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LongText Report for: 6iey-pdb

Name Class
6iey-pdb
HEADER    HYDROLASE                               18-SEP-18   6IEY              
TITLE     CRYSTAL STRUCTURE OF CHLORAMPHENICOL-METABOLIZAING ENZYME ESTDL136-   
TITLE    2 CHLORAMPHENICOL COMPLEX                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTERASE;                                                  
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 EC: 3.1.1.1;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 OTHER_DETAILS: TO MAKE ESTDL136 CRYSTAL, INTERNAL RESIDUES FROM P37  
COMPND   8 TO P39 WERE DELETED                                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;                           
SOURCE   3 ORGANISM_TAXID: 77133;                                               
SOURCE   4 GENE: ESTDL136;                                                      
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    CHLORAMPHENICOL, METAGENOME, HORNOME SENSITIVE LIPASE, HSL, ESTDL136, 
KEYWDS   2 ESTERASE, HYDROLASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.H.KIM,P.A.KANG,K.T.HAN,S.W.LEE,S.K.RHEE                             
REVDAT   1   06-FEB-19 6IEY    0                                                
JRNL        AUTH   S.H.KIM,P.A.KANG,K.T.HAN,S.W.LEE,S.K.RHEE                    
JRNL        TITL   CRYSTAL STRUCTURE OF CHLORAMPHENICOL-METABOLIZING ENZYME     
JRNL        TITL 2 ESTDL136 FROM A METAGENOME.                                  
JRNL        REF    PLOS ONE                      V.  14 10298 2019              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   30645605                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0210298                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.04                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 45505                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 29.0426 -  5.0459    1.00     3500   161  0.1746 0.1980        
REMARK   3     2  5.0459 -  4.0084    1.00     3337   153  0.1715 0.2170        
REMARK   3     3  4.0084 -  3.5027    1.00     3332   153  0.1864 0.2557        
REMARK   3     4  3.5027 -  3.1829    1.00     3260   151  0.2122 0.2613        
REMARK   3     5  3.1829 -  2.9550    0.99     3206   147  0.2268 0.2888        
REMARK   3     6  2.9550 -  2.7809    0.97     3164   145  0.2292 0.2709        
REMARK   3     7  2.7809 -  2.6417    0.95     3094   143  0.2300 0.3132        
REMARK   3     8  2.6417 -  2.5268    0.94     3058   140  0.2388 0.2895        
REMARK   3     9  2.5268 -  2.4296    0.93     2996   138  0.2367 0.3280        
REMARK   3    10  2.4296 -  2.3458    0.93     2992   137  0.2338 0.2723        
REMARK   3    11  2.3458 -  2.2725    0.93     2997   138  0.2383 0.2977        
REMARK   3    12  2.2725 -  2.2075    0.93     2982   137  0.2505 0.3167        
REMARK   3    13  2.2075 -  2.1494    0.93     3037   139  0.2615 0.3319        
REMARK   3    14  2.1494 -  2.0970    0.80     2550   118  0.2655 0.3109        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.160           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           4781                                  
REMARK   3   ANGLE     :  1.161           6536                                  
REMARK   3   CHIRALITY :  0.044            711                                  
REMARK   3   PLANARITY :  0.007            872                                  
REMARK   3   DIHEDRAL  : 13.009           1677                                  
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 6IEY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300009077.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 7A (6B, 6C1)                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97933                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46963                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.093                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 263.0000                           
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 500MM AMMONIUM FLUORIDE (PH6.5), 30%     
REMARK 280  PEG 3350, 5% GLYCEOL AND 120MM TCEP., VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 295K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       59.23150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.20550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.23150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       76.20550            
REMARK 290   SMTRY3   4  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: 5120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 B   308                                                      
