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LongText Report for: 5k3f-pdb

Name Class
5k3f-pdb
HEADER    HYDROLASE                               19-MAY-16   5K3F              
TITLE     CRYSTAL STRUCTURE OF THE FLUOROACETATE DEHALOGENASE RPA1163 -         
TITLE    2 HIS280ASN/FLUOROACETATE - COCRYSTALLIZED - SINGLE PROTOMER REACTED   
TITLE    3 WITH LIGAND                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FLUOROACETATE DEHALOGENASE;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.8.1.3;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: FLUOROACETATE DEHALOGENASE;                                
COMPND   8 CHAIN: B;                                                            
COMPND   9 EC: 3.8.1.3;                                                         
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS (STRAIN ATCC BAA-98  
SOURCE   3 / CGA009);                                                           
SOURCE   4 ORGANISM_TAXID: 258594;                                              
SOURCE   5 STRAIN: ATCC BAA-98 / CGA009;                                        
SOURCE   6 GENE: RPA1163;                                                       
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS (STRAIN ATCC BAA-98  
SOURCE  11 / CGA009);                                                           
SOURCE  12 ORGANISM_TAXID: 258594;                                              
SOURCE  13 STRAIN: ATCC BAA-98 / CGA009;                                        
SOURCE  14 GENE: RPA1163;                                                       
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HOMODIMER, HYDROLASE, DEHALOGENASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.MEHRABI,T.H.KIM,S.R.PROSSER,E.F.PAI                                 
REVDAT   1   01-FEB-17 5K3F    0                                                
JRNL        AUTH   T.H.KIM,P.MEHRABI,Z.REN,A.SLJOKA,C.ING,A.BEZGINOV,L.YE,      
JRNL        AUTH 2 R.POMES,R.S.PROSSER,E.F.PAI                                  
JRNL        TITL   THE ROLE OF DIMER ASYMMETRY AND PROTOMER DYNAMICS IN ENZYME  
JRNL        TITL 2 CATALYSIS.                                                   
JRNL        REF    SCIENCE                       V. 355       2017              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   28104837                                                     
JRNL        DOI    10.1126/SCIENCE.AAG2355                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.54 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.81                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 74512                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3749                            
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 36.8173 -  4.6168    0.99     2899   127  0.1476 0.1607        
REMARK   3     2  4.6168 -  3.6656    0.87     2314   124  0.1217 0.1477        
REMARK   3     3  3.6656 -  3.2025    0.80     2109   129  0.1509 0.1840        
REMARK   3     4  3.2025 -  2.9099    0.98     2793   162  0.1647 0.2126        
REMARK   3     5  2.9099 -  2.7014    0.98     2773   143  0.1723 0.2135        
REMARK   3     6  2.7014 -  2.5421    0.97     2758   149  0.1720 0.2173        
REMARK   3     7  2.5421 -  2.4148    0.97     2764   126  0.1722 0.2244        
REMARK   3     8  2.4148 -  2.3097    0.97     2730   147  0.1726 0.2409        
REMARK   3     9  2.3097 -  2.2208    0.94     2661   141  0.1976 0.2359        
REMARK   3    10  2.2208 -  2.1442    0.95     2677   147  0.1751 0.2157        
REMARK   3    11  2.1442 -  2.0772    0.96     2712   152  0.1876 0.2487        
REMARK   3    12  2.0772 -  2.0178    0.94     2657   130  0.2043 0.2299        
REMARK   3    13  2.0178 -  1.9647    0.95     2692   141  0.1849 0.2406        
REMARK   3    14  1.9647 -  1.9168    0.93     2590   136  0.2265 0.2314        
REMARK   3    15  1.9168 -  1.8732    0.93     2615   162  0.2250 0.2860        
REMARK   3    16  1.8732 -  1.8333    0.94     2606   145  0.1971 0.2419        
REMARK   3    17  1.8333 -  1.7966    0.93     2678   126  0.1896 0.2263        
REMARK   3    18  1.7966 -  1.7627    0.93     2628   125  0.1914 0.2381        
REMARK   3    19  1.7627 -  1.7313    0.92     2617   119  0.1908 0.2576        
REMARK   3    20  1.7313 -  1.7019    0.92     2627   143  0.1947 0.2429        
REMARK   3    21  1.7019 -  1.6745    0.93     2573   132  0.1983 0.2532        
REMARK   3    22  1.6745 -  1.6487    0.90     2573   139  0.2176 0.2389        
REMARK   3    23  1.6487 -  1.6245    0.92     2580   152  0.2185 0.2699        
REMARK   3    24  1.6245 -  1.6016    0.91     2570   132  0.2301 0.2730        
REMARK   3    25  1.6016 -  1.5799    0.89     2531   136  0.2507 0.3174        
REMARK   3    26  1.5799 -  1.5594    0.90     2516   139  0.2580 0.3386        
REMARK   3    27  1.5594 -  1.5399    0.90     2520   145  0.2707 0.3144        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.100           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.70                          
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      :  0.007           4861                                  
REMARK   3   ANGLE     :  1.154           6631                                  
