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LongText Report for: 4X85-pdb

Name Class
4X85-pdb
HEADER    HYDROLASE                               10-DEC-14   4X85              
TITLE     CRYSTAL STRUCTURE OF LIPASE FROM GEOBACILLUS STEAROTHERMOPHILUS T6    
TITLE    2 METHANOL STABLE VARIANT H86Y/A269T/R374W                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.1.3;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS T6;              
SOURCE   3 ORGANISM_TAXID: 646309;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET9A                                     
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KANTEEV,A.DROR,S.GIHAZ,A.FISHMAN                                    
REVDAT   1   10-JUN-15 4X85    0                                                
JRNL        AUTH   A.DROR,M.KANTEEV,I.KAGAN,S.GIHAZ,A.SHAHAR,A.FISHMAN          
JRNL        TITL   STRUCTURAL INSIGHTS INTO METHANOL-STABLE VARIANTS OF LIPASE  
JRNL        TITL 2 T6 FROM GEOBACILLUS STEAROTHERMOPHILUS.                      
JRNL        REF    APPL.MICROBIOL.BIOTECHNOL.                 2015              
JRNL        REFN                   ESSN 1432-0614                               
JRNL        PMID   26026940                                                     
JRNL        DOI    10.1007/S00253-015-6700-4                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.85                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20085                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.230                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1050                            
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 24.8496 -  4.3765    0.94     2528   128  0.1827 0.2006        
REMARK   3     2  4.3765 -  3.4768    0.94     2426   124  0.1719 0.1988        
REMARK   3     3  3.4768 -  3.0382    0.94     2341   168  0.2015 0.2338        
REMARK   3     4  3.0382 -  2.7608    0.95     2367   148  0.2187 0.2386        
REMARK   3     5  2.7608 -  2.5631    0.94     2366   127  0.2285 0.2746        
REMARK   3     6  2.5631 -  2.4121    0.94     2365   117  0.2325 0.2816        
REMARK   3     7  2.4121 -  2.2914    0.94     2336   118  0.2229 0.2528        
REMARK   3     8  2.2914 -  2.1917    0.92     2306   120  0.2414 0.3213        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.11                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 35.39                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.960           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.84380                                             
REMARK   3    B22 (A**2) : -4.74040                                             
REMARK   3    B33 (A**2) : 7.58410                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.020           3210                                  
REMARK   3   ANGLE     :  1.291           4375                                  
REMARK   3   CHIRALITY :  0.084            451                                  
REMARK   3   PLANARITY :  0.006            570                                  
REMARK   3   DIHEDRAL  : 13.524           1130                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 5:86)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  19.4746  -8.3861 -17.5857              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1551 T22:   0.1798                                     
REMARK   3      T33:   0.1710 T12:  -0.0411                                     
REMARK   3      T13:   0.0018 T23:   0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2185 L22:   0.2728                                     
REMARK   3      L33:   0.1488 L12:  -0.3183                                     
REMARK   3      L13:   0.2202 L23:  -0.1615                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0349 S12:   0.0464 S13:   0.0019                       
REMARK   3      S21:  -0.0418 S22:  -0.1665 S23:  -0.1505                       
REMARK   3      S31:   0.0165 S32:   0.1179 S33:  -0.0325                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 87:107)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9782 -17.5155 -13.0059              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2533 T22:   0.2809                                     
REMARK   3      T33:   0.2878 T12:   0.0128                                     
REMARK   3      T13:   0.0020 T23:   0.0497                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1786 L22:   0.2485                                     
REMARK   3      L33:   0.3611 L12:  -0.0606                                     
REMARK   3      L13:   0.1023 L23:   0.0966                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1062 S12:  -0.2294 S13:   0.1438                       
REMARK   3      S21:   0.0616 S22:  -0.1970 S23:  -0.0881                       