REMARK 465     HIS B   309                                                      
REMARK 465     HIS B   310                                                      
REMARK 465     HIS B   311                                                      
REMARK 465     HIS B   312                                                      
REMARK 465     HIS B   313                                                      
REMARK 465     HIS B   314                                                      
REMARK 465     HIS B   315                                                      
REMARK 465     PRO A    20                                                      
REMARK 465     ASP A    21                                                      
REMARK 465     PHE A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     VAL A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     ASN A    26                                                      
REMARK 465     HIS A   315                                                      
REMARK 465     HIS A   316                                                      
REMARK 465     HIS A   317                                                      
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     MET B   1    CG   SD   CE                                        
REMARK 470     GLU A  29    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  45    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   N    MET A     1     O    HOH A   501              2.18            
REMARK 500   OH   TYR A   127     O    HOH A   502              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 120   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    PRO B 120   C   -  N   -  CD  ANGL. DEV. = -25.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO B  20       49.87   -105.76                                   
REMARK 500    ASP B  21       66.24    -55.33                                   
REMARK 500    TYR B 119       99.56    -59.19                                   
REMARK 500    ALA B 153     -117.47     59.40                                   
REMARK 500    TYR B 181       65.85     24.73                                   
REMARK 500    TYR B 201       55.84   -115.35                                   
REMARK 500    TYR B 202      -83.80     67.27                                   
REMARK 500    ALA B 227      -65.94    -96.91                                   
REMARK 500    ALA A 153     -121.15     56.48                                   
REMARK 500    TYR A 181       70.59     22.33                                   
REMARK 500    ASN A 186       41.49   -109.65                                   
REMARK 500    TYR A 202      -64.49     75.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR B  119     PRO B  120                   95.74                    
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 CLM A 401                 
DBREF  6IEY B    1   305  UNP    G3CR02   G3CR02_9BACT     1    310             
DBREF  6IEY A    1   307  UNP    G3CR02   G3CR02_9BACT     1    310             
SEQADV 6IEY     B       UNP  G3CR02    PRO    37 DELETION                       
SEQADV 6IEY     B       UNP  G3CR02    MET    38 DELETION                       
SEQADV 6IEY     B       UNP  G3CR02    PRO    39 DELETION                       
SEQADV 6IEY ALA B  153  UNP  G3CR02    SER   156 ENGINEERED MUTATION            
SEQADV 6IEY LEU B  306  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY GLU B  307  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS B  308  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS B  309  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS B  310  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS B  311  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS B  312  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS B  313  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS B  314  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS B  315  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY     A       UNP  G3CR02    PRO    37 DELETION                       
SEQADV 6IEY     A       UNP  G3CR02    MET    38 DELETION                       
SEQADV 6IEY     A       UNP  G3CR02    PRO    39 DELETION                       
SEQADV 6IEY ALA A  153  UNP  G3CR02    SER   156 ENGINEERED MUTATION            
