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LongText Report for: 6igq-pdb

Name Class
6igq-pdb
HEADER    HYDROLASE                               25-SEP-18   6IGQ              
TITLE     CRYSTAL STRUCTURE OF INACTIVE STATE OF S9 PEPTIDASE FROM DEINOCOCCUS  
TITLE    2 RADIODURANS R1 (PMSF TREATED)                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACYL-PEPTIDE HYDROLASE, PUTATIVE;                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS STR. R1;                
SOURCE   3 ORGANISM_TAXID: 243230;                                              
SOURCE   4 STRAIN: R1;                                                          
SOURCE   5 GENE: DR_0165;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: PLYSS;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PST50TR                                   
KEYWDS    SERINE PEPTIDASE, MEROPS S9, POP FAMILY, HYDROLASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.YADAV,V.D.GOYAL,A.KUMAR,R.D.MAKDE                                   
REVDAT   1   14-NOV-18 6IGQ    0                                                
JRNL        AUTH   P.YADAV,V.D.GOYAL,A.KUMAR,R.D.MAKDE                          
JRNL        TITL   CRYSTAL STRUCTURE OF INACTIVE STATE OF S9 PEPTIDASE FROM     
JRNL        TITL 2 DEINOCOCCUS RADIODURANS R1 IN AMMONIUM SULPHATE CONDITION    
JRNL        TITL 3 (CONDITION 3)                                                
JRNL        REF    J.BIOL.CHEM.                               2018              
JRNL        REFN                   ESSN 1083-351X                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.87                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 134499                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6737                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 39.8782 -  7.1334    0.98     4480   232  0.1724 0.1945        
REMARK   3     2  7.1334 -  5.6672    1.00     4373   223  0.1833 0.2150        
REMARK   3     3  5.6672 -  4.9524    1.00     4346   232  0.1540 0.1878        
REMARK   3     4  4.9524 -  4.5002    1.00     4277   272  0.1478 0.1808        
REMARK   3     5  4.5002 -  4.1780    1.00     4277   244  0.1488 0.1743        
REMARK   3     6  4.1780 -  3.9319    1.00     4242   265  0.1640 0.2023        
REMARK   3     7  3.9319 -  3.7352    1.00     4264   235  0.1786 0.1951        
REMARK   3     8  3.7352 -  3.5727    1.00     4272   246  0.1749 0.1935        
REMARK   3     9  3.5727 -  3.4352    1.00     4263   223  0.1878 0.2318        
REMARK   3    10  3.4352 -  3.3168    1.00     4269   206  0.1971 0.2261        
REMARK   3    11  3.3168 -  3.2131    1.00     4243   233  0.2049 0.2364        
REMARK   3    12  3.2131 -  3.1213    1.00     4251   229  0.1995 0.2539        
REMARK   3    13  3.1213 -  3.0391    1.00     4252   217  0.1985 0.2461        
REMARK   3    14  3.0391 -  2.9650    1.00     4257   206  0.2031 0.2262        
REMARK   3    15  2.9650 -  2.8976    1.00     4223   222  0.2022 0.2670        
REMARK   3    16  2.8976 -  2.8360    1.00     4257   220  0.2061 0.2211        
REMARK   3    17  2.8360 -  2.7793    1.00     4276   182  0.2177 0.2510        
REMARK   3    18  2.7793 -  2.7268    1.00     4221   217  0.2098 0.2565        
REMARK   3    19  2.7268 -  2.6781    1.00     4261   215  0.2199 0.2567        
REMARK   3    20  2.6781 -  2.6328    1.00     4263   199  0.2254 0.2544        
REMARK   3    21  2.6328 -  2.5903    1.00     4216   217  0.2214 0.2612        
REMARK   3    22  2.5903 -  2.5505    1.00     4192   224  0.2248 0.2686        
REMARK   3    23  2.5505 -  2.5130    1.00     4254   236  0.2252 0.2908        
REMARK   3    24  2.5130 -  2.4776    1.00     4201   226  0.2282 0.2556        
REMARK   3    25  2.4776 -  2.4441    1.00     4232   207  0.2273 0.2494        
REMARK   3    26  2.4441 -  2.4123    1.00     4262   216  0.2343 0.2654        
REMARK   3    27  2.4123 -  2.3822    1.00     4220   203  0.2434 0.2768        
REMARK   3    28  2.3822 -  2.3535    1.00     4205   208  0.2454 0.2902        
REMARK   3    29  2.3535 -  2.3261    1.00     4202   235  0.2491 0.3009        
REMARK   3    30  2.3261 -  2.3000    1.00     4211   247  0.2549 0.2763        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.070           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006          18795                                  
REMARK   3   ANGLE     :  0.810          25645                                  
REMARK   3   CHIRALITY :  0.051           2695                                  
REMARK   3   PLANARITY :  0.006           3389                                  
REMARK   3   DIHEDRAL  :  3.692          12788                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -16.7989 -22.0786  48.3392              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2220 T22:   0.1981                                     
REMARK   3      T33:   0.2607 T12:  -0.0080                                     
REMARK   3      T13:   0.0030 T23:  -0.0248                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0280 L22:  -0.0243                                     
REMARK   3      L33:   0.1716 L12:  -0.0160                                     
REMARK   3      L13:   0.0483 L23:   0.0061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0225 S12:  -0.0022 S13:  -0.0173                       
REMARK   3      S21:  -0.0025 S22:  -0.0126 S23:  -0.0024                       
REMARK   3      S31:   0.0222 S32:  -0.0393 S33:   0.0353                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6IGQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-OCT-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300009158.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.8-5.3                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : RRCAT INDUS-2                      
REMARK 200  BEAMLINE                       : PX-BL21                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97947                            
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 134697                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.890                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.15700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.99700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5YZM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: CUBIOD CRYSTALS (150-200 MICRON)                             
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17M AMMONIUM SULPHATE, 25.5% PEG       
REMARK 280  4000, 15% GLYCEROL, PH 5.31, MICROBATCH, TEMPERATURE 294K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       59.82900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       97.06500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       64.99450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       97.06500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.82900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       64.99450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10900 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 82820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     SER A    40                                                      
REMARK 465     GLU A    41                                                      
REMARK 465     GLU A    42                                                      
REMARK 465     ASP A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     ALA A    45                                                      
REMARK 465     LYS A    46                                                      
REMARK 465     PRO A    47                                                      
REMARK 465     ASP A    48                                                      
REMARK 465     LYS A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     PHE A    51                                                      
REMARK 465     ALA A    52                                                      
REMARK 465     ARG A    53                                                      
REMARK 465     GLY A    99                                                      
REMARK 465     GLU A   100                                                      
REMARK 465     THR A   145                                                      
REMARK 465     GLU A   146                                                      
REMARK 465     ASP A   147                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     ARG A   149                                                      
REMARK 465     ASP A   150                                                      
REMARK 465     GLU A   151                                                      
REMARK 465     ARG A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     ALA A   155                                                      
REMARK 465     ARG A   156                                                      
REMARK 465     VAL A   157                                                      
REMARK 465     LEU A   158                                                      
REMARK 465     THR A   159                                                      
