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Database: PDB
Entry: 4FG8
LinkDB: 4FG8
Original site: 4FG8 
HEADER    TRANSFERASE                             04-JUN-12   4FG8              
TITLE     CRYSTAL STRUCTURE OF HUMAN CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE
TITLE    2 I 1-315 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 SYNONYM: CAM KINASE I, CAM-KI, CAM KINASE I ALPHA, CAMKI-ALPHA;      
COMPND   5 EC: 2.7.11.17;                                                       
COMPND   6 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 4FG8    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.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 76.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 30343                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1557                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2107                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.01                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 114                          
REMARK   3   BIN FREE R VALUE                    : 0.3030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4183                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 135                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.51                          
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): 0.046         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150         
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      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4341 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5898 ; 1.588 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   525 ; 5.670 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   198 ;39.091 ;24.596       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   717 ;17.019 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;19.705 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3257 ; 0.007 ; 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 : 0.805                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : H+K, -K, -L                                     
REMARK   3      TWIN FRACTION : 0.195                                           
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 4FG8 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 RCSB072862.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX315HE                    
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) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 76.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
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   (%): 42.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3% DIOXANE, 100MM MES, 1.5M (NH4)2SO4,   
REMARK 280  PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K             
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       76.68600            
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       76.68600            
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       76.68600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     GLU A    64                                                      
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     LYS A   300                                                      
REMARK 465     SER A   301                                                      
REMARK 465     LYS A   302                                                      
REMARK 465     TRP A   303                                                      
REMARK 465     LYS A   304                                                      
REMARK 465     GLN A   305                                                      
REMARK 465     ALA A   306                                                      
REMARK 465     PHE A   307                                                      
REMARK 465     ASN A   308                                                      
REMARK 465     ALA A   309                                                      
REMARK 465     THR A   310                                                      
REMARK 465     ALA A   311                                                      
REMARK 465     VAL A   312                                                      
REMARK 465     VAL A   313                                                      
REMARK 465     ARG A   314                                                      
REMARK 465     HIS A   315                                                      
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     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     LYS B   300                                                      
REMARK 465     SER B   301                                                      
REMARK 465     LYS B   302                                                      
REMARK 465     TRP B   303                                                      
REMARK 465     LYS B   304                                                      
REMARK 465     GLN B   305                                                      
REMARK 465     ALA B   306                                                      
REMARK 465     PHE B   307                                                      
REMARK 465     ASN B   308                                                      
REMARK 465     ALA B   309                                                      
REMARK 465     THR B   310                                                      