SEQADV 6IEY LEU A  308  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY GLU A  309  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS A  310  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS A  311  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS A  312  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS A  313  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS A  314  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS A  315  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS A  316  UNP  G3CR02              EXPRESSION TAG                 
SEQADV 6IEY HIS A  317  UNP  G3CR02              EXPRESSION TAG                 
SEQRES   1 B  317  MET PRO LEU ASN PRO HIS VAL GLU ALA LEU LEU GLN MET          
SEQRES   2 B  317  MET ALA GLN MET PRO ALA PRO ASP PHE SER VAL ALA ASN          
SEQRES   3 B  317  PRO ALA GLU ILE ARG ALA VAL PHE ASP ASN LEU ALA ALA          
SEQRES   4 B  317  PRO PRO GLN VAL ALA ARG VAL GLU ASN ILE ALA ILE SER          
SEQRES   5 B  317  LEU ASP GLY ARG ASP LEU ASP ALA ARG LEU TYR VAL PRO          
SEQRES   6 B  317  GLU ASP ALA ASP GLU ARG PRO ALA LEU MET VAL TYR TYR          
SEQRES   7 B  317  HIS GLY GLY GLY TRP VAL ILE GLY THR LEU ASP THR HIS          
SEQRES   8 B  317  ASP GLY THR CYS ARG ALA LEU ALA GLN LYS SER GLY CYS          
SEQRES   9 B  317  ALA VAL LEU SER ILE ALA TYR ARG LEU ALA PRO GLU TYR          
SEQRES  10 B  317  ARG TYR PRO ALA PRO ALA GLU ASP CYS TYR ASP ALA LEU          
SEQRES  11 B  317  VAL TRP ALA LYS GLN ASN ALA ALA THR LEU GLY VAL ASP          
SEQRES  12 B  317  GLY ASP ARG LEU ALA VAL GLY GLY ASP ALA ALA GLY GLY          
SEQRES  13 B  317  ASN LEU ALA ALA ALA VAL ALA ILE MET ALA ARG ASP ARG          
SEQRES  14 B  317  ASN GLY PRO ALA LEU ARG HIS GLN LEU LEU ILE TYR PRO          
SEQRES  15 B  317  VAL THR ASP ASN ASP PHE THR LEU ALA SER TYR ALA GLU          
SEQRES  16 B  317  ASN GLY GLY GLY GLU TYR TYR LEU SER THR ASP GLY MET          
SEQRES  17 B  317  ARG TRP PHE TRP GLY HIS TYR LEU GLY ASP THR ALA ALA          
SEQRES  18 B  317  GLU ASN ALA PRO LEU ALA ALA VAL LEU ASN VAL ALA ASP          
SEQRES  19 B  317  LEU SER GLY LEU ALA PRO ALA THR VAL ILE THR ALA GLU          
SEQRES  20 B  317  TYR ASP PRO LEU ARG ASP GLU GLY ILE ALA TYR ALA LYS          
SEQRES  21 B  317  LYS LEU ASP ALA ALA GLY VAL PRO VAL ASP ALA ALA THR          
SEQRES  22 B  317  ALA PRO GLY MET ILE HIS GLY PHE PHE SER MET PHE GLU          
SEQRES  23 B  317  ALA VAL PRO ASP SER TRP GLU TRP ILE GLU ARG GLY ALA          
SEQRES  24 B  317  SER ASN LEU LYS ARG ASP LEU ALA LEU GLU HIS HIS HIS          
SEQRES  25 B  317  HIS HIS HIS HIS HIS                                          
SEQRES   1 A  317  MET PRO LEU ASN PRO HIS VAL GLU ALA LEU LEU GLN MET          
SEQRES   2 A  317  MET ALA GLN MET PRO ALA PRO ASP PHE SER VAL ALA ASN          
SEQRES   3 A  317  PRO ALA GLU ILE ARG ALA VAL PHE ASP ASN LEU ALA ALA          
SEQRES   4 A  317  PRO PRO GLN VAL ALA ARG VAL GLU ASN ILE ALA ILE SER          
SEQRES   5 A  317  LEU ASP GLY ARG ASP LEU ASP ALA ARG LEU TYR VAL PRO          
SEQRES   6 A  317  GLU ASP ALA ASP GLU ARG PRO ALA LEU MET VAL TYR TYR          
SEQRES   7 A  317  HIS GLY GLY GLY TRP VAL ILE GLY THR LEU ASP THR HIS          
SEQRES   8 A  317  ASP GLY THR CYS ARG ALA LEU ALA GLN LYS SER GLY CYS          
SEQRES   9 A  317  ALA VAL LEU SER ILE ALA TYR ARG LEU ALA PRO GLU TYR          
SEQRES  10 A  317  ARG TYR PRO ALA PRO ALA GLU ASP CYS TYR ASP ALA LEU          
SEQRES  11 A  317  VAL TRP ALA LYS GLN ASN ALA ALA THR LEU GLY VAL ASP          
SEQRES  12 A  317  GLY ASP ARG LEU ALA VAL GLY GLY ASP ALA ALA GLY GLY          
SEQRES  13 A  317  ASN LEU ALA ALA ALA VAL ALA ILE MET ALA ARG ASP ARG          
SEQRES  14 A  317  ASN GLY PRO ALA LEU ARG HIS GLN LEU LEU ILE TYR PRO          
SEQRES  15 A  317  VAL THR ASP ASN ASP PHE THR LEU ALA SER TYR ALA GLU          
SEQRES  16 A  317  ASN GLY GLY GLY GLU TYR TYR LEU SER THR ASP GLY MET          
SEQRES  17 A  317  ARG TRP PHE TRP GLY HIS TYR LEU GLY ASP THR ALA ALA          
SEQRES  18 A  317  GLU ASN ALA PRO LEU ALA ALA VAL LEU ASN VAL ALA ASP          
SEQRES  19 A  317  LEU SER GLY LEU ALA PRO ALA THR VAL ILE THR ALA GLU          
SEQRES  20 A  317  TYR ASP PRO LEU ARG ASP GLU GLY ILE ALA TYR ALA LYS          
SEQRES  21 A  317  LYS LEU ASP ALA ALA GLY VAL PRO VAL ASP ALA ALA THR          
SEQRES  22 A  317  ALA PRO GLY MET ILE HIS GLY PHE PHE SER MET PHE GLU          
SEQRES  23 A  317  ALA VAL PRO ASP SER TRP GLU TRP ILE GLU ARG GLY ALA          
SEQRES  24 A  317  SER ASN LEU LYS ARG ASP LEU ALA LEU GLU HIS HIS HIS          
SEQRES  25 A  317  HIS HIS HIS HIS HIS                                          
HET    CLM  A 401      20                                                       
HETNAM     CLM CHLORAMPHENICOL                                                  