REMARK 465     ARG A   160                                                      
REMARK 465     PRO A   161                                                      
REMARK 465     VAL A   162                                                      
REMARK 465     TYR A   163                                                      
REMARK 465     ARG A   164                                                      
REMARK 465     ALA A   165                                                      
REMARK 465     ASN A   166                                                      
REMARK 465     GLY A   167                                                      
REMARK 465     ALA A   168                                                      
REMARK 465     ASP A   169                                                      
REMARK 465     TRP A   170                                                      
REMARK 465     LEU A   171                                                      
REMARK 465     PRO A   172                                                      
REMARK 465     GLU A   173                                                      
REMARK 465     ARG A   174                                                      
REMARK 465     ALA A   236                                                      
REMARK 465     ASP A   237                                                      
REMARK 465     ALA A   238                                                      
REMARK 465     PRO A   239                                                      
REMARK 465     ALA A   240                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     SER B    40                                                      
REMARK 465     GLU B    41                                                      
REMARK 465     GLU B    42                                                      
REMARK 465     ASP B    43                                                      
REMARK 465     PRO B    44                                                      
REMARK 465     ALA B    45                                                      
REMARK 465     LYS B    46                                                      
REMARK 465     PRO B    47                                                      
REMARK 465     ASP B    48                                                      
REMARK 465     LYS B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     PHE B    51                                                      
REMARK 465     ALA B    52                                                      
REMARK 465     ARG B    53                                                      
REMARK 465     ALA B    98                                                      
REMARK 465     GLY B    99                                                      
REMARK 465     GLU B   100                                                      
REMARK 465     ALA B   143                                                      
REMARK 465     ASP B   144                                                      
REMARK 465     THR B   145                                                      
REMARK 465     GLU B   146                                                      
REMARK 465     ASP B   147                                                      
REMARK 465     LYS B   148                                                      
REMARK 465     ARG B   149                                                      
REMARK 465     ASP B   150                                                      
REMARK 465     GLU B   151                                                      
REMARK 465     ARG B   152                                                      
REMARK 465     GLY B   153                                                      
REMARK 465     GLU B   154                                                      
REMARK 465     ALA B   155                                                      
REMARK 465     ARG B   156                                                      
REMARK 465     VAL B   157                                                      
REMARK 465     LEU B   158                                                      
REMARK 465     THR B   159                                                      
REMARK 465     ARG B   160                                                      
REMARK 465     PRO B   161                                                      
REMARK 465     VAL B   162                                                      
REMARK 465     TYR B   163                                                      
REMARK 465     ARG B   164                                                      
REMARK 465     ALA B   165                                                      
REMARK 465     ASN B   166                                                      
REMARK 465     GLY B   167                                                      
REMARK 465     ALA B   168                                                      
REMARK 465     ASP B   169                                                      
REMARK 465     TRP B   170                                                      
REMARK 465     LEU B   171                                                      
REMARK 465     PRO B   172                                                      
REMARK 465     GLU B   173                                                      
REMARK 465     ARG B   174                                                      
REMARK 465     ALA B   236                                                      
REMARK 465     ASP B   237                                                      
REMARK 465     ALA B   238                                                      
REMARK 465     PRO B   239                                                      
REMARK 465     ALA B   240                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     ASN C     2                                                      
REMARK 465     ASN C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     SER C    40                                                      
REMARK 465     GLU C    41                                                      
REMARK 465     GLU C    42                                                      
REMARK 465     ASP C    43                                                      
REMARK 465     PRO C    44                                                      
REMARK 465     ALA C    45                                                      
REMARK 465     LYS C    46                                                      
REMARK 465     PRO C    47                                                      
REMARK 465     ASP C    48                                                      
REMARK 465     LYS C    49                                                      
REMARK 465     ASP C    50                                                      
REMARK 465     PHE C    51                                                      
REMARK 465     ALA C    52                                                      
REMARK 465     ARG C    53                                                      
REMARK 465     ALA C    98                                                      
REMARK 465     GLY C    99                                                      
REMARK 465     GLU C   100                                                      
REMARK 465     VAL C   101                                                      
REMARK 465     PHE C   121                                                      
REMARK 465     LYS C   122                                                      
REMARK 465     ASN C   123                                                      
REMARK 465     THR C   142                                                      
REMARK 465     ALA C   143                                                      
REMARK 465     ASP C   144                                                      
REMARK 465     THR C   145                                                      
REMARK 465     GLU C   146                                                      
REMARK 465     ASP C   147                                                      
REMARK 465     LYS C   148                                                      
REMARK 465     ARG C   149                                                      
REMARK 465     ASP C   150                                                      
REMARK 465     GLU C   151                                                      
REMARK 465     ARG C   152                                                      
REMARK 465     GLY C   153                                                      
REMARK 465     GLU C   154                                                      
REMARK 465     ALA C   155                                                      
REMARK 465     ARG C   156                                                      
REMARK 465     VAL C   157                                                      
REMARK 465     LEU C   158                                                      
REMARK 465     THR C   159                                                      
