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LongText Report for: 3FVT-pdb

Name Class
3FVT-pdb
HEADER    HYDROLASE                               16-JAN-09   3FVT              
TITLE     CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE FROM BACILLUS              
TITLE    2 PUMILUS, MONOCLINIC CRYSTAL FORM II                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYL XYLAN ESTERASE;                                     
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, L, M, N;                           
COMPND   4 EC: 3.1.1.6;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS PUMILUS;                               
SOURCE   3 ORGANISM_TAXID: 1408;                                                
SOURCE   4 STRAIN: PS 213;                                                      
SOURCE   5 GENE: AXE;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PBPEB2                           
KEYWDS    ALPHA/BETA HYDROLASE, CARBOHYDRATE ESTERASE, CE7, BACILLUS            
KEYWDS   2 PUMILUS, HYDROLASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.KRASTANOVA,A.CASSETTA,D.LAMBA                                       
REVDAT   1   05-JAN-10 3FVT    0                                                
JRNL        AUTH   I.KRASTANOVA,A.CASSETTA,M.MASTIHUBOVA,P.BIELY,               
JRNL        AUTH 2 D.LAMBA                                                      
JRNL        TITL   STRUCTURAL AND FUNCTIONAL STUDIES OF BACILLUS                
JRNL        TITL 2 PUMILUS ACETYL XYLAN ESTERASE                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   I.KRASTANOVA,C.GUARNACCIA,S.ZAHARIEV,G.DEGRASSI,             
REMARK   1  AUTH 2 D.LAMBA                                                      
REMARK   1  TITL   HETEROLOGOUS EXPRESSION, PURIFICATION,                       
REMARK   1  TITL 2 CRYSTALLIZATION, X-RAY ANALYSIS AND PHASING OF THE           
REMARK   1  TITL 3 ACETYL XYLAN ESTERASE FROM BACILLUS PUMILUS                  
REMARK   1  REF    BIOCHIM.BIOPHYS.ACTA          V.1748   222 2005              
REMARK   1  REFN                   ISSN 0006-3002                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   G.DEGRASSI,M.KOJIC,G.LJUBIJANKIC,V.VENTURI                   
REMARK   1  TITL   THE ACETYL XYLAN ESTERASE OF BACILLUS PUMILUS                
REMARK   1  TITL 2 BELONGS TO A FAMILY OF ESTERASES WITH BROAD                  
REMARK   1  TITL 3 SUBSTRATE SPECIFICITY                                        
REMARK   1  REF    MICROBIOLOGY                  V. 146  1585 2000              
REMARK   1  REFN                   ISSN 0026-2617                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   G.DEGRASSI,B.C.OKEKE,C.V.BRUSCHI,V.VENTURI                   
REMARK   1  TITL   PURIFICATION AND CHARACTERIZATION OF AN ACETYL               
REMARK   1  TITL 2 XYLAN ESTERASE FROM BACILLUS PUMILUS                         
REMARK   1  REF    APPL.ENVIRON.MICROBIOL.       V.  64   789 1998              
REMARK   1  REFN                   ISSN 0099-2240                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 960989.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 298450                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 29799                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 39737                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400                       
REMARK   3   BIN FREE R VALUE                    : 0.3170                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 4365                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.005                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 30462                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 3152                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.73                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.82000                                             
REMARK   3    B22 (A**2) : -0.76000                                             
REMARK   3    B33 (A**2) : 2.58000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.61000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.07                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.29                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.19                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.90                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.930 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.430 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.950 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.700 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 57.81                                                
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  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : GOL.PAR                                        
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : GOL.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3FVT COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051104.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-OCT-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.278                              
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 298796                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.750                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.9                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1ODS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M LITHIUM CHLORIDE, 5% PEG 6000,      
REMARK 280  0.1M MES, PH 6.0, MICROBATCH, TEMPERATURE 293K                      
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       43.60250            
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                                                    
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18940 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 63980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -177.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D, E, 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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18900 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 64150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -183.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, M, H, N, I, 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 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     SER A   319                                                      
REMARK 465     THR A   320                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B   319                                                      
REMARK 465     THR B   320                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LEU C   318                                                      
REMARK 465     SER C   319                                                      
REMARK 465     THR C   320                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D   319                                                      
REMARK 465     THR D   320                                                      
REMARK 465     MET E     1                                                      
REMARK 465     SER E   319                                                      
REMARK 465     THR E   320                                                      
REMARK 465     MET F     1                                                      
REMARK 465     MET G     1                                                      
REMARK 465     SER G   319                                                      
REMARK 465     THR G   320                                                      
REMARK 465     MET H     1                                                      
REMARK 465     SER H   319                                                      
REMARK 465     THR H   320                                                      
REMARK 465     MET I     1                                                      
REMARK 465     SER I   319                                                      
REMARK 465     THR I   320                                                      
REMARK 465     MET L     1                                                      
REMARK 465     SER L   319                                                      
REMARK 465     THR L   320                                                      
REMARK 465     SER M   319                                                      
REMARK 465     THR M   320                                                      
REMARK 465     SER N   319                                                      
REMARK 465     THR N   320                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A   4      -27.92   -145.39                                   
