,J.A.HERMOSO                                     
JRNL        TITL   CRYSTAL STRUCTURES OF OPHIOSTOMA PICEAE STEROL ESTERASE:     
JRNL        TITL 2 STRUCTURAL INSIGHTS INTO ACTIVATION MECHANISM AND PRODUCT    
JRNL        TITL 3 RELEASE.                                                     
JRNL        REF    J.STRUCT.BIOL.                V. 187   215 2014              
JRNL        REFN                   ISSN 1047-8477                               
JRNL        PMID   25108239                                                     
JRNL        DOI    10.1016/J.JSB.2014.07.007                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.400                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 58.287                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.79                          
REMARK   3   NUMBER OF REFLECTIONS             : 49284                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1988                          
REMARK   3   R VALUE            (WORKING SET) : 0.1962                          
REMARK   3   FREE R VALUE                     : 0.2477                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.9                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2400                            
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 58.3040 -  6.1694    1.00     2840   137  0.1995 0.2055        
REMARK   3     2  6.1694 -  4.8976    1.00     2782   163  0.1970 0.2437        
REMARK   3     3  4.8976 -  4.2787    1.00     2766   139  0.1697 0.1954        
REMARK   3     4  4.2787 -  3.8876    1.00     2760   145  0.1762 0.2555        
REMARK   3     5  3.8876 -  3.6090    1.00     2776   134  0.1868 0.2489        
REMARK   3     6  3.6090 -  3.3963    1.00     2731   153  0.1894 0.2363        
REMARK   3     7  3.3963 -  3.2262    1.00     2771   126  0.1918 0.2657        
REMARK   3     8  3.2262 -  3.0858    1.00     2785   136  0.2023 0.2445        
REMARK   3     9  3.0858 -  2.9670    1.00     2741   150  0.2065 0.2984        
REMARK   3    10  2.9670 -  2.8646    1.00     2789   113  0.1956 0.2778        
REMARK   3    11  2.8646 -  2.7750    1.00     2697   163  0.2030 0.2808        
REMARK   3    12  2.7750 -  2.6957    1.00     2770   141  0.2073 0.2677        
REMARK   3    13  2.6957 -  2.6247    1.00     2725   133  0.2143 0.2667        
REMARK   3    14  2.6247 -  2.5607    1.00     2778   138  0.2269 0.3030        
REMARK   3    15  2.5607 -  2.5025    1.00     2714   145  0.2355 0.3191        
REMARK   3    16  2.5025 -  2.4492    1.00     2789   129  0.2383 0.2822        
REMARK   3    17  2.4492 -  2.4002    0.97     2670   155  0.2516 0.2935        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.30             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.72            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.13                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.010           8586                                  
REMARK   3   ANGLE     :  1.480          11691                                  
REMARK   3   CHIRALITY :  0.064           1303                                  
REMARK   3   PLANARITY :  0.010           1503                                  
REMARK   3   DIHEDRAL  : 15.219           3060                                  
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: RESIDUES 1-12 IN CHAIN A AND 1-13         
REMARK   3    IN CHAIN B ARE DISORDERED.                                        
REMARK   4                                                                      
REMARK   4 4UPD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JUN-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-60914.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49299                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.29                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.9                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.8                                
