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Database: PDB
Entry: 5IG3
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HEADER    TRANSFERASE                             26-FEB-16   5IG3              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN CAMKII-ALPHA HUB                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT
COMPND   3 ALPHA;                                                               
COMPND   4 CHAIN: A, B, C, D, E, F;                                             
COMPND   5 FRAGMENT: UNP RESIDUES 345-475;                                      
COMPND   6 SYNONYM: CAMK-II SUBUNIT ALPHA;                                      
COMPND   7 EC: 2.7.11.17;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CAMK2A, CAMKA, KIAA0968;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CA2+/CAM-DEPENDENT KINASE ALPHA, HUB, TRANSFERASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.MCSPADDEN,Y.M.CAO,M.BHATTACHARYYA,C.L.GEE,T.BARROS,J.KURIYAN        
REVDAT   6   27-SEP-23 5IG3    1       REMARK                                   
REVDAT   5   20-NOV-19 5IG3    1       REMARK                                   
REVDAT   4   27-SEP-17 5IG3    1       REMARK                                   
REVDAT   3   13-JUL-16 5IG3    1       REMARK                                   
REVDAT   2   06-APR-16 5IG3    1       AUTHOR                                   
REVDAT   1   23-MAR-16 5IG3    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.    2.75 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) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.63                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.010                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 23820                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.710                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1184                            
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 48.6384 -  6.7764    1.00     2914   161  0.2166 0.2508        
REMARK   3     2  6.7764 -  5.3809    1.00     2904   170  0.2439 0.2737        
REMARK   3     3  5.3809 -  4.7013    1.00     2919   145  0.1745 0.2222        
REMARK   3     4  4.7013 -  4.2718    1.00     2894   151  0.1654 0.2027        
REMARK   3     5  4.2718 -  3.9657    1.00     2938   162  0.1845 0.2421        
REMARK   3     6  3.9657 -  3.7320    1.00     2907   140  0.2030 0.2804        
REMARK   3     7  3.7320 -  3.5452    1.00     2945   145  0.2220 0.3004        
REMARK   3     8  3.5452 -  3.3909    1.00     2977   124  0.2465 0.3612        
REMARK   3     9  3.3909 -  3.2604    1.00     2910   132  0.2655 0.3352        
REMARK   3    10  3.2604 -  3.1479    1.00     2910   153  0.2488 0.3070        
REMARK   3    11  3.1479 -  3.0495    1.00     2930   160  0.2620 0.3020        
REMARK   3    12  3.0495 -  2.9623    1.00     2909   154  0.2879 0.3351        
REMARK   3    13  2.9623 -  2.8843    1.00     2914   124  0.3073 0.3641        
REMARK   3    14  2.8843 -  2.8140    1.00     2969   102  0.3379 0.3618        
REMARK   3    15  2.8140 -  2.7500    1.00     2950   146  0.4093 0.4363        
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)     : 0.500            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.540           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 78.00                          
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      :  0.002           6459                                  
REMARK   3   ANGLE     :  0.505           8727                                  
REMARK   3   CHIRALITY :  0.042            921                                  
REMARK   3   PLANARITY :  0.003           1131                                  
REMARK   3   DIHEDRAL  : 11.499           3798                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN 'A' AND RESID 329 THROUGH 472)                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.0728  75.2717 -10.6222              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6364 T22:   0.6067                                     
REMARK   3      T33:   0.5676 T12:  -0.0422                                     
REMARK   3      T13:   0.1766 T23:  -0.0959                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3460 L22:   3.6227                                     
REMARK   3      L33:   4.6260 L12:   0.5762                                     
REMARK   3      L13:   0.8026 L23:  -2.0140                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0342 S12:   0.3885 S13:  -0.1134                       
REMARK   3      S21:  -0.6569 S22:  -0.0480 S23:  -0.2542                       
REMARK   3      S31:   0.1548 S32:   0.5510 S33:   0.0478                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN 'B' AND RESID 344 THROUGH 473)                  
REMARK   3    ORIGIN FOR THE GROUP (A): -55.0853  49.4096 -27.8143              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6917 T22:   0.5191                                     
REMARK   3      T33:   0.5444 T12:   0.0791                                     
REMARK   3      T13:  -0.0506 T23:  -0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6877 L22:   5.4568                                     
REMARK   3      L33:   5.3146 L12:   0.6597                                     
REMARK   3      L13:  -0.4139 L23:  -1.0112                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0276 S12:   0.4719 S13:  -0.4200                       
