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LongText Report for: 4W9R-pdb

Name Class
4W9R-pdb
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   27-AUG-14   4W9R              
TITLE     CRYSTAL STRUCTURE OF UNCHARACTERISED PROTEIN COCH_1243 FROM           
TITLE    2 CAPNOCYTOPHAGA OCHRACEA DSM 7271                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UNCHARACTERIZED PROTEIN;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAPNOCYTOPHAGA OCHRACEA;                        
SOURCE   3 ORGANISM_TAXID: 521097;                                              
SOURCE   4 STRAIN: ATCC 27872 / DSM 7271 / JCM 12966 / VPI 2845;                
SOURCE   5 GENE: COCH_1243;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MAGIC;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG68                                   
KEYWDS    STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL       
KEYWDS   2 GENOMICS, MCSG, UNKNOWN FUNCTION, GEBA                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CHANG,R.WU,S.CLANCY,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL      
AUTHOR   2 GENOMICS (MCSG)                                                      
REVDAT   1   10-SEP-14 4W9R    0                                                
JRNL        AUTH   C.CHANG,R.WU,S.CLANCY,A.JOACHIMIAK                           
JRNL        TITL   CRYSTAL STRUCTURE OF UNCHARACTERISED PROTEIN COCH_1243 FROM  
JRNL        TITL 2 CAPNOCYTOPHAGA OCHRACEA DSM 7271                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.3_1479)                   
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 : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.31                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 44135                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2221                            
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 43.3147 -  6.8032    1.00     2748   141  0.1639 0.1603        
REMARK   3     2  6.8032 -  5.4032    1.00     2699   148  0.1609 0.2005        
REMARK   3     3  5.4032 -  4.7212    1.00     2703   143  0.1291 0.1563        
REMARK   3     4  4.7212 -  4.2899    1.00     2663   160  0.1250 0.1365        
REMARK   3     5  4.2899 -  3.9827    1.00     2697   144  0.1410 0.1823        
REMARK   3     6  3.9827 -  3.7480    0.99     2653   147  0.1669 0.1938        
REMARK   3     7  3.7480 -  3.5604    1.00     2685   138  0.1826 0.2064        
REMARK   3     8  3.5604 -  3.4055    0.99     2682   124  0.2156 0.2718        
REMARK   3     9  3.4055 -  3.2744    1.00     2680   148  0.2225 0.2442        
REMARK   3    10  3.2744 -  3.1615    1.00     2646   145  0.2309 0.2835        
REMARK   3    11  3.1615 -  3.0626    1.00     2690   131  0.2422 0.2549        
REMARK   3    12  3.0626 -  2.9751    0.99     2659   138  0.2500 0.3088        
REMARK   3    13  2.9751 -  2.8968    0.98     2618   128  0.2572 0.3151        
REMARK   3    14  2.8968 -  2.8261    0.96     2615   122  0.2698 0.3035        
REMARK   3    15  2.8261 -  2.7619    0.91     2411   136  0.2583 0.3191        
REMARK   3    16  2.7619 -  2.7031    0.78     2065   128  0.2559 0.2991        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.310           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.21                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.84                          
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      :  0.002           5953                                  
REMARK   3   ANGLE     :  0.692           8058                                  
REMARK   3   CHIRALITY :  0.027            880                                  
REMARK   3   PLANARITY :  0.004           1038                                  
REMARK   3   DIHEDRAL  : 10.592           2218                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 20 THROUGH 160 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2589 114.4292  11.5017              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6061 T22:  -0.2102                                     
REMARK   3      T33:   0.1396 T12:   0.1329                                     
REMARK   3      T13:   0.1055 T23:   0.0545                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0090 L22:   0.0114                                     
REMARK   3      L33:   0.0170 L12:  -0.0097                                     
REMARK   3      L13:  -0.0143 L23:   0.0040                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0713 S12:  -0.0121 S13:   0.0854                       
REMARK   3      S21:   0.1272 S22:   0.0241 S23:   0.0566                       
REMARK   3      S31:  -0.3083 S32:  -0.0932 S33:   0.1264                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 232 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7892 122.5515  11.0771              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6673 T22:   0.1099                                     
REMARK   3      T33:   0.2522 T12:  -0.2113                                     