REMARK 200  R MERGE                    (I) : 0.11                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.50                              
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) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.97                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.90                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4BE9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM NITRATE, 0.1 M              
REMARK 280  BIS-TRIS PROPANE PH 7.5, 20% PEG 3350                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y,Z                                                 
REMARK 290       7555   -Y+1/2,X,Z+3/4                                          
REMARK 290       8555   Y,-X+1/2,Z+1/4                                          
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       82.43000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       82.43000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.07000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       82.43000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       23.53500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       82.43000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       70.60500            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       82.43000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       82.43000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       47.07000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       82.43000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       70.60500            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       82.43000            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       23.53500            
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: 3280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.3 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     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     TYR A     9                                                      
REMARK 465     VAL A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     GLU B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     TYR B     9                                                      
REMARK 465     VAL B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     PHE B    12                                                      
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   CB   CYS A   279     SG   CYS A   288              1.78            
REMARK 500   OD1  ASP A   293     O    HOH A  2190              1.91            
REMARK 500   O    GLY A   306     OG   SER A   309              1.91            
REMARK 500   ND2  ASN A   362     O5   NAG A  1552              2.02            
REMARK 500   CG   ASN A   380     C1   NAG A  1553              2.17            
REMARK 500   ND2  ASN A   380     O5   NAG A  1553              1.91            
REMARK 500   OD2  ASP A   396     OG1  THR A   398              2.03            
REMARK 500   O    VAL B    15     N    GLY B    26              1.89            
REMARK 500   O    GLY B    31     C    PRO B   116              2.17            
REMARK 500   O    GLY B    31     O    PRO B   116              1.30            
REMARK 500   CG   ASP B    64     OG1  THR B    66              1.81            
REMARK 500   OD1  ASP B    64     OG1  THR B    66              1.09            
REMARK 500   OD2  ASP B    64     OG1  THR B    66              2.12            
REMARK 500   SG   CYS B    72     CB   CYS B   108              1.97            
REMARK 500   OG1  THR B   110     O    HOH B  2001              1.96            
REMARK 500   OD1  ASN B   141     ND2  ASN B   166              2.03            
REMARK 500   O    TYR B   143     OH   TYR B   474              1.80            
REMARK 500   OE1  GLU B   158     CB   THR B   494              1.77            
REMARK 500   OE1  GLU B   158     CG2  THR B   494              2.08            
