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LongText Report for: 5egn-pdb

Name Class
5egn-pdb
HEADER    HYDROLASE                               27-OCT-15   5EGN              
TITLE     EST816 AS AN N-ACYL HOMOSERINE LACTONE DEGRADING ENZYME               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTERASE;                                                  
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: UNP RESIDUES 1-261;                                        
COMPND   5 SYNONYM: AHL-LACTONASE 816;                                          
COMPND   6 EC: 3.1.1.1;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;                           
SOURCE   3 ORGANISM_TAXID: 77133;                                               
SOURCE   4 GENE: EST816;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    N-ACYL-HOMOSERINE LACTONE, LACTONASE, QUORUM-SENSING,                 
KEYWDS   2 THERMOSTABILITY, HYDROLASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.XIE,X.LIU,L.CAO,Y.LIU                                               
REVDAT   1   02-NOV-16 5EGN    0                                                
JRNL        AUTH   W.XIE,X.LIU,L.CAO,Y.LIU                                      
JRNL        TITL   EST816 AS AN N-ACYL HOMOSERINE LACTONE DEGRADING ENZYME      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.64 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 57279                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2981                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.8237 -  7.2633    0.97     2653   144  0.1768 0.1979        
REMARK   3     2  7.2633 -  5.7690    0.98     2594   157  0.2137 0.2510        
REMARK   3     3  5.7690 -  5.0409    1.00     2641   134  0.1964 0.2053        
REMARK   3     4  5.0409 -  4.5805    0.99     2632   136  0.1800 0.2175        
REMARK   3     5  4.5805 -  4.2524    1.00     2641   118  0.1795 0.2316        
REMARK   3     6  4.2524 -  4.0019    0.99     2611   142  0.1862 0.2734        
REMARK   3     7  4.0019 -  3.8016    0.99     2614   132  0.2014 0.2563        
REMARK   3     8  3.8016 -  3.6362    0.99     2592   143  0.2075 0.2675        
REMARK   3     9  3.6362 -  3.4962    0.99     2624   132  0.2164 0.2422        
REMARK   3    10  3.4962 -  3.3756    0.99     2562   137  0.2274 0.3095        
REMARK   3    11  3.3756 -  3.2701    0.99     2573   170  0.2345 0.2623        
REMARK   3    12  3.2701 -  3.1767    0.99     2606   146  0.2431 0.2851        
REMARK   3    13  3.1767 -  3.0931    0.99     2534   184  0.2490 0.2882        
REMARK   3    14  3.0931 -  3.0176    0.99     2572   131  0.2542 0.2977        
REMARK   3    15  3.0176 -  2.9490    0.99     2605   133  0.2550 0.3260        
REMARK   3    16  2.9490 -  2.8863    0.99     2562   144  0.2685 0.2900        
REMARK   3    17  2.8863 -  2.8286    0.99     2577   125  0.2742 0.3081        
REMARK   3    18  2.8286 -  2.7752    0.98     2580   137  0.2698 0.2775        
REMARK   3    19  2.7752 -  2.7256    0.99     2554   159  0.2787 0.3176        
REMARK   3    20  2.7256 -  2.6794    0.99     2534   148  0.2917 0.3425        
REMARK   3    21  2.6794 -  2.6362    0.93     2437   129  0.3028 0.3637        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.060           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003          16175                                  
REMARK   3   ANGLE     :  0.729          22017                                  
REMARK   3   CHIRALITY :  0.028           2425                                  
REMARK   3   PLANARITY :  0.004           2938                                  
REMARK   3   DIHEDRAL  : 13.882           5712                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5EGN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214679.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57955                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.630                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: 2XUA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG 3350, 0.1M SODIUM ACETATE PH     
REMARK 280  5.6, 0.2M SODIUM CHLORIDE, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       39.27250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: 2670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
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: 2670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 2590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, E                                  
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: 4                                                       
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: 2630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     ALA A   263                                                      
REMARK 465     LEU A   264                                                      
REMARK 465     GLU A   265                                                      
REMARK 465     HIS A   266                                                      
REMARK 465     HIS A   267                                                      
REMARK 465     HIS A   268                                                      
REMARK 465     HIS A   269                                                      
REMARK 465     HIS A   270                                                      
REMARK 465     HIS A   271                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     ALA B   263                                                      
REMARK 465     LEU B   264                                                      
REMARK 465     GLU B   265                                                      
REMARK 465     HIS B   266                                                      
REMARK 465     HIS B   267                                                      
REMARK 465     HIS B   268                                                      
REMARK 465     HIS B   269                                                      
REMARK 465     HIS B   270                                                      
REMARK 465     HIS B   271                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C   261                                                      
REMARK 465     ALA C   262                                                      
REMARK 465     ALA C   263                                                      
REMARK 465     LEU C   264                                                      
REMARK 465     GLU C   265                                                      
REMARK 465     HIS C   266                                                      
REMARK 465     HIS C   267                                                      
