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LongText Report for: 5CT4-pdb

Name Class
5CT4-pdb
HEADER    HYDROLASE                               23-JUL-15   5CT4              
TITLE     WILD-TYPE BACILLUS SUBTILIS LIPASE A WITH 5% [BMIM][CL]               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTERASE;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: LIPASE,LIPASE A;                                            
COMPND   5 EC: 3.1.1.3;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: LIPA, QX56_01625;                                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET21B                                    
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.M.NORDWALD,J.G.PLAKS,J.R.SNELL,M.C.SOUSA,J.L.KAAR                   
REVDAT   1   04-NOV-15 5CT4    0                                                
JRNL        AUTH   E.M.NORDWALD,J.G.PLAKS,J.R.SNELL,M.C.SOUSA,J.L.KAAR          
JRNL        TITL   CRYSTALLOGRAPHIC INVESTIGATION OF IMIDAZOLIUM IONIC LIQUID   
JRNL        TITL 2 EFFECTS ON ENZYME STRUCTURE.                                 
JRNL        REF    CHEMBIOCHEM                                2015              
JRNL        REFN                   ESSN 1439-7633                               
JRNL        PMID   26388426                                                     
JRNL        DOI    10.1002/CBIC.201500398                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7.3_928                                     
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) : 1.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.40                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 52536                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.127                           
REMARK   3   R VALUE            (WORKING SET) : 0.126                           
REMARK   3   FREE R VALUE                     : 0.156                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.810                           
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 36.4823 -  3.5780    0.98     3808   150  0.1503 0.1442        
REMARK   3     2  3.5780 -  2.8403    1.00     3692   147  0.1319 0.1667        
REMARK   3     3  2.8403 -  2.4814    1.00     3661   144  0.1264 0.1467        
REMARK   3     4  2.4814 -  2.2546    1.00     3642   144  0.1145 0.1655        
REMARK   3     5  2.2546 -  2.0930    1.00     3647   146  0.1156 0.1552        
REMARK   3     6  2.0930 -  1.9696    1.00     3611   143  0.1219 0.1495        
REMARK   3     7  1.9696 -  1.8710    1.00     3616   142  0.1183 0.1638        
REMARK   3     8  1.8710 -  1.7895    1.00     3582   142  0.1088 0.1401        
REMARK   3     9  1.7895 -  1.7206    1.00     3606   143  0.1033 0.1469        
REMARK   3    10  1.7206 -  1.6612    1.00     3575   141  0.1058 0.1585        
REMARK   3    11  1.6612 -  1.6093    1.00     3587   142  0.1075 0.1599        
REMARK   3    12  1.6093 -  1.5633    1.00     3558   141  0.1132 0.1708        
REMARK   3    13  1.5633 -  1.5221    1.00     3569   141  0.1338 0.1708        
REMARK   3    14  1.5221 -  1.4850    0.94     3382   134  0.1644 0.2168        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 36.01                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.020           
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) : -0.47210                                             
REMARK   3    B22 (A**2) : 1.05970                                              
REMARK   3    B33 (A**2) : -0.74170                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.009           2815                                  
REMARK   3   ANGLE     :  1.203           3817                                  
REMARK   3   CHIRALITY :  0.069            422                                  
REMARK   3   PLANARITY :  0.007            492                                  
REMARK   3   DIHEDRAL  : 12.547           1007                                  
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 5CT4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212139.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9999                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52595                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.490                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.12600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 7.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 35 % PEG 3350, 20 MM NASO4, 0.1M         
REMARK 280  ETHANOLAMINE, 10MM ZNCL2, PH 9.5, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       19.72000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.91000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.58000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.91000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.72000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.58000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A     2                                                      
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   HE2  HIS A     3     O    HOH A   302              1.34            