REMARK 465     ARG C   160                                                      
REMARK 465     PRO C   161                                                      
REMARK 465     VAL C   162                                                      
REMARK 465     TYR C   163                                                      
REMARK 465     ARG C   164                                                      
REMARK 465     ALA C   165                                                      
REMARK 465     ASN C   166                                                      
REMARK 465     GLY C   167                                                      
REMARK 465     ALA C   168                                                      
REMARK 465     ASP C   169                                                      
REMARK 465     TRP C   170                                                      
REMARK 465     LEU C   171                                                      
REMARK 465     PRO C   172                                                      
REMARK 465     GLU C   173                                                      
REMARK 465     ARG C   174                                                      
REMARK 465     PRO C   175                                                      
REMARK 465     GLU C   216                                                      
REMARK 465     ASP C   217                                                      
REMARK 465     GLU C   218                                                      
REMARK 465     TRP C   219                                                      
REMARK 465     GLN C   220                                                      
REMARK 465     ALA C   236                                                      
REMARK 465     ASP C   237                                                      
REMARK 465     ALA C   238                                                      
REMARK 465     PRO C   239                                                      
REMARK 465     ALA C   240                                                      
REMARK 465     ALA C   241                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     SER D     1                                                      
REMARK 465     ASN D     2                                                      
REMARK 465     ASN D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     THR D     6                                                      
REMARK 465     SER D    40                                                      
REMARK 465     GLU D    41                                                      
REMARK 465     GLU D    42                                                      
REMARK 465     ASP D    43                                                      
REMARK 465     PRO D    44                                                      
REMARK 465     ALA D    45                                                      
REMARK 465     LYS D    46                                                      
REMARK 465     PRO D    47                                                      
REMARK 465     ASP D    48                                                      
REMARK 465     LYS D    49                                                      
REMARK 465     ASP D    50                                                      
REMARK 465     PHE D    51                                                      
REMARK 465     ALA D    52                                                      
REMARK 465     ARG D    53                                                      
REMARK 465     ALA D    98                                                      
REMARK 465     GLY D    99                                                      
REMARK 465     GLU D   100                                                      
REMARK 465     VAL D   101                                                      
REMARK 465     HIS D   120                                                      
REMARK 465     PHE D   121                                                      
REMARK 465     LYS D   122                                                      
REMARK 465     ASN D   123                                                      
REMARK 465     THR D   142                                                      
REMARK 465     ALA D   143                                                      
REMARK 465     ASP D   144                                                      
REMARK 465     THR D   145                                                      
REMARK 465     GLU D   146                                                      
REMARK 465     ASP D   147                                                      
REMARK 465     LYS D   148                                                      
REMARK 465     ARG D   149                                                      
REMARK 465     ASP D   150                                                      
REMARK 465     GLU D   151                                                      
REMARK 465     ARG D   152                                                      
REMARK 465     GLY D   153                                                      
REMARK 465     GLU D   154                                                      
REMARK 465     ALA D   155                                                      
REMARK 465     ARG D   156                                                      
REMARK 465     VAL D   157                                                      
REMARK 465     LEU D   158                                                      
REMARK 465     THR D   159                                                      
REMARK 465     ARG D   160                                                      
REMARK 465     PRO D   161                                                      
REMARK 465     VAL D   162                                                      
REMARK 465     TYR D   163                                                      
REMARK 465     ARG D   164                                                      
REMARK 465     ALA D   165                                                      
REMARK 465     ASN D   166                                                      
REMARK 465     GLY D   167                                                      
REMARK 465     ALA D   168                                                      
REMARK 465     ASP D   169                                                      
REMARK 465     TRP D   170                                                      
REMARK 465     LEU D   171                                                      
REMARK 465     PRO D   172                                                      
REMARK 465     GLU D   173                                                      
REMARK 465     ARG D   174                                                      
REMARK 465     PRO D   175                                                      
REMARK 465     THR D   235                                                      
REMARK 465     ALA D   236                                                      
REMARK 465     ASP D   237                                                      
REMARK 465     ALA D   238                                                      
REMARK 465     PRO D   239                                                      
REMARK 465     ALA D   240                                                      
REMARK 465     ALA D   241                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  30    CG   CD   CE   NZ                                   
REMARK 470     GLU A  75    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 102    CG   CD   CE   NZ                                   
REMARK 470     LYS A 111    CG   CD   CE   NZ                                   
REMARK 470     LYS A 122    CG   CD   CE   NZ                                   
REMARK 470     GLU A 184    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 187    CG   CD   CE   NZ                                   
REMARK 470     GLN A 223    CG   CD   OE1  NE2                                  
REMARK 470     TRP A 224    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 224    CZ3  CH2                                            
REMARK 470     GLN A 243    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 347    CG   CD   CE   NZ                                   
REMARK 470     GLU A 421    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 554    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  75    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 102    CG   CD   CE   NZ                                   
REMARK 470     LYS B 111    CG   CD   CE   NZ                                   
REMARK 470     LYS B 122    CG   CD   CE   NZ                                   
REMARK 470     GLU B 184    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     GLU B 195    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 216    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 218    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 220    CG   CD   OE1  NE2                                  
