Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 5a2g-pdb

Name Class
5a2g-pdb
HEADER    HYDROLASE                               19-MAY-15   5A2G              
TITLE     AN ESTERASE FROM ANAEROBIC CLOSTRIDIUM HATHEWAYI CAN                  
TITLE    2 HYDROLYZE ALIPHATIC AROMATIC POLYESTERS                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: ESTERASE;                                                   
COMPND   5 EC: 3.1.1.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUNGATELLA HATHEWAYI;                           
SOURCE   3 ORGANISM_TAXID: 566550;                                              
SOURCE   4 STRAIN: DSM 13479;                                                   
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: GOLD                                      
KEYWDS    HYDROLASE, MICROBIAL POLYESTERASE, ANAEROBIC ESTERASE, POLYESTER      
KEYWDS   2 BIODEGRADATION, BIOGAS BATCH, ANAEROBIC BIODEGRADATION, CLOSTRIDIUM  
KEYWDS   3 HATHEWAYI                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.HROMIC,T.PAVKOV KELLER,G.STEINKELLNER,K.GRUBER,V.PERZ,              
AUTHOR   2 A.BAUMSCHLAGER,K.BLEYMAIER,S.ZITZENBACHER,A.ZANKEL,C.MAYRHOFER,      
AUTHOR   3 C.SINKEL,U.KUEPER,K.A.SCHLEGEL,D.RIBITSCH,G.M.GUEBITZ                
REVDAT   1   24-FEB-16 5A2G    0                                                
JRNL        AUTH   V.PERZ,K.BLEYMAIER,C.SINKEL,U.KUEPER,M.BONNEKESSEL,          
JRNL        AUTH 2 D.RIBITSCH,G.M.GUEBITZ                                       
JRNL        TITL   SUBSTRATE SPECIFICITIES OF CUTINASES ON ALIPHATIC-AROMATIC   
JRNL        TITL 2 POLYESTERS AND ON THEIR MODEL SUBSTRATES.                    
JRNL        REF    N.BIOTECHNOL                  V.  33   295 2016              
JRNL        REFN                   ISSN 1876-4347                               
JRNL        PMID   26594021                                                     
JRNL        DOI    10.1016/J.NBT.2015.11.004                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 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) : 1.899                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.103                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.39                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.53                          
REMARK   3   NUMBER OF REFLECTIONS             : 163038                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1910                          
REMARK   3   R VALUE            (WORKING SET) : 0.1886                          
REMARK   3   FREE R VALUE                     : 0.2374                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.9                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 8044                            
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 60.1332 -  5.8991    0.91     5674   273  0.1442 0.1663        
REMARK   3     2  5.8991 -  4.6829    0.96     5855   295  0.1358 0.1623        
REMARK   3     3  4.6829 -  4.0911    0.86     5296   303  0.1308 0.1597        
REMARK   3     4  4.0911 -  3.7171    0.90     5477   266  0.1460 0.1717        
REMARK   3     5  3.7171 -  3.4507    0.92     5669   270  0.1642 0.2082        
REMARK   3     6  3.4507 -  3.2473    0.94     5747   277  0.1813 0.2311        
REMARK   3     7  3.2473 -  3.0846    0.94     5805   274  0.1904 0.2313        
REMARK   3     8  3.0846 -  2.9504    0.90     5489   303  0.1970 0.2474        
REMARK   3     9  2.9504 -  2.8368    0.78     4737   280  0.1950 0.2477        
REMARK   3    10  2.8368 -  2.7389    0.85     5221   274  0.1993 0.2556        
REMARK   3    11  2.7389 -  2.6533    0.87     5375   237  0.1974 0.2423        
REMARK   3    12  2.6533 -  2.5774    0.89     5350   295  0.1973 0.2671        
REMARK   3    13  2.5774 -  2.5096    0.89     5452   305  0.1996 0.2495        
REMARK   3    14  2.5096 -  2.4483    0.90     5525   274  0.1989 0.2697        
REMARK   3    15  2.4483 -  2.3927    0.90     5455   282  0.1991 0.2723        
REMARK   3    16  2.3927 -  2.3418    0.91     5556   297  0.2089 0.2798        
REMARK   3    17  2.3418 -  2.2949    0.87     5238   269  0.2163 0.2940        
REMARK   3    18  2.2949 -  2.2516    0.74     4568   262  0.2260 0.3033        
REMARK   3    19  2.2516 -  2.2114    0.80     4815   292  0.2439 0.3016        
REMARK   3    20  2.2114 -  2.1739    0.82     5033   268  0.2331 0.3120        
REMARK   3    21  2.1739 -  2.1388    0.81     4931   237  0.2296 0.2821        
REMARK   3    22  2.1388 -  2.1059    0.82     5140   227  0.2243 0.2662        
REMARK   3    23  2.1059 -  2.0750    0.82     4898   279  0.2350 0.3032        
REMARK   3    24  2.0750 -  2.0457    0.81     4951   267  0.2454 0.3195        
REMARK   3    25  2.0457 -  2.0181    0.80     4965   237  0.2505 0.3032        
REMARK   3    26  2.0181 -  1.9919    0.79     4804   232  0.2600 0.3145        
REMARK   3    27  1.9919 -  1.9670    0.78     4757   254  0.2647 0.3201        
REMARK   3    28  1.9670 -  1.9433    0.77     4672   250  0.2748 0.3439        
REMARK   3    29  1.9433 -  1.9207    0.75     4625   245  0.2951 0.3421        
REMARK   3    30  1.9207 -  1.8991    0.65     3914   220  0.3274 0.3891        
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)     : 0.27             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.99            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.92                          
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      :  0.005          16204                                  
REMARK   3   ANGLE     :  0.914          22004                                  
REMARK   3   CHIRALITY :  0.036           2320                                  
REMARK   3   PLANARITY :  0.005           2888                                  
REMARK   3   DIHEDRAL  : 13.544           5904                                  