REMARK   3      T13:  -0.0617 T23:   0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0124 L22:   0.0211                                     
REMARK   3      L33:   0.0097 L12:   0.0146                                     
REMARK   3      L13:  -0.0048 L23:   0.0002                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0768 S12:  -0.0479 S13:   0.0438                       
REMARK   3      S21:   0.0815 S22:  -0.0542 S23:  -0.0706                       
REMARK   3      S31:  -0.0142 S32:   0.0270 S33:   0.0057                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 233 THROUGH 309 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.7842  94.5385  13.5173              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1917 T22:   0.1738                                     
REMARK   3      T33:   0.2379 T12:   0.0127                                     
REMARK   3      T13:  -0.0417 T23:   0.0774                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0197 L22:   0.0382                                     
REMARK   3      L33:   0.1366 L12:   0.0286                                     
REMARK   3      L13:  -0.0450 L23:  -0.0644                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0361 S12:  -0.1600 S13:  -0.0844                       
REMARK   3      S21:   0.0177 S22:  -0.0816 S23:  -0.0837                       
REMARK   3      S31:  -0.1381 S32:   0.2273 S33:   0.0116                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 310 THROUGH 379 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6542  71.1815  21.3490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2029 T22:   0.2219                                     
REMARK   3      T33:   0.4153 T12:   0.1153                                     
REMARK   3      T13:  -0.0028 T23:   0.1781                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0354 L22:   0.0656                                     
REMARK   3      L33:   0.0226 L12:  -0.0057                                     
REMARK   3      L13:  -0.0104 L23:   0.0104                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0336 S12:  -0.0430 S13:  -0.0692                       
REMARK   3      S21:   0.0722 S22:  -0.0629 S23:   0.0010                       
REMARK   3      S31:   0.0471 S32:   0.0687 S33:  -0.0701                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 19 THROUGH 61 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0177 100.0529 -17.0815              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3020 T22:   0.1284                                     
REMARK   3      T33:   0.2384 T12:   0.0537                                     
REMARK   3      T13:  -0.0204 T23:  -0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0060 L22:   0.0056                                     
REMARK   3      L33:   0.0058 L12:   0.0052                                     
REMARK   3      L13:   0.0018 L23:  -0.0021                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0132 S12:   0.0585 S13:  -0.0379                       
REMARK   3      S21:  -0.0144 S22:  -0.0433 S23:   0.0502                       
REMARK   3      S31:  -0.0598 S32:  -0.0560 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 62 THROUGH 160 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   7.4106  99.4759 -18.5737              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2624 T22:   0.0917                                     
REMARK   3      T33:   0.1494 T12:   0.0726                                     
REMARK   3      T13:  -0.0079 T23:   0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0563 L22:   0.0212                                     
REMARK   3      L33:   0.0211 L12:   0.0211                                     
REMARK   3      L13:   0.0155 L23:   0.0139                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0698 S12:   0.0914 S13:  -0.0150                       
REMARK   3      S21:  -0.0114 S22:  -0.0217 S23:   0.0240                       
REMARK   3      S31:  -0.1381 S32:   0.0126 S33:   0.0175                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 161 THROUGH 232 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.5780 102.7214 -16.0327              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2526 T22:   0.2182                                     
REMARK   3      T33:   0.2632 T12:   0.0042                                     
REMARK   3      T13:   0.0295 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0156 L22:   0.0156                                     
REMARK   3      L33:   0.0103 L12:   0.0110                                     
REMARK   3      L13:  -0.0022 L23:   0.0119                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1262 S12:   0.0400 S13:  -0.0093                       
REMARK   3      S21:  -0.0092 S22:  -0.0275 S23:  -0.1680                       
REMARK   3      S31:  -0.1192 S32:   0.0732 S33:  -0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 233 THROUGH 344 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5481 131.8430 -22.1404              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3939 T22:  -0.0822                                     
