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LongText Report for: 6h0t-pdb

Name Class
6h0t-pdb
HEADER    HYDROLASE                               10-JUL-18   6H0T              
TITLE     CRYSTAL STRUCTURE OF NATIVE RECOMBINANT HUMAN BILE SALT ACTIVATED     
TITLE    2 LIPASE                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BILE SALT-ACTIVATED LIPASE;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: BAL,BILE SALT-STIMULATED LIPASE,BSSL,BUCELIPASE,CARBOXYL    
COMPND   5 ESTER LIPASE,CHOLESTEROL ESTERASE,PANCREATIC LYSOPHOSPHOLIPASE,STEROL
COMPND   6 ESTERASE;                                                            
COMPND   7 EC: 3.1.1.13,3.1.1.3;                                                
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 OTHER_DETAILS: CRYSTALS WITH UNCLEAVED TAGGED ENZYME                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CEL, BAL;                                                      
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    LIPASE, ALPHA-BETA HYDROLASE., HYDROLASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.TOUVREY,X.BRAZZOLOTTO,F.NACHON                                      
REVDAT   1   27-MAR-19 6H0T    0                                                
JRNL        AUTH   C.TOUVREY,C.COURAGEUX,V.GUILLON,R.TERREUX,F.NACHON,          
JRNL        AUTH 2 X.BRAZZOLOTTO                                                
JRNL        TITL   X-RAY STRUCTURES OF HUMAN BILE-SALT ACTIVATED LIPASE         
JRNL        TITL 2 CONJUGATED TO NERVE AGENTS SURROGATES.                       
JRNL        REF    TOXICOLOGY                    V. 411    15 2019              
JRNL        REFN                   ISSN 1879-3185                               
JRNL        PMID   30359675                                                     
JRNL        DOI    10.1016/J.TOX.2018.10.015                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.93                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 49846                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.790                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2389                            
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 44.6200 -  4.8800    0.99     2969   152  0.1786 0.1988        
REMARK   3     2  4.8800 -  3.8800    0.99     2849   152  0.1602 0.1910        
REMARK   3     3  3.8800 -  3.3900    0.99     2816   154  0.1872 0.2389        
REMARK   3     4  3.3900 -  3.0800    0.99     2801   132  0.2178 0.2467        
REMARK   3     5  3.0800 -  2.8600    1.00     2812   156  0.2353 0.2608        
REMARK   3     6  2.8600 -  2.6900    1.00     2809   124  0.2301 0.2755        
REMARK   3     7  2.6900 -  2.5500    1.00     2773   143  0.2260 0.2685        
REMARK   3     8  2.5500 -  2.4400    1.00     2784   133  0.2226 0.2725        
REMARK   3     9  2.4400 -  2.3500    1.00     2799   128  0.2284 0.2991        
REMARK   3    10  2.3500 -  2.2700    1.00     2767   126  0.2305 0.2908        
REMARK   3    11  2.2700 -  2.2000    1.00     2781   138  0.2391 0.2521        
REMARK   3    12  2.2000 -  2.1300    1.00     2746   145  0.2457 0.2994        
REMARK   3    13  2.1300 -  2.0800    1.00     2752   150  0.2609 0.2905        
REMARK   3    14  2.0800 -  2.0300    0.99     2759   134  0.2907 0.3353        
REMARK   3    15  2.0300 -  1.9800    0.99     2749   155  0.3310 0.4056        
REMARK   3    16  1.9800 -  1.9400    0.99     2743   137  0.3437 0.3983        
REMARK   3    17  1.9400 -  1.9000    0.99     2748   130  0.3901 0.4283        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.254            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.562           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.21                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.12                          
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      :  0.008           4146                                  
REMARK   3   ANGLE     :  0.848           5635                                  
REMARK   3   CHIRALITY :  0.055            610                                  
REMARK   3   PLANARITY :  0.006            725                                  
REMARK   3   DIHEDRAL  :  6.000           2434                                  
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 6H0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010857.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-15                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49920                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.930                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.08457                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.0700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.23100                            