REMARK 500   O    GLY B   171     O    HOH B  2011              2.14            
REMARK 500   OG   SER B   186     O    HOH B  2013              2.04            
REMARK 500   OD2  ASP B   210     CE   LYS B   213              1.92            
REMARK 500   NH2  ARG B   246     O    VAL B   493              2.12            
REMARK 500   SG   CYS B   279     CB   CYS B   288              1.78            
REMARK 500   CG   ASP B   284     CB   ALA B   287              2.19            
REMARK 500   OD1  ASP B   284     CA   ALA B   287              2.11            
REMARK 500   OD1  ASP B   284     CB   ALA B   287              1.31            
REMARK 500   C    CYS B   288     OG1  THR B   291              2.00            
REMARK 500   O    CYS B   288     OG1  THR B   291              0.92            
REMARK 500   O    ALA B   300     OG   SER B   303              1.66            
REMARK 500   OE2  GLU B   331     NH2  ARG B   548              2.08            
REMARK 500   OE1  GLU B   350     OG   SER B   453              1.62            
REMARK 500   ND2  ASN B   362     C2   NAG B  1551              2.03            
REMARK 500   C    SER B   365     CD1  ILE B   369              1.80            
REMARK 500   O    SER B   365     CD1  ILE B   369              1.46            
REMARK 500   N    THR B   366     CD1  ILE B   369              2.19            
REMARK 500   O    THR B   366     CG2  VAL B   370              1.99            
REMARK 500   OG1  THR B   382     OE1  GLN B   385              2.13            
REMARK 500   O    PHE B   389     OG1  THR B   392              1.43            
REMARK 500   OH   TYR B   393     OD2  ASP B   424              1.73            
REMARK 500   OD2  ASP B   396     OG1  THR B   398              1.77            
REMARK 500   O    ASN B   404     OH   TYR B   456              2.20            
REMARK 500   O    ALA B   419     O    HOH B  2026              2.15            
REMARK 500   O    LEU B   435     OG   SER B   439              2.16            
REMARK 500   O    PHE B   464     OG1  THR B   467              2.13            
REMARK 500   O    TYR B   480     OG   SER B   484              1.65            
REMARK 500   O    SER B   482     CG   GLN B   486              1.82            
REMARK 500   O    HOH A  2004     O    HOH A  2006              2.16            
REMARK 500   O    HOH A  2005     O    HOH A  2007              2.19            
REMARK 500   O    HOH A  2017     O    HOH A  2092              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD1  ASN A    18     NZ   LYS A   296     7554     1.87            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 288   CA    CYS A 288   CB      0.082                       
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    CYS A 288   CA  -  CB  -  SG  ANGL. DEV. =   8.1 DEGREES          
REMARK 500    PRO B 159   C   -  N   -  CD  ANGL. DEV. = -16.2 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 220     -117.77     61.31                                   
REMARK 500    SER A 252       70.35     61.92                                   
REMARK 500    SER A 254      -94.49   -157.78                                   
REMARK 500    SER A 312     -119.29     58.23                                   
REMARK 500    VAL A 324      -65.81   -124.03                                   
REMARK 500    TYR A 377      -73.39   -106.07                                   
REMARK 500    PHE A 427      -82.01   -121.27                                   
REMARK 500    PHE A 460      -36.59     74.67                                   
REMARK 500    ASN A 479     -167.23   -166.68                                   
REMARK 500    ASN B  16      -36.47   -171.94                                   
REMARK 500    ALA B 117      117.11    113.12                                   
REMARK 500    LYS B 178      -81.48      9.79                                   
REMARK 500    SER B 220     -114.41     57.27                                   
REMARK 500    SER B 254      -95.81   -167.89                                   
