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Database: PDB
Entry: 4FG9
LinkDB: 4FG9
Original site: 4FG9 
HEADER    TRANSFERASE                             04-JUN-12   4FG9              
TITLE     CRYSTAL STRUCTURE OF HUMAN CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE
TITLE    2 I 1-320 IN COMPLEX WITH ATP                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE 1;        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 1-320;                                            
COMPND   5 SYNONYM: CAM KINASE I, CAM-KI, CAM KINASE I ALPHA, CAMKI-ALPHA;      
COMPND   6 EC: 2.7.11.17;                                                       
COMPND   7 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: CAMK1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX4T-1                                  
KEYWDS    CAMK, CALMODULIN, AUTOINHIBITION, REGULATION MECHANISM, KINASE,       
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.ZHA,C.ZHONG,Y.OU,J.WANG,L.HAN,J.DING                                
REVDAT   1   23-JAN-13 4FG9    0                                                
JRNL        AUTH   M.ZHA,C.ZHONG,Y.OU,L.HAN,J.WANG,J.DING                       
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN CAMKIALPHA REVEAL INSIGHTS INTO  
JRNL        TITL 2 THE REGULATION MECHANISM OF CAMKI.                           
JRNL        REF    PLOS ONE                      V.   7 44828 2012              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   23028635                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0044828                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 76.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 23395                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1188                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1639                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.86                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 55                           
REMARK   3   BIN FREE R VALUE                    : 0.2110                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4420                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 136                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.82                          
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.059         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.188         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.910                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4586 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6228 ; 1.137 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   551 ; 4.364 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   211 ;38.163 ;24.645       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   765 ;16.343 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;12.968 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3433 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.579                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : H+K, -K, -L                                     
REMARK   3      TWIN FRACTION : 0.421                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES      : REFINED INDIVIDUALLY      
REMARK   4                                                                      
REMARK   4 4FG9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072863.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-MAR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BSRF                               
REMARK 200  BEAMLINE                       : 1W2B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 76.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 4FG7                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M (NH4)2SO4, 100MM TRI-SODIUM         
REMARK 280  CITRATE, 0.8M LI2SO4, PH 5.6, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       76.50200            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       76.50200            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       76.50200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: MONOMERIC                         
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 22040 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 66100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000       83.09700            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       41.54850            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       71.96411            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 548  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 567  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 561  LIES ON A SPECIAL POSITION.                          
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     MET A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     ALA A    55                                                      
REMARK 465     LEU A    56                                                      
REMARK 465     GLU A    57                                                      
REMARK 465     GLY A    58                                                      
REMARK 465     LYS A    59                                                      
REMARK 465     GLU A    60                                                      
REMARK 465     GLY A    61                                                      
