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LongText Report for: 6j1q-pdb

Name Class
6j1q-pdb
HEADER    HYDROLASE                               29-DEC-18   6J1Q              
TITLE     CRYSTAL STRUCTURE OF CANDIDA ANTARCTICA LIPASE B MUTANT - RS          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE B;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CALB;                                                       
COMPND   5 EC: 3.1.1.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOZYMA ANTARCTICA;                          
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 84753;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    CALB, HYDROLASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.X.CEN,J.H.ZHOU,Q.WU                                                 
REVDAT   1   01-JAN-20 6J1Q    0                                                
JRNL        AUTH   J.XU,Y.CEN,W.SINGH,J.FAN,L.WU,X.LIN,J.ZHOU,M.HUANG,          
JRNL        AUTH 2 M.T.REETZ,Q.WU                                               
JRNL        TITL   STEREODIVERGENT PROTEIN ENGINEERING OF A LIPASE TO ACCESS    
JRNL        TITL 2 ALL POSSIBLE STEREOISOMERS OF CHIRAL ESTERS WITH TWO         
JRNL        TITL 3 STEREOCENTERS.                                               
JRNL        REF    J.AM.CHEM.SOC.                V. 141  7934 2019              
JRNL        REFN                   ESSN 1520-5126                               
JRNL        PMID   31023008                                                     
JRNL        DOI    10.1021/JACS.9B02709                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.13                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 68591                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.173                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3456                            
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 46.1445 -  4.6767    0.99     2701   154  0.1562 0.1562        
REMARK   3     2  4.6767 -  3.7126    1.00     2680   151  0.1227 0.1361        
REMARK   3     3  3.7126 -  3.2434    1.00     2647   165  0.1363 0.1713        
REMARK   3     4  3.2434 -  2.9469    1.00     2668   151  0.1526 0.1765        
REMARK   3     5  2.9469 -  2.7357    1.00     2640   141  0.1521 0.1812        
REMARK   3     6  2.7357 -  2.5744    1.00     2643   148  0.1454 0.1734        
REMARK   3     7  2.5744 -  2.4455    1.00     2674   120  0.1434 0.1519        
REMARK   3     8  2.4455 -  2.3391    1.00     2654   154  0.1436 0.1687        
REMARK   3     9  2.3391 -  2.2490    1.00     2660   134  0.1373 0.1685        
REMARK   3    10  2.2490 -  2.1714    1.00     2628   146  0.1387 0.1690        
REMARK   3    11  2.1714 -  2.1035    1.00     2676   126  0.1402 0.1602        
REMARK   3    12  2.1035 -  2.0434    1.00     2643   140  0.1441 0.1742        
REMARK   3    13  2.0434 -  1.9896    1.00     2660   133  0.1451 0.1908        
REMARK   3    14  1.9896 -  1.9411    1.00     2629   135  0.1486 0.1689        
REMARK   3    15  1.9411 -  1.8969    1.00     2648   130  0.1493 0.1829        
REMARK   3    16  1.8969 -  1.8566    1.00     2633   163  0.1554 0.1920        
REMARK   3    17  1.8566 -  1.8194    1.00     2638   141  0.1610 0.1937        
REMARK   3    18  1.8194 -  1.7851    1.00     2647   129  0.1647 0.1988        
REMARK   3    19  1.7851 -  1.7532    1.00     2632   160  0.1655 0.2064        
REMARK   3    20  1.7532 -  1.7235    1.00     2600   141  0.1835 0.2300        
REMARK   3    21  1.7235 -  1.6957    0.99     2680   135  0.1874 0.2237        
REMARK   3    22  1.6957 -  1.6696    0.97     2568   133  0.1886 0.2113        
REMARK   3    23  1.6696 -  1.6450    0.93     2458   118  0.1950 0.2111        
REMARK   3    24  1.6450 -  1.6219    0.87     2325   120  0.1935 0.2145        
REMARK   3    25  1.6219 -  1.5999    0.79     2103    88  0.1979 0.2333        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.810           
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           4964                                  
REMARK   3   ANGLE     :  1.026           6798                                  