REMARK 500    SER B 312     -124.82     57.27                                   
REMARK 500    VAL B 324      -66.41   -124.85                                   
REMARK 500    PHE B 427      -74.95   -121.16                                   
REMARK 500    ASP B 444       -5.10     86.04                                   
REMARK 500    PHE B 460      -47.58     73.98                                   
REMARK 500    ASN B 479     -163.31   -170.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 VAL B   15     ASN B   16                  -40.45                    
REMARK 500 SER B  212     LYS B  213                  146.21                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN A  16        23.6      L          L   OUTSIDE RANGE           
REMARK 500    HIS B 272        23.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7P9 A1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7P9 B1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A1551                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG A1552  BOUND TO ASN A 362                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG A1553  BOUND TO ASN A 380                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG B1551  BOUND TO ASN B 362                                       
DBREF  4UPD A   13   549  UNP    Q2TFW1   Q2TFW1_9PEZI    13    549             
DBREF  4UPD B   13   549  UNP    Q2TFW1   Q2TFW1_9PEZI    13    549             
SEQADV 4UPD GLU A    5  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD ALA A    6  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD GLU A    7  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD ALA A    8  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD TYR A    9  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD VAL A   10  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD GLU A   11  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD PHE A   12  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD TRP A  544  UNP  Q2TFW1    ILE   544 ENGINEERED MUTATION            
SEQADV 4UPD GLU B    5  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD ALA B    6  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD GLU B    7  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD ALA B    8  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD TYR B    9  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD VAL B   10  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD GLU B   11  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD PHE B   12  UNP  Q2TFW1              EXPRESSION TAG                 
SEQADV 4UPD TRP B  544  UNP  Q2TFW1    ILE   544 ENGINEERED MUTATION            
SEQRES   1 A  545  GLU ALA GLU ALA TYR VAL GLU PHE THR THR VAL ASN VAL          
SEQRES   2 A  545  ASN TYR PRO GLU GLY GLU VAL VAL GLY VAL SER VAL LEU          
SEQRES   3 A  545  GLY ILE GLU SER PHE ARG GLY VAL PRO PHE ALA GLN PRO          
SEQRES   4 A  545  PRO VAL GLY ASN LEU ARG LEU LYS PRO PRO VAL ARG TYR          
SEQRES   5 A  545  THR GLU ASN ILE GLY THR LYS ASP THR THR GLY ILE GLY          
SEQRES   6 A  545  PRO SER CYS PRO GLN MET TYR LEU SER THR GLY ASN GLY          
SEQRES   7 A  545  GLU LEU LEU PHE GLN LEU VAL GLY ASN LEU ILE ASN ILE          
SEQRES   8 A  545  PRO LEU PHE GLN THR ALA THR LEU SER SER GLU ASP CYS          
SEQRES   9 A  545  LEU THR LEU ASN ILE GLN ARG PRO ALA GLY THR THR SER          
SEQRES  10 A  545  ASN SER SER LEU PRO VAL LEU PHE TRP ILE PHE GLY GLY          
SEQRES  11 A  545  GLY PHE GLU LEU GLY THR ASN GLN TYR TYR ASP GLY ILE          
SEQRES  12 A  545  ASP LEU LEU THR GLU GLY ILE SER LEU GLY GLU PRO PHE          
SEQRES  13 A  545  ILE PHE VAL ALA ILE ASN TYR ARG VAL GLY GLY PHE GLY          
SEQRES  14 A  545  PHE LEU GLY GLY LYS GLU ILE LYS ALA ASP GLY SER SER          
SEQRES  15 A  545  ASN LEU GLY LEU LEU ASP GLN ARG ILE ALA LEU GLU TRP          
SEQRES  16 A  545  VAL ALA ASP ASN ILE ALA SER PHE GLY GLY ASP PRO SER          
