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LongText Report for: 3D2C-pdb

Name Class
3D2C-pdb
HEADER    HYDROLASE                               08-MAY-08   3D2C              
TITLE     STRUCTURE OF 4D3, A THERMOSTABLE MUTANT OF BACILLUS                   
TITLE    2 SUBTILIS LIPASE OBTAINED THROUGH DIRECTED EVOLUTION                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE;                                                    
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 SYNONYM: TRIACYLGLYCEROL LIPASE;                                     
COMPND   5 EC: 3.1.1.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 GENE: LIPA, LIP, BSU02700;                                           
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET21B                                    
KEYWDS    LIPASE, ALPHA/BETA HYDROLASE, STABILITY, DIRECTED EVOLUTION,          
KEYWDS   2 HYDROLASE, LIPID DEGRADATION, SECRETED                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.SANKARANARAYANAN,M.Z.KAMAL                                          
REVDAT   1   03-JUN-08 3D2C    0                                                
JRNL        AUTH   S.AHMAD,M.Z.KAMAL,R.SANKARANARAYANAN,N.M.RAO                 
JRNL        TITL   THERMOSTABLE BACILLUS SUBTILIS LIPASES: IN VITRO             
JRNL        TITL 2 EVOLUTION AND STRUCTURAL INSIGHT                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.18 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.18                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 133186                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6662                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16380                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 1130                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.00600                                              
REMARK   3    B22 (A**2) : -2.08500                                             
REMARK   3    B33 (A**2) : 1.07900                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.005 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.210 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 53.06                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3D2C COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.                               
REMARK 100 THE RCSB ID CODE IS RCSB047503.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 133252                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.180                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48900                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M SUCCINIC ACID, 0.1M HEPES, 1%(W/      
REMARK 280  V) POLYETHELENE GLYCOL MONOMETHYL ETHER 2000, PH 7.0, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,1/2+Z                                             
REMARK 290       3555   -X,Y,1/2-Z                                              
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   1/2+X,1/2+Y,Z                                           
REMARK 290       6555   1/2-X,1/2-Y,1/2+Z                                       
REMARK 290       7555   1/2-X,1/2+Y,1/2-Z                                       
REMARK 290       8555   1/2+X,1/2-Y,-Z                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       98.95100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       98.95100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       66.14250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       99.02100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       66.14250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       99.02100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       98.95100            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       66.14250            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       99.02100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       98.95100            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       66.14250            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       99.02100            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13               
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
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: 8                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 9                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I                                     
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: 10                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J                                     
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: 11                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K                                     
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: 12                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L                                     
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: 13                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 24MERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 24MERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 33680 ANGSTROM**2                         
REMARK 350 TOTAL SURFACE AREA FOR THE COMPLEX: 144270 ANGSTROM**2               
REMARK 350 GAIN IN SOLVENT FREE ENERGY: -268 KCAL/MOL                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350 J, K, L                                                              
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -98.95100            
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                 
REMARK 465                                                                      
REMARK 465   M RES C  SSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     ALA E     1                                                      
REMARK 465     GLU E     2                                                      
REMARK 465     ALA F     1                                                      