REMARK 470     TRP B 224    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 224    CZ3  CH2                                            
REMARK 470     ARG B 225    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 243    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 273    CG   CD   CE   NZ                                   
REMARK 470     LYS B 347    CG   CD   CE   NZ                                   
REMARK 470     GLU B 421    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 507    CG   CD   CE   NZ                                   
REMARK 470     LYS C  30    CD   CE   NZ                                        
REMARK 470     ARG C  69    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 102    CG   CD   CE   NZ                                   
REMARK 470     ARG C 116    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS C 120    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG C 135    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 184    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 187    CG   CD   CE   NZ                                   
REMARK 470     GLU C 195    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 223    CG   CD   OE1  NE2                                  
REMARK 470     TRP C 224    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C 224    CZ3  CH2                                            
REMARK 470     ARG C 225    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 243    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 244    CG   CD   CE   NZ                                   
REMARK 470     LEU C 245    CG   CD1  CD2                                       
REMARK 470     ASP C 247    CG   OD1  OD2                                       
REMARK 470     ARG C 290    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 323    CG   OD1  OD2                                       
REMARK 470     LYS C 347    CE   NZ                                             
REMARK 470     GLU C 364    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 376    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 421    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  30    CG   CD   CE   NZ                                   
REMARK 470     GLU D  64    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  69    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  75    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 102    CG   CD   CE   NZ                                   
REMARK 470     LYS D 111    CG   CD   CE   NZ                                   
REMARK 470     ARG D 116    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 135    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR D 141    OG1  CG2                                            
REMARK 470     TRP D 179    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D 179    CZ3  CH2                                            
REMARK 470     GLU D 184    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 187    CG   CD   CE   NZ                                   
REMARK 470     ARG D 189    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 190    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 195    CG   CD   OE1  OE2                                  
REMARK 470     ILE D 196    CG1  CG2  CD1                                       
REMARK 470     GLU D 216    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 218    CG   CD   OE1  OE2                                  
REMARK 470     TRP D 219    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D 219    CZ3  CH2                                            
REMARK 470     GLN D 220    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 223    CG   CD   OE1  NE2                                  
REMARK 470     TRP D 224    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D 224    CZ3  CH2                                            
REMARK 470     ARG D 225    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D 243    CG   CD   OE1  NE2                                  
REMARK 470     LEU D 245    CG   CD1  CD2                                       
REMARK 470     ASP D 247    CG   OD1  OD2                                       
REMARK 470     GLN D 262    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 273    CG   CD   CE   NZ                                   
REMARK 470     ASN D 286    CG   OD1  ND2                                       
REMARK 470     LYS D 347    CE   NZ                                             
REMARK 470     ARG D 376    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 399    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 421    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 103       87.13   -160.77                                   
REMARK 500    ALA A 143     -130.97     70.35                                   
REMARK 500    GLN A 262      -51.89   -122.03                                   
REMARK 500    ARG A 480       47.68   -150.07                                   
REMARK 500    THR A 483      -91.11   -109.45                                   
REMARK 500    SER A 514     -119.09     60.51                                   
REMARK 500    ALA B 103       88.06   -161.69                                   
REMARK 500    GLN B 262      -54.27   -121.82                                   
REMARK 500    ASP B 293       59.68    -92.13                                   
REMARK 500    ARG B 480       46.66   -149.90                                   
REMARK 500    THR B 483      -92.94   -106.60                                   
REMARK 500    SER B 514     -116.57     60.59                                   
REMARK 500    ALA C 103       89.39   -163.95                                   
REMARK 500    GLN C 262      -55.08   -121.75                                   
REMARK 500    ARG C 480       47.49   -150.66                                   
REMARK 500    THR C 483      -93.89   -107.22                                   
REMARK 500    SER C 514     -117.86     59.36                                   
REMARK 500    ALA D 103       88.33   -168.13                                   
REMARK 500    GLN D 262      -52.44   -120.88                                   
REMARK 500    ARG D 480       47.91   -151.91                                   
REMARK 500    THR D 483      -93.98   -106.21                                   
REMARK 500    SER D 514     -118.46     59.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C1040        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH C1041        DISTANCE =  6.77 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 704                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5YZM   RELATED DB: PDB                                   
REMARK 900 5YZM CONTAINS THE SAME PROTEIN CRYSTALLIZED IN DIFFERENT             
REMARK 900 CRYSTALLIZATION CONDITION                                            
DBREF  6IGQ A    2   655  UNP    Q9RXY9   Q9RXY9_DEIRA     2    655             
DBREF  6IGQ B    2   655  UNP    Q9RXY9   Q9RXY9_DEIRA     2    655             
DBREF  6IGQ C    2   655  UNP    Q9RXY9   Q9RXY9_DEIRA     2    655             
DBREF  6IGQ D    2   655  UNP    Q9RXY9   Q9RXY9_DEIRA     2    655             
SEQADV 6IGQ GLY A    0  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 6IGQ SER A    1  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 6IGQ GLY B    0  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 6IGQ SER B    1  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 6IGQ GLY C    0  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 6IGQ SER C    1  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 6IGQ GLY D    0  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 6IGQ SER D    1  UNP  Q9RXY9              EXPRESSION TAG                 
SEQRES   1 A  656  GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP          
SEQRES   2 A  656  SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL          
SEQRES   3 A  656  SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN          
SEQRES   4 A  656  ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE          
SEQRES   5 A  656  ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU          
SEQRES   6 A  656  GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY          
SEQRES   7 A  656  ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN          
SEQRES   8 A  656  ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA          
SEQRES   9 A  656  ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG          
SEQRES  10 A  656  ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN          
SEQRES  11 A  656  TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR          
SEQRES  12 A  656  ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA          
SEQRES  13 A  656  ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA          
SEQRES  14 A  656  ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR          
SEQRES  15 A  656  ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO          
SEQRES  16 A  656  GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER          
SEQRES  17 A  656  ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN          
