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LongText Report for: 4QA9-pdb

Name Class
4QA9-pdb
HEADER    HYDROLASE                               02-MAY-14   4QA9              
TITLE     ENSEMBLE REFINEMENT OF AN EPOXIDE HYDROLASE FROM STREPTOMYCES         
TITLE    2 CARZINOSTATICUS SUBSP. NEOCARZINOSTATICUS.                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPOXIDE HYDROLASE;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES CARZINOSTATICUS SUBSP.             
SOURCE   3 NEOCARZINOSTATICUS;                                                  
SOURCE   4 ORGANISM_TAXID: 167636;                                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR 
KEYWDS   2 STRUCTURAL GENOMICS, MCSG, ENZYME DISCOVERY FOR NATURAL PRODUCT      
KEYWDS   3 BIOSYNTHESIS, NATPRO, EPOXIDE HYDROLASE, PSI-BIOLOGY, HYDROLASE      
EXPDTA    X-RAY DIFFRACTION                                                     
NUMMDL    20                                                                    
AUTHOR    F.WANG,K.TAN,L.BIGELOW,S.CLANCY,G.BABNIGG,C.A.BINGMAN,R.YENNAMALLI,   
AUTHOR   2 J.LOHMAN,M.MA,B.SHEN,A.JOACHIMIAK,G.N.PHILLIPS JR.,MIDWEST CENTER    
AUTHOR   3 FOR STRUCTURAL GENOMICS (MCSG),ENZYME DISCOVERY FOR NATURAL PRODUCT  
AUTHOR   4 BIOSYNTHESIS (NATPRO)                                                
REVDAT   1   21-MAY-14 4QA9    0                                                
JRNL        AUTH   F.WANG,K.TAN,L.BIGELOW,S.CLANCY,G.BABNIGG,C.A.BINGMAN,       
JRNL        AUTH 2 R.YENNAMALLI,J.LOHMAN,M.MA,B.SHEN,A.JOACHIMIAK,              
JRNL        AUTH 3 G.N.PHILLIPS JR.                                             
JRNL        TITL   ENSEMBLE REFINEMENT OF AN EPOXIDE HYDROLASE FROM             
JRNL        TITL 2 STREPTOMYCES CARZINOSTATICUS SUBSP. NEOCARZINOSTATICUS.      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.56 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.ENSEMBLE_REFINEMENT: DEV_1420)        
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 65942                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.123                           
REMARK   3   R VALUE            (WORKING SET) : 0.122                           
REMARK   3   FREE R VALUE                     : 0.151                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3343                            
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 27.8208 -  4.4933    0.99     2943   148  0.1404 0.1322        
REMARK   3     2  4.4933 -  3.5689    1.00     2788   152  0.1210 0.1571        
REMARK   3     3  3.5689 -  3.1184    0.99     2758   148  0.1378 0.1744        
REMARK   3     4  3.1184 -  2.8336    0.99     2736   145  0.1253 0.1520        
REMARK   3     5  2.8336 -  2.6307    0.97     2632   160  0.1080 0.1407        
REMARK   3     6  2.6307 -  2.4757    0.96     2604   158  0.0977 0.1458        
REMARK   3     7  2.4757 -  2.3518    0.97     2620   154  0.0906 0.1059        
REMARK   3     8  2.3518 -  2.2494    0.95     2567   148  0.0963 0.1276        
REMARK   3     9  2.2494 -  2.1629    0.96     2585   129  0.0950 0.1369        
REMARK   3    10  2.1629 -  2.0883    0.96     2568   135  0.0989 0.1316        
REMARK   3    11  2.0883 -  2.0230    0.96     2648   131  0.1035 0.1355        
REMARK   3    12  2.0230 -  1.9652    0.97     2574   140  0.1030 0.1362        
REMARK   3    13  1.9652 -  1.9135    0.96     2591   129  0.1081 0.1564        
REMARK   3    14  1.9135 -  1.8668    0.97     2602   139  0.1085 0.1414        
REMARK   3    15  1.8668 -  1.8243    0.97     2616   122  0.1115 0.1516        
REMARK   3    16  1.8243 -  1.7855    0.97     2590   126  0.1151 0.1579        
REMARK   3    17  1.7855 -  1.7498    0.98     2580   158  0.1209 0.1564        
REMARK   3    18  1.7498 -  1.7168    0.98     2615   132  0.1326 0.1848        
REMARK   3    19  1.7168 -  1.6861    0.98     2648   127  0.1505 0.2017        
REMARK   3    20  1.6861 -  1.6576    0.98     2634   139  0.1671 0.1940        
REMARK   3    21  1.6576 -  1.6308    0.98     2590   144  0.1739 0.2219        
REMARK   3    22  1.6308 -  1.6057    0.96     2533   141  0.1846 0.2285        
REMARK   3    23  1.6057 -  1.5821    0.90     2415   118  0.2020 0.2200        
REMARK   3    24  1.5821 -  1.5599    0.82     2162   120  0.2160 0.2274        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
