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LongText Report for: 5frd-pdb

Name Class
5frd-pdb
HEADER    HYDROLASE                               17-DEC-15   5FRD              
TITLE     STRUCTURE OF A THERMOPHILIC ESTERASE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXYLESTERASE (EST-2);                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ESTERASE;                                                   
COMPND   5 EC: 3.1.1.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;                         
SOURCE   3 ORGANISM_TAXID: 2234;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: CODONPLUS-RIPL;                           
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET28                                      
KEYWDS    HYDROLASE, ESTERASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.SAYER,W.FINNIGAN,M.N.ISUPOV,M.LEVISSON,S.W.M.KENGEN,J.VAN DER OOST, 
AUTHOR   2 N.HARMER,J.A.LITTLECHILD                                             
REVDAT   1   25-MAY-16 5FRD    0                                                
JRNL        AUTH   C.SAYER,W.FINNIGAN,M.N.ISUPOV,M.LEVISSON,S.W.KENGEN,         
JRNL        AUTH 2 J.VAN DER OOST,N.J.HARMER,J.A.LITTLECHILD                    
JRNL        TITL   STRUCTURAL AND BIOCHEMICAL CHARACTERISATION OF               
JRNL        TITL 2 ARCHAEOGLOBUS FULGIDUS ESTERASE REVEALS A BOUND COA          
JRNL        TITL 3 MOLECULE IN THE VICINITY OF THE ACTIVE SITE.                 
JRNL        REF    SCI.REP.                      V.   6 25542 2016              
JRNL        REFN                   ISSN 2045-2322                               
JRNL        PMID   27160974                                                     
JRNL        DOI    10.1038/SREP25542                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0131                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.77                          
REMARK   3   NUMBER OF REFLECTIONS             : 100085                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.15686                         
REMARK   3   R VALUE            (WORKING SET) : 0.15649                         
REMARK   3   FREE R VALUE                     : 0.17347                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2013                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.400                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.437                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6538                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.86                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.308                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 125                          
REMARK   3   BIN FREE R VALUE                    : 0.354                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4704                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 128                                     
REMARK   3   SOLVENT ATOMS            : 514                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.568                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.59                                                 
REMARK   3    B22 (A**2) : 0.41                                                 
REMARK   3    B33 (A**2) : -0.99                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.058         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.057         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.043         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.107         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.976                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.970                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5024 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5109 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6935 ; 1.631 ; 2.019       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11981 ; 1.394 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   716 ; 5.236 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   237 ;37.053 ;24.473       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1048 ;14.495 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;13.126 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   776 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5701 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1091 ; 0.006 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2287 ; 3.612 ; 7.640       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2286 ; 3.589 ; 7.635       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2915 ; 4.658 ;11.434       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2737 ; 7.484 ;10.332       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 5FRD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-65800.                                       
