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LongText Report for: 4A16-pdb

Name Class
4A16-pdb
HEADER    HYDROLASE                               14-SEP-11   4A16              
TITLE     STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEX WITH HUPRINE          
TITLE    2 DERIVATIVE                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 35-574;                                           
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGS                                       
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.CARLETTI,J.P.COLLETIER,F.NACHON,M.WEIK,C.RONCO,L.JEAN,P.Y.RENARD    
REVDAT   1   28-MAR-12 4A16    0                                                
JRNL        AUTH   C.RONCO,E.CARLETTI,J.P.COLLETIER,M.WEIK,F.NACHON,L.JEAN,     
JRNL        AUTH 2 P.Y.RENARD                                                   
JRNL        TITL   NEW HUPRINES DERIVATIVES AS SUBNANOMOLAR HUMAN               
JRNL        TITL 2 ACETYLCHOLINESTERASE INHIBITORS : FROM A RATIONAL DESIGN TO  
JRNL        TITL 3 VALIDATION BY X-RAY CRYSTALLOGRAPHY                          
JRNL        REF    CHEMMEDCHEM                   V.   7   400 2012              
JRNL        REFN                   ISSN 1860-7179                               
JRNL        DOI    10.1002/CMDC.201100438                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.00                         
REMARK   3   NUMBER OF REFLECTIONS             : 150577                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.15667                         
REMARK   3   R VALUE            (WORKING SET) : 0.15517                         
REMARK   3   FREE R VALUE                     : 0.20563                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 4658                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.650                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.719                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10974                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.278                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 340                          
REMARK   3   BIN FREE R VALUE                    : 0.344                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16868                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 209                                     
REMARK   3   SOLVENT ATOMS            : 2323                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.829                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.05                                                 
REMARK   3    B22 (A**2) : -0.06                                                
REMARK   3    B33 (A**2) : 0.01                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.214         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.198         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.149         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.445        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 17603 ; 0.023 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 24108 ; 2.138 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2182 ; 7.498 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   797 ;34.234 ;22.848       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2537 ;19.283 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   147 ;21.193 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2565 ; 0.144 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 10819 ; 1.068 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17442 ; 2.074 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6784 ; 3.140 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6653 ; 5.226 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     4        A   543                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.7405 -28.5189  86.4020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0172 T22:   0.0546                                     
REMARK   3      T33:   0.0625 T12:  -0.0243                                     
REMARK   3      T13:   0.0088 T23:  -0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1962 L22:   0.6953                                     
REMARK   3      L33:   0.2017 L12:   0.0973                                     
REMARK   3      L13:  -0.0503 L23:  -0.0818                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0056 S12:   0.0308 S13:  -0.0160                       
REMARK   3      S21:   0.0628 S22:  -0.0039 S23:   0.0119                       
REMARK   3      S31:  -0.0092 S32:  -0.0224 S33:   0.0096                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     4        B   543                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4964  27.4349  66.1349              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1189 T22:   0.0765                                     
REMARK   3      T33:   0.0488 T12:   0.0910                                     
REMARK   3      T13:   0.0464 T23:   0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1555 L22:   0.7145                                     
REMARK   3      L33:   0.5608 L12:  -0.0712                                     
REMARK   3      L13:   0.0883 L23:  -0.3935                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0084 S12:  -0.0082 S13:  -0.0513                       
REMARK   3      S21:   0.1320 S22:   0.0875 S23:   0.1079                       
REMARK   3      S31:  -0.1848 S32:  -0.1115 S33:  -0.0791                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     4        C   543                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6372  12.3774  25.0398              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0300 T22:   0.0675                                     
REMARK   3      T33:   0.0513 T12:   0.0185                                     
REMARK   3      T13:   0.0309 T23:   0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1510 L22:   0.1910                                     
REMARK   3      L33:   0.6552 L12:  -0.0258                                     
REMARK   3      L13:   0.0899 L23:  -0.0655                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0416 S12:   0.0131 S13:  -0.0277                       
REMARK   3      S21:  -0.0006 S22:  -0.0104 S23:  -0.0041                       
REMARK   3      S31:  -0.0136 S32:   0.0779 S33:   0.0520                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     4        D   543                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.7352   5.6872  81.3389              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0169 T22:   0.0900                                     
REMARK   3      T33:   0.0713 T12:  -0.0230                                     
REMARK   3      T13:  -0.0294 T23:   0.0524                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1824 L22:   0.2365                                     
REMARK   3      L33:   0.8716 L12:  -0.0867                                     
REMARK   3      L13:   0.2157 L23:  -0.1135                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0030 S12:   0.0635 S13:   0.0348                       
REMARK   3      S21:   0.0296 S22:  -0.0650 S23:  -0.0309                       
REMARK   3      S31:  -0.0085 S32:   0.1445 S33:   0.0620                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 4A16 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-SEP-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-49648.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 9                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9765                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 210)                  
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 155235                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.65                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.7                                
REMARK 200  R MERGE                    (I) : 0.01                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.07                               
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: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1MAA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 74.80                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE BUFFER PH 9, 1.6 M          
REMARK 280  AMMONIUM SULFATE.                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       68.97000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      112.66000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       85.96500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      112.66000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       68.97000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       85.96500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -125.7 KCAL/MOL                       