REMARK 500    ARG A 118      112.05    -24.73                                   
REMARK 500    GLN A 120      -88.99    -95.20                                   
REMARK 500    SER A 123      144.61     68.64                                   
REMARK 500    SER A 181     -112.34     53.45                                   
REMARK 500    TYR A 204       71.54     27.02                                   
REMARK 500    PHE B   4      -22.96   -148.16                                   
REMARK 500    PHE B  64      129.87    -38.31                                   
REMARK 500    ARG B 118      107.83    -27.20                                   
REMARK 500    GLN B 120      -87.57    -92.30                                   
REMARK 500    SER B 123      141.89     70.57                                   
REMARK 500    SER B 181     -118.32     61.22                                   
REMARK 500    TYR B 204       69.21     27.60                                   
REMARK 500    LEU B 223       -8.66    -59.45                                   
REMARK 500    LEU B 316      -58.68   -120.34                                   
REMARK 500    PHE C   4      -18.90   -153.67                                   
REMARK 500    LEU C   6      152.35    -49.84                                   
REMARK 500    GLU C  41       54.21     39.59                                   
REMARK 500    PRO C  50       67.40    -68.84                                   
REMARK 500    PHE C  64      133.22    -37.77                                   
REMARK 500    ARG C 118      116.71    -28.27                                   
REMARK 500    GLN C 120      -92.47    -95.27                                   
REMARK 500    SER C 123      142.39     72.43                                   
REMARK 500    SER C 181     -112.75     57.29                                   
REMARK 500    TYR C 204       67.71     24.24                                   
REMARK 500    LEU D   3      141.15    -39.70                                   
REMARK 500    PHE D   4      -23.53   -151.08                                   
REMARK 500    SER D  63     -158.24   -140.78                                   
REMARK 500    ARG D 118      118.23    -34.04                                   
REMARK 500    GLN D 120      -89.99    -92.80                                   
REMARK 500    SER D 123      146.95     76.82                                   
REMARK 500    SER D 181     -110.53     59.53                                   
REMARK 500    TYR D 204       73.49     23.75                                   
REMARK 500    PHE E   4      -24.20   -155.00                                   
REMARK 500    ASP E   5     -156.35    -86.35                                   
REMARK 500    GLU E  41       59.16     38.76                                   
REMARK 500    ARG E 118      113.49    -22.17                                   
REMARK 500    GLN E 120      -88.96    -94.00                                   
REMARK 500    SER E 123      134.78     73.85                                   
REMARK 500    SER E 181     -112.26     51.35                                   
REMARK 500    TYR E 204       71.12     24.73                                   
REMARK 500    LEU E 317      -73.40    -78.09                                   
REMARK 500    PHE F   4      -24.98   -159.67                                   
REMARK 500    ASP F   5     -159.50    -91.35                                   
REMARK 500    GLU F  41       51.14     39.93                                   
REMARK 500    PHE F  64      137.52    -39.90                                   
REMARK 500    ARG F 118      112.98    -22.43                                   
REMARK 500    GLN F 120      -90.27    -97.67                                   
REMARK 500    SER F 123      145.19     71.92                                   
REMARK 500    SER F 181     -117.63     62.49                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     108 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PRO H  83        45.1      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 321                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 322                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 321                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 322                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 321                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 322                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 321                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 322                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E2273                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 321                  
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 322                  
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 321                  
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 322                  
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G2274                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 321                  
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 322                  
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 321                  
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 322                  
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I 321                  
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I 322                  
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL L 321                  
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL L 322                  
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 321                  
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 322                  
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL N 321                  
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL N 322                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FVR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE FROM BACILLUS             
REMARK 900 PUMILUS, MONOCLINIC CRYSTAL FORM I                                   
REMARK 900 RELATED ID: 1ODS   RELATED DB: PDB                                   
REMARK 900 CEPHALOSPORIN C DEACETYLASE FROM BACILLUS SUBTILIS                   
REMARK 900 RELATED ID: 1ODT   RELATED DB: PDB                                   
REMARK 900 CEPHALOSPORIN C DEACETYLASE MUTATED, IN COMPLEX WITH ACETATE         
REMARK 900 RELATED ID: 1L7A   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL GENOMICS, CRYSTAL STRUCTURE OF CEPHALOSPORIN C            
REMARK 900 DEACETYLASE                                                          
REMARK 900 RELATED ID: 1VLQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE (TM0077) FROM             
REMARK 900 THERMOTOGA MARITIMA AT 2.10 A RESOLUTION                             
REMARK 900 RELATED ID: 3FCY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE 1 FROM                    
REMARK 900 THERMOANAEROBACTERIUM SP. JW/SL YS485                                
DBREF  3FVT A    1   320  UNP    Q9K5F2   Q9K5F2_BACPU     1    320             
DBREF  3FVT B    1   320  UNP    Q9K5F2   Q9K5F2_BACPU     1    320             
DBREF  3FVT C    1   320  UNP    Q9K5F2   Q9K5F2_BACPU     1    320             
DBREF  3FVT D    1   320  UNP    Q9K5F2   Q9K5F2_BACPU     1    320             
DBREF  3FVT E    1   320  UNP    Q9K5F2   Q9K5F2_BACPU     1    320             
DBREF  3FVT F    1   320  UNP    Q9K5F2   Q9K5F2_BACPU     1    320             
DBREF  3FVT G    1   320  UNP    Q9K5F2   Q9K5F2_BACPU     1    320             
DBREF  3FVT H    1   320  UNP    Q9K5F2   Q9K5F2_BACPU     1    320             
DBREF  3FVT I    1   320  UNP    Q9K5F2   Q9K5F2_BACPU     1    320             
DBREF  3FVT L    1   320  UNP    Q9K5F2   Q9K5F2_BACPU     1    320             
DBREF  3FVT M    1   320  UNP    Q9K5F2   Q9K5F2_BACPU     1    320             
DBREF  3FVT N    1   320  UNP    Q9K5F2   Q9K5F2_BACPU     1    320             
SEQRES   1 A  320  MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS          
SEQRES   2 A  320  TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP          
SEQRES   3 A  320  PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU          
SEQRES   4 A  320  ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS          
SEQRES   5 A  320  GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY          
SEQRES   6 A  320  HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN          
SEQRES   7 A  320  THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR          
SEQRES   8 A  320  ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN          