REMARK   3   CHIRALITY :  0.056            780                                  
REMARK   3   PLANARITY :  0.007            886                                  
REMARK   3   DIHEDRAL  : 12.200           3001                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  34.9718   0.4834   2.9038              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0742 T22:   0.0851                                     
REMARK   3      T33:   0.0933 T12:  -0.0051                                     
REMARK   3      T13:   0.0219 T23:  -0.0024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4057 L22:   0.2821                                     
REMARK   3      L33:   0.7260 L12:  -0.2208                                     
REMARK   3      L13:   0.4713 L23:  -0.2949                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0408 S12:   0.0563 S13:  -0.0221                       
REMARK   3      S21:  -0.0312 S22:  -0.0102 S23:   0.0455                       
REMARK   3      S31:   0.0405 S32:   0.0647 S33:  -0.0270                       
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 6J1Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JAN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300010233.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUN-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97775                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69637                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
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     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 29.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 1TCA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE 0.1 M HEPES 7.0   
REMARK 280  16% PEG 4000 10% ISOPROPANOL, VAPOR DIFFUSION, SITTING DROP,        
REMARK 280  TEMPERATURE 289K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       40.22450            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -3                                                      
REMARK 465     ALA A    -2                                                      
REMARK 465     MET A    -1                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     ALA B    -2                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  29       73.88   -157.26                                   
REMARK 500    ASN A  51      -93.01   -152.17                                   
REMARK 500    ASP A  75      120.80    -30.20                                   
REMARK 500    SER A 105     -112.13     34.83                                   
REMARK 500    ASP A 134       68.06   -113.02                                   
REMARK 500    ALA A 146     -125.95     58.65                                   
REMARK 500    ALA A 305       39.90   -141.92                                   
REMARK 500    SER B  29       72.01   -155.11                                   
REMARK 500    ASN B  51      -91.47   -150.64                                   
REMARK 500    ASP B  75      121.55    -30.20                                   
REMARK 500    SER B 105     -112.70     35.59                                   
REMARK 500    ASP B 134       68.88   -115.05                                   
REMARK 500    ALA B 305       35.71   -142.78                                   
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 B 798        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH B 799        DISTANCE =  6.82 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 408                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 409                 
DBREF  6J1Q A    1   317  UNP    P41365   LIPB_PSEA2      26    342             
DBREF  6J1Q B    1   317  UNP    P41365   LIPB_PSEA2      26    342             
SEQADV 6J1Q GLY A   -3  UNP  P41365              EXPRESSION TAG                 
SEQADV 6J1Q ALA A   -2  UNP  P41365              EXPRESSION TAG                 
SEQADV 6J1Q MET A   -1  UNP  P41365              EXPRESSION TAG                 
SEQADV 6J1Q ALA A    0  UNP  P41365              EXPRESSION TAG                 
SEQADV 6J1Q ALA A   57  UNP  P41365    THR    82 ENGINEERED MUTATION            