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.7 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     THR A   545                                                      
REMARK 465     GLU A   546                                                      
REMARK 465     ALA A   547                                                      
REMARK 465     PRO A   548                                                      
REMARK 465     THR B   545                                                      
REMARK 465     GLU B   546                                                      
REMARK 465     ALA B   547                                                      
REMARK 465     PRO B   548                                                      
REMARK 465     THR C   545                                                      
REMARK 465     GLU C   546                                                      
REMARK 465     ALA C   547                                                      
REMARK 465     PRO C   548                                                      
REMARK 465     THR D   545                                                      
REMARK 465     GLU D   546                                                      
REMARK 465     ALA D   547                                                      
REMARK 465     PRO D   548                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ALA A 544    CA   C    O    CB                                   
REMARK 470     ARG B 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ALA B 544    CA   C    O    CB                                   
REMARK 470     ARG C 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ALA C 544    CA   C    O    CB                                   
REMARK 470     ARG D 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ALA D 544    CA   C    O    CB                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A     5     OH   TYR A   105              2.13            
REMARK 500   O    THR A    63     O    HOH A  2113              2.07            
REMARK 500   O    VAL A    73     O    HOH A  2142              2.19            
REMARK 500   OH   TYR A    77     O    HOH A  2151              1.94            
REMARK 500   NE   ARG A   219     O    HOH A  2342              2.15            
REMARK 500   NH2  ARG A   219     O    HOH A  2342              1.93            
REMARK 500   O    PHE A   346     O    HOH A  2465              2.18            
REMARK 500   N    LYS A   348     O    HOH A  2151              2.19            
REMARK 500   CB   LEU A   540     O    HOH A  2502              2.18            
REMARK 500   NH1  ARG B   245     O    HOH B  2254              1.96            
REMARK 500   C    GLY B   256     O    HOH B  2270              2.14            
REMARK 500   N    CYS B   257     O    HOH B  2270              1.80            
REMARK 500   O    PRO B   259     O    HOH B  2274              1.98            
REMARK 500   CA   ALA B   262     O    HOH B  2277              1.96            
REMARK 500   ND2  ASN B   464     O    HOH B  2436              2.00            
REMARK 500   O    ASP B   494     O    HOH B  2452              1.96            
REMARK 500   CB   GLU C     4     O    HOH C  2001              1.60            
REMARK 500   NE   ARG C    13     O    HOH C  2027              2.08            
REMARK 500   NH1  ARG C   107     O    HOH C  2195              2.05            
REMARK 500   O    PRO C   108     O    HOH C  2194              2.11            
REMARK 500   OD1  ASN C   265     O    HOH C  2355              2.12            
REMARK 500   CD1  LEU C   339     O    HOH C  2439              2.10            
REMARK 500   NH2  ARG C   485     O    HOH C  2243              2.10            
REMARK 500   NH1  ARG D    11     O    HOH D  2016              2.08            
REMARK 500   NH2  ARG D    54     O    HOH D  2077              2.20            
REMARK 500   O    PRO D   108     O    HOH D  2169              2.00            
REMARK 500   N    MET D   211     O    HOH D  2261              2.11            
REMARK 500   CD   PRO D   258     O    HOH D  2303              1.81            
REMARK 500   CA   GLY D   261     O    HOH A  2659              2.07            
REMARK 500   OD2  ASP D   304     O    HOH D  2227              2.17            
REMARK 500   O    ALA D   419     O    HOH D  2437              2.19            
REMARK 500   O    HOH A  2001     O    HOH A  2006              2.14            
REMARK 500   O    HOH A  2025     O    HOH A  2047              2.18            
REMARK 500   O    HOH A  2186     O    HOH A  2394              2.08            
REMARK 500   O    HOH A  2193     O    HOH D  2338              2.12            
REMARK 500   O    HOH A  2319     O    HOH A  2639              1.83            
REMARK 500   O    HOH A  2356     O    HOH A  2376              2.05            
REMARK 500   O    HOH A  2361     O    HOH A  2362              2.00            
REMARK 500   O    HOH A  2390     O    HOH A  2392              2.18            
REMARK 500   O    HOH A  2460     O    HOH A  2573              2.18            
REMARK 500   O    HOH A  2567     O    HOH A  2575              2.11            
REMARK 500   O    HOH B  2043     O    HOH B  2130              2.03            
REMARK 500   O    HOH B  2107     O    HOH B  2245              2.16            
REMARK 500   O    HOH B  2281     O    HOH B  2285              2.19            
REMARK 500   O    HOH C  2115     O    HOH C  2176              2.20            
REMARK 500   O    HOH C  2293     O    HOH C  2600              1.81            
REMARK 500   O    HOH C  2325     O    HOH C  2329              2.05            
REMARK 500   O    HOH C  2458     O    HOH C  2459              1.80            
REMARK 500   O    HOH C  2566     O    HOH C  2567              2.18            
REMARK 500   O    HOH C  2581     O    HOH C  2582              2.06            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH C  2024     O    HOH D  2077     2554     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    VAL A 340   CB    VAL A 340   CG2    -0.138                       
REMARK 500    CYS B  96   CB    CYS B  96   SG      0.119                       
REMARK 500    GLU B 268   CG    GLU B 268   CD      0.154                       
REMARK 500    GLU C   4   CD    GLU C   4   OE2     0.107                       
REMARK 500    GLU C 268   CG    GLU C 268   CD      0.107                       
REMARK 500    ASP C 304   CB    ASP C 304   CG      0.131                       
REMARK 500    TYR C 428   CB    TYR C 428   CG      0.092                       
REMARK 500    GLU D  81   CB    GLU D  81   CG      0.143                       
REMARK 500    GLU D  81   CG    GLU D  81   CD      0.114                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    LEU A  17   CA  -  CB  -  CG  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ARG A 219   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 475   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 522   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    LEU A 540   CA  -  CB  -  CG  ANGL. DEV. =  27.5 DEGREES          
REMARK 500    MET B 211   CG  -  SD  -  CE  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    LEU B 251   CA  -  CB  -  CG  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ARG B 253   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG B 253   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    CYS B 257   N   -  CA  -  C   ANGL. DEV. =  20.6 DEGREES          
REMARK 500    GLY B 263   N   -  CA  -  C   ANGL. DEV. =  18.3 DEGREES          
REMARK 500    ARG B 475   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    CYS B 529   CA  -  CB  -  SG  ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    GLU C   4   OE1 -  CD  -  OE2 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG C  13   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ARG C  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    PRO C 111   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    ARG C 246   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    PRO C 258   C   -  N   -  CA  ANGL. DEV. = -14.1 DEGREES          
REMARK 500    LEU C 269   CA  -  CB  -  CG  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    ILE C 294   CB  -  CA  -  C   ANGL. DEV. = -12.3 DEGREES          
REMARK 500    ASP C 310   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG D 245   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG D 245   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    CYS D 257   CA  -  CB  -  SG  ANGL. DEV. = -15.7 DEGREES          
REMARK 500    CYS D 257   CB  -  CA  -  C   ANGL. DEV. =   7.4 DEGREES          
REMARK 500    PRO D 258   C   -  N   -  CA  ANGL. DEV. = -16.5 DEGREES          
