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LongText Report for: 7v6d-pdb

Name Class
7v6d-pdb
HEADER    HYDROLASE                               20-AUG-21   7V6D              
TITLE     STRUCTURE OF LIPASE B FROM LASIODIPLODIA THEOBROMAE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE B;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LASIODIPLODIA THEOBROMAE;                       
SOURCE   3 ORGANISM_TAXID: 45133;                                               
SOURCE   4 GENE: LIPB, DBV05_G2145;                                             
SOURCE   5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: GS115;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: GENOME INTEGRATED LINEARIZED VECTOR;  
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPIC9K                                    
KEYWDS    ALPHA/BETA-HYDROLASES, HYDROLASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.XUE,H.F.ZHANG,G.K.T.NGUYEN,W.S.YEW                                  
REVDAT   1   13-OCT-21 7V6D    0                                                
JRNL        AUTH   A.M.J.NG,R.L.YANG,H.F.ZHANG,B.XUE,W.S.YEW,G.K.T.NGUYEN       
JRNL        TITL   A NOVEL LIPASE FROM LASIODIPLODIA THEOBROMAE EFFICIENTLY     
JRNL        TITL 2 HYDROLYSES C8-C10 METHYL ESTERS FOR THE PREPARATION OF       
JRNL        TITL 3 MEDIUM-CHAIN TRIGLYCERIDES PRECURSORS                        
JRNL        REF    INT J MOL SCI                 V.  22       2021              
JRNL        REFN                   ESSN 1422-0067                               
JRNL        DOI    10.3390/IJMS221910339                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.19.1_4122                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 31217                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1554                            
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 29.7000 -  5.5500    1.00     2871   131  0.1919 0.2300        
REMARK   3     2  5.5500 -  4.4100    1.00     2757   137  0.1791 0.2111        
REMARK   3     3  4.4100 -  3.8500    1.00     2703   145  0.1588 0.1950        
REMARK   3     4  3.8500 -  3.5000    1.00     2731   119  0.1746 0.2275        
REMARK   3     5  3.5000 -  3.2500    1.00     2658   141  0.1863 0.2170        
REMARK   3     6  3.2500 -  3.0600    1.00     2687   151  0.2047 0.2436        
REMARK   3     7  3.0600 -  2.9100    1.00     2656   149  0.2159 0.2885        
REMARK   3     8  2.9100 -  2.7800    1.00     2661   140  0.2138 0.2962        
REMARK   3     9  2.7800 -  2.6700    1.00     2647   141  0.2346 0.3288        
REMARK   3    10  2.6700 -  2.5800    1.00     2643   150  0.2413 0.3756        
REMARK   3    11  2.5800 -  2.5000    1.00     2649   150  0.2423 0.2947        
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)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.230           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.48                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.73                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
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 7V6D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-AUG-21.                  
REMARK 100 THE DEPOSITION ID IS D_1300024175.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUN-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95373                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.7.4                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31233                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 13.60                              
REMARK 200  R MERGE                    (I) : 0.19100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.20200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6IDY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% MPD, 100 MM NAOAC, PH 4.6, 10 MM     
REMARK 280  CACL2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       32.71400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       81.31950            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       83.33700            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       32.71400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       81.31950            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       83.33700            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       32.71400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       81.31950            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       83.33700            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       32.71400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       81.31950            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       83.33700            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 620 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 13810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2                            
