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Database: PDB
Entry: 5IG1
LinkDB: 5IG1
Original site: 5IG1 
HEADER    TRANSFERASE                             26-FEB-16   5IG1              
TITLE     CRYSTAL STRUCTURE OF S. ROSETTA CAMKII KINASE DOMAIN                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMK/CAMK2 PROTEIN KINASE;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1-330;                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALPINGOECA ROSETTA;                            
SOURCE   3 ORGANISM_TAXID: 946362;                                              
SOURCE   4 STRAIN: ATCC 50818 / BSB-021;                                        
SOURCE   5 GENE: PTSG_10090;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CA2+/CAM-DEPENDENT KINASE, CHOANOFLAGELLATE, TRANSFERASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.BHATTACHARYYA,C.L.GEE,T.BARROS,J.KURIYAN                            
REVDAT   5   20-NOV-19 5IG1    1       REMARK                                   
REVDAT   4   27-SEP-17 5IG1    1       REMARK                                   
REVDAT   3   13-JUL-16 5IG1    1       REMARK                                   
REVDAT   2   06-APR-16 5IG1    1       AUTHOR                                   
REVDAT   1   23-MAR-16 5IG1    0                                                
JRNL        AUTH   M.BHATTACHARYYA,M.M.STRATTON,C.C.GOING,E.D.MCSPADDEN,        
JRNL        AUTH 2 Y.HUANG,A.C.SUSA,A.ELLEMAN,Y.M.CAO,N.PAPPIREDDI,P.BURKHARDT, 
JRNL        AUTH 3 C.L.GEE,T.BARROS,H.SCHULMAN,E.R.WILLIAMS,J.KURIYAN           
JRNL        TITL   MOLECULAR MECHANISM OF ACTIVATION-TRIGGERED SUBUNIT EXCHANGE 
JRNL        TITL 2 IN CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II.            
JRNL        REF    ELIFE                         V.   5       2016              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   26949248                                                     
JRNL        DOI    10.7554/ELIFE.13405                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.58                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.010                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 25737                          
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) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.860                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1319                            
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 46.5858 -  7.5900    1.00     2785   166  0.1708 0.2341        
REMARK   3     2  7.5900 -  6.0285    1.00     2809   156  0.1817 0.2121        
REMARK   3     3  6.0285 -  5.2677    1.00     2805   134  0.1839 0.2385        
REMARK   3     4  5.2677 -  4.7866    1.00     2805   160  0.1466 0.1657        
REMARK   3     5  4.7866 -  4.4438    1.00     2779   180  0.1332 0.1591        
REMARK   3     6  4.4438 -  4.1820    1.00     2799   125  0.1364 0.1811        
REMARK   3     7  4.1820 -  3.9726    1.00     2815   147  0.1481 0.1923        
REMARK   3     8  3.9726 -  3.7998    1.00     2846   122  0.1634 0.1813        
REMARK   3     9  3.7998 -  3.6536    1.00     2801   152  0.1861 0.2364        
REMARK   3    10  3.6536 -  3.5275    1.00     2823   130  0.1959 0.2293        
REMARK   3    11  3.5275 -  3.4173    1.00     2805   146  0.2023 0.2705        
REMARK   3    12  3.4173 -  3.3196    1.00     2772   150  0.2198 0.2536        
REMARK   3    13  3.3196 -  3.2323    1.00     2826   134  0.2190 0.2914        
REMARK   3    14  3.2323 -  3.1534    1.00     2811   160  0.2425 0.3317        
REMARK   3    15  3.1534 -  3.0817    1.00     2818   128  0.2615 0.3099        
REMARK   3    16  3.0817 -  3.0162    1.00     2782   150  0.2822 0.3631        
REMARK   3    17  3.0162 -  2.9559    1.00     2832   122  0.2909 0.3733        
REMARK   3    18  2.9559 -  2.9001    1.00     2871   120  0.3121 0.3019        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.270           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.72                          
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      :  0.004           5000                                  
REMARK   3   ANGLE     :  0.599           6765                                  
REMARK   3   CHIRALITY :  0.044            737                                  
REMARK   3   PLANARITY :  0.004            866                                  
REMARK   3   DIHEDRAL  : 12.880           3025                                  
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 3 THROUGH 55 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -15.9371  28.4421 -15.1608              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4686 T22:   0.3315                                     
REMARK   3      T33:   0.3903 T12:   0.0257                                     