REMARK 500    ASP D 266   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG D 274   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    LEU D 380   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    ASP D 404   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG D 475   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG D 475   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 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    PHE A  47       -9.80     79.51                                   
REMARK 500    ALA A  62       50.92   -109.93                                   
REMARK 500    PRO A 104      150.04    -47.25                                   
REMARK 500    ALA A 167       74.24   -166.46                                   
REMARK 500    SER A 203     -125.32     57.78                                   
REMARK 500    ALA A 262     -120.16   -114.15                                   
REMARK 500    ASP A 306      -78.49   -109.07                                   
REMARK 500    GLU A 351       -7.27    -59.18                                   
REMARK 500    VAL A 407      -58.71   -130.83                                   
REMARK 500    ASP A 494      165.83    173.99                                   
REMARK 500    LYS A 496       75.71     75.97                                   
REMARK 500    PRO A 498     -165.78    -71.87                                   
REMARK 500    LEU B   8       25.17    -74.19                                   
REMARK 500    PHE B  47       -6.14     71.86                                   
REMARK 500    ALA B  62       52.72   -101.54                                   
REMARK 500    CYS B  96       -6.99   -153.46                                   
REMARK 500    LEU B  97       80.41    -68.16                                   
REMARK 500    ARG B 107      137.43    -34.26                                   
REMARK 500    ALA B 109      -97.40    -12.03                                   
REMARK 500    PRO B 111      103.67    -37.74                                   
REMARK 500    ALA B 189      -18.26    -45.53                                   
REMARK 500    PRO B 194        2.21    -58.32                                   
REMARK 500    SER B 203     -124.78     53.61                                   
REMARK 500    PRO B 217       -7.57    -59.38                                   
REMARK 500    VAL B 255     -148.29    -93.48                                   
REMARK 500    CYS B 257       94.10     81.43                                   
REMARK 500    ALA B 262      -22.32   -141.28                                   
REMARK 500    ASP B 306      -84.04   -119.23                                   
REMARK 500    ASP B 323       31.83    -96.25                                   
REMARK 500    ASN B 350     -157.96    -91.02                                   
REMARK 500    SER B 352       63.73     62.04                                   
REMARK 500    ASP B 390      106.42    -59.42                                   
REMARK 500    VAL B 407      -65.00   -127.11                                   
REMARK 500    PRO B 440      162.69    -49.73                                   
REMARK 500    LEU B 459     -116.53    -48.48                                   
REMARK 500    ASP B 460       92.15      6.25                                   
REMARK 500    ASN B 464       34.70     79.56                                   
REMARK 500    THR B 466      163.86    -41.96                                   
REMARK 500    ASP B 488      117.11   -171.61                                   
REMARK 500    LYS B 496      126.17     71.30                                   
REMARK 500    SER B 497      -53.15   -148.95                                   
REMARK 500    PRO B 498     -154.20    -88.94                                   
REMARK 500    LEU B 518      116.52    -39.87                                   
REMARK 500    ALA B 542       71.13     61.61                                   
REMARK 500    PHE C  47      -10.10     75.79                                   
REMARK 500    ALA C  62       51.96   -116.60                                   
REMARK 500    SER C 110      118.22     70.74                                   
REMARK 500    PRO C 111      114.60    -32.55                                   
REMARK 500    ALA C 167       78.20   -150.61                                   
REMARK 500    PRO C 194       -9.61    -58.32                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      78 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 CYS A  257     PRO A  258                  132.25                    
REMARK 500 GLY B  256     CYS B  257                  126.43                    
REMARK 500 CYS C  257     PRO C  258                  139.04                    
REMARK 500 SER C  495     LYS C  496                 -148.41                    
REMARK 500 ALA C  542     THR C  543                  133.91                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU A 166        22.5      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 340        24.8      L          L   OUTSIDE RANGE           
REMARK 500    TYR A 449        24.7      L          L   OUTSIDE RANGE           
REMARK 500    SER A 497        24.0      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 540        22.6      L          L   OUTSIDE RANGE           
REMARK 500    CYS B 257        12.8      L          L   OUTSIDE RANGE           
REMARK 500    LYS C  23        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ALA C 262        23.6      L          L   OUTSIDE RANGE           
REMARK 500    GLU D   4        25.0      L          L   OUTSIDE RANGE           
REMARK 500    CYS D 257        11.6      L          L   OUTSIDE RANGE           
REMARK 500    ARG D 493        23.0      L          L   OUTSIDE RANGE           
REMARK 500    ASP D 494        23.4      L          L   OUTSIDE RANGE           
REMARK 500    SER D 497        24.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG B 1546                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H34 A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1549                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H34 B1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1549                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1551                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H34 C1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1549                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H34 D1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1549                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WHQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY        
REMARK 900   SARIN (AGED) IN COMPLEX WITH HI-6                                  
REMARK 900 RELATED ID: 2JGH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED VX                                                      
REMARK 900 RELATED ID: 1MAH   RELATED DB: PDB                                   
REMARK 900  FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX                    
REMARK 900 RELATED ID: 1MAA   RELATED DB: PDB                                   
REMARK 900  MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,                        
REMARK 900  GLYCOSYLATEDPROTEIN                                                 
REMARK 900 RELATED ID: 2HA6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH SUCCINYLCHOLINE            
REMARK 900 RELATED ID: 2JGG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED SARIN                                                   
REMARK 900 RELATED ID: 2C0Q   RELATED DB: PDB                                   
REMARK 900  NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY            
REMARK 900   TABUN                                                              
REMARK 900 RELATED ID: 2JGL   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED VX AND SARIN                                                
REMARK 900 RELATED ID: 2XUG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (              
REMARK 900  1 WK)                                                               
REMARK 900 RELATED ID: 1Q84   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  TZ2PA6ANTI COMPLEX                                                  
REMARK 900 RELATED ID: 2XUD   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE Y337A MUTANT OF MOUSE                      
REMARK 900  ACETYLCHOLINESTERASE                                                
REMARK 900 RELATED ID: 2JGM   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)                           
REMARK 900 RELATED ID: 2XUJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1              
REMARK 900   MTH)                                                               
REMARK 900 RELATED ID: 1Q83   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  TZ2PA6SYN COMPLEX                                                   