REMARK   3      S31:  -0.2902 S32:  -0.3463 S33:  -0.0193                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 108:149)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  15.1020 -22.9633 -10.5067              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1630 T22:   0.1479                                     
REMARK   3      T33:   0.1222 T12:  -0.0233                                     
REMARK   3      T13:   0.0199 T23:   0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2236 L22:   0.2609                                     
REMARK   3      L33:  -0.0029 L12:  -0.2519                                     
REMARK   3      L13:   0.1439 L23:  -0.0932                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0820 S12:  -0.0117 S13:  -0.1707                       
REMARK   3      S21:  -0.0974 S22:   0.0338 S23:   0.1649                       
REMARK   3      S31:   0.0789 S32:  -0.0397 S33:  -0.0113                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 150:212)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  11.8221 -10.7945 -26.6709              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1673 T22:   0.1616                                     
REMARK   3      T33:   0.1169 T12:  -0.0029                                     
REMARK   3      T13:  -0.0006 T23:   0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0539 L22:   0.5846                                     
REMARK   3      L33:   0.1557 L12:   0.1439                                     
REMARK   3      L13:   0.0362 L23:   0.1015                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0124 S12:   0.0581 S13:   0.0897                       
REMARK   3      S21:  -0.0163 S22:  -0.0080 S23:  -0.0222                       
REMARK   3      S31:   0.0077 S32:   0.0274 S33:   0.0034                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 213:254)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6122 -18.5295 -31.1392              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1594 T22:   0.1830                                     
REMARK   3      T33:   0.1738 T12:  -0.0168                                     
REMARK   3      T13:   0.0167 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1077 L22:   0.2281                                     
REMARK   3      L33:   0.2658 L12:   0.0287                                     
REMARK   3      L13:   0.0328 L23:   0.1482                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0474 S12:  -0.0897 S13:  -0.1073                       
REMARK   3      S21:  -0.0173 S22:  -0.0314 S23:   0.0119                       
REMARK   3      S31:   0.1326 S32:   0.0581 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 255:360)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.2719  -5.1720 -16.1502              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1808 T22:   0.1712                                     
REMARK   3      T33:   0.2000 T12:  -0.0037                                     
REMARK   3      T13:   0.0173 T23:   0.0096                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5084 L22:   0.9909                                     
REMARK   3      L33:   0.3179 L12:  -0.0132                                     
REMARK   3      L13:   0.1993 L23:  -0.1036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0463 S12:   0.0088 S13:   0.0536                       
REMARK   3      S21:   0.1137 S22:  -0.0409 S23:   0.1617                       
REMARK   3      S31:   0.0063 S32:   0.0227 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 361:395)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9100   3.3134  -7.4772              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2568 T22:   0.1686                                     
REMARK   3      T33:   0.1953 T12:  -0.0123                                     
REMARK   3      T13:  -0.0229 T23:  -0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4760 L22:   0.2148                                     
REMARK   3      L33:   0.3598 L12:   0.0712                                     
REMARK   3      L13:  -0.0674 L23:   0.2765                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0348 S12:   0.0648 S13:   0.0381                       
REMARK   3      S21:   0.2288 S22:   0.1533 S23:   0.0101                       
REMARK   3      S31:  -0.0238 S32:  -0.0359 S33:   0.0012                       
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 4X85 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000205233.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.56                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69491                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.3.0                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CITRATE , 25% PEG3350,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
