Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 4QWM-pdb

Name Class
4QWM-pdb
HEADER    HYDROLASE                               16-JUL-14   4QWM              
TITLE     KINETIC CRYSTALLOGRAPHY OF ALPHA_E7-CARBOXYLESTERSE FROM LUCILLA      
TITLE    2 CUPRINA - ABSORBED X-RAY DOSE 1.85 MGY                               
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: GREENBOTTLE 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   22-JUL-15 4QWM    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.    2.17 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-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.97                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 29343                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1492                            
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 45.9788 -  4.8244    0.99     2667   158  0.1574 0.2081        
REMARK   3     2  4.8244 -  3.8298    1.00     2572   149  0.1442 0.1844        
REMARK   3     3  3.8298 -  3.3459    1.00     2559   118  0.1667 0.2098        
REMARK   3     4  3.3459 -  3.0400    1.00     2513   146  0.1836 0.2647        
REMARK   3     5  3.0400 -  2.8222    1.00     2548   129  0.1949 0.2733        
REMARK   3     6  2.8222 -  2.6558    1.00     2486   152  0.1978 0.2342        
REMARK   3     7  2.6558 -  2.5228    1.00     2521   117  0.2041 0.2872        
REMARK   3     8  2.5228 -  2.4130    1.00     2477   139  0.2055 0.3003        
REMARK   3     9  2.4130 -  2.3201    1.00     2510   125  0.2298 0.3358        
REMARK   3    10  2.3201 -  2.2400    1.00     2494   120  0.2319 0.2930        
REMARK   3    11  2.2400 -  2.1700    0.99     2504   139  0.2366 0.3048        
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)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.560           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.62                          
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     :  1.016           6341                                  
REMARK   3   CHIRALITY :  0.039            677                                  
REMARK   3   PLANARITY :  0.005            817                                  
REMARK   3   DIHEDRAL  : 14.118           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 4QWM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JUL-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB086605.                                      
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) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : 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   : 29376                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.170                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.14200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.01376                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.400                              
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: 4FNM                                                 
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      111.02950            
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      111.02950            
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       24.24500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.50000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       24.24500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.50000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      111.02950            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       24.24500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.50000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      111.02950            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       24.24500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.50000            
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 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 907  LIES ON A SPECIAL POSITION.                          
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     P1   DPF A   601              1.49            
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    ALA A  75      153.55    -49.36                                   
REMARK 500    THR A 118      143.00   -177.78                                   
REMARK 500    SER A 218     -114.80     58.92                                   
REMARK 500    THR A 320     -165.51   -119.14                                   
REMARK 500    CYS A 323      132.49    -39.32                                   
REMARK 500    TYR A 350       59.75   -142.37                                   
REMARK 500    PHE A 421      -60.85   -138.24                                   
REMARK 500    HIS A 435       29.14   -152.44                                   
REMARK 500    THR A 472       -4.56     78.23                                   
REMARK 500    GLN A 482        3.97    -68.54                                   
REMARK 500    SER A 542     -144.35   -127.42                                   
REMARK 500    HIS A 566       55.08   -145.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     DPF A  601                                                       
