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LongText Report for: 3L1H-pdb

Name Class
3L1H-pdb
HEADER    HYDROLASE                               11-DEC-09   3L1H              
TITLE     CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY FECL3                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTERASE/LIPASE;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ESTE5;                                                      
COMPND   5 EC: 3.1.1.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;                           
SOURCE   3 ORGANISM_TAXID: 77133;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 OTHER_DETAILS: SOIL METAGENOME LIBRARY                               
KEYWDS    HSL, ESTE5, ESTERASE, LIPASE, HYDROLASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.H.NAM,K.Y.HWANG                                                     
REVDAT   1   19-JAN-10 3L1H    0                                                
JRNL        AUTH   K.H.NAM,K.Y.HWANG                                            
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE NONINVASIVE INHIBITION          
JRNL        TITL 2 OF HSL-HOMOLOG ESTE5 BY ORGANIC SOLVENTS AND METAL           
JRNL        TITL 3 IONS                                                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 10962                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1083                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 420                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 55.29                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 45                           
REMARK   3   BIN FREE R VALUE                    : 0.3830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2222                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 28                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.28000                                              
REMARK   3    B22 (A**2) : 0.28000                                              
REMARK   3    B33 (A**2) : -0.55000                                             
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.813         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.306         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.229         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.867         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.899                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2275 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3086 ; 1.614 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   292 ; 6.372 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    90 ;34.956 ;24.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   376 ;17.369 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;20.720 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   338 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1724 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1463 ; 0.643 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2333 ; 1.192 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   812 ; 1.819 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   753 ; 2.920 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY                    
REMARK   4                                                                      
REMARK   4 3L1H COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-DEC-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB056713.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 6C1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.23                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10987                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 59.4                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 3FAK                                       
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: 0.1M TRIS-HCL PH 7.5, 2.2M AMMONIUM      
REMARK 280  SULFATE, 0.2M LITHIUM SULFATE, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 295.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       75.22250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       30.60800            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       30.60800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       37.61125            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       30.60800            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       30.60800            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      112.83375            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       30.60800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       30.60800            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       37.61125            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       30.60800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       30.60800            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      112.83375            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       75.22250            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A   -12                                                      
REMARK 465     ALA A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     MET A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     GLN A    -5                                                      
REMARK 465     GLN A    -4                                                      
REMARK 465     MET A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     ARG A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     VAL A   194                                                      
REMARK 465     ALA A   195                                                      
REMARK 465     PRO A   196                                                      
REMARK 465     LEU A   298                                                      
REMARK 465     ALA A   299                                                      
REMARK 465     ALA A   300                                                      
REMARK 465     ALA A   301                                                      
REMARK 465     LEU A   302                                                      
REMARK 465     GLU A   303                                                      
REMARK 465     HIS A   304                                                      
REMARK 465     HIS A   305                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     HIS A   307                                                      
REMARK 465     HIS A   308                                                      
REMARK 465     HIS A   309                                                      
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   OD1  ASP A   176     OG1  THR A   178              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    TYR A  78       -1.38     67.32                                   
REMARK 500    SER A  88      -73.24    -51.76                                   
REMARK 500    SER A 144     -119.81     60.04                                   
REMARK 500    ASP A 159      -23.67    -39.82                                   
REMARK 500    PRO A 165     -165.96    -72.61                                   
REMARK 500    PRO A 219       -6.36    -56.18                                   
