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LongText Report for: 4UBN-pdb

Name Class
4UBN-pdb
HEADER    HYDROLASE                               13-AUG-14   4UBN              
TITLE     KINETIC CRYSTALLOGRAPHY OF ALPHA_E7-CARBOXYLESTERSE FROM LUCILLA      
TITLE    2 CUPRINA - ABSORBED X-RAY DOSE 1.85 MGY TEMP 150K                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3;                                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LUCILIA CUPRINA;                                
SOURCE   3 ORGANISM_COMMON: GREEN BOTTLE FLY;                                   
SOURCE   4 ORGANISM_TAXID: 7375;                                                
SOURCE   5 STRAIN: LS2;                                                         
SOURCE   6 GENE: LCAE7;                                                         
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PETMCSIII                                 
KEYWDS    ALPHA/BETA HYDROLASE FOLD, CARBOXYLESTERASE, HYDROLASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.J.JACKSON,P.D.CARR,M.WEIK,T.HUBER,T.MEIRELLES,G.CORREY              
REVDAT   1   19-AUG-15 4UBN    0                                                
JRNL        AUTH   C.J.JACKSON,P.D.CARR,M.WEIK,T.HUBER,T.MEIRELLES,G.CORREY     
JRNL        TITL   MAPPING THE ACCESSIBLE CONFORMATIONAL LANDSCAPE OF AN        
JRNL        TITL 2 ORGANOPHOSPHATE DETOXIFYING INSECT CARBOXYLESTERASE USING    
JRNL        TITL 3 KINETIC CRYSTALLOGRAPHY AND CONFORMATIONAL ENSEMBLE ANALYSIS 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.02 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1639)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.13                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.980                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 36905                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1871                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.1460 -  4.7481    1.00     2871   168  0.1636 0.2054        
REMARK   3     2  4.7481 -  3.7693    1.00     2733   160  0.1617 0.2030        
REMARK   3     3  3.7693 -  3.2930    1.00     2764   129  0.1882 0.2418        
REMARK   3     4  3.2930 -  2.9920    1.00     2720   152  0.2159 0.2467        
REMARK   3     5  2.9920 -  2.7775    1.00     2720   147  0.2291 0.2958        
REMARK   3     6  2.7775 -  2.6138    1.00     2685   152  0.2208 0.2717        
REMARK   3     7  2.6138 -  2.4829    1.00     2696   141  0.2257 0.3190        
REMARK   3     8  2.4829 -  2.3748    1.00     2711   133  0.2283 0.3268        
REMARK   3     9  2.3748 -  2.2834    1.00     2713   132  0.2316 0.2941        
REMARK   3    10  2.2834 -  2.2046    1.00     2670   156  0.2392 0.3190        
REMARK   3    11  2.2046 -  2.1357    1.00     2677   126  0.2527 0.3047        
REMARK   3    12  2.1357 -  2.0746    0.99     2646   138  0.2772 0.3582        
REMARK   3    13  2.0746 -  2.0200    0.91     2428   137  0.3069 0.3824        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.600           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           4688                                  
REMARK   3   ANGLE     :  1.047           6341                                  
REMARK   3   CHIRALITY :  0.040            677                                  
REMARK   3   PLANARITY :  0.005            817                                  
REMARK   3   DIHEDRAL  : 13.717           1759                                  
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 4UBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203149.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 150                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9393                             