REMARK 465     GLU F     2                                                      
REMARK 465     ALA G     1                                                      
REMARK 465     GLU G     2                                                      
REMARK 465     ALA H     1                                                      
REMARK 465     GLU H     2                                                      
REMARK 465     ALA I     1                                                      
REMARK 465     GLU I     2                                                      
REMARK 465     ALA J     1                                                      
REMARK 465     GLU J     2                                                      
REMARK 465     ALA K     1                                                      
REMARK 465     GLU K     2                                                      
REMARK 465     ALA L     1                                                      
REMARK 465     GLU L     2                                                      
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    LYS A  44        3.06    -69.77                                   
REMARK 500    SER A  77     -119.34     46.48                                   
REMARK 500    LEU A  90     -149.92   -112.43                                   
REMARK 500    ALA A  97      -63.00   -106.02                                   
REMARK 500    ASN A 179       62.84   -175.13                                   
REMARK 500    THR A 180       28.87    -69.74                                   
REMARK 500    SER B  77     -118.83     43.97                                   
REMARK 500    LEU B  90     -147.25   -137.96                                   
REMARK 500    ARG B 107        5.28    -65.59                                   
REMARK 500    ASN B 179       85.69   -165.77                                   
REMARK 500    THR B 180       37.78    -87.06                                   
REMARK 500    SER C  77     -120.61     50.60                                   
REMARK 500    LEU C  90     -139.09   -116.91                                   
REMARK 500    ASN C 179       88.90   -162.63                                   
REMARK 500    THR C 180       35.92    -93.32                                   
REMARK 500    SER D  77     -123.27     52.28                                   
REMARK 500    LEU D  90     -148.31   -110.78                                   
REMARK 500    ASN D 179       88.57   -155.75                                   
REMARK 500    THR D 180       39.38    -85.89                                   
REMARK 500    SER E  77     -120.76     52.01                                   
REMARK 500    LEU E  90     -150.25    -94.92                                   
REMARK 500    ALA E 105       57.82    -92.22                                   
REMARK 500    ASN E 179       87.16   -153.32                                   
REMARK 500    SER F  77     -121.18     48.24                                   
REMARK 500    LEU F  90     -149.38   -115.24                                   
REMARK 500    ALA F 105       53.09    -96.77                                   
REMARK 500    ASN F 179      104.68   -178.16                                   
REMARK 500    SER G  77     -121.36     47.72                                   
REMARK 500    LEU G  90     -139.17   -101.22                                   
REMARK 500    ALA G 105       48.12    -88.74                                   
REMARK 500    THR G 109      -55.13   -128.24                                   
REMARK 500    ASN G 179       73.85   -168.13                                   
REMARK 500    THR G 180       28.83    -76.79                                   
REMARK 500    SER H  77     -117.67     52.59                                   
REMARK 500    LEU H  90     -149.54    -99.79                                   
REMARK 500    ASN H 179       89.02   -161.33                                   
REMARK 500    SER I  77     -117.94     50.53                                   
REMARK 500    LEU I  90     -133.98    -98.15                                   
REMARK 500    ALA I 105       49.79    -93.80                                   
REMARK 500    THR I 109      -52.14   -125.29                                   
REMARK 500    GLN I 121      125.19   -172.25                                   
REMARK 500    ASN I 179       88.58   -160.65                                   
REMARK 500    SER J  77     -119.91     44.51                                   
REMARK 500    LEU J  90     -145.24   -113.98                                   
REMARK 500    ALA J  97      -63.08   -103.44                                   
REMARK 500    ALA J 105       51.32    -90.48                                   
REMARK 500    ARG J 107        0.47    -66.03                                   
REMARK 500    GLN J 178      148.80    175.56                                   
REMARK 500    ASN J 179       81.38   -156.24                                   
REMARK 500    SER K  77     -119.74     44.61                                   
REMARK 500    LEU K  90     -145.70    -92.30                                   
REMARK 500    ALA K 105       52.09    -92.00                                   
REMARK 500    ASN K 179       95.96   -172.92                                   
REMARK 500    SER L  77     -122.51     49.44                                   
REMARK 500    LEU L  90     -141.33   -106.26                                   
REMARK 500    ASN L 179       87.30   -166.79                                   
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 L 274        DISTANCE =  7.46 ANGSTROMS                       
REMARK 525    HOH L 277        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH A 219        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH B 222        DISTANCE =  6.45 ANGSTROMS                       
REMARK 525    HOH G 227        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH K 283        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH A 244        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH K 291        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH F 252        DISTANCE =  5.57 ANGSTROMS                       