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: 1F6W                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, CACODYLATE, ZINC ACETATE,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       29.13700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.82000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.83800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       54.82000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.13700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.83800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -243.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     GLU A    -5                                                      
REMARK 465     ASN A    -4                                                      
REMARK 465     LEU A    -3                                                      
REMARK 465     TYR A    -2                                                      
REMARK 465     PHE A    -1                                                      
REMARK 465     GLN A     0                                                      
REMARK 465     MET A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     SER A   113                                                      
REMARK 465     GLY A   114                                                      
REMARK 465     HIS A   115                                                      
REMARK 465     GLY A   116                                                      
REMARK 465     ALA A   117                                                      
REMARK 465     ASN A   118                                                      
REMARK 465     PHE A   119                                                      
REMARK 465     LEU A   120                                                      
REMARK 465     ASN A   121                                                      
REMARK 465     ASN A   122                                                      
REMARK 465     VAL A   272                                                      
REMARK 465     PRO A   273                                                      
REMARK 465     LEU A   274                                                      
REMARK 465     ALA A   275                                                      
REMARK 465     GLY A   276                                                      
REMARK 465     LEU A   277                                                      
REMARK 465     GLU A   278                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A   1    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    VAL A   285     O    HOH A   701              2.16            
REMARK 500   OE2  GLU A   193     O    HOH A   702              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 176   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  68     -170.98    -63.88                                   
REMARK 500    GLN A  71       18.95     57.58                                   
REMARK 500    LYS A  92      -86.40    -86.13                                   
REMARK 500    LEU A 158       81.26   -152.07                                   
REMARK 500    SER A 194     -120.43     60.66                                   
REMARK 500    ASP A 294      -81.82   -138.15                                   
REMARK 500    MET A 329       79.50   -155.65                                   
REMARK 500    ASN A 333       34.66    -97.48                                   
REMARK 500    LYS A 334      104.68   -170.58                                   
REMARK 500    PHE A 393      -56.32   -132.70                                   
REMARK 500    LYS A 409      -83.48   -107.34                                   
REMARK 500    PRO A 428        8.39    -66.32                                   
REMARK 500    TRP A 430       41.58    -80.11                                   
REMARK 500    LEU A 524      -64.05   -106.37                                   
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                              ZN A 605  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  48   NE2                                                    
REMARK 620 2 HOH A 798   O    92.5                                              
REMARK 620 3 ACT A 611   OXT  84.6  97.9                                        
REMARK 620 4 HOH A 730   O   168.6  77.1  92.1                                  
REMARK 620 5 HOH A 716   O    98.2 105.9 155.8  89.3                            
REMARK 620 6 ACT A 611   O    97.1 157.8  63.3  91.2  92.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 603  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  77   OD2                                                    
REMARK 620 2 GLU A  78   OE1  75.8                                              
REMARK 620 3 GLU A  78   OE2 115.5  54.2                                        
REMARK 620 4 ASP A 476   OD2  43.9  64.7  76.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 606  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  97   OD1                                                    
REMARK 620 2 ASP A  97   OD2  51.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 168   NE2                                                    