REMARK   3      T13:  -0.1125 T23:   0.0359                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9930 L22:   7.0002                                     
REMARK   3      L33:   3.3288 L12:   0.8635                                     
REMARK   3      L13:   0.4996 L23:   1.2902                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3400 S12:   0.4524 S13:   0.3823                       
REMARK   3      S21:  -0.9034 S22:   0.0960 S23:   0.4985                       
REMARK   3      S31:  -0.2143 S32:  -0.2856 S33:   0.1274                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 156 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -10.3456  23.6522   0.5744              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3548 T22:   0.3062                                     
REMARK   3      T33:   0.2790 T12:   0.0804                                     
REMARK   3      T13:   0.0159 T23:  -0.0300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3277 L22:   0.9039                                     
REMARK   3      L33:   2.8634 L12:   0.2248                                     
REMARK   3      L13:   1.9628 L23:  -0.4283                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2674 S12:  -0.2077 S13:   0.5257                       
REMARK   3      S21:  -0.0857 S22:   0.0221 S23:   0.0923                       
REMARK   3      S31:  -0.3056 S32:  -0.1680 S33:   0.2652                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 157 THROUGH 286 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.5615  10.0883  11.6921              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3300 T22:   0.5139                                     
REMARK   3      T33:   0.3293 T12:   0.0816                                     
REMARK   3      T13:   0.0484 T23:   0.0900                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5940 L22:   2.3028                                     
REMARK   3      L33:   2.0131 L12:   0.5254                                     
REMARK   3      L13:   1.1268 L23:  -0.4171                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0961 S12:  -0.9218 S13:  -1.0006                       
REMARK   3      S21:   0.1474 S22:  -0.0163 S23:   0.0204                       
REMARK   3      S31:   0.2037 S32:  -0.3184 S33:  -0.0576                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 287 THROUGH 302 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.2815   9.2179  -1.6109              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5055 T22:   0.5885                                     
REMARK   3      T33:   0.3747 T12:   0.1306                                     
REMARK   3      T13:   0.1191 T23:  -0.0861                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0124 L22:   8.2349                                     
REMARK   3      L33:   9.2666 L12:   4.7790                                     
REMARK   3      L13:   6.5426 L23:   2.0607                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4602 S12:   1.0313 S13:  -0.2923                       
REMARK   3      S21:  -0.7953 S22:   0.1033 S23:  -0.7362                       
REMARK   3      S31:   0.6438 S32:   0.0123 S33:  -0.6774                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 30 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -40.5391   9.6215  -1.3748              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5202 T22:   0.8773                                     
REMARK   3      T33:   0.7512 T12:   0.0245                                     
REMARK   3      T13:   0.0963 T23:   0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5929 L22:   2.0216                                     
REMARK   3      L33:   5.2353 L12:  -1.9508                                     
REMARK   3      L13:   1.3312 L23:   0.8672                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1317 S12:   0.7979 S13:  -0.8030                       
REMARK   3      S21:  -0.1933 S22:  -0.2726 S23:   0.9077                       
REMARK   3      S31:   0.0403 S32:  -0.6178 S33:   0.3263                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 31 THROUGH 156 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -40.4532   4.2660  13.7734              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3779 T22:   0.8234                                     
REMARK   3      T33:   0.9011 T12:   0.0346                                     
REMARK   3      T13:   0.0152 T23:   0.1901                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8389 L22:   1.5329                                     
REMARK   3      L33:   2.6250 L12:   0.9760                                     
REMARK   3      L13:  -2.6914 L23:  -0.5650                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3654 S12:  -0.1711 S13:  -1.1323                       