REMARK 525    HOH L 344        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH A 253        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH B 256        DISTANCE =  7.17 ANGSTROMS                       
REMARK 525    HOH I 260        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH H 262        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH K 310        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH G 266        DISTANCE =  5.57 ANGSTROMS                       
REMARK 525    HOH D 269        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH J 329        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH G 275        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH L 373        DISTANCE =  5.82 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1T2N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1T4M   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3D2A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3D2B   RELATED DB: PDB                                   
DBREF  3D2C A    1   181  UNP    P37957   LIP_BACSU       32    212             
DBREF  3D2C B    1   181  UNP    P37957   LIP_BACSU       32    212             
DBREF  3D2C C    1   181  UNP    P37957   LIP_BACSU       32    212             
DBREF  3D2C D    1   181  UNP    P37957   LIP_BACSU       32    212             
DBREF  3D2C E    1   181  UNP    P37957   LIP_BACSU       32    212             
DBREF  3D2C F    1   181  UNP    P37957   LIP_BACSU       32    212             
DBREF  3D2C G    1   181  UNP    P37957   LIP_BACSU       32    212             
DBREF  3D2C H    1   181  UNP    P37957   LIP_BACSU       32    212             
DBREF  3D2C I    1   181  UNP    P37957   LIP_BACSU       32    212             
DBREF  3D2C J    1   181  UNP    P37957   LIP_BACSU       32    212             
DBREF  3D2C K    1   181  UNP    P37957   LIP_BACSU       32    212             
DBREF  3D2C L    1   181  UNP    P37957   LIP_BACSU       32    212             
SEQADV 3D2C SER A   15  UNP  P37957    ALA    46 ENGINEERED                     
SEQADV 3D2C SER A   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2C GLU A   20  UNP  P37957    ALA    51 ENGINEERED                     
SEQADV 3D2C TYR A   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2C ASP A  111  UNP  P37957    GLY   142 ENGINEERED                     
SEQADV 3D2C PRO A  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2C ASP A  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2C MET A  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2C TYR A  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQADV 3D2C SER B   15  UNP  P37957    ALA    46 ENGINEERED                     
SEQADV 3D2C SER B   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2C GLU B   20  UNP  P37957    ALA    51 ENGINEERED                     
SEQADV 3D2C TYR B   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2C ASP B  111  UNP  P37957    GLY   142 ENGINEERED                     
SEQADV 3D2C PRO B  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2C ASP B  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2C MET B  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2C TYR B  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQADV 3D2C SER C   15  UNP  P37957    ALA    46 ENGINEERED                     
SEQADV 3D2C SER C   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2C GLU C   20  UNP  P37957    ALA    51 ENGINEERED                     
SEQADV 3D2C TYR C   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2C ASP C  111  UNP  P37957    GLY   142 ENGINEERED                     
SEQADV 3D2C PRO C  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2C ASP C  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2C MET C  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2C TYR C  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQADV 3D2C SER D   15  UNP  P37957    ALA    46 ENGINEERED                     
SEQADV 3D2C SER D   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2C GLU D   20  UNP  P37957    ALA    51 ENGINEERED                     
SEQADV 3D2C TYR D   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2C ASP D  111  UNP  P37957    GLY   142 ENGINEERED                     
SEQADV 3D2C PRO D  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2C ASP D  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2C MET D  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2C TYR D  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQADV 3D2C SER E   15  UNP  P37957    ALA    46 ENGINEERED                     
SEQADV 3D2C SER E   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2C GLU E   20  UNP  P37957    ALA    51 ENGINEERED                     
SEQADV 3D2C TYR E   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2C ASP E  111  UNP  P37957    GLY   142 ENGINEERED                     
SEQADV 3D2C PRO E  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2C ASP E  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2C MET E  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2C TYR E  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQADV 3D2C SER F   15  UNP  P37957    ALA    46 ENGINEERED                     
SEQADV 3D2C SER F   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2C GLU F   20  UNP  P37957    ALA    51 ENGINEERED                     
SEQADV 3D2C TYR F   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2C ASP F  111  UNP  P37957    GLY   142 ENGINEERED                     
SEQADV 3D2C PRO F  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2C ASP F  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2C MET F  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2C TYR F  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQADV 3D2C SER G   15  UNP  P37957    ALA    46 ENGINEERED                     
SEQADV 3D2C SER G   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2C GLU G   20  UNP  P37957    ALA    51 ENGINEERED                     