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)     : 0.090            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.670           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           NULL                                  
REMARK   3   ANGLE     :  1.216           NULL                                  
REMARK   3   CHIRALITY :  0.069           NULL                                  
REMARK   3   PLANARITY :  0.009           NULL                                  
REMARK   3   DIHEDRAL  :  9.950           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4QA9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085800.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97915                            
REMARK 200  MONOCHROMATOR                  : SI 111 CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 65946                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.560                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.816                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX: PHASER                                        
REMARK 200 STARTING MODEL: PDB ENTRY 4I19                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM SULFATE AND 0.1M TRIS:     
REMARK 280  HCL, PH 8.5. CYRO WAS ETHYLENE GLYCOL., VAPOR DIFFUSION,            
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.51300            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       37.66500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       37.66500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       41.25650            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       37.66500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       37.66500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      123.76950            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       37.66500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       37.66500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       41.25650            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       37.66500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       37.66500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      123.76950            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       82.51300            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 512  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500  1 GLU A  44   CB    GLU A  44   CG      0.124                       
REMARK 500  2 GLU A  44   CB    GLU A  44   CG      0.141                       
REMARK 500  2 VAL A 103   CB    VAL A 103   CG2    -0.135                       
REMARK 500  2 ASP A 174   CB    ASP A 174   CG     -0.165                       
REMARK 500  3 SER A 298   CB    SER A 298   OG     -0.107                       
REMARK 500  5 MET A 237   CB    MET A 237   CG      0.339                       
REMARK 500  5 ASP A 323   CA    ASP A 323   CB      0.147                       
REMARK 500  7 MET A 237   CB    MET A 237   CG     -0.197                       
REMARK 500  8 GLU A 344   CB    GLU A 344   CG      0.146                       
REMARK 500  8 GLU A 367   CB    GLU A 367   CG     -0.226                       
REMARK 500  8 GLU A 367   CG    GLU A 367   CD     -0.098                       
REMARK 500  9 LYS A 307   CE    LYS A 307   NZ      0.196                       
REMARK 500 14 GLU A 225   CG    GLU A 225   CD      0.092                       
REMARK 500 15 MET A 326   CB    MET A 326   CG      0.204                       
REMARK 500 15 GLU A 344   CB    GLU A 344   CG      0.197                       
REMARK 500 16 MET A 237   CB    MET A 237   CG      0.331                       
REMARK 500 17 SER A 298   CB    SER A 298   OG     -0.107                       
REMARK 500 18 GLU A 225   CB    GLU A 225   CG      0.118                       
REMARK 500 20 GLU A  27   CB    GLU A  27   CG      0.119                       
REMARK 500 20 GLU A 344   CB    GLU A 344   CG      0.168                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500  1 ASP A 174   CB  -  CA  -  C   ANGL. DEV. =  16.7 DEGREES          
REMARK 500  2 ARG A 226   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500  3 ARG A 167   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500  3 ARG A 167   NE  -  CZ  -  NH2 ANGL. DEV. =   4.3 DEGREES          