REMARK 465     HIS C   268                                                      
REMARK 465     HIS C   269                                                      
REMARK 465     HIS C   270                                                      
REMARK 465     HIS C   271                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D   261                                                      
REMARK 465     ALA D   262                                                      
REMARK 465     ALA D   263                                                      
REMARK 465     LEU D   264                                                      
REMARK 465     GLU D   265                                                      
REMARK 465     HIS D   266                                                      
REMARK 465     HIS D   267                                                      
REMARK 465     HIS D   268                                                      
REMARK 465     HIS D   269                                                      
REMARK 465     HIS D   270                                                      
REMARK 465     HIS D   271                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ALA E   261                                                      
REMARK 465     ALA E   262                                                      
REMARK 465     ALA E   263                                                      
REMARK 465     LEU E   264                                                      
REMARK 465     GLU E   265                                                      
REMARK 465     HIS E   266                                                      
REMARK 465     HIS E   267                                                      
REMARK 465     HIS E   268                                                      
REMARK 465     HIS E   269                                                      
REMARK 465     HIS E   270                                                      
REMARK 465     HIS E   271                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F   262                                                      
REMARK 465     ALA F   263                                                      
REMARK 465     LEU F   264                                                      
REMARK 465     GLU F   265                                                      
REMARK 465     HIS F   266                                                      
REMARK 465     HIS F   267                                                      
REMARK 465     HIS F   268                                                      
REMARK 465     HIS F   269                                                      
REMARK 465     HIS F   270                                                      
REMARK 465     HIS F   271                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ALA G   261                                                      
REMARK 465     ALA G   262                                                      
REMARK 465     ALA G   263                                                      
REMARK 465     LEU G   264                                                      
REMARK 465     GLU G   265                                                      
REMARK 465     HIS G   266                                                      
REMARK 465     HIS G   267                                                      
REMARK 465     HIS G   268                                                      
REMARK 465     HIS G   269                                                      
REMARK 465     HIS G   270                                                      
REMARK 465     HIS G   271                                                      
REMARK 465     MET H     1                                                      
REMARK 465     VAL H   260                                                      
REMARK 465     ALA H   261                                                      
REMARK 465     ALA H   262                                                      
REMARK 465     ALA H   263                                                      
REMARK 465     LEU H   264                                                      
REMARK 465     GLU H   265                                                      
REMARK 465     HIS H   266                                                      
REMARK 465     HIS H   267                                                      
REMARK 465     HIS H   268                                                      
REMARK 465     HIS H   269                                                      
REMARK 465     HIS H   270                                                      
REMARK 465     HIS H   271                                                      
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     GLU A 129    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 135    CG   CD   OE1  NE2                                  
REMARK 470     PHE D 259    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE E 134    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PRO F 128    CG   CD                                             
REMARK 470     GLU F 129    CG   CD   OE1  OE2                                  
REMARK 470     PHE F 259    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PRO G 127    CG   CD                                             
REMARK 470     GLN G 135    CG   CD   OE1  NE2                                  
REMARK 470     ASN G 136    CG   OD1  ND2                                       
REMARK 470     LYS G 177    CG   CD   CE   NZ                                   
REMARK 470     PHE G 180    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PRO G 187    CG   CD                                             
REMARK 470     ASN G 188    CG   OD1  ND2                                       
REMARK 470     ARG G 198    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG G 257    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H  83    CG   CD   CE   NZ                                   
REMARK 470     GLN H 108    CG   CD   OE1  NE2                                  
REMARK 470     GLU H 124    CG   CD   OE1  OE2                                  
REMARK 470     PRO H 127    CG   CD                                             
REMARK 470     GLU H 233    CG   CD   OE1  OE2                                  
REMARK 470     ARG H 248    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU H 251    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 254    CG   CD   OE1  OE2                                  
REMARK 470     ARG H 257    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE H 259    CG   CD1  CD2  CE1  CE2  CZ                         
