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Database: PDB
Entry: 3FEG
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HEADER    TRANSFERASE                             29-NOV-08   3FEG              
TITLE     CRYSTAL STRUCTURE OF HUMAN CHOLINE KINASE BETA IN COMPLEX WITH        
TITLE    2 PHOSPHORYLATED HEMICHOLINIUM-3 AND ADENOSINE NUCLEOTIDE              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINE/ETHANOLAMINE KINASE;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CHOLINE KINASE BETA, CK, ETHANOLAMINE KINASE, EK;           
COMPND   5 EC: 2.7.1.32, 2.7.1.82;                                              
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: CHKB, CHETK, CHKL;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC                                
KEYWDS    NON-PROTEIN KINASE, CHOLINE KINASE, STRUCTURAL GENOMICS CONSORTIUM,   
KEYWDS   2 SGC, HEMICHOLINIUM-3, PHOSPHORYLATION, KINASE, PHOSPHOPROTEIN,       
KEYWDS   3 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.S.HONG,W.TEMPEL,W.M.RABEH,F.MACKENZIE,C.H.ARROWSMITH,A.M.EDWARDS,   
AUTHOR   2 C.BOUNTRA,J.WEIGELT,A.BOCHKAREV,H.W.PARK,STRUCTURAL GENOMICS         
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   2   01-SEP-10 3FEG    1       JRNL                                     
REVDAT   1   23-DEC-08 3FEG    0                                                
JRNL        AUTH   B.S.HONG,A.ALLALI-HASSANI,W.TEMPEL,P.J.FINERTY,F.MACKENZIE,  
JRNL        AUTH 2 S.DIMOV,M.VEDADI,H.W.PARK                                    
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN CHOLINE KINASE ISOFORMS IN       
JRNL        TITL 2 COMPLEX WITH HEMICHOLINIUM-3: SINGLE AMINO ACID NEAR THE     
JRNL        TITL 3 ACTIVE SITE INFLUENCES INHIBITOR SENSITIVITY.                
JRNL        REF    J.BIOL.CHEM.                  V. 285 16330 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20299452                                                     
JRNL        DOI    10.1074/JBC.M109.039024                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0069                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 92425                          
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) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.193                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4612                            
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) : 1.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.34                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5137                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.21                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 268                          
REMARK   3   BIN FREE R VALUE                    : 0.2970                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2732                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 298                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07700                                              
REMARK   3    B22 (A**2) : -0.12800                                             
REMARK   3    B33 (A**2) : 0.10000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.05200                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.050         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.050         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.029         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.510         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.959                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3105 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2122 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4267 ; 1.462 ; 2.015       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5114 ; 1.881 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   377 ; 5.381 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   152 ;32.734 ;23.947       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   508 ;12.047 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;14.874 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   433 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3413 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   652 ; 0.003 ; 0.020       
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):  1754 ; 2.905 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   696 ; 1.582 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2852 ; 3.720 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1351 ; 3.667 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1393 ; 4.871 ; 3.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  5227 ; 2.250 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   302 ;11.547 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  5117 ; 5.366 ; 3.000       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. HEMICHOLINIUM RESTRAINTS WERE CALCULATED BY THE PRODRG   
REMARK   3  SERVER.                                                             
REMARK   4                                                                      
REMARK   4 3FEG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050488.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97243                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 92472                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55900                            
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2IG7                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN BUFFER: 0.01M TRIS PH 8, 0.5M    
REMARK 280  SODIUM CHLORIDE, 0.005M MAGNESIUM CHLORIDE, 0.01M DTT, 0.003M       
REMARK 280  HEMICHOLINIUM-3, 0.005M ADP; PRECIPITANT: 0.1M SODIUM CACODYLATE,   