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        : 1                                  
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) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 102188                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.30                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 5.6                                
REMARK 200  R MERGE                    (I) : 0.04                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.46                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1A8Q                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.4                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.53500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.28500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.60000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.28500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.53500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.60000            
REMARK 290   SMTRY3   4  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     HIS A   257                                                      
REMARK 465     HIS A   258                                                      
REMARK 465     HIS A   259                                                      
REMARK 465     HIS A   260                                                      
REMARK 465     GLU B   253                                                      
REMARK 465     VAL B   254                                                      
REMARK 465     HIS B   255                                                      
REMARK 465     HIS B   256                                                      
REMARK 465     HIS B   257                                                      
REMARK 465     HIS B   258                                                      
REMARK 465     HIS B   259                                                      
REMARK 465     HIS B   260                                                      
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   OD2B ASP A     8     O    HOH A  2025              1.95            
REMARK 500   CD B ARG A    20     O    HOH A  2042              1.80            
REMARK 500   NE B ARG A    20     O    HOH A  2042              1.25            
REMARK 500   CZ B ARG A    20     O    HOH A  2042              0.94            
REMARK 500   NH1B ARG A    20     O    HOH A  2042              1.15            
REMARK 500   OE2A GLU A    21     O    HOH A  2046              2.13            
REMARK 500   CD C GLU A    21     O    HOH A  2037              1.96            
REMARK 500   OE2C GLU A    21     O    HOH A  2037              1.33            
REMARK 500   CD A ARG A   101     O    HOH A  2110              1.88            
REMARK 500   NE A ARG A   101     O    HOH A  2110              1.25            
REMARK 500   CZ A ARG A   101     O    HOH A  2110              1.67            
REMARK 500   CD A GLU A   149     O    HOH A  2172              2.08            
REMARK 500   OE1A GLU A   149     O    HOH A  2172              1.76            
REMARK 500   OE2A GLU A   149     O    HOH A  2172              1.94            
REMARK 500   CD B GLU A   150     O    HOH A  2170              2.05            
REMARK 500   OE1B GLU A   150     O    HOH A  2170              1.12            
REMARK 500   NZ B LYS A   154     O    HOH A  2064              1.07            
REMARK 500   CD B GLU A   219     O    HOH A  2238              1.63            
REMARK 500   OE2B GLU A   219     O    HOH A  2238              0.78            
REMARK 500   OE2A GLU A   243     O    HOH A  2050              1.74            
REMARK 500   CD B GLU A   243     O    HOH A  2082              1.99            
REMARK 500   CD B GLU A   243     O    HOH A  2250              1.85            
REMARK 500   OE1B GLU A   243     O    HOH A  2250              0.81            
REMARK 500   OE2B GLU A   243     O    HOH A  2082              1.36            
REMARK 500   CZ A ARG B    20     O    HOH B  2022              1.92            
REMARK 500   NH1A ARG B    20     O    HOH B  2022              0.93            
REMARK 500   NZ B LYS B    23     O    HOH B  2031              0.95            
REMARK 500   CD B GLU B    61     O    HOH B  2064              2.16            
REMARK 500   OE1B GLU B    61     O    HOH B  2064              1.17            
REMARK 500   ND2B ASN B    63     O    HOH B  2069              1.98            
REMARK 500   OE2B GLU B    67     O    HOH B  2065              1.62            
REMARK 500   CD A ARG B   101     O    HOH B  2074              1.85            