REMARK   3      S21:  -0.7411 S22:  -0.0312 S23:   0.0858                       
REMARK   3      S31:   0.4074 S32:  -0.1636 S33:   0.0390                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN 'C' AND RESID 331 THROUGH 472)                  
REMARK   3    ORIGIN FOR THE GROUP (A): -51.0029  24.3888  -5.5590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8046 T22:   0.4616                                     
REMARK   3      T33:   0.6548 T12:   0.0360                                     
REMARK   3      T13:  -0.0625 T23:   0.0218                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8488 L22:   4.3143                                     
REMARK   3      L33:   6.0667 L12:  -1.7309                                     
REMARK   3      L13:   1.6302 L23:  -0.8191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2155 S12:   0.0288 S13:  -0.7827                       
REMARK   3      S21:  -0.6741 S22:   0.0057 S23:   0.3548                       
REMARK   3      S31:   1.0598 S32:   0.0127 S33:  -0.1751                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN 'D' AND RESID 331 THROUGH 473)                  
REMARK   3    ORIGIN FOR THE GROUP (A): -24.7258  24.6518  15.0052              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6892 T22:   0.6674                                     
REMARK   3      T33:   0.7338 T12:   0.2513                                     
REMARK   3      T13:   0.0374 T23:  -0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5725 L22:   4.8471                                     
REMARK   3      L33:   3.7395 L12:  -0.0060                                     
REMARK   3      L13:   1.4812 L23:  -0.2240                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1072 S12:   0.2654 S13:  -0.6975                       
REMARK   3      S21:  -0.3122 S22:  -0.1248 S23:  -0.3376                       
REMARK   3      S31:   0.8125 S32:   0.6089 S33:   0.0802                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN 'E' AND RESID 344 THROUGH 473)                  
REMARK   3    ORIGIN FOR THE GROUP (A): -32.9364  75.3487 -29.6994              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1827 T22:   0.6504                                     
REMARK   3      T33:   0.5702 T12:  -0.0432                                     
REMARK   3      T13:  -0.0378 T23:   0.0475                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4790 L22:   1.4467                                     
REMARK   3      L33:   4.1374 L12:   0.6252                                     
REMARK   3      L13:   0.4026 L23:   1.2998                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0444 S12:   0.8949 S13:   0.2399                       
REMARK   3      S21:  -0.8751 S22:  -0.0450 S23:  -0.0139                       
REMARK   3      S31:  -1.0488 S32:   0.4395 S33:   0.0704                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN 'F' AND RESID 344 THROUGH 472)                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.0041  49.3238  12.8680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5275 T22:   1.1771                                     
REMARK   3      T33:   0.8518 T12:   0.0278                                     
REMARK   3      T13:   0.0657 T23:   0.0690                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1560 L22:   5.0761                                     
REMARK   3      L33:   1.8555 L12:  -0.2782                                     
REMARK   3      L13:  -0.4964 L23:  -0.9169                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1455 S12:  -0.6869 S13:  -0.4616                       
REMARK   3      S21:  -0.2924 S22:  -0.0542 S23:  -1.1331                       
REMARK   3      S31:   0.0206 S32:   1.2963 S33:   0.0954                       
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 5IG3 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_1000218779.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUL-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.3                                
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   : 25096                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.640                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.900                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : 0.07900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.12400                            
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: 1HKX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 35 % (V/V) MPD, 0.1 M HEPES PH 7.3,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.28850            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       44.94400            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       44.94400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      169.93275            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       44.94400            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       44.94400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       56.64425            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       44.94400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       44.94400            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      169.93275            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       44.94400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       44.94400            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       56.64425            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      113.28850            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 27640 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 66900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -221.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000      -89.88800            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000       89.88800            