REMARK 465     SER A    62                                                      
REMARK 465     MET A    63                                                      
REMARK 465     GLY A   164                                                      
REMARK 465     LEU A   165                                                      
REMARK 465     SER A   166                                                      
REMARK 465     LYS A   167                                                      
REMARK 465     MET A   168                                                      
REMARK 465     GLU A   169                                                      
REMARK 465     ASP A   170                                                      
REMARK 465     PRO A   171                                                      
REMARK 465     GLY A   172                                                      
REMARK 465     SER A   173                                                      
REMARK 465     VAL A   174                                                      
REMARK 465     LEU A   175                                                      
REMARK 465     SER A   176                                                      
REMARK 465     THR A   177                                                      
REMARK 465     ALA A   178                                                      
REMARK 465     CYS A   179                                                      
REMARK 465     GLY A   180                                                      
REMARK 465     THR A   181                                                      
REMARK 465     HIS A   315                                                      
REMARK 465     MET A   316                                                      
REMARK 465     ARG A   317                                                      
REMARK 465     LYS A   318                                                      
REMARK 465     LEU A   319                                                      
REMARK 465     GLN A   320                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     VAL B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     TRP B    10                                                      
REMARK 465     LYS B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     GLU B    54                                                      
REMARK 465     ALA B    55                                                      
REMARK 465     LEU B    56                                                      
REMARK 465     GLU B    57                                                      
REMARK 465     GLY B    58                                                      
REMARK 465     LYS B    59                                                      
REMARK 465     GLU B    60                                                      
REMARK 465     GLY B    61                                                      
REMARK 465     SER B    62                                                      
REMARK 465     MET B    63                                                      
REMARK 465     GLU B    64                                                      
REMARK 465     ASN B    65                                                      
REMARK 465     GLY B   164                                                      
REMARK 465     LEU B   165                                                      
REMARK 465     SER B   166                                                      
REMARK 465     LYS B   167                                                      
REMARK 465     MET B   168                                                      
REMARK 465     GLU B   169                                                      
REMARK 465     ASP B   170                                                      
REMARK 465     PRO B   171                                                      
REMARK 465     GLY B   172                                                      
REMARK 465     SER B   173                                                      
REMARK 465     HIS B   315                                                      
REMARK 465     MET B   316                                                      
REMARK 465     ARG B   317                                                      
REMARK 465     LYS B   318                                                      
REMARK 465     LEU B   319                                                      
REMARK 465     GLN B   320                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  14    CG   CD   OE1  OE2                                  
REMARK 470     PHE A  31    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  72    CG   CD   CE   NZ                                   
REMARK 470     LYS A  74    CG   CD   CE   NZ                                   
REMARK 470     GLU A  86    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 193    CG   CD   CE   NZ                                   
REMARK 470     TYR A 219    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 221    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 232    CG   CD   CE   NZ                                   
REMARK 470     GLU A 262    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 314    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  14    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  15    CG   OD1  OD2                                       
REMARK 470     GLU B  66    CG   CD   OE1  OE2                                  