SEQRES  18 A  656  ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU          
SEQRES  19 A  656  PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU          
SEQRES  20 A  656  ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO          
SEQRES  21 A  656  ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY          
SEQRES  22 A  656  LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU          
SEQRES  23 A  656  ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS          
SEQRES  24 A  656  PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY          
SEQRES  25 A  656  ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR          
SEQRES  26 A  656  LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU          
SEQRES  27 A  656  PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP          
SEQRES  28 A  656  HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN          
SEQRES  29 A  656  GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG          
SEQRES  30 A  656  PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP          
SEQRES  31 A  656  LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN          
SEQRES  32 A  656  ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY          
SEQRES  33 A  656  TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA          
SEQRES  34 A  656  LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY          
SEQRES  35 A  656  HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG          
SEQRES  36 A  656  GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL          
SEQRES  37 A  656  GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG          
SEQRES  38 A  656  TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE          
SEQRES  39 A  656  ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA          
SEQRES  40 A  656  LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET          
SEQRES  41 A  656  THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA          
SEQRES  42 A  656  ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE          
SEQRES  43 A  656  GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP          
SEQRES  44 A  656  GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU          
SEQRES  45 A  656  LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN          
SEQRES  46 A  656  VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP          
SEQRES  47 A  656  HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA          
SEQRES  48 A  656  ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG          
SEQRES  49 A  656  PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG          
SEQRES  50 A  656  PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA          
SEQRES  51 A  656  TRP LEU GLU ARG TRP LEU                                      
SEQRES   1 B  656  GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP          
SEQRES   2 B  656  SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL          
SEQRES   3 B  656  SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN          
SEQRES   4 B  656  ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE          
SEQRES   5 B  656  ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU          
SEQRES   6 B  656  GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY          
SEQRES   7 B  656  ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN          
SEQRES   8 B  656  ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA          
SEQRES   9 B  656  ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG          
SEQRES  10 B  656  ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN          
SEQRES  11 B  656  TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR          
SEQRES  12 B  656  ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA          
SEQRES  13 B  656  ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA          
SEQRES  14 B  656  ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR          
SEQRES  15 B  656  ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO          
SEQRES  16 B  656  GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER          
SEQRES  17 B  656  ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN          
SEQRES  18 B  656  ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU          
SEQRES  19 B  656  PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU          
SEQRES  20 B  656  ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO          
SEQRES  21 B  656  ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY          
SEQRES  22 B  656  LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU          
SEQRES  23 B  656  ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS          
SEQRES  24 B  656  PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY          
SEQRES  25 B  656  ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR          
SEQRES  26 B  656  LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU          
SEQRES  27 B  656  PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP          
SEQRES  28 B  656  HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN          
SEQRES  29 B  656  GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG          
SEQRES  30 B  656  PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP          
SEQRES  31 B  656  LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN          
SEQRES  32 B  656  ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY          
SEQRES  33 B  656  TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA          
SEQRES  34 B  656  LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY          
SEQRES  35 B  656  HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG          
SEQRES  36 B  656  GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL          
SEQRES  37 B  656  GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG          
SEQRES  38 B  656  TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE          
SEQRES  39 B  656  ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA          
SEQRES  40 B  656  LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET          
SEQRES  41 B  656  THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA          
SEQRES  42 B  656  ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE          
SEQRES  43 B  656  GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP          
SEQRES  44 B  656  GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU          
SEQRES  45 B  656  LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN          
SEQRES  46 B  656  VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP          
SEQRES  47 B  656  HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA          
SEQRES  48 B  656  ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG          
SEQRES  49 B  656  PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG          
SEQRES  50 B  656  PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA          
SEQRES  51 B  656  TRP LEU GLU ARG TRP LEU                                      
SEQRES   1 C  656  GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP          
SEQRES   2 C  656  SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL          
SEQRES   3 C  656  SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN          
SEQRES   4 C  656  ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE          
SEQRES   5 C  656  ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU          
SEQRES   6 C  656  GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY          
SEQRES   7 C  656  ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN          
SEQRES   8 C  656  ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA          
SEQRES   9 C  656  ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG          
SEQRES  10 C  656  ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN          
SEQRES  11 C  656  TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR          
SEQRES  12 C  656  ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA          
SEQRES  13 C  656  ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA          
SEQRES  14 C  656  ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR          
SEQRES  15 C  656  ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO          
SEQRES  16 C  656  GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER          
SEQRES  17 C  656  ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN          
SEQRES  18 C  656  ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU          
SEQRES  19 C  656  PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU          
SEQRES  20 C  656  ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO          
SEQRES  21 C  656  ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY          
SEQRES  22 C  656  LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU          
SEQRES  23 C  656  ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS          
SEQRES  24 C  656  PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY          
SEQRES  25 C  656  ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR          
