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LongText Report for: 5k3c-pdb

Name Class
5k3c-pdb
HEADER    HYDROLASE                               19-MAY-16   5K3C              
TITLE     CRYSTAL STRUCTURE OF THE FLUOROACETATE DEHALOGENASE RPA1163 - WT/5-   
TITLE    2 FLUOROTRYPTOPHAN                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FLUOROACETATE DEHALOGENASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.8.1.3;                                                         
COMPND   5 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                                         
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 5K3C    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) : 19.14                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 77192                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3883                            
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 19.1394 -  4.6582    0.96     2667   138  0.1513 0.1724        
REMARK   3     2  4.6582 -  3.7062    0.99     2740   141  0.1241 0.1527        
REMARK   3     3  3.7062 -  3.2403    0.99     2713   136  0.1612 0.1914        
REMARK   3     4  3.2403 -  2.9452    0.99     2725   139  0.1699 0.1800        
REMARK   3     5  2.9452 -  2.7347    0.99     2690   171  0.1800 0.2299        
REMARK   3     6  2.7347 -  2.5739    0.99     2683   143  0.1712 0.1881        
REMARK   3     7  2.5739 -  2.4452    0.99     2689   141  0.1686 0.2250        
REMARK   3     8  2.4452 -  2.3390    0.99     2682   152  0.1759 0.2222        
REMARK   3     9  2.3390 -  2.2491    0.98     2678   150  0.1825 0.2191        
REMARK   3    10  2.2491 -  2.1716    0.98     2663   136  0.1769 0.2550        
REMARK   3    11  2.1716 -  2.1038    0.99     2635   156  0.1760 0.2334        
REMARK   3    12  2.1038 -  2.0437    0.99     2695   160  0.1839 0.1888        
REMARK   3    13  2.0437 -  1.9900    0.98     2608   151  0.1836 0.2226        
REMARK   3    14  1.9900 -  1.9415    0.98     2690   139  0.1908 0.2445        
REMARK   3    15  1.9415 -  1.8974    0.97     2645   127  0.1924 0.2345        
REMARK   3    16  1.8974 -  1.8570    0.97     2645   133  0.1861 0.2300        
REMARK   3    17  1.8570 -  1.8199    0.98     2640   130  0.1882 0.2326        
REMARK   3    18  1.8199 -  1.7856    0.97     2706   115  0.1832 0.2223        
REMARK   3    19  1.7856 -  1.7537    0.97     2593   140  0.1836 0.2199        
REMARK   3    20  1.7537 -  1.7240    0.97     2645   125  0.1893 0.2242        
REMARK   3    21  1.7240 -  1.6962    0.97     2626   134  0.1855 0.2408        
REMARK   3    22  1.6962 -  1.6701    0.96     2611   126  0.1919 0.2791        
REMARK   3    23  1.6701 -  1.6456    0.96     2616   161  0.1919 0.2467        
REMARK   3    24  1.6456 -  1.6224    0.96     2604   131  0.1991 0.2419        
REMARK   3    25  1.6224 -  1.6005    0.96     2602   132  0.1997 0.2517        
REMARK   3    26  1.6005 -  1.5797    0.96     2586   140  0.2030 0.2478        
REMARK   3    27  1.5797 -  1.5600    0.90     2419   137  0.2680 0.3018        
REMARK   3    28  1.5600 -  1.5412    0.67     1813    99  0.3239 0.2847        
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)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.660           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.39                          
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      :  0.013           4821                                  
REMARK   3   ANGLE     :  1.588           6581                                  
REMARK   3   CHIRALITY :  0.062            668                                  
REMARK   3   PLANARITY :  0.008            857                                  
REMARK   3   DIHEDRAL  : 13.416           1747                                  
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 5K3C 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_1000221624.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-13                          
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-D                        
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                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77192                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.541                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.138                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.02100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 25.2000                            
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   (%): 40.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
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       39.73000            
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: 2710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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     GLN A   255                                                      
REMARK 465     SER A   256                                                      
REMARK 465     ALA A   257                                                      
REMARK 465     ALA A   258                                                      
REMARK 465     ALA A   300                                                      
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     ASP B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     GLY B   252                                                      
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     GLU B  75    CG   CD   OE1  OE2                                  
REMARK 470     SER B 251    OG                                                  
REMARK 470     THR B 259    OG1  CG2                                            
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   503     O    HOH A   559              2.15            
REMARK 500   O    HOH A   506     O    HOH A   765              2.16            
REMARK 500   O    HOH A   519     O    HOH A   776              2.18            
REMARK 500   O    HOH B   501     O    HOH B   655              2.19            
REMARK 500   O    SER A   299     O    HOH A   501              2.19            
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    GLN A  42     -169.10   -121.36                                   
REMARK 500    ASP A 110     -129.56     61.73                                   
REMARK 500    TYR A 224      -96.98   -122.74                                   
REMARK 500    PRO B  41       70.93   -102.70                                   