REMARK 620 2 ACT A 610   OXT 120.5                                              
REMARK 620 3 GLU A 342   OE2  37.3 113.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 607  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 322   ND1                                                    
REMARK 620 2 ASP A 434   OD2  84.1                                              
REMARK 620 3 ACT A 612   O   125.0 129.4                                        
REMARK 620 4 ACT A 612   OXT  94.3  87.0  54.2                                  
REMARK 620 5 HOH A 805   O    90.5 104.2 114.5 168.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 602  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 487   NE2                                                    
REMARK 620 2 GLU A 489   OE1 102.4                                              
REMARK 620 3 ACT A 609   O   142.3 103.0                                        
REMARK 620 4 ACT A 609   OXT  86.4 115.5  57.6                                  
REMARK 620 5 ASP A  79   OD2  64.8  89.0  88.3  37.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 607                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 608                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 613                 
DBREF  6H0T A    2   533  UNP    P19835   CEL_HUMAN       22    553             
SEQADV 6H0T HIS A  -13  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T HIS A  -12  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T HIS A  -11  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T HIS A  -10  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T HIS A   -9  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T HIS A   -8  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T HIS A   -7  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T HIS A   -6  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T GLU A   -5  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T ASN A   -4  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T LEU A   -3  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T TYR A   -2  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T PHE A   -1  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T GLN A    0  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T SER A    1  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H0T ASP A  186  UNP  P19835    ASN   206 ENGINEERED MUTATION            
SEQADV 6H0T ASP A  298  UNP  P19835    ALA   318 ENGINEERED MUTATION            
SEQRES   1 A  547  HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE          
SEQRES   2 A  547  GLN SER LYS LEU GLY ALA VAL TYR THR GLU GLY GLY PHE          
SEQRES   3 A  547  VAL GLU GLY VAL ASN LYS LYS LEU GLY LEU LEU GLY ASP          
SEQRES   4 A  547  SER VAL ASP ILE PHE LYS GLY ILE PRO PHE ALA ALA PRO          
SEQRES   5 A  547  THR LYS ALA LEU GLU ASN PRO GLN PRO HIS PRO GLY TRP          
SEQRES   6 A  547  GLN GLY THR LEU LYS ALA LYS ASN PHE LYS LYS ARG CYS          
SEQRES   7 A  547  LEU GLN ALA THR ILE THR GLN ASP SER THR TYR GLY ASP          
SEQRES   8 A  547  GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO GLN GLY          
SEQRES   9 A  547  ARG LYS GLN VAL SER ARG ASP LEU PRO VAL MET ILE TRP          
SEQRES  10 A  547  ILE TYR GLY GLY ALA PHE LEU MET GLY SER GLY HIS GLY          
SEQRES  11 A  547  ALA ASN PHE LEU ASN ASN TYR LEU TYR ASP GLY GLU GLU          
SEQRES  12 A  547  ILE ALA THR ARG GLY ASN VAL ILE VAL VAL THR PHE ASN          
SEQRES  13 A  547  TYR ARG VAL GLY PRO LEU GLY PHE LEU SER THR GLY ASP          
SEQRES  14 A  547  ALA ASN LEU PRO GLY ASN TYR GLY LEU ARG ASP GLN HIS          
SEQRES  15 A  547  MET ALA ILE ALA TRP VAL LYS ARG ASN ILE ALA ALA PHE          
SEQRES  16 A  547  GLY GLY ASP PRO ASP ASN ILE THR LEU PHE GLY GLU SER          
SEQRES  17 A  547  ALA GLY GLY ALA SER VAL SER LEU GLN THR LEU SER PRO          
SEQRES  18 A  547  TYR ASN LYS GLY LEU ILE ARG ARG ALA ILE SER GLN SER          
SEQRES  19 A  547  GLY VAL ALA LEU SER PRO TRP VAL ILE GLN LYS ASN PRO          
SEQRES  20 A  547  LEU PHE TRP ALA LYS LYS VAL ALA GLU LYS VAL GLY CYS          
SEQRES  21 A  547  PRO VAL GLY ASP ALA ALA ARG MET ALA GLN CYS LEU LYS          
SEQRES  22 A  547  VAL THR ASP PRO ARG ALA LEU THR LEU ALA TYR LYS VAL          
SEQRES  23 A  547  PRO LEU ALA GLY LEU GLU TYR PRO MET LEU HIS TYR VAL          
SEQRES  24 A  547  GLY PHE VAL PRO VAL ILE ASP GLY ASP PHE ILE PRO ASP          
SEQRES  25 A  547  ASP PRO ILE ASN LEU TYR ALA ASN ALA ALA ASP ILE ASP          
SEQRES  26 A  547  TYR ILE ALA GLY THR ASN ASN MET ASP GLY HIS ILE PHE          
SEQRES  27 A  547  ALA SER ILE ASP MET PRO ALA ILE ASN LYS GLY ASN LYS          
SEQRES  28 A  547  LYS VAL THR GLU GLU ASP PHE TYR LYS LEU VAL SER GLU          
SEQRES  29 A  547  PHE THR ILE THR LYS GLY LEU ARG GLY ALA LYS THR THR          
SEQRES  30 A  547  PHE ASP VAL TYR THR GLU SER TRP ALA GLN ASP PRO SER          