SEQRES  17 A  545  LYS VAL THR ILE TRP GLY GLU SER ALA GLY SER ILE SER          
SEQRES  18 A  545  VAL PHE ASP GLN MET ALA LEU TYR GLY GLY ASN ASN LYS          
SEQRES  19 A  545  TYR LYS GLY LYS ALA LEU PHE ARG GLY GLY ILE MET ASN          
SEQRES  20 A  545  SER GLY SER VAL VAL PRO ALA ALA PRO VAL ASP GLY VAL          
SEQRES  21 A  545  LYS ALA GLN ALA ILE TYR ASP HIS VAL VAL SER GLU ALA          
SEQRES  22 A  545  GLY CYS ALA GLY THR SER ASP THR LEU ALA CYS LEU ARG          
SEQRES  23 A  545  THR VAL ASP TYR THR LYS PHE LEU THR ALA VAL ASN SER          
SEQRES  24 A  545  VAL PRO GLY ILE VAL SER TYR SER SER ILE ALA LEU SER          
SEQRES  25 A  545  TYR LEU PRO ARG PRO ASP GLY VAL VAL LEU ILE ASP SER          
SEQRES  26 A  545  PRO GLU GLU ILE VAL LYS ASN LYS GLN TYR ALA ALA VAL          
SEQRES  27 A  545  PRO MET ILE ILE GLY ASP GLN GLU ASP GLU GLY THR LEU          
SEQRES  28 A  545  PHE ALA VAL LEU PRO ASN ASN ILE THR SER THR ALA LYS          
SEQRES  29 A  545  ILE VAL GLN TYR PHE GLN ASP LEU TYR PHE TYR ASN ALA          
SEQRES  30 A  545  THR LYS GLU GLN LEU THR ALA PHE VAL ASN THR TYR PRO          
SEQRES  31 A  545  THR ASP ILE THR ALA GLY SER PRO PHE ASN THR GLY ILE          
SEQRES  32 A  545  PHE ASN GLU LEU TYR PRO GLY PHE LYS ARG LEU ALA ALA          
SEQRES  33 A  545  ILE LEU GLY ASP MET THR PHE THR LEU ALA ARG ARG ALA          
SEQRES  34 A  545  PHE LEU GLN LEU CYS SER GLU VAL ASN PRO ASP VAL PRO          
SEQRES  35 A  545  SER TRP SER TYR LEU ALA SER TYR ASP TYR GLY PHE PRO          
SEQRES  36 A  545  PHE LEU GLY THR PHE HIS ALA THR ASP ILE LEU GLN VAL          
SEQRES  37 A  545  PHE TYR GLY VAL LEU PRO ASN TYR ALA SER GLY SER ILE          
SEQRES  38 A  545  GLN LYS TYR TYR ILE ASN PHE VAL THR THR GLY ASP PRO          
SEQRES  39 A  545  ASN LYS GLY ALA ALA VAL ASP ILE GLN TRP PRO GLN TRP          
SEQRES  40 A  545  SER ALA LYS LYS ASN ILE LEU GLN ILE TYR ALA THR LYS          
SEQRES  41 A  545  ALA VAL ILE VAL ALA ASP ASN PHE ARG ALA LYS SER TYR          
SEQRES  42 A  545  GLU TYR LEU TYR ASN ASN TRP GLY ILE PHE ARG ILE              
SEQRES   1 B  545  GLU ALA GLU ALA TYR VAL GLU PHE THR THR VAL ASN VAL          
SEQRES   2 B  545  ASN TYR PRO GLU GLY GLU VAL VAL GLY VAL SER VAL LEU          
SEQRES   3 B  545  GLY ILE GLU SER PHE ARG GLY VAL PRO PHE ALA GLN PRO          
SEQRES   4 B  545  PRO VAL GLY ASN LEU ARG LEU LYS PRO PRO VAL ARG TYR          
SEQRES   5 B  545  THR GLU ASN ILE GLY THR LYS ASP THR THR GLY ILE GLY          
SEQRES   6 B  545  PRO SER CYS PRO GLN MET TYR LEU SER THR GLY ASN GLY          
SEQRES   7 B  545  GLU LEU LEU PHE GLN LEU VAL GLY ASN LEU ILE ASN ILE          
SEQRES   8 B  545  PRO LEU PHE GLN THR ALA THR LEU SER SER GLU ASP CYS          
SEQRES   9 B  545  LEU THR LEU ASN ILE GLN ARG PRO ALA GLY THR THR SER          
SEQRES  10 B  545  ASN SER SER LEU PRO VAL LEU PHE TRP ILE PHE GLY GLY          
SEQRES  11 B  545  GLY PHE GLU LEU GLY THR ASN GLN TYR TYR ASP GLY ILE          
SEQRES  12 B  545  ASP LEU LEU THR GLU GLY ILE SER LEU GLY GLU PRO PHE          
SEQRES  13 B  545  ILE PHE VAL ALA ILE ASN TYR ARG VAL GLY GLY PHE GLY          
SEQRES  14 B  545  PHE LEU GLY GLY LYS GLU ILE LYS ALA ASP GLY SER SER          
SEQRES  15 B  545  ASN LEU GLY LEU LEU ASP GLN ARG ILE ALA LEU GLU TRP          
SEQRES  16 B  545  VAL ALA ASP ASN ILE ALA SER PHE GLY GLY ASP PRO SER          
SEQRES  17 B  545  LYS VAL THR ILE TRP GLY GLU SER ALA GLY SER ILE SER          
SEQRES  18 B  545  VAL PHE ASP GLN MET ALA LEU TYR GLY GLY ASN ASN LYS          
SEQRES  19 B  545  TYR LYS GLY LYS ALA LEU PHE ARG GLY GLY ILE MET ASN          
SEQRES  20 B  545  SER GLY SER VAL VAL PRO ALA ALA PRO VAL ASP GLY VAL          
SEQRES  21 B  545  LYS ALA GLN ALA ILE TYR ASP HIS VAL VAL SER GLU ALA          
SEQRES  22 B  545  GLY CYS ALA GLY THR SER ASP THR LEU ALA CYS LEU ARG          
SEQRES  23 B  545  THR VAL ASP TYR THR LYS PHE LEU THR ALA VAL ASN SER          
SEQRES  24 B  545  VAL PRO GLY ILE VAL SER TYR SER SER ILE ALA LEU SER          