REMARK 500    ASP B 110     -130.27     57.98                                   
REMARK 500    ASN B 146     -168.05   -101.45                                   
REMARK 500    ILE B 153       59.17   -116.74                                   
REMARK 500    TYR B 224      -95.95   -119.30                                   
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 850        DISTANCE =  5.81 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 A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
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: 5K3D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5K3F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5K3E   RELATED DB: PDB                                   
DBREF  5K3C A    3   300  UNP    Q6NAM1   DEHA_RHOPA       3    300             
DBREF  5K3C B    3   300  UNP    Q6NAM1   DEHA_RHOPA       3    300             
SEQADV 5K3C GLY A   -1  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C HIS A    0  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C MET A    1  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C PRO A    2  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C ALA A  301  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C PRO A  302  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C GLY A  303  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C SER A  304  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C GLY B   -1  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C HIS B    0  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C MET B    1  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C PRO B    2  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C ALA B  301  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C PRO B  302  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C GLY B  303  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 5K3C 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 FTR 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 FTR 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 FTR 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 ASP 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  FTR GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR          
SEQRES  13 A  306  HIS FTR 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 FTR 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 FTR GLY ALA SER GLY ILE ALA GLN SER ALA ALA          
SEQRES  21 A  306  THR PRO LEU ASP VAL FTR ARG LYS FTR ALA SER ASP VAL          
SEQRES  22 A  306  GLN GLY ALA PRO ILE GLU SER GLY HIS 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 FTR 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 FTR 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 FTR 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  FTR GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR          
SEQRES  13 B  306  HIS FTR 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 FTR 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 FTR GLY ALA SER GLY ILE ALA GLN SER ALA ALA          
SEQRES  21 B  306  THR PRO LEU ASP VAL FTR ARG LYS FTR ALA SER ASP VAL          
SEQRES  22 B  306  GLN GLY ALA PRO ILE GLU SER GLY HIS 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 5K3C FTR A   15  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR A   47  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR A   70  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR A  142  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR A  156  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR A  185  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR A  248  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR A  264  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR A  267  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR B   15  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR B   47  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR B   70  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR B  142  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR B  156  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR B  185  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR B  248  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR B  264  TRP  MODIFIED RESIDUE                                   
MODRES 5K3C FTR B  267  TRP  MODIFIED RESIDUE                                   
HET    FTR  A  15      15                                                       
HET    FTR  A  47      15                                                       
HET    FTR  A  70      15                                                       
HET    FTR  A 142      15                                                       
HET    FTR  A 156      15                                                       
HET    FTR  A 185      15                                                       
HET    FTR  A 248      15                                                       
HET    FTR  A 264      15                                                       
HET    FTR  A 267      15                                                       
HET    FTR  B  15      15                                                       
HET    FTR  B  47      15                                                       
HET    FTR  B  70      15                                                       
HET    FTR  B 142      15                                                       
HET    FTR  B 156      15                                                       
HET    FTR  B 185      15                                                       
HET    FTR  B 248      15                                                       
HET    FTR  B 264      15                                                       
HET    FTR  B 267      15                                                       
HET     CL  A 401       1                                                       
HET     CL  A 402       1                                                       
HET     CL  B 401       1                                                       
HETNAM     FTR FLUOROTRYPTOPHANE                                                
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  FTR    18(C11 H11 F N2 O2)                                          
FORMUL   3   CL    3(CL 1-)                                                     
FORMUL   6  HOH   *573(H2 O)                                                    
HELIX    1 AA1 THR A   43  HIS A   48  5                                   6    