SEQRES  31 A  547  GLN GLU ASN LYS LYS LYS THR VAL VAL ASP PHE GLU THR          
SEQRES  32 A  547  ASP VAL LEU PHE LEU VAL PRO THR GLU ILE ALA LEU ALA          
SEQRES  33 A  547  GLN HIS ARG ALA ASN ALA LYS SER ALA LYS THR TYR ALA          
SEQRES  34 A  547  TYR LEU PHE SER HIS PRO SER ARG MET PRO VAL TYR PRO          
SEQRES  35 A  547  LYS TRP VAL GLY ALA ASP HIS ALA ASP ASP ILE GLN TYR          
SEQRES  36 A  547  VAL PHE GLY LYS PRO PHE ALA THR PRO THR GLY TYR ARG          
SEQRES  37 A  547  PRO GLN ASP ARG THR VAL SER LYS ALA MET ILE ALA TYR          
SEQRES  38 A  547  TRP THR ASN PHE ALA LYS THR GLY ASP PRO ASN MET GLY          
SEQRES  39 A  547  ASP SER ALA VAL PRO THR HIS TRP GLU PRO TYR THR THR          
SEQRES  40 A  547  GLU ASN SER GLY TYR LEU GLU ILE THR LYS LYS MET GLY          
SEQRES  41 A  547  SER SER SER MET LYS ARG SER LEU ARG THR ASN PHE LEU          
SEQRES  42 A  547  ARG TYR TRP THR LEU THR TYR LEU ALA LEU PRO THR VAL          
SEQRES  43 A  547  THR                                                          
HET     ZN  A 601       1                                                       
HET     ZN  A 602       1                                                       
HET     ZN  A 603       1                                                       
HET     ZN  A 604       1                                                       
HET     ZN  A 605       1                                                       
HET     ZN  A 606       1                                                       
HET     ZN  A 607       1                                                       
HET     ZN  A 608       1                                                       
HET    ACT  A 609       4                                                       
HET    ACT  A 610       4                                                       
HET    ACT  A 611       4                                                       
HET    ACT  A 612       4                                                       
HET    GOL  A 613       6                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   ZN    8(ZN 2+)                                                     
FORMUL  10  ACT    4(C2 H3 O2 1-)                                               
FORMUL  14  GOL    C3 H8 O3                                                     
FORMUL  15  HOH   *112(H2 O)                                                    
HELIX    1 AA1 GLY A  127  ASN A  135  1                                   9    
HELIX    2 AA2 GLY A  146  LEU A  151  1                                   6    
HELIX    3 AA3 ASN A  161  ILE A  178  1                                  18    
HELIX    4 AA4 ALA A  179  PHE A  181  5                                   3    
HELIX    5 AA5 SER A  194  SER A  206  1                                  13    
HELIX    6 AA6 PRO A  207  LYS A  210  5                                   4    
HELIX    7 AA7 ASN A  232  GLY A  245  1                                  14    
HELIX    8 AA8 ASP A  250  VAL A  260  1                                  11    
HELIX    9 AA9 ASP A  262  ALA A  269  1                                   8    
HELIX   10 AB1 PRO A  280  VAL A  285  5                                   6    
HELIX   11 AB2 ASP A  299  ALA A  308  5                                  10    
HELIX   12 AB3 GLY A  321  MET A  329  1                                   9    
HELIX   13 AB4 PRO A  330  LYS A  334  5                                   5    
HELIX   14 AB5 THR A  340  THR A  352  1                                  13    
HELIX   15 AB6 LYS A  355  THR A  368  1                                  14    
HELIX   16 AB7 GLU A  369  ALA A  372  5                                   4    
HELIX   17 AB8 SER A  376  PHE A  393  1                                  18    
HELIX   18 AB9 PHE A  393  ALA A  408  1                                  16    
HELIX   19 AC1 ASP A  437  PHE A  443  1                                   7    
HELIX   20 AC2 GLY A  444  THR A  449  1                                   6    
HELIX   21 AC3 PRO A  450  TYR A  453  5                                   4    
HELIX   22 AC4 ARG A  454  GLY A  475  1                                  22    
HELIX   23 AC5 GLY A  506  SER A  508  5                                   3    
HELIX   24 AC6 ARG A  515  LEU A  524  1                                  10    
HELIX   25 AC7 LEU A  524  LEU A  529  1                                   6    
SHEET    1 AA1 3 ALA A   5  THR A   8  0                                        
SHEET    2 AA1 3 GLY A  11  GLU A  14 -1  O  VAL A  13   N  VAL A   6           
SHEET    3 AA1 3 THR A  54  LYS A  56  1  O  LEU A  55   N  PHE A  12           
SHEET    1 AA211 VAL A  16  LYS A  19  0                                        
SHEET    2 AA211 SER A  26  PRO A  34 -1  O  ILE A  29   N  VAL A  16           
SHEET    3 AA211 TYR A  82  GLN A  89 -1  O  VAL A  87   N  ASP A  28           
SHEET    4 AA211 ILE A 137  PHE A 141 -1  O  THR A 140   N  ASN A  84           
SHEET    5 AA211 LEU A  98  ILE A 104  1  N  MET A 101   O  ILE A 137           