SEQRES  25 B  545  TYR LEU PRO ARG PRO ASP GLY VAL VAL LEU ILE ASP SER          
SEQRES  26 B  545  PRO GLU GLU ILE VAL LYS ASN LYS GLN TYR ALA ALA VAL          
SEQRES  27 B  545  PRO MET ILE ILE GLY ASP GLN GLU ASP GLU GLY THR LEU          
SEQRES  28 B  545  PHE ALA VAL LEU PRO ASN ASN ILE THR SER THR ALA LYS          
SEQRES  29 B  545  ILE VAL GLN TYR PHE GLN ASP LEU TYR PHE TYR ASN ALA          
SEQRES  30 B  545  THR LYS GLU GLN LEU THR ALA PHE VAL ASN THR TYR PRO          
SEQRES  31 B  545  THR ASP ILE THR ALA GLY SER PRO PHE ASN THR GLY ILE          
SEQRES  32 B  545  PHE ASN GLU LEU TYR PRO GLY PHE LYS ARG LEU ALA ALA          
SEQRES  33 B  545  ILE LEU GLY ASP MET THR PHE THR LEU ALA ARG ARG ALA          
SEQRES  34 B  545  PHE LEU GLN LEU CYS SER GLU VAL ASN PRO ASP VAL PRO          
SEQRES  35 B  545  SER TRP SER TYR LEU ALA SER TYR ASP TYR GLY PHE PRO          
SEQRES  36 B  545  PHE LEU GLY THR PHE HIS ALA THR ASP ILE LEU GLN VAL          
SEQRES  37 B  545  PHE TYR GLY VAL LEU PRO ASN TYR ALA SER GLY SER ILE          
SEQRES  38 B  545  GLN LYS TYR TYR ILE ASN PHE VAL THR THR GLY ASP PRO          
SEQRES  39 B  545  ASN LYS GLY ALA ALA VAL ASP ILE GLN TRP PRO GLN TRP          
SEQRES  40 B  545  SER ALA LYS LYS ASN ILE LEU GLN ILE TYR ALA THR LYS          
SEQRES  41 B  545  ALA VAL ILE VAL ALA ASP ASN PHE ARG ALA LYS SER TYR          
SEQRES  42 B  545  GLU TYR LEU TYR ASN ASN TRP GLY ILE PHE ARG ILE              
HET    7P9  A1550      28                                                       
HET    7P9  B1550      28                                                       
HET    PGE  A1551      10                                                       
HET    NAG  A1552      14                                                       
HET    NAG  A1553      14                                                       
HET    NAG  B1551      14                                                       
HETNAM     7P9 [(2R)-2-HEPTANOYLOXY-3-PHOSPHONOOXY-PROPYL]                      
HETNAM   2 7P9  NONANOATE                                                       
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   3  7P9    2(C19 H37 O8 P)                                              
FORMUL   4  PGE    C6 H14 O4                                                    
FORMUL   5  NAG    3(C8 H15 N O6)                                               
FORMUL   6  HOH   *335(H2 O)                                                    
HELIX    1   1 VAL A   45  ARG A   49  5                                   5    
HELIX    2   2 GLU A   83  ASN A   94  1                                  12    
HELIX    3   3 ILE A   95  THR A  102  1                                   8    
HELIX    4   4 THR A  140  TYR A  144  5                                   5    
HELIX    5   5 GLY A  146  LEU A  156  1                                  11    
HELIX    6   6 VAL A  169  GLY A  173  5                                   5    
HELIX    7   7 GLY A  177  GLY A  184  1                                   8    
HELIX    8   8 ASN A  187  ILE A  204  1                                  18    
HELIX    9   9 ALA A  205  PHE A  207  5                                   3    
HELIX   10  10 SER A  220  ASN A  236  1                                  17    
HELIX   11  11 GLY A  263  ALA A  277  1                                  15    
HELIX   12  12 ASP A  284  VAL A  292  1                                   9    
HELIX   13  13 ASP A  293  ASN A  302  1                                  10    
HELIX   14  14 SER A  329  ASN A  336  1                                   8    
HELIX   15  15 THR A  354  VAL A  358  5                                   5    
HELIX   16  16 SER A  365  TYR A  377  1                                  13    
HELIX   17  17 THR A  382  ASN A  391  1                                  10    
HELIX   18  18 ASP A  396  GLY A  400  5                                   5    
HELIX   19  19 GLY A  414  PHE A  427  1                                  14    
HELIX   20  20 PHE A  427  ASN A  442  1                                  16    