REMARK 280  30% PEG-4000, 0.2M AMMONIUM SULFATE, VAPOR DIFFUSION, TEMPERATURE   
REMARK 280  291K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       48.99700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.49350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       48.99700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       36.49350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL                        
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   BIOMT1   2 -1.000000  0.000000  0.000000       68.93141            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       55.21550            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     HIS A    20                                                      
REMARK 465     HIS A    21                                                      
REMARK 465     HIS A    22                                                      
REMARK 465     HIS A    23                                                      
REMARK 465     HIS A    24                                                      
REMARK 465     HIS A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     GLY A    28                                                      
REMARK 465     LEU A    29                                                      
REMARK 465     VAL A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     ARG A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     SER A    34                                                      
REMARK 465     ARG A    35                                                      
REMARK 465     ARG A    36                                                      
REMARK 465     ARG A    37                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     SER A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     LEU A    41                                                      
REMARK 465     SER A    75                                                      
REMARK 465     GLY A    76                                                      
REMARK 465     GLY A    77                                                      
REMARK 465     LEU A    78                                                      
REMARK 465     SER A    79                                                      
REMARK 465     ALA A   108                                                      
REMARK 465     ILE A   109                                                      
REMARK 465     LEU A   110                                                      
REMARK 465     GLU A   255                                                      
REMARK 465     ASN A   256                                                      
REMARK 465     ALA A   257                                                      
REMARK 465     THR A   389                                                      
REMARK 465     SER A   390                                                      
REMARK 465     VAL A   391                                                      
REMARK 465     HIS A   392                                                      
REMARK 465     SER A   393                                                      
REMARK 465     SER A   394                                                      
REMARK 465     SER A   395                                                      
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  43    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A  47    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A  48    NE   CZ   NH1  NH2                                  
REMARK 470     GLN A  51    OE1  NE2                                            
REMARK 470     ARG A  62    CZ   NH1  NH2                                       
REMARK 470     ARG A  63    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 154    NZ                                                  
REMARK 470     GLU A 184    CD   OE1  OE2                                       
REMARK 470     LYS A 197    CE   NZ                                             
REMARK 470     LYS A 219    CE   NZ                                             
REMARK 470     LYS A 227    CD   CE   NZ                                        
REMARK 470     GLU A 291    CD   OE1  OE2                                       
REMARK 470     GLU A 292    CD   OE1  OE2                                       
REMARK 470     LYS A 297    CE   NZ                                             
REMARK 470     ARG A 299    CZ   NH1  NH2                                       
REMARK 470     GLN A 328    OE1  NE2                                            
REMARK 470     GLN A 331    CD   OE1  NE2                                       
REMARK 470     ARG A 332    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 333    CE   NZ                                             
REMARK 470     GLU A 336    OE1  OE2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG A   226     OE2  GLU A   230              1.96            
REMARK 500   OE1  GLN A   156     NH1  ARG A   159              2.02            
REMARK 500   OE1  GLU A   307     O    HOH A   483              2.10            
REMARK 500   OE1  GLU A   283    UNK   UNX A   400              2.15            
REMARK 500   O3'  ADP A   397     O    HOH A   630              2.16            
REMARK 500   O    TYR A   286    UNK   UNX A   400              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 145   CD    GLU A 145   OE2    -0.077                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 150      176.01    179.69                                   
REMARK 500    PRO A 180       48.04    -84.64                                   
REMARK 500    PRO A 185       49.74    -83.56                                   
REMARK 500    ASN A 241        1.91     81.70                                   
