Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 7z2v-pdb

Name Class
7z2v-pdb
HEADER    HYDROLASE                               28-FEB-22   7Z2V              
TITLE     FERULIC ACID ESTERASE VARIANT S114A FROM LACTOBACILLUS BUCHNERI       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FERULIC ACID ESTERASE;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.73;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LENTILACTOBACILLUS BUCHNERI;                    
SOURCE   3 ORGANISM_TAXID: 1581;                                                
SOURCE   4 GENE: FAEA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;                               
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 37762;                                      
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: T1;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    FERULIC ACID ESTERASE, LACTOBACILLUS BUCHNERI, MUTANT S114, HYDROLASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.K.MOGODINIYAI,T.REICHENBACH,D.C.KALYANI,M.M.KESKITALO,C.DIVNE       
REVDAT   1   30-NOV-22 7Z2V    0                                                
JRNL        AUTH   K.K.MOGODINIYAI,T.REICHENBACH,D.C.KALYANI,A.JIMENEZ QUERO,   
JRNL        AUTH 2 M.M.KESKITALO,F.VILAPLANA,C.DIVNE                            
JRNL        TITL   FERULIC ACID ESTERASE VARIANT S114A FROM LACTOBACILLUS       
JRNL        TITL 2 BUCHNERI                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.19.2_4158                                   
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) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.14                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 130607                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.177                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.530                           
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 40.1400 -  3.4900    1.00     9851   154  0.1418 0.1513        
REMARK   3     2  3.4900 -  2.7700    1.00     9439   146  0.1619 0.1626        
REMARK   3     3  2.7700 -  2.4200    1.00     9312   145  0.1664 0.1681        
REMARK   3     4  2.4200 -  2.2000    1.00     9286   144  0.1668 0.1762        
REMARK   3     5  2.2000 -  2.0400    1.00     9229   143  0.1610 0.1968        
REMARK   3     6  2.0400 -  1.9200    1.00     9208   144  0.1645 0.1802        
REMARK   3     7  1.9200 -  1.8300    1.00     9157   142  0.1744 0.1902        
REMARK   3     8  1.8300 -  1.7500    1.00     9177   143  0.1765 0.1779        
REMARK   3     9  1.7500 -  1.6800    1.00     9142   142  0.1752 0.1957        
REMARK   3    10  1.6800 -  1.6200    1.00     9122   142  0.1891 0.2068        
REMARK   3    11  1.6200 -  1.5700    1.00     9067   141  0.2144 0.2341        
REMARK   3    12  1.5700 -  1.5300    1.00     9129   142  0.2527 0.2836        
REMARK   3    13  1.5300 -  1.4900    0.99     8973   139  0.2925 0.2968        
REMARK   3    14  1.4900 -  1.4500    0.94     8515   133  0.3385 0.3354        
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)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.490           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.76                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.15                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
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 7Z2V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-FEB-22.                  
REMARK 100 THE DEPOSITION ID IS D_1292121410.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-20                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97629                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER2 XE 16M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 130627                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.410                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 22.50                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 25.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
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         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: L. BUCHNERI FAE                                      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE PH 6.5, 0.2 M    
REMARK 280  CALCIUM ACETATE, 18% PEG8000, VAPOR DIFFUSION, SITTING DROP,        
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
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      113.97000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       39.98000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       39.98000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      170.95500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       39.98000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       39.98000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       56.98500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       39.98000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       39.98000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      170.95500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       39.98000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       39.98000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       56.98500            