HELIX    2 AA2 VAL A   50  GLU A   56  1                                   7    
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 ASP A  110  SER A  123  1                                  14    
HELIX    6 AA6 PRO A  137  MET A  145  1                                   9    
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  172  1                                   9    
HELIX   10 AB1 ASP A  173  FTR 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 PRO A  260  LYS A  266  1                                   7    
HELIX   15 AB6 PHE A  281  ALA A  286  1                                   6    
HELIX   16 AB7 ALA A  286  SER A  299  1                                  14    
HELIX   17 AB8 THR B   43  HIS B   48  5                                   6    
HELIX   18 AB9 VAL B   50  GLU B   56  1                                   7    
HELIX   19 AC1 HIS B   80  TYR B   83  5                                   4    
HELIX   20 AC2 THR B   84  LEU B   99  1                                  16    
HELIX   21 AC3 ASP B  110  SER B  123  1                                  14    
HELIX   22 AC4 PRO B  137  ARG B  144  1                                   8    
HELIX   23 AC5 ASN B  146  ILE B  153  1                                   8    
HELIX   24 AC6 TYR B  154  LEU B  159  1                                   6    
HELIX   25 AC7 PRO B  164  GLY B  171  1                                   8    
HELIX   26 AC8 ASP B  173  FTR B  185  1                                  13    
HELIX   27 AC9 ASP B  195  ALA B  207  1                                  13    
HELIX   28 AD1 ASP B  208  TYR B  224  1                                  17    
HELIX   29 AD2 TYR B  224  GLY B  237  1                                  14    
HELIX   30 AD3 THR B  259  ARG B  265  1                                   7    
HELIX   31 AD4 PHE B  281  ALA B  286  1                                   6    
HELIX   32 AD5 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  34   O  ILE A  61           
SHEET    5 AA1 8 PHE A 104  HIS A 109  1  O  ALA A 107   N  LEU A  35           
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 PHE B  11  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  LEU B 130           
SHEET    8 AA2 8 VAL B 271  ILE B 276  1  O  ILE B 276   N  FTR B 248           
LINK         C   GLU A  14                 N   FTR A  15     1555   1555  1.33  
LINK         C   FTR A  15                 N   ILE A  16     1555   1555  1.32  
LINK         C   MET A  46                 N   FTR A  47     1555   1555  1.34  
LINK         C   FTR A  47                 N   HIS A  48     1555   1555  1.33  
LINK         C   GLY A  69                 N   FTR A  70     1555   1555  1.33  
LINK         C   FTR A  70                 N   SER A  71     1555   1555  1.33  
LINK         C   TYR A 141                 N   FTR A 142     1555   1555  1.32  
LINK         C   FTR A 142                 N   GLN A 143     1555   1555  1.33  
LINK         C   HIS A 155                 N   FTR A 156     1555   1555  1.34  
LINK         C   FTR A 156                 N   SER A 157     1555   1555  1.34  
LINK         C   SER A 184                 N   FTR A 185     1555   1555  1.32  
LINK         C   FTR A 185                 N   THR A 186     1555   1555  1.34  
LINK         C   LEU A 247                 N   FTR A 248     1555   1555  1.32  
LINK         C   FTR A 248                 N   GLY A 249     1555   1555  1.32  
LINK         C   VAL A 263                 N   FTR A 264     1555   1555  1.34  
LINK         C   FTR A 264                 N   ARG A 265     1555   1555  1.34  
LINK         C   LYS A 266                 N   FTR A 267     1555   1555  1.34  
LINK         C   FTR A 267                 N   ALA A 268     1555   1555  1.33  
LINK         C   GLU B  14                 N   FTR B  15     1555   1555  1.33  
LINK         C   FTR B  15                 N   ILE B  16     1555   1555  1.33  
LINK         C   MET B  46                 N   FTR B  47     1555   1555  1.34  
LINK         C   FTR B  47                 N   HIS B  48     1555   1555  1.34  
LINK         C   GLY B  69                 N   FTR B  70     1555   1555  1.33  
LINK         C   FTR B  70                 N   SER B  71     1555   1555  1.32  
LINK         C  ATYR B 141                 N   FTR B 142     1555   1555  1.33  
LINK         C  BTYR B 141                 N   FTR B 142     1555   1555  1.34  
LINK         C   FTR B 142                 N   GLN B 143     1555   1555  1.33  
LINK         C   HIS B 155                 N   FTR B 156     1555   1555  1.34  
LINK         C   FTR B 156                 N   SER B 157     1555   1555  1.32  
LINK         C   SER B 184                 N   FTR B 185     1555   1555  1.33  
LINK         C   FTR B 185                 N   THR B 186     1555   1555  1.34  
LINK         C   LEU B 247                 N   FTR B 248     1555   1555  1.33  
LINK         C   FTR B 248                 N   GLY B 249     1555   1555  1.33  
LINK         C   VAL B 263                 N   FTR B 264     1555   1555  1.33  
LINK         C   FTR B 264                 N   ARG B 265     1555   1555  1.33  
LINK         C   LYS B 266                 N   FTR B 267     1555   1555  1.34  
LINK         C   FTR B 267                 N   ALA B 268     1555   1555  1.32  
CISPEP   1 PHE A   40    PRO A   41          0        -3.92                     
CISPEP   2 ALA A  163    PRO A  164          0         4.05                     
CISPEP   3 PHE B   40    PRO B   41          0        -3.33                     
CISPEP   4 ALA B  163    PRO B  164          0         5.44                     
SITE     1 AC1  3 ARG A 114  LEU A 136  HOH A 585                               
SITE     1 AC2  3 ASP A 110  ARG A 111  ARG A 114                               
SITE     1 AC3  3 ASP B 110  ARG B 111  ARG B 114                               
CRYST1   41.890   79.460   85.240  90.00 103.02  90.00 P 1 21 1      4          
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      0.023872  0.000000  0.005518        0.00000                         
SCALE2      0.000000  0.012585  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012041        0.00000                         
TER    2355      SER A 299                                                      
TER    4666      SER B 299                                                      
MASTER      333    0   21   32   16    0    3    6 5193    2  307   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:
ESTHER Home Page and ACEDB Home Page
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