REMARK   3   CHIRALITY :  0.044            678                                  
REMARK   3   PLANARITY :  0.006            874                                  
REMARK   3   DIHEDRAL  : 13.108           1744                                  
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 5K3F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221626.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E DW                     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN A200                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74512                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.540                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.807                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : 0.02500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 19.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3R3U                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350 19-22%, 200MM CALCIUM           
REMARK 280  CHLORIDE, 100MM TRIS HCL PH 8.5, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 298K                                                    
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       39.81000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ALA A   301                                                      
REMARK 465     PRO A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     SER A   304                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     ILE B   253                                                      
REMARK 465     ALA B   254                                                      
REMARK 465     GLN B   255                                                      
REMARK 465     SER B   256                                                      
REMARK 465     ALA B   300                                                      
REMARK 465     ALA B   301                                                      
REMARK 465     PRO B   302                                                      
REMARK 465     GLY B   303                                                      
REMARK 465     SER B   304                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 152    CG   CD   CE   NZ                                   
REMARK 470     ASP B   3    CG   OD1  OD2                                       
REMARK 470     LEU B   4    CG   CD1  CD2                                       
REMARK 470     LYS B  53    CG   CD   CE   NZ                                   
REMARK 470     ARG B  57    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  78    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 292    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 296    CG   CD   NE   CZ   NH1  NH2                        
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   O    HOH A   404     O    HOH A   423              1.98            
REMARK 500   O    HOH B   502     O    HOH B   523              2.11            
REMARK 500   O    HOH A   494     O    HOH A   706              2.16            
REMARK 500   OE1  GLU B   235     O    HOH B   501              2.18            
REMARK 500   O    HOH B   607     O    HOH B   673              2.19            
REMARK 500   O    HOH B   765     O    HOH B   788              2.19            
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   O    HOH A   462     O    HOH B   784     1556     2.12            
REMARK 500   O    HOH A   569     O    HOH A   601     2557     2.17            
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    PRO A  41       66.38   -100.48                                   
REMARK 500    ASB A 110     -126.48     62.12                                   
REMARK 500    ASP A 173       63.08   -151.24                                   
REMARK 500    ASP A 173       63.08   -150.73                                   
REMARK 500    TYR A 224      -97.26   -124.07                                   
REMARK 500    ALA A 257       50.90   -140.94                                   
REMARK 500    PRO B  41       67.20   -102.09                                   
REMARK 500    GLN B  42     -168.34   -124.69                                   
REMARK 500    ASP B 110     -126.65     54.20                                   
REMARK 500    ASN B 146     -167.77   -103.02                                   
REMARK 500    ILE B 153       54.54   -111.22                                   
REMARK 500    ASP B 173       72.61   -151.55                                   
REMARK 500    TYR B 224      -91.59   -122.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 778        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A 779        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A 780        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH A 781        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH B 832        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH B 833        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH B 834        DISTANCE =  6.25 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5K3B   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5K3A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5K3C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5K3D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5K3E   RELATED DB: PDB                                   