REMARK   3      S21:  -0.0014 S22:  -0.1052 S23:  -0.4210                       
REMARK   3      S31:   0.3615 S32:  -0.0603 S33:   0.3783                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 157 THROUGH 195 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -54.9617   0.9800  22.4106              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4234 T22:   0.7478                                     
REMARK   3      T33:   0.7747 T12:  -0.0253                                     
REMARK   3      T13:   0.1262 T23:   0.2991                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5079 L22:   1.7801                                     
REMARK   3      L33:   1.7058 L12:   1.2787                                     
REMARK   3      L13:  -0.1730 L23:  -1.5401                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4314 S12:  -0.8736 S13:  -1.7509                       
REMARK   3      S21:   0.0677 S22:   0.0363 S23:  -0.2137                       
REMARK   3      S31:   0.0656 S32:  -0.0081 S33:   0.3510                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 196 THROUGH 265 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -48.7115 -13.4248  28.1610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7543 T22:   1.0873                                     
REMARK   3      T33:   2.1985 T12:   0.1895                                     
REMARK   3      T13:   0.2994 T23:   0.9637                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8887 L22:   2.0069                                     
REMARK   3      L33:   4.5231 L12:  -1.8528                                     
REMARK   3      L13:   0.5202 L23:   0.4502                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4306 S12:  -0.7888 S13:  -2.2712                       
REMARK   3      S21:  -0.0434 S22:  -0.6001 S23:  -0.4612                       
REMARK   3      S31:   1.7862 S32:  -0.0117 S33:  -0.0978                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 266 THROUGH 302 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -36.4785 -11.8724  26.1004              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7480 T22:   1.2711                                     
REMARK   3      T33:   2.0199 T12:   0.1459                                     
REMARK   3      T13:   0.3002 T23:   0.6410                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4932 L22:   6.4089                                     
REMARK   3      L33:   2.9007 L12:  -4.0066                                     
REMARK   3      L13:  -0.5745 L23:   0.4475                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2661 S12:  -1.1781 S13:  -1.5790                       
REMARK   3      S21:   0.2020 S22:   0.0114 S23:  -0.9982                       
REMARK   3      S31:   0.6718 S32:   0.5944 S33:   0.0930                       
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 5IG1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218774.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : M1: PARABOLA M2: TORROID           
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27096                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.580                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.10300                            
REMARK 200  R SYM                      (I) : 0.10300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2BDW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M SODIUM PHOSPHATE MONOBASIC         
REMARK 280  MONOHYDRATE, POTASSIUM PHOSPHATE DIBASIC PH 6.9, VAPOR DIFFUSION,   
REMARK 280  SITTING DROP, TEMPERATURE 295K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
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,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
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       61.89600            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       92.84400            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       30.94800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: AS PER THE AUTHORS THE BIOLOGICAL ASSEMBLY IS UNKNOWN        
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     LYS A   303                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     GLY A   305                                                      
REMARK 465     VAL A   306                                                      
REMARK 465     ASN A   307                                                      
REMARK 465     ALA A   308                                                      
REMARK 465     VAL A   309                                                      
REMARK 465     ILE A   310                                                      