REMARK 900 RELATED ID: 2JGE   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED METHAMIDOPHOS                                           
REMARK 900 RELATED ID: 2WLS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUS MUSCULUS ACETYLCHOLINESTERASE IN           
REMARK 900   COMPLEX WITH AMTS13                                                
REMARK 900 RELATED ID: 2XUP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX              
REMARK 900   WITH SOAKED TZ2PA6 SYN INHIBITOR                                   
REMARK 900 RELATED ID: 2XUK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (               
REMARK 900  10 MTH)                                                             
REMARK 900 RELATED ID: 2HA3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH CHOLINE                                               
REMARK 900 RELATED ID: 2Y2U   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY             
REMARK 900  VX-UPDATE                                                           
REMARK 900 RELATED ID: 1C2B   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
REMARK 900 RELATED ID: 2HA0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM                           
REMARK 900 RELATED ID: 2XUF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (              
REMARK 900  1 MTH)                                                              
REMARK 900 RELATED ID: 2WU3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX          
REMARK 900   WITH FENAMIPHOS AND HI-6                                           
REMARK 900 RELATED ID: 2JEY   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH HLO-7             
REMARK 900 RELATED ID: 2JGI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)                       
REMARK 900 RELATED ID: 1N5R   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  PROPIDIUM COMPLEX                                                   
REMARK 900 RELATED ID: 2XUH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (              
REMARK 900  10 MTH)                                                             
REMARK 900 RELATED ID: 2JGJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED METHAMIDOPHOS                                               
REMARK 900 RELATED ID: 1J06   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN THE              
REMARK 900  APOFORM                                                             
REMARK 900 RELATED ID: 2C0P   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY                
REMARK 900  TABUN                                                               
REMARK 900 RELATED ID: 2JF0   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN             
REMARK 900  AND ORTHO-7                                                         
REMARK 900 RELATED ID: 2XUO   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A MUTANT IN COMPLEX                  
REMARK 900  WITH SOAKED TZ2PA6 ANTI INHIBITOR                                   
REMARK 900 RELATED ID: 2XUI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1              
REMARK 900   WK)                                                                
REMARK 900 RELATED ID: 2H9Y   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH M-(N,N,N-TRIMETHYLAMMONIO)                            
REMARK 900  TRIFLUOROACETOPHENONE                                               
REMARK 900 RELATED ID: 2WHR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH           
REMARK 900   K027                                                               
REMARK 900 RELATED ID: 1N5M   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  GALLAMINE COMPLEX                                                   
REMARK 900 RELATED ID: 2HA5   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  ACETYLCHOLINESTERASECOMPLEXED WITH ACETYLTHIOCHOLINE                
REMARK 900 RELATED ID: 2XUQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX              
REMARK 900   WITH SOAKED TZ2PA6 ANTI-SYN INHIBITORS                             
REMARK 900 RELATED ID: 2HA2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH SUCCINYLCHOLINE                                       
REMARK 900 RELATED ID: 2WHP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY        
REMARK 900   SARIN AND IN COMPLEX WITH HI-6                                     
REMARK 900 RELATED ID: 2JEZ   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN             
REMARK 900  AND HLO-7                                                           
REMARK 900 RELATED ID: 2JGK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED FENAMIPHOS                                                  
REMARK 900 RELATED ID: 1KU6   RELATED DB: PDB                                   
REMARK 900  FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX                     
REMARK 900 RELATED ID: 2HA4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH ACETYLCHOLINE              
REMARK 900 RELATED ID: 1J07   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  DECIDIUM COMPLEX                                                    
REMARK 900 RELATED ID: 2HA7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH BUTYRYLTHIOCHOLINE         
REMARK 900 RELATED ID: 2JGF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED FENAMIPHOS                                              
REMARK 900 RELATED ID: 2WU4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX          
REMARK 900   WITH FENAMIPHOS AND ORTHO-7                                        
REMARK 900 RELATED ID: 2Y2V   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY             
REMARK 900  SARIN-UPDATE                                                        
REMARK 900 RELATED ID: 1C2O   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CONTAINS MUTATION L544STOP TO PRODUCE TRUNCATION                     
DBREF  4A16 A    4   543  UNP    P21836   ACES_MOUSE      35    574             
DBREF  4A16 B    4   543  UNP    P21836   ACES_MOUSE      35    574             
DBREF  4A16 C    4   543  UNP    P21836   ACES_MOUSE      35    574             
DBREF  4A16 D    4   543  UNP    P21836   ACES_MOUSE      35    574             
SEQADV 4A16 ALA A  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 THR A  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 GLU A  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 ALA A  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 PRO A  548  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 ALA B  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 THR B  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 GLU B  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 ALA B  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 PRO B  548  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 ALA C  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 THR C  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 GLU C  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 ALA C  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 PRO C  548  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 ALA D  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 THR D  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 GLU D  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 ALA D  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4A16 PRO D  548  UNP  P21836              EXPRESSION TAG                 
SEQRES   1 A  545  GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG GLY GLY GLN          
SEQRES   2 A  545  LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY GLY PRO VAL          
SEQRES   3 A  545  SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL          
SEQRES   4 A  545  GLY SER ARG ARG PHE MET PRO PRO GLU PRO LYS ARG PRO          
SEQRES   5 A  545  TRP SER GLY VAL LEU ASP ALA THR THR PHE GLN ASN VAL          
SEQRES   6 A  545  CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU          
SEQRES   7 A  545  GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU          
SEQRES   8 A  545  ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG          
SEQRES   9 A  545  PRO ALA SER PRO THR PRO VAL LEU ILE TRP ILE TYR GLY          
SEQRES  10 A  545  GLY GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR          
SEQRES  11 A  545  ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY ALA VAL LEU          
SEQRES  12 A  545  VAL SER MET ASN TYR ARG VAL GLY THR PHE GLY PHE LEU          
SEQRES  13 A  545  ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY          
SEQRES  14 A  545  LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU          
SEQRES  15 A  545  ASN ILE ALA ALA PHE GLY GLY ASP PRO MET SER VAL THR          
SEQRES  16 A  545  LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET          
SEQRES  17 A  545  HIS ILE LEU SER LEU PRO SER ARG SER LEU PHE HIS ARG          