REMARK 470     ILE B  67    CG1  CG2  CD1                                       
REMARK 470     LYS B  72    CG   CD   CE   NZ                                   
REMARK 470     LYS B  74    CG   CD   CE   NZ                                   
REMARK 470     THR B 181    OG1  CG2                                            
REMARK 470     GLU B 221    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 234    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 314    CG   CD   NE   CZ   NH1  NH2                        
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    ARG A  23     -120.30   -116.69                                   
REMARK 500    LYS A  53       93.42    -65.93                                   
REMARK 500    SER A  87     -166.80   -106.78                                   
REMARK 500    ARG A 140      -19.91     75.14                                   
REMARK 500    ASN A 285       95.79    -69.31                                   
REMARK 500    ARG B  23     -124.84   -116.86                                   
REMARK 500    ARG B 140      -17.09     67.77                                   
REMARK 500    SER B 196     -148.09   -143.42                                   
REMARK 500    CYS B 213      -24.09   -142.86                                   
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 ATP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FG7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FG8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FGB   RELATED DB: PDB                                   
DBREF  4FG9 A    1   320  UNP    Q14012   KCC1A_HUMAN      1    320             
DBREF  4FG9 B    1   320  UNP    Q14012   KCC1A_HUMAN      1    320             
SEQRES   1 A  320  MET LEU GLY ALA VAL GLU GLY PRO ARG TRP LYS GLN ALA          
SEQRES   2 A  320  GLU ASP ILE ARG ASP ILE TYR ASP PHE ARG ASP VAL LEU          
SEQRES   3 A  320  GLY THR GLY ALA PHE SER GLU VAL ILE LEU ALA GLU ASP          
SEQRES   4 A  320  LYS ARG THR GLN LYS LEU VAL ALA ILE LYS CYS ILE ALA          
SEQRES   5 A  320  LYS GLU ALA LEU GLU GLY LYS GLU GLY SER MET GLU ASN          
SEQRES   6 A  320  GLU ILE ALA VAL LEU HIS LYS ILE LYS HIS PRO ASN ILE          
SEQRES   7 A  320  VAL ALA LEU ASP ASP ILE TYR GLU SER GLY GLY HIS LEU          
SEQRES   8 A  320  TYR LEU ILE MET GLN LEU VAL SER GLY GLY GLU LEU PHE          
SEQRES   9 A  320  ASP ARG ILE VAL GLU LYS GLY PHE TYR THR GLU ARG ASP          
SEQRES  10 A  320  ALA SER ARG LEU ILE PHE GLN VAL LEU ASP ALA VAL LYS          
SEQRES  11 A  320  TYR LEU HIS ASP LEU GLY ILE VAL HIS ARG ASP LEU LYS          
SEQRES  12 A  320  PRO GLU ASN LEU LEU TYR TYR SER LEU ASP GLU ASP SER          
SEQRES  13 A  320  LYS ILE MET ILE SER ASP PHE GLY LEU SER LYS MET GLU          
SEQRES  14 A  320  ASP PRO GLY SER VAL LEU SER THR ALA CYS GLY THR PRO          
SEQRES  15 A  320  GLY TYR VAL ALA PRO GLU VAL LEU ALA GLN LYS PRO TYR          
SEQRES  16 A  320  SER LYS ALA VAL ASP CYS TRP SER ILE GLY VAL ILE ALA          
SEQRES  17 A  320  TYR ILE LEU LEU CYS GLY TYR PRO PRO PHE TYR ASP GLU          
SEQRES  18 A  320  ASN ASP ALA LYS LEU PHE GLU GLN ILE LEU LYS ALA GLU          
SEQRES  19 A  320  TYR GLU PHE ASP SER PRO TYR TRP ASP ASP ILE SER ASP          
SEQRES  20 A  320  SER ALA LYS ASP PHE ILE ARG HIS LEU MET GLU LYS ASP          
SEQRES  21 A  320  PRO GLU LYS ARG PHE THR CYS GLU GLN ALA LEU GLN HIS          
SEQRES  22 A  320  PRO TRP ILE ALA GLY ASP THR ALA LEU ASP LYS ASN ILE          
SEQRES  23 A  320  HIS GLN SER VAL SER GLU GLN ILE LYS LYS ASN PHE ALA          
SEQRES  24 A  320  LYS SER LYS TRP LYS GLN ALA PHE ASN ALA THR ALA VAL          
SEQRES  25 A  320  VAL ARG HIS MET ARG LYS LEU GLN                              
SEQRES   1 B  320  MET LEU GLY ALA VAL GLU GLY PRO ARG TRP LYS GLN ALA          
SEQRES   2 B  320  GLU ASP ILE ARG ASP ILE TYR ASP PHE ARG ASP VAL LEU          
SEQRES   3 B  320  GLY THR GLY ALA PHE SER GLU VAL ILE LEU ALA GLU ASP          
SEQRES   4 B  320  LYS ARG THR GLN LYS LEU VAL ALA ILE LYS CYS ILE ALA          
SEQRES   5 B  320  LYS GLU ALA LEU GLU GLY LYS GLU GLY SER MET GLU ASN          
SEQRES   6 B  320  GLU ILE ALA VAL LEU HIS LYS ILE LYS HIS PRO ASN ILE          
SEQRES   7 B  320  VAL ALA LEU ASP ASP ILE TYR GLU SER GLY GLY HIS LEU          
SEQRES   8 B  320  TYR LEU ILE MET GLN LEU VAL SER GLY GLY GLU LEU PHE          
SEQRES   9 B  320  ASP ARG ILE VAL GLU LYS GLY PHE TYR THR GLU ARG ASP          
SEQRES  10 B  320  ALA SER ARG LEU ILE PHE GLN VAL LEU ASP ALA VAL LYS          
SEQRES  11 B  320  TYR LEU HIS ASP LEU GLY ILE VAL HIS ARG ASP LEU LYS          
SEQRES  12 B  320  PRO GLU ASN LEU LEU TYR TYR SER LEU ASP GLU ASP SER          
SEQRES  13 B  320  LYS ILE MET ILE SER ASP PHE GLY LEU SER LYS MET GLU          
SEQRES  14 B  320  ASP PRO GLY SER VAL LEU SER THR ALA CYS GLY THR PRO          
SEQRES  15 B  320  GLY TYR VAL ALA PRO GLU VAL LEU ALA GLN LYS PRO TYR          
SEQRES  16 B  320  SER LYS ALA VAL ASP CYS TRP SER ILE GLY VAL ILE ALA          
SEQRES  17 B  320  TYR ILE LEU LEU CYS GLY TYR PRO PRO PHE TYR ASP GLU          
SEQRES  18 B  320  ASN ASP ALA LYS LEU PHE GLU GLN ILE LEU LYS ALA GLU          
SEQRES  19 B  320  TYR GLU PHE ASP SER PRO TYR TRP ASP ASP ILE SER ASP          
SEQRES  20 B  320  SER ALA LYS ASP PHE ILE ARG HIS LEU MET GLU LYS ASP          
SEQRES  21 B  320  PRO GLU LYS ARG PHE THR CYS GLU GLN ALA LEU GLN HIS          
