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LongText Report for: 5thm-pdb

Name Class
5thm-pdb
HEADER    HYDROLASE                               29-SEP-16   5THM              
TITLE     ESTERASE-6 FROM DROSOPHILA MELANOGASTER                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTERASE-6;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EST-6,CARBOXYLIC-ESTER HYDROLASE 6,CARBOXYLESTERASE-6;      
COMPND   5 EC: 3.1.1.1;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE   4 ORGANISM_TAXID: 7227;                                                
SOURCE   5 GENE: EST-6, EST6, CG6917;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CARBOXYLESTERASE, HYDROLASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.J.FRASER,C.J.JACKSON                                                
REVDAT   1   08-MAR-17 5THM    0                                                
JRNL        AUTH   F.YOUNUS,N.J.FRASER,C.COPPIN,J.W.LIU,T.CHERTEMPS,G.PANDEY,   
JRNL        AUTH 2 M.MAIBECHE-COISNE,R.J.RUSSELL,C.J.JACKSON,J.G.OAKESHOTT      
JRNL        TITL   STRUCTURE AND KINETIC PROPERTIES OF ESTERASE 6, AN ODORANT   
JRNL        TITL 2 DEGRADING ENZYME (ODE) IN DROSOPHILA                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.32                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 31400                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1588                            
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 40.3296 -  4.7792    1.00     2975   166  0.1397 0.1604        
REMARK   3     2  4.7792 -  3.7943    1.00     2862   155  0.1274 0.1561        
REMARK   3     3  3.7943 -  3.3149    1.00     2833   151  0.1551 0.2207        
REMARK   3     4  3.3149 -  3.0120    1.00     2793   153  0.1759 0.2388        
REMARK   3     5  3.0120 -  2.7961    1.00     2795   148  0.1716 0.2355        
REMARK   3     6  2.7961 -  2.6313    1.00     2773   139  0.1710 0.2314        
REMARK   3     7  2.6313 -  2.4996    0.99     2776   139  0.1677 0.2567        
REMARK   3     8  2.4996 -  2.3908    1.00     2767   139  0.1584 0.2140        
REMARK   3     9  2.3908 -  2.2987    0.99     2760   147  0.1542 0.2162        
REMARK   3    10  2.2987 -  2.2194    0.90     2496   127  0.1668 0.3017        
REMARK   3    11  2.2194 -  2.1500    0.72     1982   124  0.1696 0.2318        
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)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.130           
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      :  0.007           4364                                  
REMARK   3   ANGLE     :  0.915           5926                                  
REMARK   3   CHIRALITY :  0.055            603                                  
REMARK   3   PLANARITY :  0.005            776                                  
REMARK   3   DIHEDRAL  : 13.613           2548                                  
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 5THM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217040.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9655                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31402                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.322                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 11.70                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.52                     
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: MOLREP                                                
REMARK 200 STARTING MODEL: 4FNG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M TRIS PH    
REMARK 280  8.5 AND 25 % W/V POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 277.15K                                   
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       33.85650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.51900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.32250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.51900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.85650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.32250            