REMARK 465     ALA B   311                                                      
REMARK 465     VAL B   312                                                      
REMARK 465     VAL B   313                                                      
REMARK 465     ARG B   314                                                      
REMARK 465     HIS B   315                                                      
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  54    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  65    CG   OD1  ND2                                       
REMARK 470     GLU A  66    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  67    CG1  CG2  CD1                                       
REMARK 470     LYS A  72    CG   CD   CE   NZ                                   
REMARK 470     LYS A  74    CG   CD   CE   NZ                                   
REMARK 470     ASP A 162    CG   OD1  OD2                                       
REMARK 470     PHE A 163    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR A 181    OG1  CG2                                            
REMARK 470     LYS A 193    CG   CD   CE   NZ                                   
REMARK 470     GLU A 221    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 223    CG   OD1  OD2                                       
REMARK 470     LYS A 232    CG   CD   CE   NZ                                   
REMARK 470     GLU A 262    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  14    CG   CD   OE1  OE2                                  
REMARK 470     PHE B  31    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN B  65    CG   OD1  ND2                                       
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     ASP B 162    CG   OD1  OD2                                       
REMARK 470     PHE B 163    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR B 181    OG1  CG2                                            
REMARK 470     TYR B 219    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 221    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 232    CG   CD   CE   NZ                                   
REMARK 470     GLU B 262    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  14      -72.42    -69.79                                   
REMARK 500    ARG A  23     -117.00   -110.72                                   
REMARK 500    PHE A  31       50.80   -141.07                                   
REMARK 500    LYS A  53       37.46    -81.85                                   
REMARK 500    ARG A 140      -12.61     73.69                                   
REMARK 500    PRO A 182      130.31    -37.24                                   
REMARK 500    SER A 196     -161.98   -117.86                                   
REMARK 500    ARG B  23     -137.94   -108.68                                   
REMARK 500    ARG B 140      -21.60     82.66                                   
REMARK 500    PHE B 163      -74.73   -127.71                                   
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: 4FG9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FGB   RELATED DB: PDB                                   
DBREF  4FG8 A    1   315  UNP    Q14012   KCC1A_HUMAN      1    315             
DBREF  4FG8 B    1   315  UNP    Q14012   KCC1A_HUMAN      1    315             
SEQRES   1 A  315  MET LEU GLY ALA VAL GLU GLY PRO ARG TRP LYS GLN ALA          
SEQRES   2 A  315  GLU ASP ILE ARG ASP ILE TYR ASP PHE ARG ASP VAL LEU          
SEQRES   3 A  315  GLY THR GLY ALA PHE SER GLU VAL ILE LEU ALA GLU ASP          
SEQRES   4 A  315  LYS ARG THR GLN LYS LEU VAL ALA ILE LYS CYS ILE ALA          
SEQRES   5 A  315  LYS GLU ALA LEU GLU GLY LYS GLU GLY SER MET GLU ASN          
SEQRES   6 A  315  GLU ILE ALA VAL LEU HIS LYS ILE LYS HIS PRO ASN ILE          
SEQRES   7 A  315  VAL ALA LEU ASP ASP ILE TYR GLU SER GLY GLY HIS LEU          
SEQRES   8 A  315  TYR LEU ILE MET GLN LEU VAL SER GLY GLY GLU LEU PHE          
SEQRES   9 A  315  ASP ARG ILE VAL GLU LYS GLY PHE TYR THR GLU ARG ASP          
SEQRES  10 A  315  ALA SER ARG LEU ILE PHE GLN VAL LEU ASP ALA VAL LYS          
SEQRES  11 A  315  TYR LEU HIS ASP LEU GLY ILE VAL HIS ARG ASP LEU LYS          
SEQRES  12 A  315  PRO GLU ASN LEU LEU TYR TYR SER LEU ASP GLU ASP SER          
SEQRES  13 A  315  LYS ILE MET ILE SER ASP PHE GLY LEU SER LYS MET GLU          
SEQRES  14 A  315  ASP PRO GLY SER VAL LEU SER THR ALA CYS GLY THR PRO          
SEQRES  15 A  315  GLY TYR VAL ALA PRO GLU VAL LEU ALA GLN LYS PRO TYR          
SEQRES  16 A  315  SER LYS ALA VAL ASP CYS TRP SER ILE GLY VAL ILE ALA          
SEQRES  17 A  315  TYR ILE LEU LEU CYS GLY TYR PRO PRO PHE TYR ASP GLU          
SEQRES  18 A  315  ASN ASP ALA LYS LEU PHE GLU GLN ILE LEU LYS ALA GLU          
SEQRES  19 A  315  TYR GLU PHE ASP SER PRO TYR TRP ASP ASP ILE SER ASP          
SEQRES  20 A  315  SER ALA LYS ASP PHE ILE ARG HIS LEU MET GLU LYS ASP          
SEQRES  21 A  315  PRO GLU LYS ARG PHE THR CYS GLU GLN ALA LEU GLN HIS          
SEQRES  22 A  315  PRO TRP ILE ALA GLY ASP THR ALA LEU ASP LYS ASN ILE          
SEQRES  23 A  315  HIS GLN SER VAL SER GLU GLN ILE LYS LYS ASN PHE ALA          
SEQRES  24 A  315  LYS SER LYS TRP LYS GLN ALA PHE ASN ALA THR ALA VAL          
SEQRES  25 A  315  VAL ARG HIS                                                  
SEQRES   1 B  315  MET LEU GLY ALA VAL GLU GLY PRO ARG TRP LYS GLN ALA          
SEQRES   2 B  315  GLU ASP ILE ARG ASP ILE TYR ASP PHE ARG ASP VAL LEU          