REMARK 465     GLY A   311                                                      
REMARK 465     VAL A   312                                                      
REMARK 465     SER A   313                                                      
REMARK 465     LYS A   314                                                      
REMARK 465     MET A   315                                                      
REMARK 465     MET A   316                                                      
REMARK 465     ARG A   317                                                      
REMARK 465     THR A   318                                                      
REMARK 465     MET A   319                                                      
REMARK 465     GLN A   320                                                      
REMARK 465     GLU A   321                                                      
REMARK 465     ALA A   322                                                      
REMARK 465     THR A   323                                                      
REMARK 465     ARG A   324                                                      
REMARK 465     ALA A   325                                                      
REMARK 465     LEU A   326                                                      
REMARK 465     THR A   327                                                      
REMARK 465     LEU A   328                                                      
REMARK 465     SER A   329                                                      
REMARK 465     ALA A   330                                                      
REMARK 465     LYS A   331                                                      
REMARK 465     SER A   332                                                      
REMARK 465     ALA A   333                                                      
REMARK 465     ALA A   334                                                      
REMARK 465     ALA A   335                                                      
REMARK 465     LEU A   336                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     HIS A   338                                                      
REMARK 465     HIS A   339                                                      
REMARK 465     HIS A   340                                                      
REMARK 465     HIS A   341                                                      
REMARK 465     HIS A   342                                                      
REMARK 465     HIS A   343                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     PRO B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     ASN B   307                                                      
REMARK 465     ALA B   308                                                      
REMARK 465     VAL B   309                                                      
REMARK 465     ILE B   310                                                      
REMARK 465     GLY B   311                                                      
REMARK 465     VAL B   312                                                      
REMARK 465     SER B   313                                                      
REMARK 465     LYS B   314                                                      
REMARK 465     MET B   315                                                      
REMARK 465     MET B   316                                                      
REMARK 465     ARG B   317                                                      
REMARK 465     THR B   318                                                      
REMARK 465     MET B   319                                                      
REMARK 465     GLN B   320                                                      
REMARK 465     GLU B   321                                                      
REMARK 465     ALA B   322                                                      
REMARK 465     THR B   323                                                      
REMARK 465     ARG B   324                                                      
REMARK 465     ALA B   325                                                      
REMARK 465     LEU B   326                                                      
REMARK 465     THR B   327                                                      
REMARK 465     LEU B   328                                                      
REMARK 465     SER B   329                                                      
REMARK 465     ALA B   330                                                      
REMARK 465     LYS B   331                                                      
REMARK 465     SER B   332                                                      
REMARK 465     ALA B   333                                                      
REMARK 465     ALA B   334                                                      