SEQRES  26 C  656  LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU          
SEQRES  27 C  656  PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP          
SEQRES  28 C  656  HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN          
SEQRES  29 C  656  GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG          
SEQRES  30 C  656  PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP          
SEQRES  31 C  656  LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN          
SEQRES  32 C  656  ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY          
SEQRES  33 C  656  TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA          
SEQRES  34 C  656  LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY          
SEQRES  35 C  656  HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG          
SEQRES  36 C  656  GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL          
SEQRES  37 C  656  GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG          
SEQRES  38 C  656  TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE          
SEQRES  39 C  656  ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA          
SEQRES  40 C  656  LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET          
SEQRES  41 C  656  THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA          
SEQRES  42 C  656  ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE          
SEQRES  43 C  656  GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP          
SEQRES  44 C  656  GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU          
SEQRES  45 C  656  LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN          
SEQRES  46 C  656  VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP          
SEQRES  47 C  656  HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA          
SEQRES  48 C  656  ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG          
SEQRES  49 C  656  PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG          
SEQRES  50 C  656  PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA          
SEQRES  51 C  656  TRP LEU GLU ARG TRP LEU                                      
SEQRES   1 D  656  GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP          
SEQRES   2 D  656  SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL          
SEQRES   3 D  656  SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN          
SEQRES   4 D  656  ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE          
SEQRES   5 D  656  ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU          
SEQRES   6 D  656  GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY          
SEQRES   7 D  656  ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN          
SEQRES   8 D  656  ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA          
SEQRES   9 D  656  ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG          
SEQRES  10 D  656  ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN          
SEQRES  11 D  656  TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR          
SEQRES  12 D  656  ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA          
SEQRES  13 D  656  ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA          
SEQRES  14 D  656  ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR          
SEQRES  15 D  656  ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO          
SEQRES  16 D  656  GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER          
SEQRES  17 D  656  ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN          
SEQRES  18 D  656  ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU          
SEQRES  19 D  656  PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU          
SEQRES  20 D  656  ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO          
SEQRES  21 D  656  ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY          
SEQRES  22 D  656  LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU          
SEQRES  23 D  656  ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS          
SEQRES  24 D  656  PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY          
SEQRES  25 D  656  ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR          
SEQRES  26 D  656  LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU          
SEQRES  27 D  656  PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP          
SEQRES  28 D  656  HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN          
SEQRES  29 D  656  GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG          
SEQRES  30 D  656  PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP          
SEQRES  31 D  656  LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN          
SEQRES  32 D  656  ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY          
SEQRES  33 D  656  TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA          
SEQRES  34 D  656  LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY          
SEQRES  35 D  656  HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG          
SEQRES  36 D  656  GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL          
SEQRES  37 D  656  GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG          
SEQRES  38 D  656  TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE          
SEQRES  39 D  656  ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA          
SEQRES  40 D  656  LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET          
SEQRES  41 D  656  THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA          
SEQRES  42 D  656  ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE          
SEQRES  43 D  656  GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP          
SEQRES  44 D  656  GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU          
SEQRES  45 D  656  LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN          
SEQRES  46 D  656  VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP          
SEQRES  47 D  656  HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA          
SEQRES  48 D  656  ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG          
SEQRES  49 D  656  PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG          
SEQRES  50 D  656  PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA          
SEQRES  51 D  656  TRP LEU GLU ARG TRP LEU                                      
HET    GOL  A 701       6                                                       
HET    GOL  A 702       6                                                       
HET    GOL  A 703       6                                                       
HET    SO4  A 704       5                                                       
HET    GOL  B 701       6                                                       
HET    GOL  B 702       6                                                       
HET    GOL  B 703       6                                                       
HET    SO4  B 704       5                                                       
HET    GOL  C 701       6                                                       
HET    GOL  C 702       6                                                       
HET    SO4  C 703       5                                                       
HET    GOL  D 701       6                                                       
HET    GOL  D 702       6                                                       
HET    GOL  D 703       6                                                       
HET    SO4  D 704       5                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    11(C3 H8 O3)                                                 
FORMUL   8  SO4    4(O4 S 2-)                                                   
FORMUL  20  HOH   *992(H2 O)                                                    
HELIX    1 AA1 GLY A   10  LEU A   17  5                                   8    
HELIX    2 AA2 ASP A  217  GLN A  223  1                                   7    
HELIX    3 AA3 LEU A  390  PHE A  394  5                                   5    
HELIX    4 AA4 THR A  445  ARG A  454  1                                  10    
HELIX    5 AA5 GLY A  470  ALA A  476  1                                   7    
HELIX    6 AA6 THR A  483  VAL A  500  1                                  18    
HELIX    7 AA7 SER A  514  GLY A  525  1                                  12    
HELIX    8 AA8 ASN A  541  SER A  549  1                                   9    
HELIX    9 AA9 ILE A  551  GLY A  561  1                                  11    
HELIX   10 AB1 ARG A  566  LEU A  576  1                                  11    
HELIX   11 AB2 SER A  577  VAL A  585  5                                   9    
HELIX   12 AB3 VAL A  602  HIS A  615  1                                  14    
HELIX   13 AB4 HIS A  629  GLY A  635  1                                   7    
HELIX   14 AB5 PRO A  637  LEU A  655  1                                  19    
HELIX   15 AB6 GLY B   10  LEU B   17  5                                   8    
HELIX   16 AB7 ASP B  217  GLN B  223  1                                   7    
