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LongText Report for: 6o4w-pdb

Name Class
6o4w-pdb
HEADER    HYDROLASE                               01-MAR-19   6O4W              
TITLE     BINARY COMPLEX OF NATIVE HACHE WITH DONEPEZIL                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 32-578;                                           
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACHE;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK293                                  
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.GERLITS,A.KOVALEVSKY,Z.RADIC                                        
REVDAT   1   19-JUN-19 6O4W    0                                                
JRNL        AUTH   O.GERLITS,K.Y.HO,X.CHENG,D.BLUMENTHAL,P.TAYLOR,A.KOVALEVSKY, 
JRNL        AUTH 2 Z.RADIC                                                      
JRNL        TITL   A NEW CRYSTAL FORM OF HUMAN ACETYLCHOLINESTERASE FOR         
JRNL        TITL 2 EXPLORATORY ROOM-TEMPERATURE CRYSTALLOGRAPHY STUDIES.        
JRNL        REF    CHEM.BIOL.INTERACT.                        2019              
JRNL        REFN                   ISSN 0009-2797                               
JRNL        PMID   31176713                                                     
JRNL        DOI    10.1016/J.CBI.2019.06.011                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155)                                 
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) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.67                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.980                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 81980                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.410                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1978                            
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 38.6745 -  5.6511    0.93     6004   151  0.1454 0.1686        
REMARK   3     2  5.6511 -  4.4876    0.89     5729   144  0.1376 0.1555        
REMARK   3     3  4.4876 -  3.9210    0.95     6150   158  0.1431 0.1545        
REMARK   3     4  3.9210 -  3.5628    0.89     5758   139  0.1739 0.1821        
REMARK   3     5  3.5628 -  3.3076    0.93     5959   154  0.1900 0.2202        
REMARK   3     6  3.3076 -  3.1126    0.94     6076   151  0.2022 0.2494        
REMARK   3     7  3.1126 -  2.9568    0.95     6106   153  0.2098 0.2402        
REMARK   3     8  2.9568 -  2.8281    0.88     5733   139  0.2082 0.2381        
REMARK   3     9  2.8281 -  2.7193    0.89     5743   141  0.2244 0.2509        
REMARK   3    10  2.7193 -  2.6255    0.92     5933   142  0.2454 0.2722        
REMARK   3    11  2.6255 -  2.5434    0.92     6000   136  0.2571 0.3212        
REMARK   3    12  2.5434 -  2.4707    0.90     5767   145  0.2518 0.3194        
REMARK   3    13  2.4707 -  2.4057    0.80     5187   128  0.2649 0.3083        
REMARK   3    14  2.4057 -  2.3470    0.60     3857    97  0.2962 0.3570        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.490           
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      :  0.003           8744                                  
REMARK   3   ANGLE     :  0.655          11946                                  
REMARK   3   CHIRALITY :  0.044           1258                                  
REMARK   3   PLANARITY :  0.005           1576                                  
REMARK   3   DIHEDRAL  : 14.971           5092                                  
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 6O4W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000240021.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-APR-16                          
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               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66738                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.1                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : 0.03000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42500                            
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: 4EY4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM SODIUM CITRATE, 100 MM HEPES, PH   
REMARK 280  7, AND 6-8 % PEG6000 OR PEG3350, VAPOR DIFFUSION, SITTING DROP,     
