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LongText Report for: 6fz9-pdb

Name Class
6fz9-pdb
HEADER    HYDROLASE                               14-MAR-18   6FZ9              
TITLE     CRYSTAL STRUCTURE OF LIPASE FROM GEOBACILLUS STEAROTHERMOPHILUS T6    
TITLE    2 METHANOL STABLE VARIANT A187F/L360F                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;                 
SOURCE   3 ORGANISM_TAXID: 1422;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    LIPASE, METHANOL, ORGANIC SOLVENT, HYDROLASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.GIHAZ,M.KANTEEV,Y.PAZY,A.FISHMAN                                    
REVDAT   1   17-OCT-18 6FZ9    0                                                
JRNL        AUTH   S.GIHAZ,M.KANTEEV,Y.PAZY,A.FISHMAN                           
JRNL        TITL   FILLING THE VOID: INTRODUCING AROMATIC INTERACTIONS INTO     
JRNL        TITL 2 SOLVENT TUNNELS TOWARDS LIPASE STABILITY IN METHANOL.        
JRNL        REF    APPL. ENVIRON. MICROBIOL.                  2018              
JRNL        REFN                   ESSN 1098-5336                               
JRNL        PMID   30217852                                                     
JRNL        DOI    10.1128/AEM.02143-18                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.72                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 113090                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.159                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.177                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5732                            
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 45.7458 -  3.8719    1.00     3884   177  0.1710 0.2128        
REMARK   3     2  3.8719 -  3.0734    1.00     3695   218  0.1711 0.1830        
REMARK   3     3  3.0734 -  2.6850    1.00     3663   194  0.1817 0.1895        
REMARK   3     4  2.6850 -  2.4395    1.00     3651   179  0.1722 0.1667        
REMARK   3     5  2.4395 -  2.2646    1.00     3594   213  0.1508 0.1713        
REMARK   3     6  2.2646 -  2.1311    1.00     3619   189  0.1470 0.1663        
REMARK   3     7  2.1311 -  2.0244    1.00     3590   201  0.1479 0.1728        
REMARK   3     8  2.0244 -  1.9363    1.00     3577   202  0.1436 0.1564        
REMARK   3     9  1.9363 -  1.8617    1.00     3608   190  0.1411 0.1441        
REMARK   3    10  1.8617 -  1.7975    1.00     3610   172  0.1423 0.1568        
REMARK   3    11  1.7975 -  1.7413    1.00     3568   187  0.1388 0.1373        
REMARK   3    12  1.7413 -  1.6915    1.00     3595   207  0.1387 0.1423        
REMARK   3    13  1.6915 -  1.6470    1.00     3580   182  0.1351 0.1386        
REMARK   3    14  1.6470 -  1.6068    1.00     3529   204  0.1376 0.1793        
REMARK   3    15  1.6068 -  1.5703    1.00     3604   184  0.1381 0.1811        
REMARK   3    16  1.5703 -  1.5368    1.00     3566   194  0.1364 0.1722        
REMARK   3    17  1.5368 -  1.5061    1.00     3547   190  0.1355 0.1802        
REMARK   3    18  1.5061 -  1.4777    1.00     3575   179  0.1364 0.1664        
REMARK   3    19  1.4777 -  1.4513    1.00     3575   188  0.1415 0.1781        
REMARK   3    20  1.4513 -  1.4267    1.00     3507   187  0.1459 0.1872        
REMARK   3    21  1.4267 -  1.4037    1.00     3587   205  0.1484 0.1651        
REMARK   3    22  1.4037 -  1.3821    1.00     3526   198  0.1512 0.1944        
REMARK   3    23  1.3821 -  1.3617    1.00     3554   189  0.1495 0.1774        
REMARK   3    24  1.3617 -  1.3426    1.00     3585   191  0.1542 0.1715        
REMARK   3    25  1.3426 -  1.3244    1.00     3551   190  0.1606 0.1822        
REMARK   3    26  1.3244 -  1.3072    1.00     3563   193  0.1586 0.1815        
REMARK   3    27  1.3072 -  1.2909    1.00     3546   178  0.1653 0.2076        
REMARK   3    28  1.2909 -  1.2753    0.99     3487   193  0.1773 0.1975        
REMARK   3    29  1.2753 -  1.2605    0.98     3489   187  0.1922 0.2133        
REMARK   3    30  1.2605 -  1.2463    0.95     3333   171  0.2069 0.2317        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.100            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.020           
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.027           3208                                  