REMARK   3      T33:   0.2362 T12:   0.0013                                     
REMARK   3      T13:   0.0712 T23:   0.1796                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0003 L22:   0.0134                                     
REMARK   3      L33:   0.0341 L12:   0.0005                                     
REMARK   3      L13:   0.0165 L23:  -0.0202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0212 S12:   0.0488 S13:   0.1040                       
REMARK   3      S21:  -0.0647 S22:  -0.0318 S23:   0.0226                       
REMARK   3      S31:  -0.0435 S32:   0.0337 S33:  -0.0049                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 345 THROUGH 379 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.9057 150.6329 -24.5712              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3268 T22:   0.1611                                     
REMARK   3      T33:   0.5170 T12:  -0.0136                                     
REMARK   3      T13:   0.0219 T23:   0.1066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0051 L22:   0.0008                                     
REMARK   3      L33:   0.0017 L12:  -0.0021                                     
REMARK   3      L13:   0.0028 L23:  -0.0003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0309 S12:   0.0243 S13:   0.0253                       
REMARK   3      S21:  -0.0006 S22:   0.0048 S23:   0.0409                       
REMARK   3      S31:  -0.0408 S32:  -0.0183 S33:  -0.0000                       
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 4W9R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203391.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 1000                               
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) : 0.97921                            
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SCALEPACK                          
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45202                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.10                              
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.70                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.79500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: HKL-3000                                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17M SODIUM ACETATE, 0.085M TRIS-CL,    
REMARK 280  25.5% PEG4000, 15% GLYCEROL                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.13033            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       92.26067            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       69.19550            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      115.32583            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       23.06517            
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
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: 3820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    17                                                      
REMARK 465     ASN A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     LYS A   380                                                      
REMARK 465     ARG A   381                                                      
REMARK 465     LYS A   382                                                      
REMARK 465     SER A   383                                                      
REMARK 465     LYS A   384                                                      
REMARK 465     HIS A   385                                                      
REMARK 465     THR A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     VAL A   388                                                      
REMARK 465     ILE A   389                                                      
REMARK 465     GLU A   390                                                      
REMARK 465     PRO A   391                                                      
REMARK 465     ILE A   392                                                      
REMARK 465     GLU A   393                                                      
REMARK 465     PRO A   394                                                      
REMARK 465     THR A   395                                                      
REMARK 465     GLU A   396                                                      
REMARK 465     GLU A   397                                                      
REMARK 465     VAL A   398                                                      
REMARK 465     ALA A   399                                                      
REMARK 465     PRO A   400                                                      
REMARK 465     ALA A   401                                                      
REMARK 465     GLN A   402                                                      
REMARK 465     GLU A   403                                                      
REMARK 465     GLU A   404                                                      