REMARK 280  TEMPERATURE 283K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.13767            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       86.27533            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     PRO A    -1                                                      
REMARK 465     LEU A     0                                                      
REMARK 465     GLU A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     ASP A   544                                                      
REMARK 465     THR A   545                                                      
REMARK 465     LEU A   546                                                      
REMARK 465     ASP A   547                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     PRO B    -1                                                      
REMARK 465     LEU B     0                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     ASP B   544                                                      
REMARK 465     THR B   545                                                      
REMARK 465     LEU B   546                                                      
REMARK 465     ASP B   547                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 290   O   -  C   -  N   ANGL. DEV. = -10.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 203     -118.91     51.86                                   
REMARK 500    ASP A 306      -82.67   -101.78                                   
REMARK 500    VAL A 407      -61.16   -127.66                                   
REMARK 500    ASN A 464       40.85   -101.76                                   
REMARK 500    SER B 203     -117.34     52.20                                   
REMARK 500    ASP B 306      -81.03   -100.88                                   
REMARK 500    VAL B 407      -60.17   -126.95                                   
REMARK 500    ASN B 464       41.59   -106.55                                   
REMARK 500    ARG B 493      -71.75    -97.20                                   
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 GOL A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E20 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E20 B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 B 607                 
DBREF  6O4W A    1   547  UNP    P22303   ACES_HUMAN      32    578             
DBREF  6O4W B    1   547  UNP    P22303   ACES_HUMAN      32    578             
SEQADV 6O4W GLY A   -2  UNP  P22303              EXPRESSION TAG                 
SEQADV 6O4W PRO A   -1  UNP  P22303              EXPRESSION TAG                 
SEQADV 6O4W LEU A    0  UNP  P22303              EXPRESSION TAG                 
SEQADV 6O4W GLY B   -2  UNP  P22303              EXPRESSION TAG                 
SEQADV 6O4W PRO B   -1  UNP  P22303              EXPRESSION TAG                 
SEQADV 6O4W LEU B    0  UNP  P22303              EXPRESSION TAG                 
SEQRES   1 A  550  GLY PRO LEU GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL          
SEQRES   2 A  550  THR VAL ARG GLY GLY ARG LEU ARG GLY ILE ARG LEU LYS          
SEQRES   3 A  550  THR PRO GLY GLY PRO VAL SER ALA PHE LEU GLY ILE PRO          
SEQRES   4 A  550  PHE ALA GLU PRO PRO MET GLY PRO ARG ARG PHE LEU PRO          
SEQRES   5 A  550  PRO GLU PRO LYS GLN PRO TRP SER GLY VAL VAL ASP ALA          
SEQRES   6 A  550  THR THR PHE GLN SER VAL CYS TYR GLN TYR VAL ASP THR          
SEQRES   7 A  550  LEU TYR PRO GLY PHE GLU GLY THR GLU MET TRP ASN PRO          
SEQRES   8 A  550  ASN ARG GLU LEU SER GLU ASP CYS LEU TYR LEU ASN VAL          
SEQRES   9 A  550  TRP THR PRO TYR PRO ARG PRO THR SER PRO THR PRO VAL          
SEQRES  10 A  550  LEU VAL TRP ILE TYR GLY GLY GLY PHE TYR SER GLY ALA          
SEQRES  11 A  550  SER SER LEU ASP VAL TYR ASP GLY ARG PHE LEU VAL GLN          
SEQRES  12 A  550  ALA GLU ARG THR VAL LEU VAL SER MET ASN TYR ARG VAL          
SEQRES  13 A  550  GLY ALA PHE GLY PHE LEU ALA LEU PRO GLY SER ARG GLU          
SEQRES  14 A  550  ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA          
SEQRES  15 A  550  LEU GLN TRP VAL GLN GLU ASN VAL ALA ALA PHE GLY GLY          
SEQRES  16 A  550  ASP PRO THR SER VAL THR LEU PHE GLY GLU SER ALA GLY          