SEQRES   9 A  320  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 A  320  ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO          
SEQRES  11 A  320  GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 A  320  SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 A  320  ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU          
SEQRES  14 A  320  VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN          
SEQRES  15 A  320  GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 A  320  ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 A  320  ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO          
SEQRES  18 A  320  TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP          
SEQRES  19 A  320  PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR          
SEQRES  20 A  320  PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO          
SEQRES  21 A  320  THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO          
SEQRES  22 A  320  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 A  320  ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 A  320  PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU          
SEQRES  25 A  320  GLN LYS HIS LEU LEU LEU SER THR                              
SEQRES   1 B  320  MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS          
SEQRES   2 B  320  TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP          
SEQRES   3 B  320  PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU          
SEQRES   4 B  320  ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS          
SEQRES   5 B  320  GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY          
SEQRES   6 B  320  HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN          
SEQRES   7 B  320  THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR          
SEQRES   8 B  320  ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN          
SEQRES   9 B  320  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 B  320  ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO          
SEQRES  11 B  320  GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 B  320  SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 B  320  ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU          
SEQRES  14 B  320  VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN          
SEQRES  15 B  320  GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 B  320  ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 B  320  ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO          
SEQRES  18 B  320  TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP          
SEQRES  19 B  320  PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR          
SEQRES  20 B  320  PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO          
SEQRES  21 B  320  THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO          
SEQRES  22 B  320  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 B  320  ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 B  320  PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU          
SEQRES  25 B  320  GLN LYS HIS LEU LEU LEU SER THR                              
SEQRES   1 C  320  MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS          
SEQRES   2 C  320  TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP          
SEQRES   3 C  320  PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU          
SEQRES   4 C  320  ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS          
SEQRES   5 C  320  GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY          
SEQRES   6 C  320  HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN          
SEQRES   7 C  320  THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR          
SEQRES   8 C  320  ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN          
SEQRES   9 C  320  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 C  320  ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO          
SEQRES  11 C  320  GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 C  320  SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 C  320  ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU          
SEQRES  14 C  320  VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN          
SEQRES  15 C  320  GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 C  320  ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 C  320  ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO          
SEQRES  18 C  320  TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP          
SEQRES  19 C  320  PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR          
SEQRES  20 C  320  PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO          
SEQRES  21 C  320  THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO          
SEQRES  22 C  320  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 C  320  ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 C  320  PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU          
SEQRES  25 C  320  GLN LYS HIS LEU LEU LEU SER THR                              
SEQRES   1 D  320  MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS          
SEQRES   2 D  320  TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP          
SEQRES   3 D  320  PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU          
SEQRES   4 D  320  ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS          
SEQRES   5 D  320  GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY          
SEQRES   6 D  320  HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN          
SEQRES   7 D  320  THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR          
SEQRES   8 D  320  ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN          
SEQRES   9 D  320  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 D  320  ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO          
SEQRES  11 D  320  GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 D  320  SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 D  320  ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU          
SEQRES  14 D  320  VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN          
SEQRES  15 D  320  GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 D  320  ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 D  320  ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO          
SEQRES  18 D  320  TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP          
SEQRES  19 D  320  PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR          
SEQRES  20 D  320  PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO          
SEQRES  21 D  320  THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO          
SEQRES  22 D  320  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 D  320  ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 D  320  PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU          
SEQRES  25 D  320  GLN LYS HIS LEU LEU LEU SER THR                              
SEQRES   1 E  320  MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS          
SEQRES   2 E  320  TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP          
SEQRES   3 E  320  PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU          
SEQRES   4 E  320  ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS          
SEQRES   5 E  320  GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY          
SEQRES   6 E  320  HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN          
SEQRES   7 E  320  THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR          
SEQRES   8 E  320  ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN          
SEQRES   9 E  320  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 E  320  ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO          
SEQRES  11 E  320  GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 E  320  SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 E  320  ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU          
SEQRES  14 E  320  VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN          
SEQRES  15 E  320  GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 E  320  ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 E  320  ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO          
SEQRES  18 E  320  TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP          
SEQRES  19 E  320  PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR          
SEQRES  20 E  320  PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO          
SEQRES  21 E  320  THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO          