REMARK 500    ASP A 242       50.64   -154.96                                   
REMARK 500    ASP A 264       84.88     71.48                                   
REMARK 500    THR A 365      -88.29   -126.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 FOR THE LIGAND HC7 THE STEREO-CENTER AT THE "2" POSITION IS          
REMARK 600 SPECIFIED AS (2S), HOWEVER CAN BE (2R) OR (2S) AS THE MORPHOLINIUM   
REMARK 600 RING CAN OPEN LOSING THE SPECIFIED CONFIGURATION.                    
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 399  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 247   OD1                                                    
REMARK 620 2 ASP A 264   OD2  89.7                                              
REMARK 620 3 ADP A 397   O3B 173.7  96.3                                        
REMARK 620 4 ADP A 397   O1A  88.6 104.0  88.0                                  
REMARK 620 5 HOH A 671   O    94.9 166.9  79.7  88.4                            
REMARK 620 6 HOH A 633   O    68.1 140.1 105.9  45.7  52.7                      
REMARK 620 7 HOH A 672   O    93.2  83.9  89.4 172.0  83.6 128.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HC7 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 396                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 397                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A 398                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 399                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 400                 
DBREF  3FEG A   35   395  UNP    Q9Y259   CHKB_HUMAN      35    395             
SEQADV 3FEG GLY A   17  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG SER A   18  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG SER A   19  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG HIS A   20  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG HIS A   21  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG HIS A   22  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG HIS A   23  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG HIS A   24  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG HIS A   25  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG SER A   26  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG SER A   27  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG GLY A   28  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG LEU A   29  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG VAL A   30  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG PRO A   31  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG ARG A   32  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG GLY A   33  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 3FEG SER A   34  UNP  Q9Y259              EXPRESSION TAG                 
SEQRES   1 A  379  GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 A  379  VAL PRO ARG GLY SER ARG ARG ARG ALA SER SER LEU SER          
SEQRES   3 A  379  ARG ASP ALA GLU ARG ARG ALA TYR GLN TRP CYS ARG GLU          
SEQRES   4 A  379  TYR LEU GLY GLY ALA TRP ARG ARG VAL GLN PRO GLU GLU          
SEQRES   5 A  379  LEU ARG VAL TYR PRO VAL SER GLY GLY LEU SER ASN LEU          
SEQRES   6 A  379  LEU PHE ARG CYS SER LEU PRO ASP HIS LEU PRO SER VAL          
SEQRES   7 A  379  GLY GLU GLU PRO ARG GLU VAL LEU LEU ARG LEU TYR GLY          
SEQRES   8 A  379  ALA ILE LEU GLN GLY VAL ASP SER LEU VAL LEU GLU SER          
SEQRES   9 A  379  VAL MET PHE ALA ILE LEU ALA GLU ARG SER LEU GLY PRO          
SEQRES  10 A  379  GLN LEU TYR GLY VAL PHE PRO GLU GLY ARG LEU GLU GLN          
SEQRES  11 A  379  TYR ILE PRO SER ARG PRO LEU LYS THR GLN GLU LEU ARG          
SEQRES  12 A  379  GLU PRO VAL LEU SER ALA ALA ILE ALA THR LYS MET ALA          
SEQRES  13 A  379  GLN PHE HIS GLY MET GLU MET PRO PHE THR LYS GLU PRO          
SEQRES  14 A  379  HIS TRP LEU PHE GLY THR MET GLU ARG TYR LEU LYS GLN          
SEQRES  15 A  379  ILE GLN ASP LEU PRO PRO THR GLY LEU PRO GLU MET ASN          
SEQRES  16 A  379  LEU LEU GLU MET TYR SER LEU LYS ASP GLU MET GLY ASN          
SEQRES  17 A  379  LEU ARG LYS LEU LEU GLU SER THR PRO SER PRO VAL VAL          
SEQRES  18 A  379  PHE CYS HIS ASN ASP ILE GLN GLU GLY ASN ILE LEU LEU          
SEQRES  19 A  379  LEU SER GLU PRO GLU ASN ALA ASP SER LEU MET LEU VAL          
SEQRES  20 A  379  ASP PHE GLU TYR SER SER TYR ASN TYR ARG GLY PHE ASP          
SEQRES  21 A  379  ILE GLY ASN HIS PHE CYS GLU TRP VAL TYR ASP TYR THR          
SEQRES  22 A  379  HIS GLU GLU TRP PRO PHE TYR LYS ALA ARG PRO THR ASP          
SEQRES  23 A  379  TYR PRO THR GLN GLU GLN GLN LEU HIS PHE ILE ARG HIS          
SEQRES  24 A  379  TYR LEU ALA GLU ALA LYS LYS GLY GLU THR LEU SER GLN          
SEQRES  25 A  379  GLU GLU GLN ARG LYS LEU GLU GLU ASP LEU LEU VAL GLU          
SEQRES  26 A  379  VAL SER ARG TYR ALA LEU ALA SER HIS PHE PHE TRP GLY          
SEQRES  27 A  379  LEU TRP SER ILE LEU GLN ALA SER MET SER THR ILE GLU          
SEQRES  28 A  379  PHE GLY TYR LEU ASP TYR ALA GLN SER ARG PHE GLN PHE          
SEQRES  29 A  379  TYR PHE GLN GLN LYS GLY GLN LEU THR SER VAL HIS SER          
SEQRES  30 A  379  SER SER                                                      
HET    HC7  A   1      68                                                       
HET    SO4  A 396       5                                                       
HET    ADP  A 397      27                                                       
HET    AMP  A 398      23                                                       
HET     MG  A 399       1                                                       
HET    UNX  A 400       1                                                       
HET    UNX  A   2       1                                                       
