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Database: PDB
Entry: 4FG7
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Original site: 4FG7 
HEADER    TRANSFERASE                             04-JUN-12   4FG7              
TITLE     CRYSTAL STRUCTURE OF HUMAN CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE
TITLE    2 I 1-293 IN COMPLEX WITH ATP                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE 1;        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-293;                                            
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 4FG7    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.    2.70 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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 59.46                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 8918                           
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) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 461                             
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 609                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.70                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2410                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 27                           
REMARK   3   BIN FREE R VALUE                    : 0.4670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2008                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 79                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.02                          
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): 0.072         
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      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2087 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2832 ; 1.435 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   246 ; 5.119 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   100 ;38.569 ;24.900       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   354 ;15.950 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;18.640 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1570 ; 0.006 ; 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  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     9        A   277                          
REMARK   3    ORIGIN FOR THE GROUP (A): 129.3778 -22.3634  24.2949              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1232 T22:   0.1690                                     
REMARK   3      T33:   0.0438 T12:  -0.0037                                     
REMARK   3      T13:  -0.0124 T23:   0.0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0607 L22:   2.7372                                     
REMARK   3      L33:   0.3986 L12:  -0.8340                                     
REMARK   3      L13:  -0.2944 L23:  -0.2469                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0294 S12:   0.0580 S13:   0.1097                       
REMARK   3      S21:   0.1406 S22:  -0.0171 S23:  -0.0350                       
REMARK   3      S31:   0.0706 S32:   0.0583 S33:  -0.0122                       
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      : RESIDUAL ONLY             
REMARK   4                                                                      
REMARK   4 4FG7 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 RCSB072861.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAR-07                          
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               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
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          : ADSC QUANTUM 4                     
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) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.460                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 33.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.900                              
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 1A06                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM NH4AC, 100MM (CH3)2ASO2NA, 25%     
REMARK 280  PEG 8000, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.94450            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       32.84050            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       32.84050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.97225            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       32.84050            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       32.84050            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      104.91675            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       32.84050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       32.84050            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       34.97225            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       32.84050            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       32.84050            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      104.91675            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       69.94450            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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     LYS A    53                                                      
REMARK 465     GLU A    54                                                      
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     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     PRO A   194                                                      
REMARK 465     TYR A   195                                                      
REMARK 465     GLY A   278                                                      
REMARK 465     ASP A   279                                                      
REMARK 465     THR A   280                                                      
REMARK 465     ALA A   281                                                      
REMARK 465     LEU A   282                                                      
REMARK 465     ASP A   283                                                      
REMARK 465     LYS A   284                                                      
REMARK 465     ASN A   285                                                      