SEQRES  17 A  550  ALA ALA SER VAL GLY MET HIS LEU LEU SER PRO PRO SER          
SEQRES  18 A  550  ARG GLY LEU PHE HIS ARG ALA VAL LEU GLN SER GLY ALA          
SEQRES  19 A  550  PRO ASN GLY PRO TRP ALA THR VAL GLY MET GLY GLU ALA          
SEQRES  20 A  550  ARG ARG ARG ALA THR GLN LEU ALA HIS LEU VAL GLY CYS          
SEQRES  21 A  550  PRO PRO GLY GLY THR GLY GLY ASN ASP THR GLU LEU VAL          
SEQRES  22 A  550  ALA CYS LEU ARG THR ARG PRO ALA GLN VAL LEU VAL ASN          
SEQRES  23 A  550  HIS GLU TRP HIS VAL LEU PRO GLN GLU SER VAL PHE ARG          
SEQRES  24 A  550  PHE SER PHE VAL PRO VAL VAL ASP GLY ASP PHE LEU SER          
SEQRES  25 A  550  ASP THR PRO GLU ALA LEU ILE ASN ALA GLY ASP PHE HIS          
SEQRES  26 A  550  GLY LEU GLN VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY          
SEQRES  27 A  550  SER TYR PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS          
SEQRES  28 A  550  ASP ASN GLU SER LEU ILE SER ARG ALA GLU PHE LEU ALA          
SEQRES  29 A  550  GLY VAL ARG VAL GLY VAL PRO GLN VAL SER ASP LEU ALA          
SEQRES  30 A  550  ALA GLU ALA VAL VAL LEU HIS TYR THR ASP TRP LEU HIS          
SEQRES  31 A  550  PRO GLU ASP PRO ALA ARG LEU ARG GLU ALA LEU SER ASP          
SEQRES  32 A  550  VAL VAL GLY ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN          
SEQRES  33 A  550  LEU ALA GLY ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR          
SEQRES  34 A  550  ALA TYR VAL PHE GLU HIS ARG ALA SER THR LEU SER TRP          
SEQRES  35 A  550  PRO LEU TRP MET GLY VAL PRO HIS GLY TYR GLU ILE GLU          
SEQRES  36 A  550  PHE ILE PHE GLY ILE PRO LEU ASP PRO SER ARG ASN TYR          
SEQRES  37 A  550  THR ALA GLU GLU LYS ILE PHE ALA GLN ARG LEU MET ARG          
SEQRES  38 A  550  TYR TRP ALA ASN PHE ALA ARG THR GLY ASP PRO ASN GLU          
SEQRES  39 A  550  PRO ARG ASP PRO LYS ALA PRO GLN TRP PRO PRO TYR THR          
SEQRES  40 A  550  ALA GLY ALA GLN GLN TYR VAL SER LEU ASP LEU ARG PRO          
SEQRES  41 A  550  LEU GLU VAL ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA          
SEQRES  42 A  550  PHE TRP ASN ARG PHE LEU PRO LYS LEU LEU SER ALA THR          
SEQRES  43 A  550  ASP THR LEU ASP                                              
SEQRES   1 B  550  GLY PRO LEU GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL          
SEQRES   2 B  550  THR VAL ARG GLY GLY ARG LEU ARG GLY ILE ARG LEU LYS          
SEQRES   3 B  550  THR PRO GLY GLY PRO VAL SER ALA PHE LEU GLY ILE PRO          
SEQRES   4 B  550  PHE ALA GLU PRO PRO MET GLY PRO ARG ARG PHE LEU PRO          
SEQRES   5 B  550  PRO GLU PRO LYS GLN PRO TRP SER GLY VAL VAL ASP ALA          
SEQRES   6 B  550  THR THR PHE GLN SER VAL CYS TYR GLN TYR VAL ASP THR          
SEQRES   7 B  550  LEU TYR PRO GLY PHE GLU GLY THR GLU MET TRP ASN PRO          
SEQRES   8 B  550  ASN ARG GLU LEU SER GLU ASP CYS LEU TYR LEU ASN VAL          
SEQRES   9 B  550  TRP THR PRO TYR PRO ARG PRO THR SER PRO THR PRO VAL          
SEQRES  10 B  550  LEU VAL TRP ILE TYR GLY GLY GLY PHE TYR SER GLY ALA          
SEQRES  11 B  550  SER SER LEU ASP VAL TYR ASP GLY ARG PHE LEU VAL GLN          
SEQRES  12 B  550  ALA GLU ARG THR VAL LEU VAL SER MET ASN TYR ARG VAL          
SEQRES  13 B  550  GLY ALA PHE GLY PHE LEU ALA LEU PRO GLY SER ARG GLU          
SEQRES  14 B  550  ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA          
SEQRES  15 B  550  LEU GLN TRP VAL GLN GLU ASN VAL ALA ALA PHE GLY GLY          
SEQRES  16 B  550  ASP PRO THR SER VAL THR LEU PHE GLY GLU SER ALA GLY          
SEQRES  17 B  550  ALA ALA SER VAL GLY MET HIS LEU LEU SER PRO PRO SER          
SEQRES  18 B  550  ARG GLY LEU PHE HIS ARG ALA VAL LEU GLN SER GLY ALA          
SEQRES  19 B  550  PRO ASN GLY PRO TRP ALA THR VAL GLY MET GLY GLU ALA          
SEQRES  20 B  550  ARG ARG ARG ALA THR GLN LEU ALA HIS LEU VAL GLY CYS          
SEQRES  21 B  550  PRO PRO GLY GLY THR GLY GLY ASN ASP THR GLU LEU VAL          
SEQRES  22 B  550  ALA CYS LEU ARG THR ARG PRO ALA GLN VAL LEU VAL ASN          
SEQRES  23 B  550  HIS GLU TRP HIS VAL LEU PRO GLN GLU SER VAL PHE ARG          
SEQRES  24 B  550  PHE SER PHE VAL PRO VAL VAL ASP GLY ASP PHE LEU SER          
SEQRES  25 B  550  ASP THR PRO GLU ALA LEU ILE ASN ALA GLY ASP PHE HIS          