REMARK 350 SURFACE AREA OF THE COMPLEX: 13660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
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     ALA A    19                                                      
REMARK 465     PRO A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     PRO A    22                                                      
REMARK 465     VAL A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     GLU A    25                                                      
REMARK 465     ASN A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     LEU A    28                                                      
REMARK 465     GLU A    29                                                      
REMARK 465     LYS A    30                                                      
REMARK 465     ARG A    31                                                      
REMARK 465     GLN A    32                                                      
REMARK 465     SER A    33                                                      
REMARK 465     LEU A    34                                                      
REMARK 465     SER A    35                                                      
REMARK 465     SER A    36                                                      
REMARK 465     VAL A    37                                                      
REMARK 465     LEU A    38                                                      
REMARK 465     SER A    39                                                      
REMARK 465     ALA A    40                                                      
REMARK 465     LEU A    41                                                      
REMARK 465     SER A    42                                                      
REMARK 465     GLY A    43                                                      
REMARK 465     LEU A    44                                                      
REMARK 465     THR A    45                                                      
REMARK 465     GLU A    46                                                      
REMARK 465     PRO A    47                                                      
REMARK 465     THR A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     ILE A    50                                                      
REMARK 465     LEU A    51                                                      
REMARK 465     SER A    52                                                      
REMARK 465     GLN A    53                                                      
REMARK 465     LEU A    54                                                      
REMARK 465     GLU A    55                                                      
REMARK 465     ALA A    56                                                      
REMARK 465     VAL A    57                                                      
REMARK 465     GLU A    58                                                      
REMARK 465     ALA A    59                                                      
REMARK 465     THR A    60                                                      
REMARK 465     SER A    61                                                      
REMARK 465     THR A    62                                                      
REMARK 465     PRO A    63                                                      
REMARK 465     THR A    64                                                      
REMARK 465     SER A    65                                                      
REMARK 465     VAL A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     ALA A    69                                                      
REMARK 465     GLN A    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     GLN A    72                                                      
REMARK 465     LEU A    73                                                      
REMARK 465     GLU A    74                                                      
REMARK 465     ALA A    75                                                      
REMARK 465     ILE A    76                                                      
REMARK 465     TYR A    77                                                      
REMARK 465     GLY A    78                                                      
REMARK 465     THR A    79                                                      
REMARK 465     THR A    80                                                      
REMARK 465     PRO A    81                                                      
REMARK 465     THR A    82                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     PRO B    20                                                      
REMARK 465     ALA B    21                                                      
REMARK 465     PRO B    22                                                      