REMARK 465     ILE A   286                                                      
REMARK 465     HIS A   287                                                      
REMARK 465     GLN A   288                                                      
REMARK 465     SER A   289                                                      
REMARK 465     VAL A   290                                                      
REMARK 465     SER A   291                                                      
REMARK 465     GLU A   292                                                      
REMARK 465     GLN A   293                                                      
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     ARG A   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  17    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 167    CG   CD   CE   NZ                                   
REMARK 470     LYS A 193    CG   CD   CE   NZ                                   
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     -126.18   -116.63                                   
REMARK 500    ASP A  83     -175.99   -173.88                                   
REMARK 500    GLU A 109       24.24    -78.79                                   
REMARK 500    LYS A 110      -27.21   -153.08                                   
REMARK 500    ARG A 140       -3.11     76.61                                   
REMARK 500    ASP A 141       39.67   -145.87                                   
REMARK 500    ASP A 162       83.23     56.25                                   
REMARK 500    GLN A 192     -124.09   -141.02                                   
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 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FG8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FG9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FGB   RELATED DB: PDB                                   
DBREF  4FG7 A    1   293  UNP    Q14012   KCC1A_HUMAN      1    293             
SEQRES   1 A  293  MET LEU GLY ALA VAL GLU GLY PRO ARG TRP LYS GLN ALA          
SEQRES   2 A  293  GLU ASP ILE ARG ASP ILE TYR ASP PHE ARG ASP VAL LEU          
SEQRES   3 A  293  GLY THR GLY ALA PHE SER GLU VAL ILE LEU ALA GLU ASP          
SEQRES   4 A  293  LYS ARG THR GLN LYS LEU VAL ALA ILE LYS CYS ILE ALA          
SEQRES   5 A  293  LYS GLU ALA LEU GLU GLY LYS GLU GLY SER MET GLU ASN          
SEQRES   6 A  293  GLU ILE ALA VAL LEU HIS LYS ILE LYS HIS PRO ASN ILE          
SEQRES   7 A  293  VAL ALA LEU ASP ASP ILE TYR GLU SER GLY GLY HIS LEU          
SEQRES   8 A  293  TYR LEU ILE MET GLN LEU VAL SER GLY GLY GLU LEU PHE          
SEQRES   9 A  293  ASP ARG ILE VAL GLU LYS GLY PHE TYR THR GLU ARG ASP          
SEQRES  10 A  293  ALA SER ARG LEU ILE PHE GLN VAL LEU ASP ALA VAL LYS          
SEQRES  11 A  293  TYR LEU HIS ASP LEU GLY ILE VAL HIS ARG ASP LEU LYS          
SEQRES  12 A  293  PRO GLU ASN LEU LEU TYR TYR SER LEU ASP GLU ASP SER          
SEQRES  13 A  293  LYS ILE MET ILE SER ASP PHE GLY LEU SER LYS MET GLU          
SEQRES  14 A  293  ASP PRO GLY SER VAL LEU SER THR ALA CYS GLY THR PRO          
SEQRES  15 A  293  GLY TYR VAL ALA PRO GLU VAL LEU ALA GLN LYS PRO TYR          
SEQRES  16 A  293  SER LYS ALA VAL ASP CYS TRP SER ILE GLY VAL ILE ALA          
SEQRES  17 A  293  TYR ILE LEU LEU CYS GLY TYR PRO PRO PHE TYR ASP GLU          
SEQRES  18 A  293  ASN ASP ALA LYS LEU PHE GLU GLN ILE LEU LYS ALA GLU          
SEQRES  19 A  293  TYR GLU PHE ASP SER PRO TYR TRP ASP ASP ILE SER ASP          
SEQRES  20 A  293  SER ALA LYS ASP PHE ILE ARG HIS LEU MET GLU LYS ASP          
SEQRES  21 A  293  PRO GLU LYS ARG PHE THR CYS GLU GLN ALA LEU GLN HIS          
SEQRES  22 A  293  PRO TRP ILE ALA GLY ASP THR ALA LEU ASP LYS ASN ILE          
SEQRES  23 A  293  HIS GLN SER VAL SER GLU GLN                                  
HET    ATP  A 301      31                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   2  ATP    C10 H16 N5 O13 P3                                            
FORMUL   3  HOH   *79(H2 O)                                                     
HELIX    1   1 ASP A   15  ASP A   18  5                                   4    
HELIX    2   2 MET A   63  ILE A   73  1                                  11    
HELIX    3   3 GLU A  102  GLU A  109  1                                   8    
HELIX    4   4 THR A  114  ASP A  134  1                                  21    
HELIX    5   5 ALA A  186  GLN A  192  1                                   7    
HELIX    6   6 LYS A  197  GLY A  214  1                                  18    
HELIX    7   7 ASN A  222  ALA A  233  1                                  12    
HELIX    8   8 SER A  246  MET A  257  1                                  12    
HELIX    9   9 THR A  266  HIS A  273  1                                   8    
SHEET    1   A 6 LYS A  11  GLN A  12  0                                        
SHEET    2   A 6 LEU A  81  SER A  87  1  O  GLU A  86   N  LYS A  11           
SHEET    3   A 6 HIS A  90  MET A  95 -1  O  ILE A  94   N  ASP A  83           
SHEET    4   A 6 LEU A  45  ILE A  51 -1  N  ALA A  47   O  MET A  95           
SHEET    5   A 6 SER A  32  ASP A  39 -1  N  GLU A  33   O  CYS A  50           
SHEET    6   A 6 TYR A  20  THR A  28 -1  N  ARG A  23   O  LEU A  36           
SHEET    1   B 2 ILE A 137  VAL A 138  0                                        
SHEET    2   B 2 LYS A 167  MET A 168 -1  O  LYS A 167   N  VAL A 138           
SHEET    1   C 2 LEU A 147  TYR A 149  0                                        
SHEET    2   C 2 ILE A 158  ILE A 160 -1  O  MET A 159   N  LEU A 148           
CISPEP   1 SER A  239    PRO A  240          0         5.69                     
SITE     1 AC1 18 GLY A  27  THR A  28  GLY A  29  ALA A  30                    
SITE     2 AC1 18 PHE A  31  SER A  32  VAL A  34  ALA A  47                    
SITE     3 AC1 18 LYS A  49  VAL A  79  GLN A  96  VAL A  98                    
SITE     4 AC1 18 GLU A 102  ASP A 162  HOH A 407  HOH A 427                    
SITE     5 AC1 18 HOH A 430  HOH A 435                                          
CRYST1   65.681   65.681  139.889  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015225  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015225  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007149        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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