REMARK 500   O    PRO A   119     O    HOH A   301              1.89            
REMARK 500   NE2  HIS A     3     O    HOH A   302              1.99            
REMARK 500   O    HOH B   344     O    HOH B   458              1.99            
REMARK 500   O    HOH B   334     O    HOH B   545              2.02            
REMARK 500   O    HOH B   356     O    HOH B   445              2.06            
REMARK 500   O    HOH A   304     O    HOH A   499              2.10            
REMARK 500   O    HOH B   368     O    HOH B   382              2.11            
REMARK 500   O    PHE B    17     O    HOH B   301              2.12            
REMARK 500   O    HOH B   304     O    HOH B   311              2.13            
REMARK 500   O    HOH A   463     O    HOH A   470              2.13            
REMARK 500   O    HOH A   452     O    HOH B   502              2.15            
REMARK 500   O    HOH A   449     O    HOH A   492              2.16            
REMARK 500   O    HOH A   511     O    HOH A   521              2.16            
REMARK 500   O    HOH A   319     O    HOH A   470              2.18            
REMARK 500   O    HOH B   500     O    HOH B   508              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   SD   MET A   134     O    HOH B   301     2555     2.11            
REMARK 500   SD   MET A   134     O    HOH B   368     2555     2.12            
REMARK 500   O    HOH A   480     O    HOH B   491     2555     2.16            
REMARK 500   O    HOH A   486     O    HOH B   483     2555     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    SER A  77     -130.77     63.04                                   
REMARK 500    LEU A  90     -142.95   -110.28                                   
REMARK 500    ALA A  97      -62.44   -107.58                                   
REMARK 500    SER B  77     -126.57     58.74                                   
REMARK 500    LEU B  90     -146.80   -119.66                                   
REMARK 500    ALA B  97      -65.48   -102.69                                   
REMARK 500    GLN B 121      106.47   -161.01                                   
REMARK 500    TYR B 161       56.60   -142.08                                   
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 530        DISTANCE =  5.92 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BM0 A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BM0 A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 202                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5CRI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5CT5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5CT6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5CT8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5CT9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5CTA   RELATED DB: PDB                                   
DBREF  5CT4 A    2   181  UNP    I6V559   I6V559_BACIU    33    212             
DBREF  5CT4 B    2   181  UNP    I6V559   I6V559_BACIU    33    212             
SEQRES   1 A  180  GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY          
SEQRES   2 A  180  ALA SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL          
SEQRES   3 A  180  SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP          
SEQRES   4 A  180  PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO          
SEQRES   5 A  180  VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR          
SEQRES   6 A  180  GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY          
SEQRES   7 A  180  GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY          
SEQRES   8 A  180  GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA          
SEQRES   9 A  180  ASN ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP          
SEQRES  10 A  180  PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER          
SEQRES  11 A  180  ALA ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP          
SEQRES  12 A  180  GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE          
SEQRES  13 A  180  GLY LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS          
SEQRES  14 A  180  GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN                  
SEQRES   1 B  180  GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY          
SEQRES   2 B  180  ALA SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL          
SEQRES   3 B  180  SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP          
SEQRES   4 B  180  PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO          
SEQRES   5 B  180  VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR          
SEQRES   6 B  180  GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY          
SEQRES   7 B  180  GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY          
SEQRES   8 B  180  GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA          
SEQRES   9 B  180  ASN ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP          
SEQRES  10 B  180  PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER          
SEQRES  11 B  180  ALA ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP          