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   O    GLY G    55     O    HOH G   301              1.91            
REMARK 500   O    ASN G   174     O    HOH G   301              2.04            
REMARK 500   OD1  ASP E    80     NH2  ARG E   109              2.14            
REMARK 500   O    LEU D   256     O    HOH D   301              2.14            
REMARK 500   NZ   LYS G    61     O    SER G   173              2.15            
REMARK 500   OE1  GLU A   251     O    HOH A   301              2.17            
REMARK 500   OD1  ASP F    80     NH2  ARG F   109              2.19            
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   OG1  THR D    64     ND2  ASN D   238     2547     2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  29       -4.81     72.66                                   
REMARK 500    THR A  30     -157.10   -103.36                                   
REMARK 500    SER A  93     -107.59     53.40                                   
REMARK 500    VAL A 260      -48.45   -133.48                                   
REMARK 500    SER B  29       -4.95     74.47                                   
REMARK 500    THR B  30     -158.33   -105.72                                   
REMARK 500    SER B  93     -106.28     53.42                                   
REMARK 500    VAL B 260       89.46    -60.88                                   
REMARK 500    SER C  29       -8.36     73.85                                   
REMARK 500    THR C  30     -157.45   -105.13                                   
REMARK 500    SER C  93     -108.70     55.32                                   
REMARK 500    GLN C 135      -73.03    -45.94                                   
REMARK 500    PHE C 243       68.06   -119.19                                   
REMARK 500    SER D  29       -5.68     72.63                                   
REMARK 500    THR D  30     -159.07   -104.68                                   
REMARK 500    SER D  93     -112.98     55.70                                   
REMARK 500    PHE D 243       71.90   -119.54                                   
REMARK 500    SER E  29       -7.67     75.27                                   
REMARK 500    THR E  30     -158.88   -111.31                                   
REMARK 500    SER E  93     -103.25     50.77                                   
REMARK 500    SER F  29       -4.60     73.72                                   
REMARK 500    THR F  30     -157.46   -105.25                                   
REMARK 500    SER F  93     -107.11     53.42                                   
REMARK 500    THR G  30     -159.56   -103.20                                   
REMARK 500    ASP G  85      -79.93    -81.08                                   
REMARK 500    SER G  93     -110.81     53.95                                   
REMARK 500    PHE G 259      -70.37    -85.24                                   
REMARK 500    SER H  29       -3.56     73.60                                   
REMARK 500    THR H  30     -156.72   -104.21                                   
REMARK 500    SER H  93     -106.73     51.99                                   
REMARK 500    ASP H 197      -94.78    -17.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH H 336        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH H 337        DISTANCE =  6.93 ANGSTROMS                       
DBREF  5EGN A    1   261  UNP    I6YRG4   I6YRG4_9BACT     1    261             
DBREF  5EGN B    1   261  UNP    I6YRG4   I6YRG4_9BACT     1    261             
DBREF  5EGN C    1   261  UNP    I6YRG4   I6YRG4_9BACT     1    261             
DBREF  5EGN D    1   261  UNP    I6YRG4   I6YRG4_9BACT     1    261             
DBREF  5EGN E    1   261  UNP    I6YRG4   I6YRG4_9BACT     1    261             
DBREF  5EGN F    1   261  UNP    I6YRG4   I6YRG4_9BACT     1    261             
DBREF  5EGN G    1   261  UNP    I6YRG4   I6YRG4_9BACT     1    261             
DBREF  5EGN H    1   261  UNP    I6YRG4   I6YRG4_9BACT     1    261             
SEQADV 5EGN VAL A  216  UNP  I6YRG4    ALA   216 ENGINEERED MUTATION            
SEQADV 5EGN ASN A  238  UNP  I6YRG4    LYS   238 ENGINEERED MUTATION            
SEQADV 5EGN ALA A  262  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN ALA A  263  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN LEU A  264  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN GLU A  265  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS A  266  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS A  267  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS A  268  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS A  269  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS A  270  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS A  271  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN VAL B  216  UNP  I6YRG4    ALA   216 ENGINEERED MUTATION            
SEQADV 5EGN ASN B  238  UNP  I6YRG4    LYS   238 ENGINEERED MUTATION            
SEQADV 5EGN ALA B  262  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN ALA B  263  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN LEU B  264  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN GLU B  265  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS B  266  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS B  267  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS B  268  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS B  269  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS B  270  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS B  271  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN VAL C  216  UNP  I6YRG4    ALA   216 ENGINEERED MUTATION            
SEQADV 5EGN ASN C  238  UNP  I6YRG4    LYS   238 ENGINEERED MUTATION            
SEQADV 5EGN ALA C  262  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN ALA C  263  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN LEU C  264  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN GLU C  265  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS C  266  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS C  267  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS C  268  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS C  269  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS C  270  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS C  271  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN VAL D  216  UNP  I6YRG4    ALA   216 ENGINEERED MUTATION            
SEQADV 5EGN ASN D  238  UNP  I6YRG4    LYS   238 ENGINEERED MUTATION            