HELIX   21  21 ALA A  466  VAL A  472  1                                   7    
HELIX   22  22 ASN A  479  GLY A  496  1                                  18    
HELIX   23  23 GLN A  510  LYS A  515  1                                   6    
HELIX   24  24 ARG A  533  ASN A  543  1                                  11    
HELIX   25  25 TRP A  544  ARG A  548  5                                   5    
HELIX   26  26 VAL B   45  ARG B   49  5                                   5    
HELIX   27  27 GLU B   83  ASN B   94  1                                  12    
HELIX   28  28 ILE B   95  THR B  102  1                                   8    
HELIX   29  29 GLY B  146  LEU B  156  1                                  11    
HELIX   30  30 VAL B  169  LEU B  175  1                                   7    
HELIX   31  31 GLY B  177  ASP B  183  1                                   7    
HELIX   32  32 ASN B  187  ILE B  204  1                                  18    
HELIX   33  33 ALA B  205  PHE B  207  5                                   3    
HELIX   34  34 SER B  220  ASN B  236  1                                  17    
HELIX   35  35 GLY B  263  GLY B  278  1                                  16    
HELIX   36  36 ASP B  284  ARG B  290  1                                   7    
HELIX   37  37 ASP B  293  ASN B  302  1                                  10    
HELIX   38  38 SER B  329  ASN B  336  1                                   8    
HELIX   39  39 GLY B  353  VAL B  358  1                                   6    
HELIX   40  40 SER B  365  TYR B  377  1                                  13    
HELIX   41  41 THR B  382  THR B  392  1                                  11    
HELIX   42  42 ASP B  396  GLY B  400  5                                   5    
HELIX   43  43 GLY B  414  PHE B  427  1                                  14    
HELIX   44  44 PHE B  427  ASN B  442  1                                  16    
HELIX   45  45 ALA B  466  VAL B  472  1                                   7    
HELIX   46  46 ASN B  479  GLY B  496  1                                  18    
HELIX   47  47 GLN B  510  LYS B  515  1                                   6    
HELIX   48  48 ARG B  533  ASN B  543  1                                  11    
HELIX   49  49 TRP B  544  ARG B  548  5                                   5    
SHEET    1  AA 2 THR A  13  TYR A  19  0                                        
SHEET    2  AA 2 GLY A  22  VAL A  29 -1  O  GLY A  22   N  TYR A  19           
SHEET    1  AB 2 THR A  62  ASP A  64  0                                        
SHEET    2  AB 2 GLY A  22  VAL A  29  1  O  GLU A  23   N  LYS A  63           
SHEET    1  AC12 ALA A 525  ALA A 529  0                                        
SHEET    2  AC12 ASN A 516  ILE A 520 -1  O  ILE A 517   N  VAL A 528           
SHEET    3  AC12 SER A 447  ALA A 452  1  O  SER A 449   N  LEU A 518           
SHEET    4  AC12 MET A 344  GLN A 349  1  O  MET A 344   N  TRP A 448           
SHEET    5  AC12 GLY A 247  ASN A 251  1  O  GLY A 248   N  ILE A 345           
SHEET    6  AC12 GLY A 209  GLU A 219  1  O  ILE A 216   N  ILE A 249           
SHEET    7  AC12 LEU A 125  ILE A 131  1  O  LEU A 125   N  ASP A 210           
SHEET    8  AC12 ILE A 161  ILE A 165  1  O  ILE A 161   N  LEU A 128           
SHEET    9  AC12 THR A 110  PRO A 116 -1  O  ASN A 112   N  ALA A 164           
SHEET   10  AC12 ILE A  32  PRO A  39 -1  O  GLU A  33   N  ARG A 115           
SHEET   11  AC12 GLY A  22  VAL A  29 -1  O  VAL A  27   N  SER A  34           
SHEET   12  AC12 THR A  62  ASP A  64  1  O  LYS A  63   N  VAL A  25           
SHEET    1  AD12 ALA A 525  ALA A 529  0                                        
SHEET    2  AD12 ASN A 516  ILE A 520 -1  O  ILE A 517   N  VAL A 528           
SHEET    3  AD12 SER A 447  ALA A 452  1  O  SER A 449   N  LEU A 518           
SHEET    4  AD12 MET A 344  GLN A 349  1  O  MET A 344   N  TRP A 448           
SHEET    5  AD12 GLY A 247  ASN A 251  1  O  GLY A 248   N  ILE A 345           