HELIX   17 AB8 LEU B  390  PHE B  394  5                                   5    
HELIX   18 AB9 THR B  445  ARG B  454  1                                  10    
HELIX   19 AC1 GLY B  470  ALA B  476  1                                   7    
HELIX   20 AC2 THR B  483  VAL B  500  1                                  18    
HELIX   21 AC3 SER B  514  GLY B  525  1                                  12    
HELIX   22 AC4 ASN B  541  SER B  549  1                                   9    
HELIX   23 AC5 ILE B  551  GLY B  561  1                                  11    
HELIX   24 AC6 ARG B  566  LEU B  576  1                                  11    
HELIX   25 AC7 SER B  577  VAL B  585  5                                   9    
HELIX   26 AC8 VAL B  602  HIS B  615  1                                  14    
HELIX   27 AC9 HIS B  629  GLY B  635  1                                   7    
HELIX   28 AD1 PRO B  637  LEU B  655  1                                  19    
HELIX   29 AD2 GLY C   10  LEU C   17  5                                   8    
HELIX   30 AD3 LEU C  390  PHE C  394  5                                   5    
HELIX   31 AD4 THR C  445  ARG C  454  1                                  10    
HELIX   32 AD5 GLY C  470  ALA C  476  1                                   7    
HELIX   33 AD6 THR C  483  VAL C  500  1                                  18    
HELIX   34 AD7 SER C  514  GLY C  525  1                                  12    
HELIX   35 AD8 ASN C  541  SER C  549  1                                   9    
HELIX   36 AD9 ILE C  551  GLY C  561  1                                  11    
HELIX   37 AE1 ARG C  566  LEU C  576  1                                  11    
HELIX   38 AE2 SER C  577  VAL C  585  5                                   9    
HELIX   39 AE3 VAL C  602  HIS C  615  1                                  14    
HELIX   40 AE4 HIS C  629  GLY C  635  1                                   7    
HELIX   41 AE5 PRO C  637  LEU C  655  1                                  19    
HELIX   42 AE6 GLY D   10  LEU D   17  5                                   8    
HELIX   43 AE7 ASP D  217  GLN D  223  1                                   7    
HELIX   44 AE8 LEU D  390  PHE D  394  5                                   5    
HELIX   45 AE9 THR D  445  ARG D  454  1                                  10    
HELIX   46 AF1 GLY D  470  ALA D  476  1                                   7    
HELIX   47 AF2 THR D  483  VAL D  500  1                                  18    
HELIX   48 AF3 SER D  514  GLY D  525  1                                  12    
HELIX   49 AF4 ASN D  541  SER D  549  1                                   9    
HELIX   50 AF5 ILE D  551  GLY D  561  1                                  11    
HELIX   51 AF6 ARG D  566  LEU D  576  1                                  11    
HELIX   52 AF7 SER D  577  VAL D  585  5                                   9    
HELIX   53 AF8 VAL D  602  HIS D  615  1                                  14    
HELIX   54 AF9 HIS D  629  GLY D  635  1                                   7    
HELIX   55 AG1 PRO D  637  LEU D  655  1                                  19    
SHEET    1 AA1 4 PHE A  19  VAL A  25  0                                        
SHEET    2 AA1 4 VAL A  32  GLN A  38 -1  O  VAL A  35   N  SER A  21           
SHEET    3 AA1 4 ARG A  57  SER A  63 -1  O  TRP A  61   N  PHE A  34           
SHEET    4 AA1 4 ARG A  69  PRO A  70 -1  O  ARG A  69   N  LEU A  62           
SHEET    1 AA2 4 GLY A  79  TRP A  85  0                                        
SHEET    2 AA2 4 ASN A  91  SER A  97 -1  O  VAL A  95   N  SER A  81           
SHEET    3 AA2 4 ALA A 104  PRO A 109 -1  O  MET A 106   N  PHE A  94           
SHEET    4 AA2 4 ARG A 116  ARG A 117 -1  O  ARG A 116   N  LEU A 107           
SHEET    1 AA3 4 VAL A 125  TRP A 130  0                                        
SHEET    2 AA3 4 PHE A 136  THR A 141 -1  O  ALA A 138   N  GLN A 129           
SHEET    3 AA3 4 ALA A 177  ASP A 182 -1  O  TRP A 179   N  PHE A 139           
SHEET    4 AA3 4 LYS A 187  TYR A 192 -1  O  LYS A 187   N  ASP A 182           
SHEET    1 AA4 4 LEU A 201  TRP A 203  0                                        
SHEET    2 AA4 4 GLY A 209  GLN A 214 -1  O  LEU A 211   N  SER A 202           
SHEET    3 AA4 4 GLN A 226  PRO A 232 -1  O  TYR A 229   N  ILE A 212           
SHEET    4 AA4 4 GLN A 243  SER A 250 -1  O  GLN A 243   N  ASP A 230           
SHEET    1 AA5 4 ALA A 252  PRO A 257  0                                        
SHEET    2 AA5 4 PHE A 264  GLY A 268 -1  O  ALA A 265   N  ALA A 256           
SHEET    3 AA5 4 HIS A 280  GLU A 285 -1  O  ILE A 284   N  PHE A 264           
SHEET    4 AA5 4 GLN A 288  ARG A 291 -1  O  ARG A 290   N  LEU A 283           
SHEET    1 AA6 4 ARG A 318  TRP A 319  0                                        
SHEET    2 AA6 4 THR A 324  VAL A 331 -1  O  LEU A 326   N  ARG A 318           
SHEET    3 AA6 4 SER A 334  HIS A 341 -1  O  PHE A 338   N  PHE A 327           
SHEET    4 AA6 4 GLY A 344  ASP A 350 -1  O  ASP A 350   N  LEU A 337           
SHEET    1 AA7 4 GLY A 355  ASN A 363  0                                        
SHEET    2 AA7 4 GLY A 366  SER A 373 -1  O  GLU A 372   N  VAL A 356           
SHEET    3 AA7 4 ARG A 376  LEU A 382 -1  O  GLU A 381   N  LEU A 369           
SHEET    4 AA7 4 GLN A 385  ARG A 386 -1  O  GLN A 385   N  LEU A 382           
SHEET    1 AA8 8 GLN A 402  PHE A 406  0                                        
SHEET    2 AA8 8 GLY A 413  LEU A 418 -1  O  GLY A 413   N  PHE A 406           
SHEET    3 AA8 8 GLY A 457  SER A 461 -1  O  TYR A 460   N  TRP A 416           
SHEET    4 AA8 8 VAL A 426  ILE A 432  1  N  PRO A 427   O  GLY A 457           
SHEET    5 AA8 8 LEU A 503  GLY A 513  1  O  ALA A 509   N  LEU A 430           
SHEET    6 AA8 8 ALA A 532  ASP A 536  1  O  ASP A 536   N  GLY A 512           
SHEET    7 AA8 8 THR A 589  SER A 594  1  O  LEU A 590   N  THR A 535           
SHEET    8 AA8 8 VAL A 619  PHE A 624  1  O  ARG A 620   N  ILE A 591           
SHEET    1 AA9 4 PHE B  19  VAL B  25  0                                        
SHEET    2 AA9 4 VAL B  32  GLN B  38 -1  O  ALA B  33   N  GLN B  24           
SHEET    3 AA9 4 ARG B  57  SER B  63 -1  O  TRP B  61   N  PHE B  34           
SHEET    4 AA9 4 ARG B  69  PRO B  70 -1  O  ARG B  69   N  LEU B  62           
SHEET    1 AB1 4 GLY B  79  TRP B  85  0                                        
SHEET    2 AB1 4 ASN B  91  SER B  97 -1  O  ALA B  93   N  ARG B  84           
SHEET    3 AB1 4 ALA B 104  PRO B 109 -1  O  MET B 106   N  PHE B  94           
SHEET    4 AB1 4 ARG B 116  ARG B 117 -1  O  ARG B 116   N  LEU B 107           
SHEET    1 AB2 4 VAL B 125  TRP B 130  0                                        
SHEET    2 AB2 4 PHE B 136  THR B 141 -1  O  ALA B 138   N  GLN B 129           
SHEET    3 AB2 4 ALA B 177  ASP B 182 -1  O  TRP B 179   N  PHE B 139           
SHEET    4 AB2 4 LYS B 187  TYR B 192 -1  O  TYR B 192   N  LEU B 178           
SHEET    1 AB3 4 LEU B 201  TRP B 203  0                                        
SHEET    2 AB3 4 GLY B 209  GLN B 214 -1  O  LEU B 211   N  SER B 202           
SHEET    3 AB3 4 GLN B 226  PRO B 232 -1  O  TYR B 229   N  ILE B 212           
SHEET    4 AB3 4 GLN B 243  SER B 250 -1  O  GLN B 243   N  ASP B 230           
SHEET    1 AB4 4 ALA B 252  PRO B 257  0                                        
SHEET    2 AB4 4 PHE B 264  GLY B 268 -1  O  ILE B 267   N  HIS B 253           
SHEET    3 AB4 4 HIS B 280  GLU B 285 -1  O  ILE B 284   N  PHE B 264           
SHEET    4 AB4 4 GLN B 288  ARG B 291 -1  O  ARG B 290   N  LEU B 283           
SHEET    1 AB5 4 ARG B 318  TRP B 319  0                                        
SHEET    2 AB5 4 THR B 324  VAL B 331 -1  O  LEU B 326   N  ARG B 318           
SHEET    3 AB5 4 SER B 334  HIS B 341 -1  O  PHE B 338   N  PHE B 327           
SHEET    4 AB5 4 VAL B 346  ASP B 350 -1  O  ASP B 350   N  LEU B 337           
SHEET    1 AB6 4 VAL B 356  ALA B 362  0                                        
SHEET    2 AB6 4 VAL B 367  SER B 373 -1  O  GLU B 372   N  VAL B 356           
SHEET    3 AB6 4 ARG B 376  LEU B 382 -1  O  GLU B 381   N  LEU B 369           
SHEET    4 AB6 4 GLN B 385  ARG B 386 -1  O  GLN B 385   N  LEU B 382           
SHEET    1 AB7 8 GLN B 402  PHE B 406  0                                        
SHEET    2 AB7 8 GLY B 413  LEU B 418 -1  O  GLY B 413   N  PHE B 406           
SHEET    3 AB7 8 GLY B 457  SER B 461 -1  O  TYR B 460   N  TRP B 416           
SHEET    4 AB7 8 VAL B 426  ILE B 432  1  N  PRO B 427   O  GLY B 457           
SHEET    5 AB7 8 LEU B 503  GLY B 513  1  O  ALA B 509   N  LEU B 430           
SHEET    6 AB7 8 ALA B 532  ASP B 536  1  O  ASP B 536   N  GLY B 512           
SHEET    7 AB7 8 THR B 589  SER B 594  1  O  LEU B 590   N  THR B 535           
SHEET    8 AB7 8 VAL B 619  PHE B 624  1  O  VAL B 622   N  ILE B 591           
SHEET    1 AB8 4 PHE C  19  VAL C  25  0                                        
SHEET    2 AB8 4 VAL C  32  GLN C  38 -1  O  ALA C  33   N  GLN C  24           
SHEET    3 AB8 4 ARG C  57  SER C  63 -1  O  TRP C  61   N  PHE C  34           