REMARK 500   NE A ARG B   101     O    HOH B  2074              1.25            
REMARK 500   CZ A ARG B   101     O    HOH B  2074              1.95            
REMARK 500   CD B GLU B   104     O    HOH B  2095              1.66            
REMARK 500   OE2B GLU B   104     O    HOH B  2095              0.47            
REMARK 500   OE2A GLU B   126     O    HOH B  2116              1.79            
REMARK 500   OE1A GLU B   131     O    HOH B  2123              2.04            
REMARK 500   OE2B GLU B   131     O    HOH B  2108              2.14            
REMARK 500   OE1B GLU B   152     O    HOH B  2149              1.63            
REMARK 500   CD A ARG B   156     O    HOH B  2160              1.50            
REMARK 500   CE B LYS B   201     O    HOH B  2201              2.04            
REMARK 500   NZ B LYS B   201     O    HOH B  2201              1.00            
REMARK 500   OE2A GLU B   219     O    HOH B  2190              1.25            
REMARK 500   OE2A GLU B   240     O    HOH B  2228              1.80            
REMARK 500   CD B GLU B   243     O    HOH B  2225              1.78            
REMARK 500   OE1B GLU B   243     O    HOH B  2225              1.63            
REMARK 500   OE2B GLU B   243     O    HOH B  2225              1.96            
REMARK 500   O    HOH A  2017     O    HOH A  2032              2.18            
REMARK 500   O    HOH A  2032     O    HOH A  2033              1.70            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      56 CLOSE CONTACTS                                
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   NH2B ARG A   182     OE2B GLU B    61     3545     2.18            
REMARK 500   OE1A GLU B   126     OE2B GLU B   237     3455     1.66            
REMARK 500   OE1B GLU B   126     OE1B GLU B   237     3455     1.71            
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  32     -164.69   -116.98                                   
REMARK 500    SER A  89     -117.16     56.10                                   
REMARK 500    SER A 227     -141.22   -112.69                                   
REMARK 500    MET A 229       44.53    -89.02                                   
REMARK 500    SER B  32     -165.24   -114.64                                   
REMARK 500    ASN B  53       -0.84     80.52                                   
REMARK 500    SER B  89     -117.20     57.29                                   
REMARK 500    ASN B 217       28.65    -68.69                                   
REMARK 500    SER B 227     -140.59   -107.99                                   
REMARK 500    MET B 229       48.73    -89.47                                   
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 PGE B1253                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC B1254                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA B1255                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A1257                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1256                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1258                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1257                 
DBREF  5FRD A    1   256  UNP    O28735   O28735_ARCFU     1    256             
DBREF  5FRD B    1   252  UNP    O28735   O28735_ARCFU     1    252             
SEQADV 5FRD HIS A  257  UNP  O28735              EXPRESSION TAG                 
SEQADV 5FRD HIS A  258  UNP  O28735              EXPRESSION TAG                 
SEQADV 5FRD HIS A  259  UNP  O28735              EXPRESSION TAG                 
SEQADV 5FRD HIS A  260  UNP  O28735              EXPRESSION TAG                 
SEQADV 5FRD GLU B  253  UNP  O28735              EXPRESSION TAG                 
SEQADV 5FRD VAL B  254  UNP  O28735              EXPRESSION TAG                 
SEQADV 5FRD HIS B  255  UNP  O28735              EXPRESSION TAG                 
SEQADV 5FRD HIS B  256  UNP  O28735              EXPRESSION TAG                 
SEQADV 5FRD HIS B  257  UNP  O28735              EXPRESSION TAG                 
SEQADV 5FRD HIS B  258  UNP  O28735              EXPRESSION TAG                 
SEQADV 5FRD HIS B  259  UNP  O28735              EXPRESSION TAG                 
SEQADV 5FRD HIS B  260  UNP  O28735              EXPRESSION TAG                 
SEQRES   1 A  260  MET LEU GLU ARG VAL PHE ILE ASP VAL ASP GLY VAL LYS          
SEQRES   2 A  260  VAL SER LEU LEU LYS GLY ARG GLU ARG LYS VAL PHE TYR          
SEQRES   3 A  260  ILE HIS SER SER GLY SER ASP ALA THR GLN TRP VAL ASN          
SEQRES   4 A  260  GLN LEU THR ALA ILE GLY GLY TYR ALA ILE ASP LEU PRO          
SEQRES   5 A  260  ASN HIS GLY GLN SER ASP THR VAL GLU VAL ASN SER VAL          