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 5A2G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-63816.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III                          
REMARK 200  BEAMLINE                       : P11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M-F)               
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 163181                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.90                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.1                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.1                               
REMARK 200  DATA REDUNDANCY                : 2.9                                
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09                               
REMARK 200   FOR THE DATA SET  : 7.80                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.59                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.10                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: XDS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 2OGS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M AMMONIUM SULFATE, 0.1 M            
REMARK 280  HEPES, PH 7.0 AND 0.5 % W/V POLYETHYLENE GLYCOL 8000                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      120.91500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 3990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 3990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.1 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     MET A     1                                                      
REMARK 465     PRO A   503                                                      
REMARK 465     ASN A   504                                                      
REMARK 465     LEU A   505                                                      
REMARK 465     THR A   506                                                      
REMARK 465     LEU A   507                                                      
REMARK 465     ALA A   508                                                      
REMARK 465     ASN A   509                                                      
REMARK 465     ILE A   510                                                      
REMARK 465     THR A   511                                                      
REMARK 465     GLN A   512                                                      
REMARK 465     GLU A   513                                                      
REMARK 465     ASP A   514                                                      
REMARK 465     ASN A   515                                                      
REMARK 465     GLN A   516                                                      
REMARK 465     ILE A   517                                                      
REMARK 465     GLN A   518                                                      
REMARK 465     HIS A   519                                                      
REMARK 465     ALA A   520                                                      
REMARK 465     LEU A   521                                                      
REMARK 465     GLU A   522                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B   503                                                      
REMARK 465     ASN B   504                                                      
REMARK 465     LEU B   505                                                      
REMARK 465     THR B   506                                                      
REMARK 465     LEU B   507                                                      
REMARK 465     ALA B   508                                                      
REMARK 465     ASN B   509                                                      
REMARK 465     ILE B   510                                                      
REMARK 465     THR B   511                                                      
REMARK 465     GLN B   512                                                      
REMARK 465     GLU B   513                                                      
REMARK 465     ASP B   514                                                      
REMARK 465     ASN B   515                                                      
REMARK 465     GLN B   516                                                      
REMARK 465     ILE B   517                                                      
REMARK 465     GLN B   518                                                      
REMARK 465     HIS B   519                                                      
REMARK 465     ALA B   520                                                      
REMARK 465     LEU B   521                                                      
REMARK 465     GLU B   522                                                      
REMARK 465     MET C     1                                                      
REMARK 465     PRO C   503                                                      
REMARK 465     ASN C   504                                                      
REMARK 465     LEU C   505                                                      
REMARK 465     THR C   506                                                      
REMARK 465     LEU C   507                                                      
REMARK 465     ALA C   508                                                      
REMARK 465     ASN C   509                                                      
REMARK 465     ILE C   510                                                      
REMARK 465     THR C   511                                                      
REMARK 465     GLN C   512                                                      
REMARK 465     GLU C   513                                                      
REMARK 465     ASP C   514                                                      
REMARK 465     ASN C   515                                                      
REMARK 465     GLN C   516                                                      