REMARK 350   BIOMT3   2  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   323                                                      
REMARK 465     SER A   324                                                      
REMARK 465     SER A   325                                                      
REMARK 465     HIS A   326                                                      
REMARK 465     HIS A   327                                                      
REMARK 465     HIS A   328                                                      
REMARK 465     PRO A   473                                                      
REMARK 465     SER A   474                                                      
REMARK 465     VAL A   475                                                      
REMARK 465     GLY B   323                                                      
REMARK 465     SER B   324                                                      
REMARK 465     SER B   325                                                      
REMARK 465     HIS B   326                                                      
REMARK 465     HIS B   327                                                      
REMARK 465     HIS B   328                                                      
REMARK 465     HIS B   329                                                      
REMARK 465     HIS B   330                                                      
REMARK 465     HIS B   331                                                      
REMARK 465     SER B   332                                                      
REMARK 465     SER B   333                                                      
REMARK 465     GLY B   334                                                      
REMARK 465     LEU B   335                                                      
REMARK 465     GLU B   336                                                      
REMARK 465     VAL B   337                                                      
REMARK 465     LEU B   338                                                      
REMARK 465     PHE B   339                                                      
REMARK 465     GLN B   340                                                      
REMARK 465     GLY B   341                                                      
REMARK 465     PRO B   342                                                      
REMARK 465     HIS B   343                                                      
REMARK 465     SER B   404                                                      
REMARK 465     ARG B   405                                                      
REMARK 465     ASN B   406                                                      
REMARK 465     SER B   474                                                      
REMARK 465     VAL B   475                                                      
REMARK 465     GLY C   323                                                      
REMARK 465     SER C   324                                                      
REMARK 465     SER C   325                                                      
REMARK 465     HIS C   326                                                      
REMARK 465     HIS C   327                                                      
REMARK 465     HIS C   328                                                      
REMARK 465     HIS C   329                                                      
REMARK 465     HIS C   330                                                      
REMARK 465     LEU C   335                                                      
REMARK 465     GLU C   336                                                      
REMARK 465     VAL C   337                                                      
REMARK 465     LEU C   338                                                      
REMARK 465     PHE C   339                                                      
REMARK 465     GLN C   340                                                      
REMARK 465     GLY C   341                                                      
REMARK 465     PRO C   342                                                      
REMARK 465     ARG C   405                                                      
REMARK 465     ASN C   406                                                      
REMARK 465     PRO C   473                                                      
REMARK 465     SER C   474                                                      
REMARK 465     VAL C   475                                                      
REMARK 465     GLY D   323                                                      
REMARK 465     SER D   324                                                      
REMARK 465     SER D   325                                                      
REMARK 465     HIS D   326                                                      
REMARK 465     HIS D   327                                                      
REMARK 465     HIS D   328                                                      
REMARK 465     HIS D   329                                                      