REMARK 465     GLN A   405                                                      
REMARK 465     ASN A   406                                                      
REMARK 465     PRO A   407                                                      
REMARK 465     THR A   408                                                      
REMARK 465     ASP A   409                                                      
REMARK 465     GLU A   410                                                      
REMARK 465     SER A   411                                                      
REMARK 465     ASN A   412                                                      
REMARK 465     GLN A   413                                                      
REMARK 465     ASN A   414                                                      
REMARK 465     SER B    17                                                      
REMARK 465     ASN B    18                                                      
REMARK 465     LYS B   380                                                      
REMARK 465     ARG B   381                                                      
REMARK 465     LYS B   382                                                      
REMARK 465     SER B   383                                                      
REMARK 465     LYS B   384                                                      
REMARK 465     HIS B   385                                                      
REMARK 465     THR B   386                                                      
REMARK 465     LYS B   387                                                      
REMARK 465     VAL B   388                                                      
REMARK 465     ILE B   389                                                      
REMARK 465     GLU B   390                                                      
REMARK 465     PRO B   391                                                      
REMARK 465     ILE B   392                                                      
REMARK 465     GLU B   393                                                      
REMARK 465     PRO B   394                                                      
REMARK 465     THR B   395                                                      
REMARK 465     GLU B   396                                                      
REMARK 465     GLU B   397                                                      
REMARK 465     VAL B   398                                                      
REMARK 465     ALA B   399                                                      
REMARK 465     PRO B   400                                                      
REMARK 465     ALA B   401                                                      
REMARK 465     GLN B   402                                                      
REMARK 465     GLU B   403                                                      
REMARK 465     GLU B   404                                                      
REMARK 465     GLN B   405                                                      
REMARK 465     ASN B   406                                                      
REMARK 465     PRO B   407                                                      
REMARK 465     THR B   408                                                      
REMARK 465     ASP B   409                                                      
REMARK 465     GLU B   410                                                      
REMARK 465     SER B   411                                                      
REMARK 465     ASN B   412                                                      
REMARK 465     GLN B   413                                                      
REMARK 465     ASN B   414                                                      
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     GLN A  20    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 100    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 152    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 153    CG   CD   CE   NZ                                   
REMARK 470     LYS A 229    CG   CD   CE   NZ                                   
REMARK 470     LYS B  44    CG   CD   CE   NZ                                   
REMARK 470     ARG B  48    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 152    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 153    CG   CD   CE   NZ                                   
REMARK 470     GLU B 173    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    GLU A  89       70.59     51.12                                   
REMARK 500    VAL A 101      -66.88   -105.28                                   
REMARK 500    ASN A 106     -119.65     57.13                                   
REMARK 500    GLU A 118      -64.01   -128.86                                   
REMARK 500    GLU A 139     -129.77     56.27                                   
REMARK 500    LYS A 154      138.18    178.96                                   
REMARK 500    ASN A 185      -75.71   -115.28                                   
REMARK 500    GLU A 197       18.82     56.89                                   