SEQRES  22 E  320  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 E  320  ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 E  320  PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU          
SEQRES  25 E  320  GLN LYS HIS LEU LEU LEU SER THR                              
SEQRES   1 F  320  MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS          
SEQRES   2 F  320  TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP          
SEQRES   3 F  320  PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU          
SEQRES   4 F  320  ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS          
SEQRES   5 F  320  GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY          
SEQRES   6 F  320  HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN          
SEQRES   7 F  320  THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR          
SEQRES   8 F  320  ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN          
SEQRES   9 F  320  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 F  320  ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO          
SEQRES  11 F  320  GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 F  320  SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 F  320  ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU          
SEQRES  14 F  320  VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN          
SEQRES  15 F  320  GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 F  320  ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 F  320  ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO          
SEQRES  18 F  320  TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP          
SEQRES  19 F  320  PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR          
SEQRES  20 F  320  PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO          
SEQRES  21 F  320  THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO          
SEQRES  22 F  320  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 F  320  ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 F  320  PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU          
SEQRES  25 F  320  GLN LYS HIS LEU LEU LEU SER THR                              
SEQRES   1 G  320  MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS          
SEQRES   2 G  320  TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP          
SEQRES   3 G  320  PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU          
SEQRES   4 G  320  ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS          
SEQRES   5 G  320  GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY          
SEQRES   6 G  320  HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN          
SEQRES   7 G  320  THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR          
SEQRES   8 G  320  ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN          
SEQRES   9 G  320  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 G  320  ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO          
SEQRES  11 G  320  GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 G  320  SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 G  320  ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU          
SEQRES  14 G  320  VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN          
SEQRES  15 G  320  GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 G  320  ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 G  320  ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO          
SEQRES  18 G  320  TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP          
SEQRES  19 G  320  PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR          
SEQRES  20 G  320  PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO          
SEQRES  21 G  320  THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO          
SEQRES  22 G  320  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 G  320  ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 G  320  PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU          
SEQRES  25 G  320  GLN LYS HIS LEU LEU LEU SER THR                              
SEQRES   1 H  320  MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS          
SEQRES   2 H  320  TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP          
SEQRES   3 H  320  PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU          
SEQRES   4 H  320  ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS          
SEQRES   5 H  320  GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY          
SEQRES   6 H  320  HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN          
SEQRES   7 H  320  THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR          
SEQRES   8 H  320  ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN          
SEQRES   9 H  320  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 H  320  ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO          
SEQRES  11 H  320  GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 H  320  SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 H  320  ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU          
SEQRES  14 H  320  VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN          
SEQRES  15 H  320  GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 H  320  ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 H  320  ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO          
SEQRES  18 H  320  TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP          
SEQRES  19 H  320  PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR          
SEQRES  20 H  320  PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO          
SEQRES  21 H  320  THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO          
SEQRES  22 H  320  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 H  320  ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 H  320  PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU          
SEQRES  25 H  320  GLN LYS HIS LEU LEU LEU SER THR                              
SEQRES   1 I  320  MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS          
SEQRES   2 I  320  TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP          
SEQRES   3 I  320  PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU          
SEQRES   4 I  320  ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS          
SEQRES   5 I  320  GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY          
SEQRES   6 I  320  HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN          
SEQRES   7 I  320  THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR          
SEQRES   8 I  320  ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN          
SEQRES   9 I  320  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 I  320  ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO          
SEQRES  11 I  320  GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 I  320  SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 I  320  ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU          
SEQRES  14 I  320  VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN          
SEQRES  15 I  320  GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 I  320  ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 I  320  ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO          
SEQRES  18 I  320  TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP          
SEQRES  19 I  320  PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR          
SEQRES  20 I  320  PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO          
SEQRES  21 I  320  THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO          
SEQRES  22 I  320  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 I  320  ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 I  320  PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU          
SEQRES  25 I  320  GLN LYS HIS LEU LEU LEU SER THR                              
SEQRES   1 L  320  MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS          
SEQRES   2 L  320  TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP          
SEQRES   3 L  320  PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU          
SEQRES   4 L  320  ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS          
SEQRES   5 L  320  GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY          
SEQRES   6 L  320  HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN          
SEQRES   7 L  320  THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR          
SEQRES   8 L  320  ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN          
SEQRES   9 L  320  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 L  320  ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO          