REMARK 465     ILE C   517                                                      
REMARK 465     GLN C   518                                                      
REMARK 465     HIS C   519                                                      
REMARK 465     ALA C   520                                                      
REMARK 465     LEU C   521                                                      
REMARK 465     GLU C   522                                                      
REMARK 465     MET D     1                                                      
REMARK 465     PRO D   503                                                      
REMARK 465     ASN D   504                                                      
REMARK 465     LEU D   505                                                      
REMARK 465     THR D   506                                                      
REMARK 465     LEU D   507                                                      
REMARK 465     ALA D   508                                                      
REMARK 465     ASN D   509                                                      
REMARK 465     ILE D   510                                                      
REMARK 465     THR D   511                                                      
REMARK 465     GLN D   512                                                      
REMARK 465     GLU D   513                                                      
REMARK 465     ASP D   514                                                      
REMARK 465     ASN D   515                                                      
REMARK 465     GLN D   516                                                      
REMARK 465     ILE D   517                                                      
REMARK 465     GLN D   518                                                      
REMARK 465     HIS D   519                                                      
REMARK 465     ALA D   520                                                      
REMARK 465     LEU D   521                                                      
REMARK 465     GLU D   522                                                      
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   OD2  ASP A    86     NH1  ARG B    69              2.18            
REMARK 500   O    LEU B   153     OG   SER B   165              2.19            
REMARK 500   OH   TYR B   498     O    HOH B  2261              2.17            
REMARK 500   N    ALA D     2     O    HOH C  2413              2.17            
REMARK 500   O    LYS D    16     O    HOH D  2019              2.18            
REMARK 500   O    HOH A  2030     O    HOH A  2189              2.15            
REMARK 500   O    HOH A  2072     O    HOH A  2226              2.11            
REMARK 500   O    HOH B  2119     O    HOH B  2121              2.19            
REMARK 500   O    HOH C  2052     O    HOH C  2133              2.14            
REMARK 500   O    HOH D  2089     O    HOH D  2191              2.13            
REMARK 500   O    HOH D  2165     O    HOH D  2314              2.19            
REMARK 500   O    HOH D  2230     O    HOH C  2286              2.15            
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    TYR A   7      -61.78   -141.34                                   
REMARK 500    ALA A  57       77.52   -117.92                                   
REMARK 500    ALA A 115     -133.55     46.65                                   
REMARK 500    ASN A 148     -130.24     36.59                                   
REMARK 500    PRO A 157        2.99    -69.68                                   
REMARK 500    SER A 200     -119.28     58.86                                   
REMARK 500    ASP A 294     -153.38   -159.23                                   
REMARK 500    GLU A 323      -76.03    -35.27                                   
REMARK 500    ASN A 410       73.08     65.56                                   
REMARK 500    CYS A 417       -0.60     87.04                                   
REMARK 500    ILE A 438      -54.30   -134.76                                   
REMARK 500    ASN A 489       41.44     38.17                                   
REMARK 500    TYR B   7      -56.57   -140.01                                   
REMARK 500    ALA B 115     -132.87     48.60                                   
REMARK 500    ASN B 148     -125.48     36.02                                   
REMARK 500    SER B 200     -119.71     51.99                                   
REMARK 500    ASP B 294     -158.88   -163.12                                   
REMARK 500    GLU B 323      -86.35    -25.40                                   
REMARK 500    CYS B 417      -10.25     86.48                                   
REMARK 500    ILE B 438      -47.68   -132.47                                   
REMARK 500    ALA B 501       33.78    -84.57                                   
REMARK 500    TYR C   7      -58.85   -141.93                                   
REMARK 500    ALA C 115     -132.66     45.37                                   
REMARK 500    ASN C 148     -127.42     38.36                                   
REMARK 500    SER C 200     -117.28     54.75                                   
REMARK 500    LEU C 233       75.66   -118.89                                   
REMARK 500    ASP C 294     -152.62   -159.00                                   
REMARK 500    GLU C 323      -72.18    -39.82                                   
REMARK 500    ASN C 410       74.08     62.22                                   
REMARK 500    CYS C 417       -9.20     80.98                                   
REMARK 500    ILE C 438      -50.32   -133.70                                   
REMARK 500    TYR D   7      -58.25   -134.33                                   
REMARK 500    ALA D  58       12.92   -141.35                                   
REMARK 500    ALA D 115     -135.88     46.41                                   
REMARK 500    ASN D 148     -126.13     41.20                                   