REMARK 465     HIS D   330                                                      
REMARK 465     GLY D   334                                                      
REMARK 465     LEU D   335                                                      
REMARK 465     GLU D   336                                                      
REMARK 465     VAL D   337                                                      
REMARK 465     LEU D   338                                                      
REMARK 465     PHE D   339                                                      
REMARK 465     GLN D   340                                                      
REMARK 465     GLY D   341                                                      
REMARK 465     PRO D   342                                                      
REMARK 465     HIS D   343                                                      
REMARK 465     TRP D   403                                                      
REMARK 465     SER D   404                                                      
REMARK 465     ARG D   405                                                      
REMARK 465     ASN D   406                                                      
REMARK 465     SER D   407                                                      
REMARK 465     LYS D   408                                                      
REMARK 465     SER D   474                                                      
REMARK 465     VAL D   475                                                      
REMARK 465     GLY E   323                                                      
REMARK 465     SER E   324                                                      
REMARK 465     SER E   325                                                      
REMARK 465     HIS E   326                                                      
REMARK 465     HIS E   327                                                      
REMARK 465     HIS E   328                                                      
REMARK 465     HIS E   329                                                      
REMARK 465     HIS E   330                                                      
REMARK 465     HIS E   331                                                      
REMARK 465     SER E   332                                                      
REMARK 465     SER E   333                                                      
REMARK 465     GLY E   334                                                      
REMARK 465     LEU E   335                                                      
REMARK 465     GLU E   336                                                      
REMARK 465     VAL E   337                                                      
REMARK 465     LEU E   338                                                      
REMARK 465     PHE E   339                                                      
REMARK 465     GLN E   340                                                      
REMARK 465     GLY E   341                                                      
REMARK 465     PRO E   342                                                      
REMARK 465     TRP E   403                                                      
REMARK 465     SER E   404                                                      
REMARK 465     ARG E   405                                                      
REMARK 465     ASN E   406                                                      
REMARK 465     SER E   407                                                      
REMARK 465     LYS E   408                                                      
REMARK 465     SER E   474                                                      
REMARK 465     VAL E   475                                                      
REMARK 465     GLY F   323                                                      
REMARK 465     SER F   324                                                      
REMARK 465     SER F   325                                                      
REMARK 465     HIS F   326                                                      
REMARK 465     HIS F   327                                                      
REMARK 465     HIS F   328                                                      
REMARK 465     HIS F   329                                                      
REMARK 465     HIS F   330                                                      
REMARK 465     HIS F   331                                                      
REMARK 465     SER F   332                                                      
REMARK 465     SER F   333                                                      
REMARK 465     GLY F   334                                                      
REMARK 465     LEU F   335                                                      
REMARK 465     GLU F   336                                                      
REMARK 465     VAL F   337                                                      
REMARK 465     LEU F   338                                                      
REMARK 465     PHE F   339                                                      
REMARK 465     GLN F   340                                                      
REMARK 465     GLY F   341                                                      
REMARK 465     PRO F   342                                                      
REMARK 465     HIS F   343                                                      
REMARK 465     LEU F   402                                                      
