GenomeNet

Database: PDB
Entry: 6O50
LinkDB: 6O50
Original site: 6O50 
HEADER    HYDROLASE                               01-MAR-19   6O50              
TITLE     BINARY COMPLEX OF NATIVE HACHE WITH BW284C51                          
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    BW284C51, HYDROLASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.GERLITS,A.KOVALEVSKY,Z.RADIC                                        
REVDAT   2   10-JUL-19 6O50    1       JRNL                                     
REVDAT   1   19-JUN-19 6O50    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.           V. 309 08698 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) : 27.92                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.970                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 70.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 66738                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3352                            
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 27.9197 -  6.7535    0.60     2271   113  0.1421 0.1652        
REMARK   3     2  6.7535 -  5.3729    0.69     2563   155  0.1589 0.1966        
REMARK   3     3  5.3729 -  4.6974    0.71     2651   131  0.1525 0.1920        
REMARK   3     4  4.6974 -  4.2696    0.73     2748   150  0.1464 0.1861        
REMARK   3     5  4.2696 -  3.9645    0.75     2830   152  0.1649 0.2245        
REMARK   3     6  3.9645 -  3.7313    0.77     2870   175  0.1786 0.2361        
REMARK   3     7  3.7313 -  3.5448    0.79     2941   137  0.1944 0.2424        
REMARK   3     8  3.5448 -  3.3908    0.79     2937   182  0.2038 0.2170        
REMARK   3     9  3.3908 -  3.2605    0.80     3027   152  0.2059 0.2371        
REMARK   3    10  3.2605 -  3.1481    0.81     3025   160  0.2130 0.2321        
REMARK   3    11  3.1481 -  3.0498    0.82     3016   172  0.2275 0.2790        
REMARK   3    12  3.0498 -  2.9627    0.83     3131   155  0.2321 0.2676        
REMARK   3    13  2.9627 -  2.8848    0.83     3132   166  0.2385 0.2825        
REMARK   3    14  2.8848 -  2.8145    0.84     3151   134  0.2411 0.2544        
REMARK   3    15  2.8145 -  2.7506    0.84     3181   179  0.2576 0.3117        
REMARK   3    16  2.7506 -  2.6921    0.84     3149   166  0.2701 0.3086        
REMARK   3    17  2.6921 -  2.6383    0.84     3171   163  0.2796 0.3064        
REMARK   3    18  2.6383 -  2.5885    0.84     3181   168  0.2954 0.3471        
REMARK   3    19  2.5885 -  2.5423    0.79     2866   173  0.2954 0.3445        
REMARK   3    20  2.5423 -  2.4992    0.69     2596   140  0.2993 0.3879        
REMARK   3    21  2.4992 -  2.4590    0.55     2077   105  0.3184 0.3699        
REMARK   3    22  2.4590 -  2.4211    0.39     1505    61  0.3067 0.3417        
REMARK   3    23  2.4211 -  2.3856    0.23      862    44  0.3191 0.3778        
REMARK   3    24  2.3856 -  2.3520    0.13      505    19  0.3083 0.4032        
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)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.030           
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      :  0.002           8725                                  
REMARK   3   ANGLE     :  0.606          11927                                  
REMARK   3   CHIRALITY :  0.043           1256                                  
REMARK   3   PLANARITY :  0.005           1575                                  
REMARK   3   DIHEDRAL  : 16.203           5134                                  
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 6O50 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_1000240037.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : 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 X 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     (%) : 80.1                               
REMARK 200  DATA REDUNDANCY                : 1.200                              
REMARK 200  R MERGE                    (I) : 0.02600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.5000                            
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) : 0.64200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> 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   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
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       43.42667            
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       86.85333            
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: 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  62       53.72   -118.32                                   
REMARK 500    ASN A 170       15.17     59.17                                   
REMARK 500    SER A 203     -119.45     54.69                                   
REMARK 500    ASP A 306      -83.32   -104.38                                   
REMARK 500    VAL A 367       76.72   -119.71                                   
REMARK 500    GLU A 389       18.00   -140.22                                   
REMARK 500    VAL A 407      -59.79   -121.48                                   
REMARK 500    ASP A 514     -164.85   -160.74                                   
REMARK 500    PHE B 158       10.89   -143.12                                   
REMARK 500    ASN B 186      -13.82   -141.27                                   
REMARK 500    SER B 203     -115.41     54.61                                   
REMARK 500    ASP B 306      -79.61    -97.24                                   
REMARK 500    VAL B 407      -64.17   -121.76                                   
REMARK 500    ASP B 494      -53.10   -122.82                                   
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 EBW 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 NO3 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EBW B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 603                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6O4W   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6O4X   RELATED DB: PDB                                   
