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LongText Report for: 6h18-pdb

Name Class
6h18-pdb
HEADER    HYDROLASE                               11-JUL-18   6H18              
TITLE     CRYSTAL STRUCTURE OF SARIN SURROGATE NIMP INHIBITED RECOMBINANT HUMAN 
TITLE    2 BILE SALT ACTIVATED 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: SGB = SERINE RESIDUE INHIBITED BY SARIN (SEE          
COMPND  11 HTTP://WWW.RCSB.ORG/LIGAND/SGB)                                      
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, SARIN INHIBITION, HYDROLASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.TOUVREY,X.BRAZZOLOTTO,F.NACHON                                      
REVDAT   1   27-MAR-19 6H18    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.    1.85 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) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.43                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 52177                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2550                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   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 6H18 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010871.                                   
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          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52277                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.430                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.09432                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.8800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1F6W                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
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       27.85100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.44400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.02750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.44400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.85100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.02750            
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: 2510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -312.0 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     SER A   422                                                      
REMARK 465     ARG A   423                                                      
REMARK 465     MET A   424                                                      
REMARK 465     PRO A   425                                                      
REMARK 465     VAL A   426                                                      
REMARK 465     TYR A   427                                                      
REMARK 465     PRO A   428                                                      
REMARK 465     LYS A   429                                                      
REMARK 465     TRP A   430                                                      
REMARK 465     VAL A   431                                                      
REMARK 465     GLY A   432                                                      
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     GLN A   0    CG   CD   OE1  NE2                                  
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   NE2  GLN A    46     O    HOH A   701              2.18            
REMARK 500   O    HOH A   723     O    HOH A   847              2.19            
REMARK 500   O    HOH A   772     O    HOH A   880              2.19            
REMARK 500   O    HOH A   802     O    HOH A   870              2.19            
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    LEU A 158       83.88   -153.39                                   
REMARK 500    SGB A 194     -120.00     58.12                                   
REMARK 500    ALA A 275      142.69   -175.87                                   
REMARK 500    ASP A 294      -84.35   -133.85                                   
REMARK 500    PHE A 393      -58.90   -132.10                                   
REMARK 500    LYS A 409      -88.61   -101.88                                   
REMARK 500    SER A 496       46.97     38.84                                   
REMARK 500    LEU A 524      -63.96   -120.17                                   
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 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  48   NE2                                                    
REMARK 620 2 ACT A 614   O   104.1                                              
REMARK 620 3 HOH A 731   O    94.8 106.2                                        
REMARK 620 4 ACT A 614   OXT  89.5  60.5 166.7                                  
REMARK 620 5 HOH A 714   O   175.2  80.6  83.0  93.6                            
REMARK 620 6 HOH A 867   O    97.7 150.2  91.7 100.3  78.1                      
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   OD1                                                    
REMARK 620 2 GLU A  78   OE2 114.5                                              
REMARK 620 3 ASP A 476   OD2  45.7  73.6                                        
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 ASP A  97   OD1                                                    
REMARK 620 2 ASP A  97   OD2  52.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 604  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 115   NE2                                                    
REMARK 620 2 ACT A 615   O   108.2                                              
REMARK 620 N                    1                                               
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 168   NE2                                                    