REMARK 465     TRP F   403                                                      
REMARK 465     SER F   404                                                      
REMARK 465     ARG F   405                                                      
REMARK 465     ASN F   406                                                      
REMARK 465     SER F   407                                                      
REMARK 465     PRO F   473                                                      
REMARK 465     SER F   474                                                      
REMARK 465     VAL F   475                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP C   374     NH1  ARG C   458              1.90            
REMARK 500   OD1  ASP B   374     NH1  ARG B   458              1.93            
REMARK 500   OD2  ASP E   365     OG   SER E   368              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A 343       73.18   -107.25                                   
REMARK 500    ASP A 439     -160.06    -77.18                                   
REMARK 500    ASN C 401      -73.80    -83.73                                   
REMARK 500    ALA C 440     -107.30     51.55                                   
REMARK 500    ILE C 443       77.43     57.08                                   
REMARK 500    GLU D 425       13.97   -143.68                                   
REMARK 500    ASN E 401       13.96   -142.10                                   
REMARK 500    MET E 422       66.60   -119.88                                   
REMARK 500    GLU E 425       11.29   -151.93                                   
REMARK 500    ALA F 440      -62.31     18.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5IG0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IG1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IG4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5IG5   RELATED DB: PDB                                   
DBREF  5IG3 A  345   475  UNP    Q9UQM7   KCC2A_HUMAN    345    475             
DBREF  5IG3 B  345   475  UNP    Q9UQM7   KCC2A_HUMAN    345    475             
DBREF  5IG3 C  345   475  UNP    Q9UQM7   KCC2A_HUMAN    345    475             
DBREF  5IG3 D  345   475  UNP    Q9UQM7   KCC2A_HUMAN    345    475             
DBREF  5IG3 E  345   475  UNP    Q9UQM7   KCC2A_HUMAN    345    475             
DBREF  5IG3 F  345   475  UNP    Q9UQM7   KCC2A_HUMAN    345    475             
SEQADV 5IG3 GLY A  323  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER A  324  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER A  325  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS A  326  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS A  327  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS A  328  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS A  329  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS A  330  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS A  331  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER A  332  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER A  333  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY A  334  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 LEU A  335  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLU A  336  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 VAL A  337  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 LEU A  338  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 PHE A  339  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLN A  340  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY A  341  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 PRO A  342  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS A  343  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 MET A  344  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY B  323  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER B  324  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER B  325  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS B  326  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS B  327  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS B  328  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS B  329  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS B  330  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS B  331  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER B  332  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER B  333  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY B  334  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 LEU B  335  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLU B  336  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 VAL B  337  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 LEU B  338  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 PHE B  339  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLN B  340  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY B  341  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 PRO B  342  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS B  343  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 MET B  344  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY C  323  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER C  324  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER C  325  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS C  326  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS C  327  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS C  328  