REMARK 200  MONOCHROMATOR                  : CHANNEL CUT                        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36959                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.020                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.130                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.800                              
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: 4QWM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM PEG2000, 0.1M MES, PH 4.6, VAPOR   
REMARK 280  DIFFUSION, TEMPERATURE 298K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      111.49550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      111.49550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       24.65150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.67550            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       24.65150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.67550            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      111.49550            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       24.65150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.67550            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      111.49550            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       24.65150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.67550            
REMARK 290   SMTRY3   8  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: 380 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 22060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 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     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     PHE A     3                                                      
REMARK 465     ASN A     4                                                      
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   OG   SER A   218     O4   DPF A   601              2.04            
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    PHE A  73       -2.04     74.12                                   
REMARK 500    ASN A 122       65.99   -119.70                                   
REMARK 500    SER A 218     -119.97     58.42                                   
REMARK 500    PHE A 421      -60.17   -132.23                                   
REMARK 500    HIS A 435       52.53   -142.25                                   
REMARK 500    HIS A 471      128.75    -38.88                                   
REMARK 500    THR A 472       -8.92     83.94                                   
REMARK 500    SER A 542     -143.16   -126.16                                   
REMARK 500    HIS A 566       42.39   -151.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DPF A 601                 
DBREF  4UBN A    1   570  UNP    Q25252   Q25252_LUCCU     1    570             
SEQADV 4UBN LEU A  364  UNP  Q25252    MET   364 ENGINEERED MUTATION            
SEQADV 4UBN PHE A  419  UNP  Q25252    ILE   419 ENGINEERED MUTATION            
SEQADV 4UBN THR A  472  UNP  Q25252    ALA   472 ENGINEERED MUTATION            
SEQADV 4UBN THR A  505  UNP  Q25252    ILE   505 ENGINEERED MUTATION            
SEQADV 4UBN GLU A  530  UNP  Q25252    LYS   530 ENGINEERED MUTATION            
SEQADV 4UBN GLY A  554  UNP  Q25252    ASP   554 ENGINEERED MUTATION            
SEQRES   1 A  570  MET ASN PHE ASN VAL SER LEU MET GLU LYS LEU LYS TRP          
SEQRES   2 A  570  LYS ILE LYS CYS ILE GLU ASN LYS PHE LEU ASN TYR ARG          
SEQRES   3 A  570  LEU THR THR ASN GLU THR VAL VAL ALA GLU THR GLU TYR          
SEQRES   4 A  570  GLY LYS VAL LYS GLY VAL LYS ARG LEU THR VAL TYR ASP          
SEQRES   5 A  570  ASP SER TYR TYR SER PHE GLU GLY ILE PRO TYR ALA GLN          
SEQRES   6 A  570  PRO PRO VAL GLY GLU LEU ARG PHE LYS ALA PRO GLN ARG          
SEQRES   7 A  570  PRO THR PRO TRP ASP GLY VAL ARG ASP CYS CYS ASN HIS          
SEQRES   8 A  570  LYS ASP LYS SER VAL GLN VAL ASP PHE ILE THR GLY LYS          
SEQRES   9 A  570  VAL CYS GLY SER GLU ASP CYS LEU TYR LEU SER VAL TYR          