REMARK 500    SER D 200     -119.48     54.60                                   
REMARK 500    ASP D 294     -148.93   -150.63                                   
REMARK 500    GLU D 323      -83.58    -33.53                                   
REMARK 500    PRO D 330       20.38    -70.50                                   
REMARK 500    ASN D 410       66.54     61.95                                   
REMARK 500    CYS D 417       -6.82     80.66                                   
REMARK 500    GLU D 437      -61.65     75.17                                   
REMARK 500    ALA D 501       44.29    -87.20                                   
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 PO4 A1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D1503                 
DBREF  5A2G A    1   414  UNP    D3AU79   D3AU79_9FIRM     1    414             
DBREF  5A2G A  415   522  PDB    5A2G     5A2G           415    522             
DBREF  5A2G B    1   414  UNP    D3AU79   D3AU79_9FIRM     1    414             
DBREF  5A2G B  415   522  PDB    5A2G     5A2G           415    522             
DBREF  5A2G C    1   414  UNP    D3AU79   D3AU79_9FIRM     1    414             
DBREF  5A2G C  415   522  PDB    5A2G     5A2G           415    522             
DBREF  5A2G D    1   414  UNP    D3AU79   D3AU79_9FIRM     1    414             
DBREF  5A2G D  415   522  PDB    5A2G     5A2G           415    522             
SEQRES   1 A  522  MET ALA LYS GLN PHE LEU TYR ASP ASN LEU PRO VAL VAL          
SEQRES   2 A  522  GLU THR LYS ALA GLY LYS LEU ARG GLY TYR GLN TRP GLU          
SEQRES   3 A  522  GLY THR TYR ILE PHE LYS GLY ILE ARG TYR ALA ARG ALA          
SEQRES   4 A  522  ASN ARG PHE GLN LEU PRO GLU GLU VAL GLU PRO TRP GLU          
SEQRES   5 A  522  GLY VAL LYS GLU ALA ALA SER TYR GLY PHE VAL CYS PRO          
SEQRES   6 A  522  MET LEU THR ARG ASP HIS PRO GLN GLY GLU LEU LEU VAL          
SEQRES   7 A  522  PRO HIS ARG TYR TRP PRO GLN ASP GLU ASP CYS LEU SER          
SEQRES   8 A  522  LEU ASN ILE TRP SER GLN SER LEU ASP ARG SER ALA LYS          
SEQRES   9 A  522  LYS PRO VAL MET PHE TRP ILE HIS GLY GLY ALA PHE SER          
SEQRES  10 A  522  MET GLY SER SER ILE GLU GLN LYS ALA TYR ASN GLY GLU          
SEQRES  11 A  522  ASN MET SER ARG TYR GLY ASP VAL VAL VAL VAL THR VAL          
SEQRES  12 A  522  ASN HIS ARG LEU ASN ILE LEU GLY TYR LEU ASP LEU SER          
SEQRES  13 A  522  PRO TYR GLY GLU ARG TYR ALA GLY SER ALA ASN ALA GLY          
SEQRES  14 A  522  GLN ALA ASP LEU VAL ALA ALA LEU LYS TRP VAL ARG ASP          
SEQRES  15 A  522  ASN ILE GLU ALA PHE GLY GLY ASP PRO ASP ASN VAL THR          
SEQRES  16 A  522  ILE PHE GLY GLN SER GLY GLY GLY MET LYS VAL SER GLY          
SEQRES  17 A  522  LEU MET GLN THR PRO GLU ALA ASP GLY LEU PHE HIS ARG          
SEQRES  18 A  522  ALA MET ILE MET SER GLY VAL ALA GLY ASP VAL LEU PRO          
SEQRES  19 A  522  TYR SER THR GLY ASP SER ARG PRO LEU ILE GLN ALA MET          
SEQRES  20 A  522  LEU LYS GLU LEU GLY LEU ALA GLU GLN GLU ALA GLY ARG          
SEQRES  21 A  522  LEU GLU THR VAL PRO TYR TYR ASP LEU ALA ALA ALA TYR          
SEQRES  22 A  522  ASN ARG VAL SER PRO ALA ILE ALA ARG ALA GLY GLY TYR          
SEQRES  23 A  522  ILE GLY CYS THR PRO ARG PRO ASP ASP PHE TYR LYS GLY          
SEQRES  24 A  522  GLU GLY PRO ALA VAL GLY PHE THR ASP HIS ALA LYS THR          
SEQRES  25 A  522  ILE PRO VAL MET VAL GLY THR VAL PHE GLY GLU PHE ALA          
SEQRES  26 A  522  MET MET PRO LEU PRO PHE ASN LYS GLU THR ILE SER GLU          
SEQRES  27 A  522  ALA GLU LEU ASP GLU ILE LEU ASP LYS ARG PHE GLN GLY          
SEQRES  28 A  522  HIS GLY LYS GLU LEU LYS THR VAL PHE ALA GLU ALA TYR          
SEQRES  29 A  522  PRO GLY LYS SER PRO VAL ASP LEU LEU THR LEU ASP THR          
SEQRES  30 A  522  ILE PHE ARG GLY PRO THR LYS GLU PHE VAL ARG SER LEU          
SEQRES  31 A  522  ALA ALA ALA GLY GLY SER VAL TYR SER TYR LEU PHE ALA          
SEQRES  32 A  522  LEU GLU PHE PRO TYR GLN ASN GLN LYS THR ALA TRP HIS          
SEQRES  33 A  522  CYS SER ASP ILE PRO PHE ILE PHE HIS ASN THR GLU LEU          
SEQRES  34 A  522  VAL PRO VAL THR ASN ILE PRO GLU ILE SER ASP LYS LEU          
SEQRES  35 A  522  GLU LYS GLN MET PHE ASP ALA VAL ILE HIS PHE VAL GLU          
SEQRES  36 A  522  THR GLY ASP PRO ASN HIS LEU GLY ILE PRO GLN TRP PRO          
SEQRES  37 A  522  VAL SER THR GLU ASP ARG GLU ALA THR MET ILE PHE ASP          
SEQRES  38 A  522  ARG VAL CYS THR VAL ARG PHE ASN PHE ASP ASP TYR LEU          
SEQRES  39 A  522  LEU GLU LEU TYR LYS LYS ALA LEU PRO ASN LEU THR LEU          
SEQRES  40 A  522  ALA ASN ILE THR GLN GLU ASP ASN GLN ILE GLN HIS ALA          
SEQRES  41 A  522  LEU GLU                                                      
SEQRES   1 B  522  MET ALA LYS GLN PHE LEU TYR ASP ASN LEU PRO VAL VAL          
SEQRES   2 B  522  GLU THR LYS ALA GLY LYS LEU ARG GLY TYR GLN TRP GLU          
SEQRES   3 B  522  GLY THR TYR ILE PHE LYS GLY ILE ARG TYR ALA ARG ALA          
SEQRES   4 B  522  ASN ARG PHE GLN LEU PRO GLU GLU VAL GLU PRO TRP GLU          
SEQRES   5 B  522  GLY VAL LYS GLU ALA ALA SER TYR GLY PHE VAL CYS PRO          
SEQRES   6 B  522  MET LEU THR ARG ASP HIS PRO GLN GLY GLU LEU LEU VAL          
SEQRES   7 B  522  PRO HIS ARG TYR TRP PRO GLN ASP GLU ASP CYS LEU SER          
SEQRES   8 B  522  LEU ASN ILE TRP SER GLN SER LEU ASP ARG SER ALA LYS          
SEQRES   9 B  522  LYS PRO VAL MET PHE TRP ILE HIS GLY GLY ALA PHE SER          
SEQRES  10 B  522  MET GLY SER SER ILE GLU GLN LYS ALA TYR ASN GLY GLU          
SEQRES  11 B  522  ASN MET SER ARG TYR GLY ASP VAL VAL VAL VAL THR VAL          
SEQRES  12 B  522  ASN HIS ARG LEU ASN ILE LEU GLY TYR LEU ASP LEU SER          
SEQRES  13 B  522  PRO TYR GLY GLU ARG TYR ALA GLY SER ALA ASN ALA GLY          
SEQRES  14 B  522  GLN ALA ASP LEU VAL ALA ALA LEU LYS TRP VAL ARG ASP          
SEQRES  15 B  522  ASN ILE GLU ALA PHE GLY GLY ASP PRO ASP ASN VAL THR          