SEQRES  18 A  545  ALA VAL LEU GLN SER GLY THR PRO ASN GLY PRO TRP ALA          
SEQRES  19 A  545  THR VAL SER ALA GLY GLU ALA ARG ARG ARG ALA THR LEU          
SEQRES  20 A  545  LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY GLY ALA GLY          
SEQRES  21 A  545  GLY ASN ASP THR GLU LEU ILE ALA CYS LEU ARG THR ARG          
SEQRES  22 A  545  PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP HIS VAL LEU          
SEQRES  23 A  545  PRO GLN GLU SER ILE PHE ARG PHE SER PHE VAL PRO VAL          
SEQRES  24 A  545  VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU          
SEQRES  25 A  545  ILE ASN THR GLY ASP PHE GLN ASP LEU GLN VAL LEU VAL          
SEQRES  26 A  545  GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR          
SEQRES  27 A  545  GLY VAL PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE          
SEQRES  28 A  545  SER ARG ALA GLN PHE LEU ALA GLY VAL ARG ILE GLY VAL          
SEQRES  29 A  545  PRO GLN ALA SER ASP LEU ALA ALA GLU ALA VAL VAL LEU          
SEQRES  30 A  545  HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO THR HIS          
SEQRES  31 A  545  LEU ARG ASP ALA MET SER ALA VAL VAL GLY ASP HIS ASN          
SEQRES  32 A  545  VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA          
SEQRES  33 A  545  ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE PHE GLU HIS          
SEQRES  34 A  545  ARG ALA SER THR LEU THR TRP PRO LEU TRP MET GLY VAL          
SEQRES  35 A  545  PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY LEU PRO          
SEQRES  36 A  545  LEU ASP PRO SER LEU ASN TYR THR THR GLU GLU ARG ILE          
SEQRES  37 A  545  PHE ALA GLN ARG LEU MET LYS TYR TRP THR ASN PHE ALA          
SEQRES  38 A  545  ARG THR GLY ASP PRO ASN ASP PRO ARG ASP SER LYS SER          
SEQRES  39 A  545  PRO GLN TRP PRO PRO TYR THR THR ALA ALA GLN GLN TYR          
SEQRES  40 A  545  VAL SER LEU ASN LEU LYS PRO LEU GLU VAL ARG ARG GLY          
SEQRES  41 A  545  LEU ARG ALA GLN THR CYS ALA PHE TRP ASN ARG PHE LEU          
SEQRES  42 A  545  PRO LYS LEU LEU SER ALA THR ALA THR GLU ALA PRO              
SEQRES   1 B  545  GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG GLY GLY GLN          
SEQRES   2 B  545  LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY GLY PRO VAL          
SEQRES   3 B  545  SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL          
SEQRES   4 B  545  GLY SER ARG ARG PHE MET PRO PRO GLU PRO LYS ARG PRO          
SEQRES   5 B  545  TRP SER GLY VAL LEU ASP ALA THR THR PHE GLN ASN VAL          
SEQRES   6 B  545  CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU          
SEQRES   7 B  545  GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU          
SEQRES   8 B  545  ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG          
SEQRES   9 B  545  PRO ALA SER PRO THR PRO VAL LEU ILE TRP ILE TYR GLY          
SEQRES  10 B  545  GLY GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR          
SEQRES  11 B  545  ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY ALA VAL LEU          
SEQRES  12 B  545  VAL SER MET ASN TYR ARG VAL GLY THR PHE GLY PHE LEU          
SEQRES  13 B  545  ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY          
SEQRES  14 B  545  LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU          
SEQRES  15 B  545  ASN ILE ALA ALA PHE GLY GLY ASP PRO MET SER VAL THR          
SEQRES  16 B  545  LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET          
SEQRES  17 B  545  HIS ILE LEU SER LEU PRO SER ARG SER LEU PHE HIS ARG          
SEQRES  18 B  545  ALA VAL LEU GLN SER GLY THR PRO ASN GLY PRO TRP ALA          
SEQRES  19 B  545  THR VAL SER ALA GLY GLU ALA ARG ARG ARG ALA THR LEU          
SEQRES  20 B  545  LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY GLY ALA GLY          
SEQRES  21 B  545  GLY ASN ASP THR GLU LEU ILE ALA CYS LEU ARG THR ARG          
SEQRES  22 B  545  PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP HIS VAL LEU          
SEQRES  23 B  545  PRO GLN GLU SER ILE PHE ARG PHE SER PHE VAL PRO VAL          
SEQRES  24 B  545  VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU          
SEQRES  25 B  545  ILE ASN THR GLY ASP PHE GLN ASP LEU GLN VAL LEU VAL          
SEQRES  26 B  545  GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR          
SEQRES  27 B  545  GLY VAL PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE          
SEQRES  28 B  545  SER ARG ALA GLN PHE LEU ALA GLY VAL ARG ILE GLY VAL          
SEQRES  29 B  545  PRO GLN ALA SER ASP LEU ALA ALA GLU ALA VAL VAL LEU          
SEQRES  30 B  545  HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO THR HIS          
SEQRES  31 B  545  LEU ARG ASP ALA MET SER ALA VAL VAL GLY ASP HIS ASN          
SEQRES  32 B  545  VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA          
SEQRES  33 B  545  ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE PHE GLU HIS          
SEQRES  34 B  545  ARG ALA SER THR LEU THR TRP PRO LEU TRP MET GLY VAL          
SEQRES  35 B  545  PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY LEU PRO          
SEQRES  36 B  545  LEU ASP PRO SER LEU ASN TYR THR THR GLU GLU ARG ILE          
SEQRES  37 B  545  PHE ALA GLN ARG LEU MET LYS TYR TRP THR ASN PHE ALA          
SEQRES  38 B  545  ARG THR GLY ASP PRO ASN ASP PRO ARG ASP SER LYS SER          
SEQRES  39 B  545  PRO GLN TRP PRO PRO TYR THR THR ALA ALA GLN GLN TYR          
SEQRES  40 B  545  VAL SER LEU ASN LEU LYS PRO LEU GLU VAL ARG ARG GLY          
SEQRES  41 B  545  LEU ARG ALA GLN THR CYS ALA PHE TRP ASN ARG PHE LEU          
SEQRES  42 B  545  PRO LYS LEU LEU SER ALA THR ALA THR GLU ALA PRO              
SEQRES   1 C  545  GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG GLY GLY GLN          
SEQRES   2 C  545  LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY GLY PRO VAL          
SEQRES   3 C  545  SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL          
SEQRES   4 C  545  GLY SER ARG ARG PHE MET PRO PRO GLU PRO LYS ARG PRO          
SEQRES   5 C  545  TRP SER GLY VAL LEU ASP ALA THR THR PHE GLN ASN VAL          
SEQRES   6 C  545  CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU          
SEQRES   7 C  545  GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU          
SEQRES   8 C  545  ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG          
SEQRES   9 C  545  PRO ALA SER PRO THR PRO VAL LEU ILE TRP ILE TYR GLY          
SEQRES  10 C  545  GLY GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR          
SEQRES  11 C  545  ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY ALA VAL LEU          
SEQRES  12 C  545  VAL SER MET ASN TYR ARG VAL GLY THR PHE GLY PHE LEU          
SEQRES  13 C  545  ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY          
SEQRES  14 C  545  LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU          
SEQRES  15 C  545  ASN ILE ALA ALA PHE GLY GLY ASP PRO MET SER VAL THR          
SEQRES  16 C  545  LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET          
SEQRES  17 C  545  HIS ILE LEU SER LEU PRO SER ARG SER LEU PHE HIS ARG          
SEQRES  18 C  545  ALA VAL LEU GLN SER GLY THR PRO ASN GLY PRO TRP ALA          
SEQRES  19 C  545  THR VAL SER ALA GLY GLU ALA ARG ARG ARG ALA THR LEU          
SEQRES  20 C  545  LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY GLY ALA GLY          
SEQRES  21 C  545  GLY ASN ASP THR GLU LEU ILE ALA CYS LEU ARG THR ARG          
SEQRES  22 C  545  PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP HIS VAL LEU          
SEQRES  23 C  545  PRO GLN GLU SER ILE PHE ARG PHE SER PHE VAL PRO VAL          
SEQRES  24 C  545  VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU          
SEQRES  25 C  545  ILE ASN THR GLY ASP PHE GLN ASP LEU GLN VAL LEU VAL          
SEQRES  26 C  545  GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR          
SEQRES  27 C  545  GLY VAL PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE          
SEQRES  28 C  545  SER ARG ALA GLN PHE LEU ALA GLY VAL ARG ILE GLY VAL          
SEQRES  29 C  545  PRO GLN ALA SER ASP LEU ALA ALA GLU ALA VAL VAL LEU          
SEQRES  30 C  545  HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO THR HIS          
SEQRES  31 C  545  LEU ARG ASP ALA MET SER ALA VAL VAL GLY ASP HIS ASN          
SEQRES  32 C  545  VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA          
SEQRES  33 C  545  ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE PHE GLU HIS          
SEQRES  34 C  545  ARG ALA SER THR LEU THR TRP PRO LEU TRP MET GLY VAL          
SEQRES  35 C  545  PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY LEU PRO          
SEQRES  36 C  545  LEU ASP PRO SER LEU ASN TYR THR THR GLU GLU ARG ILE          
SEQRES  37 C  545  PHE ALA GLN ARG LEU MET LYS TYR TRP THR ASN PHE ALA          
SEQRES  38 C  545  ARG THR GLY ASP PRO ASN ASP PRO ARG ASP SER LYS SER          
SEQRES  39 C  545  PRO GLN TRP PRO PRO TYR THR THR ALA ALA GLN GLN TYR          