REMARK   3   ANGLE     :  1.646           4361                                  
REMARK   3   CHIRALITY :  0.126            450                                  
REMARK   3   PLANARITY :  0.009            573                                  
REMARK   3   DIHEDRAL  : 13.718           1135                                  
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 6FZ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009173.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-OCT-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.975997                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 113094                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.246                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.715                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4X6U                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CITRATE, 25% PEG 3350,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
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       24.98000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.66500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.63000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.66500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.98000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.63000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2                            
REMARK 350 SURFACE AREA OF THE COMPLEX: 15480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   504     O    HOH A   796              1.74            
REMARK 500   O    HOH A   815     O    HOH A   818              1.87            
REMARK 500   O    HOH A   634     O    HOH A   723              1.96            
REMARK 500   O    HOH A   777     O    HOH A   887              1.98            
REMARK 500   O    HOH A   933     O    HOH A   935              1.98            
REMARK 500   O    HOH A   758     O    HOH A   887              2.04            
REMARK 500   O    HOH A   896     O    HOH A   905              2.05            
REMARK 500   O    HOH A   796     O    HOH A   813              2.07            
REMARK 500   O    HOH A   506     O    HOH A   823              2.10            
REMARK 500   O    HOH A   834     O    HOH A   870              2.11            
REMARK 500   O    HOH A   508     O    HOH A   794              2.13            
REMARK 500   O    HOH A   702     O    HOH A   728              2.15            
REMARK 500   O    HOH A   834     O    HOH A   892              2.15            
REMARK 500   ND1  HIS A   393     O    HOH A   501              2.15            
REMARK 500   O    HOH A   675     O    HOH A   758              2.15            
REMARK 500   O    HOH A   804     O    HOH A   869              2.18            
REMARK 500   O    HOH A   504     O    HOH A   816              2.18            
REMARK 500   O    HOH A   926     O    HOH A   952              2.19            
REMARK 500   O    HOH A   501     O    HOH A   826              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 114     -134.51     55.95                                   
REMARK 500    VAL A 204      -57.92     67.55                                   
REMARK 500    LEU A 209       35.20    -94.51                                   
REMARK 500    ARG A 272       44.99   -147.48                                   
REMARK 500    ILE A 320      -45.05   -135.95                                   
REMARK 500    LYS A 330      -51.29   -130.26                                   
REMARK 500    ASN A 368       89.65   -166.34                                   
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 950        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A 951        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH A 952        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH A 953        DISTANCE =  6.72 ANGSTROMS                       
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                              ZN A 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  62   OD1                                                    
REMARK 620 2 HIS A  82   NE2 101.3                                              
REMARK 620 3 HIS A  88   NE2 111.5 104.8                                        
REMARK 620 4 ASP A 239   OD2 131.6 107.9  97.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 287   O                                                      