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      113.97000            
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     GLY A   -12                                                      
REMARK 465     VAL A   -11                                                      
REMARK 465     ASP A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     THR A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     ASN A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     LYS A   260                                                      
REMARK 465     MET B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     GLY B   -12                                                      
REMARK 465     VAL B   -11                                                      
REMARK 465     ASP B   -10                                                      
REMARK 465     LEU B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     THR B    -7                                                      
REMARK 465     GLU B    -6                                                      
REMARK 465     ASN B    -5                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     ALA B   259                                                      
REMARK 465     LYS B   260                                                      
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    GLU A  44     -175.31     54.86                                   
REMARK 500    ALA A 114     -123.57     61.55                                   
REMARK 500    ARG A 127       57.63   -118.24                                   
REMARK 500    ALA A 140       49.72    -89.94                                   
REMARK 500    GLN A 236       40.05   -107.58                                   
REMARK 500    GLU B  44     -175.11     55.96                                   
REMARK 500    ALA B 114     -126.33     63.07                                   
REMARK 500    ALA B 140       46.99    -89.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 302  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A  -1   OE1                                                    
REMARK 620 2 ASP A  22   OD1  71.6                                              
REMARK 620 3 ASP A  22   OD2  90.2  49.0                                        
REMARK 620 4 HOH A 406   O    63.4  63.7 112.6                                  
REMARK 620 5 HOH A 590   O   146.4  78.5  81.2  90.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  13   OG1                                                    
REMARK 620 2 ASP A  75   OD2  76.6                                              
REMARK 620 3 HOH A 462   O    73.6  86.3                                        
REMARK 620 4 HOH A 483   O   106.9  76.8 162.3                                  
REMARK 620 5 HOH A 514   O    72.2 140.2  61.8 135.8                            
REMARK 620 6 HOH A 579   O    73.9 131.1 120.5  75.6  61.4                      
REMARK 620 7 HOH A 601   O   147.8  77.8  85.6  85.6 119.2 138.3                
REMARK 620 8 HOH A 691   O   142.0 141.4 103.0  87.4  73.2  76.1  66.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 305  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 218   O                                                      
REMARK 620 2 HOH A 418   O    33.5                                              
REMARK 620 3 HOH A 609   O    37.2   4.2                                        
REMARK 620 4 HOH A 611   O    33.4   3.0   4.0                                  
REMARK 620 5 GLU B   8   O    34.3   2.8   3.1   0.9                            
REMARK 620 6 HOH B 535   O    36.2   4.7   2.4   2.9   2.2                      
REMARK 620 7 HOH B 603   O    36.4   2.9   1.8   4.1   3.3   3.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 302  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN B  -1   OE1                                                    
REMARK 620 2 ASP B  22   OD1  74.0                                              
REMARK 620 3 ASP B  22   OD2  82.9  50.9                                        
REMARK 620 4 HOH B 553   O    77.6  75.6 126.2                                  
REMARK 620 5 HOH B 615   O   148.7  76.1  85.5  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  13   OG1                                                    
REMARK 620 2 ASP B  75   OD2  77.5                                              
REMARK 620 3 HOH B 482   O   108.6  77.4                                        
REMARK 620 4 HOH B 516   O    71.4  87.6 164.4                                  
REMARK 620 5 HOH B 557   O    74.0 129.7  73.7 120.0                            
REMARK 620 6 HOH B 569   O   147.1  78.4  87.4  85.6 138.8                      
REMARK 620 7 HOH B 610   O    81.9 151.7 128.2  67.3  60.5 111.1                