SEQADV 5EGN ALA D  262  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN ALA D  263  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN LEU D  264  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN GLU D  265  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS D  266  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS D  267  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS D  268  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS D  269  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS D  270  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS D  271  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN VAL E  216  UNP  I6YRG4    ALA   216 ENGINEERED MUTATION            
SEQADV 5EGN ASN E  238  UNP  I6YRG4    LYS   238 ENGINEERED MUTATION            
SEQADV 5EGN ALA E  262  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN ALA E  263  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN LEU E  264  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN GLU E  265  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS E  266  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS E  267  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS E  268  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS E  269  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS E  270  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS E  271  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN VAL F  216  UNP  I6YRG4    ALA   216 ENGINEERED MUTATION            
SEQADV 5EGN ASN F  238  UNP  I6YRG4    LYS   238 ENGINEERED MUTATION            
SEQADV 5EGN ALA F  262  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN ALA F  263  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN LEU F  264  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN GLU F  265  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS F  266  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS F  267  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS F  268  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS F  269  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS F  270  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS F  271  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN VAL G  216  UNP  I6YRG4    ALA   216 ENGINEERED MUTATION            
SEQADV 5EGN ASN G  238  UNP  I6YRG4    LYS   238 ENGINEERED MUTATION            
SEQADV 5EGN ALA G  262  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN ALA G  263  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN LEU G  264  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN GLU G  265  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS G  266  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS G  267  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS G  268  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS G  269  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS G  270  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS G  271  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN VAL H  216  UNP  I6YRG4    ALA   216 ENGINEERED MUTATION            
SEQADV 5EGN ASN H  238  UNP  I6YRG4    LYS   238 ENGINEERED MUTATION            
SEQADV 5EGN ALA H  262  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN ALA H  263  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN LEU H  264  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN GLU H  265  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS H  266  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS H  267  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS H  268  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS H  269  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS H  270  UNP  I6YRG4              EXPRESSION TAG                 
SEQADV 5EGN HIS H  271  UNP  I6YRG4              EXPRESSION TAG                 
SEQRES   1 A  271  MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR          
SEQRES   2 A  271  ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS          
SEQRES   3 A  271  PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR          
SEQRES   4 A  271  PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP          
SEQRES   5 A  271  HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY          
SEQRES   6 A  271  TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL          
SEQRES   7 A  271  LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY          
SEQRES   8 A  271  ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU          
SEQRES   9 A  271  ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER          
SEQRES  10 A  271  SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA          
SEQRES  11 A  271  GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY          
SEQRES  12 A  271  GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG          
SEQRES  13 A  271  GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE          
SEQRES  14 A  271  SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA          
SEQRES  15 A  271  ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE          
SEQRES  16 A  271  LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL          
SEQRES  17 A  271  VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN          
SEQRES  18 A  271  ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU          
SEQRES  19 A  271  ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU          
SEQRES  20 A  271  ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL          
SEQRES  21 A  271  ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B  271  MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR          
SEQRES   2 B  271  ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS          
SEQRES   3 B  271  PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR          
SEQRES   4 B  271  PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP          
SEQRES   5 B  271  HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY          
SEQRES   6 B  271  TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL          
SEQRES   7 B  271  LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY          
SEQRES   8 B  271  ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU          
SEQRES   9 B  271  ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER          
SEQRES  10 B  271  SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA          
SEQRES  11 B  271  GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY          
SEQRES  12 B  271  GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG          
SEQRES  13 B  271  GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE          
SEQRES  14 B  271  SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA          
SEQRES  15 B  271  ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE          
SEQRES  16 B  271  LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL          
SEQRES  17 B  271  VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN          