SEQADV 6J1Q THR A   89  UNP  P41365    ALA   114 ENGINEERED MUTATION            
SEQADV 6J1Q ALA A  104  UNP  P41365    TRP   129 ENGINEERED MUTATION            
SEQADV 6J1Q VAL A  189  UNP  P41365    ILE   214 ENGINEERED MUTATION            
SEQADV 6J1Q GLY B   -3  UNP  P41365              EXPRESSION TAG                 
SEQADV 6J1Q ALA B   -2  UNP  P41365              EXPRESSION TAG                 
SEQADV 6J1Q MET B   -1  UNP  P41365              EXPRESSION TAG                 
SEQADV 6J1Q ALA B    0  UNP  P41365              EXPRESSION TAG                 
SEQADV 6J1Q ALA B   57  UNP  P41365    THR    82 ENGINEERED MUTATION            
SEQADV 6J1Q THR B   89  UNP  P41365    ALA   114 ENGINEERED MUTATION            
SEQADV 6J1Q ALA B  104  UNP  P41365    TRP   129 ENGINEERED MUTATION            
SEQADV 6J1Q VAL B  189  UNP  P41365    ILE   214 ENGINEERED MUTATION            
SEQRES   1 A  321  GLY ALA MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE          
SEQRES   2 A  321  SER GLN PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS          
SEQRES   3 A  321  GLN GLY ALA SER PRO SER SER VAL SER LYS PRO ILE LEU          
SEQRES   4 A  321  LEU VAL PRO GLY THR GLY THR THR GLY PRO GLN SER PHE          
SEQRES   5 A  321  ASP SER ASN TRP ILE PRO LEU SER ALA GLN LEU GLY TYR          
SEQRES   6 A  321  THR PRO CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN          
SEQRES   7 A  321  ASP THR GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE          
SEQRES   8 A  321  THR THR LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO          
SEQRES   9 A  321  VAL LEU THR ALA SER GLN GLY GLY LEU VAL ALA GLN TRP          
SEQRES  10 A  321  GLY LEU THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP          
SEQRES  11 A  321  ARG LEU MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL          
SEQRES  12 A  321  LEU ALA GLY PRO LEU ASP ALA LEU ALA VAL SER ALA PRO          
SEQRES  13 A  321  SER VAL TRP GLN GLN THR THR GLY SER ALA LEU THR THR          
SEQRES  14 A  321  ALA LEU ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO          
SEQRES  15 A  321  THR THR ASN LEU TYR SER ALA THR ASP GLU VAL VAL GLN          
SEQRES  16 A  321  PRO GLN VAL SER ASN SER PRO LEU ASP SER SER TYR LEU          
SEQRES  17 A  321  PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY          
SEQRES  18 A  321  PRO LEU PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER          
SEQRES  19 A  321  GLN PHE SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER          
SEQRES  20 A  321  THR THR GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR          
SEQRES  21 A  321  ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU          
SEQRES  22 A  321  GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA PRO ALA ALA          
SEQRES  23 A  321  ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO          
SEQRES  24 A  321  ASP LEU MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS          
SEQRES  25 A  321  ARG THR CYS SER GLY ILE VAL THR PRO                          
SEQRES   1 B  321  GLY ALA MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE          
SEQRES   2 B  321  SER GLN PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS          
SEQRES   3 B  321  GLN GLY ALA SER PRO SER SER VAL SER LYS PRO ILE LEU          
SEQRES   4 B  321  LEU VAL PRO GLY THR GLY THR THR GLY PRO GLN SER PHE          
SEQRES   5 B  321  ASP SER ASN TRP ILE PRO LEU SER ALA GLN LEU GLY TYR          
SEQRES   6 B  321  THR PRO CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN          
SEQRES   7 B  321  ASP THR GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE          
SEQRES   8 B  321  THR THR LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO          
SEQRES   9 B  321  VAL LEU THR ALA SER GLN GLY GLY LEU VAL ALA GLN TRP          
SEQRES  10 B  321  GLY LEU THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP          
SEQRES  11 B  321  ARG LEU MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL          
SEQRES  12 B  321  LEU ALA GLY PRO LEU ASP ALA LEU ALA VAL SER ALA PRO          
SEQRES  13 B  321  SER VAL TRP GLN GLN THR THR GLY SER ALA LEU THR THR          