REMARK 465     ALA B   335                                                      
REMARK 465     LEU B   336                                                      
REMARK 465     GLU B   337                                                      
REMARK 465     HIS B   338                                                      
REMARK 465     HIS B   339                                                      
REMARK 465     HIS B   340                                                      
REMARK 465     HIS B   341                                                      
REMARK 465     HIS B   342                                                      
REMARK 465     HIS B   343                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  52      -73.10    -46.95                                   
REMARK 500    ASP A  86     -152.87   -109.41                                   
REMARK 500    SER A  88      -21.32   -150.10                                   
REMARK 500    ARG A 139      -17.47     71.09                                   
REMARK 500    ASP A 161       81.21     53.72                                   
REMARK 500    ASP A 195     -158.55   -151.44                                   
REMARK 500    LEU A 256       38.14    -99.50                                   
REMARK 500    SER B  22       33.70    -91.90                                   
REMARK 500    PHE B  29       23.72   -152.33                                   
REMARK 500    ASP B  86     -167.85   -111.15                                   
REMARK 500    THR B 108       46.88   -102.00                                   
REMARK 500    ARG B 139      -18.33     68.70                                   
REMARK 500    ASP B 161       71.50     52.53                                   
REMARK 500    GLN B 170       48.75   -146.04                                   
REMARK 500    ASP B 195     -158.15   -138.79                                   
REMARK 500    LEU B 210       -6.29    -58.64                                   
REMARK 500    CYS B 232       75.25     53.66                                   
REMARK 500    GLN B 233       72.78   -119.18                                   
REMARK 500    PHE B 236       72.43   -115.95                                   
REMARK 500    LEU B 256       33.33    -90.18                                   
REMARK 500    GLN B 287      -38.34   -131.64                                   
REMARK 500    LYS B 303      161.69     68.48                                   
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 PO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5IG0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IG3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IG4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IG5   RELATED DB: PDB                                   
DBREF  5IG1 A    3   332  UNP    F2UPG5   F2UPG5_SALR5     1    330             
DBREF  5IG1 B    3   332  UNP    F2UPG5   F2UPG5_SALR5     1    330             
SEQADV 5IG1 GLY A    0  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 PRO A    1  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS A    2  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 ALA A  333  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 ALA A  334  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 ALA A  335  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 LEU A  336  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 GLU A  337  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS A  338  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS A  339  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS A  340  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS A  341  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS A  342  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS A  343  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 GLY B    0  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 PRO B    1  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS B    2  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 ALA B  333  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 ALA B  334  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 ALA B  335  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 LEU B  336  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 GLU B  337  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS B  338  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS B  339  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS B  340  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS B  341  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS B  342  UNP  F2UPG5              EXPRESSION TAG                 
SEQADV 5IG1 HIS B  343  UNP  F2UPG5              EXPRESSION TAG                 
SEQRES   1 A  344  GLY PRO HIS MET GLU THR GLU THR SER PHE PHE ASP LEU          