REMARK 620 8 HOH B 658   O   140.4 142.1  85.4 104.5  75.0  67.2  61.4          
REMARK 620 N                    1     2     3     4     5     6     7           
DBREF  7Z2V A    1   260  UNP    D7RU28   D7RU28_LENBU     1    260             
DBREF  7Z2V B    1   260  UNP    D7RU28   D7RU28_LENBU     1    260             
SEQADV 7Z2V MET A  -21  UNP  D7RU28              INITIATING METHIONINE          
SEQADV 7Z2V HIS A  -20  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V HIS A  -19  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V HIS A  -18  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V HIS A  -17  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V HIS A  -16  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V HIS A  -15  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V SER A  -14  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V SER A  -13  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V GLY A  -12  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V VAL A  -11  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V ASP A  -10  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V LEU A   -9  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V GLY A   -8  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V THR A   -7  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V GLU A   -6  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V ASN A   -5  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V LEU A   -4  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V TYR A   -3  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V PHE A   -2  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V GLN A   -1  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V SER A    0  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V ALA A  114  UNP  D7RU28    SER   114 ENGINEERED MUTATION            
SEQADV 7Z2V MET B  -21  UNP  D7RU28              INITIATING METHIONINE          
SEQADV 7Z2V HIS B  -20  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V HIS B  -19  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V HIS B  -18  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V HIS B  -17  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V HIS B  -16  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V HIS B  -15  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V SER B  -14  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V SER B  -13  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V GLY B  -12  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V VAL B  -11  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V ASP B  -10  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V LEU B   -9  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V GLY B   -8  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V THR B   -7  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V GLU B   -6  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V ASN B   -5  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V LEU B   -4  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V TYR B   -3  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V PHE B   -2  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V GLN B   -1  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V SER B    0  UNP  D7RU28              EXPRESSION TAG                 
SEQADV 7Z2V ALA B  114  UNP  D7RU28    SER   114 ENGINEERED MUTATION            
SEQRES   1 A  282  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  282  GLY THR GLU ASN LEU TYR PHE GLN SER MET ILE LYS PHE          
SEQRES   3 A  282  VAL THR THR GLU ILE ASN GLY LEU THR LEU ARG GLY THR          
SEQRES   4 A  282  ALA HIS VAL PRO ASP GLY GLU PRO GLY GLN GLN PHE PRO          
SEQRES   5 A  282  THR VAL LEU MET PHE HIS GLY PHE GLY ALA VAL ARG ASP          
SEQRES   6 A  282  GLU GLY PHE ARG LEU PHE ILE GLN MET SER ASN ARG LEU          
SEQRES   7 A  282  MET GLU ASN GLY ILE ALA ALA VAL ARG PHE ASP PHE GLY          
SEQRES   8 A  282  CYS HIS GLY GLU SER ASP GLY GLU PHE GLU ASP PHE THR          
SEQRES   9 A  282  PHE SER GLN GLU LEU ASN GLU GLY SER ALA LEU ILE ASP          
SEQRES  10 A  282  ALA VAL LYS SER MET SER PHE VAL ASP SER THR LYS PHE          
SEQRES  11 A  282  SER LEU LEU GLY GLU ALA LEU GLY SER VAL ALA ALA SER          
SEQRES  12 A  282  ILE VAL ALA GLY LYS ARG SER THR GLU LEU THR SER LEU          
SEQRES  13 A  282  CYS MET TRP SER PRO ALA ALA SER PHE LEU ASP GLU ILE          
SEQRES  14 A  282  LEU ASN ASP HIS THR LEU GLN GLY LYS THR VAL ASP ASN          
SEQRES  15 A  282  VAL GLU LYS ASP GLY TYR PHE ASP PHE TYR GLY LEU LYS          
SEQRES  16 A  282  LEU GLY LYS ALA PHE PHE ASP ASP LEU LYS ASN ILE ASN          
SEQRES  17 A  282  ILE PHE ASP ASN ALA LYS LYS TYR GLN GLY PRO VAL LYS          
SEQRES  18 A  282  ILE VAL TYR GLY THR ASN ASP PHE ILE PRO GLU LYS TYR          
SEQRES  19 A  282  SER HIS LYS TYR MET ASP GLY TYR GLU ASN GLY GLU LEU          
SEQRES  20 A  282  VAL ILE VAL GLN ASP GLY ASP HIS GLY TRP GLN SER VAL          