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  4QWM A    1   570  UNP    Q25252   Q25252_LUCCU     1    570             
SEQADV 4QWM LEU A  364  UNP  Q25252    MET   364 ENGINEERED MUTATION            
SEQADV 4QWM PHE A  419  UNP  Q25252    ILE   419 ENGINEERED MUTATION            
SEQADV 4QWM THR A  472  UNP  Q25252    ALA   472 ENGINEERED MUTATION            
SEQADV 4QWM THR A  505  UNP  Q25252    ILE   505 ENGINEERED MUTATION            
SEQADV 4QWM GLU A  530  UNP  Q25252    LYS   530 ENGINEERED MUTATION            
SEQADV 4QWM 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   *208(H2 O)                                                    
HELIX    1   1 SER A    6  LEU A   27  1                                  22    
HELIX    2   2 VAL A   68  ARG A   72  5                                   5    
HELIX    3   3 TYR A  152  LYS A  156  5                                   5    
HELIX    4   4 LEU A  167  LEU A  173  1                                   7    
HELIX    5   5 SER A  177  ASN A  181  5                                   5    
HELIX    6   6 ASN A  185  CYS A  202  1                                  18    
HELIX    7   7 ALA A  203  PHE A  205  5                                   3    
HELIX    8   8 SER A  218  THR A  230  1                                  13    
HELIX    9   9 GLU A  231  ARG A  234  5                                   4    
HELIX   10  10 HIS A  258  ALA A  267  1                                  10    
HELIX   11  11 ASN A  274  MET A  283  1                                  10    
HELIX   12  12 LYS A  286  LEU A  293  1                                   8    
HELIX   13  13 GLU A  294  VAL A  297  5                                   4    
HELIX   14  14 THR A  299  ASN A  305  1                                   7    
HELIX   15  15 HIS A  328  VAL A  333  1                                   6    
HELIX   16  16 LYS A  334  THR A  335  5                                   2    
HELIX   17  17 ALA A  336  ILE A  341  5                                   6    
HELIX   18  18 TYR A  350  PHE A  354  5                                   5    
HELIX   19  19 PHE A  355  MET A  362  1                                   8    
HELIX   20  20 PRO A  363  THR A  371  5                                   9    
HELIX   21  21 CYS A  372  VAL A  376  5                                   5    
HELIX   22  22 ALA A  387  VAL A  402  1                                  16    
HELIX   23  23 THR A  408  PHE A  421  1                                  14    
HELIX   24  24 PHE A  421  ASN A  434  1                                  14    
HELIX   25  25 PRO A  456  ARG A  461  1                                   6    
HELIX   26  26 GLU A  474  PHE A  478  5                                   5    
HELIX   27  27 SER A  491  GLY A  511  1                                  21    
HELIX   28  28 GLU A  552  SER A  561  1                                  10    
HELIX   29  29 MET A  562  GLU A  564  5                                   3    
HELIX   30  30 HIS A  566  PHE A  570  5                                   5    
SHEET    1   A 3 THR A  28  ALA A  35  0                                        
SHEET    2   A 3 LYS A  41  LEU A  48 -1  O  GLY A  44   N  VAL A  33           
SHEET    3   A 3 VAL A  85  ASP A  87  1  O  ARG A  86   N  LYS A  43           
SHEET    1   B12 THR A  28  ALA A  35  0                                        
SHEET    2   B12 LYS A  41  LEU A  48 -1  O  GLY A  44   N  VAL A  33           
SHEET    3   B12 SER A  54  PRO A  62 -1  O  TYR A  55   N  ARG A  47           
SHEET    4   B12 TYR A 113  THR A 118 -1  O  THR A 118   N  TYR A  56           
SHEET    5   B12 VAL A 159  ILE A 163 -1  O  LEU A 160   N  TYR A 117           
SHEET    6   B12 ARG A 127  ILE A 133  1  N  TYR A 132   O  ILE A 161           
SHEET    7   B12 GLY A 207  GLU A 217  1  O  THR A 213   N  VAL A 129           
SHEET    8   B12 ARG A 239  MET A 243  1  O  MET A 243   N  GLY A 216           
SHEET    9   B12 THR A 343  THR A 348  1  O  MET A 344   N  LEU A 242           
SHEET   10   B12 VAL A 441  PHE A 446  1  O  PHE A 446   N  ASN A 347           
SHEET   11   B12 LYS A 537  ILE A 541  1  O  ILE A 541   N  ARG A 445           
SHEET   12   B12 LEU A 545  ASP A 549 -1  O  LYS A 546   N  ASN A 540           
SHEET    1   C 2 GLN A  97  VAL A  98  0                                        
SHEET    2   C 2 VAL A 105  CYS A 106 -1  O  CYS A 106   N  GLN A  97           
SITE     1 AC1  9 GLY A 136  GLY A 137  SER A 218  ALA A 219                    
SITE     2 AC1  9 TRP A 251  MET A 308  PHE A 354  TYR A 457                    
SITE     3 AC1  9 HIS A 471                                                     
CRYST1   48.490  101.000  222.059  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      0.020623  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009901  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004503        0.00000                         
TER    4565      PHE A 570                                                      
MASTER      286    0    1   30   17    0    3    6 4775    1    8   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
webmaster

Acknowledgements and disclaimer