SEQRES   2 A  344  TYR ASP VAL ASP LEU LYS ASP LYS ARG SER VAL ILE GLY          
SEQRES   3 A  344  LYS GLY ALA PHE SER THR VAL HIS ARG CYS VAL ASN LYS          
SEQRES   4 A  344  ARG THR GLY GLU VAL CYS ALA VAL LYS VAL ILE ALA LEU          
SEQRES   5 A  344  LYS SER LEU ARG SER SER GLU ILE ASN LYS ILE LYS ARG          
SEQRES   6 A  344  GLU ILE GLY ILE CYS SER SER LEU GLN HIS GLU HIS ILE          
SEQRES   7 A  344  VAL SER MET ARG ARG ALA PHE ARG ASP GLU SER HIS PHE          
SEQRES   8 A  344  TYR LEU VAL PHE GLU TYR VAL SER GLY GLY GLU LEU PHE          
SEQRES   9 A  344  ASP GLU ILE VAL THR ARG LYS PHE TYR ASN GLU LYS ASP          
SEQRES  10 A  344  ALA SER ALA CYS MET HIS GLN ILE LEU SER ALA LEU GLN          
SEQRES  11 A  344  HIS CYS HIS SER LYS ASN ILE ILE HIS ARG ASP LEU LYS          
SEQRES  12 A  344  PRO GLU ASN LEU LEU LEU ALA SER LYS ASP PRO ASN ALA          
SEQRES  13 A  344  PRO VAL LYS ILE THR ASP PHE GLY LEU ALA VAL ILE MET          
SEQRES  14 A  344  GLU GLN GLY PRO THR TYR PHE GLY PHE ALA GLY THR PRO          
SEQRES  15 A  344  GLY TYR LEU SER PRO GLU VAL ILE ARG ARG VAL PRO TYR          
SEQRES  16 A  344  ASP THR ALA VAL ASP VAL TRP ALA CYS GLY VAL ILE LEU          
SEQRES  17 A  344  TYR ILE LEU LEU VAL GLY TYR PRO PRO PHE TRP GLU GLU          
SEQRES  18 A  344  ASP HIS GLN LYS LEU TYR ALA GLN ILE LYS ASN CYS GLN          
SEQRES  19 A  344  TYR ASP PHE PRO SER PRO GLU TRP ASP SER VAL THR THR          
SEQRES  20 A  344  ALA ALA LYS GLU LEU ILE LYS ALA MET LEU GLU PRO ASN          
SEQRES  21 A  344  PRO LYS ARG ARG PRO THR VAL GLN GLU LEU LEU GLN HIS          
SEQRES  22 A  344  PRO TRP ILE ALA ARG ARG ASP VAL PRO GLY SER VAL HIS          
SEQRES  23 A  344  ARG GLN ALA THR LEU GLU GLU LEU LYS LYS PHE ASN ALA          
SEQRES  24 A  344  ARG ARG LYS LEU LYS GLY GLY VAL ASN ALA VAL ILE GLY          
SEQRES  25 A  344  VAL SER LYS MET MET ARG THR MET GLN GLU ALA THR ARG          
SEQRES  26 A  344  ALA LEU THR LEU SER ALA LYS SER ALA ALA ALA LEU GLU          
SEQRES  27 A  344  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 B  344  GLY PRO HIS MET GLU THR GLU THR SER PHE PHE ASP LEU          
SEQRES   2 B  344  TYR ASP VAL ASP LEU LYS ASP LYS ARG SER VAL ILE GLY          
SEQRES   3 B  344  LYS GLY ALA PHE SER THR VAL HIS ARG CYS VAL ASN LYS          
SEQRES   4 B  344  ARG THR GLY GLU VAL CYS ALA VAL LYS VAL ILE ALA LEU          
SEQRES   5 B  344  LYS SER LEU ARG SER SER GLU ILE ASN LYS ILE LYS ARG          
SEQRES   6 B  344  GLU ILE GLY ILE CYS SER SER LEU GLN HIS GLU HIS ILE          
SEQRES   7 B  344  VAL SER MET ARG ARG ALA PHE ARG ASP GLU SER HIS PHE          
SEQRES   8 B  344  TYR LEU VAL PHE GLU TYR VAL SER GLY GLY GLU LEU PHE          
SEQRES   9 B  344  ASP GLU ILE VAL THR ARG LYS PHE TYR ASN GLU LYS ASP          
SEQRES  10 B  344  ALA SER ALA CYS MET HIS GLN ILE LEU SER ALA LEU GLN          
SEQRES  11 B  344  HIS CYS HIS SER LYS ASN ILE ILE HIS ARG ASP LEU LYS          
SEQRES  12 B  344  PRO GLU ASN LEU LEU LEU ALA SER LYS ASP PRO ASN ALA          
SEQRES  13 B  344  PRO VAL LYS ILE THR ASP PHE GLY LEU ALA VAL ILE MET          
SEQRES  14 B  344  GLU GLN GLY PRO THR TYR PHE GLY PHE ALA GLY THR PRO          
SEQRES  15 B  344  GLY TYR LEU SER PRO GLU VAL ILE ARG ARG VAL PRO TYR          
SEQRES  16 B  344  ASP THR ALA VAL ASP VAL TRP ALA CYS GLY VAL ILE LEU          
SEQRES  17 B  344  TYR ILE LEU LEU VAL GLY TYR PRO PRO PHE TRP GLU GLU          
SEQRES  18 B  344  ASP HIS GLN LYS LEU TYR ALA GLN ILE LYS ASN CYS GLN          
SEQRES  19 B  344  TYR ASP PHE PRO SER PRO GLU TRP ASP SER VAL THR THR          
SEQRES  20 B  344  ALA ALA LYS GLU LEU ILE LYS ALA MET LEU GLU PRO ASN          
SEQRES  21 B  344  PRO LYS ARG ARG PRO THR VAL GLN GLU LEU LEU GLN HIS          
SEQRES  22 B  344  PRO TRP ILE ALA ARG ARG ASP VAL PRO GLY SER VAL HIS          
SEQRES  23 B  344  ARG GLN ALA THR LEU GLU GLU LEU LYS LYS PHE ASN ALA          
SEQRES  24 B  344  ARG ARG LYS LEU LYS GLY GLY VAL ASN ALA VAL ILE GLY          
SEQRES  25 B  344  VAL SER LYS MET MET ARG THR MET GLN GLU ALA THR ARG          
SEQRES  26 B  344  ALA LEU THR LEU SER ALA LYS SER ALA ALA ALA LEU GLU          
SEQRES  27 B  344  HIS HIS HIS HIS HIS HIS                                      
HET    PO4  A 401       5                                                       
HET    PO4  A 402       5                                                       
HET    PO4  B 401       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   3  PO4    3(O4 P 3-)                                                   
FORMUL   6  HOH   *35(H2 O)                                                     
HELIX    1 AA1 SER A    8  LEU A   12  1                                   5    
HELIX    2 AA2 ASP A   19  ARG A   21  5                                   3    
HELIX    3 AA3 ARG A   55  LEU A   72  1                                  18    