SEQRES  40 C  545  VAL SER LEU ASN LEU LYS PRO LEU GLU VAL ARG ARG GLY          
SEQRES  41 C  545  LEU ARG ALA GLN THR CYS ALA PHE TRP ASN ARG PHE LEU          
SEQRES  42 C  545  PRO LYS LEU LEU SER ALA THR ALA THR GLU ALA PRO              
SEQRES   1 D  545  GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG GLY GLY GLN          
SEQRES   2 D  545  LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY GLY PRO VAL          
SEQRES   3 D  545  SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL          
SEQRES   4 D  545  GLY SER ARG ARG PHE MET PRO PRO GLU PRO LYS ARG PRO          
SEQRES   5 D  545  TRP SER GLY VAL LEU ASP ALA THR THR PHE GLN ASN VAL          
SEQRES   6 D  545  CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU          
SEQRES   7 D  545  GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU          
SEQRES   8 D  545  ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG          
SEQRES   9 D  545  PRO ALA SER PRO THR PRO VAL LEU ILE TRP ILE TYR GLY          
SEQRES  10 D  545  GLY GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR          
SEQRES  11 D  545  ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY ALA VAL LEU          
SEQRES  12 D  545  VAL SER MET ASN TYR ARG VAL GLY THR PHE GLY PHE LEU          
SEQRES  13 D  545  ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY          
SEQRES  14 D  545  LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU          
SEQRES  15 D  545  ASN ILE ALA ALA PHE GLY GLY ASP PRO MET SER VAL THR          
SEQRES  16 D  545  LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET          
SEQRES  17 D  545  HIS ILE LEU SER LEU PRO SER ARG SER LEU PHE HIS ARG          
SEQRES  18 D  545  ALA VAL LEU GLN SER GLY THR PRO ASN GLY PRO TRP ALA          
SEQRES  19 D  545  THR VAL SER ALA GLY GLU ALA ARG ARG ARG ALA THR LEU          
SEQRES  20 D  545  LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY GLY ALA GLY          
SEQRES  21 D  545  GLY ASN ASP THR GLU LEU ILE ALA CYS LEU ARG THR ARG          
SEQRES  22 D  545  PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP HIS VAL LEU          
SEQRES  23 D  545  PRO GLN GLU SER ILE PHE ARG PHE SER PHE VAL PRO VAL          
SEQRES  24 D  545  VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU          
SEQRES  25 D  545  ILE ASN THR GLY ASP PHE GLN ASP LEU GLN VAL LEU VAL          
SEQRES  26 D  545  GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR          
SEQRES  27 D  545  GLY VAL PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE          
SEQRES  28 D  545  SER ARG ALA GLN PHE LEU ALA GLY VAL ARG ILE GLY VAL          
SEQRES  29 D  545  PRO GLN ALA SER ASP LEU ALA ALA GLU ALA VAL VAL LEU          
SEQRES  30 D  545  HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO THR HIS          
SEQRES  31 D  545  LEU ARG ASP ALA MET SER ALA VAL VAL GLY ASP HIS ASN          
SEQRES  32 D  545  VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA          
SEQRES  33 D  545  ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE PHE GLU HIS          
SEQRES  34 D  545  ARG ALA SER THR LEU THR TRP PRO LEU TRP MET GLY VAL          
SEQRES  35 D  545  PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY LEU PRO          
SEQRES  36 D  545  LEU ASP PRO SER LEU ASN TYR THR THR GLU GLU ARG ILE          
SEQRES  37 D  545  PHE ALA GLN ARG LEU MET LYS TYR TRP THR ASN PHE ALA          
SEQRES  38 D  545  ARG THR GLY ASP PRO ASN ASP PRO ARG ASP SER LYS SER          
SEQRES  39 D  545  PRO GLN TRP PRO PRO TYR THR THR ALA ALA GLN GLN TYR          
SEQRES  40 D  545  VAL SER LEU ASN LEU LYS PRO LEU GLU VAL ARG ARG GLY          
SEQRES  41 D  545  LEU ARG ALA GLN THR CYS ALA PHE TRP ASN ARG PHE LEU          
SEQRES  42 D  545  PRO LYS LEU LEU SER ALA THR ALA THR GLU ALA PRO              
HET    H34  A1545      30                                                       
HET    SO4  A1546       5                                                       
HET    SO4  A1547       5                                                       
HET    SO4  A1548       5                                                       
HET     CL  A1549       1                                                       
HET     CL  A1550       1                                                       
HET    H34  B1545      30                                                       
HET    NAG  B1546      14                                                       
HET    SO4  B1547       5                                                       
HET    SO4  B1548       5                                                       
HET    SO4  B1549       5                                                       
HET    SO4  B1550       5                                                       
HET     CL  B1551       1                                                       
HET    H34  C1545      30                                                       
HET    SO4  C1546       5                                                       
HET    SO4  C1547       5                                                       
HET    SO4  C1548       5                                                       
HET     CL  C1549       1                                                       
HET     CL  C1550       1                                                       
HET    H34  D1545      30                                                       
HET    SO4  D1546       5                                                       
HET    SO4  D1547       5                                                       
HET    SO4  D1548       5                                                       
HET    SO4  D1549       5                                                       
HETNAM     H34 (1-{4-[(7S,11S)-12-AMINO-3-CHLORO-6,7,10,11-                     
HETNAM   2 H34  TETRAHYDRO-7,11-METHANOCYCLOOCTA[B]QUINOLIN-9-                  
HETNAM   3 H34  YL]BUTYL}-1H-1,2,3-TRIAZOL-4-YL)METHANOL                        
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   5  H34    4(C23 H26 CL N5 O)                                           
FORMUL   6  SO4    14(O4 S 2-)                                                  
FORMUL   7   CL    5(CL 1-)                                                     
FORMUL   8  NAG    C8 H15 N O6                                                  
FORMUL   9  HOH   *2323(H2 O)                                                   
HELIX    1   1 VAL A   42  ARG A   46  5                                   5    
HELIX    2   2 PHE A   80  MET A   85  1                                   6    
HELIX    3   3 LEU A  130  ASP A  134  5                                   5    
HELIX    4   4 GLY A  135  GLY A  143  1                                   9    
HELIX    5   5 VAL A  153  LEU A  159  1                                   7    
HELIX    6   6 ASN A  170  ILE A  187  1                                  18    
HELIX    7   7 ALA A  188  PHE A  190  5                                   3    
HELIX    8   8 SER A  203  LEU A  214  1                                  12    
HELIX    9   9 SER A  215  SER A  220  1                                   6    
HELIX   10  10 SER A  240  VAL A  255  1                                  16    
HELIX   11  11 ASN A  265  THR A  275  1                                  11    
HELIX   12  12 PRO A  277  GLU A  285  1                                   9    
HELIX   13  13 TRP A  286  LEU A  289  5                                   4    
HELIX   14  14 THR A  311  GLY A  319  1                                   9    
HELIX   15  15 GLY A  335  VAL A  343  1                                   9    
HELIX   16  16 SER A  355  VAL A  367  1                                  13    
HELIX   17  17 SER A  371  THR A  383  1                                  13    
HELIX   18  18 ASP A  390  VAL A  407  1                                  18    
HELIX   19  19 VAL A  407  GLN A  421  1                                  15    
HELIX   20  20 PRO A  440  GLY A  444  5                                   5    
HELIX   21  21 GLU A  450  PHE A  455  1                                   6    
HELIX   22  22 GLY A  456  ASP A  460  5                                   5    
HELIX   23  23 ASP A  460  ASN A  464  5                                   5    
HELIX   24  24 THR A  466  GLY A  487  1                                  22    
HELIX   25  25 ARG A  525  ARG A  534  1                                  10    
HELIX   26  26 ARG A  534  ALA A  542  1                                   9    
HELIX   27  27 ASP B    5  GLN B    7  5                                   3    
HELIX   28  28 VAL B   42  ARG B   46  5                                   5    
HELIX   29  29 PHE B   80  MET B   85  1                                   6    
HELIX   30  30 LEU B  130  ASP B  134  5                                   5    
HELIX   31  31 GLY B  135  VAL B  141  1                                   7    