REMARK 500    THR A 262      -64.13    -99.46                                   
REMARK 500    ASP A 362     -127.64     52.22                                   
REMARK 500    THR B  61      -61.27   -109.30                                   
REMARK 500    ASN B 106     -120.57     52.20                                   
REMARK 500    GLU B 118      -64.70   -123.60                                   
REMARK 500    GLU B 139     -129.66     56.70                                   
REMARK 500    LYS B 154      138.85   -176.58                                   
REMARK 500    ASN B 185      -76.41   -116.96                                   
REMARK 500    GLU B 197       18.49     56.89                                   
REMARK 500    THR B 262      -63.02    -99.56                                   
REMARK 500    MSE B 264      -62.87   -109.02                                   
REMARK 500    ASP B 362     -125.18     52.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: MCSG-APC103154   RELATED DB: TARGETTRACK                 
DBREF  4W9R A   20   414  UNP    C7M590   C7M590_CAPOD    20    414             
DBREF  4W9R B   20   414  UNP    C7M590   C7M590_CAPOD    20    414             
SEQADV 4W9R SER A   17  UNP  C7M590              EXPRESSION TAG                 
SEQADV 4W9R ASN A   18  UNP  C7M590              EXPRESSION TAG                 
SEQADV 4W9R ALA A   19  UNP  C7M590              EXPRESSION TAG                 
SEQADV 4W9R SER B   17  UNP  C7M590              EXPRESSION TAG                 
SEQADV 4W9R ASN B   18  UNP  C7M590              EXPRESSION TAG                 
SEQADV 4W9R ALA B   19  UNP  C7M590              EXPRESSION TAG                 
SEQRES   1 A  398  SER ASN ALA GLN VAL ILE SER GLU THR PHE SER SER GLY          
SEQRES   2 A  398  ARG LEU ASN ARG LYS GLN LYS ILE GLY ILE TYR LYS PRO          
SEQRES   3 A  398  GLU LYS TYR THR ASP ARG GLN ALA TYR PRO LEU ILE VAL          
SEQRES   4 A  398  VAL LEU ASN ALA GLU THR LEU MSE GLU PRO VAL VAL SER          
SEQRES   5 A  398  MSE VAL ARG TYR TYR GLU GLN PHE GLY GLU MSE PRO LYS          
SEQRES   6 A  398  CYS ILE VAL VAL GLY VAL TYR GLU PRO LYS GLN GLU ASP          
SEQRES   7 A  398  VAL THR VAL VAL GLU GLU VAL GLY ARG PRO ILE ASN GLU          
SEQRES   8 A  398  SER ALA ARG PHE PHE GLU PHE VAL SER ALA GLU LEU VAL          
SEQRES   9 A  398  PRO TYR ILE GLN GLY LYS TYR PRO ILE ALA ASP LEU LYS          
SEQRES  10 A  398  GLY VAL ILE ALA SER GLU GLU ALA GLY PHE LEU ALA ASN          
SEQRES  11 A  398  TYR TYR MSE LEU ALA GLU LYS LYS PRO THR PHE ASN MSE          
SEQRES  12 A  398  ILE VAL SER LEU ASN PRO VAL ALA LEU PRO ARG MSE GLY          
SEQRES  13 A  398  GLU GLU PHE SER HIS ALA LEU ALA ALA GLY VAL PRO ASN          
SEQRES  14 A  398  ARG LEU PHE TYR TYR MSE ALA THR ALA ASP VAL GLU ASN          
SEQRES  15 A  398  LYS VAL VAL TYR ASP LYS ALA ILE GLN PHE GLU ARG ALA          
SEQRES  16 A  398  MSE ARG SER ALA PRO VAL HIS GLU SER VAL GLU TYR HIS          
SEQRES  17 A  398  PHE VAL ASP PHE LYS GLY SER SER VAL ASN ALA ALA LYS          
SEQRES  18 A  398  LEU GLN GLY ILE ALA GLN ALA LEU ASP MSE CYS PHE ASP          
SEQRES  19 A  398  ILE TYR LYS PRO ILE GLY GLY LYS GLU PHE LYS THR GLN          
SEQRES  20 A  398  MSE GLU THR LEU GLU THR GLY ILE TYR GLU TYR LEU GLU          
SEQRES  21 A  398  ASN LYS TYR ASN THR ILE TYR LYS GLN LEU GLY VAL LYS          
SEQRES  22 A  398  LYS VAL PRO ILE LEU ASN ASP VAL MSE ALA THR TYR THR          
SEQRES  23 A  398  ALA ILE ASN SER SER GLN ASP TRP GLU SER LEU LYS LYS          
SEQRES  24 A  398  LEU ALA LYS TYR VAL GLU SER ASN GLY TYR LEU LYS THR          
SEQRES  25 A  398  ALA MSE PRO ASN PHE PHE LEU ALA GLU TYR TYR GLU LYS          
SEQRES  26 A  398  ILE GLY ASP ASP LYS LYS ALA LEU LYS THR TYR GLN LYS          
SEQRES  27 A  398  ALA TYR THR GLU PRO ASN ILE ASP PHE ILE THR GLY ASP          
SEQRES  28 A  398  LEU ILE ASN GLU ARG ILE THR HIS LEU GLN ALA THR LYS          
SEQRES  29 A  398  ARG LYS SER LYS HIS THR LYS VAL ILE GLU PRO ILE GLU          
SEQRES  30 A  398  PRO THR GLU GLU VAL ALA PRO ALA GLN GLU GLU GLN ASN          
SEQRES  31 A  398  PRO THR ASP GLU SER ASN GLN ASN                              
SEQRES   1 B  398  SER ASN ALA GLN VAL ILE SER GLU THR PHE SER SER GLY          
SEQRES   2 B  398  ARG LEU ASN ARG LYS GLN LYS ILE GLY ILE TYR LYS PRO          
SEQRES   3 B  398  GLU LYS TYR THR ASP ARG GLN ALA TYR PRO LEU ILE VAL          
SEQRES   4 B  398  VAL LEU ASN ALA GLU THR LEU MSE GLU PRO VAL VAL SER          
SEQRES   5 B  398  MSE VAL ARG TYR TYR GLU GLN PHE GLY GLU MSE PRO LYS          
SEQRES   6 B  398  CYS ILE VAL VAL GLY VAL TYR GLU PRO LYS GLN GLU ASP          
SEQRES   7 B  398  VAL THR VAL VAL GLU GLU VAL GLY ARG PRO ILE ASN GLU          
SEQRES   8 B  398  SER ALA ARG PHE PHE GLU PHE VAL SER ALA GLU LEU VAL          
SEQRES   9 B  398  PRO TYR ILE GLN GLY LYS TYR PRO ILE ALA ASP LEU LYS          
SEQRES  10 B  398  GLY VAL ILE ALA SER GLU GLU ALA GLY PHE LEU ALA ASN          
SEQRES  11 B  398  TYR TYR MSE LEU ALA GLU LYS LYS PRO THR PHE ASN MSE          
SEQRES  12 B  398  ILE VAL SER LEU ASN PRO VAL ALA LEU PRO ARG MSE GLY          