REMARK 500  5 GLU A 211   N   -  CA  -  C   ANGL. DEV. = -18.6 DEGREES          
REMARK 500  5 MET A 326   CG  -  SD  -  CE  ANGL. DEV. = -14.4 DEGREES          
REMARK 500  6 ASP A 217   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500  6 ARG A 226   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  6 ARG A 226   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500  6 ASP A 276   CB  -  CA  -  C   ANGL. DEV. =  17.3 DEGREES          
REMARK 500  6 LEU A 356   CA  -  CB  -  CG  ANGL. DEV. =  16.4 DEGREES          
REMARK 500  7 MET A 237   CG  -  SD  -  CE  ANGL. DEV. =  17.2 DEGREES          
REMARK 500  7 ARG A 358   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500  9 ASP A 187   CB  -  CG  -  OD1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500  9 LYS A 307   CD  -  CE  -  NZ  ANGL. DEV. =  18.3 DEGREES          
REMARK 500  9 ARG A 340   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500  9 ARG A 340   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500 10 ARG A  61   CG  -  CD  -  NE  ANGL. DEV. =  14.7 DEGREES          
REMARK 500 10 ARG A  61   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500 10 ARG A  61   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500 10 LEU A 210   CA  -  CB  -  CG  ANGL. DEV. =  19.4 DEGREES          
REMARK 500 10 ARG A 226   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500 11 ARG A  50   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500 11 ARG A  61   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500 11 ASP A 323   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500 11 MET A 326   CB  -  CG  -  SD  ANGL. DEV. = -21.7 DEGREES          
REMARK 500 13 ARG A 226   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500 13 ARG A 358   CG  -  CD  -  NE  ANGL. DEV. =  13.1 DEGREES          
REMARK 500 13 ARG A 358   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500 13 ARG A 358   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500 14 ARG A 226   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500 14 MET A 237   CG  -  SD  -  CE  ANGL. DEV. =  16.9 DEGREES          
REMARK 500 15 ARG A 226   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500 15 MET A 237   CB  -  CG  -  SD  ANGL. DEV. = -30.4 DEGREES          
REMARK 500 15 MET A 326   CG  -  SD  -  CE  ANGL. DEV. = -10.0 DEGREES          
REMARK 500 16 ASP A  88   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500 16 ASP A  88   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500 16 ASP A 229   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500 16 MET A 237   CB  -  CG  -  SD  ANGL. DEV. = -22.4 DEGREES          
REMARK 500 16 MET A 237   CG  -  SD  -  CE  ANGL. DEV. = -22.8 DEGREES          
REMARK 500 17 ARG A 220   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500 18 ARG A  50   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500 18 ARG A  61   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500 18 LEU A 210   CB  -  CG  -  CD1 ANGL. DEV. =  11.1 DEGREES          
REMARK 500 18 GLU A 211   N   -  CA  -  C   ANGL. DEV. = -16.5 DEGREES          
REMARK 500 18 MET A 237   CB  -  CG  -  SD  ANGL. DEV. =  22.6 DEGREES          
REMARK 500 18 MET A 237   CG  -  SD  -  CE  ANGL. DEV. =  11.0 DEGREES          
REMARK 500 18 ASP A 373   CB  -  CG  -  OD1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500 19 ASP A 174   CB  -  CG  -  OD1 ANGL. DEV. =  -8.1 DEGREES          
REMARK 500 19 ASP A 174   CB  -  CG  -  OD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      59 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500  1 ASP A  73       28.79     43.89                                   
REMARK 500  1 PRO A  99       76.25   -104.50                                   
REMARK 500  1 ALA A 145     -168.34   -123.15                                   
REMARK 500  1 ASP A 174     -133.22     55.88                                   
REMARK 500  1 GLU A 209      -83.53   -121.42                                   
REMARK 500  1 LEU A 210       61.90    -55.05                                   
REMARK 500  1 GLU A 211      -49.05   -160.28                                   
REMARK 500  1 SER A 214      163.66    -49.52                                   
REMARK 500  1 SER A 224      -25.99    -34.95                                   