HELIX   32  32 VAL B  153  LEU B  159  1                                   7    
HELIX   33  33 ASN B  170  ILE B  187  1                                  18    
HELIX   34  34 ALA B  188  PHE B  190  5                                   3    
HELIX   35  35 SER B  203  SER B  215  1                                  13    
HELIX   36  36 LEU B  216  PHE B  222  5                                   7    
HELIX   37  37 ALA B  241  VAL B  255  1                                  15    
HELIX   38  38 ASN B  265  THR B  275  1                                  11    
HELIX   39  39 PRO B  277  ASP B  283  1                                   7    
HELIX   40  40 HIS B  284  LEU B  289  5                                   6    
HELIX   41  41 THR B  311  GLY B  319  1                                   9    
HELIX   42  42 GLY B  335  VAL B  343  1                                   9    
HELIX   43  43 SER B  355  VAL B  367  1                                  13    
HELIX   44  44 SER B  371  THR B  383  1                                  13    
HELIX   45  45 ASP B  390  VAL B  407  1                                  18    
HELIX   46  46 VAL B  407  GLN B  421  1                                  15    
HELIX   47  47 PRO B  440  GLY B  444  5                                   5    
HELIX   48  48 GLU B  450  GLY B  456  1                                   7    
HELIX   49  49 ASP B  460  ASN B  464  5                                   5    
HELIX   50  50 THR B  466  GLY B  487  1                                  22    
HELIX   51  51 ARG B  525  ARG B  534  1                                  10    
HELIX   52  52 ARG B  534  SER B  541  1                                   8    
HELIX   53  53 VAL C   42  ARG C   46  5                                   5    
HELIX   54  54 PHE C   80  MET C   85  1                                   6    
HELIX   55  55 LEU C  130  ASP C  134  5                                   5    
HELIX   56  56 GLY C  135  GLY C  143  1                                   9    
HELIX   57  57 VAL C  153  LEU C  159  1                                   7    
HELIX   58  58 ASN C  170  ILE C  187  1                                  18    
HELIX   59  59 ALA C  188  PHE C  190  5                                   3    
HELIX   60  60 SER C  203  LEU C  214  1                                  12    
HELIX   61  61 SER C  215  SER C  220  1                                   6    
HELIX   62  62 ALA C  241  VAL C  255  1                                  15    
HELIX   63  63 ASN C  265  ARG C  274  1                                  10    
HELIX   64  64 PRO C  277  ASP C  283  1                                   7    
HELIX   65  65 HIS C  284  LEU C  289  5                                   6    
HELIX   66  66 THR C  311  THR C  318  1                                   8    
HELIX   67  67 GLY C  335  VAL C  343  1                                   9    
HELIX   68  68 SER C  355  VAL C  367  1                                  13    
HELIX   69  69 SER C  371  THR C  383  1                                  13    
HELIX   70  70 ASP C  390  VAL C  407  1                                  18    
HELIX   71  71 VAL C  407  GLN C  421  1                                  15    
HELIX   72  72 PRO C  440  GLY C  444  5                                   5    
HELIX   73  73 GLU C  450  PHE C  455  1                                   6    
HELIX   74  74 GLY C  456  ASP C  460  5                                   5    
HELIX   75  75 ASP C  460  ASN C  464  5                                   5    
HELIX   76  76 THR C  466  GLY C  487  1                                  22    
HELIX   77  77 ARG C  525  ARG C  534  1                                  10    
HELIX   78  78 ARG C  534  SER C  541  1                                   8    
HELIX   79  79 ASP D    5  GLN D    7  5                                   3    
HELIX   80  80 VAL D   42  ARG D   46  5                                   5    
HELIX   81  81 PHE D   80  MET D   85  1                                   6    
HELIX   82  82 LEU D  130  ASP D  134  5                                   5    
HELIX   83  83 GLY D  135  GLY D  143  1                                   9    
HELIX   84  84 VAL D  153  LEU D  159  1                                   7    
HELIX   85  85 ASN D  170  ILE D  187  1                                  18    
HELIX   86  86 ALA D  188  PHE D  190  5                                   3    
HELIX   87  87 SER D  203  SER D  215  1                                  13    
HELIX   88  88 SER D  215  SER D  220  1                                   6    
HELIX   89  89 ALA D  241  VAL D  255  1                                  15    
HELIX   90  90 ASN D  265  ARG D  274  1                                  10    
HELIX   91  91 PRO D  277  ASP D  283  1                                   7    
HELIX   92  92 HIS D  284  LEU D  289  5                                   6    
HELIX   93  93 THR D  311  GLY D  319  1                                   9    
HELIX   94  94 GLY D  335  VAL D  343  1                                   9    
HELIX   95  95 SER D  355  VAL D  367  1                                  13    
HELIX   96  96 SER D  371  THR D  383  1                                  13    
HELIX   97  97 ASP D  390  VAL D  407  1                                  18    
HELIX   98  98 VAL D  407  GLN D  421  1                                  15    
HELIX   99  99 PRO D  440  GLY D  444  5                                   5    
HELIX  100 100 GLU D  450  GLY D  456  1                                   7    
HELIX  101 101 LEU D  457  ASN D  464  5                                   8    
HELIX  102 102 THR D  466  GLY D  487  1                                  22    
HELIX  103 103 ARG D  525  PHE D  535  1                                  11    
HELIX  104 104 PHE D  535  THR D  543  1                                   9    
SHEET    1  AA 3 LEU A   9  VAL A  12  0                                        
SHEET    2  AA 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3  AA 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  ARG A  18           
SHEET    1  AB11 ILE A  20  ALA A  24  0                                        
SHEET    2  AB11 GLY A  27  PRO A  36 -1  O  GLY A  27   N  ALA A  24           
SHEET    3  AB11 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4  AB11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5  AB11 THR A 112  ILE A 118  1  O  PRO A 113   N  VAL A 145           
SHEET    6  AB11 GLY A 192  GLU A 202  1  N  ASP A 193   O  THR A 112           
SHEET    7  AB11 ARG A 224  GLN A 228  1  O  ARG A 224   N  LEU A 199           
SHEET    8  AB11 GLN A 325  VAL A 331  1  O  GLN A 325   N  ALA A 225           
SHEET    9  AB11 ARG A 424  PHE A 430  1  O  ARG A 424   N  VAL A 326           
SHEET   10  AB11 GLN A 509  LEU A 513  1  O  VAL A 511   N  ILE A 429           
SHEET   11  AB11 GLU A 519  ARG A 522 -1  O  GLU A 519   N  SER A 512           
SHEET    1  AC 2 VAL A  68  CYS A  69  0                                        
SHEET    2  AC 2 LEU A  92  SER A  93  1  N  SER A  93   O  VAL A  68           
SHEET    1  BA 3 LEU B   9  VAL B  12  0                                        
SHEET    2  BA 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12           
SHEET    3  BA 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  ARG B  18           
SHEET    1  BB11 ILE B  20  ALA B  24  0                                        
SHEET    2  BB11 GLY B  27  PRO B  36 -1  O  GLY B  27   N  ALA B  24           
SHEET    3  BB11 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4  BB11 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5  BB11 THR B 112  ILE B 118  1  O  PRO B 113   N  VAL B 145           
SHEET    6  BB11 GLY B 192  GLU B 202  1  N  ASP B 193   O  THR B 112           
SHEET    7  BB11 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8  BB11 GLN B 325  VAL B 331  1  O  GLN B 325   N  ALA B 225           
SHEET    9  BB11 ARG B 424  PHE B 430  1  O  ARG B 424   N  VAL B 326           
SHEET   10  BB11 GLN B 509  LEU B 513  1  O  VAL B 511   N  ILE B 429           
SHEET   11  BB11 GLU B 519  ARG B 522 -1  O  GLU B 519   N  SER B 512           
SHEET    1  BC 2 VAL B  68  CYS B  69  0                                        
SHEET    2  BC 2 LEU B  92  SER B  93  1  N  SER B  93   O  VAL B  68           
SHEET    1  BD 2 VAL B 239  SER B 240  0                                        
SHEET    2  BD 2 VAL B 302  VAL B 303  1  N  VAL B 303   O  VAL B 239           
SHEET    1  CA 3 LEU C   9  VAL C  12  0                                        
SHEET    2  CA 3 GLY C  15  ARG C  18 -1  O  GLY C  15   N  VAL C  12           
SHEET    3  CA 3 VAL C  59  ASP C  61  1  O  LEU C  60   N  ARG C  18           
SHEET    1  CB11 ILE C  20  ALA C  24  0                                        
SHEET    2  CB11 GLY C  27  PRO C  36 -1  O  GLY C  27   N  ALA C  24           