SEQRES  18 B  271  ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU          
SEQRES  19 B  271  ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU          
SEQRES  20 B  271  ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL          
SEQRES  21 B  271  ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS                  
SEQRES   1 C  271  MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR          
SEQRES   2 C  271  ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS          
SEQRES   3 C  271  PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR          
SEQRES   4 C  271  PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP          
SEQRES   5 C  271  HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY          
SEQRES   6 C  271  TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL          
SEQRES   7 C  271  LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY          
SEQRES   8 C  271  ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU          
SEQRES   9 C  271  ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER          
SEQRES  10 C  271  SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA          
SEQRES  11 C  271  GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY          
SEQRES  12 C  271  GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG          
SEQRES  13 C  271  GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE          
SEQRES  14 C  271  SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA          
SEQRES  15 C  271  ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE          
SEQRES  16 C  271  LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL          
SEQRES  17 C  271  VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN          
SEQRES  18 C  271  ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU          
SEQRES  19 C  271  ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU          
SEQRES  20 C  271  ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL          
SEQRES  21 C  271  ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS                  
SEQRES   1 D  271  MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR          
SEQRES   2 D  271  ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS          
SEQRES   3 D  271  PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR          
SEQRES   4 D  271  PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP          
SEQRES   5 D  271  HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY          
SEQRES   6 D  271  TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL          
SEQRES   7 D  271  LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY          
SEQRES   8 D  271  ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU          
SEQRES   9 D  271  ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER          
SEQRES  10 D  271  SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA          
SEQRES  11 D  271  GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY          
SEQRES  12 D  271  GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG          
SEQRES  13 D  271  GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE          
SEQRES  14 D  271  SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA          
SEQRES  15 D  271  ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE          
SEQRES  16 D  271  LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL          
SEQRES  17 D  271  VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN          
SEQRES  18 D  271  ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU          
SEQRES  19 D  271  ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU          
SEQRES  20 D  271  ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL          
SEQRES  21 D  271  ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS                  
SEQRES   1 E  271  MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR          
SEQRES   2 E  271  ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS          
SEQRES   3 E  271  PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR          
SEQRES   4 E  271  PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP          
SEQRES   5 E  271  HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY          
SEQRES   6 E  271  TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL          
SEQRES   7 E  271  LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY          
SEQRES   8 E  271  ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU          
SEQRES   9 E  271  ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER          
SEQRES  10 E  271  SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA          
SEQRES  11 E  271  GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY          
SEQRES  12 E  271  GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG          
SEQRES  13 E  271  GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE          
SEQRES  14 E  271  SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA          
SEQRES  15 E  271  ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE          
SEQRES  16 E  271  LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL          
SEQRES  17 E  271  VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN          
SEQRES  18 E  271  ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU          
SEQRES  19 E  271  ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU          
SEQRES  20 E  271  ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL          
SEQRES  21 E  271  ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS                  
SEQRES   1 F  271  MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR          
SEQRES   2 F  271  ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS          
SEQRES   3 F  271  PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR          
SEQRES   4 F  271  PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP          
SEQRES   5 F  271  HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY          
SEQRES   6 F  271  TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL          
SEQRES   7 F  271  LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY          
SEQRES   8 F  271  ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU          
SEQRES   9 F  271  ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER          
SEQRES  10 F  271  SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA          
SEQRES  11 F  271  GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY          
SEQRES  12 F  271  GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG          
SEQRES  13 F  271  GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE          