SHEET    6  AD12 GLY A 209  GLU A 219  1  O  ILE A 216   N  ILE A 249           
SHEET    7  AD12 LEU A 125  ILE A 131  1  O  LEU A 125   N  ASP A 210           
SHEET    8  AD12 ILE A 161  ILE A 165  1  O  ILE A 161   N  LEU A 128           
SHEET    9  AD12 THR A 110  PRO A 116 -1  O  ASN A 112   N  ALA A 164           
SHEET   10  AD12 ILE A  32  PRO A  39 -1  O  GLU A  33   N  ARG A 115           
SHEET   11  AD12 GLY A  22  VAL A  29 -1  O  VAL A  27   N  SER A  34           
SHEET   12  AD12 THR A  13  TYR A  19 -1  O  THR A  13   N  SER A  28           
SHEET    1  AE 2 LYS A 238  TYR A 239  0                                        
SHEET    2  AE 2 LYS A 242  ALA A 243 -1  O  LYS A 242   N  TYR A 239           
SHEET    1  BA 2 GLY B  22  VAL B  25  0                                        
SHEET    2  BA 2 GLY B  61  ASP B  64  1  O  GLY B  61   N  GLU B  23           
SHEET    1  BB11 VAL B  27  VAL B  29  0                                        
SHEET    2  BB11 ILE B  32  PRO B  39 -1  O  ILE B  32   N  VAL B  29           
SHEET    3  BB11 THR B 110  ARG B 115 -1  O  LEU B 111   N  VAL B  38           
SHEET    4  BB11 ILE B 161  ILE B 165 -1  O  PHE B 162   N  GLN B 114           
SHEET    5  BB11 LEU B 125  ILE B 131  1  O  PRO B 126   N  ILE B 161           
SHEET    6  BB11 GLY B 209  GLU B 219  1  N  ASP B 210   O  LEU B 125           
SHEET    7  BB11 GLY B 247  ASN B 251  1  O  GLY B 247   N  ILE B 216           
SHEET    8  BB11 MET B 344  GLN B 349  1  O  ILE B 345   N  MET B 250           
SHEET    9  BB11 SER B 447  ALA B 452  1  O  TRP B 448   N  ILE B 346           
SHEET   10  BB11 ASN B 516  ILE B 520  1  O  LEU B 518   N  LEU B 451           
SHEET   11  BB11 ALA B 525  ALA B 529 -1  O  VAL B 526   N  GLN B 519           
SHEET    1  BC 2 LYS B 238  TYR B 239  0                                        
SHEET    2  BC 2 LYS B 242  ALA B 243 -1  O  LYS B 242   N  TYR B 239           
LINK         ND2 ASN A 362                 C1  NAG A1552     1555   1555  1.53  
LINK         ND2 ASN A 380                 C1  NAG A1553     1555   1555  1.08  
LINK         ND2 ASN B 362                 C1  NAG B1551     1555   1555  1.25  
CISPEP   1 SER A  401    PRO A  402          0        12.12                     
CISPEP   2 VAL A  476    LEU A  477          0        -6.75                     
CISPEP   3 SER B  401    PRO B  402          0        10.04                     
CISPEP   4 VAL B  476    LEU B  477          0       -12.92                     
SITE     1 AC1  9 ASP A 455  PHE A 458  GLN A 471  VAL A 476                    
SITE     2 AC1  9 LEU A 477  ASN A 479  HOH A2256  HOH A2257                    
SITE     3 AC1  9 HOH A2285                                                     
SITE     1 AC2  6 ASP B 455  GLN B 471  VAL B 476  LEU B 477                    
SITE     2 AC2  6 ASN B 479  HOH B2040                                          
SITE     1 AC3  4 SER A 220  ILE A 307  THR A 426  HIS A 465                    
SITE     1 AC4  3 TYR A 310  ASN A 362  ILE A 363                               
SITE     1 AC5  6 ALA A 259  ASN A 380  GLU A 384  ARG A 548                    
SITE     2 AC5  6 HOH A2283  HOH A2286                                          
SITE     1 AC6  2 TYR B 310  ASN B 362                                          
CRYST1  164.860  164.860   94.140  90.00  90.00  90.00 I 41         16          
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      0.006066  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006066  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010622        0.00000                         
TER    4138      ILE A 549                                                      
TER    8265      ILE B 549                                                      
MASTER      461    0    6   49   45    0   10    6 8706    2  111   84          
END                                                                             

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