SEQRES  14 B  321  ALA LEU ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO          
SEQRES  15 B  321  THR THR ASN LEU TYR SER ALA THR ASP GLU VAL VAL GLN          
SEQRES  16 B  321  PRO GLN VAL SER ASN SER PRO LEU ASP SER SER TYR LEU          
SEQRES  17 B  321  PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY          
SEQRES  18 B  321  PRO LEU PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER          
SEQRES  19 B  321  GLN PHE SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER          
SEQRES  20 B  321  THR THR GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR          
SEQRES  21 B  321  ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU          
SEQRES  22 B  321  GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA PRO ALA ALA          
SEQRES  23 B  321  ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO          
SEQRES  24 B  321  ASP LEU MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS          
SEQRES  25 B  321  ARG THR CYS SER GLY ILE VAL THR PRO                          
HET    SO4  A 401       5                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    EDO  A 405       4                                                       
HET    EDO  A 406       4                                                       
HET    EDO  A 407       4                                                       
HET    EDO  A 408       4                                                       
HET    EDO  A 409       4                                                       
HET    EDO  A 410       4                                                       
HET    EDO  A 411       4                                                       
HET    EPE  A 412      15                                                       
HET    EPE  A 413      15                                                       
HET    PEG  A 414       7                                                       
HET    PEG  A 415       7                                                       
HET    SO4  B 401       5                                                       
HET    SO4  B 402       5                                                       
HET    EDO  B 403       4                                                       
HET    EDO  B 404       4                                                       
HET    EDO  B 405       4                                                       
HET    PEG  B 406       7                                                       
HET    PEG  B 407       7                                                       
HET     CL  B 408       1                                                       
HET    1PE  B 409      16                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      CL CHLORIDE ION                                                     
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     EPE HEPES                                                            
HETSYN     1PE PEG400                                                           
FORMUL   3  SO4    6(O4 S 2-)                                                   
FORMUL   7  EDO    10(C2 H6 O2)                                                 
FORMUL  14  EPE    2(C8 H18 N2 O4 S)                                            
FORMUL  16  PEG    4(C4 H10 O3)                                                 
FORMUL  25   CL    CL 1-                                                        
FORMUL  26  1PE    C10 H22 O6                                                   
FORMUL  27  HOH   *569(H2 O)                                                    
HELIX    1 AA1 PRO A   12  GLY A   19  1                                   8    
HELIX    2 AA2 THR A   43  ASP A   49  1                                   7    
HELIX    3 AA3 ASN A   51  LEU A   59  1                                   9    
HELIX    4 AA4 ASP A   75  SER A   94  1                                  20    
HELIX    5 AA5 SER A  105  PHE A  118  1                                  14    
HELIX    6 AA6 PRO A  119  ARG A  122  5                                   4    
HELIX    7 AA7 ALA A  151  GLN A  157  1                                   7    