SEQRES  22 B  320  PRO TRP ILE ALA GLY ASP THR ALA LEU ASP LYS ASN ILE          
SEQRES  23 B  320  HIS GLN SER VAL SER GLU GLN ILE LYS LYS ASN PHE ALA          
SEQRES  24 B  320  LYS SER LYS TRP LYS GLN ALA PHE ASN ALA THR ALA VAL          
SEQRES  25 B  320  VAL ARG HIS MET ARG LYS LEU GLN                              
HET    ATP  A 401      31                                                       
HET    ATP  B 401      31                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   3  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL   5  HOH   *136(H2 O)                                                    
HELIX    1   1 ASP A   15  ASP A   18  5                                   4    
HELIX    2   2 ASN A   65  LYS A   72  1                                   8    
HELIX    3   3 LEU A  103  LYS A  110  1                                   8    
HELIX    4   4 THR A  114  GLY A  136  1                                  23    
HELIX    5   5 LYS A  143  GLU A  145  5                                   3    
HELIX    6   6 ALA A  186  ALA A  191  1                                   6    
HELIX    7   7 LYS A  197  GLY A  214  1                                  18    
HELIX    8   8 ASN A  222  LYS A  232  1                                  11    
HELIX    9   9 SER A  246  MET A  257  1                                  12    
HELIX   10  10 THR A  266  HIS A  273  1                                   8    
HELIX   11  11 HIS A  273  GLY A  278  1                                   6    
HELIX   12  12 ILE A  286  PHE A  298  1                                  13    
HELIX   13  13 LYS A  300  VAL A  312  1                                  13    
HELIX   14  14 ASP B   15  ASP B   18  5                                   4    
HELIX   15  15 ILE B   67  HIS B   71  1                                   5    
HELIX   16  16 LEU B  103  LYS B  110  1                                   8    
HELIX   17  17 THR B  114  GLY B  136  1                                  23    
HELIX   18  18 LYS B  143  GLU B  145  5                                   3    
HELIX   19  19 LEU B  175  THR B  181  1                                   7    
HELIX   20  20 ALA B  186  ALA B  191  1                                   6    
HELIX   21  21 LYS B  197  GLY B  214  1                                  18    
HELIX   22  22 ASN B  222  LYS B  232  1                                  11    
HELIX   23  23 SER B  246  MET B  257  1                                  12    
HELIX   24  24 THR B  266  GLN B  272  1                                   7    
HELIX   25  25 HIS B  273  GLY B  278  1                                   6    
HELIX   26  26 ILE B  286  PHE B  298  1                                  13    
HELIX   27  27 ALA B  299  ARG B  314  1                                  16    
SHEET    1   A 5 TYR A  20  THR A  28  0                                        
SHEET    2   A 5 SER A  32  ASP A  39 -1  O  LEU A  36   N  ASP A  24           
SHEET    3   A 5 LEU A  45  ALA A  52 -1  O  VAL A  46   N  ALA A  37           
SHEET    4   A 5 HIS A  90  GLN A  96 -1  O  MET A  95   N  ALA A  47           
SHEET    5   A 5 LEU A  81  GLU A  86 -1  N  TYR A  85   O  TYR A  92           
SHEET    1   B 3 GLY A 101  GLU A 102  0                                        
SHEET    2   B 3 LEU A 147  TYR A 149 -1  O  TYR A 149   N  GLY A 101           
SHEET    3   B 3 ILE A 158  ILE A 160 -1  O  MET A 159   N  LEU A 148           
SHEET    1   C 5 TYR B  20  THR B  28  0                                        
SHEET    2   C 5 SER B  32  ASP B  39 -1  O  LEU B  36   N  ASP B  24           
SHEET    3   C 5 LEU B  45  ALA B  52 -1  O  VAL B  46   N  ALA B  37           
SHEET    4   C 5 HIS B  90  MET B  95 -1  O  LEU B  91   N  ILE B  51           
SHEET    5   C 5 LEU B  81  GLU B  86 -1  N  ASP B  83   O  ILE B  94           
SHEET    1   D 3 GLY B 101  GLU B 102  0                                        
SHEET    2   D 3 LEU B 147  TYR B 149 -1  O  TYR B 149   N  GLY B 101           
SHEET    3   D 3 ILE B 158  ILE B 160 -1  O  MET B 159   N  LEU B 148           
CISPEP   1 SER A  239    PRO A  240          0        -0.64                     
CISPEP   2 SER B  239    PRO B  240          0        -2.51                     
SITE     1 AC1 18 GLY A  27  THR A  28  GLY A  29  ALA A  30                    
SITE     2 AC1 18 SER A  32  VAL A  34  ALA A  47  LYS A  49                    
SITE     3 AC1 18 GLN A  96  VAL A  98  GLU A 102  ASP A 141                    
SITE     4 AC1 18 LYS A 143  GLU A 145  ASN A 146  LEU A 148                    
SITE     5 AC1 18 ASP A 162  HOH A 563                                          
SITE     1 AC2 21 LEU B  26  GLY B  27  GLY B  29  ALA B  30                    
SITE     2 AC2 21 SER B  32  VAL B  34  ALA B  47  LYS B  49                    
SITE     3 AC2 21 VAL B  79  GLN B  96  VAL B  98  GLU B 102                    
SITE     4 AC2 21 LYS B 143  ASN B 146  LEU B 148  ASP B 162                    
SITE     5 AC2 21 HOH B 550  HOH B 551  HOH B 559  HOH B 564                    
SITE     6 AC2 21 HOH B 565                                                     
CRYST1   83.097   83.097  153.004  90.00  90.00 120.00 P 63         12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012034  0.006948  0.000000        0.00000                         
SCALE2      0.000000  0.013896  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006536        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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