REMARK 500  1 GLU A 271      -80.11   -104.78                                   
REMARK 500  1 GLN A 349       54.55   -143.02                                   
REMARK 500  2 PRO A  99       77.63   -100.07                                   
REMARK 500  2 HIS A 118       27.01   -143.96                                   
REMARK 500  2 ASP A 174     -135.00     65.87                                   
REMARK 500  2 GLU A 209      -57.33   -123.25                                   
REMARK 500  2 GLU A 271      -95.17    -98.22                                   
REMARK 500  3 ASN A  -1     -119.07   -116.19                                   
REMARK 500  3 ASP A  51      -96.62    -80.68                                   
REMARK 500  3 ASP A 174     -133.82     57.45                                   
REMARK 500  3 PRO A 207       49.70    -65.08                                   
REMARK 500  3 ASN A 272      -46.89   -142.87                                   
REMARK 500  3 PHE A 362       66.35   -106.19                                   
REMARK 500  4 ALA A   0      140.23    -31.01                                   
REMARK 500  4 ASP A  30       52.44    -95.68                                   
REMARK 500  4 ASP A  73       61.27     34.81                                   
REMARK 500  4 ALA A 145     -161.52   -100.40                                   
REMARK 500  4 ASP A 174     -121.50     68.46                                   
REMARK 500  4 SER A 252      112.62   -161.69                                   
REMARK 500  4 ASN A 272      -32.23   -141.76                                   
REMARK 500  4 SER A 314      144.29   -171.78                                   
REMARK 500  4 ASP A 357      -23.72   -171.51                                   
REMARK 500  5 ALA A 145     -166.26   -112.67                                   
REMARK 500  5 ASP A 174     -128.26     59.73                                   
REMARK 500  5 LEU A 210       57.56   -115.86                                   
REMARK 500  5 GLU A 211       46.57   -145.83                                   
REMARK 500  5 THR A 212        4.51   -157.03                                   
REMARK 500  5 ASN A 272      -49.32   -146.64                                   
REMARK 500  5 GLU A 275        2.38    -63.26                                   
REMARK 500  5 GLN A 349       58.00   -141.14                                   
REMARK 500  5 GLU A 355       72.86   -117.90                                   
REMARK 500  5 LEU A 356      150.51    -43.39                                   
REMARK 500  6 ASP A 174     -132.66     61.04                                   
REMARK 500  6 GLU A 271      -69.86    -98.29                                   
REMARK 500  6 SER A 314      140.99   -173.43                                   
REMARK 500  6 GLN A 349       57.25   -143.42                                   
REMARK 500  6 GLU A 367       64.35   -119.62                                   
REMARK 500  6 ASP A 373      -67.43    -26.78                                   
REMARK 500  7 HIS A 118       46.75   -140.35                                   
REMARK 500  7 ALA A 145     -154.13   -114.16                                   
REMARK 500  7 ASP A 174     -122.41     51.06                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     165 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN A   -1     ALA A    0          2      -146.40                    
REMARK 500 LEU A  356     ASP A  357          4      -143.55                    
REMARK 500 ASN A   -1     ALA A    0          7      -149.26                    
REMARK 500 LEU A  356     ASP A  357         12      -133.00                    
REMARK 500 SER A  232     GLY A  233         16       144.58                    
REMARK 500 ALA A    0     MET A    1         17      -125.09                    
REMARK 500 ALA A  222     VAL A  223         18       144.28                    
REMARK 500 VAL A  223     SER A  224         19       138.74                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500  2 ASN A  -1        24.4      L          L   OUTSIDE RANGE           
REMARK 500  3 ASP A 346        17.0      L          L   OUTSIDE RANGE           
REMARK 500  3 ASP A 357        21.2      L          L   OUTSIDE RANGE           