FORMUL   3  CLM    C11 H12 CL2 N2 O5                                            
FORMUL   4  HOH   *204(H2 O)                                                    
HELIX    1 AA1 ASN B    4  GLN B   16  1                                  13    
HELIX    2 AA2 ASN B   26  ALA B   39  1                                  14    
HELIX    3 AA3 HIS B   91  GLY B  103  1                                  13    
HELIX    4 AA4 PRO B  120  ASN B  136  1                                  17    
HELIX    5 AA5 ASN B  136  GLY B  141  1                                   6    
HELIX    6 AA6 ALA B  153  ARG B  169  1                                  17    
HELIX    7 AA7 LEU B  190  GLY B  197  1                                   8    
HELIX    8 AA8 SER B  204  GLY B  217  1                                  14    
HELIX    9 AA9 ALA B  220  ALA B  224  5                                   5    
HELIX   10 AB1 ALA B  228  VAL B  232  5                                   5    
HELIX   11 AB2 LEU B  251  ALA B  265  1                                  15    
HELIX   12 AB3 GLY B  278  PHE B  283  5                                   6    
HELIX   13 AB4 ASP B  288  LEU B  304  1                                  17    
HELIX   14 AB5 ASN A    4  GLN A   16  1                                  13    
HELIX   15 AB6 ALA A   28  ASP A   35  1                                   8    
HELIX   16 AB7 HIS A   91  GLY A  103  1                                  13    
HELIX   17 AB8 PRO A  120  ASN A  136  1                                  17    
HELIX   18 AB9 ASN A  136  GLY A  141  1                                   6    
HELIX   19 AC1 ALA A  153  ARG A  169  1                                  17    
HELIX   20 AC2 LEU A  190  GLY A  197  1                                   8    
HELIX   21 AC3 SER A  204  GLY A  217  1                                  14    
HELIX   22 AC4 ALA A  220  ALA A  224  5                                   5    
HELIX   23 AC5 ALA A  228  VAL A  232  5                                   5    
HELIX   24 AC6 LEU A  251  ALA A  265  1                                  15    
HELIX   25 AC7 GLY A  280  PHE A  285  5                                   6    
HELIX   26 AC8 ASP A  290  LEU A  306  1                                  17    
SHEET    1 AA1 8 ARG B  45  LEU B  53  0                                        
SHEET    2 AA1 8 ARG B  56  VAL B  64 -1  O  VAL B  64   N  ARG B  45           
SHEET    3 AA1 8 ALA B 105  ILE B 109 -1  O  SER B 108   N  ARG B  61           
SHEET    4 AA1 8 ALA B  73  TYR B  78  1  N  TYR B  77   O  LEU B 107           
SHEET    5 AA1 8 ASP B 143  ASP B 152  1  O  ALA B 148   N  VAL B  76           
SHEET    6 AA1 8 LEU B 174  ILE B 180  1  O  ARG B 175   N  LEU B 147           
SHEET    7 AA1 8 ALA B 241  ALA B 246  1  O  THR B 242   N  LEU B 179           
SHEET    8 AA1 8 VAL B 269  ALA B 272  1  O  ALA B 272   N  THR B 245           
SHEET    1 AA2 8 ARG A  45  SER A  52  0                                        
SHEET    2 AA2 8 ASP A  57  VAL A  64 -1  O  LEU A  58   N  ILE A  51           
SHEET    3 AA2 8 ALA A 105  ILE A 109 -1  O  SER A 108   N  ARG A  61           
SHEET    4 AA2 8 LEU A  74  TYR A  78  1  N  MET A  75   O  LEU A 107           
SHEET    5 AA2 8 LEU A 147  ASP A 152  1  O  ALA A 148   N  VAL A  76           
SHEET    6 AA2 8 HIS A 176  ILE A 180  1  O  ILE A 180   N  GLY A 151           
SHEET    7 AA2 8 ALA A 241  ALA A 246  1  O  THR A 242   N  LEU A 179           
SHEET    8 AA2 8 VAL A 269  ALA A 274  1  O  ASP A 270   N  VAL A 243           
CISPEP   1 ALA B  114    PRO B  115          0        -2.74                     
CISPEP   2 ALA A  114    PRO A  115          0         1.27                     
CISPEP   3 TYR A  119    PRO A  120          0         5.33                     
SITE     1 AC1 11 HIS A  91  ASP A 152  TYR A 181  TYR A 202                    
SITE     2 AC1 11 LEU A 203  HIS A 279  GLY A 280  SER A 283                    
SITE     3 AC1 11 HOH A 542  PHE B  34  ALA B  38                               
CRYST1  118.463  152.411   44.137  90.00  90.00  90.00 P 21 21 2     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      0.008441  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006561  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022657        0.00000                         
TER    2327      GLU B 307                                                      
TER    4645      HIS A 314                                                      
MASTER      317    0    1   26   16    0    3    6 4867    2   20   50          
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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