SEQRES  16 B  522  ILE PHE GLY GLN SER GLY GLY GLY MET LYS VAL SER GLY          
SEQRES  17 B  522  LEU MET GLN THR PRO GLU ALA ASP GLY LEU PHE HIS ARG          
SEQRES  18 B  522  ALA MET ILE MET SER GLY VAL ALA GLY ASP VAL LEU PRO          
SEQRES  19 B  522  TYR SER THR GLY ASP SER ARG PRO LEU ILE GLN ALA MET          
SEQRES  20 B  522  LEU LYS GLU LEU GLY LEU ALA GLU GLN GLU ALA GLY ARG          
SEQRES  21 B  522  LEU GLU THR VAL PRO TYR TYR ASP LEU ALA ALA ALA TYR          
SEQRES  22 B  522  ASN ARG VAL SER PRO ALA ILE ALA ARG ALA GLY GLY TYR          
SEQRES  23 B  522  ILE GLY CYS THR PRO ARG PRO ASP ASP PHE TYR LYS GLY          
SEQRES  24 B  522  GLU GLY PRO ALA VAL GLY PHE THR ASP HIS ALA LYS THR          
SEQRES  25 B  522  ILE PRO VAL MET VAL GLY THR VAL PHE GLY GLU PHE ALA          
SEQRES  26 B  522  MET MET PRO LEU PRO PHE ASN LYS GLU THR ILE SER GLU          
SEQRES  27 B  522  ALA GLU LEU ASP GLU ILE LEU ASP LYS ARG PHE GLN GLY          
SEQRES  28 B  522  HIS GLY LYS GLU LEU LYS THR VAL PHE ALA GLU ALA TYR          
SEQRES  29 B  522  PRO GLY LYS SER PRO VAL ASP LEU LEU THR LEU ASP THR          
SEQRES  30 B  522  ILE PHE ARG GLY PRO THR LYS GLU PHE VAL ARG SER LEU          
SEQRES  31 B  522  ALA ALA ALA GLY GLY SER VAL TYR SER TYR LEU PHE ALA          
SEQRES  32 B  522  LEU GLU PHE PRO TYR GLN ASN GLN LYS THR ALA TRP HIS          
SEQRES  33 B  522  CYS SER ASP ILE PRO PHE ILE PHE HIS ASN THR GLU LEU          
SEQRES  34 B  522  VAL PRO VAL THR ASN ILE PRO GLU ILE SER ASP LYS LEU          
SEQRES  35 B  522  GLU LYS GLN MET PHE ASP ALA VAL ILE HIS PHE VAL GLU          
SEQRES  36 B  522  THR GLY ASP PRO ASN HIS LEU GLY ILE PRO GLN TRP PRO          
SEQRES  37 B  522  VAL SER THR GLU ASP ARG GLU ALA THR MET ILE PHE ASP          
SEQRES  38 B  522  ARG VAL CYS THR VAL ARG PHE ASN PHE ASP ASP TYR LEU          
SEQRES  39 B  522  LEU GLU LEU TYR LYS LYS ALA LEU PRO ASN LEU THR LEU          
SEQRES  40 B  522  ALA ASN ILE THR GLN GLU ASP ASN GLN ILE GLN HIS ALA          
SEQRES  41 B  522  LEU GLU                                                      
SEQRES   1 C  522  MET ALA LYS GLN PHE LEU TYR ASP ASN LEU PRO VAL VAL          
SEQRES   2 C  522  GLU THR LYS ALA GLY LYS LEU ARG GLY TYR GLN TRP GLU          
SEQRES   3 C  522  GLY THR TYR ILE PHE LYS GLY ILE ARG TYR ALA ARG ALA          
SEQRES   4 C  522  ASN ARG PHE GLN LEU PRO GLU GLU VAL GLU PRO TRP GLU          
SEQRES   5 C  522  GLY VAL LYS GLU ALA ALA SER TYR GLY PHE VAL CYS PRO          
SEQRES   6 C  522  MET LEU THR ARG ASP HIS PRO GLN GLY GLU LEU LEU VAL          
SEQRES   7 C  522  PRO HIS ARG TYR TRP PRO GLN ASP GLU ASP CYS LEU SER          
SEQRES   8 C  522  LEU ASN ILE TRP SER GLN SER LEU ASP ARG SER ALA LYS          
SEQRES   9 C  522  LYS PRO VAL MET PHE TRP ILE HIS GLY GLY ALA PHE SER          
SEQRES  10 C  522  MET GLY SER SER ILE GLU GLN LYS ALA TYR ASN GLY GLU          
SEQRES  11 C  522  ASN MET SER ARG TYR GLY ASP VAL VAL VAL VAL THR VAL          
SEQRES  12 C  522  ASN HIS ARG LEU ASN ILE LEU GLY TYR LEU ASP LEU SER          
SEQRES  13 C  522  PRO TYR GLY GLU ARG TYR ALA GLY SER ALA ASN ALA GLY          
SEQRES  14 C  522  GLN ALA ASP LEU VAL ALA ALA LEU LYS TRP VAL ARG ASP          
SEQRES  15 C  522  ASN ILE GLU ALA PHE GLY GLY ASP PRO ASP ASN VAL THR          
SEQRES  16 C  522  ILE PHE GLY GLN SER GLY GLY GLY MET LYS VAL SER GLY          
SEQRES  17 C  522  LEU MET GLN THR PRO GLU ALA ASP GLY LEU PHE HIS ARG          
SEQRES  18 C  522  ALA MET ILE MET SER GLY VAL ALA GLY ASP VAL LEU PRO          
SEQRES  19 C  522  TYR SER THR GLY ASP SER ARG PRO LEU ILE GLN ALA MET          
SEQRES  20 C  522  LEU LYS GLU LEU GLY LEU ALA GLU GLN GLU ALA GLY ARG          
SEQRES  21 C  522  LEU GLU THR VAL PRO TYR TYR ASP LEU ALA ALA ALA TYR          
SEQRES  22 C  522  ASN ARG VAL SER PRO ALA ILE ALA ARG ALA GLY GLY TYR          
SEQRES  23 C  522  ILE GLY CYS THR PRO ARG PRO ASP ASP PHE TYR LYS GLY          
SEQRES  24 C  522  GLU GLY PRO ALA VAL GLY PHE THR ASP HIS ALA LYS THR          
SEQRES  25 C  522  ILE PRO VAL MET VAL GLY THR VAL PHE GLY GLU PHE ALA          
SEQRES  26 C  522  MET MET PRO LEU PRO PHE ASN LYS GLU THR ILE SER GLU          
SEQRES  27 C  522  ALA GLU LEU ASP GLU ILE LEU ASP LYS ARG PHE GLN GLY          
SEQRES  28 C  522  HIS GLY LYS GLU LEU LYS THR VAL PHE ALA GLU ALA TYR          
SEQRES  29 C  522  PRO GLY LYS SER PRO VAL ASP LEU LEU THR LEU ASP THR          
SEQRES  30 C  522  ILE PHE ARG GLY PRO THR LYS GLU PHE VAL ARG SER LEU          
SEQRES  31 C  522  ALA ALA ALA GLY GLY SER VAL TYR SER TYR LEU PHE ALA          
SEQRES  32 C  522  LEU GLU PHE PRO TYR GLN ASN GLN LYS THR ALA TRP HIS          
SEQRES  33 C  522  CYS SER ASP ILE PRO PHE ILE PHE HIS ASN THR GLU LEU          
SEQRES  34 C  522  VAL PRO VAL THR ASN ILE PRO GLU ILE SER ASP LYS LEU          
SEQRES  35 C  522  GLU LYS GLN MET PHE ASP ALA VAL ILE HIS PHE VAL GLU          
SEQRES  36 C  522  THR GLY ASP PRO ASN HIS LEU GLY ILE PRO GLN TRP PRO          
SEQRES  37 C  522  VAL SER THR GLU ASP ARG GLU ALA THR MET ILE PHE ASP          
SEQRES  38 C  522  ARG VAL CYS THR VAL ARG PHE ASN PHE ASP ASP TYR LEU          
SEQRES  39 C  522  LEU GLU LEU TYR LYS LYS ALA LEU PRO ASN LEU THR LEU          
SEQRES  40 C  522  ALA ASN ILE THR GLN GLU ASP ASN GLN ILE GLN HIS ALA          
SEQRES  41 C  522  LEU GLU                                                      
SEQRES   1 D  522  MET ALA LYS GLN PHE LEU TYR ASP ASN LEU PRO VAL VAL          
SEQRES   2 D  522  GLU THR LYS ALA GLY LYS LEU ARG GLY TYR GLN TRP GLU          
SEQRES   3 D  522  GLY THR TYR ILE PHE LYS GLY ILE ARG TYR ALA ARG ALA          
SEQRES   4 D  522  ASN ARG PHE GLN LEU PRO GLU GLU VAL GLU PRO TRP GLU          
SEQRES   5 D  522  GLY VAL LYS GLU ALA ALA SER TYR GLY PHE VAL CYS PRO          
SEQRES   6 D  522  MET LEU THR ARG ASP HIS PRO GLN GLY GLU LEU LEU VAL          
SEQRES   7 D  522  PRO HIS ARG TYR TRP PRO GLN ASP GLU ASP CYS LEU SER          
SEQRES   8 D  522  LEU ASN ILE TRP SER GLN SER LEU ASP ARG SER ALA LYS          