SEQRES   6 A  260  ASP GLU TYR ALA TYR TYR ALA SER GLU SER LEU LYS LYS          
SEQRES   7 A  260  THR VAL GLY LYS ALA VAL VAL VAL GLY HIS SER LEU GLY          
SEQRES   8 A  260  GLY ALA VAL ALA GLN LYS LEU TYR LEU ARG ASN PRO GLU          
SEQRES   9 A  260  ILE CYS LEU ALA LEU VAL LEU VAL GLY THR GLY ALA ARG          
SEQRES  10 A  260  LEU ARG VAL LEU PRO GLU ILE LEU GLU GLY LEU LYS LYS          
SEQRES  11 A  260  GLU PRO GLU LYS ALA VAL ASP LEU MET LEU SER MET ALA          
SEQRES  12 A  260  PHE ALA SER LYS GLY GLU GLU TYR GLU LYS LYS ARG ARG          
SEQRES  13 A  260  GLU PHE LEU ASP ARG VAL ASP VAL LEU HIS LEU ASP LEU          
SEQRES  14 A  260  SER LEU CYS ASP ARG PHE ASP LEU LEU GLU ASP TYR ARG          
SEQRES  15 A  260  ASN GLY LYS LEU LYS ILE GLY VAL PRO THR LEU VAL ILE          
SEQRES  16 A  260  VAL GLY GLU GLU ASP LYS LEU THR PRO LEU LYS TYR HIS          
SEQRES  17 A  260  GLU PHE PHE HIS LYS HIS ILE PRO ASN SER GLU LEU VAL          
SEQRES  18 A  260  VAL ILE PRO GLY ALA SER HIS MET VAL MET LEU GLU LYS          
SEQRES  19 A  260  HIS VAL GLU PHE ASN GLU ALA LEU GLU LYS PHE LEU LYS          
SEQRES  20 A  260  LYS VAL GLY VAL ALA GLU VAL HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  260  MET LEU GLU ARG VAL PHE ILE ASP VAL ASP GLY VAL LYS          
SEQRES   2 B  260  VAL SER LEU LEU LYS GLY ARG GLU ARG LYS VAL PHE TYR          
SEQRES   3 B  260  ILE HIS SER SER GLY SER ASP ALA THR GLN TRP VAL ASN          
SEQRES   4 B  260  GLN LEU THR ALA ILE GLY GLY TYR ALA ILE ASP LEU PRO          
SEQRES   5 B  260  ASN HIS GLY GLN SER ASP THR VAL GLU VAL ASN SER VAL          
SEQRES   6 B  260  ASP GLU TYR ALA TYR TYR ALA SER GLU SER LEU LYS LYS          
SEQRES   7 B  260  THR VAL GLY LYS ALA VAL VAL VAL GLY HIS SER LEU GLY          
SEQRES   8 B  260  GLY ALA VAL ALA GLN LYS LEU TYR LEU ARG ASN PRO GLU          
SEQRES   9 B  260  ILE CYS LEU ALA LEU VAL LEU VAL GLY THR GLY ALA ARG          
SEQRES  10 B  260  LEU ARG VAL LEU PRO GLU ILE LEU GLU GLY LEU LYS LYS          
SEQRES  11 B  260  GLU PRO GLU LYS ALA VAL ASP LEU MET LEU SER MET ALA          
SEQRES  12 B  260  PHE ALA SER LYS GLY GLU GLU TYR GLU LYS LYS ARG ARG          
SEQRES  13 B  260  GLU PHE LEU ASP ARG VAL ASP VAL LEU HIS LEU ASP LEU          
SEQRES  14 B  260  SER LEU CYS ASP ARG PHE ASP LEU LEU GLU ASP TYR ARG          
SEQRES  15 B  260  ASN GLY LYS LEU LYS ILE GLY VAL PRO THR LEU VAL ILE          
SEQRES  16 B  260  VAL GLY GLU GLU ASP LYS LEU THR PRO LEU LYS TYR HIS          
SEQRES  17 B  260  GLU PHE PHE HIS LYS HIS ILE PRO ASN SER GLU LEU VAL          
SEQRES  18 B  260  VAL ILE PRO GLY ALA SER HIS MET VAL MET LEU GLU LYS          
SEQRES  19 B  260  HIS VAL GLU PHE ASN GLU ALA LEU GLU LYS PHE LEU LYS          
SEQRES  20 B  260  LYS VAL GLY VAL ALA GLU VAL HIS HIS HIS HIS HIS HIS          
HET    PGE  B1253      10                                                       
HET    FLC  B1254      13                                                       
HET    COA  B1255      48                                                       
HET    COA  A1257      48                                                       
HET     CL  B1256       1                                                       
HET     CL  A1258       1                                                       
HET    PEG  B1257       7                                                       
HETNAM     COA COENZYME A                                                       
HETNAM     FLC CITRATE ANION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   3  COA    2(C21 H36 N7 O16 P3 S)                                       
FORMUL   4  FLC    C6 H5 O7 3-                                                  
FORMUL   5   CL    2(CL 1-)                                                     
FORMUL   6  PGE    C6 H14 O4                                                    
FORMUL   7  PEG    C4 H10 O3                                                    
FORMUL   8  HOH   *514(H2 O)                                                    
HELIX    1   1 ASP A   33  GLN A   36  5                                   4    
HELIX    2   2 TRP A   37  ILE A   44  1                                   8    
HELIX    3   3 SER A   64  VAL A   80  1                                  17    
HELIX    4   4 SER A   89  ASN A  102  1                                  14    
HELIX    5   5 LEU A  121  GLU A  126  1                                   6    
HELIX    6   6 GLU A  126  GLU A  131  1                                   6    
HELIX    7   7 GLU A  131  MET A  142  1                                  12    
HELIX    8   8 GLY A  148  ARG A  161  1                                  14    
HELIX    9   9 ARG A  161  ARG A  174  1                                  14    
HELIX   10  10 LEU A  177  ASN A  183  1                                   7    