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       24.84800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.78200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.69550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.78200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.84800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.69550            
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
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: 15470 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: 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    LYS A 103       34.39    -79.83                                   
REMARK 500    ARG A 104       37.55   -164.80                                   
REMARK 500    SER A 114     -139.01     58.80                                   
REMARK 500    VAL A 204      -57.87     69.00                                   
REMARK 500    LEU A 209       38.00    -87.97                                   
REMARK 500    ARG A 272       47.75   -146.55                                   
REMARK 500    ASP A 311     -163.53   -118.00                                   
REMARK 500    ILE A 320      -43.31   -135.01                                   
REMARK 500    LYS A 330      -50.31   -137.39                                   
REMARK 500    ASP A 351       99.20    -63.81                                   
REMARK 500    HIS A 359      -72.36    -28.94                                   
REMARK 500    ASN A 368       89.94   -161.46                                   
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 737        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH A 754        DISTANCE =  5.95 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 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  62   OD1                                                    
REMARK 620 2 ASP A  62   OD2  54.2                                              
REMARK 620 3 HIS A  82   NE2  98.7 152.8                                        
REMARK 620 4 HIS A  88   NE2 116.7  91.3 104.5                                  
REMARK 620 5 ASP A 239   OD1 100.1 102.3  79.0 141.5                            
REMARK 620 6 ASP A 239   OD2 137.0  92.7 109.7  87.1  56.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 287   O                                                      
REMARK 620 2 GLU A 361   OE2  89.9                                              
REMARK 620 3 ASP A 366   OD2 102.9 103.5                                        
REMARK 620 4 PRO A 367   O   167.7  96.2  86.1                                  
REMARK 620 5 HOH A 616   O    82.4 158.4  59.3  95.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402                  
DBREF  4X85 A    5   389  UNP    Q93A71   Q93A71_GEOSE    34    418             
SEQADV 4X85 TYR A   86  UNP  Q93A71    HIS   115 ENGINEERED MUTATION            
SEQADV 4X85 THR A  269  UNP  Q93A71    ALA   298 ENGINEERED MUTATION            
SEQADV 4X85 ALA A  323  UNP  Q93A71    THR   352 CONFLICT                       
SEQADV 4X85 TRP A  374  UNP  Q93A71    ARG   403 ENGINEERED MUTATION            
SEQADV 4X85 HIS A  390  UNP  Q93A71              EXPRESSION TAG                 
SEQADV 4X85 HIS A  391  UNP  Q93A71              EXPRESSION TAG                 
SEQADV 4X85 HIS A  392  UNP  Q93A71              EXPRESSION TAG                 
SEQADV 4X85 HIS A  393  UNP  Q93A71              EXPRESSION TAG                 
SEQADV 4X85 HIS A  394  UNP  Q93A71              EXPRESSION TAG                 
SEQADV 4X85 HIS A  395  UNP  Q93A71              EXPRESSION TAG                 
SEQRES   1 A  391  ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS GLY PHE          
SEQRES   2 A  391  THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE LYS TYR          
SEQRES   3 A  391  TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP LEU ASN          
SEQRES   4 A  391  ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL GLY PRO          
SEQRES   5 A  391  LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA TYR ALA          
SEQRES   6 A  391  GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA ALA HIS          
SEQRES   7 A  391  ALA ALA LYS TYR GLY HIS ALA ARG PHE GLY ARG THR TYR          
SEQRES   8 A  391  PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY ARG ILE          
SEQRES   9 A  391  HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR ALA ARG          
SEQRES  10 A  391  MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN GLU GLU          
SEQRES  11 A  391  ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU SER PRO          
SEQRES  12 A  391  LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER VAL THR          
SEQRES  13 A  391  THR ILE ALA THR PRO HIS ASP GLY THR THR LEU VAL ASN          
SEQRES  14 A  391  MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU GLN LYS          
SEQRES  15 A  391  ALA VAL LEU LYS ALA ALA ALA VAL ALA SER ASN VAL PRO          
SEQRES  16 A  391  TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP GLN TRP          
SEQRES  17 A  391  GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP GLN TYR          