SEQRES  14 F  271  SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA          
SEQRES  15 F  271  ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE          
SEQRES  16 F  271  LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL          
SEQRES  17 F  271  VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN          
SEQRES  18 F  271  ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU          
SEQRES  19 F  271  ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU          
SEQRES  20 F  271  ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL          
SEQRES  21 F  271  ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS                  
SEQRES   1 G  271  MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR          
SEQRES   2 G  271  ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS          
SEQRES   3 G  271  PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR          
SEQRES   4 G  271  PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP          
SEQRES   5 G  271  HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY          
SEQRES   6 G  271  TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL          
SEQRES   7 G  271  LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY          
SEQRES   8 G  271  ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU          
SEQRES   9 G  271  ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER          
SEQRES  10 G  271  SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA          
SEQRES  11 G  271  GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY          
SEQRES  12 G  271  GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG          
SEQRES  13 G  271  GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE          
SEQRES  14 G  271  SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA          
SEQRES  15 G  271  ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE          
SEQRES  16 G  271  LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL          
SEQRES  17 G  271  VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN          
SEQRES  18 G  271  ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU          
SEQRES  19 G  271  ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU          
SEQRES  20 G  271  ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL          
SEQRES  21 G  271  ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS                  
SEQRES   1 H  271  MET PRO HIS VAL GLU ASN ASP GLY VAL LYS ILE TYR TYR          
SEQRES   2 H  271  ASP SER TYR GLY GLU GLY VAL PRO ILE VAL PHE LEU HIS          
SEQRES   3 H  271  PRO PHE SER THR ASN GLY GLY ILE TRP TYR PHE GLN THR          
SEQRES   4 H  271  PHE PRO PHE ALA GLN THR ASN HIS VAL ILE VAL ILE ASP          
SEQRES   5 H  271  HIS ARG GLY HIS GLY ARG SER ASP LYS PRO ALA THR GLY          
SEQRES   6 H  271  TYR SER ILE MET GLU HIS ALA ASP ASP VAL VAL ALA VAL          
SEQRES   7 H  271  LEU ASP ALA LEU LYS VAL ASP ARG ALA VAL PHE VAL GLY          
SEQRES   8 H  271  ASN SER ILE GLY GLY MET ILE ALA MET GLN LEU ASN LEU          
SEQRES   9 H  271  ASP HIS PRO GLN ARG VAL ILE GLY ASN LEU ILE LEU SER          
SEQRES  10 H  271  SER GLY THR GLY LEU GLY GLU GLY MET PRO PRO GLU ALA          
SEQRES  11 H  271  GLY ALA ALA PHE GLN ASN ASP TYR ILE GLY ALA PHE GLY          
SEQRES  12 H  271  GLY LEU LEU GLU GLY ALA VAL SER ALA ARG SER LYS ARG          
SEQRES  13 H  271  GLU ARG PRO GLU ILE LEU ALA VAL MET LYS ALA HIS PHE          
SEQRES  14 H  271  SER VAL PRO SER ASN PHE PRO LYS HIS VAL PHE ASP ALA          
SEQRES  15 H  271  ALA THR ALA ASP PRO ASN GLY VAL PHE ALA TRP ASN ILE          
SEQRES  16 H  271  LYS ASP ARG LEU SER SER ILE GLN ALA PRO THR LEU VAL          
SEQRES  17 H  271  VAL ALA GLY GLU GLU ASP LEU VAL THR THR VAL ALA ASN          
SEQRES  18 H  271  ASN GLN LEU LEU ALA ASP ASN ILE PRO GLY ALA GLU LEU          
SEQRES  19 H  271  ARG VAL ILE ASN ASP VAL GLY HIS PHE TYR GLN LEU GLU          
SEQRES  20 H  271  ARG PRO SER GLU PHE ASN GLU LEU LEU ARG GLY PHE VAL          
SEQRES  21 H  271  ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS                  
FORMUL   9  HOH   *400(H2 O)                                                    
HELIX    1 AA1 ASN A   31  ILE A   34  5                                   4    
HELIX    2 AA2 TRP A   35  PHE A   40  1                                   6    
HELIX    3 AA3 SER A   67  LEU A   82  1                                  16    
HELIX    4 AA4 SER A   93  HIS A  106  1                                  14    
HELIX    5 AA5 GLY A  121  MET A  126  1                                   6    
HELIX    6 AA6 PRO A  127  ASP A  137  1                                  11    
HELIX    7 AA7 ASP A  137  GLU A  147  1                                  11    
HELIX    8 AA8 SER A  151  ARG A  158  1                                   8    
HELIX    9 AA9 PRO A  159  PHE A  169  1                                  11    
HELIX   10 AB1 PRO A  176  ASP A  186  1                                  11    
HELIX   11 AB2 ILE A  195  ILE A  202  5                                   8    
HELIX   12 AB3 THR A  218  ILE A  229  1                                  12    
HELIX   13 AB4 PHE A  243  ARG A  248  1                                   6    
HELIX   14 AB5 ARG A  248  GLY A  258  1                                  11    
HELIX   15 AB6 ASN B   31  ILE B   34  5                                   4    
HELIX   16 AB7 TRP B   35  PHE B   40  1                                   6    
HELIX   17 AB8 SER B   67  LEU B   82  1                                  16    
HELIX   18 AB9 SER B   93  HIS B  106  1                                  14    
HELIX   19 AC1 LEU B  122  MET B  126  5                                   5    
HELIX   20 AC2 GLU B  129  ASP B  137  1                                   9    
HELIX   21 AC3 ASP B  137  GLU B  147  1                                  11    
HELIX   22 AC4 SER B  151  ARG B  158  1                                   8    
HELIX   23 AC5 ARG B  158  VAL B  171  1                                  14    
HELIX   24 AC6 PRO B  176  ASP B  186  1                                  11    
HELIX   25 AC7 ARG B  198  ILE B  202  5                                   5    
HELIX   26 AC8 THR B  218  ILE B  229  1                                  12    
HELIX   27 AC9 PHE B  243  ARG B  248  1                                   6    
HELIX   28 AD1 ARG B  248  VAL B  260  1                                  13    
HELIX   29 AD2 ASN C   31  ILE C   34  5                                   4    
HELIX   30 AD3 TRP C   35  PHE C   40  1                                   6    
HELIX   31 AD4 PRO C   41  THR C   45  5                                   5    
HELIX   32 AD5 SER C   67  LEU C   82  1                                  16    