SEQRES   9 D  522  LYS PRO VAL MET PHE TRP ILE HIS GLY GLY ALA PHE SER          
SEQRES  10 D  522  MET GLY SER SER ILE GLU GLN LYS ALA TYR ASN GLY GLU          
SEQRES  11 D  522  ASN MET SER ARG TYR GLY ASP VAL VAL VAL VAL THR VAL          
SEQRES  12 D  522  ASN HIS ARG LEU ASN ILE LEU GLY TYR LEU ASP LEU SER          
SEQRES  13 D  522  PRO TYR GLY GLU ARG TYR ALA GLY SER ALA ASN ALA GLY          
SEQRES  14 D  522  GLN ALA ASP LEU VAL ALA ALA LEU LYS TRP VAL ARG ASP          
SEQRES  15 D  522  ASN ILE GLU ALA PHE GLY GLY ASP PRO ASP ASN VAL THR          
SEQRES  16 D  522  ILE PHE GLY GLN SER GLY GLY GLY MET LYS VAL SER GLY          
SEQRES  17 D  522  LEU MET GLN THR PRO GLU ALA ASP GLY LEU PHE HIS ARG          
SEQRES  18 D  522  ALA MET ILE MET SER GLY VAL ALA GLY ASP VAL LEU PRO          
SEQRES  19 D  522  TYR SER THR GLY ASP SER ARG PRO LEU ILE GLN ALA MET          
SEQRES  20 D  522  LEU LYS GLU LEU GLY LEU ALA GLU GLN GLU ALA GLY ARG          
SEQRES  21 D  522  LEU GLU THR VAL PRO TYR TYR ASP LEU ALA ALA ALA TYR          
SEQRES  22 D  522  ASN ARG VAL SER PRO ALA ILE ALA ARG ALA GLY GLY TYR          
SEQRES  23 D  522  ILE GLY CYS THR PRO ARG PRO ASP ASP PHE TYR LYS GLY          
SEQRES  24 D  522  GLU GLY PRO ALA VAL GLY PHE THR ASP HIS ALA LYS THR          
SEQRES  25 D  522  ILE PRO VAL MET VAL GLY THR VAL PHE GLY GLU PHE ALA          
SEQRES  26 D  522  MET MET PRO LEU PRO PHE ASN LYS GLU THR ILE SER GLU          
SEQRES  27 D  522  ALA GLU LEU ASP GLU ILE LEU ASP LYS ARG PHE GLN GLY          
SEQRES  28 D  522  HIS GLY LYS GLU LEU LYS THR VAL PHE ALA GLU ALA TYR          
SEQRES  29 D  522  PRO GLY LYS SER PRO VAL ASP LEU LEU THR LEU ASP THR          
SEQRES  30 D  522  ILE PHE ARG GLY PRO THR LYS GLU PHE VAL ARG SER LEU          
SEQRES  31 D  522  ALA ALA ALA GLY GLY SER VAL TYR SER TYR LEU PHE ALA          
SEQRES  32 D  522  LEU GLU PHE PRO TYR GLN ASN GLN LYS THR ALA TRP HIS          
SEQRES  33 D  522  CYS SER ASP ILE PRO PHE ILE PHE HIS ASN THR GLU LEU          
SEQRES  34 D  522  VAL PRO VAL THR ASN ILE PRO GLU ILE SER ASP LYS LEU          
SEQRES  35 D  522  GLU LYS GLN MET PHE ASP ALA VAL ILE HIS PHE VAL GLU          
SEQRES  36 D  522  THR GLY ASP PRO ASN HIS LEU GLY ILE PRO GLN TRP PRO          
SEQRES  37 D  522  VAL SER THR GLU ASP ARG GLU ALA THR MET ILE PHE ASP          
SEQRES  38 D  522  ARG VAL CYS THR VAL ARG PHE ASN PHE ASP ASP TYR LEU          
SEQRES  39 D  522  LEU GLU LEU TYR LYS LYS ALA LEU PRO ASN LEU THR LEU          
SEQRES  40 D  522  ALA ASN ILE THR GLN GLU ASP ASN GLN ILE GLN HIS ALA          
SEQRES  41 D  522  LEU GLU                                                      
HET    PO4  A1503       5                                                       
HET    PO4  B1503       5                                                       
HET    PO4  C1503       5                                                       
HET    PO4  D1503       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   5  PO4    4(O4 P 3-)                                                   
FORMUL   9  HOH   *1592(H2 O)                                                   
HELIX    1   1 LYS A  125  ASN A  128  5                                   4    
HELIX    2   2 GLY A  129  ASP A  137  1                                   9    
HELIX    3   3 LEU A  147  TYR A  152  1                                   6    
HELIX    4   4 LEU A  155  GLY A  159  5                                   5    
HELIX    5   5 GLY A  159  ALA A  163  5                                   5    
HELIX    6   6 GLY A  164  ALA A  166  5                                   3    
HELIX    7   7 ASN A  167  ILE A  184  1                                  18    
HELIX    8   8 GLU A  185  PHE A  187  5                                   3    
HELIX    9   9 SER A  200  GLN A  211  1                                  12    
HELIX   10  10 THR A  212  ASP A  216  5                                   5    
HELIX   11  11 ALA A  229  LEU A  233  5                                   5    
HELIX   12  12 SER A  240  LEU A  251  1                                  12    
HELIX   13  13 ALA A  254  THR A  263  5                                  10    
HELIX   14  14 PRO A  265  ALA A  283  1                                  19    
HELIX   15  15 GLU A  300  GLY A  305  1                                   6    
HELIX   16  16 HIS A  309  ILE A  313  5                                   5    
HELIX   17  17 SER A  337  PHE A  349  1                                  13    
HELIX   18  18 HIS A  352  TYR A  364  1                                  13    
HELIX   19  19 SER A  368  THR A  374  5                                   7    
HELIX   20  20 PHE A  379  ALA A  393  1                                  15    
HELIX   21  21 ASP A  419  PHE A  424  1                                   6    
HELIX   22  22 ASN A  426  VAL A  430  5                                   5    
HELIX   23  23 VAL A  430  ASN A  434  5                                   5    
HELIX   24  24 ILE A  438  GLY A  457  1                                  20    
HELIX   25  25 ASP A  491  LEU A  502  1                                  12    
HELIX   26  26 LYS B  125  ASN B  128  5                                   4    
HELIX   27  27 GLY B  129  ASP B  137  1                                   9    
HELIX   28  28 LEU B  147  TYR B  152  1                                   6    
HELIX   29  29 LEU B  155  GLY B  159  5                                   5    
HELIX   30  30 GLY B  164  ALA B  166  5                                   3    
HELIX   31  31 ASN B  167  ILE B  184  1                                  18    
HELIX   32  32 GLU B  185  PHE B  187  5                                   3    
HELIX   33  33 SER B  200  GLN B  211  1                                  12    
HELIX   34  34 THR B  212  ASP B  216  5                                   5    
HELIX   35  35 ALA B  229  LEU B  233  5                                   5    