SEQRES   3 B  315  GLY THR GLY ALA PHE SER GLU VAL ILE LEU ALA GLU ASP          
SEQRES   4 B  315  LYS ARG THR GLN LYS LEU VAL ALA ILE LYS CYS ILE ALA          
SEQRES   5 B  315  LYS GLU ALA LEU GLU GLY LYS GLU GLY SER MET GLU ASN          
SEQRES   6 B  315  GLU ILE ALA VAL LEU HIS LYS ILE LYS HIS PRO ASN ILE          
SEQRES   7 B  315  VAL ALA LEU ASP ASP ILE TYR GLU SER GLY GLY HIS LEU          
SEQRES   8 B  315  TYR LEU ILE MET GLN LEU VAL SER GLY GLY GLU LEU PHE          
SEQRES   9 B  315  ASP ARG ILE VAL GLU LYS GLY PHE TYR THR GLU ARG ASP          
SEQRES  10 B  315  ALA SER ARG LEU ILE PHE GLN VAL LEU ASP ALA VAL LYS          
SEQRES  11 B  315  TYR LEU HIS ASP LEU GLY ILE VAL HIS ARG ASP LEU LYS          
SEQRES  12 B  315  PRO GLU ASN LEU LEU TYR TYR SER LEU ASP GLU ASP SER          
SEQRES  13 B  315  LYS ILE MET ILE SER ASP PHE GLY LEU SER LYS MET GLU          
SEQRES  14 B  315  ASP PRO GLY SER VAL LEU SER THR ALA CYS GLY THR PRO          
SEQRES  15 B  315  GLY TYR VAL ALA PRO GLU VAL LEU ALA GLN LYS PRO TYR          
SEQRES  16 B  315  SER LYS ALA VAL ASP CYS TRP SER ILE GLY VAL ILE ALA          
SEQRES  17 B  315  TYR ILE LEU LEU CYS GLY TYR PRO PRO PHE TYR ASP GLU          
SEQRES  18 B  315  ASN ASP ALA LYS LEU PHE GLU GLN ILE LEU LYS ALA GLU          
SEQRES  19 B  315  TYR GLU PHE ASP SER PRO TYR TRP ASP ASP ILE SER ASP          
SEQRES  20 B  315  SER ALA LYS ASP PHE ILE ARG HIS LEU MET GLU LYS ASP          
SEQRES  21 B  315  PRO GLU LYS ARG PHE THR CYS GLU GLN ALA LEU GLN HIS          
SEQRES  22 B  315  PRO TRP ILE ALA GLY ASP THR ALA LEU ASP LYS ASN ILE          
SEQRES  23 B  315  HIS GLN SER VAL SER GLU GLN ILE LYS LYS ASN PHE ALA          
SEQRES  24 B  315  LYS SER LYS TRP LYS GLN ALA PHE ASN ALA THR ALA VAL          
SEQRES  25 B  315  VAL ARG HIS                                                  
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   *135(H2 O)                                                    
HELIX    1   1 ASP A   15  ASP A   18  5                                   4    
HELIX    2   2 GLU A   66  HIS A   71  1                                   6    
HELIX    3   3 GLU A  102  LYS A  110  1                                   9    
HELIX    4   4 THR A  114  LEU A  135  1                                  22    
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  ALA A  233  1                                  12    
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 ASP B   15  ASP B   18  5                                   4    
HELIX   14  14 GLU B   66  HIS B   71  1                                   6    
HELIX   15  15 LEU B  103  LYS B  110  1                                   8    
HELIX   16  16 THR B  114  LEU B  135  1                                  22    
HELIX   17  17 LYS B  143  GLU B  145  5                                   3    
HELIX   18  18 SER B  173  CYS B  179  1                                   7    
HELIX   19  19 ALA B  186  ALA B  191  1                                   6    
HELIX   20  20 LYS B  197  GLY B  214  1                                  18    
HELIX   21  21 ASN B  222  LYS B  232  1                                  11    
HELIX   22  22 SER B  246  MET B  257  1                                  12    
HELIX   23  23 THR B  266  HIS B  273  1                                   8    
HELIX   24  24 HIS B  273  GLY B  278  1                                   6    
HELIX   25  25 ILE B  286  PHE B  298  1                                  13    
SHEET    1   A 6 LYS A  11  GLN A  12  0                                        
SHEET    2   A 6 LEU A  81  GLU A  86  1  O  ILE A  84   N  LYS A  11           
SHEET    3   A 6 HIS A  90  MET A  95 -1  O  TYR A  92   N  TYR A  85           
SHEET    4   A 6 LEU A  45  ALA A  52 -1  N  ALA A  47   O  MET A  95           
SHEET    5   A 6 SER A  32  ASP A  39 -1  N  ILE A  35   O  ILE A  48           
SHEET    6   A 6 TYR A  20  GLY A  29 -1  N  GLY A  29   O  SER A  32           
SHEET    1   B 2 LEU A 147  TYR A 149  0                                        
SHEET    2   B 2 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  ARG B  23           
SHEET    3   C 5 LEU B  45  ALA B  52 -1  O  ILE B  48   N  ILE B  35           
SHEET    4   C 5 HIS B  90  GLN B  96 -1  O  LEU B  91   N  ILE B  51           
SHEET    5   C 5 LEU B  81  SER B  87 -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         0.88                     
CISPEP   2 SER B  239    PRO B  240          0        -3.57                     
SITE     1 AC1 18 LEU A  26  GLY A  29  ALA A  30  SER A  32                    
SITE     2 AC1 18 VAL A  34  ALA A  47  LYS A  49  VAL A  79                    
SITE     3 AC1 18 GLN A  96  VAL A  98  GLU A 102  GLU A 145                    
SITE     4 AC1 18 ASN A 146  LEU A 148  SER A 161  HOH A 503                    
SITE     5 AC1 18 HOH A 514  HOH A 546                                          
SITE     1 AC2 12 GLY B  27  THR B  28  GLY B  29  SER B  32                    
SITE     2 AC2 12 VAL B  34  ALA B  47  LYS B  49  VAL B  79                    
SITE     3 AC2 12 GLN B  96  VAL B  98  ASN B 146  HOH B 536                    
CRYST1   83.415   83.415  153.372  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      0.011988  0.006921  0.000000        0.00000                         
SCALE2      0.000000  0.013843  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006520        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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