SEQRES  26 B  550  GLY LEU GLN VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY          
SEQRES  27 B  550  SER TYR PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS          
SEQRES  28 B  550  ASP ASN GLU SER LEU ILE SER ARG ALA GLU PHE LEU ALA          
SEQRES  29 B  550  GLY VAL ARG VAL GLY VAL PRO GLN VAL SER ASP LEU ALA          
SEQRES  30 B  550  ALA GLU ALA VAL VAL LEU HIS TYR THR ASP TRP LEU HIS          
SEQRES  31 B  550  PRO GLU ASP PRO ALA ARG LEU ARG GLU ALA LEU SER ASP          
SEQRES  32 B  550  VAL VAL GLY ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN          
SEQRES  33 B  550  LEU ALA GLY ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR          
SEQRES  34 B  550  ALA TYR VAL PHE GLU HIS ARG ALA SER THR LEU SER TRP          
SEQRES  35 B  550  PRO LEU TRP MET GLY VAL PRO HIS GLY TYR GLU ILE GLU          
SEQRES  36 B  550  PHE ILE PHE GLY ILE PRO LEU ASP PRO SER ARG ASN TYR          
SEQRES  37 B  550  THR ALA GLU GLU LYS ILE PHE ALA GLN ARG LEU MET ARG          
SEQRES  38 B  550  TYR TRP ALA ASN PHE ALA ARG THR GLY ASP PRO ASN GLU          
SEQRES  39 B  550  PRO ARG ASP PRO LYS ALA PRO GLN TRP PRO PRO TYR THR          
SEQRES  40 B  550  ALA GLY ALA GLN GLN TYR VAL SER LEU ASP LEU ARG PRO          
SEQRES  41 B  550  LEU GLU VAL ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA          
SEQRES  42 B  550  PHE TRP ASN ARG PHE LEU PRO LYS LEU LEU SER ALA THR          
SEQRES  43 B  550  ASP THR LEU ASP                                              
HET    GOL  A 601       6                                                       
HET    GOL  A 602       6                                                       
HET    GOL  A 603       6                                                       
HET    E20  A 604      28                                                       
HET    NO3  A 605       4                                                       
HET    GOL  B 601       6                                                       
HET    GOL  B 602       6                                                       
HET    GOL  B 603       6                                                       
HET    E20  B 604      28                                                       
HET    NO3  B 605       4                                                       
HET    NO3  B 606       4                                                       
HET    NO3  B 607       4                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     E20 1-BENZYL-4-[(5,6-DIMETHOXY-1-INDANON-2-YL)                       
HETNAM   2 E20  METHYL]PIPERIDINE                                               
HETNAM     NO3 NITRATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     E20 E2020                                                            
FORMUL   3  GOL    6(C3 H8 O3)                                                  
FORMUL   6  E20    2(C24 H29 N O3)                                              
FORMUL   7  NO3    4(N O3 1-)                                                   
FORMUL  15  HOH   *370(H2 O)                                                    
HELIX    1 AA1 ASP A    5  GLU A    7  5                                   3    
HELIX    2 AA2 MET A   42  ARG A   46  5                                   5    
HELIX    3 AA3 PHE A   80  MET A   85  1                                   6    
HELIX    4 AA4 LEU A  130  ASP A  134  5                                   5    
HELIX    5 AA5 GLY A  135  ARG A  143  1                                   9    
HELIX    6 AA6 VAL A  153  LEU A  159  1                                   7    
HELIX    7 AA7 ASN A  170  VAL A  187  1                                  18    
HELIX    8 AA8 ALA A  188  PHE A  190  5                                   3    
HELIX    9 AA9 SER A  203  LEU A  214  1                                  12    
HELIX   10 AB1 SER A  215  GLY A  220  1                                   6    
HELIX   11 AB2 GLY A  240  VAL A  255  1                                  16    
HELIX   12 AB3 ASN A  265  ARG A  276  1                                  12    
HELIX   13 AB4 PRO A  277  ASN A  283  1                                   7    
HELIX   14 AB5 HIS A  284  LEU A  289  5                                   6    
HELIX   15 AB6 THR A  311  GLY A  319  1                                   9    