SEQADV 3D2C TYR G   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2C ASP G  111  UNP  P37957    GLY   142 ENGINEERED                     
SEQADV 3D2C PRO G  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2C ASP G  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2C MET G  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2C TYR G  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQADV 3D2C SER H   15  UNP  P37957    ALA    46 ENGINEERED                     
SEQADV 3D2C SER H   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2C GLU H   20  UNP  P37957    ALA    51 ENGINEERED                     
SEQADV 3D2C TYR H   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2C ASP H  111  UNP  P37957    GLY   142 ENGINEERED                     
SEQADV 3D2C PRO H  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2C ASP H  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2C MET H  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2C TYR H  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQADV 3D2C SER I   15  UNP  P37957    ALA    46 ENGINEERED                     
SEQADV 3D2C SER I   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2C GLU I   20  UNP  P37957    ALA    51 ENGINEERED                     
SEQADV 3D2C TYR I   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2C ASP I  111  UNP  P37957    GLY   142 ENGINEERED                     
SEQADV 3D2C PRO I  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2C ASP I  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2C MET I  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2C TYR I  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQADV 3D2C SER J   15  UNP  P37957    ALA    46 ENGINEERED                     
SEQADV 3D2C SER J   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2C GLU J   20  UNP  P37957    ALA    51 ENGINEERED                     
SEQADV 3D2C TYR J   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2C ASP J  111  UNP  P37957    GLY   142 ENGINEERED                     
SEQADV 3D2C PRO J  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2C ASP J  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2C MET J  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2C TYR J  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQADV 3D2C SER K   15  UNP  P37957    ALA    46 ENGINEERED                     
SEQADV 3D2C SER K   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2C GLU K   20  UNP  P37957    ALA    51 ENGINEERED                     
SEQADV 3D2C TYR K   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2C ASP K  111  UNP  P37957    GLY   142 ENGINEERED                     
SEQADV 3D2C PRO K  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2C ASP K  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2C MET K  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2C TYR K  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQADV 3D2C SER L   15  UNP  P37957    ALA    46 ENGINEERED                     
SEQADV 3D2C SER L   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2C GLU L   20  UNP  P37957    ALA    51 ENGINEERED                     
SEQADV 3D2C TYR L   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2C ASP L  111  UNP  P37957    GLY   142 ENGINEERED                     
SEQADV 3D2C PRO L  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2C ASP L  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2C MET L  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2C TYR L  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQRES   1 A  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 A  181  GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU          
SEQRES   3 A  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 A  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 A  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 A  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 A  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 A  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 A  181  ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR          
SEQRES  10 A  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 A  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 A  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 A  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 A  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
SEQRES   1 B  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 B  181  GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU          
SEQRES   3 B  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 B  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 B  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 B  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 B  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 B  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 B  181  ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR          
SEQRES  10 B  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 B  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 B  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 B  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 B  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
SEQRES   1 C  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 C  181  GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU          
SEQRES   3 C  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 C  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 C  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 C  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 C  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 C  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 C  181  ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR          
SEQRES  10 C  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 C  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 C  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 C  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 C  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
SEQRES   1 D  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 D  181  GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU          