REMARK 500  4 ASP A  30        23.6      L          L   OUTSIDE RANGE           
REMARK 500  7 ASN A  -1        24.0      L          L   OUTSIDE RANGE           
REMARK 500  9 ASP A 229        23.7      L          L   OUTSIDE RANGE           
REMARK 500 18 GLU A 211        46.5      L          L   OUTSIDE RANGE           
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 A 609        DISTANCE =  5.25 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 416                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4I19   RELATED DB: PDB                                   
REMARK 900 RELATED ID: MCSG-APC109144   RELATED DB: TARGETTRACK                 
REMARK 900 RELATED ID: NATPRO-GO.119835   RELATED DB: TARGETTRACK               
DBREF  4QA9 A    1   385  UNP    Q84HB8   Q84HB8_STRCZ     1    385             
SEQADV 4QA9 SER A   -2  UNP  Q84HB8              EXPRESSION TAG                 
SEQADV 4QA9 ASN A   -1  UNP  Q84HB8              EXPRESSION TAG                 
SEQADV 4QA9 ALA A    0  UNP  Q84HB8              EXPRESSION TAG                 
SEQRES   1 A  388  SER ASN ALA MET ARG PRO PHE GLN VAL GLN ILE PRO GLN          
SEQRES   2 A  388  ALA ASP ILE ASP ASP LEU LYS ARG ARG LEU SER GLU THR          
SEQRES   3 A  388  ARG TRP PRO GLU LEU VAL ASP VAL GLY TRP SER ARG GLY          
SEQRES   4 A  388  ALA PRO LEU SER TYR ILE LYS GLU LEU ALA GLU TYR TRP          
SEQRES   5 A  388  ARG ASP GLY PHE ASP TRP ARG ALA ALA GLU ARG ARG ILE          
SEQRES   6 A  388  ASN GLN TYR PRO GLN PHE THR THR GLU ILE ASP GLY ALA          
SEQRES   7 A  388  THR ILE HIS PHE LEU HIS VAL ARG SER PRO GLU PRO ASP          
SEQRES   8 A  388  ALA THR PRO MET VAL ILE THR HIS GLY TRP PRO GLY THR          
SEQRES   9 A  388  PRO VAL GLU PHE LEU ASP ILE ILE GLY PRO LEU THR ASP          
SEQRES  10 A  388  PRO ARG ALA HIS GLY GLY ASP PRO ALA ASP ALA PHE HIS          
SEQRES  11 A  388  LEU VAL ILE PRO SER LEU PRO GLY PHE GLY LEU SER GLY          
SEQRES  12 A  388  PRO LEU LYS SER ALA GLY TRP GLU LEU GLY ARG ILE ALA          
SEQRES  13 A  388  MET ALA TRP SER LYS LEU MET ALA SER LEU GLY TYR GLU          
SEQRES  14 A  388  ARG TYR ILE ALA GLN GLY GLY ASP ILE GLY ALA PHE THR          
SEQRES  15 A  388  SER LEU LEU LEU GLY ALA ILE ASP PRO SER HIS LEU ALA          
SEQRES  16 A  388  GLY ILE HIS VAL ASN LEU LEU GLN THR ASN LEU SER GLY          
SEQRES  17 A  388  GLU PRO GLY GLU LEU GLU THR LEU SER ASP ALA ASP LYS          
SEQRES  18 A  388  ALA ARG LEU ALA VAL SER GLU ARG PHE LEU ASP ASP LEU          
SEQRES  19 A  388  SER GLY PRO MET LYS MET GLN SER THR ARG PRO HIS THR          
SEQRES  20 A  388  ILE GLY TYR MET LEU ASN ASP SER PRO VAL ALA GLN LEU          
SEQRES  21 A  388  ALA TYR LEU LEU GLU MET PHE LYS HIS TRP ALA GLN THR          
SEQRES  22 A  388  GLU ASN VAL PRO GLU ASP ALA VAL ASP ARG ASP LEU MET          
SEQRES  23 A  388  LEU THR HIS ILE SER LEU PHE TRP PHE THR ALA THR GLY          
SEQRES  24 A  388  GLY SER ALA ALA GLN ALA HIS TYR GLU LEU LYS PRO PHE          
SEQRES  25 A  388  LEU PRO ILE THR SER LEU ILE GLY ARG SER PRO THR LEU          
SEQRES  26 A  388  ASP VAL PRO MET GLY VAL ALA VAL TYR PRO GLY ALA LEU          
SEQRES  27 A  388  PHE GLN PRO VAL ARG SER LEU ALA GLU ARG ASP PHE LYS          
SEQRES  28 A  388  GLN ILE VAL HIS TRP ALA GLU LEU ASP ARG GLY GLY HIS          
SEQRES  29 A  388  PHE SER ALA MET GLU GLU PRO ASP LEU PHE VAL ASP ASP          
SEQRES  30 A  388  LEU ARG THR PHE ASN ARG THR LEU LYS LYS LEU                  
HET    SO4  A 401       5                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    EDO  A 405      10                                                       
HET    EDO  A 406      10                                                       
HET    EDO  A 407      10                                                       
HET    EDO  A 408      10                                                       
HET    EDO  A 409      10                                                       
HET    EDO  A 410      10                                                       
HET    EDO  A 411      10                                                       
HET    EDO  A 412      10                                                       
HET    EDO  A 413      10                                                       
HET    EDO  A 414      10                                                       