HETNAM     HC7 (2S)-2-[4'-({DIMETHYL[2-(PHOSPHONOOXY)                           
HETNAM   2 HC7  ETHYL]AMMONIO}ACETYL)BIPHENYL-4-YL]-2-HYDROXY-4,4-              
HETNAM   3 HC7  DIMETHYLMORPHOLIN-4-IUM                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETSYN     HC7 2-{4-[4-(2-{DIMETHYL[2-(PHOSPHONATOOXY)                          
HETSYN   2 HC7  ETHYL]AZANIUMYL}ACETYL)PHENYL]PHENYL}-2-HYDROXY-4,4-            
HETSYN   3 HC7  DIMETHYLMORPHOLIN-4-IUM                                         
FORMUL   2  HC7    C24 H35 N2 O7 P 2+                                           
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  ADP    C10 H15 N5 O10 P2                                            
FORMUL   5  AMP    C10 H14 N5 O7 P                                              
FORMUL   6   MG    MG 2+                                                        
FORMUL   7  UNX    2(X)                                                         
FORMUL   9  HOH   *298(H2 O)                                                    
HELIX    1   1 SER A   42  GLY A   58  1                                  17    
HELIX    2   2 GLY A   59  VAL A   64  5                                   6    
HELIX    3   3 GLN A   65  LEU A   69  5                                   5    
HELIX    4   4 GLY A  112  ARG A  129  1                                  18    
HELIX    5   5 LYS A  154  ARG A  159  5                                   6    
HELIX    6   6 GLU A  160  GLY A  176  1                                  17    
HELIX    7   7 HIS A  186  LEU A  202  1                                  17    
HELIX    8   8 ASN A  211  TYR A  216  1                                   6    
HELIX    9   9 SER A  217  SER A  231  1                                  15    
HELIX   10  10 GLN A  244  GLY A  246  5                                   3    
HELIX   11  11 ARG A  273  TRP A  284  1                                  12    
HELIX   12  12 PRO A  300  TYR A  303  5                                   4    
HELIX   13  13 THR A  305  LYS A  321  1                                  17    
HELIX   14  14 SER A  327  SER A  362  1                                  36    
HELIX   15  15 GLY A  369  GLN A  387  1                                  19    
SHEET    1   A 5 TYR A  72  PRO A  73  0                                        
SHEET    2   A 5 LEU A  82  SER A  86 -1  O  ARG A  84   N  TYR A  72           
SHEET    3   A 5 GLU A 100  LEU A 105 -1  O  LEU A 103   N  PHE A  83           
SHEET    4   A 5 GLY A 142  GLN A 146 -1  O  GLU A 145   N  LEU A 102           
SHEET    5   A 5 LEU A 135  PHE A 139 -1  N  TYR A 136   O  LEU A 144           
SHEET    1   B 3 SER A 150  PRO A 152  0                                        
SHEET    2   B 3 ILE A 248  LEU A 251 -1  O  LEU A 250   N  ARG A 151           
SHEET    3   B 3 LEU A 260  LEU A 262 -1  O  MET A 261   N  LEU A 249           
SHEET    1   C 2 VAL A 236  CYS A 239  0                                        
SHEET    2   C 2 SER A 269  TYR A 272 -1  O  SER A 269   N  CYS A 239           
SHEET    1   D 2 TYR A 286  ASP A 287  0                                        
SHEET    2   D 2 LYS A 297  ALA A 298 -1  O  LYS A 297   N  ASP A 287           
LINK         OD1 ASN A 247                MG    MG A 399     1555   1555  2.25  
LINK         OD2 ASP A 264                MG    MG A 399     1555   1555  2.48  
LINK         O3B ADP A 397                MG    MG A 399     1555   1555  2.00  
LINK         O1A ADP A 397                MG    MG A 399     1555   1555  1.93  
LINK        MG    MG A 399                 O   HOH A 671     1555   1555  2.08  
LINK        MG    MG A 399                 O   HOH A 633     1555   1555  2.48  
LINK        MG    MG A 399                 O   HOH A 672     1555   1555  1.80  
CISPEP   1 TRP A  293    PRO A  294          0        13.96                     
SITE     1 AC1 18 ASP A 242  GLN A 244  ASP A 264  TYR A 267                    
SITE     2 AC1 18 GLU A 283  TYR A 288  PHE A 295  TRP A 353                    
SITE     3 AC1 18 TRP A 356  GLU A 367  PHE A 368  TYR A 370                    
SITE     4 AC1 18 TYR A 373  HOH A 527  HOH A 613  HOH A 631                    
SITE     5 AC1 18 HOH A 632  HOH A 672                                          
SITE     1 AC2  3 HIS A 311  ARG A 314  HIS A 315                               
SITE     1 AC3 21 LEU A  82  LEU A 102  ARG A 104  PRO A 133                    
SITE     2 AC3 21 GLU A 145  GLN A 146  TYR A 147  ILE A 148                    
SITE     3 AC3 21 GLY A 246  ASN A 247  LEU A 249  ASP A 264                    
SITE     4 AC3 21 AMP A 398   MG A 399  HOH A 527  HOH A 630                    
SITE     5 AC3 21 HOH A 632  HOH A 633  HOH A 634  HOH A 671                    
SITE     6 AC3 21 HOH A 672                                                     
SITE     1 AC4 16 VAL A  74  LEU A  82  LEU A 102  PRO A 133                    
SITE     2 AC4 16 GLU A 145  GLN A 146  TYR A 147  ILE A 148                    
SITE     3 AC4 16 GLY A 246  LEU A 249  ADP A 397  HOH A 507                    
SITE     4 AC4 16 HOH A 630  HOH A 633  HOH A 634  HOH A 671                    
SITE     1 AC5  6 ASN A 247  ASP A 264  ADP A 397  HOH A 633                    
SITE     2 AC5  6 HOH A 671  HOH A 672                                          
SITE     1 AC6  4 GLU A 245  GLU A 283  TYR A 286  TYR A 288                    
CRYST1   97.994   72.987   62.397  90.00 117.76  90.00 C 1 2 1       4          
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      0.010205  0.000000  0.005372        0.00000                         
SCALE2      0.000000  0.013701  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018111        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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