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS C  329  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS C  330  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS C  331  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER C  332  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER C  333  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY C  334  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 LEU C  335  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLU C  336  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 VAL C  337  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 LEU C  338  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 PHE C  339  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLN C  340  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY C  341  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 PRO C  342  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS C  343  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 MET C  344  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY D  323  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER D  324  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER D  325  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS D  326  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS D  327  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS D  328  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS D  329  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS D  330  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS D  331  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER D  332  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER D  333  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY D  334  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 LEU D  335  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLU D  336  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 VAL D  337  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 LEU D  338  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 PHE D  339  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLN D  340  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY D  341  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 PRO D  342  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS D  343  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 MET D  344  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY E  323  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER E  324  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER E  325  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS E  326  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS E  327  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS E  328  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS E  329  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS E  330  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS E  331  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER E  332  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER E  333  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY E  334  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 LEU E  335  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLU E  336  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 VAL E  337  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 LEU E  338  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 PHE E  339  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLN E  340  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY E  341  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 PRO E  342  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS E  343  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 MET E  344  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY F  323  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER F  324  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER F  325  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS F  326  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS F  327  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS F  328  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS F  329  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS F  330  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS F  331  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER F  332  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 SER F  333  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY F  334  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 LEU F  335  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLU F  336  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 VAL F  337  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 LEU F  338  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 PHE F  339  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLN F  340  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 GLY F  341  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 PRO F  342  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 HIS F  343  UNP  Q9UQM7              EXPRESSION TAG                 
SEQADV 5IG3 MET F  344  UNP  Q9UQM7              EXPRESSION TAG                 
SEQRES   1 A  153  GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 A  153  GLU VAL LEU PHE GLN GLY PRO HIS MET VAL ARG LYS GLN          
SEQRES   3 A  153  GLU ILE ILE LYS VAL THR GLU GLN LEU ILE GLU ALA ILE          
SEQRES   4 A  153  SER ASN GLY ASP PHE GLU SER TYR THR LYS MET CYS ASP          