SEQRES  18 A  391  PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR SER THR          
SEQRES  19 A  391  ASP THR ALA ARG TYR ASP LEU SER VAL PRO GLY ALA GLU          
SEQRES  20 A  391  LYS LEU ASN GLN TRP VAL LYS ALA SER PRO ASN THR TYR          
SEQRES  21 A  391  TYR LEU SER PHE THR THR GLU ARG THR TYR ARG GLY ALA          
SEQRES  22 A  391  LEU THR GLY ASN TYR TYR PRO GLU LEU GLY MET ASN ALA          
SEQRES  23 A  391  PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY SER TYR          
SEQRES  24 A  391  ARG ASN ALA THR LEU GLY ILE ASP ASP ARG TRP LEU GLU          
SEQRES  25 A  391  ASN ASP GLY ILE VAL ASN ALA PHE SER MET ASN GLY PRO          
SEQRES  26 A  391  LYS ARG GLY SER THR ASP ARG ILE VAL PRO TYR ASP GLY          
SEQRES  27 A  391  THR ILE LYS LYS GLY VAL TRP ASN ASP MET GLY THR TYR          
SEQRES  28 A  391  ASN VAL ASP HIS LEU GLU VAL ILE GLY VAL ASP PRO ASN          
SEQRES  29 A  391  PRO LEU PHE ASP ILE TRP ALA PHE TYR LEU ARG LEU ALA          
SEQRES  30 A  391  GLU GLN LEU ALA SER LEU GLN PRO HIS HIS HIS HIS HIS          
SEQRES  31 A  391  HIS                                                          
HET     ZN  A 401       1                                                       
HET     CA  A 402       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *259(H2 O)                                                    
HELIX    1 AA1 GLU A   24  PHE A   28  5                                   5    
HELIX    2 AA2 ASP A   37  ASN A   45  1                                   9    
HELIX    3 AA3 SER A   59  GLY A   73  1                                  15    
HELIX    4 AA4 GLY A   79  GLY A   87  1                                   9    
HELIX    5 AA5 LEU A   99  GLY A  105  5                                   7    
HELIX    6 AA6 GLN A  115  GLY A  130  1                                  16    
HELIX    7 AA7 SER A  131  ASN A  142  1                                  12    
HELIX    8 AA8 SER A  146  GLU A  150  5                                   5    
HELIX    9 AA9 THR A  169  MET A  174  5                                   6    
HELIX   10 AB1 ASP A  176  ALA A  192  1                                  17    
HELIX   11 AB2 LEU A  209  GLY A  213  5                                   5    
HELIX   12 AB3 SER A  221  ARG A  231  1                                  11    
HELIX   13 AB4 SER A  232  SER A  237  1                                   6    
HELIX   14 AB5 THR A  240  SER A  246  1                                   7    
HELIX   15 AB6 SER A  246  GLN A  255  1                                  10    
HELIX   16 AB7 ASN A  289  CYS A  296  1                                   8    
HELIX   17 AB8 CYS A  296  GLY A  301  1                                   6    
HELIX   18 AB9 ASP A  311  LEU A  315  5                                   5    
HELIX   19 AC1 ASN A  322  MET A  326  5                                   5    
HELIX   20 AC2 ASP A  358  VAL A  362  5                                   5    
HELIX   21 AC3 ASP A  372  ALA A  385  1                                  14    
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  HIS A 109   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  PHE A 268   N  THR A 161           
SHEET    6 AA1 7 TRP A 349  TYR A 355  1  O  TYR A 355   N  THR A 269           
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 401     1555   1555  2.05  
LINK         OD2 ASP A  62                ZN    ZN A 401     1555   1555  2.63  
LINK         NE2 HIS A  82                ZN    ZN A 401     1555   1555  2.09  
LINK         NE2 HIS A  88                ZN    ZN A 401     1555   1555  2.14  
LINK         OD1 ASP A 239                ZN    ZN A 401     1555   1555  2.39  
LINK         OD2 ASP A 239                ZN    ZN A 401     1555   1555  2.10  
LINK         O   GLY A 287                CA    CA A 402     1555   1555  2.27  
LINK         OE2 GLU A 361                CA    CA A 402     1555   1555  1.97  
LINK         OD2 ASP A 366                CA    CA A 402     1555   1555  2.46  
LINK         O   PRO A 367                CA    CA A 402     1555   1555  2.38  
LINK        CA    CA A 402                 O   HOH A 616     1555   1555  2.49  
SITE     1 AC1  4 ASP A  62  HIS A  82  HIS A  88  ASP A 239                    
SITE     1 AC2  5 GLY A 287  GLU A 361  ASP A 366  PRO A 367                    
SITE     2 AC2  5 HOH A 616                                                     
CRYST1   49.696   71.391  113.564  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      0.020122  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014007  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008806        0.00000                         
TER    3109      HIS A 395                                                      
MASTER      382    0    2   21   11    0    3    6 3369    1   15   31          
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.
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