HELIX   16 AB7 GLY A  335  VAL A  340  1                                   6    
HELIX   17 AB8 SER A  355  VAL A  367  1                                  13    
HELIX   18 AB9 SER A  371  THR A  383  1                                  13    
HELIX   19 AC1 ASP A  390  VAL A  407  1                                  18    
HELIX   20 AC2 VAL A  407  ALA A  420  1                                  14    
HELIX   21 AC3 PRO A  440  GLY A  444  5                                   5    
HELIX   22 AC4 GLU A  450  PHE A  455  1                                   6    
HELIX   23 AC5 GLY A  456  ASP A  460  5                                   5    
HELIX   24 AC6 THR A  466  GLY A  487  1                                  22    
HELIX   25 AC7 ARG A  525  ARG A  534  1                                  10    
HELIX   26 AC8 ARG A  534  ALA A  542  1                                   9    
HELIX   27 AC9 ASP B    5  GLU B    7  5                                   3    
HELIX   28 AD1 MET B   42  ARG B   46  5                                   5    
HELIX   29 AD2 PHE B   80  MET B   85  1                                   6    
HELIX   30 AD3 LEU B  130  ASP B  134  5                                   5    
HELIX   31 AD4 GLY B  135  ARG B  143  1                                   9    
HELIX   32 AD5 VAL B  153  LEU B  159  1                                   7    
HELIX   33 AD6 ASN B  170  VAL B  187  1                                  18    
HELIX   34 AD7 ALA B  188  PHE B  190  5                                   3    
HELIX   35 AD8 SER B  203  LEU B  214  1                                  12    
HELIX   36 AD9 SER B  215  GLY B  220  1                                   6    
HELIX   37 AE1 GLY B  240  VAL B  255  1                                  16    
HELIX   38 AE2 ASN B  265  THR B  275  1                                  11    
HELIX   39 AE3 PRO B  277  ASN B  283  1                                   7    
HELIX   40 AE4 HIS B  284  LEU B  289  5                                   6    
HELIX   41 AE5 THR B  311  GLY B  319  1                                   9    
HELIX   42 AE6 GLY B  335  VAL B  340  1                                   6    
HELIX   43 AE7 SER B  355  VAL B  367  1                                  13    
HELIX   44 AE8 SER B  371  THR B  383  1                                  13    
HELIX   45 AE9 ASP B  390  VAL B  407  1                                  18    
HELIX   46 AF1 VAL B  407  ALA B  420  1                                  14    
HELIX   47 AF2 PRO B  440  GLY B  444  5                                   5    
HELIX   48 AF3 GLU B  450  PHE B  455  1                                   6    
HELIX   49 AF4 GLY B  456  ASP B  460  5                                   5    
HELIX   50 AF5 THR B  466  GLY B  487  1                                  22    
HELIX   51 AF6 ARG B  525  ARG B  534  1                                  10    
HELIX   52 AF7 ARG B  534  ALA B  542  1                                   9    
SHEET    1 AA1 3 LEU A   9  VAL A  12  0                                        
SHEET    2 AA1 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3 AA1 3 VAL A  59  ASP A  61  1  O  VAL A  60   N  ARG A  16           
SHEET    1 AA211 ILE A  20  THR A  24  0                                        
SHEET    2 AA211 GLY A  27  PRO A  36 -1  O  ALA A  31   N  ILE A  20           
SHEET    3 AA211 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4 AA211 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5 AA211 THR A 112  ILE A 118  1  N  LEU A 115   O  VAL A 147           
SHEET    6 AA211 GLY A 192  GLU A 202  1  O  ASP A 193   N  THR A 112           
SHEET    7 AA211 ARG A 224  GLN A 228  1  O  GLN A 228   N  GLY A 201           
SHEET    8 AA211 GLN A 325  VAL A 331  1  O  LEU A 327   N  LEU A 227           
SHEET    9 AA211 ARG A 424  PHE A 430  1  O  ARG A 424   N  VAL A 326           
SHEET   10 AA211 GLN A 509  LEU A 513  1  O  LEU A 513   N  VAL A 429           
SHEET   11 AA211 GLU A 519  ARG A 522 -1  O  ARG A 521   N  TYR A 510           
SHEET    1 AA3 2 VAL A  68  CYS A  69  0                                        
SHEET    2 AA3 2 LEU A  92  SER A  93  1  O  SER A  93   N  VAL A  68           
SHEET    1 AA4 3 LEU B   9  VAL B  12  0                                        