HELIX   36  36 SER B  240  LEU B  251  1                                  12    
HELIX   37  37 GLU B  257  THR B  263  5                                   7    
HELIX   38  38 PRO B  265  ALA B  283  1                                  19    
HELIX   39  39 GLU B  300  GLY B  305  1                                   6    
HELIX   40  40 HIS B  309  ILE B  313  5                                   5    
HELIX   41  41 SER B  337  PHE B  349  1                                  13    
HELIX   42  42 HIS B  352  TYR B  364  1                                  13    
HELIX   43  43 SER B  368  THR B  374  5                                   7    
HELIX   44  44 PHE B  379  ALA B  393  1                                  15    
HELIX   45  45 ASP B  419  PHE B  424  1                                   6    
HELIX   46  46 ASN B  426  VAL B  430  5                                   5    
HELIX   47  47 VAL B  430  ASN B  434  5                                   5    
HELIX   48  48 ILE B  438  GLY B  457  1                                  20    
HELIX   49  49 ASP B  491  ALA B  501  1                                  11    
HELIX   50  50 LYS C  125  ASN C  128  5                                   4    
HELIX   51  51 GLY C  129  ASP C  137  1                                   9    
HELIX   52  52 LEU C  147  TYR C  152  1                                   6    
HELIX   53  53 LEU C  155  GLY C  159  5                                   5    
HELIX   54  54 GLY C  159  ALA C  163  5                                   5    
HELIX   55  55 GLY C  164  ALA C  166  5                                   3    
HELIX   56  56 ASN C  167  ILE C  184  1                                  18    
HELIX   57  57 GLU C  185  PHE C  187  5                                   3    
HELIX   58  58 SER C  200  GLN C  211  1                                  12    
HELIX   59  59 THR C  212  ASP C  216  5                                   5    
HELIX   60  60 ALA C  229  LEU C  233  5                                   5    
HELIX   61  61 SER C  240  LEU C  251  1                                  12    
HELIX   62  62 ALA C  254  THR C  263  5                                  10    
HELIX   63  63 PRO C  265  ALA C  283  1                                  19    
HELIX   64  64 GLU C  300  GLY C  305  1                                   6    
HELIX   65  65 HIS C  309  ILE C  313  5                                   5    
HELIX   66  66 SER C  337  PHE C  349  1                                  13    
HELIX   67  67 HIS C  352  TYR C  364  1                                  13    
HELIX   68  68 SER C  368  THR C  374  5                                   7    
HELIX   69  69 PHE C  379  ALA C  393  1                                  15    
HELIX   70  70 ASP C  419  PHE C  424  1                                   6    
HELIX   71  71 ASN C  426  VAL C  430  5                                   5    
HELIX   72  72 VAL C  430  ASN C  434  5                                   5    
HELIX   73  73 ILE C  438  GLY C  457  1                                  20    
HELIX   74  74 ASP C  491  LEU C  502  1                                  12    
HELIX   75  75 LYS D  125  ASN D  128  5                                   4    
HELIX   76  76 GLY D  129  ASP D  137  1                                   9    
HELIX   77  77 LEU D  147  TYR D  152  1                                   6    
HELIX   78  78 GLY D  164  ALA D  166  5                                   3    
HELIX   79  79 ASN D  167  ILE D  184  1                                  18    
HELIX   80  80 GLU D  185  PHE D  187  5                                   3    
HELIX   81  81 SER D  200  GLN D  211  1                                  12    
HELIX   82  82 THR D  212  ASP D  216  5                                   5    
HELIX   83  83 ALA D  229  LEU D  233  5                                   5    
HELIX   84  84 SER D  240  LEU D  251  1                                  12    
HELIX   85  85 GLU D  257  THR D  263  5                                   7    
HELIX   86  86 PRO D  265  ALA D  283  1                                  19    
HELIX   87  87 GLU D  300  GLY D  305  1                                   6    
HELIX   88  88 THR D  307  THR D  312  1                                   6    
HELIX   89  89 SER D  337  PHE D  349  1                                  13    
HELIX   90  90 HIS D  352  TYR D  364  1                                  13    
HELIX   91  91 SER D  368  THR D  374  5                                   7    
HELIX   92  92 PHE D  379  ALA D  393  1                                  15    
HELIX   93  93 ASP D  419  PHE D  424  1                                   6    
HELIX   94  94 ASN D  426  VAL D  430  5                                   5    
HELIX   95  95 VAL D  430  ASN D  434  5                                   5    
HELIX   96  96 GLU D  437  GLY D  457  1                                  21    
HELIX   97  97 ASP D  491  ALA D  501  1                                  11    
SHEET    1  AA12 PHE A   5  LEU A   6  0                                        
SHEET    2  AA12 TYR A  23  TRP A  25 -1  O  GLN A  24   N  LEU A   6           
SHEET    3  AA12 THR A  28  ARG A  35 -1  O  THR A  28   N  TRP A  25           
SHEET    4  AA12 SER A  91  SER A  96 -1  O  LEU A  92   N  ILE A  34           
SHEET    5  AA12 VAL A 139  VAL A 143 -1  O  VAL A 140   N  TRP A  95           
SHEET    6  AA12 LYS A 105  ILE A 111  1  O  PRO A 106   N  VAL A 139           
SHEET    7  AA12 GLY A 189  GLN A 199  1  N  ASP A 190   O  LYS A 105           
SHEET    8  AA12 ARG A 221  MET A 225  1  O  ARG A 221   N  ILE A 196           
SHEET    9  AA12 VAL A 315  VAL A 320  1  O  MET A 316   N  ILE A 224           
SHEET   10  AA12 VAL A 397  PHE A 402  1  O  TYR A 398   N  VAL A 317           
SHEET   11  AA12 ALA A 476  PHE A 480  1  O  ALA A 476   N  SER A 399           
SHEET   12  AA12 THR A 485  PHE A 488 -1  O  THR A 485   N  ILE A 479           
SHEET    1  AB 3 VAL A  13  GLU A  14  0                                        