DBREF  5K3F A    1   302  UNP    Q6NAM1   DEHA_RHOPA       1    302             
DBREF  5K3F B    1   302  UNP    Q6NAM1   DEHA_RHOPA       1    302             
SEQADV 5K3F GLY A   -1  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3F HIS A    0  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3F ASN A  280  UNP  Q6NAM1    HIS   280 ENGINEERED MUTATION            
SEQADV 5K3F GLY A  303  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3F SER A  304  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3F GLY B   -1  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3F HIS B    0  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3F ASN B  280  UNP  Q6NAM1    HIS   280 ENGINEERED MUTATION            
SEQADV 5K3F GLY B  303  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3F SER B  304  UNP  Q6NAM1              EXPRESSION TAG                 
SEQRES   1 A  306  GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE          
SEQRES   2 A  306  GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE          
SEQRES   3 A  306  ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU          
SEQRES   4 A  306  HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL          
SEQRES   5 A  306  ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA          
SEQRES   6 A  306  ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER          
SEQRES   7 A  306  ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA          
SEQRES   8 A  306  LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL          
SEQRES   9 A  306  HIS PHE ALA LEU ALA GLY HIS ASB ARG GLY ALA ARG VAL          
SEQRES  10 A  306  SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER          
SEQRES  11 A  306  LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR          
SEQRES  12 A  306  TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR          
SEQRES  13 A  306  HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU          
SEQRES  14 A  306  ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA          
SEQRES  15 A  306  LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA          
SEQRES  16 A  306  PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE          
SEQRES  17 A  306  ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR          
SEQRES  18 A  306  ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE          
SEQRES  19 A  306  ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU          
SEQRES  20 A  306  ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA          
SEQRES  21 A  306  THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL          
SEQRES  22 A  306  GLN GLY ALA PRO ILE GLU SER GLY ASN PHE LEU PRO GLU          
SEQRES  23 A  306  GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE          
SEQRES  24 A  306  PHE SER ALA ALA PRO GLY SER                                  
SEQRES   1 B  306  GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE          
SEQRES   2 B  306  GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE          
SEQRES   3 B  306  ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU          
SEQRES   4 B  306  HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL          
SEQRES   5 B  306  ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA          
SEQRES   6 B  306  ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER          
SEQRES   7 B  306  ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA          
SEQRES   8 B  306  LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL          
SEQRES   9 B  306  HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL          
SEQRES  10 B  306  SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER          
SEQRES  11 B  306  LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR          
SEQRES  12 B  306  TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR          
SEQRES  13 B  306  HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU          
SEQRES  14 B  306  ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA          
SEQRES  15 B  306  LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA          
SEQRES  16 B  306  PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE          
SEQRES  17 B  306  ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR          
SEQRES  18 B  306  ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE          
SEQRES  19 B  306  ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU          
SEQRES  20 B  306  ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA          
SEQRES  21 B  306  THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL          
SEQRES  22 B  306  GLN GLY ALA PRO ILE GLU SER GLY ASN PHE LEU PRO GLU          
SEQRES  23 B  306  GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE          
SEQRES  24 B  306  PHE SER ALA ALA PRO GLY SER                                  
MODRES 5K3F ASB A  110  ASP  MODIFIED RESIDUE                                   
HET    ASB  A 110      12                                                       
HET     CL  B 401       1                                                       
HETNAM     ASB ASPARTIC ACID-4-CARBOXYMETHYL ESTER                              
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  ASB    C6 H9 N O6                                                   