SEQRES  11 L  320  GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 L  320  SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 L  320  ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU          
SEQRES  14 L  320  VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN          
SEQRES  15 L  320  GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 L  320  ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 L  320  ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO          
SEQRES  18 L  320  TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP          
SEQRES  19 L  320  PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR          
SEQRES  20 L  320  PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO          
SEQRES  21 L  320  THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO          
SEQRES  22 L  320  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 L  320  ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 L  320  PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU          
SEQRES  25 L  320  GLN LYS HIS LEU LEU LEU SER THR                              
SEQRES   1 M  320  MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS          
SEQRES   2 M  320  TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP          
SEQRES   3 M  320  PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU          
SEQRES   4 M  320  ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS          
SEQRES   5 M  320  GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY          
SEQRES   6 M  320  HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN          
SEQRES   7 M  320  THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR          
SEQRES   8 M  320  ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN          
SEQRES   9 M  320  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 M  320  ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO          
SEQRES  11 M  320  GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 M  320  SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 M  320  ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU          
SEQRES  14 M  320  VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN          
SEQRES  15 M  320  GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 M  320  ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 M  320  ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO          
SEQRES  18 M  320  TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP          
SEQRES  19 M  320  PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR          
SEQRES  20 M  320  PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO          
SEQRES  21 M  320  THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO          
SEQRES  22 M  320  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 M  320  ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 M  320  PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU          
SEQRES  25 M  320  GLN LYS HIS LEU LEU LEU SER THR                              
SEQRES   1 N  320  MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS          
SEQRES   2 N  320  TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP          
SEQRES   3 N  320  PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU          
SEQRES   4 N  320  ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS          
SEQRES   5 N  320  GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY          
SEQRES   6 N  320  HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN          
SEQRES   7 N  320  THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR          
SEQRES   8 N  320  ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN          
SEQRES   9 N  320  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 N  320  ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO          
SEQRES  11 N  320  GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 N  320  SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 N  320  ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU          
SEQRES  14 N  320  VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN          
SEQRES  15 N  320  GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 N  320  ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 N  320  ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO          
SEQRES  18 N  320  TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP          
SEQRES  19 N  320  PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR          
SEQRES  20 N  320  PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO          
SEQRES  21 N  320  THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO          
SEQRES  22 N  320  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 N  320  ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 N  320  PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU          
SEQRES  25 N  320  GLN LYS HIS LEU LEU LEU SER THR                              
HET     CL  A 321       1                                                       
HET     CL  A 322       1                                                       
HET     CL  B 321       1                                                       
HET     CL  B 322       1                                                       
HET     CL  C 321       1                                                       
HET     CL  C 322       1                                                       
HET     CL  D 321       1                                                       
HET     CL  D 322       1                                                       
HET    GOL  E2273       6                                                       
HET     CL  E 321       1                                                       
HET     CL  E 322       1                                                       
HET     CL  F 321       1                                                       
HET     CL  F 322       1                                                       
HET    GOL  G2274       6                                                       
HET     CL  G 321       1                                                       
HET     CL  G 322       1                                                       
HET     CL  H 321       1                                                       
HET     CL  H 322       1                                                       
HET     CL  I 321       1                                                       
HET     CL  I 322       1                                                       
HET     CL  L 321       1                                                       
HET     CL  L 322       1                                                       
HET     CL  M 321       1                                                       
HET     CL  M 322       1                                                       
HET     CL  N 321       1                                                       
HET     CL  N 322       1                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
FORMUL  13   CL    24(CL 1-)                                                    
FORMUL  21  GOL    2(C3 H8 O3)                                                  
FORMUL  39  HOH   *3152(H2 O)                                                   
HELIX    1   1 SER A    7  TYR A   14  1                                   8    
HELIX    2   2 ASP A   23  GLN A   37  1                                  15    
HELIX    3   3 PHE A   64  HIS A   66  5                                   3    
HELIX    4   4 TYR A   95  GLY A   97  5                                   3    
HELIX    5   5 GLY A   98  HIS A  108  1                                  11    
HELIX    6   6 TYR A  148  SER A  166  1                                  19    
HELIX    7   7 SER A  181  SER A  194  1                                  14    
HELIX    8   8 ASN A  209  ALA A  217  1                                   9    
HELIX    9   9 TYR A  222  ASN A  232  1                                  11    
HELIX   10  10 ASP A  234  TYR A  247  1                                  14    
HELIX   11  11 ASP A  249  ALA A  254  1                                   6    
HELIX   12  12 GLY A  255  VAL A  257  5                                   3    
HELIX   13  13 PRO A  273  HIS A  283  1                                  11    
HELIX   14  14 ILE A  301  LEU A  316  1                                  16    
HELIX   15  15 SER B    7  TYR B   14  1                                   8    
HELIX   16  16 ASP B   23  GLN B   37  1                                  15    
HELIX   17  17 PHE B   64  HIS B   66  5                                   3    