SEQRES  13 B  398  GLU GLU PHE SER HIS ALA LEU ALA ALA GLY VAL PRO ASN          
SEQRES  14 B  398  ARG LEU PHE TYR TYR MSE ALA THR ALA ASP VAL GLU ASN          
SEQRES  15 B  398  LYS VAL VAL TYR ASP LYS ALA ILE GLN PHE GLU ARG ALA          
SEQRES  16 B  398  MSE ARG SER ALA PRO VAL HIS GLU SER VAL GLU TYR HIS          
SEQRES  17 B  398  PHE VAL ASP PHE LYS GLY SER SER VAL ASN ALA ALA LYS          
SEQRES  18 B  398  LEU GLN GLY ILE ALA GLN ALA LEU ASP MSE CYS PHE ASP          
SEQRES  19 B  398  ILE TYR LYS PRO ILE GLY GLY LYS GLU PHE LYS THR GLN          
SEQRES  20 B  398  MSE GLU THR LEU GLU THR GLY ILE TYR GLU TYR LEU GLU          
SEQRES  21 B  398  ASN LYS TYR ASN THR ILE TYR LYS GLN LEU GLY VAL LYS          
SEQRES  22 B  398  LYS VAL PRO ILE LEU ASN ASP VAL MSE ALA THR TYR THR          
SEQRES  23 B  398  ALA ILE ASN SER SER GLN ASP TRP GLU SER LEU LYS LYS          
SEQRES  24 B  398  LEU ALA LYS TYR VAL GLU SER ASN GLY TYR LEU LYS THR          
SEQRES  25 B  398  ALA MSE PRO ASN PHE PHE LEU ALA GLU TYR TYR GLU LYS          
SEQRES  26 B  398  ILE GLY ASP ASP LYS LYS ALA LEU LYS THR TYR GLN LYS          
SEQRES  27 B  398  ALA TYR THR GLU PRO ASN ILE ASP PHE ILE THR GLY ASP          
SEQRES  28 B  398  LEU ILE ASN GLU ARG ILE THR HIS LEU GLN ALA THR LYS          
SEQRES  29 B  398  ARG LYS SER LYS HIS THR LYS VAL ILE GLU PRO ILE GLU          
SEQRES  30 B  398  PRO THR GLU GLU VAL ALA PRO ALA GLN GLU GLU GLN ASN          
SEQRES  31 B  398  PRO THR ASP GLU SER ASN GLN ASN                              
MODRES 4W9R MSE A   63  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE A   69  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE A   79  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE A  149  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE A  159  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE A  171  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE A  191  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE A  212  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE A  247  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE A  264  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE A  298  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE A  330  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE B   63  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE B   69  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE B   79  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE B  149  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE B  159  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE B  171  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE B  191  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE B  212  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE B  247  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE B  264  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE B  298  MET  MODIFIED RESIDUE                                   
MODRES 4W9R MSE B  330  MET  MODIFIED RESIDUE                                   
HET    MSE  A  63       8                                                       
HET    MSE  A  69       8                                                       
HET    MSE  A  79       8                                                       
HET    MSE  A 149       8                                                       
HET    MSE  A 159       8                                                       
HET    MSE  A 171       8                                                       
HET    MSE  A 191       8                                                       
HET    MSE  A 212       8                                                       
HET    MSE  A 247       8                                                       
HET    MSE  A 264       8                                                       
HET    MSE  A 298       8                                                       
HET    MSE  A 330       8                                                       
HET    MSE  B  63       8                                                       
HET    MSE  B  69       8                                                       
HET    MSE  B  79       8                                                       
HET    MSE  B 149       8                                                       
HET    MSE  B 159       8                                                       
HET    MSE  B 171       8                                                       
HET    MSE  B 191       8                                                       
HET    MSE  B 212       8                                                       
HET    MSE  B 247       8                                                       
HET    MSE  B 264       8                                                       
HET    MSE  B 298       8                                                       
HET    MSE  B 330       8                                                       
HET    GOL  A 501       6                                                       
HET    GOL  A 502       6                                                       