REMARK 500    ASP A 237       44.42   -102.66                                   
REMARK 500    ASP A 265       -9.19     64.81                                   
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 337        DISTANCE =  6.25 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FAK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ESTE5 (NATIVE)                                  
REMARK 900 RELATED ID: 3H17   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ESTE5-PMSF (I)                                  
REMARK 900 RELATED ID: 3H18   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ESTE5-PMSF (II)                                 
REMARK 900 RELATED ID: 3H19   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY METHYL ALCOHOL             
REMARK 900 RELATED ID: 3H1A   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY ETHYL ALCOHOL              
REMARK 900 RELATED ID: 3H1B   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY ISOPROPYL ALCOHOL          
REMARK 900 RELATED ID: 3L1I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY CUSO4                      
REMARK 900 RELATED ID: 3L1J   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY ZNSO4                      
DBREF  3L1H A    1   297  UNP    Q0GMU2   Q0GMU2_9BACT     1    297             
SEQADV 3L1H MET A  -12  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H ALA A  -11  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H SER A  -10  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H MET A   -9  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H THR A   -8  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H GLY A   -7  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H GLY A   -6  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H GLN A   -5  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H GLN A   -4  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H MET A   -3  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H GLY A   -2  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H ARG A   -1  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H GLY A    0  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H LEU A  298  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H ALA A  299  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H ALA A  300  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H ALA A  301  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H LEU A  302  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H GLU A  303  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H HIS A  304  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H HIS A  305  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H HIS A  306  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H HIS A  307  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H HIS A  308  UNP  Q0GMU2              EXPRESSION TAG                 
SEQADV 3L1H HIS A  309  UNP  Q0GMU2              EXPRESSION TAG                 
SEQRES   1 A  322  MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY          
SEQRES   2 A  322  MET ALA GLY PRO GLU ILE VAL LYS LEU LYS LYS ILE LEU          
SEQRES   3 A  322  ARG GLU LYS ALA VAL PRO PRO GLY THR GLU VAL PRO LEU          
SEQRES   4 A  322  ASP VAL MET ARG LYS GLY MET GLU LYS VAL ALA PHE LYS          
SEQRES   5 A  322  ALA ALA ASP ASP ILE GLN VAL GLU GLN VAL THR VAL ALA          
SEQRES   6 A  322  GLY CYS ALA ALA GLU TRP VAL ARG ALA PRO GLY CYS GLN          
SEQRES   7 A  322  ALA GLY LYS ALA ILE LEU TYR LEU HIS GLY GLY GLY TYR          
SEQRES   8 A  322  VAL MET GLY SER ILE ASN THR HIS ARG SER MET VAL GLY          
SEQRES   9 A  322  GLU ILE SER ARG ALA SER GLN ALA ALA ALA LEU LEU LEU          
SEQRES  10 A  322  ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA          
SEQRES  11 A  322  VAL GLU ASP GLY VAL ALA ALA TYR ARG TRP LEU LEU ASP          
SEQRES  12 A  322  GLN GLY PHE LYS PRO GLN HIS LEU SER ILE SER GLY ASP          
SEQRES  13 A  322  SER ALA GLY GLY GLY LEU VAL LEU ALA VAL LEU VAL SER          
SEQRES  14 A  322  ALA ARG ASP GLN GLY LEU PRO MET PRO ALA SER ALA ILE          
SEQRES  15 A  322  PRO ILE SER PRO TRP ALA ASP MET THR CYS THR ASN ASP          
SEQRES  16 A  322  SER PHE LYS THR ARG ALA GLU ALA ASP PRO MET VAL ALA          
SEQRES  17 A  322  PRO GLY GLY ILE ASN LYS MET ALA ALA ARG TYR LEU ASN          
SEQRES  18 A  322  GLY ALA ASP ALA LYS HIS PRO TYR ALA SER PRO ASN PHE          
SEQRES  19 A  322  ALA ASN LEU LYS GLY LEU PRO PRO LEU LEU ILE HIS VAL          
SEQRES  20 A  322  GLY ARG ASP GLU VAL LEU LEU ASP ASP SER ILE LYS LEU          
SEQRES  21 A  322  ASP ALA LYS ALA LYS ALA ASP GLY VAL LYS SER THR LEU          
SEQRES  22 A  322  GLU ILE TRP ASP ASP MET ILE HIS VAL TRP HIS ALA PHE          
SEQRES  23 A  322  HIS PRO MET LEU PRO GLU GLY LYS GLN ALA ILE VAL ARG          
SEQRES  24 A  322  VAL GLY GLU PHE MET ARG GLU GLN TRP ALA ALA LEU ALA          
SEQRES  25 A  322  ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS                      
FORMUL   2  HOH   *28(H2 O)                                                     
HELIX    1   1 GLY A    3  ALA A   17  1                                  15    
HELIX    2   2 PRO A   25  ALA A   37  1                                  13    
HELIX    3   3 SER A   82  GLN A   98  1                                  17    
HELIX    4   4 PRO A  115  GLN A  131  1                                  17    
HELIX    5   5 LYS A  134  GLN A  136  5                                   3    
HELIX    6   6 SER A  144  GLN A  160  1                                  17    
HELIX    7   7 ASP A  182  ARG A  187  1                                   6    
HELIX    8   8 ALA A  188  ASP A  191  5                                   4    
HELIX    9   9 GLY A  198  ASN A  208  1                                  11    
HELIX   10  10 SER A  218  ALA A  222  5                                   5    
HELIX   11  11 LEU A  240  ASP A  254  1                                  15    
HELIX   12  12 VAL A  269  HIS A  274  5                                   6    
HELIX   13  13 LEU A  277  ALA A  297  1                                  21    
SHEET    1   A 6 GLN A  45  VAL A  51  0                                        
SHEET    2   A 6 CYS A  54  ARG A  60 -1  O  CYS A  54   N  VAL A  51           
SHEET    3   A 6 ALA A 100  LEU A 104 -1  O  LEU A 103   N  GLU A  57           
SHEET    4   A 6 ALA A  69  LEU A  73  1  N  ILE A  70   O  LEU A 102           
SHEET    5   A 6 LEU A 138  ASP A 143  1  O  SER A 139   N  LEU A  71           
SHEET    6   A 6 SER A 167  ILE A 171  1  O  ILE A 171   N  GLY A 142           
SHEET    1   B 2 LEU A 230  GLY A 235  0                                        
SHEET    2   B 2 SER A 258  TRP A 263  1  O  THR A 259   N  ILE A 232           
CISPEP   1 ALA A  109    PRO A  110          0         3.10                     
CISPEP   2 PHE A  114    PRO A  115          0         7.21                     
CRYST1   61.216   61.216  150.445  90.00  90.00  90.00 P 41 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      0.016336  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016336  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006647        0.00000                         
TER    2223      ALA A 297                                                      
MASTER      349    0    0   13    8    0    0    6 2250    1    0   25          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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