SEQRES   3 D  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 D  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 D  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 D  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 D  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 D  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 D  181  ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR          
SEQRES  10 D  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 D  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 D  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 D  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 D  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
SEQRES   1 E  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 E  181  GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU          
SEQRES   3 E  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 E  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 E  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 E  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 E  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 E  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 E  181  ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR          
SEQRES  10 E  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 E  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 E  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 E  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 E  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
SEQRES   1 F  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 F  181  GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU          
SEQRES   3 F  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 F  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 F  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 F  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 F  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 F  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 F  181  ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR          
SEQRES  10 F  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 F  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 F  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 F  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 F  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
SEQRES   1 G  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 G  181  GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU          
SEQRES   3 G  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 G  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 G  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 G  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 G  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 G  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 G  181  ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR          
SEQRES  10 G  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 G  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 G  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 G  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 G  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
SEQRES   1 H  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 H  181  GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU          
SEQRES   3 H  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 H  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 H  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 H  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 H  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 H  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 H  181  ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR          
SEQRES  10 H  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 H  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 H  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 H  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 H  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
SEQRES   1 I  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 I  181  GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU          
SEQRES   3 I  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 I  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 I  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 I  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 I  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 I  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 I  181  ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR          
SEQRES  10 I  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 I  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 I  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 I  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 I  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
SEQRES   1 J  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 J  181  GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU          
SEQRES   3 J  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 J  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 J  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 J  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 J  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 J  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 J  181  ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR          
SEQRES  10 J  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 J  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 J  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 J  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 J  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
SEQRES   1 K  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 K  181  GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU          