REMARK 465     VAL B    23                                                      
REMARK 465     PRO B    24                                                      
REMARK 465     GLU B    25                                                      
REMARK 465     ASN B    26                                                      
REMARK 465     GLY B    27                                                      
REMARK 465     LEU B    28                                                      
REMARK 465     GLU B    29                                                      
REMARK 465     LYS B    30                                                      
REMARK 465     ARG B    31                                                      
REMARK 465     GLN B    32                                                      
REMARK 465     SER B    33                                                      
REMARK 465     LEU B    34                                                      
REMARK 465     SER B    35                                                      
REMARK 465     SER B    36                                                      
REMARK 465     VAL B    37                                                      
REMARK 465     LEU B    38                                                      
REMARK 465     SER B    39                                                      
REMARK 465     ALA B    40                                                      
REMARK 465     LEU B    41                                                      
REMARK 465     SER B    42                                                      
REMARK 465     GLY B    43                                                      
REMARK 465     LEU B    44                                                      
REMARK 465     THR B    45                                                      
REMARK 465     GLU B    46                                                      
REMARK 465     PRO B    47                                                      
REMARK 465     THR B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     ILE B    50                                                      
REMARK 465     LEU B    51                                                      
REMARK 465     SER B    52                                                      
REMARK 465     GLN B    53                                                      
REMARK 465     LEU B    54                                                      
REMARK 465     GLU B    55                                                      
REMARK 465     ALA B    56                                                      
REMARK 465     VAL B    57                                                      
REMARK 465     GLU B    58                                                      
REMARK 465     ALA B    59                                                      
REMARK 465     THR B    60                                                      
REMARK 465     SER B    61                                                      
REMARK 465     THR B    62                                                      
REMARK 465     PRO B    63                                                      
REMARK 465     THR B    64                                                      
REMARK 465     SER B    65                                                      
REMARK 465     VAL B    66                                                      
REMARK 465     GLU B    67                                                      
REMARK 465     GLN B    68                                                      
REMARK 465     ALA B    69                                                      
REMARK 465     GLN B    70                                                      
REMARK 465     GLU B    71                                                      
REMARK 465     GLN B    72                                                      
REMARK 465     LEU B    73                                                      
REMARK 465     GLU B    74                                                      
REMARK 465     ALA B    75                                                      
REMARK 465     ILE B    76                                                      
REMARK 465     TYR B    77                                                      
REMARK 465     GLY B    78                                                      
REMARK 465     THR B    79                                                      
REMARK 465     THR B    80                                                      
REMARK 465     PRO B    81                                                      
REMARK 465     THR B    82                                                      
REMARK 465     ASN B    83                                                      
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    ASN A 180     -117.05   -134.23                                   