SHEET    4 AB8 4 ARG C  69  PRO C  70 -1  O  ARG C  69   N  LEU C  62           
SHEET    1 AB9 4 GLY C  79  TRP C  85  0                                        
SHEET    2 AB9 4 ASN C  91  SER C  97 -1  O  ALA C  93   N  ARG C  84           
SHEET    3 AB9 4 ALA C 104  PRO C 109 -1  O  MET C 106   N  PHE C  94           
SHEET    4 AB9 4 ARG C 116  ARG C 117 -1  O  ARG C 116   N  LEU C 107           
SHEET    1 AC1 4 SER C 126  TRP C 130  0                                        
SHEET    2 AC1 4 PHE C 136  THR C 140 -1  O  ALA C 138   N  GLN C 129           
SHEET    3 AC1 4 LEU C 178  ASP C 182 -1  O  TRP C 179   N  PHE C 139           
SHEET    4 AC1 4 LYS C 187  TYR C 192 -1  O  TYR C 192   N  LEU C 178           
SHEET    1 AC2 4 LEU C 201  TRP C 203  0                                        
SHEET    2 AC2 4 GLY C 209  GLN C 214 -1  O  LEU C 211   N  SER C 202           
SHEET    3 AC2 4 GLN C 226  PRO C 232 -1  O  TYR C 229   N  ILE C 212           
SHEET    4 AC2 4 GLN C 243  SER C 250 -1  O  GLN C 243   N  ASP C 230           
SHEET    1 AC3 4 ALA C 252  PRO C 257  0                                        
SHEET    2 AC3 4 PHE C 264  GLY C 268 -1  O  ILE C 267   N  HIS C 253           
SHEET    3 AC3 4 HIS C 280  GLU C 285 -1  O  ILE C 284   N  PHE C 264           
SHEET    4 AC3 4 GLN C 288  ARG C 291 -1  O  GLN C 288   N  GLU C 285           
SHEET    1 AC4 4 ARG C 318  TRP C 319  0                                        
SHEET    2 AC4 4 THR C 324  VAL C 331 -1  O  LEU C 326   N  ARG C 318           
SHEET    3 AC4 4 SER C 334  HIS C 341 -1  O  PHE C 338   N  PHE C 327           
SHEET    4 AC4 4 VAL C 346  ASP C 350 -1  O  ASP C 350   N  LEU C 337           
SHEET    1 AC5 4 GLY C 355  ALA C 362  0                                        
SHEET    2 AC5 4 VAL C 367  SER C 373 -1  O  GLU C 372   N  VAL C 356           
SHEET    3 AC5 4 ARG C 376  LEU C 382 -1  O  GLU C 381   N  LEU C 369           
SHEET    4 AC5 4 GLN C 385  ARG C 386 -1  O  GLN C 385   N  LEU C 382           
SHEET    1 AC6 8 GLN C 402  THR C 408  0                                        
SHEET    2 AC6 8 GLY C 411  LEU C 418 -1  O  GLY C 413   N  PHE C 406           
SHEET    3 AC6 8 GLY C 457  SER C 461 -1  O  TYR C 460   N  TRP C 416           
SHEET    4 AC6 8 VAL C 426  ILE C 432  1  N  PRO C 427   O  GLY C 457           
SHEET    5 AC6 8 LEU C 503  GLY C 513  1  O  ALA C 509   N  LEU C 430           
SHEET    6 AC6 8 ALA C 532  ASP C 536  1  O  ASP C 536   N  GLY C 512           
SHEET    7 AC6 8 THR C 589  SER C 594  1  O  LEU C 590   N  THR C 535           
SHEET    8 AC6 8 VAL C 619  PHE C 624  1  O  ARG C 620   N  ILE C 591           
SHEET    1 AC7 4 PHE D  19  VAL D  25  0                                        
SHEET    2 AC7 4 VAL D  32  GLN D  38 -1  O  ALA D  33   N  GLN D  24           
SHEET    3 AC7 4 ARG D  57  SER D  63 -1  O  ARG D  57   N  GLN D  38           
SHEET    4 AC7 4 ARG D  69  PRO D  70 -1  O  ARG D  69   N  LEU D  62           
SHEET    1 AC8 4 ASP D  80  TRP D  85  0                                        
SHEET    2 AC8 4 ASN D  91  ARG D  96 -1  O  ALA D  93   N  ARG D  84           
SHEET    3 AC8 4 ALA D 104  PRO D 109 -1  O  MET D 106   N  PHE D  94           
SHEET    4 AC8 4 ARG D 116  ARG D 117 -1  O  ARG D 116   N  LEU D 107           
SHEET    1 AC9 4 SER D 126  TRP D 130  0                                        
SHEET    2 AC9 4 PHE D 136  THR D 140 -1  O  ALA D 138   N  GLN D 129           
SHEET    3 AC9 4 LEU D 178  ASP D 182 -1  O  TRP D 179   N  PHE D 139           
SHEET    4 AC9 4 LYS D 187  TYR D 192 -1  O  ARG D 189   N  LEU D 180           
SHEET    1 AD1 4 LEU D 201  TRP D 203  0                                        
SHEET    2 AD1 4 GLY D 209  GLN D 214 -1  O  LEU D 211   N  SER D 202           
SHEET    3 AD1 4 GLN D 226  PRO D 232 -1  O  TYR D 229   N  ILE D 212           
SHEET    4 AD1 4 GLN D 243  SER D 250 -1  O  GLN D 243   N  ASP D 230           
SHEET    1 AD2 4 ALA D 252  PRO D 257  0                                        
SHEET    2 AD2 4 PHE D 264  GLY D 268 -1  O  ALA D 265   N  ALA D 256           
SHEET    3 AD2 4 HIS D 280  GLU D 285 -1  O  ILE D 284   N  PHE D 264           
SHEET    4 AD2 4 GLN D 288  ARG D 291 -1  O  GLN D 288   N  GLU D 285           
SHEET    1 AD3 4 ARG D 318  TRP D 319  0                                        
SHEET    2 AD3 4 THR D 324  VAL D 331 -1  O  LEU D 326   N  ARG D 318           
SHEET    3 AD3 4 SER D 334  HIS D 341 -1  O  PHE D 338   N  PHE D 327           
SHEET    4 AD3 4 VAL D 346  ASP D 350 -1  O  ASP D 350   N  LEU D 337           
SHEET    1 AD4 4 GLY D 355  ALA D 362  0                                        
SHEET    2 AD4 4 VAL D 367  SER D 373 -1  O  GLU D 372   N  VAL D 356           
SHEET    3 AD4 4 ARG D 376  LEU D 382 -1  O  GLU D 381   N  LEU D 369           
SHEET    4 AD4 4 GLN D 385  ARG D 386 -1  O  GLN D 385   N  LEU D 382           
SHEET    1 AD5 8 GLN D 402  THR D 408  0                                        
SHEET    2 AD5 8 GLY D 411  LEU D 418 -1  O  GLY D 413   N  PHE D 406           
SHEET    3 AD5 8 GLY D 457  SER D 461 -1  O  TYR D 460   N  TRP D 416           
SHEET    4 AD5 8 VAL D 426  ILE D 432  1  N  PRO D 427   O  GLY D 457           
SHEET    5 AD5 8 LEU D 503  GLY D 513  1  O  ALA D 509   N  LEU D 430           
SHEET    6 AD5 8 ALA D 532  ASP D 536  1  O  ASP D 536   N  GLY D 512           
SHEET    7 AD5 8 THR D 589  SER D 594  1  O  LEU D 590   N  THR D 535           
SHEET    8 AD5 8 VAL D 619  PHE D 624  1  O  ARG D 620   N  ILE D 591           
CISPEP   1 GLY A  435    PRO A  436          0         7.83                     
CISPEP   2 GLY B  435    PRO B  436          0         7.56                     
CISPEP   3 GLY C  435    PRO C  436          0         5.98                     
CISPEP   4 GLY D  435    PRO D  436          0         7.15                     
SITE     1 AC1  7 TYR A 349  ASP A 350  GLU A 381  ASN A 383                    
SITE     2 AC1  7 GLY A 384  HOH A 815  HOH D 803                               
SITE     1 AC2  6 ALA A 374  GLY A 443  THR A 445  PHE A 448                    
SITE     2 AC2  6 GLN A 449  TYR A 460                                          
SITE     1 AC3  6 GLY A 435  SER A 514  ARG A 537  PHE A 555                    
SITE     2 AC3  6 ARG A 599  CYS A 600                                          
SITE     1 AC4 10 ASN A 628  HIS A 629  GLU A 630  LEU A 631                    
SITE     2 AC4 10 ARG A 639  ARG A 640  HOH A 820  HOH A 881                    
SITE     3 AC4 10 HOH A 948  HOH A 974                                          
SITE     1 AC5  9 TYR B 349  ASP B 350  VAL B 367  LEU B 369                    
SITE     2 AC5  9 GLU B 381  ASN B 383  GLY B 384  HOH B 808                    
SITE     3 AC5  9 ARG C 566                                                     
SITE     1 AC6  6 GLU B 400  VAL B 417  LEU B 419  HOH B 809                    
SITE     2 AC6  6 GLU C 409  ARG C 480                                          
SITE     1 AC7  6 ALA B 374  GLY B 443  THR B 445  PHE B 448                    
SITE     2 AC7  6 GLN B 449  TYR B 460                                          
SITE     1 AC8  9 HIS B 629  GLU B 630  LEU B 631  ARG B 639                    
SITE     2 AC8  9 ARG B 640  HOH B 816  HOH B 826  HOH B 848                    
SITE     3 AC8  9 HOH B 882                                                     
SITE     1 AC9  7 ALA C 374  GLY C 441  GLY C 443  THR C 445                    
SITE     2 AC9  7 PHE C 448  GLN C 449  TYR C 460                               
SITE     1 AD1  5 ARG C 332  LEU C 410  GLU C 412  TYR C 469                    
SITE     2 AD1  5 TRP C 473                                                     
SITE     1 AD2  8 HIS C 629  GLU C 630  LEU C 631  ARG C 640                    
SITE     2 AD2  8 HOH C 812  HOH C 871  HOH C 896  HOH C 948                    
SITE     1 AD3  7 ARG A 399  GLU A 400  VAL A 417  LEU A 418                    
SITE     2 AD3  7 LEU A 419  GLU D 409  ARG D 480                               
SITE     1 AD4  4 GLY A 411  GLU A 412  TYR D 282  ARG D 291                    
SITE     1 AD5  6 LEU A 571  LEU D 571  ASP D 575  GLN D 580                    
SITE     2 AD5  6 HOH D 820  HOH D 828                                          
SITE     1 AD6  7 HIS D 629  GLU D 630  LEU D 631  ARG D 640                    
SITE     2 AD6  7 HOH D 812  HOH D 870  HOH D 890                               
CRYST1  119.658  129.989  194.130  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008357  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007693  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005151        0.00000                         
TER    4650      LEU A 655                                                      
TER    9261      LEU B 655                                                      
TER   13729      LEU C 655                                                      
TER   18176      LEU D 655                                                      
MASTER      724    0   15   55  144    0   32    619224    4   86  204          
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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