SHEET    3  CB11 TYR C  98  PRO C 104 -1  O  LEU C  99   N  ILE C  35           
SHEET    4  CB11 VAL C 145  MET C 149 -1  O  LEU C 146   N  TRP C 102           
SHEET    5  CB11 THR C 112  ILE C 118  1  O  PRO C 113   N  VAL C 145           
SHEET    6  CB11 GLY C 192  GLU C 202  1  N  ASP C 193   O  THR C 112           
SHEET    7  CB11 ARG C 224  GLN C 228  1  O  ARG C 224   N  LEU C 199           
SHEET    8  CB11 GLN C 325  VAL C 331  1  O  GLN C 325   N  ALA C 225           
SHEET    9  CB11 ARG C 424  PHE C 430  1  O  ARG C 424   N  VAL C 326           
SHEET   10  CB11 GLN C 509  LEU C 513  1  O  VAL C 511   N  ILE C 429           
SHEET   11  CB11 GLU C 519  ARG C 522 -1  O  GLU C 519   N  SER C 512           
SHEET    1  CC 2 VAL C  68  CYS C  69  0                                        
SHEET    2  CC 2 LEU C  92  SER C  93  1  N  SER C  93   O  VAL C  68           
SHEET    1  CD 2 VAL C 239  SER C 240  0                                        
SHEET    2  CD 2 VAL C 302  VAL C 303  1  N  VAL C 303   O  VAL C 239           
SHEET    1  DA 3 LEU D   9  VAL D  12  0                                        
SHEET    2  DA 3 GLY D  15  ARG D  18 -1  O  GLY D  15   N  VAL D  12           
SHEET    3  DA 3 VAL D  59  ASP D  61  1  O  LEU D  60   N  ARG D  18           
SHEET    1  DB11 ILE D  20  ALA D  24  0                                        
SHEET    2  DB11 GLY D  27  PRO D  36 -1  O  GLY D  27   N  ALA D  24           
SHEET    3  DB11 TYR D  98  PRO D 104 -1  O  LEU D  99   N  ILE D  35           
SHEET    4  DB11 VAL D 145  MET D 149 -1  O  LEU D 146   N  TRP D 102           
SHEET    5  DB11 THR D 112  ILE D 118  1  O  PRO D 113   N  VAL D 145           
SHEET    6  DB11 GLY D 192  GLU D 202  1  N  ASP D 193   O  THR D 112           
SHEET    7  DB11 ARG D 224  GLN D 228  1  O  ARG D 224   N  LEU D 199           
SHEET    8  DB11 GLN D 325  VAL D 331  1  O  GLN D 325   N  ALA D 225           
SHEET    9  DB11 ARG D 424  PHE D 430  1  O  ARG D 424   N  VAL D 326           
SHEET   10  DB11 GLN D 509  LEU D 513  1  O  VAL D 511   N  ILE D 429           
SHEET   11  DB11 GLU D 519  ARG D 522 -1  O  GLU D 519   N  SER D 512           
SHEET    1  DC 2 VAL D  68  CYS D  69  0                                        
SHEET    2  DC 2 LEU D  92  SER D  93  1  N  SER D  93   O  VAL D  68           
SHEET    1  DD 2 VAL D 239  SER D 240  0                                        
SHEET    2  DD 2 VAL D 302  VAL D 303  1  N  VAL D 303   O  VAL D 239           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.16  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.20  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.12  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.10  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.27  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.14  
SSBOND   7 CYS C   69    CYS C   96                          1555   1555  2.12  
SSBOND   8 CYS C  257    CYS C  272                          1555   1555  2.19  
SSBOND   9 CYS C  409    CYS C  529                          1555   1555  2.16  
SSBOND  10 CYS D   69    CYS D   96                          1555   1555  2.09  
SSBOND  11 CYS D  257    CYS D  272                          1555   1555  2.27  
SSBOND  12 CYS D  409    CYS D  529                          1555   1555  2.10  
CISPEP   1 TYR A  105    PRO A  106          0        -5.69                     
CISPEP   2 PRO A  258    PRO A  259          0        25.99                     
CISPEP   3 SER A  497    PRO A  498          0       -11.09                     
CISPEP   4 TYR B  105    PRO B  106          0         3.33                     
CISPEP   5 CYS B  257    PRO B  258          0       -11.13                     
CISPEP   6 SER B  497    PRO B  498          0       -10.09                     
CISPEP   7 TYR C  105    PRO C  106          0        -1.22                     
CISPEP   8 PRO C  258    PRO C  259          0         9.22                     
CISPEP   9 SER C  497    PRO C  498          0        -4.37                     
CISPEP  10 TYR D  105    PRO D  106          0         1.91                     
CISPEP  11 SER D  497    PRO D  498          0         3.17                     
SITE     1 AC1 16 TRP A  86  GLY A 121  TYR A 124  GLU A 202                    
SITE     2 AC1 16 SER A 203  TRP A 286  PHE A 295  TYR A 337                    
SITE     3 AC1 16 PHE A 338  TYR A 341  TRP A 439  HIS A 447                    
SITE     4 AC1 16 TYR A 449  HOH A2148  HOH A2157  HOH A2428                    
SITE     1 AC2  5 ARG A 525  ALA A 526  GLN A 527  THR A 528                    
SITE     2 AC2  5 HOH A2660                                                     
SITE     1 AC3  3 GLN A 413  ARG A 417  ASN A 533                               
SITE     1 AC4  5 ARG A 356  LEU A 360  HOH A2661  HOH A2663                    
SITE     2 AC4  5 ARG B 534                                                     
SITE     1 AC5  3 ARG A 136  HOH A2057  HOH A2060                               
SITE     1 AC6  3 HOH A2174  HOH A2183  HOH A2250                               
SITE     1 AC7 19 TRP B  86  GLY B 120  GLY B 121  TYR B 124                    
SITE     2 AC7 19 GLU B 202  SER B 203  TRP B 286  PHE B 295                    
SITE     3 AC7 19 ARG B 296  PHE B 297  TYR B 337  PHE B 338                    
SITE     4 AC7 19 TYR B 341  TRP B 439  HIS B 447  TYR B 449                    
SITE     5 AC7 19 HOH B2095  HOH B2325  HOH B2496                               
SITE     1 AC8  9 ASN B 265  GLU B 268  HOH B2287  HOH B2294                    
SITE     2 AC8  9 HOH B2497  HOH B2498  HOH B2499  HOH B2501                    
SITE     3 AC8  9 HOH B2502                                                     
SITE     1 AC9  5 ARG B 525  ALA B 526  GLN B 527  THR B 528                    
SITE     2 AC9  5 HOH B2477                                                     
SITE     1 BC1  5 HIS B 387  PRO B 388  GLU B 389  ASP B 390                    
SITE     2 BC1  5 HOH B2403                                                     
SITE     1 BC2  3 ARG A 534  ARG B 356  HOH B2503                               
SITE     1 BC3  3 GLN B 413  ARG B 417  ASN B 533                               
SITE     1 BC4  2 HOH B2474  HOH B2475                                          
SITE     1 BC5 20 HOH B2276  TRP C  86  GLY C 121  TYR C 124                    
SITE     2 BC5 20 GLU C 202  SER C 203  TRP C 286  SER C 293                    
SITE     3 BC5 20 ILE C 294  PHE C 295  ARG C 296  TYR C 337                    
SITE     4 BC5 20 PHE C 338  TYR C 341  TRP C 439  HIS C 447                    
SITE     5 BC5 20 TYR C 449  HOH C2133  HOH C2220  HOH C2396                    
SITE     1 BC6  5 ARG C 525  ALA C 526  GLN C 527  THR C 528                    
SITE     2 BC6  5 HOH C2604                                                     
SITE     1 BC7  5 VAL C  42  GLY C  43  SER C  44  HOH C2620                    
SITE     2 BC7  5 HOH C2621                                                     
SITE     1 BC8  3 GLN C 413  ARG C 417  HOH C2613                               
SITE     1 BC9  3 GLU C 452  HOH C2522  HOH C2523                               
SITE     1 CC1  2 ARG C 136  HOH C2044                                          
SITE     1 CC2 17 TRP D  86  GLY D 121  TYR D 124  GLU D 202                    
SITE     2 CC2 17 TRP D 286  SER D 293  PHE D 295  ARG D 296                    
SITE     3 CC2 17 TYR D 337  PHE D 338  TYR D 341  TRP D 439                    
SITE     4 CC2 17 HIS D 447  TYR D 449  HOH D2114  HOH D2349                    
SITE     5 CC2 17 HOH D2529                                                     
SITE     1 CC3  6 ARG D 525  ALA D 526  GLN D 527  THR D 528                    
SITE     2 CC3  6 HOH D2511  HOH D2518                                          
SITE     1 CC4  2 ARG D 356  HOH D2530                                          
SITE     1 CC5  3 GLN D 413  ARG D 417  ASN D 533                               
SITE     1 CC6  5 GLU D 519  ARG D 521  ARG D 522  HOH D2505                    
SITE     2 CC6  5 HOH D2533                                                     
CRYST1  137.940  171.930  225.320  90.00  90.00  90.00 P 21 21 21   16          
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      0.007250  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005816  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004438        0.00000                         
TER    4237      ALA A 544                                                      
TER    8454      ALA B 544                                                      
TER   12657      ALA C 544                                                      
TER   16872      ALA D 544                                                      
MASTER      885    0   24  104   70    0   49    619400    4  228  168          
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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