SEQRES  10 A  570  THR ASN ASN LEU ASN PRO GLU THR LYS ARG PRO VAL LEU          
SEQRES  11 A  570  VAL TYR ILE HIS GLY GLY GLY PHE ILE ILE GLY GLU ASN          
SEQRES  12 A  570  HIS ARG ASP MET TYR GLY PRO ASP TYR PHE ILE LYS LYS          
SEQRES  13 A  570  ASP VAL VAL LEU ILE ASN ILE GLN TYR ARG LEU GLY ALA          
SEQRES  14 A  570  LEU GLY PHE LEU SER LEU ASN SER GLU ASP LEU ASN VAL          
SEQRES  15 A  570  PRO GLY ASN ALA GLY LEU LYS ASP GLN VAL MET ALA LEU          
SEQRES  16 A  570  ARG TRP ILE LYS ASN ASN CYS ALA ASN PHE GLY GLY ASN          
SEQRES  17 A  570  PRO ASP ASN ILE THR VAL PHE GLY GLU SER ALA GLY ALA          
SEQRES  18 A  570  ALA SER THR HIS TYR MET MET LEU THR GLU GLN THR ARG          
SEQRES  19 A  570  GLY LEU PHE HIS ARG GLY ILE LEU MET SER GLY ASN ALA          
SEQRES  20 A  570  ILE CYS PRO TRP ALA ASN THR GLN CYS GLN HIS ARG ALA          
SEQRES  21 A  570  PHE THR LEU ALA LYS LEU ALA GLY TYR LYS GLY GLU ASP          
SEQRES  22 A  570  ASN ASP LYS ASP VAL LEU GLU PHE LEU MET LYS ALA LYS          
SEQRES  23 A  570  PRO GLN ASP LEU ILE LYS LEU GLU GLU LYS VAL LEU THR          
SEQRES  24 A  570  LEU GLU GLU ARG THR ASN LYS VAL MET PHE PRO PHE GLY          
SEQRES  25 A  570  PRO THR VAL GLU PRO TYR GLN THR ALA ASP CYS VAL LEU          
SEQRES  26 A  570  PRO LYS HIS PRO ARG GLU MET VAL LYS THR ALA TRP GLY          
SEQRES  27 A  570  ASN SER ILE PRO THR MET MET GLY ASN THR SER TYR GLU          
SEQRES  28 A  570  GLY LEU PHE PHE THR SER ILE LEU LYS GLN MET PRO LEU          
SEQRES  29 A  570  LEU VAL LYS GLU LEU GLU THR CYS VAL ASN PHE VAL PRO          
SEQRES  30 A  570  SER GLU LEU ALA ASP ALA GLU ARG THR ALA PRO GLU THR          
SEQRES  31 A  570  LEU GLU MET GLY ALA LYS ILE LYS LYS ALA HIS VAL THR          
SEQRES  32 A  570  GLY GLU THR PRO THR ALA ASP ASN PHE MET ASP LEU CYS          
SEQRES  33 A  570  SER HIS PHE TYR PHE TRP PHE PRO MET HIS ARG LEU LEU          
SEQRES  34 A  570  GLN LEU ARG PHE ASN HIS THR SER GLY THR PRO VAL TYR          
SEQRES  35 A  570  LEU TYR ARG PHE ASP PHE ASP SER GLU ASP LEU ILE ASN          
SEQRES  36 A  570  PRO TYR ARG ILE MET ARG SER GLY ARG GLY VAL LYS GLY          
SEQRES  37 A  570  VAL SER HIS THR ASP GLU LEU THR TYR PHE PHE TRP ASN          
SEQRES  38 A  570  GLN LEU ALA LYS ARG MET PRO LYS GLU SER ARG GLU TYR          
SEQRES  39 A  570  LYS THR ILE GLU ARG MET THR GLY ILE TRP THR GLN PHE          
SEQRES  40 A  570  ALA THR THR GLY ASN PRO TYR SER ASN GLU ILE GLU GLY          
SEQRES  41 A  570  MET GLU ASN VAL SER TRP ASP PRO ILE GLU LYS SER ASP          
SEQRES  42 A  570  GLU VAL TYR LYS CYS LEU ASN ILE SER ASP GLU LEU LYS          
SEQRES  43 A  570  MET ILE ASP VAL PRO GLU MET GLY LYS ILE LYS GLN TRP          
SEQRES  44 A  570  GLU SER MET PHE GLU LYS HIS ARG ASP LEU PHE                  
HET    DPF  A 601       8                                                       
HETNAM     DPF DIETHYL HYDROGEN PHOSPHATE                                       
FORMUL   2  DPF    C4 H11 O4 P                                                  
FORMUL   3  HOH   *203(H2 O)                                                    
HELIX    1 AA1 SER A    6  LEU A   27  1                                  22    
HELIX    2 AA2 VAL A   68  ARG A   72  5                                   5    
HELIX    3 AA3 HIS A  144  GLY A  149  1                                   6    
HELIX    4 AA4 TYR A  152  LYS A  156  5                                   5    
HELIX    5 AA5 LEU A  167  LEU A  173  1                                   7    
HELIX    6 AA6 SER A  177  ASN A  181  5                                   5    
HELIX    7 AA7 ASN A  185  CYS A  202  1                                  18    
HELIX    8 AA8 ALA A  203  PHE A  205  5                                   3    
HELIX    9 AA9 SER A  218  THR A  230  1                                  13    
HELIX   10 AB1 GLU A  231  ARG A  234  5                                   4    