REMARK 500    SER A 235     -128.02     61.99                                   
REMARK 500    TRP A 248       77.93   -112.21                                   
REMARK 500    ASP A 264       75.27   -119.71                                   
REMARK 500    GLN A 332       42.19   -153.30                                   
REMARK 500    ASN B 180     -118.68   -133.49                                   
REMARK 500    SER B 235     -124.81     58.17                                   
REMARK 500    TRP B 248       79.08   -117.44                                   
REMARK 500    PHE B 324      100.87   -164.67                                   
REMARK 500    GLN B 332       45.49   -145.71                                   
REMARK 500    ASP B 343       48.46   -145.54                                   
REMARK 500    CYS B 404        3.85    -68.63                                   
REMARK 500    MET B 445      153.80    -49.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 257   OD1                                                    
REMARK 620 2 ASP A 257   OD2  52.1                                              
REMARK 620 3 ALA A 386   O    81.4  77.2                                        
REMARK 620 4 HIS A 389   O   153.1 146.7  86.2                                  
REMARK 620 5 GLY A 391   O    75.4 126.7 106.2  85.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 257   OD1                                                    
REMARK 620 2 ASP B 257   OD2  48.2                                              
REMARK 620 3 ALA B 386   O    79.0  66.3                                        
REMARK 620 4 HIS B 389   O   161.0 137.2  87.9                                  
REMARK 620 5 GLY B 391   O    80.2 127.8 101.7  89.2                            
REMARK 620 N                    1     2     3     4                             
DBREF1 7V6D A   19   449  UNP                  A0A5N5DNA6_9PEZI                 
DBREF2 7V6D A     A0A5N5DNA6                         19         449             
DBREF1 7V6D B   19   449  UNP                  A0A5N5DNA6_9PEZI                 
DBREF2 7V6D B     A0A5N5DNA6                         19         449             
SEQRES   1 A  431  ALA PRO ALA PRO VAL PRO GLU ASN GLY LEU GLU LYS ARG          
SEQRES   2 A  431  GLN SER LEU SER SER VAL LEU SER ALA LEU SER GLY LEU          
SEQRES   3 A  431  THR GLU PRO THR ALA ILE LEU SER GLN LEU GLU ALA VAL          
SEQRES   4 A  431  GLU ALA THR SER THR PRO THR SER VAL GLU GLN ALA GLN          
SEQRES   5 A  431  GLU GLN LEU GLU ALA ILE TYR GLY THR THR PRO THR ASN          
SEQRES   6 A  431  ILE PHE GLU ASN ILE ALA GLN GLN ILE ALA ASP GLY LEU          
SEQRES   7 A  431  SER THR LEU THR ILE VAL GLN ALA LEU GLY PHE SER PRO          
SEQRES   8 A  431  SER GLY GLU ASN SER GLU THR ASN SER ASN THR ARG GLU          
SEQRES   9 A  431  PRO SER THR THR ILE TYR PRO LYS LYS SER SER SER ASP          
SEQRES  10 A  431  ALA PRO TYR SER ILE THR GLU GLU GLU LEU ARG GLN ALA          
SEQRES  11 A  431  ILE TYR ILE PRO SER ASP PHE THR TYR GLY ASP LYS PRO          
SEQRES  12 A  431  PRO VAL ILE PHE VAL PRO GLY THR GLY SER TYR GLY GLY          
SEQRES  13 A  431  ILE SER PHE GLY SER ASN LEU ARG LYS LEU LEU THR GLY          
SEQRES  14 A  431  VAL SER TYR ALA ASP PRO VAL TRP LEU ASN VAL PRO ASP          
SEQRES  15 A  431  ALA LEU LEU ARG ASP ALA GLN THR ASN GLY GLU PHE VAL          
SEQRES  16 A  431  ALA TYR ALA ILE ASN TYR ILE SER GLY ILE SER GLY ASP          
SEQRES  17 A  431  ALA ASN VAL SER VAL VAL SER TRP SER GLN GLY GLY LEU          
SEQRES  18 A  431  ASP THR GLN TRP ALA PHE THR TYR TRP PRO SER THR ARG          
SEQRES  19 A  431  ALA LEU VAL SER ASP PHE VAL PRO VAL SER PRO ASP PHE          
SEQRES  20 A  431  HIS GLY THR VAL LEU ALA ASN VAL ILE CYS LEU ASN PRO          
SEQRES  21 A  431  GLY ALA GLY GLY VAL GLY LEU GLY PRO CYS ALA PRO ALA          
SEQRES  22 A  431  VAL LEU GLN GLN GLU TYR ASN SER ASN PHE VAL THR ALA          
SEQRES  23 A  431  LEU ARG ALA ALA GLY GLY ALA ASP ALA TYR VAL PRO THR          
SEQRES  24 A  431  THR SER VAL PHE SER GLY PHE LEU ASP GLU ILE VAL GLN          
SEQRES  25 A  431  PRO GLN SER GLY THR GLY ALA SER ALA TYR ILE ASN ASP          
SEQRES  26 A  431  ALA ARG GLY VAL GLY THR THR ASN ALA GLU VAL GLN VAL          
SEQRES  27 A  431  VAL CYS LYS GLY LYS GLY PRO ALA GLY GLY PHE TYR THR          
SEQRES  28 A  431  HIS GLU SER LEU LEU VAL ASN PRO LEU THR TYR ALA LEU          
SEQRES  29 A  431  LEU VAL ASP ALA LEU THR HIS ASP GLY PRO GLY SER VAL          
SEQRES  30 A  431  ASP ARG LEU ASP LEU ASP THR VAL CYS SER THR VAL VAL          
SEQRES  31 A  431  ALA PRO GLY LEU GLY LEU ASP ALA LEU LEU GLU ILE GLU          
SEQRES  32 A  431  GLY VAL ASN VAL LEU ALA ALA VAL ASN LEU LEU THR TYR          
SEQRES  33 A  431  SER ASP ARG ARG LEU ALA GLU PRO ALA LEU MET SER TYR          
SEQRES  34 A  431  ALA ALA                                                      