REMARK 620 2 ACT A 613   OXT 113.3                                              
REMARK 620 3 GLU A 342   OE1  29.2 111.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 611  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 193   OE2                                                    
REMARK 620 2 ASP A 437   OD1 127.9                                              
REMARK 620 3 ASP A 438   OD1 142.5  89.1                                        
REMARK 620 4 HOH A 702   O   106.3 111.2  56.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 608  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 283   ND1                                                    
REMARK 620 2 ACT A 618   O   105.1                                              
REMARK 620 3 HOH A 855   O    98.3  96.7                                        
REMARK 620 N                    1     2                                         
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 435   NE2                                                    
REMARK 620 2 ARG A 454   NH2 123.5                                              
REMARK 620 3 ASP A 457   OD1 109.3  93.2                                        
REMARK 620 N                    1     2                                         
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 HIS A 487   NE2                                                    
REMARK 620 2 GLU A 489   OE1  97.4                                              
REMARK 620 3 ACT A 612   O   143.4 110.7                                        
REMARK 620 4 ACT A 612   OXT  85.6 118.7  60.8                                  
REMARK 620 5 ASP A  79   OD2  65.4  89.8  91.1  36.9                            
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 ZN A 609                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 610                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN 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 ACT A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 618                 
DBREF  6H18 A    2   533  UNP    P19835   CEL_HUMAN       22    553             
SEQADV 6H18 HIS A  -13  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 HIS A  -12  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 HIS A  -11  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 HIS A  -10  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 HIS A   -9  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 HIS A   -8  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 HIS A   -7  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 HIS A   -6  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 GLU A   -5  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 ASN A   -4  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 LEU A   -3  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 TYR A   -2  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 PHE A   -1  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 GLN A    0  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 SER A    1  UNP  P19835              EXPRESSION TAG                 
SEQADV 6H18 ASP A  186  UNP  P19835    ASN   206 ENGINEERED MUTATION            
SEQADV 6H18 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 SGB          
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                                                          
MODRES 6H18 SGB A  194  SER  MODIFIED RESIDUE                                   
HET    SGB  A 194      13                                                       
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     ZN  A 609       1                                                       
HET     ZN  A 610       1                                                       
HET     ZN  A 611       1                                                       
HET    ACT  A 612       4                                                       
HET    ACT  A 613       4                                                       
HET    ACT  A 614       4                                                       
HET    ACT  A 615       4                                                       
HET    ACT  A 616       4                                                       
HET    ACT  A 617       4                                                       
HET    ACT  A 618       4                                                       
HETNAM     SGB O-[(S)-METHYL(1-METHYLETHOXY)PHOSPHORYL]-L-SERINE                
HETNAM      ZN ZINC ION                                                         
HETNAM     ACT ACETATE ION                                                      
FORMUL   1  SGB    C7 H16 N O5 P                                                
FORMUL   2   ZN    11(ZN 2+)                                                    
FORMUL  13  ACT    7(C2 H3 O2 1-)                                               
FORMUL  20  HOH   *186(H2 O)                                                    
HELIX    1 AA1 GLY A  127  ASN A  135  1                                   9    
HELIX    2 AA2 VAL A  145  LEU A  151  1                                   7    
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 SGB A  194  SER A  206  1                                  13    
HELIX    6 AA6 PRO A  207  LYS A  210  5                                   4    
HELIX    7 AA7 ASN A  232  VAL A  244  1                                  13    
HELIX    8 AA8 ASP A  250  VAL A  260  1                                  11    
HELIX    9 AA9 ASP A  262  LEU A  268  1                                   7    
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  ASN A  333  5                                   4    
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  ASN A  407  1                                  15    