HET    GOL  A 503       6                                                       
HET    ACT  A 504       4                                                       
HET    ACT  A 505       4                                                       
HET    GOL  B 501       6                                                       
HET    ACT  B 502       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     GOL GLYCEROL                                                         
HETNAM     ACT ACETATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    24(C5 H11 N O2 SE)                                           
FORMUL   3  GOL    4(C3 H8 O3)                                                  
FORMUL   6  ACT    3(C2 H3 O2 1-)                                               
FORMUL  10  HOH   *95(H2 O)                                                     
HELIX    1 AA1 ASN A   58  PHE A   76  1                                  19    
HELIX    2 AA2 LYS A   91  THR A   96  1                                   6    
HELIX    3 AA3 ASN A  106  GLU A  118  1                                  13    
HELIX    4 AA4 GLU A  118  TYR A  127  1                                  10    
HELIX    5 AA5 GLU A  139  ALA A  145  1                                   7    
HELIX    6 AA6 ASN A  146  ALA A  151  5                                   6    
HELIX    7 AA7 LEU A  168  ARG A  170  5                                   3    
HELIX    8 AA8 MSE A  171  GLY A  182  1                                  12    
HELIX    9 AA9 ASN A  198  ARG A  213  1                                  16    
HELIX   10 AB1 VAL A  233  PHE A  249  1                                  17    
HELIX   11 AB2 ASP A  250  LYS A  253  5                                   4    
HELIX   12 AB3 GLY A  256  MSE A  264  1                                   9    
HELIX   13 AB4 GLY A  270  GLY A  287  1                                  18    
HELIX   14 AB5 ILE A  293  SER A  307  1                                  15    
HELIX   15 AB6 ASP A  309  ASN A  323  1                                  15    
HELIX   16 AB7 ALA A  329  GLY A  343  1                                  15    
HELIX   17 AB8 ASP A  344  TYR A  356  1                                  13    
HELIX   18 AB9 THR A  365  THR A  379  1                                  15    
HELIX   19 AC1 ASN B   58  PHE B   76  1                                  19    
HELIX   20 AC2 LYS B   91  THR B   96  1                                   6    
HELIX   21 AC3 ASN B  106  GLU B  118  1                                  13    
HELIX   22 AC4 GLU B  118  TYR B  127  1                                  10    
HELIX   23 AC5 GLU B  139  ALA B  145  1                                   7    
HELIX   24 AC6 ASN B  146  ALA B  151  5                                   6    
HELIX   25 AC7 LEU B  168  ARG B  170  5                                   3    
HELIX   26 AC8 MSE B  171  GLY B  182  1                                  12    
HELIX   27 AC9 ASN B  198  ARG B  213  1                                  16    
HELIX   28 AD1 VAL B  233  PHE B  249  1                                  17    
HELIX   29 AD2 ASP B  250  LYS B  253  5                                   4    
HELIX   30 AD3 GLY B  256  MSE B  264  1                                   9    
HELIX   31 AD4 GLY B  270  GLY B  287  1                                  18    
HELIX   32 AD5 ILE B  293  SER B  307  1                                  15    
HELIX   33 AD6 ASP B  309  ASN B  323  1                                  15    
HELIX   34 AD7 ALA B  329  ILE B  342  1                                  14    
HELIX   35 AD8 ASP B  344  TYR B  356  1                                  13    
HELIX   36 AD9 THR B  365  THR B  379  1                                  15    
SHEET    1 AA1 8 VAL A  21  SER A  28  0                                        
SHEET    2 AA1 8 ARG A  33  TYR A  40 -1  O  GLN A  35   N  PHE A  26           
SHEET    3 AA1 8 ILE A  83  VAL A  87 -1  O  VAL A  84   N  TYR A  40           
SHEET    4 AA1 8 TYR A  51  VAL A  56  1  N  VAL A  56   O  VAL A  85           
SHEET    5 AA1 8 ILE A 129  SER A 138  1  O  ILE A 136   N  VAL A  55           
SHEET    6 AA1 8 MSE A 159  PRO A 165  1  O  LEU A 163   N  ALA A 137           
SHEET    7 AA1 8 LEU A 187  VAL A 196  1  O  TYR A 190   N  SER A 162           
SHEET    8 AA1 8 VAL A 221  SER A 232  1  O  GLU A 222   N  LEU A 187           
SHEET    1 AA2 8 VAL B  21  SER B  28  0                                        
SHEET    2 AA2 8 ARG B  33  TYR B  40 -1  O  GLN B  35   N  PHE B  26           
SHEET    3 AA2 8 ILE B  83  VAL B  87 -1  O  VAL B  84   N  TYR B  40           
SHEET    4 AA2 8 TYR B  51  VAL B  56  1  N  VAL B  56   O  VAL B  87           
SHEET    5 AA2 8 ILE B 129  SER B 138  1  O  GLY B 134   N  LEU B  53           
SHEET    6 AA2 8 MSE B 159  PRO B 165  1  O  VAL B 161   N  VAL B 135           
SHEET    7 AA2 8 LEU B 187  VAL B 196  1  O  TYR B 190   N  SER B 162           
SHEET    8 AA2 8 VAL B 221  SER B 232  1  O  GLU B 222   N  LEU B 187           
LINK         C   LEU A  62                 N   MSE A  63     1555   1555  1.33  