HELIX    8 AA8 SER A  161  ALA A  170  1                                  10    
HELIX    9 AA9 ALA A  212  GLY A  217  1                                   6    
HELIX   10 AB1 ASP A  223  SER A  230  1                                   8    
HELIX   11 AB2 SER A  230  SER A  243  1                                  14    
HELIX   12 AB3 ARG A  249  TYR A  253  5                                   5    
HELIX   13 AB4 GLY A  254  CYS A  258  5                                   5    
HELIX   14 AB5 THR A  267  ALA A  276  1                                  10    
HELIX   15 AB6 LEU A  278  GLY A  288  1                                  11    
HELIX   16 AB7 ALA A  301  VAL A  306  5                                   6    
HELIX   17 AB8 PRO B   12  GLY B   19  1                                   8    
HELIX   18 AB9 THR B   43  ASP B   49  1                                   7    
HELIX   19 AC1 ASN B   51  LEU B   59  1                                   9    
HELIX   20 AC2 ASP B   75  SER B   94  1                                  20    
HELIX   21 AC3 SER B  105  PHE B  118  1                                  14    
HELIX   22 AC4 PRO B  119  SER B  123  5                                   5    
HELIX   23 AC5 PRO B  143  LEU B  147  5                                   5    
HELIX   24 AC6 ALA B  151  GLN B  157  1                                   7    
HELIX   25 AC7 SER B  161  ALA B  170  1                                  10    
HELIX   26 AC8 ALA B  212  GLY B  217  1                                   6    
HELIX   27 AC9 ASP B  223  SER B  230  1                                   8    
HELIX   28 AD1 SER B  230  SER B  243  1                                  14    
HELIX   29 AD2 ARG B  249  TYR B  253  5                                   5    
HELIX   30 AD3 GLY B  254  CYS B  258  5                                   5    
HELIX   31 AD4 THR B  267  ALA B  276  1                                  10    
HELIX   32 AD5 LEU B  278  GLY B  288  1                                  11    
HELIX   33 AD6 ALA B  301  VAL B  306  5                                   6    
SHEET    1 AA1 7 LEU A  20  CYS A  22  0                                        
SHEET    2 AA1 7 THR A  62  ILE A  66 -1  O  TRP A  65   N  THR A  21           
SHEET    3 AA1 7 PRO A  33  VAL A  37  1  N  LEU A  36   O  CYS A  64           
SHEET    4 AA1 7 LEU A  99  ALA A 104  1  O  LEU A 102   N  LEU A  35           
SHEET    5 AA1 7 VAL A 125  PHE A 131  1  O  MET A 129   N  VAL A 101           
SHEET    6 AA1 7 THR A 179  TYR A 183  1  O  THR A 180   N  ALA A 130           
SHEET    7 AA1 7 LYS A 208  GLN A 211  1  O  VAL A 210   N  ASN A 181           
SHEET    1 AA2 2 ARG A 309  THR A 310  0                                        
SHEET    2 AA2 2 GLY A 313  ILE A 314 -1  O  GLY A 313   N  THR A 310           
SHEET    1 AA3 7 LEU B  20  CYS B  22  0                                        
SHEET    2 AA3 7 THR B  62  ILE B  66 -1  O  TRP B  65   N  THR B  21           
SHEET    3 AA3 7 PRO B  33  VAL B  37  1  N  LEU B  36   O  CYS B  64           
SHEET    4 AA3 7 LEU B  99  ALA B 104  1  O  LEU B 102   N  LEU B  35           
SHEET    5 AA3 7 VAL B 125  PHE B 131  1  O  MET B 129   N  VAL B 101           
SHEET    6 AA3 7 THR B 179  TYR B 183  1  O  THR B 180   N  ALA B 130           
SHEET    7 AA3 7 LYS B 208  GLN B 211  1  O  VAL B 210   N  ASN B 181           
SHEET    1 AA4 2 ARG B 309  THR B 310  0                                        
SHEET    2 AA4 2 GLY B 313  ILE B 314 -1  O  GLY B 313   N  THR B 310           
SSBOND   1 CYS A   22    CYS A   64                          1555   1555  2.06  
SSBOND   2 CYS A  216    CYS A  258                          1555   1555  2.03  
SSBOND   3 CYS A  293    CYS A  311                          1555   1555  2.02  
SSBOND   4 CYS B   22    CYS B   64                          1555   1555  2.06  
SSBOND   5 CYS B  216    CYS B  258                          1555   1555  2.03  
SSBOND   6 CYS B  293    CYS B  311                          1555   1555  2.02  
CISPEP   1 PRO A   69    PRO A   70          0       -13.61                     
CISPEP   2 GLN A  191    PRO A  192          0         2.29                     