HELIX   11 AB2 HIS A  258  ALA A  267  1                                  10    
HELIX   12 AB3 ASN A  274  ALA A  285  1                                  12    
HELIX   13 AB4 LYS A  286  LEU A  293  1                                   8    
HELIX   14 AB5 GLU A  294  VAL A  297  5                                   4    
HELIX   15 AB6 THR A  299  ASN A  305  1                                   7    
HELIX   16 AB7 HIS A  328  LYS A  334  1                                   7    
HELIX   17 AB8 THR A  335  ILE A  341  5                                   7    
HELIX   18 AB9 TYR A  350  PHE A  354  5                                   5    
HELIX   19 AC1 PHE A  355  MET A  362  1                                   8    
HELIX   20 AC2 PRO A  363  THR A  371  5                                   9    
HELIX   21 AC3 CYS A  372  VAL A  376  5                                   5    
HELIX   22 AC4 ALA A  387  VAL A  402  1                                  16    
HELIX   23 AC5 THR A  408  PHE A  421  1                                  14    
HELIX   24 AC6 PHE A  421  ASN A  434  1                                  14    
HELIX   25 AC7 PRO A  456  ARG A  461  1                                   6    
HELIX   26 AC8 THR A  472  PHE A  478  5                                   7    
HELIX   27 AC9 SER A  491  GLY A  511  1                                  21    
HELIX   28 AD1 GLU A  552  SER A  561  1                                  10    
HELIX   29 AD2 MET A  562  GLU A  564  5                                   3    
HELIX   30 AD3 HIS A  566  PHE A  570  5                                   5    
SHEET    1 AA1 3 THR A  28  ALA A  35  0                                        
SHEET    2 AA1 3 LYS A  41  LEU A  48 -1  O  GLY A  44   N  VAL A  33           
SHEET    3 AA1 3 VAL A  85  ASP A  87  1  O  ARG A  86   N  LYS A  43           
SHEET    1 AA212 THR A  28  ALA A  35  0                                        
SHEET    2 AA212 LYS A  41  LEU A  48 -1  O  GLY A  44   N  VAL A  33           
SHEET    3 AA212 SER A  54  PRO A  62 -1  O  SER A  57   N  VAL A  45           
SHEET    4 AA212 TYR A 113  THR A 118 -1  O  THR A 118   N  TYR A  56           
SHEET    5 AA212 VAL A 159  ILE A 163 -1  O  LEU A 160   N  TYR A 117           
SHEET    6 AA212 ARG A 127  ILE A 133  1  N  TYR A 132   O  ILE A 161           
SHEET    7 AA212 GLY A 207  GLU A 217  1  O  ASN A 208   N  ARG A 127           
SHEET    8 AA212 ARG A 239  MET A 243  1  O  ARG A 239   N  VAL A 214           
SHEET    9 AA212 THR A 343  THR A 348  1  O  MET A 344   N  LEU A 242           
SHEET   10 AA212 VAL A 441  PHE A 446  1  O  TYR A 442   N  MET A 345           
SHEET   11 AA212 LYS A 537  ILE A 541  1  O  ILE A 541   N  ARG A 445           
SHEET   12 AA212 LEU A 545  ASP A 549 -1  O  ILE A 548   N  CYS A 538           
SHEET    1 AA3 2 GLN A  97  VAL A  98  0                                        
SHEET    2 AA3 2 VAL A 105  CYS A 106 -1  O  CYS A 106   N  GLN A  97           
LINK         OG  SER A 218                 P1  DPF A 601     1555   1555  1.48  
SITE     1 AC1 10 GLY A 136  GLY A 137  SER A 218  ALA A 219                    
SITE     2 AC1 10 TRP A 251  MET A 308  PHE A 354  TYR A 457                    
SITE     3 AC1 10 HIS A 471  THR A 472                                          
CRYST1   49.303  101.351  222.991  90.00  90.00  90.00 C 2 2 21      8          
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      0.020283  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009867  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004484        0.00000                         
TER    4565      PHE A 570                                                      
MASTER      272    0    1   30   17    0    3    6 4770    1    9   44          
END                                                                             

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