SEQRES   3 K  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 K  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 K  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 K  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 K  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 K  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 K  181  ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR          
SEQRES  10 K  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 K  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 K  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 K  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 K  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
SEQRES   1 L  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 L  181  GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU          
SEQRES   3 L  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 L  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 L  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 L  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 L  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 L  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 L  181  ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR          
SEQRES  10 L  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 L  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 L  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 L  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 L  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
FORMUL  13  HOH   *1130(H2 O)                                                   
HELIX    1   1 SER A   15  ASN A   18  5                                   4    
HELIX    2   2 PHE A   19  GLN A   29  1                                  11    
HELIX    3   3 SER A   32  ASP A   34  5                                   3    
HELIX    4   4 THR A   47  GLY A   67  1                                  21    
HELIX    5   5 MET A   78  LEU A   90  1                                  13    
HELIX    6   6 ASP A   91  ASN A   94  5                                   4    
HELIX    7   7 ALA A  105  THR A  109  5                                   5    
HELIX    8   8 MET A  137  ARG A  142  1                                   6    
HELIX    9   9 HIS A  156  TYR A  161  5                                   6    
HELIX   10  10 SER A  162  ASN A  174  1                                  13    
HELIX   11  11 SER B   15  ASN B   18  5                                   4    
HELIX   12  12 PHE B   19  GLN B   29  1                                  11    
HELIX   13  13 SER B   32  ASP B   34  5                                   3    
HELIX   14  14 THR B   47  GLY B   67  1                                  21    
HELIX   15  15 MET B   78  LEU B   90  1                                  13    
HELIX   16  16 ASP B   91  ASN B   94  5                                   4    
HELIX   17  17 ALA B  105  THR B  109  5                                   5    
HELIX   18  18 MET B  137  ARG B  142  1                                   6    
HELIX   19  19 MET B  157  TYR B  161  5                                   5    
HELIX   20  20 SER B  162  ASN B  174  1                                  13    
HELIX   21  21 SER C   15  ASN C   18  5                                   4    
HELIX   22  22 PHE C   19  GLN C   29  1                                  11    
HELIX   23  23 SER C   32  ASP C   34  5                                   3    
HELIX   24  24 THR C   47  GLY C   67  1                                  21    
HELIX   25  25 MET C   78  LEU C   90  1                                  13    
HELIX   26  26 ASP C   91  ASN C   94  5                                   4    
HELIX   27  27 ALA C  105  THR C  109  5                                   5    
HELIX   28  28 MET C  137  ARG C  142  1                                   6    
HELIX   29  29 MET C  157  TYR C  161  5                                   5    
HELIX   30  30 SER C  162  ASN C  174  1                                  13    
HELIX   31  31 SER D   15  ASN D   18  5                                   4    
HELIX   32  32 PHE D   19  GLN D   29  1                                  11    
HELIX   33  33 SER D   32  ASP D   34  5                                   3    
HELIX   34  34 THR D   47  GLY D   67  1                                  21    
HELIX   35  35 MET D   78  LEU D   90  1                                  13    
HELIX   36  36 ASP D   91  ASN D   94  5                                   4    
HELIX   37  37 ALA D  105  THR D  109  5                                   5    
HELIX   38  38 MET D  137  ARG D  142  1                                   6    
HELIX   39  39 MET D  157  TYR D  161  5                                   5    
HELIX   40  40 SER D  162  ASN D  174  1                                  13    
HELIX   41  41 SER E   15  ASN E   18  5                                   4    
HELIX   42  42 PHE E   19  GLN E   29  1                                  11    
HELIX   43  43 SER E   32  ASP E   34  5                                   3    
HELIX   44  44 THR E   47  GLY E   67  1                                  21    
HELIX   45  45 MET E   78  TYR E   89  1                                  12    
HELIX   46  46 LEU E   90  ASN E   94  5                                   5    
HELIX   47  47 ALA E  105  THR E  109  5                                   5    
HELIX   48  48 MET E  137  ARG E  142  1                                   6    
HELIX   49  49 MET E  157  TYR E  161  5                                   5    
HELIX   50  50 SER E  162  ASN E  174  1                                  13    
HELIX   51  51 SER F   15  ASN F   18  5                                   4    
HELIX   52  52 PHE F   19  GLN F   29  1                                  11    
HELIX   53  53 SER F   32  ASP F   34  5                                   3    
HELIX   54  54 THR F   47  GLY F   67  1                                  21    
HELIX   55  55 MET F   78  LEU F   90  1                                  13    
HELIX   56  56 ALA F  105  THR F  109  5                                   5    
HELIX   57  57 MET F  137  ARG F  142  1                                   6    