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: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 20900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     THR A     3                                                      
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   OG   SER A   188    HN11  7BZ A   601              1.42            
REMARK 500   OG   SER A   188     BN1  7BZ A   601              1.99            
REMARK 500   SG   CYS A    65     O    HOH A   960              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 230   NE  -  CZ  -  NH1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG A 230   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
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    ALA A  58       39.57    -98.54                                   
REMARK 500    ASN A  94      113.54   -160.80                                   
REMARK 500    PHE A 144       12.16   -142.28                                   
REMARK 500    SER A 188     -126.17     58.07                                   
REMARK 500    VAL A 222      -81.13    -91.16                                   
REMARK 500    SER A 272     -131.71     57.12                                   
REMARK 500    PHE A 397      -45.32   -133.09                                   
REMARK 500    ASN A 423       84.77   -168.96                                   
REMARK 500    HIS A 445      116.52    -28.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BZ A 601                 
DBREF  5THM A    1   523  UNP    P08171   EST6_DROME      22    544             
SEQADV 5THM MET A   -9  UNP  P08171              INITIATING METHIONINE          
SEQADV 5THM HIS A   -8  UNP  P08171              EXPRESSION TAG                 
SEQADV 5THM HIS A   -7  UNP  P08171              EXPRESSION TAG                 
SEQADV 5THM HIS A   -6  UNP  P08171              EXPRESSION TAG                 
SEQADV 5THM HIS A   -5  UNP  P08171              EXPRESSION TAG                 
SEQADV 5THM HIS A   -4  UNP  P08171              EXPRESSION TAG                 
SEQADV 5THM HIS A   -3  UNP  P08171              EXPRESSION TAG                 
SEQADV 5THM ASP A   -2  UNP  P08171              EXPRESSION TAG                 
SEQADV 5THM HIS A   -1  UNP  P08171              EXPRESSION TAG                 
SEQADV 5THM MET A    0  UNP  P08171              EXPRESSION TAG                 
SEQADV 5THM VAL A   15  UNP  P08171    LYS    36 ENGINEERED MUTATION            
SEQADV 5THM LEU A  145  UNP  P08171    VAL   166 ENGINEERED MUTATION            
SEQADV 5THM MLY A  208  UNP  P08171    ARG   229 ENGINEERED MUTATION            
SEQADV 5THM GLU A  229  UNP  P08171    GLY   250 ENGINEERED MUTATION            
SEQADV 5THM SER A  237  UNP  P08171    ASN   258 ENGINEERED MUTATION            
SEQADV 5THM ALA A  247  UNP  P08171    THR   268 ENGINEERED MUTATION            
SEQADV 5THM GLY A  290  UNP  P08171    ASP   311 ENGINEERED MUTATION            
SEQADV 5THM PHE A  292  UNP  P08171    ILE   313 ENGINEERED MUTATION            
SEQADV 5THM VAL A  335  UNP  P08171    ILE   356 ENGINEERED MUTATION            
SEQADV 5THM GLY A  383  UNP  P08171    GLU   404 ENGINEERED MUTATION            
SEQADV 5THM GLY A  400  UNP  P08171    SER   421 ENGINEERED MUTATION            
SEQADV 5THM VAL A  416  UNP  P08171    ALA   437 ENGINEERED MUTATION            
SEQADV 5THM SER A  450  UNP  P08171    PHE   471 ENGINEERED MUTATION            
SEQADV 5THM SER A  456  UNP  P08171    PHE   477 ENGINEERED MUTATION            
SEQADV 5THM ASP A  485  UNP  P08171    ASN   506 ENGINEERED MUTATION            
SEQADV 5THM THR A  511  UNP  P08171    ILE   532 ENGINEERED MUTATION            
SEQRES   1 A  533  MET HIS HIS HIS HIS HIS HIS ASP HIS MET SER ASP THR          
SEQRES   2 A  533  ASP ASP PRO LEU LEU VAL GLN LEU PRO GLN GLY VAL LEU          
SEQRES   3 A  533  ARG GLY ARG ASP ASN GLY SER TYR TYR SER TYR GLU SER          
SEQRES   4 A  533  ILE PRO TYR ALA GLU PRO PRO THR GLY ASP LEU ARG PHE          
SEQRES   5 A  533  GLU ALA PRO GLU PRO TYR MLY GLN MLY TRP SER ASP ILE          
SEQRES   6 A  533  PHE ASP ALA THR MLY THR PRO VAL ALA CYS LEU GLN TRP          
SEQRES   7 A  533  ASP GLN PHE THR PRO GLY ALA ASN MLY LEU VAL GLY GLU          
SEQRES   8 A  533  GLU ASP CYS LEU THR VAL SER VAL TYR MLY PRO MLY ASN          
SEQRES   9 A  533  SER MLY ARG ASN SER PHE PRO VAL VAL ALA HIS ILE HIS          
SEQRES  10 A  533  GLY GLY ALA PHE MET PHE GLY ALA ALA TRP GLN ASN GLY          
SEQRES  11 A  533  HIS GLU ASN VAL MET ARG GLU GLY MLY PHE ILE LEU VAL          
SEQRES  12 A  533  LYS ILE SER TYR ARG LEU GLY PRO LEU GLY PHE LEU SER          
SEQRES  13 A  533  THR GLY ASP ARG ASP LEU PRO GLY ASN TYR GLY LEU LYS          
SEQRES  14 A  533  ASP GLN ARG LEU ALA LEU MLY TRP ILE MLY GLN ASN ILE          
SEQRES  15 A  533  ALA SER PHE GLY GLY GLU PRO GLN ASN VAL LEU LEU VAL          
SEQRES  16 A  533  GLY HIS SER ALA GLY GLY ALA SER VAL HIS LEU GLN MET          
SEQRES  17 A  533  LEU ARG GLU ASP PHE GLY GLN LEU ALA MLY ALA ALA PHE          
SEQRES  18 A  533  SER PHE SER GLY ASN ALA LEU ASP PRO TRP VAL ILE GLN          
SEQRES  19 A  533  MLY GLY ALA ARG GLU ARG ALA PHE GLU LEU GLY ARG SER          
SEQRES  20 A  533  VAL GLY CYS GLU SER ALA GLU ASP SER ALA SER LEU MLY          
SEQRES  21 A  533  MLY CYS LEU MLY SER MLY PRO ALA SER GLU LEU VAL THR          
SEQRES  22 A  533  ALA VAL ARG MLY PHE LEU ILE PHE SER TYR VAL PRO PHE          
SEQRES  23 A  533  ALA PRO PHE SER PRO VAL LEU GLU PRO SER ASP ALA PRO          
SEQRES  24 A  533  GLY ALA PHE ILE THR GLN ASP PRO ARG ASP VAL ILE MLY          
SEQRES  25 A  533  SER GLY MLY PHE GLY GLN VAL PRO TRP ALA VAL SER TYR          
SEQRES  26 A  533  VAL THR GLU ASP GLY GLY TYR ASN ALA ALA LEU LEU LEU          
SEQRES  27 A  533  MLY GLU ARG MLY SER GLY VAL VAL ILE ASP ASP LEU ASN          
SEQRES  28 A  533  GLU ARG TRP LEU GLU LEU ALA PRO TYR LEU LEU PHE TYR          
SEQRES  29 A  533  ARG ASP THR MLY THR MLY MLY ASP MET ASP ASP TYR SER          
SEQRES  30 A  533  ARG MLY ILE MLY GLN GLU TYR ILE GLY ASN GLN ARG PHE          
SEQRES  31 A  533  ASP ILE GLY SER TYR SER GLU LEU GLN ARG LEU PHE THR          
SEQRES  32 A  533  ASP ILE LEU PHE LYS ASN GLY THR GLN GLU SER LEU ASP          
SEQRES  33 A  533  LEU HIS ARG MLY TYR GLY MLY SER PRO VAL TYR ALA TYR          
SEQRES  34 A  533  VAL TYR ASP ASN PRO ALA GLU MLY GLY ILE ALA GLN VAL          
SEQRES  35 A  533  LEU ALA ASN ARG THR ASP TYR ASP PHE GLY THR VAL HIS          
SEQRES  36 A  533  GLY ASP ASP TYR SER LEU ILE PHE GLU ASN SER VAL ARG          
SEQRES  37 A  533  ASP VAL GLU MET ARG PRO ASP GLU GLN ILE ILE SER ARG          
SEQRES  38 A  533  ASN PHE ILE ASN MET LEU ALA ASP PHE ALA SER SER ASP          
SEQRES  39 A  533  ASP GLY SER LEU MLY TYR GLY GLU CYS ASP PHE MLY ASP          
SEQRES  40 A  533  ASN VAL GLY SER GLU MLY PHE GLN LEU LEU ALA ILE TYR          
SEQRES  41 A  533  THR ASP GLY CYS GLN ASN ARG GLN HIS VAL GLU PHE PRO          
MODRES 5THM MLY A   49  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A   51  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A   60  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A   77  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A   91  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A   93  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A   96  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  129  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  166  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  169  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  225  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  250  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  251  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  254  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  256  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  267  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  302  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  305  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  329  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  332  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  358  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  360  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  361  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  369  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  371  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  410  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  413  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  427  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  489  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  496  LYS  MODIFIED RESIDUE                                   
MODRES 5THM MLY A  503  LYS  MODIFIED RESIDUE                                   
HET    MLY  A  49      11                                                       
HET    MLY  A  51      11                                                       
HET    MLY  A  60      11                                                       
HET    MLY  A  77      11                                                       
HET    MLY  A  91      11                                                       
HET    MLY  A  93      11                                                       
HET    MLY  A  96      11                                                       
HET    MLY  A 129      11                                                       
HET    MLY  A 166      11                                                       
HET    MLY  A 169      11                                                       
HET    MLY  A 208      11                                                       
HET    MLY  A 225      11                                                       
HET    MLY  A 250      11                                                       
HET    MLY  A 251      11                                                       
HET    MLY  A 254      11                                                       
HET    MLY  A 256      11                                                       
HET    MLY  A 267      11                                                       
HET    MLY  A 302      11                                                       
HET    MLY  A 305      11                                                       
HET    MLY  A 329      11                                                       
HET    MLY  A 332      11                                                       
HET    MLY  A 358      11                                                       
HET    MLY  A 360      11                                                       
HET    MLY  A 361      11                                                       
HET    MLY  A 369      11                                                       
HET    MLY  A 371      11                                                       
HET    MLY  A 410      11                                                       
HET    MLY  A 413      11                                                       
HET    MLY  A 427      11                                                       
HET    MLY  A 489      11                                                       
HET    MLY  A 496      11                                                       
HET    MLY  A 503      11                                                       
HET    7BZ  A 601      12                                                       
HETNAM     MLY N-DIMETHYL-LYSINE                                                
HETNAM     7BZ N,N-DIMETHYLBORANAMINE                                           
FORMUL   1  MLY    32(C8 H18 N2 O2)                                             
FORMUL   2  7BZ    C2 H8 B N                                                    
FORMUL   3  HOH   *322(H2 O)                                                    
HELIX    1 AA1 THR A   37  ARG A   41  5                                   5    
HELIX    2 AA2 ALA A  115  ASN A  119  5                                   5    
HELIX    3 AA3 HIS A  121  GLY A  128  1                                   8    
HELIX    4 AA4 LEU A  139  LEU A  145  1                                   7    
HELIX    5 AA5 ASN A  155  ILE A  172  1                                  18    
HELIX    6 AA6 ALA A  173  PHE A  175  5                                   3    
HELIX    7 AA7 SER A  188  LEU A  199  1                                  12    
HELIX    8 AA8 ASP A  202  LEU A  206  5                                   5    
HELIX    9 AA9 GLY A  226  VAL A  238  1                                  13    
HELIX   10 AB1 ASP A  245  SER A  255  1                                  11    
HELIX   11 AB2 PRO A  257  ALA A  264  1                                   8    
HELIX   12 AB3 VAL A  265  LEU A  269  5                                   5    
HELIX   13 AB4 ASP A  296  GLY A  304  1                                   9    
HELIX   14 AB5 GLY A  320  ALA A  325  1                                   6    
HELIX   15 AB6 LEU A  326  MLY A  329  5                                   4    
HELIX   16 AB7 VAL A  335  ASP A  338  5                                   4    
HELIX   17 AB8 ASP A  339  LEU A  352  1                                  14    
HELIX   18 AB9 THR A  359  GLY A  376  1                                  18    
HELIX   19 AC1 SER A  384  PHE A  397  1                                  14    
HELIX   20 AC2 PHE A  397  GLY A  412  1                                  16    
HELIX   21 AC3 GLY A  428  ASN A  435  1                                   8    
HELIX   22 AC4 ASP A  448  PHE A  453  1                                   6    
HELIX   23 AC5 ARG A  463  SER A  483  1                                  21    
SHEET    1 AA1 3 LEU A   8  LEU A  11  0                                        
SHEET    2 AA1 3 GLY A  14  ARG A  17 -1  O  GLY A  14   N  LEU A  11           
SHEET    3 AA1 3 PHE A  56  ASP A  57  1  O  PHE A  56   N  ARG A  17           
SHEET    1 AA211 ARG A  19  ASP A  20  0                                        
SHEET    2 AA211 TYR A  24  PRO A  31 -1  O  SER A  26   N  ARG A  19           
SHEET    3 AA211 THR A  86  PRO A  92 -1  O  MLY A  91   N  TYR A  25           
SHEET    4 AA211 ILE A 131  ILE A 135 -1  O  LEU A 132   N  TYR A  90           
SHEET    5 AA211 PHE A 100  ILE A 106  1  N  HIS A 105   O  VAL A 133           
SHEET    6 AA211 GLY A 177  HIS A 187  1  O  VAL A 185   N  ALA A 104           
SHEET    7 AA211 ALA A 209  PHE A 213  1  O  PHE A 213   N  GLY A 186           
SHEET    8 AA211 TRP A 311  VAL A 316  1  O  ALA A 312   N  SER A 212           
SHEET    9 AA211 VAL A 416  ASP A 422  1  O  TYR A 417   N  TRP A 311           
SHEET   10 AA211 PHE A 504  TYR A 510  1  O  LEU A 507   N  ALA A 418           
SHEET   11 AA211 GLY A 513  HIS A 519 -1  O  GLN A 515   N  ALA A 508           
SHEET    1 AA3 2 GLN A  67  TRP A  68  0                                        
SHEET    2 AA3 2 LEU A  78  VAL A  79 -1  O  VAL A  79   N  GLN A  67           
SHEET    1 AA4 2 MLY A 489  TYR A 490  0                                        
SHEET    2 AA4 2 CYS A 493  ASP A 494 -1  O  CYS A 493   N  TYR A 490           
SSBOND   1 CYS A   65    CYS A   84                          1555   1555  2.05  
SSBOND   2 CYS A  240    CYS A  252                          1555   1555  2.07  
LINK         C   TYR A  48                 N   MLY A  49     1555   1555  1.33  
LINK         C   MLY A  49                 N   GLN A  50     1555   1555  1.33  
LINK         C   GLN A  50                 N   MLY A  51     1555   1555  1.33  
LINK         C   MLY A  51                 N   TRP A  52     1555   1555  1.33  
LINK         C   THR A  59                 N   MLY A  60     1555   1555  1.33  
LINK         C   MLY A  60                 N   THR A  61     1555   1555  1.32  
LINK         C   ASN A  76                 N   MLY A  77     1555   1555  1.33  
LINK         C   MLY A  77                 N   LEU A  78     1555   1555  1.33  
LINK         C   TYR A  90                 N   MLY A  91     1555   1555  1.33  
LINK         C   MLY A  91                 N   PRO A  92     1555   1555  1.34  
LINK         C   PRO A  92                 N   MLY A  93     1555   1555  1.33  
LINK         C   MLY A  93                 N   ASN A  94     1555   1555  1.32  
LINK         C   SER A  95                 N   MLY A  96     1555   1555  1.33  
LINK         C   MLY A  96                 N   ARG A  97     1555   1555  1.33  
LINK         C   GLY A 128                 N   MLY A 129     1555   1555  1.33  
LINK         C   MLY A 129                 N   PHE A 130     1555   1555  1.33  
LINK         C   LEU A 165                 N   MLY A 166     1555   1555  1.33  
LINK         C   MLY A 166                 N   TRP A 167     1555   1555  1.33  
LINK         C   ILE A 168                 N   MLY A 169     1555   1555  1.33  
LINK         C   MLY A 169                 N   GLN A 170     1555   1555  1.33  
LINK         C   ALA A 207                 N   MLY A 208     1555   1555  1.33  
LINK         C   MLY A 208                 N   ALA A 209     1555   1555  1.34  
LINK         C   GLN A 224                 N   MLY A 225     1555   1555  1.33  
LINK         C   MLY A 225                 N   GLY A 226     1555   1555  1.33  
LINK         C   LEU A 249                 N   MLY A 250     1555   1555  1.33  
LINK         C   MLY A 250                 N   MLY A 251     1555   1555  1.33  
LINK         C   MLY A 251                 N   CYS A 252     1555   1555  1.33  
LINK         C   LEU A 253                 N   MLY A 254     1555   1555  1.33  
LINK         C   MLY A 254                 N   SER A 255     1555   1555  1.34  
LINK         C   SER A 255                 N   MLY A 256     1555   1555  1.33  
LINK         C   MLY A 256                 N   PRO A 257     1555   1555  1.34  
LINK         C   ARG A 266                 N   MLY A 267     1555   1555  1.33  
LINK         C   MLY A 267                 N   PHE A 268     1555   1555  1.33  
LINK         C   ILE A 301                 N   MLY A 302     1555   1555  1.33  
LINK         C   MLY A 302                 N   SER A 303     1555   1555  1.33  
LINK         C   GLY A 304                 N   MLY A 305     1555   1555  1.33  
LINK         C   MLY A 305                 N   PHE A 306     1555   1555  1.33  
LINK         C   LEU A 328                 N   MLY A 329     1555   1555  1.33  
LINK         C   MLY A 329                 N   GLU A 330     1555   1555  1.33  
LINK         C   ARG A 331                 N   MLY A 332     1555   1555  1.33  
LINK         C   MLY A 332                 N   SER A 333     1555   1555  1.33  
LINK         C   THR A 357                 N   MLY A 358     1555   1555  1.33  
LINK         C   MLY A 358                 N   THR A 359     1555   1555  1.33  
LINK         C   THR A 359                 N   MLY A 360     1555   1555  1.33  
LINK         C   MLY A 360                 N   MLY A 361     1555   1555  1.34  
LINK         C   MLY A 361                 N   ASP A 362     1555   1555  1.33  
LINK         C   ARG A 368                 N   MLY A 369     1555   1555  1.33  
LINK         C   MLY A 369                 N   ILE A 370     1555   1555  1.34  
LINK         C   ILE A 370                 N   MLY A 371     1555   1555  1.33  
LINK         C   MLY A 371                 N   GLN A 372     1555   1555  1.33  
LINK         C   ARG A 409                 N   MLY A 410     1555   1555  1.33  
LINK         C   MLY A 410                 N   TYR A 411     1555   1555  1.33  
LINK         C   GLY A 412                 N   MLY A 413     1555   1555  1.33  
LINK         C   MLY A 413                 N   SER A 414     1555   1555  1.33  
LINK         C   GLU A 426                 N   MLY A 427     1555   1555  1.33  
LINK         C   MLY A 427                 N   GLY A 428     1555   1555  1.33  
LINK         C   LEU A 488                 N   MLY A 489     1555   1555  1.33  
LINK         C   MLY A 489                 N   TYR A 490     1555   1555  1.33  
LINK         C   PHE A 495                 N   MLY A 496     1555   1555  1.32  
LINK         C   MLY A 496                 N   ASP A 497     1555   1555  1.34  
LINK         C   GLU A 502                 N   MLY A 503     1555   1555  1.33  
LINK         C   MLY A 503                 N   PHE A 504     1555   1555  1.33  
CISPEP   1 VAL A  274    PRO A  275          0        -4.55                     
CISPEP   2 TYR A  322    ASN A  323          0         7.81                     
SITE     1 AC1  7 GLY A 109  ALA A 110  PHE A 113  SER A 188                    
SITE     2 AC1  7 ALA A 189  TYR A 322  HIS A 445                               
CRYST1   67.713   80.645  107.038  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      0.014768  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012400  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009342        0.00000                         
TER    4253      PRO A 523                                                      
MASTER      286    0   33   23   18    0    2    6 4513    1  428   41          
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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