SEQRES  12 B  180  GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE          
SEQRES  13 B  180  GLY LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS          
SEQRES  14 B  180  GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN                  
HET    BM0  A 201      25                                                       
HET    BM0  A 202      25                                                       
HET    SO4  A 203       5                                                       
HET     CL  A 204       1                                                       
HET    SO4  B 201       5                                                       
HET    SO4  B 202       5                                                       
HETNAM     BM0 1-BUTYL-3-METHYL-1H-IMIDAZOL-3-IUM                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETSYN     BM0 1-BUTYL-3-METHYLIMIDAZOLIUM                                      
FORMUL   3  BM0    2(C8 H15 N2 1+)                                              
FORMUL   5  SO4    3(O4 S 2-)                                                   
FORMUL   6   CL    CL 1-                                                        
FORMUL   9  HOH   *501(H2 O)                                                    
HELIX    1 AA1 ALA A   15  ASN A   18  5                                   4    
HELIX    2 AA2 PHE A   19  GLN A   29  1                                  11    
HELIX    3 AA3 SER A   32  ASP A   34  5                                   3    
HELIX    4 AA4 THR A   47  GLY A   67  1                                  21    
HELIX    5 AA5 MET A   78  LEU A   90  1                                  13    
HELIX    6 AA6 ASP A   91  ASN A   94  5                                   4    
HELIX    7 AA7 ALA A  105  THR A  109  5                                   5    
HELIX    8 AA8 MET A  137  ARG A  142  1                                   6    
HELIX    9 AA9 HIS A  156  TYR A  161  5                                   6    
HELIX   10 AB1 SER A  162  ASN A  174  1                                  13    
HELIX   11 AB2 PHE B   19  GLN B   29  1                                  11    
HELIX   12 AB3 SER B   32  ASP B   34  5                                   3    
HELIX   13 AB4 THR B   47  GLY B   67  1                                  21    
HELIX   14 AB5 MET B   78  LEU B   90  1                                  13    
HELIX   15 AB6 ASP B   91  ASN B   94  5                                   4    
HELIX   16 AB7 ALA B  105  THR B  109  5                                   5    
HELIX   17 AB8 MET B  137  ARG B  142  1                                   6    
HELIX   18 AB9 HIS B  156  TYR B  161  5                                   6    
HELIX   19 AC1 SER B  162  ASN B  174  1                                  13    
SHEET    1 AA1 6 LEU A  36  ALA A  38  0                                        
SHEET    2 AA1 6 VAL A   6  VAL A   9  1  N  VAL A   6   O  TYR A  37           
SHEET    3 AA1 6 VAL A  71  HIS A  76  1  O  ASP A  72   N  VAL A   7           
SHEET    4 AA1 6 VAL A  96  LEU A 102  1  O  VAL A 100   N  ALA A  75           
SHEET    5 AA1 6 LEU A 124  SER A 130  1  O  LEU A 124   N  VAL A  99           
SHEET    6 AA1 6 ARG A 147  ILE A 151  1  O  VAL A 149   N  SER A 127           
SHEET    1 AA2 6 LEU B  36  ALA B  38  0                                        
SHEET    2 AA2 6 VAL B   6  VAL B   9  1  N  MET B   8   O  TYR B  37           
SHEET    3 AA2 6 VAL B  71  HIS B  76  1  O  ASP B  72   N  VAL B   7           
SHEET    4 AA2 6 VAL B  96  LEU B 102  1  O  VAL B 100   N  ILE B  73           
SHEET    5 AA2 6 LEU B 124  SER B 130  1  O  LEU B 124   N  VAL B  99           
SHEET    6 AA2 6 ARG B 147  ILE B 151  1  O  VAL B 149   N  SER B 127           
SITE     1 AC1  9 LYS A  23  SER A  24  VAL A  27  ARG A  33                    
SITE     2 AC1  9 ASP A  64  HOH A 392  HOH A 407  HOH A 412                    
SITE     3 AC1  9 HOH A 437                                                     
SITE     1 AC2  4 HOH A 468  LYS B  88  ASN B  89  LEU B  90                    
SITE     1 AC3  4 SER A 162  SER A 163  GLN A 164  HOH A 342                    
SITE     1 AC4  3 MET A 134  HIS A 156  HOH A 334                               
SITE     1 AC5  7 ARG A 142  HOH A 369  ARG B  33  MET B 137                    
SITE     2 AC5  7 TYR B 139  HOH B 328  HOH B 472                               
SITE     1 AC6  6 TYR B 129  ARG B 142  GLN B 150  HOH B 302                    
SITE     2 AC6  6 HOH B 307  HOH B 371                                          
CRYST1   39.440   83.160   95.820  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.025355  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012025  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010436        0.00000                         
TER    2711      ASN A 181                                                      
TER    5457      ASN B 181                                                      
MASTER      334    0    6   19   12    0   10    6 3248    2   65   28          
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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