SHEET    2 AA4 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12           
SHEET    3 AA4 3 VAL B  59  ASP B  61  1  O  VAL B  60   N  ARG B  16           
SHEET    1 AA511 ILE B  20  LEU B  22  0                                        
SHEET    2 AA511 VAL B  29  PRO B  36 -1  O  ALA B  31   N  ILE B  20           
SHEET    3 AA511 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4 AA511 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100           
SHEET    5 AA511 THR B 112  ILE B 118  1  N  TRP B 117   O  VAL B 147           
SHEET    6 AA511 GLY B 192  GLU B 202  1  O  ASP B 193   N  THR B 112           
SHEET    7 AA511 ARG B 224  GLN B 228  1  O  GLN B 228   N  GLY B 201           
SHEET    8 AA511 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9 AA511 ARG B 424  PHE B 430  1  O  ARG B 424   N  VAL B 326           
SHEET   10 AA511 GLN B 509  LEU B 513  1  O  LEU B 513   N  VAL B 429           
SHEET   11 AA511 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1 AA6 2 VAL B  68  CYS B  69  0                                        
SHEET    2 AA6 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.04  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.04  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.04  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.04  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.05  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.04  
CISPEP   1 TYR A  105    PRO A  106          0        -0.93                     
CISPEP   2 CYS A  257    PRO A  258          0        -3.37                     
CISPEP   3 GLY A  260    GLY A  261          0        -1.22                     
CISPEP   4 TYR B  105    PRO B  106          0        -0.72                     
CISPEP   5 CYS B  257    PRO B  258          0        -4.38                     
SITE     1 AC1  8 GLU A  81  MET A  85  THR A 436  LEU A 437                    
SITE     2 AC1  8 SER A 438  TYR A 449  GLU A 452  HOH A 842                    
SITE     1 AC2  4 TYR A 341  E20 A 604  HOH A 718  HOH A 788                    
SITE     1 AC3  5 ARG A  46  ARG A 274  THR A 275  PRO A 277                    
SITE     2 AC3  5 HOH A 833                                                     
SITE     1 AC4 13 TYR A  72  TRP A  86  TYR A 124  GLU A 202                    
SITE     2 AC4 13 TRP A 286  SER A 293  PHE A 295  TYR A 337                    
SITE     3 AC4 13 PHE A 338  TYR A 341  GOL A 602  HOH A 708                    
SITE     4 AC4 13 HOH A 832                                                     
SITE     1 AC5  3 ASP A 333  TRP A 442  HOH A 755                               
SITE     1 AC6  8 GLU B  81  MET B  85  THR B 436  LEU B 437                    
SITE     2 AC6  8 SER B 438  TYR B 449  GLU B 452  HOH B 846                    
SITE     1 AC7  6 LEU B  76  TYR B 341  E20 B 604  HOH B 712                    
SITE     2 AC7  6 HOH B 789  HOH B 811                                          
SITE     1 AC8  3 ARG B 274  PRO B 277  HOH B 755                               
SITE     1 AC9 13 TYR B  72  TRP B  86  TYR B 124  GLU B 202                    
SITE     2 AC9 13 TRP B 286  SER B 293  PHE B 295  TYR B 337                    
SITE     3 AC9 13 PHE B 338  TYR B 341  GOL B 602  HOH B 701                    
SITE     4 AC9 13 HOH B 847                                                     
SITE     1 AD1  4 LYS B 332  ASP B 333  GLU B 396  TRP B 442                    
SITE     1 AD2  2 PRO B  36  TYR B  98                                          
SITE     1 AD3  4 PRO B  88  ASN B  89  ARG B  90  GLU B  91                    
CRYST1  123.792  123.792  129.413  90.00  90.00 120.00 P 31          6          
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      0.008078  0.004664  0.000000        0.00000                         
SCALE2      0.000000  0.009328  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007727        0.00000                         
TER    4189      THR A 543                                                      
TER    8378      THR B 543                                                      
MASTER      318    0   12   52   32    0   22    6 8854    2  120   86          
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
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