HELIX   18  18 TYR B   95  GLY B   97  5                                   3    
HELIX   19  19 GLY B   98  HIS B  108  1                                  11    
HELIX   20  20 TYR B  148  SER B  166  1                                  19    
HELIX   21  21 SER B  181  SER B  194  1                                  14    
HELIX   22  22 ASN B  209  ALA B  217  1                                   9    
HELIX   23  23 TYR B  222  ASN B  232  1                                  11    
HELIX   24  24 ASP B  234  TYR B  247  1                                  14    
HELIX   25  25 ASP B  249  ALA B  254  1                                   6    
HELIX   26  26 GLY B  255  VAL B  257  5                                   3    
HELIX   27  27 PRO B  273  ASN B  282  1                                  10    
HELIX   28  28 ILE B  301  LEU B  316  1                                  16    
HELIX   29  29 SER C    7  TYR C   14  1                                   8    
HELIX   30  30 ASP C   23  GLN C   37  1                                  15    
HELIX   31  31 PHE C   64  HIS C   66  5                                   3    
HELIX   32  32 TYR C   95  GLY C   97  5                                   3    
HELIX   33  33 GLY C   98  HIS C  108  1                                  11    
HELIX   34  34 TYR C  148  PHE C  167  1                                  20    
HELIX   35  35 SER C  181  SER C  194  1                                  14    
HELIX   36  36 ASN C  209  ALA C  217  1                                   9    
HELIX   37  37 TYR C  222  ASN C  232  1                                  11    
HELIX   38  38 ASP C  234  TYR C  247  1                                  14    
HELIX   39  39 ASP C  249  ALA C  254  1                                   6    
HELIX   40  40 GLY C  255  VAL C  257  5                                   3    
HELIX   41  41 PRO C  273  ASN C  282  1                                  10    
HELIX   42  42 ILE C  301  LEU C  317  1                                  17    
HELIX   43  43 SER D    7  LYS D   13  1                                   7    
HELIX   44  44 ASP D   23  VAL D   38  1                                  16    
HELIX   45  45 PHE D   64  HIS D   66  5                                   3    
HELIX   46  46 TYR D   95  GLY D   97  5                                   3    
HELIX   47  47 GLY D   98  HIS D  108  1                                  11    
HELIX   48  48 TYR D  148  PHE D  167  1                                  20    
HELIX   49  49 SER D  181  SER D  194  1                                  14    
HELIX   50  50 ASN D  209  ALA D  217  1                                   9    
HELIX   51  51 TYR D  222  ASN D  232  1                                  11    
HELIX   52  52 ASP D  234  TYR D  247  1                                  14    
HELIX   53  53 ASP D  249  ALA D  254  1                                   6    
HELIX   54  54 GLY D  255  VAL D  257  5                                   3    
HELIX   55  55 PRO D  273  HIS D  283  1                                  11    
HELIX   56  56 ILE D  301  LEU D  316  1                                  16    
HELIX   57  57 SER E    7  LYS E   13  1                                   7    
HELIX   58  58 ASP E   23  GLN E   37  1                                  15    
HELIX   59  59 PHE E   64  HIS E   66  5                                   3    
HELIX   60  60 TYR E   95  GLY E   97  5                                   3    
HELIX   61  61 GLY E   98  HIS E  108  1                                  11    
HELIX   62  62 TYR E  148  PHE E  167  1                                  20    
HELIX   63  63 SER E  181  SER E  194  1                                  14    
HELIX   64  64 ASN E  209  ALA E  217  1                                   9    
HELIX   65  65 TYR E  222  ASN E  232  1                                  11    
HELIX   66  66 ASP E  234  TYR E  247  1                                  14    
HELIX   67  67 ASP E  249  ALA E  254  1                                   6    
HELIX   68  68 GLY E  255  VAL E  257  5                                   3    
HELIX   69  69 PRO E  273  HIS E  283  1                                  11    
HELIX   70  70 ILE E  301  LEU E  316  1                                  16    
HELIX   71  71 SER F    7  TYR F   14  1                                   8    
HELIX   72  72 ASP F   23  GLN F   37  1                                  15    
HELIX   73  73 PHE F   64  HIS F   66  5                                   3    
HELIX   74  74 TYR F   95  GLY F   97  5                                   3    
HELIX   75  75 GLY F   98  HIS F  108  1                                  11    
HELIX   76  76 TYR F  148  SER F  166  1                                  19    
HELIX   77  77 SER F  181  SER F  194  1                                  14    
HELIX   78  78 ASN F  209  ALA F  217  1                                   9    
HELIX   79  79 TYR F  222  ASN F  232  1                                  11    
HELIX   80  80 ASP F  234  TYR F  247  1                                  14    
HELIX   81  81 ASP F  249  ALA F  254  1                                   6    
HELIX   82  82 GLY F  255  VAL F  257  5                                   3    
HELIX   83  83 PRO F  273  HIS F  283  1                                  11    
HELIX   84  84 ILE F  301  LEU F  316  1                                  16    
HELIX   85  85 SER G    7  LYS G   12  1                                   6    
HELIX   86  86 ASP G   23  VAL G   38  1                                  16    
HELIX   87  87 PHE G   64  HIS G   66  5                                   3    
HELIX   88  88 TYR G   95  GLY G   97  5                                   3    
HELIX   89  89 GLY G   98  HIS G  108  1                                  11    
HELIX   90  90 TYR G  148  SER G  166  1                                  19    
HELIX   91  91 SER G  181  SER G  194  1                                  14    
HELIX   92  92 ASN G  209  ALA G  217  1                                   9    
HELIX   93  93 LEU G  223  ASN G  232  1                                  10    
HELIX   94  94 ASP G  234  TYR G  247  1                                  14    
HELIX   95  95 ASP G  249  ALA G  254  1                                   6    
HELIX   96  96 GLY G  255  VAL G  257  5                                   3    
HELIX   97  97 PRO G  273  ASN G  282  1                                  10    
HELIX   98  98 ILE G  301  LEU G  316  1                                  16    
HELIX   99  99 SER H    7  TYR H   14  1                                   8    
HELIX  100 100 ASP H   23  GLN H   37  1                                  15    
HELIX  101 101 PHE H   64  HIS H   66  5                                   3    
HELIX  102 102 TYR H   95  GLY H   97  5                                   3    
HELIX  103 103 GLY H   98  HIS H  108  1                                  11    
HELIX  104 104 TYR H  148  SER H  166  1                                  19    
HELIX  105 105 SER H  181  SER H  194  1                                  14    
HELIX  106 106 ASN H  209  ALA H  217  1                                   9    
HELIX  107 107 TYR H  222  ASN H  232  1                                  11    
HELIX  108 108 ASP H  234  TYR H  247  1                                  14    
HELIX  109 109 ASP H  249  ALA H  254  1                                   6    
HELIX  110 110 GLY H  255  VAL H  257  5                                   3    
HELIX  111 111 PRO H  273  ASN H  282  1                                  10    
HELIX  112 112 ILE H  301  LEU H  316  1                                  16    
HELIX  113 113 SER I    7  TYR I   14  1                                   8    
HELIX  114 114 ASP I   23  GLN I   37  1                                  15    
HELIX  115 115 PHE I   64  HIS I   66  5                                   3    
HELIX  116 116 TYR I   95  GLY I   97  5                                   3    
HELIX  117 117 GLY I   98  HIS I  108  1                                  11    
HELIX  118 118 TYR I  148  PHE I  167  1                                  20    
HELIX  119 119 SER I  181  SER I  194  1                                  14    
HELIX  120 120 ASN I  209  ALA I  217  1                                   9    
HELIX  121 121 TYR I  222  ASN I  232  1                                  11    
HELIX  122 122 ASP I  234  TYR I  247  1                                  14    
HELIX  123 123 ASP I  249  ALA I  254  1                                   6    
HELIX  124 124 GLY I  255  VAL I  257  5                                   3    
HELIX  125 125 PRO I  273  HIS I  283  1                                  11    
HELIX  126 126 ILE I  301  LEU I  317  1                                  17    
HELIX  127 127 SER L    7  TYR L   14  1                                   8    