REMARK 620 2 GLU A 361   OE2  87.4                                              
REMARK 620 3 ASP A 366   OD2  98.8 112.6                                        
REMARK 620 4 PRO A 367   O   172.3  92.6  88.2                                  
REMARK 620 5 HOH A 578   O    83.5 169.3  63.4  97.1                            
REMARK 620 6 HOH A 820   O    89.8  95.5 150.8  82.6  90.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4X6U   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6FZ1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6FZ7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6FZ8   RELATED DB: PDB                                   
DBREF  6FZ9 A    4   389  UNP    Q93A71   Q93A71_GEOSE    33    418             
SEQADV 6FZ9 PHE A  187  UNP  Q93A71    ALA   216 ENGINEERED MUTATION            
SEQADV 6FZ9 ALA A  323  UNP  Q93A71    THR   352 CONFLICT                       
SEQADV 6FZ9 PHE A  360  UNP  Q93A71    LEU   389 ENGINEERED MUTATION            
SEQADV 6FZ9 HIS A  390  UNP  Q93A71              EXPRESSION TAG                 
SEQADV 6FZ9 HIS A  391  UNP  Q93A71              EXPRESSION TAG                 
SEQADV 6FZ9 HIS A  392  UNP  Q93A71              EXPRESSION TAG                 
SEQADV 6FZ9 HIS A  393  UNP  Q93A71              EXPRESSION TAG                 
SEQADV 6FZ9 HIS A  394  UNP  Q93A71              EXPRESSION TAG                 
SEQADV 6FZ9 HIS A  395  UNP  Q93A71              EXPRESSION TAG                 
SEQRES   1 A  392  SER ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS GLY          
SEQRES   2 A  392  PHE THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE LYS          
SEQRES   3 A  392  TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP LEU          
SEQRES   4 A  392  ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL GLY          
SEQRES   5 A  392  PRO LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA TYR          
SEQRES   6 A  392  ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA ALA          
SEQRES   7 A  392  HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG THR          
SEQRES   8 A  392  TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY ARG          
SEQRES   9 A  392  ILE HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR ALA          
SEQRES  10 A  392  ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN GLU          
SEQRES  11 A  392  GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU SER          
SEQRES  12 A  392  PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER VAL          
SEQRES  13 A  392  THR THR ILE ALA THR PRO HIS ASP GLY THR THR LEU VAL          
SEQRES  14 A  392  ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU GLN          
SEQRES  15 A  392  LYS PHE VAL LEU LYS ALA ALA ALA VAL ALA SER ASN VAL          
SEQRES  16 A  392  PRO TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP GLN          
SEQRES  17 A  392  TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP GLN          
SEQRES  18 A  392  TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR SER          
SEQRES  19 A  392  THR ASP THR ALA ARG TYR ASP LEU SER VAL PRO GLY ALA          
SEQRES  20 A  392  GLU LYS LEU ASN GLN TRP VAL LYS ALA SER PRO ASN THR          
SEQRES  21 A  392  TYR TYR LEU SER PHE ALA THR GLU ARG THR TYR ARG GLY          
SEQRES  22 A  392  ALA LEU THR GLY ASN TYR TYR PRO GLU LEU GLY MET ASN          
SEQRES  23 A  392  ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY SER          
SEQRES  24 A  392  TYR ARG ASN ALA THR LEU GLY ILE ASP ASP ARG TRP LEU          
SEQRES  25 A  392  GLU ASN ASP GLY ILE VAL ASN ALA PHE SER MET ASN GLY          
SEQRES  26 A  392  PRO LYS ARG GLY SER THR ASP ARG ILE VAL PRO TYR ASP          
SEQRES  27 A  392  GLY THR ILE LYS LYS GLY VAL TRP ASN ASP MET GLY THR          
SEQRES  28 A  392  TYR ASN VAL ASP HIS PHE GLU VAL ILE GLY VAL ASP PRO          
SEQRES  29 A  392  ASN PRO LEU PHE ASP ILE ARG ALA PHE TYR LEU ARG LEU          
SEQRES  30 A  392  ALA GLU GLN LEU ALA SER LEU GLN PRO HIS HIS HIS HIS          
SEQRES  31 A  392  HIS HIS                                                      
HET     CA  A 401       1                                                       
HET     ZN  A 402       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      ZN ZINC ION                                                         