SEQRES   1 B  431  ALA PRO ALA PRO VAL PRO GLU ASN GLY LEU GLU LYS ARG          
SEQRES   2 B  431  GLN SER LEU SER SER VAL LEU SER ALA LEU SER GLY LEU          
SEQRES   3 B  431  THR GLU PRO THR ALA ILE LEU SER GLN LEU GLU ALA VAL          
SEQRES   4 B  431  GLU ALA THR SER THR PRO THR SER VAL GLU GLN ALA GLN          
SEQRES   5 B  431  GLU GLN LEU GLU ALA ILE TYR GLY THR THR PRO THR ASN          
SEQRES   6 B  431  ILE PHE GLU ASN ILE ALA GLN GLN ILE ALA ASP GLY LEU          
SEQRES   7 B  431  SER THR LEU THR ILE VAL GLN ALA LEU GLY PHE SER PRO          
SEQRES   8 B  431  SER GLY GLU ASN SER GLU THR ASN SER ASN THR ARG GLU          
SEQRES   9 B  431  PRO SER THR THR ILE TYR PRO LYS LYS SER SER SER ASP          
SEQRES  10 B  431  ALA PRO TYR SER ILE THR GLU GLU GLU LEU ARG GLN ALA          
SEQRES  11 B  431  ILE TYR ILE PRO SER ASP PHE THR TYR GLY ASP LYS PRO          
SEQRES  12 B  431  PRO VAL ILE PHE VAL PRO GLY THR GLY SER TYR GLY GLY          
SEQRES  13 B  431  ILE SER PHE GLY SER ASN LEU ARG LYS LEU LEU THR GLY          
SEQRES  14 B  431  VAL SER TYR ALA ASP PRO VAL TRP LEU ASN VAL PRO ASP          
SEQRES  15 B  431  ALA LEU LEU ARG ASP ALA GLN THR ASN GLY GLU PHE VAL          
SEQRES  16 B  431  ALA TYR ALA ILE ASN TYR ILE SER GLY ILE SER GLY ASP          
SEQRES  17 B  431  ALA ASN VAL SER VAL VAL SER TRP SER GLN GLY GLY LEU          
SEQRES  18 B  431  ASP THR GLN TRP ALA PHE THR TYR TRP PRO SER THR ARG          
SEQRES  19 B  431  ALA LEU VAL SER ASP PHE VAL PRO VAL SER PRO ASP PHE          
SEQRES  20 B  431  HIS GLY THR VAL LEU ALA ASN VAL ILE CYS LEU ASN PRO          
SEQRES  21 B  431  GLY ALA GLY GLY VAL GLY LEU GLY PRO CYS ALA PRO ALA          
SEQRES  22 B  431  VAL LEU GLN GLN GLU TYR ASN SER ASN PHE VAL THR ALA          
SEQRES  23 B  431  LEU ARG ALA ALA GLY GLY ALA ASP ALA TYR VAL PRO THR          
SEQRES  24 B  431  THR SER VAL PHE SER GLY PHE LEU ASP GLU ILE VAL GLN          
SEQRES  25 B  431  PRO GLN SER GLY THR GLY ALA SER ALA TYR ILE ASN ASP          
SEQRES  26 B  431  ALA ARG GLY VAL GLY THR THR ASN ALA GLU VAL GLN VAL          
SEQRES  27 B  431  VAL CYS LYS GLY LYS GLY PRO ALA GLY GLY PHE TYR THR          
SEQRES  28 B  431  HIS GLU SER LEU LEU VAL ASN PRO LEU THR TYR ALA LEU          
SEQRES  29 B  431  LEU VAL ASP ALA LEU THR HIS ASP GLY PRO GLY SER VAL          
SEQRES  30 B  431  ASP ARG LEU ASP LEU ASP THR VAL CYS SER THR VAL VAL          
SEQRES  31 B  431  ALA PRO GLY LEU GLY LEU ASP ALA LEU LEU GLU ILE GLU          
SEQRES  32 B  431  GLY VAL ASN VAL LEU ALA ALA VAL ASN LEU LEU THR TYR          
SEQRES  33 B  431  SER ASP ARG ARG LEU ALA GLU PRO ALA LEU MET SER TYR          
SEQRES  34 B  431  ALA ALA                                                      
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET     CA  A 501       1                                                       
HET     CA  B 501       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      CA CALCIUM ION                                                      
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   6  HOH   *118(H2 O)                                                    
HELIX    1 AA1 ASN A   83  SER A   97  1                                  15    
HELIX    2 AA2 LEU A   99  LEU A  105  1                                   7    
HELIX    3 AA3 SER A  110  SER A  114  5                                   5    
HELIX    4 AA4 THR A  141  ALA A  148  1                                   8    
HELIX    5 AA5 TYR A  172  GLY A  178  1                                   7    
HELIX    6 AA6 ASN A  180  LEU A  185  1                                   6    
HELIX    7 AA7 ASP A  205  ILE A  223  1                                  19    
HELIX    8 AA8 SER A  235  TRP A  248  1                                  14    
HELIX    9 AA9 PRO A  249  ALA A  253  5                                   5    
HELIX   10 AB1 THR A  268  CYS A  275  1                                   8    
HELIX   11 AB2 ALA A  289  GLN A  295  1                                   7    
HELIX   12 AB3 SER A  299  ALA A  308  1                                  10    
HELIX   13 AB4 SER A  333  ALA A  337  5                                   5    
HELIX   14 AB5 VAL A  354  CYS A  358  1                                   5    
HELIX   15 AB6 GLY A  362  GLY A  366  5                                   5    
HELIX   16 AB7 GLU A  371  VAL A  375  5                                   5    
HELIX   17 AB8 ASN A  376  THR A  388  1                                  13    
HELIX   18 AB9 ASP A  399  CYS A  404  1                                   6    
HELIX   19 AC1 GLY A  413  TYR A  434  1                                  22    
HELIX   20 AC2 PHE B   85  SER B   97  1                                  13    
HELIX   21 AC3 LEU B   99  LEU B  105  1                                   7    
HELIX   22 AC4 SER B  110  SER B  114  5                                   5    