HELIX   19 AC1 ASP A  438  PHE A  443  1                                   6    
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    
SHEET    1 AA1 3 VAL A   6  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  GLU A  14           
SHEET    1 AA211 VAL A  16  LEU A  20  0                                        
SHEET    2 AA211 ASP A  25  PRO A  34 -1  O  ILE A  29   N  VAL A  16           
SHEET    3 AA211 TYR A  82  GLN A  89 -1  O  ILE A  85   N  PHE A  30           
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 601     1555   1555  2.19  
LINK         OD1 ASP A  77                ZN    ZN A 603     1555   1555  1.96  
LINK         OE2 GLU A  78                ZN    ZN A 603     1555   1555  1.99  
LINK         OD1 ASP A  97                ZN    ZN A 607     1555   1555  2.56  
LINK         OD2 ASP A  97                ZN    ZN A 607     1555   1555  2.39  
LINK         NE2 HIS A 115                ZN    ZN A 604     1555   1555  2.29  
LINK         NE2 HIS A 168                ZN    ZN A 602     1555   1555  2.07  
LINK         C   GLU A 193                 N   SGB A 194     1555   1555  1.33  
LINK         OE2 GLU A 193                ZN    ZN A 611     1555   1555  2.42  
LINK         C   SGB A 194                 N   ALA A 195     1555   1555  1.34  
LINK         ND1 HIS A 283                ZN    ZN A 608     1555   1555  2.10  
LINK         OE1 GLU A 350                ZN    ZN A 609     1555   1555  2.09  
LINK         NE2 HIS A 435                ZN    ZN A 605     1555   1555  2.18  
LINK         OD1 ASP A 437                ZN    ZN A 611     1555   1555  2.36  
LINK         OD1 ASP A 438                ZN    ZN A 611     1555   1555  2.38  
LINK         NH2 ARG A 454                ZN    ZN A 605     1555   1555  2.46  
LINK         OD1 ASP A 457                ZN    ZN A 605     1555   1555  2.06  
LINK         NE2 HIS A 487                ZN    ZN A 606     1555   1555  2.09  
LINK         OE1 GLU A 489                ZN    ZN A 606     1555   1555  1.96  
LINK        ZN    ZN A 601                 O   ACT A 614     1555   1555  2.18  
LINK        ZN    ZN A 601                 O   HOH A 731     1555   1555  2.08  
LINK        ZN    ZN A 601                 OXT ACT A 614     1555   1555  2.34  
LINK        ZN    ZN A 601                 O   HOH A 714     1555   1555  2.40  
LINK        ZN    ZN A 601                 O   HOH A 867     1555   1555  2.11  
LINK        ZN    ZN A 602                 OXT ACT A 613     1555   1555  1.95  
LINK        ZN    ZN A 604                 O   ACT A 615     1555   1555  2.46  
LINK        ZN    ZN A 606                 O   ACT A 612     1555   1555  2.05  
LINK        ZN    ZN A 606                 OXT ACT A 612     1555   1555  2.37  
LINK        ZN    ZN A 608                 O   ACT A 618     1555   1555  2.62  
LINK        ZN    ZN A 608                 O   HOH A 855     1555   1555  2.29  
LINK        ZN    ZN A 611                 O   HOH A 702     1555   1555  2.33  
LINK         OD2 ASP A  79                ZN    ZN A 606     1555   3555  2.17  
LINK         OE1 GLU A 342                ZN    ZN A 602     1555   2554  1.96  
LINK         OD2 ASP A 476                ZN    ZN A 603     1555   3545  1.99  
CISPEP   1 ALA A  275    GLY A  276          0        -5.09                     
CISPEP   2 HIS A  420    PRO A  421          0        -7.42                     
SITE     1 AC1  5 HIS A  48  ACT A 614  HOH A 714  HOH A 731                    
SITE     2 AC1  5 HOH A 867                                                     
SITE     1 AC2  3 HIS A 168  GLU A 342  ACT A 613                               
SITE     1 AC3  3 ASP A  77  GLU A  78  ASP A 476                               
SITE     1 AC4  3 HIS A 115  ACT A 615  ACT A 616                               
SITE     1 AC5  5 HIS A 420  HIS A 435  TYR A 441  ARG A 454                    
SITE     2 AC5  5 ASP A 457                                                     
SITE     1 AC6  4 ASP A  79  HIS A 487  GLU A 489  ACT A 612                    
SITE     1 AC7  1 ASP A  97                                                     
SITE     1 AC8  3 HIS A 283  ACT A 618  HOH A 855                               
SITE     1 AC9  1 GLU A 350                                                     
SITE     1 AD1  3 HIS A 322  ASP A 434  ASP A 437                               
SITE     1 AD2  6 GLU A 193  ASN A 317  ASP A 437  ASP A 438                    
SITE     2 AD2  6 ACT A 617  HOH A 702                                          
SITE     1 AD3  6 ASP A  77  ASP A  79  HIS A 487  GLU A 489                    
SITE     2 AD3  6 PRO A 490   ZN A 606                                          
SITE     1 AD4  6 HIS A 168  TYR A 208  GLU A 341  GLU A 342                    
SITE     2 AD4  6  ZN A 602  HOH A 745                                          
SITE     1 AD5  4 HIS A  48  TYR A  82   ZN A 601  HOH A 714                    
SITE     1 AD6  3 PHE A  60   ZN A 604  ACT A 616                               
SITE     1 AD7  4 ARG A  63  TYR A  75   ZN A 604  ACT A 615                    
SITE     1 AD8  6 GLU A 193  SGB A 194  ASP A 320  ILE A 323                    
SITE     2 AD8  6 ASP A 437   ZN A 611                                          
SITE     1 AD9  4 HIS A 283  GLU A 350   ZN A 608  HOH A 855                    
CRYST1   55.702   98.055  110.888  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      0.017953  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010198  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009018        0.00000                         
TER    4111      THR A 533                                                      
MASTER      421    0   19   24   16    0   24    6 4296    1   80   43          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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