HELIX   58  58 HIS F  156  TYR F  161  5                                   6    
HELIX   59  59 SER F  162  ASN F  174  1                                  13    
HELIX   60  60 SER G   15  ASN G   18  5                                   4    
HELIX   61  61 PHE G   19  GLN G   29  1                                  11    
HELIX   62  62 SER G   32  ASP G   34  5                                   3    
HELIX   63  63 THR G   47  GLY G   67  1                                  21    
HELIX   64  64 MET G   78  LEU G   90  1                                  13    
HELIX   65  65 ALA G  105  THR G  109  5                                   5    
HELIX   66  66 MET G  137  ARG G  142  1                                   6    
HELIX   67  67 HIS G  156  TYR G  161  5                                   6    
HELIX   68  68 SER G  162  ASN G  174  1                                  13    
HELIX   69  69 SER H   15  ASN H   18  5                                   4    
HELIX   70  70 PHE H   19  GLN H   29  1                                  11    
HELIX   71  71 SER H   32  ASP H   34  5                                   3    
HELIX   72  72 THR H   47  GLY H   67  1                                  21    
HELIX   73  73 MET H   78  LEU H   90  1                                  13    
HELIX   74  74 ASP H   91  ASN H   94  5                                   4    
HELIX   75  75 ALA H  105  THR H  109  5                                   5    
HELIX   76  76 MET H  137  ARG H  142  1                                   6    
HELIX   77  77 MET H  157  TYR H  161  5                                   5    
HELIX   78  78 SER H  162  ASN H  174  1                                  13    
HELIX   79  79 SER I   15  ASN I   18  5                                   4    
HELIX   80  80 PHE I   19  GLN I   29  1                                  11    
HELIX   81  81 SER I   32  ASP I   34  5                                   3    
HELIX   82  82 THR I   47  GLY I   67  1                                  21    
HELIX   83  83 MET I   78  LEU I   90  1                                  13    
HELIX   84  84 ASP I   91  ASN I   94  5                                   4    
HELIX   85  85 ALA I  105  THR I  109  5                                   5    
HELIX   86  86 MET I  137  ARG I  142  1                                   6    
HELIX   87  87 HIS I  156  TYR I  161  5                                   6    
HELIX   88  88 SER I  162  ASN I  174  1                                  13    
HELIX   89  89 SER J   15  ASN J   18  5                                   4    
HELIX   90  90 PHE J   19  GLN J   29  1                                  11    
HELIX   91  91 SER J   32  ASP J   34  5                                   3    
HELIX   92  92 THR J   47  GLY J   67  1                                  21    
HELIX   93  93 MET J   78  LEU J   90  1                                  13    
HELIX   94  94 ASP J   91  ASN J   94  5                                   4    
HELIX   95  95 ALA J  105  THR J  109  5                                   5    
HELIX   96  96 MET J  137  ARG J  142  1                                   6    
HELIX   97  97 MET J  157  TYR J  161  5                                   5    
HELIX   98  98 SER J  162  ASN J  174  1                                  13    
HELIX   99  99 SER K   15  ASN K   18  5                                   4    
HELIX  100 100 PHE K   19  GLN K   29  1                                  11    
HELIX  101 101 SER K   32  ASP K   34  5                                   3    
HELIX  102 102 THR K   47  GLY K   67  1                                  21    
HELIX  103 103 MET K   78  TYR K   89  1                                  12    
HELIX  104 104 ASP K   91  ASN K   94  5                                   4    
HELIX  105 105 ALA K  105  THR K  109  5                                   5    
HELIX  106 106 MET K  137  ARG K  142  1                                   6    
HELIX  107 107 HIS K  156  TYR K  161  5                                   6    
HELIX  108 108 SER K  162  ASN K  174  1                                  13    
HELIX  109 109 SER L   15  ASN L   18  5                                   4    
HELIX  110 110 PHE L   19  GLN L   29  1                                  11    
HELIX  111 111 SER L   32  ASP L   34  5                                   3    
HELIX  112 112 THR L   47  GLY L   67  1                                  21    
HELIX  113 113 MET L   78  LEU L   90  1                                  13    
HELIX  114 114 ASP L   91  ASN L   94  5                                   4    
HELIX  115 115 ALA L  105  THR L  109  5                                   5    
HELIX  116 116 MET L  137  ARG L  142  1                                   6    
HELIX  117 117 HIS L  156  TYR L  161  5                                   6    
HELIX  118 118 SER L  162  ASN L  174  1                                  13    
SHEET    1   A 6 LEU A  36  ALA A  38  0                                        
SHEET    2   A 6 VAL A   6  VAL A   9  1  N  VAL A   6   O  TYR A  37           
SHEET    3   A 6 VAL A  71  HIS A  76  1  O  ASP A  72   N  VAL A   7           
SHEET    4   A 6 VAL A  96  LEU A 102  1  O  VAL A 100   N  ILE A  73           
SHEET    5   A 6 LEU A 124  SER A 130  1  O  ILE A 128   N  THR A 101           
SHEET    6   A 6 ARG A 147  ILE A 151  1  O  ARG A 147   N  SER A 127           
SHEET    1   B 6 LEU B  36  ALA B  38  0                                        
SHEET    2   B 6 VAL B   6  VAL B   9  1  N  VAL B   6   O  TYR B  37           
SHEET    3   B 6 VAL B  71  HIS B  76  1  O  ASP B  72   N  VAL B   7           
SHEET    4   B 6 VAL B  96  LEU B 102  1  O  LEU B 102   N  ALA B  75           
SHEET    5   B 6 LEU B 124  SER B 130  1  O  ILE B 128   N  THR B 101           
SHEET    6   B 6 ARG B 147  ILE B 151  1  O  ARG B 147   N  SER B 127           
SHEET    1   C 6 LEU C  36  ALA C  38  0                                        
SHEET    2   C 6 VAL C   6  VAL C   9  1  N  VAL C   6   O  TYR C  37           
SHEET    3   C 6 VAL C  71  HIS C  76  1  O  ASP C  72   N  VAL C   7           