HET    EDO  A 415      10                                                       
HET    EDO  A 416      10                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  SO4    4(O4 S 2-)                                                   
FORMUL   6  EDO    12(C2 H6 O2)                                                 
FORMUL  18  HOH   *271(H2 O)                                                    
HELIX    1   1 PRO A    9  GLU A   22  1                                  14    
HELIX    2   2 PRO A   38  GLY A   52  1                                  15    
HELIX    3   3 ASP A   54  GLN A   64  1                                  11    
HELIX    4   4 THR A  101  GLU A  104  5                                   4    
HELIX    5   5 PHE A  105  ASP A  114  1                                  10    
HELIX    6   6 ASP A  121  ASP A  124  5                                   4    
HELIX    7   7 PHE A  136  GLY A  140  5                                   5    
HELIX    8   8 GLU A  148  GLY A  164  1                                  17    
HELIX    9   9 ASP A  174  ASP A  187  1                                  14    
HELIX   10  10 SER A  214  SER A  224  1                                  11    
HELIX   11  11 SER A  224  LEU A  231  1                                   8    
HELIX   12  12 SER A  232  ARG A  241  1                                  10    
HELIX   13  13 ARG A  241  ASP A  251  1                                  11    
HELIX   14  14 SER A  252  TRP A  267  1                                  16    
HELIX   15  15 VAL A  273  ALA A  277  5                                   5    
HELIX   16  16 ASP A  279  ALA A  294  1                                  16    
HELIX   17  17 THR A  295  LEU A  306  1                                  12    
HELIX   18  18 LYS A  307  LEU A  310  5                                   4    
HELIX   19  19 VAL A  339  PHE A  347  1                                   9    
HELIX   20  20 PHE A  362  GLU A  367  1                                   6    
HELIX   21  21 GLU A  367  LYS A  384  1                                  18    
SHEET    1   A 9 ARG A   2  PHE A   4  0                                        
SHEET    2   A 9 GLN A  67  ILE A  72 -1  O  THR A  69   N  ARG A   2           
SHEET    3   A 9 ALA A  75  VAL A  82 -1  O  PHE A  79   N  PHE A  68           
SHEET    4   A 9 PHE A 126  PRO A 131 -1  O  LEU A 128   N  VAL A  82           
SHEET    5   A 9 THR A  90  THR A  95  1  N  MET A  92   O  VAL A 129           
SHEET    6   A 9 TYR A 168  GLY A 172  1  O  GLN A 171   N  VAL A  93           
SHEET    7   A 9 LEU A 191  VAL A 196  1  O  HIS A 195   N  ALA A 170           
SHEET    8   A 9 MET A 326  VAL A 330  1  O  GLY A 327   N  ILE A 194           
SHEET    9   A 9 ILE A 350  GLU A 355  1  O  ALA A 354   N  VAL A 330           
CISPEP   1 TRP A   98    PRO A   99          1         6.65                     
CISPEP   2 TRP A   98    PRO A   99          2         1.76                     
CISPEP   3 TRP A   98    PRO A   99          3         8.18                     
CISPEP   4 TRP A   98    PRO A   99          4        -6.01                     
CISPEP   5 TRP A   98    PRO A   99          5        -2.82                     
CISPEP   6 TRP A   98    PRO A   99          6         3.05                     
CISPEP   7 TRP A   98    PRO A   99          7       -10.72                     
CISPEP   8 TRP A   98    PRO A   99          8         1.59                     
CISPEP   9 TRP A   98    PRO A   99          9        -5.52                     
CISPEP  10 TRP A   98    PRO A   99         10        -3.46                     
CISPEP  11 TRP A   98    PRO A   99         11        -4.24                     
CISPEP  12 TRP A   98    PRO A   99         12         7.39                     
CISPEP  13 TRP A   98    PRO A   99         13        -0.92                     
CISPEP  14 TRP A   98    PRO A   99         14        -4.66                     
CISPEP  15 TRP A   98    PRO A   99         15         3.62                     
CISPEP  16 TRP A   98    PRO A   99         16        -1.87                     
CISPEP  17 TRP A   98    PRO A   99         17         3.69                     
CISPEP  18 TRP A   98    PRO A   99         18         5.71                     
CISPEP  19 TRP A   98    PRO A   99         19         0.76                     