HELIX  128 128 ASP L   23  GLN L   37  1                                  15    
HELIX  129 129 PHE L   64  HIS L   66  5                                   3    
HELIX  130 130 TYR L   95  GLY L   97  5                                   3    
HELIX  131 131 GLY L   98  HIS L  108  1                                  11    
HELIX  132 132 TYR L  148  PHE L  167  1                                  20    
HELIX  133 133 SER L  181  SER L  194  1                                  14    
HELIX  134 134 ASN L  209  ALA L  217  1                                   9    
HELIX  135 135 LEU L  223  ASN L  232  1                                  10    
HELIX  136 136 ASP L  234  TYR L  247  1                                  14    
HELIX  137 137 ASP L  249  ALA L  254  1                                   6    
HELIX  138 138 GLY L  255  VAL L  257  5                                   3    
HELIX  139 139 PRO L  273  ASN L  282  1                                  10    
HELIX  140 140 ILE L  301  LEU L  316  1                                  16    
HELIX  141 141 SER M    7  TYR M   14  1                                   8    
HELIX  142 142 ASP M   23  GLN M   37  1                                  15    
HELIX  143 143 PHE M   64  HIS M   66  5                                   3    
HELIX  144 144 TYR M   95  GLY M   97  5                                   3    
HELIX  145 145 GLY M   98  HIS M  108  1                                  11    
HELIX  146 146 TYR M  148  GLN M  165  1                                  18    
HELIX  147 147 SER M  181  SER M  194  1                                  14    
HELIX  148 148 ASN M  209  ALA M  217  1                                   9    
HELIX  149 149 TYR M  222  ASN M  232  1                                  11    
HELIX  150 150 ASP M  234  TYR M  247  1                                  14    
HELIX  151 151 ASP M  249  ALA M  254  1                                   6    
HELIX  152 152 GLY M  255  VAL M  257  5                                   3    
HELIX  153 153 PRO M  273  HIS M  283  1                                  11    
HELIX  154 154 ILE M  301  LEU M  316  1                                  16    
HELIX  155 155 SER N    7  TYR N   14  1                                   8    
HELIX  156 156 ASP N   23  GLN N   37  1                                  15    
HELIX  157 157 PHE N   64  HIS N   66  5                                   3    
HELIX  158 158 TYR N   95  GLY N   97  5                                   3    
HELIX  159 159 GLY N   98  HIS N  108  1                                  11    
HELIX  160 160 TYR N  148  PHE N  167  1                                  20    
HELIX  161 161 SER N  181  SER N  194  1                                  14    
HELIX  162 162 ASN N  209  ALA N  217  1                                   9    
HELIX  163 163 TYR N  222  ASN N  232  1                                  11    
HELIX  164 164 ASP N  234  TYR N  247  1                                  14    
HELIX  165 165 ASP N  249  ALA N  254  1                                   6    
HELIX  166 166 GLY N  255  VAL N  257  5                                   3    
HELIX  167 167 PRO N  273  ASN N  282  1                                  10    
HELIX  168 168 ILE N  301  LEU N  316  1                                  16    
SHEET    1   A 9 THR A  43  SER A  46  0                                        
SHEET    2   A 9 VAL A  54  SER A  63 -1  O  THR A  60   N  THR A  43           
SHEET    3   A 9 SER A  67  PRO A  76 -1  O  VAL A  75   N  LYS A  55           
SHEET    4   A 9 ALA A 111  MET A 115 -1  O  THR A 112   N  ALA A  74           
SHEET    5   A 9 HIS A  82  PHE A  88  1  N  PRO A  83   O  ALA A 111           
SHEET    6   A 9 VAL A 170  GLY A 180  1  O  ASP A 171   N  HIS A  82           
SHEET    7   A 9 VAL A 199  ASP A 203  1  O  ASP A 203   N  GLY A 179           
SHEET    8   A 9 THR A 261  GLY A 266  1  O  LEU A 262   N  ALA A 202           
SHEET    9   A 9 LYS A 288  TYR A 293  1  O  TYR A 293   N  ILE A 265           
SHEET    1   B 9 THR B  43  SER B  46  0                                        
SHEET    2   B 9 VAL B  54  SER B  63 -1  O  ARG B  58   N  GLU B  45           
SHEET    3   B 9 SER B  67  PRO B  76 -1  O  ILE B  69   N  TYR B  61           
SHEET    4   B 9 ALA B 111  MET B 115 -1  O  GLY B 114   N  PHE B  72           
SHEET    5   B 9 HIS B  82  PHE B  88  1  N  ARG B  87   O  PHE B 113           
SHEET    6   B 9 VAL B 170  GLY B 180  1  O  ASP B 171   N  HIS B  82           
SHEET    7   B 9 VAL B 199  ASP B 203  1  O  VAL B 201   N  VAL B 177           
SHEET    8   B 9 THR B 261  GLY B 266  1  O  LEU B 262   N  ALA B 202           
SHEET    9   B 9 LYS B 288  TYR B 293  1  O  TYR B 293   N  ILE B 265           
SHEET    1   C 9 THR C  43  SER C  46  0                                        
SHEET    2   C 9 VAL C  54  SER C  63 -1  O  ARG C  58   N  GLU C  45           
SHEET    3   C 9 SER C  67  PRO C  76 -1  O  ILE C  69   N  TYR C  61           
SHEET    4   C 9 ALA C 111  MET C 115 -1  O  THR C 112   N  ALA C  74           
SHEET    5   C 9 HIS C  82  PHE C  88  1  N  PRO C  83   O  ALA C 111           
SHEET    6   C 9 VAL C 170  GLY C 180  1  O  ASP C 171   N  HIS C  82           
SHEET    7   C 9 VAL C 199  ASP C 203  1  O  ASP C 203   N  GLY C 179           
SHEET    8   C 9 THR C 261  GLY C 266  1  O  LEU C 262   N  ALA C 202           
SHEET    9   C 9 LYS C 288  TYR C 293  1  O  LYS C 291   N  MET C 263           
SHEET    1   D 9 THR D  43  SER D  46  0                                        
SHEET    2   D 9 VAL D  54  SER D  63 -1  O  THR D  60   N  THR D  43           
SHEET    3   D 9 SER D  67  PRO D  76 -1  O  VAL D  75   N  LYS D  55           
SHEET    4   D 9 ALA D 111  MET D 115 -1  O  THR D 112   N  ALA D  74           
SHEET    5   D 9 HIS D  82  PHE D  88  1  N  LEU D  85   O  ALA D 111           
SHEET    6   D 9 VAL D 170  GLY D 180  1  O  ARG D 174   N  ALA D  84           
SHEET    7   D 9 VAL D 199  ASP D 203  1  O  ASP D 203   N  GLY D 179           
SHEET    8   D 9 THR D 261  GLY D 266  1  O  LEU D 262   N  ALA D 202           
SHEET    9   D 9 LYS D 288  TYR D 293  1  O  LYS D 291   N  MET D 263           
SHEET    1   E 9 THR E  43  SER E  46  0                                        
SHEET    2   E 9 VAL E  54  SER E  63 -1  O  ARG E  58   N  GLU E  45           
SHEET    3   E 9 SER E  67  PRO E  76 -1  O  ILE E  69   N  TYR E  61           
SHEET    4   E 9 ALA E 111  MET E 115 -1  O  THR E 112   N  ALA E  74           
SHEET    5   E 9 HIS E  82  PHE E  88  1  N  PRO E  83   O  ALA E 111           
SHEET    6   E 9 VAL E 170  GLY E 180  1  O  GLY E 176   N  ALA E  84           
SHEET    7   E 9 VAL E 199  ASP E 203  1  O  VAL E 201   N  VAL E 177           
SHEET    8   E 9 THR E 261  GLY E 266  1  O  LEU E 262   N  ALA E 202           
SHEET    9   E 9 LYS E 288  TYR E 293  1  O  LYS E 291   N  MET E 263           
SHEET    1   F 9 THR F  43  SER F  46  0                                        
SHEET    2   F 9 VAL F  54  SER F  63 -1  O  ARG F  58   N  GLU F  45           
SHEET    3   F 9 SER F  67  PRO F  76 -1  O  VAL F  75   N  LYS F  55           
SHEET    4   F 9 ALA F 111  MET F 115 -1  O  THR F 112   N  ALA F  74           
SHEET    5   F 9 HIS F  82  PHE F  88  1  N  ARG F  87   O  PHE F 113           
SHEET    6   F 9 VAL F 170  GLY F 180  1  O  ARG F 174   N  ALA F  84           
SHEET    7   F 9 VAL F 199  ASP F 203  1  O  ASP F 203   N  GLY F 179           
SHEET    8   F 9 THR F 261  GLY F 266  1  O  LEU F 262   N  VAL F 200           
SHEET    9   F 9 LYS F 288  TYR F 293  1  O  ASP F 289   N  MET F 263           
SHEET    1   G 9 THR G  43  TYR G  47  0                                        
SHEET    2   G 9 VAL G  54  SER G  63 -1  O  VAL G  56   N  TYR G  47           
SHEET    3   G 9 SER G  67  PRO G  76 -1  O  VAL G  75   N  LYS G  55           
SHEET    4   G 9 ALA G 111  MET G 115 -1  O  GLY G 114   N  PHE G  72           
SHEET    5   G 9 HIS G  82  PHE G  88  1  N  ARG G  87   O  PHE G 113           
SHEET    6   G 9 VAL G 170  GLY G 180  1  O  ASP G 171   N  HIS G  82           
SHEET    7   G 9 VAL G 199  ASP G 203  1  O  ASP G 203   N  GLY G 179           
SHEET    8   G 9 THR G 261  GLY G 266  1  O  LEU G 262   N  ALA G 202           
SHEET    9   G 9 LYS G 288  TYR G 293  1  O  TYR G 293   N  ILE G 265           
SHEET    1   H 9 THR H  43  SER H  46  0                                        
SHEET    2   H 9 VAL H  54  SER H  63 -1  O  ARG H  58   N  GLU H  45           
SHEET    3   H 9 SER H  67  PRO H  76 -1  O  ILE H  69   N  TYR H  61           
SHEET    4   H 9 ALA H 111  MET H 115 -1  O  GLY H 114   N  PHE H  72           
SHEET    5   H 9 HIS H  82  PHE H  88  1  N  ARG H  87   O  PHE H 113           
SHEET    6   H 9 VAL H 170  GLY H 180  1  O  ASP H 171   N  HIS H  82           