SHEET    4   C 6 VAL C  96  LEU C 102  1  O  VAL C 100   N  ALA C  75           
SHEET    5   C 6 LEU C 124  SER C 130  1  O  ILE C 128   N  THR C 101           
SHEET    6   C 6 ARG C 147  ILE C 151  1  O  VAL C 149   N  SER C 127           
SHEET    1   D 6 LEU D  36  ALA D  38  0                                        
SHEET    2   D 6 VAL D   6  VAL D   9  1  N  VAL D   6   O  TYR D  37           
SHEET    3   D 6 VAL D  71  HIS D  76  1  O  HIS D  76   N  VAL D   9           
SHEET    4   D 6 VAL D  96  LEU D 102  1  O  ASN D  98   N  ILE D  73           
SHEET    5   D 6 LEU D 124  SER D 130  1  O  ILE D 128   N  THR D 101           
SHEET    6   D 6 ARG D 147  ILE D 151  1  O  VAL D 149   N  SER D 127           
SHEET    1   E 6 LEU E  36  ALA E  38  0                                        
SHEET    2   E 6 VAL E   6  VAL E   9  1  N  VAL E   6   O  TYR E  37           
SHEET    3   E 6 VAL E  71  HIS E  76  1  O  HIS E  76   N  VAL E   9           
SHEET    4   E 6 VAL E  96  LEU E 102  1  O  LEU E 102   N  ALA E  75           
SHEET    5   E 6 LEU E 124  SER E 130  1  O  ILE E 128   N  THR E 101           
SHEET    6   E 6 ARG E 147  ILE E 151  1  O  VAL E 149   N  SER E 127           
SHEET    1   F 6 LEU F  36  ALA F  38  0                                        
SHEET    2   F 6 VAL F   6  VAL F   9  1  N  VAL F   6   O  TYR F  37           
SHEET    3   F 6 VAL F  71  HIS F  76  1  O  HIS F  76   N  VAL F   9           
SHEET    4   F 6 VAL F  96  LEU F 102  1  O  LEU F 102   N  ALA F  75           
SHEET    5   F 6 LEU F 124  SER F 130  1  O  LEU F 124   N  VAL F  99           
SHEET    6   F 6 ARG F 147  ILE F 151  1  O  VAL F 149   N  SER F 127           
SHEET    1   G 6 LEU G  36  ALA G  38  0                                        
SHEET    2   G 6 VAL G   6  VAL G   9  1  N  VAL G   6   O  TYR G  37           
SHEET    3   G 6 VAL G  71  HIS G  76  1  O  ASP G  72   N  VAL G   7           
SHEET    4   G 6 VAL G  96  LEU G 102  1  O  LEU G 102   N  ALA G  75           
SHEET    5   G 6 LEU G 124  SER G 130  1  O  ILE G 128   N  THR G 101           
SHEET    6   G 6 ARG G 147  ILE G 151  1  O  VAL G 149   N  SER G 127           
SHEET    1   H 6 LEU H  36  ALA H  38  0                                        
SHEET    2   H 6 VAL H   6  VAL H   9  1  N  VAL H   6   O  TYR H  37           
SHEET    3   H 6 VAL H  71  HIS H  76  1  O  HIS H  76   N  VAL H   9           
SHEET    4   H 6 VAL H  96  LEU H 102  1  O  VAL H 100   N  ALA H  75           
SHEET    5   H 6 LEU H 124  SER H 130  1  O  LEU H 124   N  ALA H  97           
SHEET    6   H 6 ARG H 147  ILE H 151  1  O  VAL H 149   N  SER H 127           
SHEET    1   I 6 LEU I  36  ALA I  38  0                                        
SHEET    2   I 6 VAL I   6  VAL I   9  1  N  VAL I   6   O  TYR I  37           
SHEET    3   I 6 VAL I  71  HIS I  76  1  O  ASP I  72   N  VAL I   7           
SHEET    4   I 6 VAL I  96  LEU I 102  1  O  LEU I 102   N  ALA I  75           
SHEET    5   I 6 LEU I 124  SER I 130  1  O  ILE I 128   N  THR I 101           
SHEET    6   I 6 ARG I 147  ILE I 151  1  O  VAL I 149   N  SER I 127           
SHEET    1   J 6 LEU J  36  ALA J  38  0                                        
SHEET    2   J 6 VAL J   6  VAL J   9  1  N  VAL J   6   O  TYR J  37           
SHEET    3   J 6 VAL J  71  HIS J  76  1  O  HIS J  76   N  VAL J   9           
SHEET    4   J 6 VAL J  96  LEU J 102  1  O  LEU J 102   N  ALA J  75           
SHEET    5   J 6 LEU J 124  SER J 130  1  O  ILE J 128   N  THR J 101           
SHEET    6   J 6 ARG J 147  ILE J 151  1  O  VAL J 149   N  SER J 127           
SHEET    1   K 6 LEU K  36  ALA K  38  0                                        
SHEET    2   K 6 VAL K   6  VAL K   9  1  N  VAL K   6   O  TYR K  37           
SHEET    3   K 6 VAL K  71  HIS K  76  1  O  ASP K  72   N  VAL K   7           
SHEET    4   K 6 VAL K  96  LEU K 102  1  O  ASN K  98   N  ILE K  73           
SHEET    5   K 6 LEU K 124  SER K 130  1  O  LEU K 124   N  VAL K  99           
SHEET    6   K 6 ARG K 147  ILE K 151  1  O  VAL K 149   N  SER K 127           
SHEET    1   L 6 LEU L  36  ALA L  38  0                                        
SHEET    2   L 6 VAL L   6  VAL L   9  1  N  VAL L   6   O  TYR L  37           
SHEET    3   L 6 VAL L  71  HIS L  76  1  O  ASP L  72   N  VAL L   7           
SHEET    4   L 6 VAL L  96  LEU L 102  1  O  LEU L 102   N  ALA L  75           
SHEET    5   L 6 LEU L 124  SER L 130  1  O  ILE L 128   N  THR L 101           
SHEET    6   L 6 ARG L 147  ILE L 151  1  O  VAL L 149   N  SER L 127           
CRYST1  132.285  198.042  197.902  90.00  90.00  90.00 C 2 2 21     96          
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      0.007559  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005049  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005053        0.00000                         
TER    1366      ASN A 181                                                      
TER    2732      ASN B 181                                                      
TER    4098      ASN C 181                                                      
TER    5464      ASN D 181                                                      
TER    6830      ASN E 181                                                      
TER    8196      ASN F 181                                                      
TER    9562      ASN G 181                                                      
TER   10928      ASN H 181                                                      
TER   12294      ASN I 181                                                      
TER   13660      ASN J 181                                                      
TER   15026      ASN K 181                                                      
TER   16392      ASN L 181                                                      
MASTER      465    0    0  118   72    0    0    617510   12    0  168          
END                                                                             

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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.
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