SEQRES  21 A  282  PRO SER ARG LYS ARG ILE LEU ASP GLU THR MET LYS PHE          
SEQRES  22 A  282  PHE ARG LYS THR LEU LEU GLU ALA LYS                          
SEQRES   1 B  282  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  282  GLY THR GLU ASN LEU TYR PHE GLN SER MET ILE LYS PHE          
SEQRES   3 B  282  VAL THR THR GLU ILE ASN GLY LEU THR LEU ARG GLY THR          
SEQRES   4 B  282  ALA HIS VAL PRO ASP GLY GLU PRO GLY GLN GLN PHE PRO          
SEQRES   5 B  282  THR VAL LEU MET PHE HIS GLY PHE GLY ALA VAL ARG ASP          
SEQRES   6 B  282  GLU GLY PHE ARG LEU PHE ILE GLN MET SER ASN ARG LEU          
SEQRES   7 B  282  MET GLU ASN GLY ILE ALA ALA VAL ARG PHE ASP PHE GLY          
SEQRES   8 B  282  CYS HIS GLY GLU SER ASP GLY GLU PHE GLU ASP PHE THR          
SEQRES   9 B  282  PHE SER GLN GLU LEU ASN GLU GLY SER ALA LEU ILE ASP          
SEQRES  10 B  282  ALA VAL LYS SER MET SER PHE VAL ASP SER THR LYS PHE          
SEQRES  11 B  282  SER LEU LEU GLY GLU ALA LEU GLY SER VAL ALA ALA SER          
SEQRES  12 B  282  ILE VAL ALA GLY LYS ARG SER THR GLU LEU THR SER LEU          
SEQRES  13 B  282  CYS MET TRP SER PRO ALA ALA SER PHE LEU ASP GLU ILE          
SEQRES  14 B  282  LEU ASN ASP HIS THR LEU GLN GLY LYS THR VAL ASP ASN          
SEQRES  15 B  282  VAL GLU LYS ASP GLY TYR PHE ASP PHE TYR GLY LEU LYS          
SEQRES  16 B  282  LEU GLY LYS ALA PHE PHE ASP ASP LEU LYS ASN ILE ASN          
SEQRES  17 B  282  ILE PHE ASP ASN ALA LYS LYS TYR GLN GLY PRO VAL LYS          
SEQRES  18 B  282  ILE VAL TYR GLY THR ASN ASP PHE ILE PRO GLU LYS TYR          
SEQRES  19 B  282  SER HIS LYS TYR MET ASP GLY TYR GLU ASN GLY GLU LEU          
SEQRES  20 B  282  VAL ILE VAL GLN ASP GLY ASP HIS GLY TRP GLN SER VAL          
SEQRES  21 B  282  PRO SER ARG LYS ARG ILE LEU ASP GLU THR MET LYS PHE          
SEQRES  22 B  282  PHE ARG LYS THR LEU LEU GLU ALA LYS                          
HET     CA  A 301       1                                                       
HET     CA  A 302       1                                                       
HET    ACT  A 303       4                                                       
HET     CA  B 301       1                                                       
HET     CA  B 302       1                                                       
HET    ACT  B 303       4                                                       
HET    ACT  B 304       4                                                       
HET     CA  B 305       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACT ACETATE ION                                                      
FORMUL   3   CA    5(CA 2+)                                                     
FORMUL   5  ACT    3(C2 H3 O2 1-)                                               
FORMUL  11  HOH   *575(H2 O)                                                    
HELIX    1 AA1 GLU A   44  PHE A   46  5                                   3    
HELIX    2 AA2 ARG A   47  ASN A   59  1                                  13    
HELIX    3 AA3 GLU A   77  PHE A   81  5                                   5    
HELIX    4 AA4 THR A   82  SER A   99  1                                  18    
HELIX    5 AA5 ALA A  114  ARG A  127  1                                  14    
HELIX    6 AA6 SER A  142  ASP A  150  1                                   9    
HELIX    7 AA7 ASN A  160  GLY A  165  1                                   6    
HELIX    8 AA8 LYS A  176  LEU A  182  1                                   7    
HELIX    9 AA9 LYS A  183  ILE A  185  5                                   3    
HELIX   10 AB1 ILE A  187  LYS A  192  1                                   6    
HELIX   11 AB2 GLU A  210  TYR A  220  1                                  11    
HELIX   12 AB3 SER A  237  LEU A  257  1                                  21    
HELIX   13 AB4 GLU B   44  PHE B   46  5                                   3    
HELIX   14 AB5 ARG B   47  ASN B   59  1                                  13    
HELIX   15 AB6 GLU B   77  PHE B   81  5                                   5    
HELIX   16 AB7 THR B   82  SER B   99  1                                  18    
HELIX   17 AB8 ALA B  114  ARG B  127  1                                  14    
HELIX   18 AB9 SER B  128  LEU B  131  5                                   4    
HELIX   19 AC1 SER B  142  HIS B  151  1                                  10    
HELIX   20 AC2 ASN B  160  GLY B  165  1                                   6    
HELIX   21 AC3 GLY B  175  LEU B  182  1                                   8    
HELIX   22 AC4 LYS B  183  ILE B  185  5                                   3    
HELIX   23 AC5 ILE B  187  LYS B  192  1                                   6    
HELIX   24 AC6 GLU B  210  TYR B  220  1                                  11    
HELIX   25 AC7 SER B  237  LEU B  257  1                                  21    
SHEET    1 AA1 8 MET A   1  ILE A   9  0                                        
SHEET    2 AA1 8 LEU A  12  VAL A  20 -1  O  ALA A  18   N  LYS A   3           