SHEET    2  AB 3 LYS A  19  ARG A  21 -1  O  LEU A  20   N  VAL A  13           
SHEET    3  AB 3 VAL A  54  GLU A  56  1  O  LYS A  55   N  ARG A  21           
SHEET    1  BA12 PHE B   5  LEU B   6  0                                        
SHEET    2  BA12 TYR B  23  TRP B  25 -1  O  GLN B  24   N  LEU B   6           
SHEET    3  BA12 THR B  28  ARG B  35 -1  O  THR B  28   N  TRP B  25           
SHEET    4  BA12 SER B  91  SER B  96 -1  O  LEU B  92   N  ILE B  34           
SHEET    5  BA12 VAL B 139  VAL B 143 -1  O  VAL B 140   N  TRP B  95           
SHEET    6  BA12 LYS B 105  ILE B 111  1  O  PRO B 106   N  VAL B 139           
SHEET    7  BA12 GLY B 189  GLN B 199  1  N  ASP B 190   O  LYS B 105           
SHEET    8  BA12 ARG B 221  MET B 225  1  O  ARG B 221   N  ILE B 196           
SHEET    9  BA12 VAL B 315  VAL B 320  1  O  MET B 316   N  ILE B 224           
SHEET   10  BA12 VAL B 397  PHE B 402  1  O  TYR B 398   N  VAL B 317           
SHEET   11  BA12 ALA B 476  PHE B 480  1  O  ALA B 476   N  SER B 399           
SHEET   12  BA12 THR B 485  PHE B 488 -1  O  THR B 485   N  ILE B 479           
SHEET    1  BB 3 VAL B  13  THR B  15  0                                        
SHEET    2  BB 3 GLY B  18  ARG B  21 -1  O  GLY B  18   N  THR B  15           
SHEET    3  BB 3 VAL B  54  GLU B  56  1  O  LYS B  55   N  ARG B  21           
SHEET    1  BC 2 GLU B 405  PHE B 406  0                                        
SHEET    2  BC 2 LYS B 412  THR B 413 -1  O  LYS B 412   N  PHE B 406           
SHEET    1  CA12 PHE C   5  LEU C   6  0                                        
SHEET    2  CA12 TYR C  23  TRP C  25 -1  O  GLN C  24   N  LEU C   6           
SHEET    3  CA12 THR C  28  ARG C  35 -1  O  THR C  28   N  TRP C  25           
SHEET    4  CA12 SER C  91  SER C  96 -1  O  LEU C  92   N  ILE C  34           
SHEET    5  CA12 VAL C 139  VAL C 143 -1  O  VAL C 140   N  TRP C  95           
SHEET    6  CA12 LYS C 105  ILE C 111  1  O  PRO C 106   N  VAL C 139           
SHEET    7  CA12 GLY C 189  GLN C 199  1  N  ASP C 190   O  LYS C 105           
SHEET    8  CA12 ARG C 221  MET C 225  1  O  ARG C 221   N  ILE C 196           
SHEET    9  CA12 VAL C 315  VAL C 320  1  O  MET C 316   N  ILE C 224           
SHEET   10  CA12 VAL C 397  PHE C 402  1  O  TYR C 398   N  VAL C 317           
SHEET   11  CA12 ALA C 476  PHE C 480  1  O  ALA C 476   N  SER C 399           
SHEET   12  CA12 THR C 485  PHE C 488 -1  O  THR C 485   N  ILE C 479           
SHEET    1  CB 3 VAL C  13  GLU C  14  0                                        
SHEET    2  CB 3 LYS C  19  ARG C  21 -1  O  LEU C  20   N  VAL C  13           
SHEET    3  CB 3 VAL C  54  GLU C  56  1  O  LYS C  55   N  ARG C  21           
SHEET    1  CC 2 GLU C 405  PHE C 406  0                                        
SHEET    2  CC 2 LYS C 412  THR C 413 -1  O  LYS C 412   N  PHE C 406           
SHEET    1  DA12 PHE D   5  LEU D   6  0                                        
SHEET    2  DA12 TYR D  23  TRP D  25 -1  O  GLN D  24   N  LEU D   6           
SHEET    3  DA12 THR D  28  ARG D  35 -1  O  THR D  28   N  TRP D  25           
SHEET    4  DA12 SER D  91  SER D  96 -1  O  LEU D  92   N  ILE D  34           
SHEET    5  DA12 VAL D 139  VAL D 143 -1  O  VAL D 140   N  TRP D  95           
SHEET    6  DA12 LYS D 105  ILE D 111  1  O  PRO D 106   N  VAL D 139           
SHEET    7  DA12 GLY D 189  GLN D 199  1  N  ASP D 190   O  LYS D 105           
SHEET    8  DA12 ARG D 221  MET D 225  1  O  ARG D 221   N  ILE D 196           
SHEET    9  DA12 VAL D 315  VAL D 320  1  O  MET D 316   N  ILE D 224           
SHEET   10  DA12 VAL D 397  PHE D 402  1  O  TYR D 398   N  VAL D 317           
SHEET   11  DA12 ALA D 476  PHE D 480  1  O  ALA D 476   N  SER D 399           
SHEET   12  DA12 THR D 485  PHE D 488 -1  O  THR D 485   N  ILE D 479           
SHEET    1  DB 3 VAL D  13  GLU D  14  0                                        
SHEET    2  DB 3 LYS D  19  ARG D  21 -1  O  LEU D  20   N  VAL D  13           
SHEET    3  DB 3 VAL D  54  GLU D  56  1  O  LYS D  55   N  ARG D  21           
SHEET    1  DC 2 GLU D 405  PHE D 406  0                                        
SHEET    2  DC 2 LYS D 412  THR D 413 -1  O  LYS D 412   N  PHE D 406           
SITE     1 AC1 11 LYS A  32  TYR A  60  ARG A  81  ASN A 128                    
SITE     2 AC1 11 HOH A2026  HOH A2042  HOH A2131  HOH A2148                    
SITE     3 AC1 11 HOH A2189  LYS B 125  HOH B3460                               
SITE     1 AC2 11 LYS A 125  HOH A2183  LYS B  32  TYR B  60                    
SITE     2 AC2 11 ARG B  81  ASN B 128  HOH B2027  HOH B2041                    
SITE     3 AC2 11 HOH B2114  HOH B2144  HOH B3330                               
SITE     1 AC3 10 LYS C  32  TYR C  60  ARG C  81  ASN C 128                    
SITE     2 AC3 10 HOH C2036  HOH C2054  HOH C2137  HOH C2152                    
SITE     3 AC3 10 HOH C2191  LYS D 125                                          
SITE     1 AC4 11 LYS C 125  LYS D  32  TYR D  60  ARG D  81                    
SITE     2 AC4 11 ASN D 128  HOH D2027  HOH D2045  HOH D2119                    
SITE     3 AC4 11 HOH D2133  HOH D2168  HOH D2169                               
CRYST1   62.050  241.830   83.580  90.00  90.00  90.00 P 1 21 1      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      0.016116  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004135  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011965        0.00000                         
TER    3941      LEU A 502                                                      
TER    7882      LEU B 502                                                      
TER   11823      LEU C 502                                                      
TER   15764      LEU D 502                                                      
MASTER      414    0    4   97   66    0   12    617372    4   20  164          
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