HELIX   33 AD6 SER C   93  HIS C  106  1                                  14    
HELIX   34 AD7 GLY C  121  MET C  126  5                                   6    
HELIX   35 AD8 PRO C  127  GLU C  129  5                                   3    
HELIX   36 AD9 ALA C  130  ASP C  137  1                                   8    
HELIX   37 AE1 ASP C  137  GLU C  147  1                                  11    
HELIX   38 AE2 SER C  151  ARG C  158  1                                   8    
HELIX   39 AE3 PRO C  159  VAL C  171  1                                  13    
HELIX   40 AE4 PRO C  176  ASP C  186  1                                  11    
HELIX   41 AE5 ILE C  195  ILE C  202  5                                   8    
HELIX   42 AE6 THR C  218  ILE C  229  1                                  12    
HELIX   43 AE7 PHE C  243  ARG C  248  1                                   6    
HELIX   44 AE8 ARG C  248  PHE C  259  1                                  12    
HELIX   45 AE9 ASN D   31  ILE D   34  5                                   4    
HELIX   46 AF1 TRP D   35  ALA D   43  1                                   9    
HELIX   47 AF2 SER D   67  LEU D   82  1                                  16    
HELIX   48 AF3 SER D   93  HIS D  106  1                                  14    
HELIX   49 AF4 LEU D  122  MET D  126  5                                   5    
HELIX   50 AF5 PRO D  127  ASP D  137  1                                  11    
HELIX   51 AF6 ASP D  137  GLU D  147  1                                  11    
HELIX   52 AF7 SER D  151  ARG D  158  1                                   8    
HELIX   53 AF8 PRO D  159  PHE D  169  1                                  11    
HELIX   54 AF9 PRO D  176  ASP D  186  1                                  11    
HELIX   55 AG1 ARG D  198  ILE D  202  5                                   5    
HELIX   56 AG2 THR D  218  ILE D  229  1                                  12    
HELIX   57 AG3 PHE D  243  ARG D  248  1                                   6    
HELIX   58 AG4 ARG D  248  VAL D  260  1                                  13    
HELIX   59 AG5 ASN E   31  ILE E   34  5                                   4    
HELIX   60 AG6 TRP E   35  PHE E   40  1                                   6    
HELIX   61 AG7 SER E   67  LEU E   82  1                                  16    
HELIX   62 AG8 SER E   93  HIS E  106  1                                  14    
HELIX   63 AG9 GLY E  121  MET E  126  1                                   6    
HELIX   64 AH1 PRO E  127  ASP E  137  1                                  11    
HELIX   65 AH2 ASP E  137  GLU E  147  1                                  11    
HELIX   66 AH3 SER E  151  ARG E  158  1                                   8    
HELIX   67 AH4 PRO E  159  VAL E  171  1                                  13    
HELIX   68 AH5 PRO E  176  ASP E  186  1                                  11    
HELIX   69 AH6 ILE E  195  ILE E  202  5                                   8    
HELIX   70 AH7 THR E  218  ILE E  229  1                                  12    
HELIX   71 AH8 PHE E  243  ARG E  248  1                                   6    
HELIX   72 AH9 ARG E  248  GLY E  258  1                                  11    
HELIX   73 AI1 ASN F   31  ILE F   34  5                                   4    
HELIX   74 AI2 TRP F   35  PHE F   40  1                                   6    
HELIX   75 AI3 SER F   67  LEU F   82  1                                  16    
HELIX   76 AI4 SER F   93  HIS F  106  1                                  14    
HELIX   77 AI5 GLY F  121  MET F  126  1                                   6    
HELIX   78 AI6 GLU F  129  ASP F  137  1                                   9    
HELIX   79 AI7 ASP F  137  GLU F  147  1                                  11    
HELIX   80 AI8 SER F  151  ARG F  158  1                                   8    
HELIX   81 AI9 PRO F  159  PHE F  169  1                                  11    
HELIX   82 AJ1 PRO F  176  ASP F  186  1                                  11    
HELIX   83 AJ2 ILE F  195  ILE F  202  5                                   8    
HELIX   84 AJ3 THR F  218  ILE F  229  1                                  12    
HELIX   85 AJ4 PHE F  243  ARG F  248  1                                   6    
HELIX   86 AJ5 ARG F  248  GLY F  258  1                                  11    
HELIX   87 AJ6 ASN G   31  ILE G   34  5                                   4    
HELIX   88 AJ7 TRP G   35  PHE G   40  1                                   6    
HELIX   89 AJ8 PRO G   41  GLN G   44  5                                   4    
HELIX   90 AJ9 SER G   67  LEU G   82  1                                  16    
HELIX   91 AK1 SER G   93  HIS G  106  1                                  14    
HELIX   92 AK2 GLY G  121  MET G  126  5                                   6    
HELIX   93 AK3 PRO G  127  ASP G  137  1                                  11    
HELIX   94 AK4 ASP G  137  GLY G  148  1                                  12    
HELIX   95 AK5 SER G  151  ARG G  158  1                                   8    
HELIX   96 AK6 PRO G  159  VAL G  171  1                                  13    
HELIX   97 AK7 PRO G  176  ASP G  186  1                                  11    
HELIX   98 AK8 ILE G  195  SER G  200  1                                   6    
HELIX   99 AK9 THR G  218  ILE G  229  1                                  12    
HELIX  100 AL1 PHE G  243  ARG G  248  1                                   6    
HELIX  101 AL2 ARG G  248  GLY G  258  1                                  11    
HELIX  102 AL3 ASN H   31  ILE H   34  5                                   4    
HELIX  103 AL4 TRP H   35  PHE H   40  1                                   6    
HELIX  104 AL5 SER H   67  LEU H   82  1                                  16    
HELIX  105 AL6 SER H   93  HIS H  106  1                                  14    
HELIX  106 AL7 GLY H  121  MET H  126  1                                   6    
HELIX  107 AL8 PRO H  127  ASP H  137  1                                  11    
HELIX  108 AL9 ASP H  137  GLY H  148  1                                  12    
HELIX  109 AM1 SER H  151  ARG H  158  1                                   8    
HELIX  110 AM2 ARG H  158  VAL H  171  1                                  14    
HELIX  111 AM3 PRO H  176  ASP H  186  1                                  11    
HELIX  112 AM4 ILE H  195  SER H  200  1                                   6    
HELIX  113 AM5 THR H  218  ASN H  228  1                                  11    
HELIX  114 AM6 PHE H  243  ARG H  248  1                                   6    
HELIX  115 AM7 ARG H  248  GLY H  258  1                                  11    
SHEET    1 AA1 8 HIS A   3  ASN A   6  0                                        