LINK         C   MSE A  63                 N   GLU A  64     1555   1555  1.33  
LINK         C   SER A  68                 N   MSE A  69     1555   1555  1.33  
LINK         C   MSE A  69                 N   VAL A  70     1555   1555  1.33  
LINK         C   GLU A  78                 N   MSE A  79     1555   1555  1.33  
LINK         C   MSE A  79                 N   PRO A  80     1555   1555  1.34  
LINK         C   TYR A 148                 N   MSE A 149     1555   1555  1.33  
LINK         C   MSE A 149                 N   LEU A 150     1555   1555  1.33  
LINK         C   ASN A 158                 N   MSE A 159     1555   1555  1.33  
LINK         C   MSE A 159                 N   ILE A 160     1555   1555  1.33  
LINK         C   ARG A 170                 N   MSE A 171     1555   1555  1.33  
LINK         C   MSE A 171                 N   GLY A 172     1555   1555  1.33  
LINK         C   TYR A 190                 N   MSE A 191     1555   1555  1.33  
LINK         C   MSE A 191                 N   ALA A 192     1555   1555  1.33  
LINK         C   ALA A 211                 N   MSE A 212     1555   1555  1.33  
LINK         C   MSE A 212                 N   ARG A 213     1555   1555  1.33  
LINK         C   ASP A 246                 N   MSE A 247     1555   1555  1.33  
LINK         C   MSE A 247                 N   CYS A 248     1555   1555  1.33  
LINK         C   GLN A 263                 N   MSE A 264     1555   1555  1.33  
LINK         C   MSE A 264                 N   GLU A 265     1555   1555  1.33  
LINK         C   VAL A 297                 N   MSE A 298     1555   1555  1.33  
LINK         C   MSE A 298                 N   ALA A 299     1555   1555  1.33  
LINK         C   ALA A 329                 N   MSE A 330     1555   1555  1.33  
LINK         C   MSE A 330                 N   PRO A 331     1555   1555  1.35  
LINK         C   LEU B  62                 N   MSE B  63     1555   1555  1.33  
LINK         C   MSE B  63                 N   GLU B  64     1555   1555  1.33  
LINK         C   SER B  68                 N   MSE B  69     1555   1555  1.33  
LINK         C   MSE B  69                 N   VAL B  70     1555   1555  1.33  
LINK         C   GLU B  78                 N   MSE B  79     1555   1555  1.33  
LINK         C   MSE B  79                 N   PRO B  80     1555   1555  1.34  
LINK         C   TYR B 148                 N   MSE B 149     1555   1555  1.33  
LINK         C   MSE B 149                 N   LEU B 150     1555   1555  1.33  
LINK         C   ASN B 158                 N   MSE B 159     1555   1555  1.33  
LINK         C   MSE B 159                 N   ILE B 160     1555   1555  1.33  
LINK         C   ARG B 170                 N   MSE B 171     1555   1555  1.33  
LINK         C   MSE B 171                 N   GLY B 172     1555   1555  1.33  
LINK         C   TYR B 190                 N   MSE B 191     1555   1555  1.33  
LINK         C   MSE B 191                 N   ALA B 192     1555   1555  1.33  
LINK         C   ALA B 211                 N   MSE B 212     1555   1555  1.33  
LINK         C   MSE B 212                 N  AARG B 213     1555   1555  1.33  
LINK         C   MSE B 212                 N  BARG B 213     1555   1555  1.33  
LINK         C   ASP B 246                 N   MSE B 247     1555   1555  1.33  
LINK         C   MSE B 247                 N   CYS B 248     1555   1555  1.33  
LINK         C   GLN B 263                 N   MSE B 264     1555   1555  1.33  
LINK         C   MSE B 264                 N   GLU B 265     1555   1555  1.33  
LINK         C   VAL B 297                 N   MSE B 298     1555   1555  1.33  
LINK         C   MSE B 298                 N   ALA B 299     1555   1555  1.33  
LINK         C   ALA B 329                 N   MSE B 330     1555   1555  1.33  
LINK         C   MSE B 330                 N   PRO B 331     1555   1555  1.35  
SITE     1 AC1  5 ASP A 246  MSE A 247  ASP A 250  GLY B 230                    
SITE     2 AC1  5 SER B 232                                                     
SITE     1 AC2  1 GLY A 324                                                     
SITE     1 AC3  4 GLY A 230  SER A 232  ASP B 246  ASP B 250                    
SITE     1 AC4  4 TYR A 301  GLU A 337  ARG A 372  ASP B 362                    
SITE     1 AC5  1 GLY B 324                                                     
SITE     1 AC6  4 ASP A 362  TYR B 301  GLU B 337  ARG B 372                    
CRYST1  145.229  145.229  138.391  90.00  90.00 120.00 P 61         12          
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      0.006886  0.003975  0.000000        0.00000                         
SCALE2      0.000000  0.007951  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007226        0.00000                         
TER    2898      THR A 379                                                      
TER    5792      THR B 379                                                      
MASTER      514    0   31   36   16    0    7    6 5874    2  277   62          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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