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  HOH   *715(H2 O)                                                    
HELIX    1 AA1 THR A   43  HIS A   48  5                                   6    
HELIX    2 AA2 VAL A   50  ALA A   55  1                                   6    
HELIX    3 AA3 HIS A   80  TYR A   83  5                                   4    
HELIX    4 AA4 THR A   84  LEU A   99  1                                  16    
HELIX    5 AA5 ASB A  110  SER A  123  1                                  14    
HELIX    6 AA6 PRO A  137  ARG A  144  1                                   8    
HELIX    7 AA7 ASN A  146  ILE A  153  1                                   8    
HELIX    8 AA8 TYR A  154  LEU A  159  1                                   6    
HELIX    9 AA9 PRO A  164  GLY A  171  1                                   8    
HELIX   10 AB1 ASP A  173  TRP A  185  1                                  13    
HELIX   11 AB2 ASP A  195  ALA A  207  1                                  13    
HELIX   12 AB3 ASP A  208  TYR A  224  1                                  17    
HELIX   13 AB4 TYR A  224  GLY A  237  1                                  14    
HELIX   14 AB5 GLY A  252  SER A  256  5                                   5    
HELIX   15 AB6 THR A  259  ALA A  268  1                                  10    
HELIX   16 AB7 PHE A  281  ALA A  286  1                                   6    
HELIX   17 AB8 ALA A  286  ALA A  300  1                                  15    
HELIX   18 AB9 THR B   43  HIS B   48  5                                   6    
HELIX   19 AC1 VAL B   50  GLU B   56  1                                   7    
HELIX   20 AC2 HIS B   80  TYR B   83  5                                   4    
HELIX   21 AC3 THR B   84  LEU B   99  1                                  16    
HELIX   22 AC4 ASP B  110  SER B  123  1                                  14    
HELIX   23 AC5 PRO B  137  ARG B  144  1                                   8    
HELIX   24 AC6 ASN B  146  ILE B  153  1                                   8    
HELIX   25 AC7 TYR B  154  LEU B  159  1                                   6    
HELIX   26 AC8 PRO B  164  GLY B  171  1                                   8    
HELIX   27 AC9 ASP B  173  TRP B  185  1                                  13    
HELIX   28 AD1 ASP B  195  ASP B  208  1                                  14    
HELIX   29 AD2 ASP B  208  TYR B  224  1                                  17    
HELIX   30 AD3 TYR B  224  GLY B  237  1                                  14    
HELIX   31 AD4 THR B  259  ARG B  265  1                                   7    
HELIX   32 AD5 PHE B  281  ALA B  286  1                                   6    
HELIX   33 AD6 ALA B  286  SER B  299  1                                  14    
SHEET    1 AA1 8 GLY A  12  ILE A  16  0                                        
SHEET    2 AA1 8 ILE A  23  GLY A  29 -1  O  VAL A  27   N  GLY A  12           
SHEET    3 AA1 8 LYS A  59  ALA A  63 -1  O  VAL A  62   N  ARG A  26           
SHEET    4 AA1 8 PRO A  33  LEU A  37  1  N  LEU A  36   O  ILE A  61           
SHEET    5 AA1 8 PHE A 104  HIS A 109  1  O  HIS A 109   N  LEU A  37           
SHEET    6 AA1 8 LEU A 127  LEU A 133  1  O  ALA A 131   N  LEU A 106           
SHEET    7 AA1 8 MET A 244  GLY A 249  1  O  LEU A 245   N  VAL A 132           
SHEET    8 AA1 8 VAL A 271  ILE A 276  1  O  GLN A 272   N  ALA A 246           
SHEET    1 AA2 8 GLY B  12  ILE B  16  0                                        
SHEET    2 AA2 8 ILE B  23  GLY B  29 -1  O  VAL B  27   N  GLY B  12           
SHEET    3 AA2 8 LYS B  59  ALA B  63 -1  O  VAL B  60   N  GLY B  28           
SHEET    4 AA2 8 PRO B  33  LEU B  37  1  N  LEU B  34   O  LYS B  59           
SHEET    5 AA2 8 PHE B 104  HIS B 109  1  O  ALA B 105   N  LEU B  35           
SHEET    6 AA2 8 LEU B 127  LEU B 133  1  O  ALA B 131   N  LEU B 106           
SHEET    7 AA2 8 MET B 244  GLY B 249  1  O  LEU B 245   N  VAL B 132           
SHEET    8 AA2 8 VAL B 271  ILE B 276  1  O  GLN B 272   N  MET B 244           
LINK         C   HIS A 109                 N   ASB A 110     1555   1555  1.33  
LINK         C   ASB A 110                 N   ARG A 111     1555   1555  1.33  
CISPEP   1 PHE A   40    PRO A   41          0        -3.25                     
CISPEP   2 ALA A  163    PRO A  164          0         2.48                     
CISPEP   3 PHE B   40    PRO B   41          0        -1.79                     
CISPEP   4 ALA B  163    PRO B  164          0         4.94                     
SITE     1 AC1  3 ASP B 110  ARG B 111  ARG B 114                               
CRYST1   41.830   79.620   85.230  90.00 103.09  90.00 P 1 21 1      2          
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      0.023906  0.000000  0.005557        0.00000                         
SCALE2      0.000000  0.012560  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012046        0.00000                         
TER    2393      ALA A 300                                                      
TER    4697      SER B 299                                                      
MASTER      350    0    2   33   16    0    1    6 5353    2   14   48          
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:
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