HELIX    4 AA4 LEU A  102  VAL A  107  1                                   6    
HELIX    5 AA5 ASN A  113  LYS A  134  1                                  22    
HELIX    6 AA6 LYS A  142  GLU A  144  5                                   3    
HELIX    7 AA7 THR A  180  LEU A  184  5                                   5    
HELIX    8 AA8 SER A  185  ARG A  190  1                                   6    
HELIX    9 AA9 THR A  196  GLY A  213  1                                  18    
HELIX   10 AB1 ASP A  221  ASN A  231  1                                  11    
HELIX   11 AB2 PRO A  239  VAL A  244  5                                   6    
HELIX   12 AB3 THR A  245  LEU A  256  1                                  12    
HELIX   13 AB4 ASN A  259  ARG A  263  5                                   5    
HELIX   14 AB5 THR A  265  GLN A  271  1                                   7    
HELIX   15 AB6 HIS A  272  ARG A  277  1                                   6    
HELIX   16 AB7 ARG A  286  LEU A  302  1                                  17    
HELIX   17 AB8 SER B    8  LEU B   12  1                                   5    
HELIX   18 AB9 LYS B   52  LEU B   54  5                                   3    
HELIX   19 AC1 ARG B   55  SER B   71  1                                  17    
HELIX   20 AC2 LEU B  102  VAL B  107  1                                   6    
HELIX   21 AC3 ASN B  113  LYS B  134  1                                  22    
HELIX   22 AC4 LYS B  142  GLU B  144  5                                   3    
HELIX   23 AC5 THR B  180  LEU B  184  5                                   5    
HELIX   24 AC6 SER B  185  ARG B  191  1                                   7    
HELIX   25 AC7 THR B  196  GLY B  213  1                                  18    
HELIX   26 AC8 ASP B  221  CYS B  232  1                                  12    
HELIX   27 AC9 THR B  245  LEU B  256  1                                  12    
HELIX   28 AD1 THR B  265  LEU B  270  1                                   6    
HELIX   29 AD2 GLN B  287  LYS B  301  1                                  15    
SHEET    1 AA1 3 TYR A  13  ASP A  14  0                                        
SHEET    2 AA1 3 THR A  31  ASN A  37 -1  O  VAL A  36   N  ASP A  14           
SHEET    3 AA1 3 VAL A  23  LYS A  26 -1  N  GLY A  25   O  VAL A  32           
SHEET    1 AA2 5 TYR A  13  ASP A  14  0                                        
SHEET    2 AA2 5 THR A  31  ASN A  37 -1  O  VAL A  36   N  ASP A  14           
SHEET    3 AA2 5 VAL A  43  ALA A  50 -1  O  CYS A  44   N  CYS A  35           
SHEET    4 AA2 5 HIS A  89  GLU A  95 -1  O  PHE A  90   N  ILE A  49           
SHEET    5 AA2 5 MET A  80  ARG A  85 -1  N  PHE A  84   O  TYR A  91           
SHEET    1 AA3 3 GLY A 100  GLU A 101  0                                        
SHEET    2 AA3 3 LEU A 146  LEU A 148 -1  O  LEU A 148   N  GLY A 100           
SHEET    3 AA3 3 VAL A 157  ILE A 159 -1  O  LYS A 158   N  LEU A 147           
SHEET    1 AA4 2 ILE A 136  ILE A 137  0                                        
SHEET    2 AA4 2 VAL A 166  ILE A 167 -1  O  VAL A 166   N  ILE A 137           
SHEET    1 AA5 3 TYR B  13  ASP B  14  0                                        
SHEET    2 AA5 3 SER B  30  ASN B  37 -1  O  VAL B  36   N  ASP B  14           
SHEET    3 AA5 3 VAL B  23  LYS B  26 -1  N  ILE B  24   O  VAL B  32           
SHEET    1 AA6 5 TYR B  13  ASP B  14  0                                        
SHEET    2 AA6 5 SER B  30  ASN B  37 -1  O  VAL B  36   N  ASP B  14           
SHEET    3 AA6 5 VAL B  43  ALA B  50 -1  O  CYS B  44   N  CYS B  35           
SHEET    4 AA6 5 HIS B  89  GLU B  95 -1  O  PHE B  94   N  ALA B  45           
SHEET    5 AA6 5 MET B  80  ARG B  85 -1  N  PHE B  84   O  TYR B  91           
SHEET    1 AA7 2 ILE B 136  ILE B 137  0                                        
SHEET    2 AA7 2 VAL B 166  ILE B 167 -1  O  VAL B 166   N  ILE B 137           
SHEET    1 AA8 2 LEU B 146  LEU B 148  0                                        
SHEET    2 AA8 2 VAL B 157  ILE B 159 -1  O  LYS B 158   N  LEU B 147           
CISPEP   1 SER A  238    PRO A  239          0         0.14                     
CISPEP   2 SER B  238    PRO B  239          0        -0.03                     
SITE     1 AC1  4 ARG A  34  TYR A  96  TYR B 174  ARG B 191                    
SITE     1 AC2  2 LYS A  63  ARG A  85                                          
SITE     1 AC3  4 TYR A 174  ARG A 191  ARG B  34  TYR B  96                    
CRYST1  100.031  100.031  123.792  90.00  90.00  90.00 P 43          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      0.009997  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009997  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008078        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system