DBREF  6O50 A    1   547  UNP    P22303   ACES_HUMAN      32    578             
DBREF  6O50 B    1   547  UNP    P22303   ACES_HUMAN      32    578             
SEQADV 6O50 GLY A   -2  UNP  P22303              EXPRESSION TAG                 
SEQADV 6O50 PRO A   -1  UNP  P22303              EXPRESSION TAG                 
SEQADV 6O50 LEU A    0  UNP  P22303              EXPRESSION TAG                 
SEQADV 6O50 GLY B   -2  UNP  P22303              EXPRESSION TAG                 
SEQADV 6O50 PRO B   -1  UNP  P22303              EXPRESSION TAG                 
SEQADV 6O50 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    EBW  A 601      30                                                       
HET    GOL  A 602       6                                                       
HET    GOL  A 603       6                                                       
HET    NO3  A 604       4                                                       
HET    EBW  B 601      30                                                       
HET    GOL  B 602       6                                                       
HET    GOL  B 603       6                                                       
HETNAM     EBW 4-(5-{4-[DIMETHYL(PROP-2-ENYL)AMMONIO]PHENYL}-3-                 
HETNAM   2 EBW  OXOPENTYL)-N,N-DIMETHYL-N-PROP-2-ENYLBENZENAMINIUM              
HETNAM     GOL GLYCEROL                                                         
HETNAM     NO3 NITRATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  EBW    2(C27 H38 N2 O 2+)                                           
FORMUL   4  GOL    4(C3 H8 O3)                                                  
FORMUL   6  NO3    N O3 1-                                                      
FORMUL  10  HOH   *217(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 GLY A  154  LEU A  159  1                                   6    
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  274  1                                  10    
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  ALA A  318  1                                   8    
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  GLN A  421  1                                  15    
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  VAL B  288  5                                   5    
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  GLN B  421  1                                  15    
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  THR B  543  1                                  10    
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  LEU A  22  0                                        
SHEET    2 AA211 VAL A  29  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  TRP A 117   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 3 LEU B   9  VAL B  12  0                                        
SHEET    2 AA3 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12           
SHEET    3 AA3 3 VAL B  59  ASP B  61  1  O  VAL B  60   N  ARG B  16           
SHEET    1 AA411 ILE B  20  LEU B  22  0                                        
SHEET    2 AA411 VAL B  29  PRO B  36 -1  O  ALA B  31   N  ILE B  20           
SHEET    3 AA411 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4 AA411 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5 AA411 THR B 112  ILE B 118  1  N  LEU B 115   O  VAL B 145           
SHEET    6 AA411 GLY B 192  GLU B 202  1  O  ASP B 193   N  THR B 112           
SHEET    7 AA411 ARG B 224  GLN B 228  1  O  GLN B 228   N  GLY B 201           
SHEET    8 AA411 GLN B 325  VAL B 331  1  O  LEU B 327   N  ALA B 225           
SHEET    9 AA411 ARG B 424  PHE B 430  1  O  TYR B 426   N  VAL B 328           
SHEET   10 AA411 GLN B 509  LEU B 513  1  O  LEU B 513   N  VAL B 429           
SHEET   11 AA411 VAL B 520  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.04  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.03  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.04  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.03  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.03  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.04  
CISPEP   1 TYR A  105    PRO A  106          0        -3.23                     
CISPEP   2 CYS A  257    PRO A  258          0        -3.19                     
CISPEP   3 GLY A  260    GLY A  261          0         0.53                     
CISPEP   4 TYR B  105    PRO B  106          0        -0.58                     
CISPEP   5 CYS B  257    PRO B  258          0        -2.84                     
CISPEP   6 GLU B  491    PRO B  492          0         6.50                     
CISPEP   7 ASP B  494    PRO B  495          0        -8.18                     
SITE     1 AC1 12 TYR A  72  LEU A  76  TRP A  86  TYR A 124                    
SITE     2 AC1 12 GLU A 202  SER A 203  TRP A 286  PHE A 297                    
SITE     3 AC1 12 TYR A 337  PHE A 338  TYR A 341  HIS A 447                    
SITE     1 AC2  9 GLU A  81  MET A  85  THR A 436  LEU A 437                    
SITE     2 AC2  9 SER A 438  TYR A 449  GLU A 452  TYR A 465                    
SITE     3 AC2  9 HOH A 744                                                     
SITE     1 AC3  4 ARG A  46  ARG A 274  HOH A 702  HOH A 781                    
SITE     1 AC4  3 ASP A 333  LEU A 441  TRP A 442                               
SITE     1 AC5 12 TYR B  72  LEU B  76  TRP B  86  TYR B 124                    
SITE     2 AC5 12 GLU B 202  SER B 203  TRP B 286  PHE B 297                    
SITE     3 AC5 12 TYR B 337  PHE B 338  TYR B 341  HIS B 447                    
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  TYR B 465                    
SITE     1 AC7  4 ARG B  46  ARG B 274  THR B 275  HOH B 715                    
CRYST1  125.180  125.180  130.280  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      0.007988  0.004612  0.000000        0.00000                         
SCALE2      0.000000  0.009224  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007676        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system