HELIX   11  11 PRO A  204  ILE A  215  1                                  12    
HELIX   12  12 MET A  229  LYS A  234  1                                   6    
HELIX   13  13 LYS A  234  GLY A  250  1                                  17    
HELIX   14  14 ASP B   33  GLN B   36  5                                   4    
HELIX   15  15 TRP B   37  ILE B   44  1                                   8    
HELIX   16  16 SER B   64  VAL B   80  1                                  17    
HELIX   17  17 SER B   89  ASN B  102  1                                  14    
HELIX   18  18 LEU B  121  GLU B  126  1                                   6    
HELIX   19  19 GLU B  131  MET B  142  1                                  12    
HELIX   20  20 GLY B  148  ARG B  161  1                                  14    
HELIX   21  21 ARG B  161  ARG B  174  1                                  14    
HELIX   22  22 LEU B  177  ASN B  183  1                                   7    
HELIX   23  23 PRO B  204  ILE B  215  1                                  12    
HELIX   24  24 MET B  229  LYS B  234  1                                   6    
HELIX   25  25 LYS B  234  GLY B  250  1                                  17    
SHEET    1  AA 8 GLU A   3  VAL A   9  0                                        
SHEET    2  AA 8 VAL A  12  LYS A  18 -1  O  VAL A  12   N  VAL A   9           
SHEET    3  AA 8 TYR A  47  ILE A  49 -1  O  ALA A  48   N  LEU A  17           
SHEET    4  AA 8 VAL A  24  ILE A  27  1  O  VAL A  24   N  TYR A  47           
SHEET    5  AA 8 ALA A  83  HIS A  88  1  O  VAL A  84   N  PHE A  25           
SHEET    6  AA 8 CYS A 106  VAL A 112  1  N  LEU A 107   O  ALA A  83           
SHEET    7  AA 8 THR A 192  GLY A 197  1  O  LEU A 193   N  LEU A 111           
SHEET    8  AA 8 SER A 218  ILE A 223  1  O  GLU A 219   N  VAL A 194           
SHEET    1  BA 8 GLU B   3  VAL B   9  0                                        
SHEET    2  BA 8 VAL B  12  LYS B  18 -1  O  VAL B  12   N  VAL B   9           
SHEET    3  BA 8 TYR B  47  ILE B  49 -1  O  ALA B  48   N  LEU B  17           
SHEET    4  BA 8 VAL B  24  ILE B  27  1  O  VAL B  24   N  TYR B  47           
SHEET    5  BA 8 ALA B  83  HIS B  88  1  O  VAL B  84   N  PHE B  25           
SHEET    6  BA 8 CYS B 106  VAL B 112  1  N  LEU B 107   O  ALA B  83           
SHEET    7  BA 8 THR B 192  GLY B 197  1  O  LEU B 193   N  LEU B 111           
SHEET    8  BA 8 SER B 218  ILE B 223  1  O  GLU B 219   N  VAL B 194           
SITE     1 AC1  4 THR B  42  GLU B 123  HOH B2241  HOH B2243                    
SITE     1 AC2 12 LYS A 153  ARG A 156  GLU A 157  ASP A 160                    
SITE     2 AC2 12 ARG A 161  HOH A2175  HOH A2183  GLU B 152                    
SITE     3 AC2 12 ARG B 155  HOH B2156  HOH B2159  HOH B2244                    
SITE     1 AC3 21 ALA B 116  ARG B 117  ARG B 119  VAL B 120                    
SITE     2 AC3 21 LEU B 121  GLU B 149  LEU B 202  LYS B 206                    
SITE     3 AC3 21 TYR B 207  HOH B2097  HOH B2098  HOH B2105                    
SITE     4 AC3 21 HOH B2152  HOH B2153  HOH B2184  HOH B2206                    
SITE     5 AC3 21 HOH B2245  HOH B2246  HOH B2247  HOH B2248                    
SITE     6 AC3 21 HOH B2249                                                     
SITE     1 AC4 14 ALA A 116  ARG A 117  ARG A 119  VAL A 120                    
SITE     2 AC4 14 LEU A 121  LEU A 202  TYR A 207  HOH A2139                    
SITE     3 AC4 14 HOH A2140  HOH A2143  HOH A2202  HOH A2227                    
SITE     4 AC4 14 HOH A2262  HOH A2263                                          
SITE     1 AC5  4 SER B  30  SER B  89  LEU B  90  HOH B2090                    
SITE     1 AC6  3 SER A  30  SER A  89  LEU A  90                               
SITE     1 AC7  6 LEU A   2  HOH A2016  ARG B 182  GLY B 184                    
SITE     2 AC7  6 HOH B2182  HOH B2211                                          
CRYST1   55.070   67.200  140.570  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018159  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014881  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007114        0.00000                         
MTRIX1   1  0.858880  0.493590  0.136720      -24.40808    1                    
MTRIX2   1  0.470640 -0.865900  0.169470       -0.45999    1                    
MTRIX3   1  0.202030 -0.081210 -0.976010       33.27924    1                    
TER    2407      HIS A 256                                                      
TER    4706      ALA B 252                                                      
MASTER      396    0    7   25   16    0   18    9 5346    2  126   40          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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