CISPEP   3 PRO B   69    PRO B   70          0       -12.82                     
CISPEP   4 GLN B  191    PRO B  192          0         1.34                     
SITE     1 AC1  5 LYS A 208  ARG A 249  SER A 250  HOH A 531                    
SITE     2 AC1  5 HOH A 536                                                     
SITE     1 AC2  6 SER A  26  PRO A  27  HOH A 522  HOH A 660                    
SITE     2 AC2  6 HOH A 690  SER B 123                                          
SITE     1 AC3 10 SER A 120  LYS A 124  EPE A 413  HOH A 516                    
SITE     2 AC3 10 HOH A 588  HOH A 617  HOH A 662  THR B 245                    
SITE     3 AC3 10 GLN B 247  HOH B 537                                          
SITE     1 AC4  4 TYR A 203  PHE A 205  ASN A 206  HOH A 525                    
SITE     1 AC5  7 THR A  21  PRO A  45  TRP A  65  SER A  67                    
SITE     2 AC5  7 EDO A 407  HOH A 544  HOH A 582                               
SITE     1 AC6  1 ARG A 242                                                     
SITE     1 AC7  5 THR A  43  PRO A  45  GLN A  46  EDO A 405                    
SITE     2 AC7  5 HOH A 653                                                     
SITE     1 AC8  1 EDO A 409                                                     
SITE     1 AC9  7 THR A  40  SER A 105  GLN A 106  GLN A 157                    
SITE     2 AC9  7 VAL A 189  EDO A 408  HOH A 549                               
SITE     1 AD1  6 GLN A 231  TYR A 234  ARG A 238  ASP A 265                    
SITE     2 AD1  6 EPE A 412  HOH A 501                                          
SITE     1 AD2  4 ALA A   8  PRO A 299  TYR A 300  HOH A 686                    
SITE     1 AD3  9 ARG A 238  ASP A 252  GLY A 254  ILE A 255                    
SITE     2 AD3  9 THR A 256  ASP A 257  EDO A 410  HOH A 501                    
SITE     3 AD3  9 HOH A 503                                                     
SITE     1 AD4 11 GLY A   4  PRO A 119  SER A 120  ARG A 122                    
SITE     2 AD4 11 SO4 A 403  HOH A 532  HOH A 562  HOH A 622                    
SITE     3 AD4 11 ALA B  25  SER B  26  SO4 B 401                               
SITE     1 AD5  4 CYS A 258  LEU B 147  VAL B 149  HOH B 633                    
SITE     1 AD6  5 ALA A 214  VAL A 215  GLY A 217  HOH A 665                    
SITE     2 AD6  5 GLY B 142                                                     
SITE     1 AD7  6 EPE A 413  LYS B 208  ARG B 249  SER B 250                    
SITE     2 AD7  6 HOH B 537  HOH B 588                                          
SITE     1 AD8  3 THR B 165  ARG B 168  LYS B 308                               
SITE     1 AD9  5 PRO B   7  ALA B   8  PRO B 299  TYR B 300                    
SITE     2 AD9  5 HOH B 505                                                     
SITE     1 AE1  4 ASN B 169  PHE B 304  HOH B 514  HOH B 709                    
SITE     1 AE2  5 GLU A 188  HOH A 715  ALA B 283  HOH B 557                    
SITE     2 AE2  5 HOH B 626                                                     
SITE     1 AE3  4 ALA B 287  GLY B 288  PRO B 289  HOH B 515                    
SITE     1 AE4  5 HOH A 736  THR B 138  VAL B 154  HOH B 512                    
SITE     2 AE4  5 HOH B 621                                                     
SITE     1 AE5  4 PRO B  45  SER B  67  HOH B 698  HOH B 781                    
SITE     1 AE6  8 LEU B 144  ASN B 292  ARG B 309  THR B 310                    
SITE     2 AE6  8 CYS B 311  GLY B 313  HOH B 503  HOH B 731                    
CRYST1   46.530   80.449   72.588  90.00  97.56  90.00 P 1 21 1      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      0.021492  0.000000  0.002853        0.00000                         
SCALE2      0.000000  0.012430  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013897        0.00000                         
TER    2367      PRO A 317                                                      
TER    4717      PRO B 317                                                      
MASTER      381    0   24   33   18    0   42    6 5347    2  156   50          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
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