HELIX   23 AC5 THR B  141  ALA B  148  1                                   8    
HELIX   24 AC6 TYR B  172  GLY B  178  1                                   7    
HELIX   25 AC7 ASN B  180  LEU B  185  1                                   6    
HELIX   26 AC8 VAL B  198  LEU B  203  5                                   6    
HELIX   27 AC9 ASP B  205  ILE B  223  1                                  19    
HELIX   28 AD1 SER B  235  TRP B  248  1                                  14    
HELIX   29 AD2 PRO B  249  ALA B  253  5                                   5    
HELIX   30 AD3 THR B  268  CYS B  275  1                                   8    
HELIX   31 AD4 ALA B  289  GLN B  295  1                                   7    
HELIX   32 AD5 SER B  299  ALA B  308  1                                  10    
HELIX   33 AD6 VAL B  354  CYS B  358  1                                   5    
HELIX   34 AD7 GLY B  362  GLY B  366  5                                   5    
HELIX   35 AD8 GLU B  371  VAL B  375  5                                   5    
HELIX   36 AD9 ASN B  376  THR B  388  1                                  13    
HELIX   37 AE1 ASP B  399  CYS B  404  1                                   6    
HELIX   38 AE2 LEU B  414  TYR B  434  1                                  21    
HELIX   39 AE3 MET B  445  ALA B  449  5                                   5    
SHEET    1 AA1 5 ILE A 149  TYR A 150  0                                        
SHEET    2 AA1 5 ASP A 192  LEU A 196 -1  O  TRP A 195   N  TYR A 150           
SHEET    3 AA1 5 PRO A 162  VAL A 166  1  N  PHE A 165   O  VAL A 194           
SHEET    4 AA1 5 VAL A 229  TRP A 234  1  O  SER A 230   N  ILE A 164           
SHEET    5 AA1 5 VAL A 255  VAL A 261  1  O  VAL A 261   N  SER A 233           
SHEET    1 AA2 2 THR A 317  PHE A 321  0                                        
SHEET    2 AA2 2 THR A 349  GLU A 353  1  O  ALA A 352   N  SER A 319           
SHEET    1 AA3 5 ILE B 149  TYR B 150  0                                        
SHEET    2 AA3 5 ASP B 192  LEU B 196 -1  O  TRP B 195   N  TYR B 150           
SHEET    3 AA3 5 PRO B 162  VAL B 166  1  N  VAL B 163   O  VAL B 194           
SHEET    4 AA3 5 VAL B 229  TRP B 234  1  O  SER B 230   N  ILE B 164           
SHEET    5 AA3 5 VAL B 255  VAL B 261  1  O  VAL B 261   N  SER B 233           
SHEET    1 AA4 2 THR B 317  PHE B 321  0                                        
SHEET    2 AA4 2 THR B 349  GLU B 353  1  O  ALA B 352   N  SER B 319           
SSBOND   1 CYS A  275    CYS A  288                          1555   1555  2.04  
SSBOND   2 CYS A  358    CYS A  404                          1555   1555  2.04  
SSBOND   3 CYS B  275    CYS B  288                          1555   1555  2.03  
SSBOND   4 CYS B  358    CYS B  404                          1555   1555  2.03  
LINK         ND2 ASN A 228                 C1  NAG C   1     1555   1555  1.46  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.44  
LINK         OD1 ASP A 257                CA    CA A 501     1555   1555  2.60  
LINK         OD2 ASP A 257                CA    CA A 501     1555   1555  2.43  
LINK         O   ALA A 386                CA    CA A 501     1555   1555  2.30  
LINK         O   HIS A 389                CA    CA A 501     1555   1555  2.33  
LINK         O   GLY A 391                CA    CA A 501     1555   1555  2.35  
LINK         OD1 ASP B 257                CA    CA B 501     1555   1555  2.45  
LINK         OD2 ASP B 257                CA    CA B 501     1555   1555  2.88  
LINK         O   ALA B 386                CA    CA B 501     1555   1555  2.28  
LINK         O   HIS B 389                CA    CA B 501     1555   1555  2.31  
LINK         O   GLY B 391                CA    CA B 501     1555   1555  2.41  
CISPEP   1 TYR A  128    PRO A  129          0         6.19                     
CISPEP   2 PHE A  324    LEU A  325          0       -26.94                     
CISPEP   3 GLN A  330    PRO A  331          0        -2.49                     
CISPEP   4 TYR B  128    PRO B  129          0         7.33                     
CISPEP   5 PHE B  324    LEU B  325          0         0.18                     
CISPEP   6 GLN B  330    PRO B  331          0        -5.82                     
CRYST1   65.428  162.639  166.674  90.00  90.00  90.00 I 2 2 2      16          
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      0.015284  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006149  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006000        0.00000                         
TER    2716      ALA A 449                                                      
TER    5424      ALA B 449                                                      
MASTER      420    0    4   39   14    0    0    6 5570    2   51   68          
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.
For technical information about these pages see:
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