SHEET    3 AA1 8 ALA A  62  PHE A  66 -1  O  ALA A  63   N  HIS A  19           
SHEET    4 AA1 8 PHE A  29  PHE A  35  1  N  MET A  34   O  VAL A  64           
SHEET    5 AA1 8 VAL A 103  GLU A 113  1  O  ASP A 104   N  PHE A  29           
SHEET    6 AA1 8 LEU A 134  TRP A 137  1  O  CYS A 135   N  LEU A 110           
SHEET    7 AA1 8 VAL A 198  GLY A 203  1  O  LYS A 199   N  MET A 136           
SHEET    8 AA1 8 GLY A 223  VAL A 228  1  O  VAL A 226   N  ILE A 200           
SHEET    1 AA2 2 THR A 152  LEU A 153  0                                        
SHEET    2 AA2 2 LYS A 156  THR A 157 -1  O  LYS A 156   N  LEU A 153           
SHEET    1 AA3 2 TYR A 166  PHE A 169  0                                        
SHEET    2 AA3 2 LEU A 172  GLY A 175 -1  O  LEU A 172   N  PHE A 169           
SHEET    1 AA4 8 MET B   1  ILE B   9  0                                        
SHEET    2 AA4 8 LEU B  12  VAL B  20 -1  O  VAL B  20   N  MET B   1           
SHEET    3 AA4 8 ALA B  62  PHE B  66 -1  O  ALA B  63   N  HIS B  19           
SHEET    4 AA4 8 PHE B  29  PHE B  35  1  N  VAL B  32   O  ALA B  62           
SHEET    5 AA4 8 VAL B 103  GLU B 113  1  O  LEU B 111   N  PHE B  35           
SHEET    6 AA4 8 LEU B 134  TRP B 137  1  O  TRP B 137   N  GLY B 112           
SHEET    7 AA4 8 VAL B 198  GLY B 203  1  O  LYS B 199   N  MET B 136           
SHEET    8 AA4 8 GLY B 223  VAL B 228  1  O  VAL B 228   N  TYR B 202           
SHEET    1 AA5 2 THR B 152  LEU B 153  0                                        
SHEET    2 AA5 2 LYS B 156  THR B 157 -1  O  LYS B 156   N  LEU B 153           
SHEET    1 AA6 2 PHE B 167  PHE B 169  0                                        
SHEET    2 AA6 2 LEU B 172  LEU B 174 -1  O  LEU B 174   N  PHE B 167           
LINK         OE1 GLN A  -1                CA    CA A 302     1555   1555  2.55  
LINK         OG1 THR A  13                CA    CA A 301     1555   1555  2.46  
LINK         OD1 ASP A  22                CA    CA A 302     1555   1555  2.88  
LINK         OD2 ASP A  22                CA    CA A 302     1555   1555  2.21  
LINK         OD2 ASP A  75                CA    CA A 301     1555   1555  2.39  
LINK         O   ASP A 218                CA    CA B 305     1555   3554  2.37  
LINK        CA    CA A 301                 O   HOH A 462     1555   1555  2.47  
LINK        CA    CA A 301                 O   HOH A 483     1555   1555  2.41  
LINK        CA    CA A 301                 O   HOH A 514     1555   1555  2.26  
LINK        CA    CA A 301                 O   HOH A 579     1555   1555  2.40  
LINK        CA    CA A 301                 O   HOH A 601     1555   1555  2.36  
LINK        CA    CA A 301                 O   HOH A 691     1555   1555  2.31  
LINK        CA    CA A 302                 O   HOH A 406     1555   1555  2.17  
LINK        CA    CA A 302                 O   HOH A 590     1555   1555  2.32  
LINK         O   HOH A 418                CA    CA B 305     4455   1555  2.42  
LINK         O   HOH A 609                CA    CA B 305     4455   1555  2.48  
LINK         O   HOH A 611                CA    CA B 305     4455   1555  2.20  
LINK         OE1 GLN B  -1                CA    CA B 302     1555   1555  2.45  
LINK         O   GLU B   8                CA    CA B 305     1555   1555  2.30  
LINK         OG1 THR B  13                CA    CA B 301     1555   1555  2.50  
LINK         OD1 ASP B  22                CA    CA B 302     1555   1555  2.75  
LINK         OD2 ASP B  22                CA    CA B 302     1555   1555  2.24  
LINK         OD2 ASP B  75                CA    CA B 301     1555   1555  2.38  
LINK        CA    CA B 301                 O   HOH B 482     1555   1555  2.44  
LINK        CA    CA B 301                 O   HOH B 516     1555   1555  2.38  
LINK        CA    CA B 301                 O   HOH B 557     1555   1555  2.31  
LINK        CA    CA B 301                 O   HOH B 569     1555   1555  2.29  
LINK        CA    CA B 301                 O   HOH B 610     1555   1555  2.32  
LINK        CA    CA B 301                 O   HOH B 658     1555   1555  2.31  
LINK        CA    CA B 302                 O   HOH B 553     1555   1555  2.14  
LINK        CA    CA B 302                 O   HOH B 615     1555   1555  2.43  
LINK        CA    CA B 305                 O   HOH B 535     1555   1555  2.37  
LINK        CA    CA B 305                 O   HOH B 603     1555   1555  2.58  
CRYST1   79.960   79.960  227.940  90.00  90.00  90.00 P 43 21 2    16          
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      0.012506  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012506  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004387        0.00000                         
TER    2103      ALA A 259                                                      
TER    4212      GLU B 258                                                      
MASTER      350    0    8   25   24    0    0    6 4743    2   50   44          
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
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer