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LongText Report for: 4EA6-pdb

Name Class
4EA6-pdb
HEADER    HYDROLASE                               22-MAR-12   4EA6              
TITLE     CRYSTAL STRUCTURE OF FUNGAL LIPASE FROM THERMOMYCES(HUMICOLA)         
TITLE    2 LANUGINOSA AT 2.30 ANGSTROM RESOLUTION.                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE;                                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: TRIACYLGLYCEROL LIPASE;                                     
COMPND   5 EC: 3.1.1.3                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOMYCES LANUGINOSUS;                        
SOURCE   3 ORGANISM_TAXID: 5541                                                 
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KUMAR,J.MUKHERJEE,M.N.GUPTA,M.SINHA,P.KAUR,S.SHARMA,T.P.SINGH       
REVDAT   1   11-APR-12 4EA6    0                                                
JRNL        AUTH   M.KUMAR,J.MUKHERJEE,M.N.GUPTA,M.SINHA,P.KAUR,S.SHARMA,       
JRNL        AUTH 2 T.P.SINGH                                                    
JRNL        TITL   CRYSTAL STRUCTURE OF FUNGAL LIPASE FROM                      
JRNL        TITL 2 THERMOMYCES(HUMICOLA) LANUGINOSA AT 2.30 ANGSTROM            
JRNL        TITL 3 RESOLUTION.                                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 37931                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2012                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2741                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.21                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 113                          
REMARK   3   BIN FREE R VALUE                    : 0.3060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4142                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 243                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 20.29000                                             
REMARK   3    B22 (A**2) : 20.29000                                             
REMARK   3    B33 (A**2) : -40.58000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.049         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.039         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.173         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.356         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.923                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4248 ; 0.005 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5790 ; 0.937 ; 1.934       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   536 ; 4.776 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   210 ;36.802 ;24.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   622 ;15.738 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;18.665 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   628 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3358 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.527                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : K, H, -L                                        
REMARK   3      TWIN FRACTION : 0.473                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4EA6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071362.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37931                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200   FOR THE DATA SET  : 15.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34600                            
REMARK 200   FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1DT3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, O.1M NACL, 1.6M AMMONIUM     
REMARK 280  SULPHATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       26.86067            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       53.72133            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.29100            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       67.15167            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       13.43033            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    ASP A  27       88.04   -166.33                                   
REMARK 500    CYS A  41       55.74   -143.97                                   
REMARK 500    ASP A  57        1.71     59.87                                   
REMARK 500    SER A 146     -125.96     59.02                                   
REMARK 500    ASN A 178     -158.99    -80.66                                   
REMARK 500    THR A 199     -132.20     36.65                                   
REMARK 500    ASN A 200       43.60    -92.49                                   
REMARK 500    GLU A 210       40.56   -103.82                                   
REMARK 500    PHE A 211       10.64   -143.73                                   
REMARK 500    PRO A 250       66.91    -69.64                                   
REMARK 500    PHE A 262      -31.40     72.02                                   
REMARK 500    PRO B  29     -149.69    -80.61                                   
REMARK 500    CYS B  41       58.75   -146.49                                   
REMARK 500    LYS B  74       62.38     63.97                                   
REMARK 500    SER B 146     -118.33     60.73                                   
REMARK 500    THR B 199     -104.70     23.34                                   
REMARK 500    ARG B 232        0.68    -63.34                                   
REMARK 500    ASN B 248       58.69   -105.94                                   
REMARK 500    PRO B 250       94.93    -69.31                                   
REMARK 500    ASN B 251     -163.48   -168.03                                   
REMARK 500    PHE B 262      -50.11     68.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DT3   RELATED DB: PDB                                   
DBREF  4EA6 A    1   269  UNP    O59952   LIP_THELA       23    291             
DBREF  4EA6 B    1   269  UNP    O59952   LIP_THELA       23    291             
SEQRES   1 A  269  GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE          
SEQRES   2 A  269  ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN          
SEQRES   3 A  269  ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN          
SEQRES   4 A  269  ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU          
SEQRES   5 A  269  TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY          
SEQRES   6 A  269  PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU          
SEQRES   7 A  269  SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY          
SEQRES   8 A  269  ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS          
SEQRES   9 A  269  SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP          
SEQRES  10 A  269  ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP          
SEQRES  11 A  269  ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR          
SEQRES  12 A  269  GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY          
SEQRES  13 A  269  ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE          
SEQRES  14 A  269  SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA          
SEQRES  15 A  269  GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG          
SEQRES  16 A  269  ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO          
SEQRES  17 A  269  ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP          
SEQRES  18 A  269  ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP          
SEQRES  19 A  269  ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN          
SEQRES  20 A  269  ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP          
SEQRES  21 A  269  TYR PHE GLY LEU ILE GLY THR CYS LEU                          
SEQRES   1 B  269  GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE          
SEQRES   2 B  269  ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN          
SEQRES   3 B  269  ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN          
SEQRES   4 B  269  ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU          
SEQRES   5 B  269  TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY          
SEQRES   6 B  269  PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU          
SEQRES   7 B  269  SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY          
SEQRES   8 B  269  ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS          
SEQRES   9 B  269  SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP          
SEQRES  10 B  269  ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP          
SEQRES  11 B  269  ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR          
SEQRES  12 B  269  GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY          
SEQRES  13 B  269  ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE          
SEQRES  14 B  269  SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA          
SEQRES  15 B  269  GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG          
SEQRES  16 B  269  ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO          
SEQRES  17 B  269  ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP          
SEQRES  18 B  269  ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP          
SEQRES  19 B  269  ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN          
SEQRES  20 B  269  ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP          
SEQRES  21 B  269  TYR PHE GLY LEU ILE GLY THR CYS LEU                          
FORMUL   3  HOH   *243(H2 O)                                                    
HELIX    1   1 SER A    3  ALA A   20  1                                  18    
HELIX    2   2 CYS A   41  LYS A   46  1                                   6    
HELIX    3   3 ILE A   86  GLY A   91  1                                   6    
HELIX    4   4 ASP A  111  HIS A  135  1                                  25    
HELIX    5   5 SER A  146  ARG A  160  1                                  15    
HELIX    6   6 ASN A  178  GLN A  188  1                                  11    
HELIX    7   7 ILE A  202  LEU A  206  5                                   5    
HELIX    8   8 PRO A  208  GLY A  212  5                                   5    
HELIX    9   9 THR A  231  ASN A  233  5                                   3    
HELIX   10  10 ILE A  255  TRP A  260  5                                   6    
HELIX   11  11 SER B    3  CYS B   22  1                                  20    
HELIX   12  12 CYS B   36  ALA B   40  5                                   5    
HELIX   13  13 CYS B   41  LYS B   46  1                                   6    
HELIX   14  14 SER B   85  ASN B   92  1                                   8    
HELIX   15  15 ASP B  111  ARG B  118  1                                   8    
HELIX   16  16 VAL B  120  HIS B  135  1                                  16    
HELIX   17  17 SER B  146  ARG B  160  1                                  15    
HELIX   18  18 ASN B  178  GLN B  188  1                                  11    
HELIX   19  19 PRO B  208  GLY B  212  5                                   5    
HELIX   20  20 ILE B  255  TRP B  260  5                                   6    
SHEET    1   A 8 ALA A  49  SER A  58  0                                        
SHEET    2   A 8 VAL A  63  ASP A  70 -1  O  LEU A  67   N  LEU A  52           
SHEET    3   A 8 LEU A  75  PHE A  80 -1  O  VAL A  77   N  ALA A  68           
SHEET    4   A 8 ARG A 139  HIS A 145  1  O  ARG A 139   N  ILE A  76           
SHEET    5   A 8 ILE A 166  TYR A 171  1  O  ASP A 167   N  PHE A 142           
SHEET    6   A 8 LEU A 193  HIS A 198  1  O  TYR A 194   N  VAL A 168           
SHEET    7   A 8 GLU A 219  ILE A 222  1  O  ILE A 222   N  THR A 197           
SHEET    8   A 8 ILE A 235  ILE A 238 -1  O  ILE A 238   N  GLU A 219           
SHEET    1   B 2 LEU A  97  GLU A  99  0                                        
SHEET    2   B 2 ARG A 108  HIS A 110 -1  O  GLY A 109   N  LYS A  98           
SHEET    1   C 8 ALA B  49  SER B  58  0                                        
SHEET    2   C 8 VAL B  63  ASP B  70 -1  O  LEU B  69   N  THR B  50           
SHEET    3   C 8 LEU B  75  PHE B  80 -1  O  VAL B  77   N  ALA B  68           
SHEET    4   C 8 ARG B 139  HIS B 145  1  O  VAL B 141   N  ILE B  76           
SHEET    5   C 8 ILE B 166  TYR B 171  1  O  ASP B 167   N  PHE B 142           
SHEET    6   C 8 LEU B 193  HIS B 198  1  O  TYR B 194   N  VAL B 168           
SHEET    7   C 8 GLU B 219  ILE B 222  1  O  TYR B 220   N  THR B 197           
SHEET    8   C 8 ILE B 235  ILE B 238 -1  O  ILE B 238   N  GLU B 219           
SHEET    1   D 2 LEU B  97  GLU B  99  0                                        
SHEET    2   D 2 ARG B 108  HIS B 110 -1  O  GLY B 109   N  LYS B  98           
SSBOND   1 CYS A   22    CYS A  268                          1555   1555  2.04  
SSBOND   2 CYS A   36    CYS A   41                          1555   1555  2.03  
SSBOND   3 CYS A  104    CYS A  107                          1555   1555  2.03  
SSBOND   4 CYS B   22    CYS B  268                          1555   1555  2.03  
SSBOND   5 CYS B   36    CYS B   41                          1555   1555  2.02  
SSBOND   6 CYS B  104    CYS B  107                          1555   1555  2.03  
CISPEP   1 LEU A  206    PRO A  207          0        -8.28                     
CISPEP   2 SER A  217    PRO A  218          0        -1.52                     
CISPEP   3 LEU B  206    PRO B  207          0       -14.07                     
CISPEP   4 SER B  217    PRO B  218          0        -1.19                     
CRYST1  140.180  140.180   80.582  90.00  90.00 120.00 P 61         12          
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      0.007134  0.004119  0.000000        0.00000                         
SCALE2      0.000000  0.008237  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012410        0.00000                         
TER    2072      LEU A 269                                                      
TER    4144      LEU B 269                                                      
MASTER      291    0    0   20   20    0    0    6 4385    2   12   42          
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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