SHEET    6 AA211 GLY A 183  GLU A 193  1  O  THR A 189   N  VAL A 100           
SHEET    7 AA211 ARG A 215  GLN A 219  1  O  GLN A 219   N  GLY A 192           
SHEET    8 AA211 ASP A 311  ASN A 317  1  O  ILE A 313   N  SER A 218           
SHEET    9 AA211 THR A 413  PHE A 418  1  O  PHE A 418   N  THR A 316           
SHEET   10 AA211 GLY A 497  ILE A 501  1  O  ILE A 501   N  LEU A 417           
SHEET   11 AA211 MET A 510  ARG A 512 -1  O  LYS A 511   N  TYR A 498           
SHEET    1 AA3 2 GLN A  66  ALA A  67  0                                        
SHEET    2 AA3 2 THR A  74  TYR A  75 -1  O  TYR A  75   N  GLN A  66           
SSBOND   1 CYS A   64    CYS A   80                          1555   1555  2.05  
SSBOND   2 CYS A  246    CYS A  257                          1555   1555  2.05  
LINK         NE2 HIS A  48                ZN    ZN A 605     1555   1555  2.15  
LINK         OD2 ASP A  77                ZN    ZN A 603     1555   1555  2.03  
LINK         OE1 GLU A  78                ZN    ZN A 603     1555   1555  2.67  
LINK         OE2 GLU A  78                ZN    ZN A 603     1555   1555  1.84  
LINK         OD1 ASP A  97                ZN    ZN A 606     1555   1555  2.66  
LINK         OD2 ASP A  97                ZN    ZN A 606     1555   1555  2.41  
LINK         NE2 HIS A 168                ZN    ZN A 601     1555   1555  2.02  
LINK         ND1 HIS A 322                ZN    ZN A 607     1555   1555  2.35  
LINK         OD2 ASP A 328                ZN    ZN A 604     1555   1555  1.82  
LINK         OD2 ASP A 434                ZN    ZN A 607     1555   1555  2.23  
LINK         NE2 HIS A 487                ZN    ZN A 602     1555   1555  2.04  
LINK         OE1 GLU A 489                ZN    ZN A 602     1555   1555  1.94  
LINK        ZN    ZN A 601                 OXT ACT A 610     1555   1555  2.09  
LINK        ZN    ZN A 602                 O   ACT A 609     1555   1555  2.24  
LINK        ZN    ZN A 602                 OXT ACT A 609     1555   1555  2.40  
LINK        ZN    ZN A 605                 O   HOH A 798     1555   1555  2.02  
LINK        ZN    ZN A 605                 OXT ACT A 611     1555   1555  2.37  
LINK        ZN    ZN A 605                 O   HOH A 730     1555   1555  2.12  
LINK        ZN    ZN A 605                 O   HOH A 716     1555   1555  2.13  
LINK        ZN    ZN A 605                 O   ACT A 611     1555   1555  1.85  
LINK        ZN    ZN A 607                 O   ACT A 612     1555   1555  2.54  
LINK        ZN    ZN A 607                 OXT ACT A 612     1555   1555  2.45  
LINK        ZN    ZN A 607                 O   HOH A 805     1555   1555  2.31  
LINK         OD2 ASP A  79                ZN    ZN A 602     1555   3645  2.04  
LINK         OE2 GLU A 342                ZN    ZN A 601     1555   2554  2.02  
LINK         OD2 ASP A 476                ZN    ZN A 603     1555   3655  1.97  
SITE     1 AC1  3 HIS A 168  GLU A 342  ACT A 610                               
SITE     1 AC2  4 ASP A  79  HIS A 487  GLU A 489  ACT A 609                    
SITE     1 AC3  3 ASP A  77  GLU A  78  ASP A 476                               
SITE     1 AC4  4 MET A 281  ASP A 328  PHE A 351  GLU A 388                    
SITE     1 AC5  5 HIS A  48  ACT A 611  HOH A 716  HOH A 730                    
SITE     2 AC5  5 HOH A 798                                                     
SITE     1 AC6  1 ASP A  97                                                     
SITE     1 AC7  4 HIS A 322  ASP A 434  ACT A 612  HOH A 805                    
SITE     1 AC8  6 GLY A 107  ALA A 108  PHE A 109  LEU A 110                    
SITE     2 AC8  6 SER A 194  ALA A 195                                          
SITE     1 AC9  6 ASP A  77  ASP A  79  HIS A 487  GLU A 489                    
SITE     2 AC9  6 PRO A 490   ZN A 602                                          
SITE     1 AD1  6 HIS A 168  TYR A 208  GLU A 341  GLU A 342                    
SITE     2 AD1  6  ZN A 601  HOH A 703                                          
SITE     1 AD2  5 HIS A  48  TYR A  82   ZN A 605  HOH A 716                    
SITE     2 AD2  5 HOH A 730                                                     
SITE     1 AD3  4 HIS A 322  ILE A 323  ASP A 434   ZN A 607                    
SITE     1 AD4  9 GLY A 315  THR A 316  LEU A 394  THR A 397                    
SITE     2 AD4  9 GLU A 398  LEU A 401  TYR A 416  TYR A 498                    
SITE     3 AD4  9 LEU A 514                                                     
CRYST1   58.274   97.676  109.640  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017160  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010238  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009121        0.00000                         
TER    4020      THR A 533                                                      
MASTER      428    0   13   25   16    0   20    6 4161    1   51   43          
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:
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