CISPEP  20 TRP A   98    PRO A   99         20        -6.71                     
SITE     1 AC1  4 LEU A 213  SER A 214  ASP A 215  LYS A 218                    
SITE     1 AC2  4 SER A  -2  ILE A  72  ASP A  73  LYS A 158                    
SITE     1 AC3  2 PRO A   9  HOH A 682                                          
SITE     1 AC4  4 ARG A  61  GLN A  64  TYR A  65  HOH A 723                    
SITE     1 AC5  8 GLN A 200  THR A 201  ASN A 202  LEU A 342                    
SITE     2 AC5  8 ALA A 343  ASP A 346  PHE A 347  EDO A 408                    
SITE     1 AC6  7 ASP A 174  PHE A 227  MET A 235  TRP A 267                    
SITE     2 AC6  7 LEU A 335  HOH A 621  HOH A 669                               
SITE     1 AC7  5 PHE A 178  PHE A 309  SER A 319  EDO A 408                    
SITE     2 AC7  5 HOH A 574                                                     
SITE     1 AC8  7 LEU A 181  LEU A 199  GLN A 200  SER A 319                    
SITE     2 AC8  7 EDO A 405  EDO A 407  EDO A 410                               
SITE     1 AC9  6 PRO A  85  ASP A 114  ARG A 116  ALA A 117                    
SITE     2 AC9  6 ALA A 185  HOH A 720                                          
SITE     1 BC1  6 PHE A 178  LEU A 181  LEU A 199  GLN A 200                    
SITE     2 BC1  6 EDO A 408  HOH A 632                                          
SITE     1 BC2  6 ASP A 174  ILE A 175  PHE A 178  HOH A 621                    
SITE     2 BC2  6 HOH A 669  HOH A 698                                          
SITE     1 BC3  5 ILE A  13  LEU A  16  LYS A  17  TRP A  49                    
SITE     2 BC3  5 PHE A 292                                                     
SITE     1 BC4  2 ARG A  61  LEU A 282                                          
SITE     1 BC5  8 PRO A 134  PHE A 136  TRP A 147  ALA A 302                    
SITE     2 BC5  8 GLU A 305  LEU A 306  HOH A 515  HOH A 715                    
SITE     1 BC6  3 PRO A 308  THR A 313  HOH A 637                               
SITE     1 BC7  4 GLY A 164  ILE A 316  HOH A 704  HOH A 712                    
CRYST1   75.330   75.330  165.026  90.00  90.00  90.00 P 41 21 2     8          
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      0.013275  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013275  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006060        0.00000                         
MODEL        1                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL        2                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL        3                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL        4                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL        5                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL        6                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL        7                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL        8                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL        9                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL       10                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL       11                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL       12                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL       13                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL       14                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL       15                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL       16                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL       17                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL       18                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL       19                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MODEL       20                                                                  
TER    6047      LEU A 385                                                      
ENDMDL                                                                          
MASTER      547    0   16   21    9    0   25    6 3390    1  140   30          
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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