SEQRES   5 A  153  PRO GLY MET THR ALA PHE GLU PRO GLU ALA LEU GLY ASN          
SEQRES   6 A  153  LEU VAL GLU GLY LEU ASP PHE HIS ARG PHE TYR PHE GLU          
SEQRES   7 A  153  ASN LEU TRP SER ARG ASN SER LYS PRO VAL HIS THR THR          
SEQRES   8 A  153  ILE LEU ASN PRO HIS ILE HIS LEU MET GLY ASP GLU SER          
SEQRES   9 A  153  ALA CYS ILE ALA TYR ILE ARG ILE THR GLN TYR LEU ASP          
SEQRES  10 A  153  ALA GLY GLY ILE PRO ARG THR ALA GLN SER GLU GLU THR          
SEQRES  11 A  153  ARG VAL TRP HIS ARG ARG ASP GLY LYS TRP GLN ILE VAL          
SEQRES  12 A  153  HIS PHE HIS ARG SER GLY ALA PRO SER VAL                      
SEQRES   1 B  153  GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 B  153  GLU VAL LEU PHE GLN GLY PRO HIS MET VAL ARG LYS GLN          
SEQRES   3 B  153  GLU ILE ILE LYS VAL THR GLU GLN LEU ILE GLU ALA ILE          
SEQRES   4 B  153  SER ASN GLY ASP PHE GLU SER TYR THR LYS MET CYS ASP          
SEQRES   5 B  153  PRO GLY MET THR ALA PHE GLU PRO GLU ALA LEU GLY ASN          
SEQRES   6 B  153  LEU VAL GLU GLY LEU ASP PHE HIS ARG PHE TYR PHE GLU          
SEQRES   7 B  153  ASN LEU TRP SER ARG ASN SER LYS PRO VAL HIS THR THR          
SEQRES   8 B  153  ILE LEU ASN PRO HIS ILE HIS LEU MET GLY ASP GLU SER          
SEQRES   9 B  153  ALA CYS ILE ALA TYR ILE ARG ILE THR GLN TYR LEU ASP          
SEQRES  10 B  153  ALA GLY GLY ILE PRO ARG THR ALA GLN SER GLU GLU THR          
SEQRES  11 B  153  ARG VAL TRP HIS ARG ARG ASP GLY LYS TRP GLN ILE VAL          
SEQRES  12 B  153  HIS PHE HIS ARG SER GLY ALA PRO SER VAL                      
SEQRES   1 C  153  GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 C  153  GLU VAL LEU PHE GLN GLY PRO HIS MET VAL ARG LYS GLN          
SEQRES   3 C  153  GLU ILE ILE LYS VAL THR GLU GLN LEU ILE GLU ALA ILE          
SEQRES   4 C  153  SER ASN GLY ASP PHE GLU SER TYR THR LYS MET CYS ASP          
SEQRES   5 C  153  PRO GLY MET THR ALA PHE GLU PRO GLU ALA LEU GLY ASN          
SEQRES   6 C  153  LEU VAL GLU GLY LEU ASP PHE HIS ARG PHE TYR PHE GLU          
SEQRES   7 C  153  ASN LEU TRP SER ARG ASN SER LYS PRO VAL HIS THR THR          
SEQRES   8 C  153  ILE LEU ASN PRO HIS ILE HIS LEU MET GLY ASP GLU SER          
SEQRES   9 C  153  ALA CYS ILE ALA TYR ILE ARG ILE THR GLN TYR LEU ASP          
SEQRES  10 C  153  ALA GLY GLY ILE PRO ARG THR ALA GLN SER GLU GLU THR          
SEQRES  11 C  153  ARG VAL TRP HIS ARG ARG ASP GLY LYS TRP GLN ILE VAL          
SEQRES  12 C  153  HIS PHE HIS ARG SER GLY ALA PRO SER VAL                      
SEQRES   1 D  153  GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 D  153  GLU VAL LEU PHE GLN GLY PRO HIS MET VAL ARG LYS GLN          
SEQRES   3 D  153  GLU ILE ILE LYS VAL THR GLU GLN LEU ILE GLU ALA ILE          
SEQRES   4 D  153  SER ASN GLY ASP PHE GLU SER TYR THR LYS MET CYS ASP          
SEQRES   5 D  153  PRO GLY MET THR ALA PHE GLU PRO GLU ALA LEU GLY ASN          
SEQRES   6 D  153  LEU VAL GLU GLY LEU ASP PHE HIS ARG PHE TYR PHE GLU          
SEQRES   7 D  153  ASN LEU TRP SER ARG ASN SER LYS PRO VAL HIS THR THR          
SEQRES   8 D  153  ILE LEU ASN PRO HIS ILE HIS LEU MET GLY ASP GLU SER          
SEQRES   9 D  153  ALA CYS ILE ALA TYR ILE ARG ILE THR GLN TYR LEU ASP          
SEQRES  10 D  153  ALA GLY GLY ILE PRO ARG THR ALA GLN SER GLU GLU THR          
SEQRES  11 D  153  ARG VAL TRP HIS ARG ARG ASP GLY LYS TRP GLN ILE VAL          
SEQRES  12 D  153  HIS PHE HIS ARG SER GLY ALA PRO SER VAL                      
SEQRES   1 E  153  GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 E  153  GLU VAL LEU PHE GLN GLY PRO HIS MET VAL ARG LYS GLN          
SEQRES   3 E  153  GLU ILE ILE LYS VAL THR GLU GLN LEU ILE GLU ALA ILE          
SEQRES   4 E  153  SER ASN GLY ASP PHE GLU SER TYR THR LYS MET CYS ASP          
SEQRES   5 E  153  PRO GLY MET THR ALA PHE GLU PRO GLU ALA LEU GLY ASN          
SEQRES   6 E  153  LEU VAL GLU GLY LEU ASP PHE HIS ARG PHE TYR PHE GLU          
SEQRES   7 E  153  ASN LEU TRP SER ARG ASN SER LYS PRO VAL HIS THR THR          
SEQRES   8 E  153  ILE LEU ASN PRO HIS ILE HIS LEU MET GLY ASP GLU SER          
SEQRES   9 E  153  ALA CYS ILE ALA TYR ILE ARG ILE THR GLN TYR LEU ASP          
SEQRES  10 E  153  ALA GLY GLY ILE PRO ARG THR ALA GLN SER GLU GLU THR          
SEQRES  11 E  153  ARG VAL TRP HIS ARG ARG ASP GLY LYS TRP GLN ILE VAL          
SEQRES  12 E  153  HIS PHE HIS ARG SER GLY ALA PRO SER VAL                      
SEQRES   1 F  153  GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 F  153  GLU VAL LEU PHE GLN GLY PRO HIS MET VAL ARG LYS GLN          
SEQRES   3 F  153  GLU ILE ILE LYS VAL THR GLU GLN LEU ILE GLU ALA ILE          
SEQRES   4 F  153  SER ASN GLY ASP PHE GLU SER TYR THR LYS MET CYS ASP          
SEQRES   5 F  153  PRO GLY MET THR ALA PHE GLU PRO GLU ALA LEU GLY ASN          
SEQRES   6 F  153  LEU VAL GLU GLY LEU ASP PHE HIS ARG PHE TYR PHE GLU          
SEQRES   7 F  153  ASN LEU TRP SER ARG ASN SER LYS PRO VAL HIS THR THR          
SEQRES   8 F  153  ILE LEU ASN PRO HIS ILE HIS LEU MET GLY ASP GLU SER          
SEQRES   9 F  153  ALA CYS ILE ALA TYR ILE ARG ILE THR GLN TYR LEU ASP          
SEQRES  10 F  153  ALA GLY GLY ILE PRO ARG THR ALA GLN SER GLU GLU THR          
SEQRES  11 F  153  ARG VAL TRP HIS ARG ARG ASP GLY LYS TRP GLN ILE VAL          
SEQRES  12 F  153  HIS PHE HIS ARG SER GLY ALA PRO SER VAL                      
FORMUL   7  HOH   *15(H2 O)                                                     
HELIX    1 AA1 LEU A  335  GLN A  340  1                                   6    