FORMUL   2   CA    CA 2+                                                        
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4  HOH   *453(H2 O)                                                    
HELIX    1 AA1 GLU A   24  PHE A   28  5                                   5    
HELIX    2 AA2 GLY A   32  GLY A   36  5                                   5    
HELIX    3 AA3 ASP A   37  ASN A   45  1                                   9    
HELIX    4 AA4 SER A   59  GLY A   73  1                                  15    
HELIX    5 AA5 GLY A   79  GLY A   87  1                                   9    
HELIX    6 AA6 LEU A   99  GLY A  105  5                                   7    
HELIX    7 AA7 GLN A  115  GLY A  130  1                                  16    
HELIX    8 AA8 SER A  131  ASN A  142  1                                  12    
HELIX    9 AA9 SER A  146  GLU A  150  5                                   5    
HELIX   10 AB1 THR A  169  MET A  174  5                                   6    
HELIX   11 AB2 ASP A  176  ALA A  192  1                                  17    
HELIX   12 AB3 LEU A  209  GLY A  213  5                                   5    
HELIX   13 AB4 SER A  221  ARG A  231  1                                  11    
HELIX   14 AB5 SER A  232  SER A  237  1                                   6    
HELIX   15 AB6 THR A  240  SER A  246  1                                   7    
HELIX   16 AB7 SER A  246  GLN A  255  1                                  10    
HELIX   17 AB8 ASN A  289  CYS A  296  1                                   8    
HELIX   18 AB9 CYS A  296  GLY A  301  1                                   6    
HELIX   19 AC1 ASP A  311  LEU A  315  5                                   5    
HELIX   20 AC2 ASN A  322  MET A  326  5                                   5    
HELIX   21 AC3 ASP A  372  SER A  386  1                                  15    
SHEET    1 AA1 7 THR A  49  LEU A  52  0                                        
SHEET    2 AA1 7 ILE A  11  LEU A  14  1  N  ILE A  11   O  TYR A  50           
SHEET    3 AA1 7 ILE A 108  HIS A 113  1  O  ILE A 111   N  VAL A  12           
SHEET    4 AA1 7 VAL A 156  ILE A 162  1  O  THR A 160   N  ALA A 112           
SHEET    5 AA1 7 TYR A 264  THR A 270  1  O  LEU A 266   N  VAL A 159           
SHEET    6 AA1 7 TRP A 349  TYR A 355  1  O  MET A 352   N  SER A 267           
SHEET    7 AA1 7 ILE A 337  PRO A 339  1  N  VAL A 338   O  TRP A 349           
SHEET    1 AA2 2 GLY A  74  ASP A  77  0                                        
SHEET    2 AA2 2 PHE A  91  TYR A  95 -1  O  ARG A  93   N  VAL A  76           
SHEET    1 AA3 2 THR A 273  ARG A 275  0                                        
SHEET    2 AA3 2 TYR A 282  PRO A 284 -1  O  TYR A 283   N  TYR A 274           
LINK         OD1 ASP A  62                ZN    ZN A 402     1555   1555  1.99  
LINK         NE2 HIS A  82                ZN    ZN A 402     1555   1555  2.03  
LINK         NE2 HIS A  88                ZN    ZN A 402     1555   1555  2.13  
LINK         OD2 ASP A 239                ZN    ZN A 402     1555   1555  2.00  
LINK         O   GLY A 287                CA    CA A 401     1555   1555  2.25  
LINK         OE2 GLU A 361                CA    CA A 401     1555   1555  2.29  
LINK         OD2 ASP A 366                CA    CA A 401     1555   1555  2.60  
LINK         O   PRO A 367                CA    CA A 401     1555   1555  2.41  
LINK        CA    CA A 401                 O   HOH A 578     1555   1555  2.57  
LINK        CA    CA A 401                 O   HOH A 820     1555   1555  2.64  
SITE     1 AC1  6 GLY A 287  GLU A 361  ASP A 366  PRO A 367                    
SITE     2 AC1  6 HOH A 578  HOH A 820                                          
SITE     1 AC2  4 ASP A  62  HIS A  82  HIS A  88  ASP A 239                    
CRYST1   49.960   71.260  113.330  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020016  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014033  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008824        0.00000                         
TER    3117      HIS A 395                                                      
MASTER      328    0    2   21   11    0    3    6 3571    1   13   31          
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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