SHEET    2 AA1 8 VAL A   9  TYR A  16 -1  O  ILE A  11   N  VAL A   4           
SHEET    3 AA1 8 HIS A  47  ILE A  51 -1  O  VAL A  50   N  ASP A  14           
SHEET    4 AA1 8 PRO A  21  LEU A  25  1  N  PHE A  24   O  ILE A  49           
SHEET    5 AA1 8 ALA A  87  ASN A  92  1  O  VAL A  88   N  VAL A  23           
SHEET    6 AA1 8 VAL A 110  LEU A 116  1  O  LEU A 116   N  GLY A  91           
SHEET    7 AA1 8 THR A 206  GLY A 211  1  O  VAL A 209   N  ILE A 115           
SHEET    8 AA1 8 GLU A 233  ILE A 237  1  O  ILE A 237   N  ALA A 210           
SHEET    1 AA2 8 HIS B   3  ASN B   6  0                                        
SHEET    2 AA2 8 VAL B   9  TYR B  16 -1  O  ILE B  11   N  VAL B   4           
SHEET    3 AA2 8 HIS B  47  ILE B  51 -1  O  VAL B  48   N  TYR B  16           
SHEET    4 AA2 8 PRO B  21  LEU B  25  1  N  ILE B  22   O  ILE B  49           
SHEET    5 AA2 8 ALA B  87  ASN B  92  1  O  VAL B  90   N  LEU B  25           
SHEET    6 AA2 8 VAL B 110  LEU B 116  1  O  LEU B 114   N  PHE B  89           
SHEET    7 AA2 8 THR B 206  GLY B 211  1  O  VAL B 209   N  ILE B 115           
SHEET    8 AA2 8 GLU B 233  ILE B 237  1  O  ILE B 237   N  ALA B 210           
SHEET    1 AA3 8 HIS C   3  ASN C   6  0                                        
SHEET    2 AA3 8 VAL C   9  TYR C  16 -1  O  ILE C  11   N  VAL C   4           
SHEET    3 AA3 8 HIS C  47  ILE C  51 -1  O  VAL C  48   N  TYR C  16           
SHEET    4 AA3 8 PRO C  21  LEU C  25  1  N  ILE C  22   O  ILE C  49           
SHEET    5 AA3 8 ALA C  87  ASN C  92  1  O  VAL C  88   N  VAL C  23           
SHEET    6 AA3 8 VAL C 110  LEU C 116  1  O  LEU C 114   N  PHE C  89           
SHEET    7 AA3 8 THR C 206  GLY C 211  1  O  LEU C 207   N  ASN C 113           
SHEET    8 AA3 8 GLU C 233  ILE C 237  1  O  ILE C 237   N  ALA C 210           
SHEET    1 AA4 8 HIS D   3  ASN D   6  0                                        
SHEET    2 AA4 8 VAL D   9  TYR D  16 -1  O  ILE D  11   N  VAL D   4           
SHEET    3 AA4 8 ASN D  46  ILE D  51 -1  O  VAL D  50   N  ASP D  14           
SHEET    4 AA4 8 VAL D  20  LEU D  25  1  N  ILE D  22   O  ILE D  49           
SHEET    5 AA4 8 ALA D  87  ASN D  92  1  O  VAL D  90   N  LEU D  25           
SHEET    6 AA4 8 VAL D 110  LEU D 116  1  O  LEU D 114   N  PHE D  89           
SHEET    7 AA4 8 THR D 206  GLY D 211  1  O  VAL D 209   N  ILE D 115           
SHEET    8 AA4 8 GLU D 233  ILE D 237  1  O  ILE D 237   N  ALA D 210           
SHEET    1 AA5 8 HIS E   3  ASN E   6  0                                        
SHEET    2 AA5 8 VAL E   9  TYR E  16 -1  O  ILE E  11   N  VAL E   4           
SHEET    3 AA5 8 HIS E  47  ILE E  51 -1  O  VAL E  48   N  TYR E  16           
SHEET    4 AA5 8 PRO E  21  LEU E  25  1  N  ILE E  22   O  ILE E  49           
SHEET    5 AA5 8 ALA E  87  ASN E  92  1  O  VAL E  90   N  VAL E  23           
SHEET    6 AA5 8 VAL E 110  LEU E 116  1  O  LEU E 116   N  GLY E  91           
SHEET    7 AA5 8 THR E 206  GLY E 211  1  O  LEU E 207   N  ASN E 113           
SHEET    8 AA5 8 GLU E 233  ILE E 237  1  O  GLU E 233   N  VAL E 208           
SHEET    1 AA6 8 HIS F   3  ASN F   6  0                                        
SHEET    2 AA6 8 VAL F   9  TYR F  16 -1  O  ILE F  11   N  VAL F   4           
SHEET    3 AA6 8 HIS F  47  ILE F  51 -1  O  VAL F  48   N  TYR F  16           
SHEET    4 AA6 8 PRO F  21  LEU F  25  1  N  ILE F  22   O  ILE F  49           
SHEET    5 AA6 8 ALA F  87  ASN F  92  1  O  VAL F  88   N  VAL F  23           
SHEET    6 AA6 8 VAL F 110  LEU F 116  1  O  LEU F 114   N  PHE F  89           
SHEET    7 AA6 8 THR F 206  GLY F 211  1  O  LEU F 207   N  ASN F 113           
SHEET    8 AA6 8 GLU F 233  ILE F 237  1  O  ILE F 237   N  ALA F 210           
SHEET    1 AA7 8 HIS G   3  ASN G   6  0                                        
SHEET    2 AA7 8 VAL G   9  TYR G  16 -1  O  VAL G   9   N  ASN G   6           
SHEET    3 AA7 8 ASN G  46  ILE G  51 -1  O  VAL G  50   N  ASP G  14           
SHEET    4 AA7 8 VAL G  20  LEU G  25  1  N  ILE G  22   O  ILE G  49           
SHEET    5 AA7 8 ALA G  87  ASN G  92  1  O  VAL G  90   N  LEU G  25           
SHEET    6 AA7 8 VAL G 110  LEU G 116  1  O  LEU G 116   N  GLY G  91           
SHEET    7 AA7 8 THR G 206  GLY G 211  1  O  VAL G 209   N  ILE G 115           
SHEET    8 AA7 8 GLU G 233  ILE G 237  1  O  GLU G 233   N  VAL G 208           
SHEET    1 AA8 8 HIS H   3  ASN H   6  0                                        
SHEET    2 AA8 8 VAL H   9  TYR H  16 -1  O  ILE H  11   N  VAL H   4           
SHEET    3 AA8 8 HIS H  47  ILE H  51 -1  O  VAL H  50   N  ASP H  14           
SHEET    4 AA8 8 PRO H  21  LEU H  25  1  N  PHE H  24   O  ILE H  49           
SHEET    5 AA8 8 ALA H  87  ASN H  92  1  O  VAL H  88   N  PRO H  21           
SHEET    6 AA8 8 VAL H 110  LEU H 116  1  O  LEU H 116   N  GLY H  91           
SHEET    7 AA8 8 THR H 206  GLY H 211  1  O  VAL H 209   N  ILE H 115           
SHEET    8 AA8 8 GLU H 233  ILE H 237  1  O  ILE H 237   N  ALA H 210           
CISPEP   1 ASN B  238    ASP B  239          0       -21.54                     
CISPEP   2 GLU C   18    GLY C   19          0        -4.91                     
CISPEP   3 THR D   64    GLY D   65          0        -4.22                     
CISPEP   4 THR E   64    GLY E   65          0        -7.43                     
CISPEP   5 THR F   64    GLY F   65          0        -6.51                     
CISPEP   6 THR G   64    GLY G   65          0        -6.92                     
CISPEP   7 THR H   64    GLY H   65          0        -4.19                     
CRYST1  109.806   78.545  116.472  90.00  99.37  90.00 P 1 21 1     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      0.009107  0.000000  0.001503        0.00000                         
SCALE2      0.000000  0.012732  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008702        0.00000                         
TER    1984      ALA A 261                                                      
TER    3976      ALA B 261                                                      
TER    5963      VAL C 260                                                      
TER    7944      VAL D 260                                                      
TER    9925      VAL E 260                                                      
TER   11905      ALA F 261                                                      
TER   13856      VAL G 260                                                      
TER   15792      PHE H 259                                                      
MASTER      471    0    0  115   64    0    0    616184    8    0  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
AcePerl Lincoln Stein Home Page
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