HELIX    2 AA2 HIS A  343  ASN A  363  1                                  21    
HELIX    3 AA3 ASP A  365  MET A  372  1                                   8    
HELIX    4 AA4 GLU A  381  LEU A  385  5                                   5    
HELIX    5 AA5 LEU A  392  ASN A  401  1                                  10    
HELIX    6 AA6 ASN A  401  ASN A  406  1                                   6    
HELIX    7 AA7 VAL B  345  GLY B  364  1                                  20    
HELIX    8 AA8 ASP B  365  MET B  372  1                                   8    
HELIX    9 AA9 GLU B  381  LEU B  385  5                                   5    
HELIX   10 AB1 LEU B  392  ASN B  401  1                                  10    
HELIX   11 AB2 MET C  344  ASN C  363  1                                  20    
HELIX   12 AB3 ASP C  365  MET C  372  1                                   8    
HELIX   13 AB4 PRO C  382  LEU C  385  5                                   4    
HELIX   14 AB5 LEU C  392  ASN C  401  1                                  10    
HELIX   15 AB6 ARG D  346  ASN D  363  1                                  18    
HELIX   16 AB7 ASP D  365  MET D  372  1                                   8    
HELIX   17 AB8 GLU D  381  LEU D  385  5                                   5    
HELIX   18 AB9 LEU D  392  LEU D  402  1                                  11    
HELIX   19 AC1 ARG E  346  ASN E  363  1                                  18    
HELIX   20 AC2 ASP E  365  MET E  372  1                                   8    
HELIX   21 AC3 GLU E  381  LEU E  385  5                                   5    
HELIX   22 AC4 LEU E  392  GLU E  400  1                                   9    
HELIX   23 AC5 ARG F  346  ASN F  363  1                                  18    
HELIX   24 AC6 ASP F  365  MET F  372  1                                   8    
HELIX   25 AC7 GLU F  381  LEU F  385  5                                   5    
HELIX   26 AC8 LEU F  392  PHE F  397  1                                   6    
SHEET    1 AA1 7 HIS A 330  SER A 332  0                                        
SHEET    2 AA1 7 HIS A 411  LEU A 421  1  O  THR A 412   N  HIS A 330           
SHEET    3 AA1 7 SER A 426  LEU A 438 -1  O  ILE A 432   N  LEU A 415           
SHEET    4 AA1 7 PRO A 444  ARG A 458 -1  O  ARG A 453   N  ILE A 429           
SHEET    5 AA1 7 LYS A 461  SER A 470 -1  O  GLN A 463   N  HIS A 456           
SHEET    6 AA1 7 CYS A 373  PHE A 380  1  N  ASP A 374   O  ILE A 464           
SHEET    7 AA1 7 VAL A 389  GLU A 390 -1  O  VAL A 389   N  ALA A 379           
SHEET    1 AA2 6 VAL B 389  GLU B 390  0                                        
SHEET    2 AA2 6 CYS B 373  PHE B 380 -1  N  ALA B 379   O  VAL B 389           
SHEET    3 AA2 6 LYS B 461  GLY B 471  1  O  ILE B 464   N  ASP B 374           
SHEET    4 AA2 6 PRO B 444  ARG B 458 -1  N  ARG B 458   O  LYS B 461           
SHEET    5 AA2 6 SER B 426  LEU B 438 -1  N  ILE B 429   O  ARG B 453           
SHEET    6 AA2 6 HIS B 411  LEU B 421 -1  N  LEU B 415   O  ILE B 432           
SHEET    1 AA3 7 SER C 332  GLY C 334  0                                        
SHEET    2 AA3 7 HIS C 411  LEU C 421  1  O  ILE C 414   N  SER C 332           
SHEET    3 AA3 7 SER C 426  LEU C 438 -1  O  CYS C 428   N  HIS C 420           
SHEET    4 AA3 7 PRO C 444  ARG C 457 -1  O  ARG C 453   N  ILE C 429           
SHEET    5 AA3 7 TRP C 462  SER C 470 -1  O  HIS C 468   N  THR C 452           
SHEET    6 AA3 7 CYS C 373  PHE C 380  1  N  ASP C 374   O  ILE C 464           
SHEET    7 AA3 7 LEU C 388  GLU C 390 -1  O  VAL C 389   N  ALA C 379           
SHEET    1 AA4 6 VAL D 389  GLU D 390  0                                        
SHEET    2 AA4 6 CYS D 373  PHE D 380 -1  N  ALA D 379   O  VAL D 389           
SHEET    3 AA4 6 TRP D 462  GLY D 471  1  O  ILE D 464   N  ASP D 374           
SHEET    4 AA4 6 PRO D 444  ARG D 457 -1  N  VAL D 454   O  VAL D 465           
SHEET    5 AA4 6 SER D 426  LEU D 438 -1  N  ILE D 429   O  ARG D 453           
SHEET    6 AA4 6 HIS D 411  LEU D 421 -1  N  HIS D 411   O  GLN D 436           
SHEET    1 AA5 6 VAL E 389  GLU E 390  0                                        
SHEET    2 AA5 6 CYS E 373  PHE E 380 -1  N  ALA E 379   O  VAL E 389           
SHEET    3 AA5 6 TRP E 462  SER E 470  1  O  PHE E 467   N  PHE E 380           
SHEET    4 AA5 6 PRO E 444  ARG E 457 -1  N  GLU E 450   O  SER E 470           
SHEET    5 AA5 6 SER E 426  LEU E 438 -1  N  ILE E 429   O  ARG E 453           
SHEET    6 AA5 6 HIS E 411  LEU E 421 -1  N  LEU E 415   O  ILE E 432           
SHEET    1 AA6 6 VAL F 389  GLU F 390  0                                        
SHEET    2 AA6 6 CYS F 373  PHE F 380 -1  N  ALA F 379   O  VAL F 389           
SHEET    3 AA6 6 TRP F 462  GLY F 471  1  O  PHE F 467   N  PHE F 380           
SHEET    4 AA6 6 ILE F 443  ARG F 457 -1  N  VAL F 454   O  VAL F 465           
SHEET    5 AA6 6 SER F 426  ASP F 439 -1  N  ILE F 429   O  ARG F 453           
SHEET    6 AA6 6 HIS F 411  LEU F 421 -1  N  LEU F 415   O  ILE F 432           
CISPEP   1 GLY C  442    ILE C  443          0         0.64                     
CISPEP   2 SER E  470    GLY E  471          0        -2.54                     
CRYST1   89.888   89.888  226.577  90.00  90.00  90.00 P 43 21 2    48          
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      0.011125  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011125  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004414        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system