SHEET    7   H 9 VAL H 199  ASP H 203  1  O  ASP H 203   N  GLY H 179           
SHEET    8   H 9 THR H 261  GLY H 266  1  O  LEU H 262   N  ALA H 202           
SHEET    9   H 9 LYS H 288  TYR H 293  1  O  LYS H 291   N  MET H 263           
SHEET    1   I 9 THR I  43  SER I  46  0                                        
SHEET    2   I 9 VAL I  54  SER I  63 -1  O  ARG I  58   N  GLU I  45           
SHEET    3   I 9 SER I  67  PRO I  76 -1  O  ILE I  69   N  TYR I  61           
SHEET    4   I 9 ALA I 111  MET I 115 -1  O  THR I 112   N  ALA I  74           
SHEET    5   I 9 HIS I  82  PHE I  88  1  N  ARG I  87   O  PHE I 113           
SHEET    6   I 9 VAL I 170  GLY I 180  1  O  ARG I 174   N  ALA I  84           
SHEET    7   I 9 VAL I 199  ASP I 203  1  O  ASP I 203   N  GLY I 179           
SHEET    8   I 9 THR I 261  GLY I 266  1  O  LEU I 262   N  VAL I 200           
SHEET    9   I 9 LYS I 288  TYR I 293  1  O  LYS I 291   N  MET I 263           
SHEET    1   J 9 THR L  43  SER L  46  0                                        
SHEET    2   J 9 VAL L  54  SER L  63 -1  O  THR L  60   N  THR L  43           
SHEET    3   J 9 SER L  67  PRO L  76 -1  O  ILE L  69   N  TYR L  61           
SHEET    4   J 9 ALA L 111  MET L 115 -1  O  GLY L 114   N  PHE L  72           
SHEET    5   J 9 HIS L  82  PHE L  88  1  N  LEU L  85   O  ALA L 111           
SHEET    6   J 9 VAL L 170  GLY L 180  1  O  ASP L 171   N  HIS L  82           
SHEET    7   J 9 VAL L 199  ASP L 203  1  O  ASP L 203   N  GLY L 179           
SHEET    8   J 9 THR L 261  GLY L 266  1  O  LEU L 262   N  ALA L 202           
SHEET    9   J 9 LYS L 288  TYR L 293  1  O  LYS L 291   N  MET L 263           
SHEET    1   K 9 THR M  43  SER M  46  0                                        
SHEET    2   K 9 VAL M  54  SER M  63 -1  O  ARG M  58   N  GLU M  45           
SHEET    3   K 9 SER M  67  PRO M  76 -1  O  VAL M  75   N  LYS M  55           
SHEET    4   K 9 ALA M 111  MET M 115 -1  O  THR M 112   N  ALA M  74           
SHEET    5   K 9 HIS M  82  PHE M  88  1  N  LEU M  85   O  PHE M 113           
SHEET    6   K 9 VAL M 170  GLY M 180  1  O  ILE M 178   N  PHE M  88           
SHEET    7   K 9 VAL M 199  ASP M 203  1  O  VAL M 201   N  VAL M 177           
SHEET    8   K 9 THR M 261  GLY M 266  1  O  LEU M 262   N  VAL M 200           
SHEET    9   K 9 LYS M 288  TYR M 293  1  O  LYS M 291   N  MET M 263           
SHEET    1   L 9 THR N  43  SER N  46  0                                        
SHEET    2   L 9 VAL N  54  SER N  63 -1  O  ARG N  58   N  GLU N  45           
SHEET    3   L 9 SER N  67  PRO N  76 -1  O  VAL N  75   N  LYS N  55           
SHEET    4   L 9 ALA N 111  MET N 115 -1  O  THR N 112   N  ALA N  74           
SHEET    5   L 9 HIS N  82  PHE N  88  1  N  PRO N  83   O  ALA N 111           
SHEET    6   L 9 VAL N 170  GLY N 180  1  O  ARG N 174   N  ALA N  84           
SHEET    7   L 9 VAL N 199  ASP N 203  1  O  ASP N 203   N  GLY N 179           
SHEET    8   L 9 THR N 261  GLY N 266  1  O  LEU N 262   N  VAL N 200           
SHEET    9   L 9 LYS N 288  TYR N 293  1  O  LYS N 291   N  MET N 263           
CISPEP   1 GLY A   80    PRO A   81          0         0.06                     
CISPEP   2 GLN A  220    PRO A  221          0         0.56                     
CISPEP   3 GLY B   80    PRO B   81          0         0.08                     
CISPEP   4 GLN B  220    PRO B  221          0         0.33                     
CISPEP   5 GLY C   80    PRO C   81          0        -0.06                     
CISPEP   6 GLN C  220    PRO C  221          0         0.47                     
CISPEP   7 GLY D   80    PRO D   81          0         0.12                     
CISPEP   8 GLN D  220    PRO D  221          0         0.11                     
CISPEP   9 GLY E   80    PRO E   81          0         0.47                     
CISPEP  10 GLN E  220    PRO E  221          0         0.21                     
CISPEP  11 GLY F   80    PRO F   81          0        -0.08                     
CISPEP  12 GLN F  220    PRO F  221          0         0.33                     
CISPEP  13 GLY G   80    PRO G   81          0         0.10                     
CISPEP  14 GLN G  220    PRO G  221          0        -0.03                     
CISPEP  15 GLY H   80    PRO H   81          0        -0.01                     
CISPEP  16 GLN H  220    PRO H  221          0         0.55                     
CISPEP  17 GLY I   80    PRO I   81          0         0.12                     
CISPEP  18 GLN I  220    PRO I  221          0         0.62                     
CISPEP  19 GLY L   80    PRO L   81          0         0.08                     
CISPEP  20 GLN L  220    PRO L  221          0         0.48                     
CISPEP  21 GLY M   80    PRO M   81          0         0.01                     
CISPEP  22 GLN M  220    PRO M  221          0         0.24                     
CISPEP  23 GLY N   80    PRO N   81          0        -0.18                     
CISPEP  24 GLN N  220    PRO N  221          0         0.90                     
SITE     1 AC1  3 LYS A 270  HIS A 298  HOH A2283                               
SITE     1 AC2  4 GLY A 141  ILE A 142  LEU A 143  HOH A 777                    
SITE     1 AC3  4 GLY B 141  ILE B 142  LEU B 143  HOH B 342                    
SITE     1 AC4  2 LYS B 270  HIS B 298                                          
SITE     1 AC5  2 LYS C 270  HIS C 298                                          
SITE     1 AC6  2 GLY C 141  LEU C 143                                          
SITE     1 AC7  4 GLY D 141  ILE D 142  LEU D 143  HOH D 988                    
SITE     1 AC8  2 LYS D 270  HIS D 298                                          
SITE     1 AC9  4 GLY E 180  TYR E 204  HOH E 341  HOH E2972                    
SITE     1 BC1  2 LYS E 270  HIS E 298                                          
SITE     1 BC2  2 GLY E 141  LEU E 143                                          
SITE     1 BC3  4 GLY F 141  LEU F 143  HOH F 339  HOH F 382                    
SITE     1 BC4  3 LYS F 270  HIS F 298  HOH F1605                               
SITE     1 BC5  8 TYR G  91  GLN G 220  PRO G 221  GLU G 224                    
SITE     2 BC5  8 HOH G 328  HOH G 514  HOH G1888  LEU M 135                    
SITE     1 BC6  2 LYS G 270  HIS G 298                                          
SITE     1 BC7  5 GLY G 141  ILE G 142  LEU G 143  HOH G 324                    
SITE     2 BC7  5 HOH G 337                                                     
SITE     1 BC8  2 LYS H 270  HIS H 298                                          
SITE     1 BC9  3 GLY H 141  LEU H 143  HOH H 470                               
SITE     1 CC1  4 GLY I 141  ILE I 142  LEU I 143  HOH I 551                    
SITE     1 CC2  2 LYS I 270  HIS I 298                                          
SITE     1 CC3  3 LYS L 270  HIS L 298  HOH L1110                               
SITE     1 CC4  4 GLY L 141  ILE L 142  LEU L 143  HOH L1364                    
SITE     1 CC5  3 GLY M 141  ILE M 142  LEU M 143                               
SITE     1 CC6  2 LYS M 270  HIS M 298                                          
SITE     1 CC7  3 ASP N 269  LYS N 270  HIS N 298                               
SITE     1 CC8  2 GLY N 141  LEU N 143                                          
CRYST1  144.039   87.205  184.825  90.00 112.87  90.00 P 1 21 1     24          
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      0.006943  0.000000  0.002928        0.00000                         
SCALE2      0.000000  0.011467  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005872        0.00000                         
TER    2545      LEU A 318                                                      
TER    5082      LEU B 318                                                      
TER    7611      LEU C 317                                                      
TER   10148      LEU D 318                                                      
TER   12685      LEU E 318                                                      
TER   15236      THR F 320                                                      
TER   17773      LEU G 318                                                      
TER   20310      LEU H 318                                                      
TER   22847      LEU I 318                                                      
TER   25384      LEU L 318                                                      
TER   27929      LEU M 318                                                      
TER   30474      LEU N 318                                                      
MASTER      473    0   26  168  108    0   28    633650   12   12  300          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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