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Database: PDB
Entry: 6CQD
LinkDB: 6CQD
Original site: 6CQD 
HEADER    TRANSFERASE                             14-MAR-18   6CQD              
TITLE     CRYSTAL STRUCTURE OF HPK1 IN COMPLEX WITH ATP ANALOGUE (AMPPNP)       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE KINASE 1;   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HKP1, HEMATOPOIETIC PROGENITOR KINASE, MAPK/ERK KINASE      
COMPND   5 KINASE KINASE 1, MEKKK 1;                                            
COMPND   6 EC: 2.7.11.1;                                                        
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: MAP4K1, HPK1;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    PROTEIN KINASE, TRANSFERASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.WU,I.LEHOUX,Y.FRANKE,K.MORTARA,W.WANG                               
REVDAT   3   13-MAR-24 6CQD    1       LINK                                     
REVDAT   2   16-JAN-19 6CQD    1       JRNL                                     
REVDAT   1   19-DEC-18 6CQD    0                                                
JRNL        AUTH   P.WU,C.J.SNEERINGER,K.E.PITTS,E.S.DAY,B.K.CHAN,B.WEI,        
JRNL        AUTH 2 I.LEHOUX,K.MORTARA,H.LI,J.WU,Y.FRANKE,J.G.MOFFAT,J.L.GROGAN, 
JRNL        AUTH 3 T.P.HEFFRON,W.WANG                                           
JRNL        TITL   HEMATOPOIETIC PROGENITOR KINASE-1 STRUCTURE IN A             
JRNL        TITL 2 DOMAIN-SWAPPED DIMER.                                        
JRNL        REF    STRUCTURE                     V.  27   125 2019              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   30503777                                                     
JRNL        DOI    10.1016/J.STR.2018.10.025                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.12 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.970                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 34951                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3303                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.9981 -  6.1109    0.99     2654   156  0.1503 0.1715        
REMARK   3     2  6.1109 -  4.8520    0.95     2523   165  0.1570 0.1847        
REMARK   3     3  4.8520 -  4.2391    0.98     2618   158  0.1330 0.1855        
REMARK   3     4  4.2391 -  3.8517    0.98     2622   147  0.1514 0.1975        
REMARK   3     5  3.8517 -  3.5758    0.96     2570   151  0.1787 0.2097        
REMARK   3     6  3.5758 -  3.3650    0.96     2614   132  0.1951 0.2616        
REMARK   3     7  3.3650 -  3.1965    0.93     2523   120  0.2184 0.3349        
REMARK   3     8  3.1965 -  3.0574    0.96     2549   116  0.2346 0.3037        
REMARK   3     9  3.0574 -  2.9397    0.97     2637   145  0.2417 0.2869        
REMARK   3    10  2.9397 -  2.8383    0.97     2561   147  0.2437 0.2855        
REMARK   3    11  2.8383 -  2.7496    0.97     2588   158  0.2463 0.2955        
REMARK   3    12  2.7496 -  2.6710    0.97     2618   119  0.2367 0.2894        
REMARK   3    13  2.6710 -  2.6007    0.97     2628   119  0.2453 0.3362        
REMARK   3    14  2.6007 -  2.5372    0.97     2636   135  0.2379 0.2966        
REMARK   3    15  2.5372 -  2.4795    0.96     2607   121  0.2483 0.3021        
REMARK   3    16  2.4795 -  2.4268    0.96     2522   138  0.2505 0.3309        
REMARK   3    17  2.4268 -  2.3782    0.95     2580   111  0.2435 0.2846        
REMARK   3    18  2.3782 -  2.3334    0.92     2437   158  0.2705 0.3244        
REMARK   3    19  2.3334 -  2.2917    0.92     2494   141  0.2615 0.3597        
REMARK   3    20  2.2917 -  2.2528    0.94     2523   120  0.2777 0.3298        
REMARK   3    21  2.2528 -  2.2165    0.95     2622   166  0.2840 0.3310        
REMARK   3    22  2.2165 -  2.1824    0.96     2497   146  0.2926 0.3008        
REMARK   3    23  2.1824 -  2.1503    0.95     2610   104  0.2966 0.3504        
REMARK   3    24  2.1503 -  2.1200    0.94     2527   130  0.3243 0.4060        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.010           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           4749                                  
REMARK   3   ANGLE     :  0.847           6415                                  
REMARK   3   CHIRALITY :  0.030            719                                  
REMARK   3   PLANARITY :  0.004            802                                  
REMARK   3   DIHEDRAL  : 14.486           1763                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 2:93                                  
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4348   9.5852  12.8207              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3404 T22:   0.2227                                     
REMARK   3      T33:   0.3081 T12:   0.0688                                     
REMARK   3      T13:  -0.0513 T23:  -0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3843 L22:   0.2132                                     
REMARK   3      L33:   0.5661 L12:   0.2034                                     
REMARK   3      L13:   0.0040 L23:  -0.1443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1610 S12:  -0.0468 S13:   0.0502                       
REMARK   3      S21:   0.1183 S22:   0.0745 S23:  -0.0592                       
REMARK   3      S31:  -0.5241 S32:  -0.0580 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 94:294                                
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5789 -10.2274  26.9589              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1432 T22:   0.1518                                     
REMARK   3      T33:   0.1844 T12:  -0.0192                                     
REMARK   3      T13:   0.0011 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6434 L22:   0.9380                                     
REMARK   3      L33:   1.8027 L12:  -0.1932                                     
REMARK   3      L13:   0.3552 L23:   0.0944                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0332 S12:  -0.0403 S13:  -0.0245                       
REMARK   3      S21:   0.0958 S22:  -0.0582 S23:   0.0512                       
REMARK   3      S31:   0.0325 S32:  -0.1285 S33:  -0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B AND RESI 4:93                                  
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7691  24.9088  59.5205              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3650 T22:   0.5224                                     
REMARK   3      T33:   0.3887 T12:   0.0772                                     
REMARK   3      T13:   0.0357 T23:   0.0710                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1772 L22:   0.4252                                     
REMARK   3      L33:   0.3893 L12:   0.0593                                     
REMARK   3      L13:   0.1403 L23:   0.0294                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0363 S12:   0.1278 S13:   0.0231                       
REMARK   3      S21:  -0.3596 S22:   0.1569 S23:  -0.0654                       
REMARK   3      S31:  -0.2569 S32:  -0.2039 S33:   0.0001                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND RESI 94:294                                
REMARK   3    ORIGIN FOR THE GROUP (A):  25.4382   4.1211  61.2632              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4161 T22:   0.2129                                     
REMARK   3      T33:   0.1787 T12:   0.0322                                     
REMARK   3      T13:   0.0662 T23:   0.0299                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5888 L22:  -0.2162                                     
REMARK   3      L33:   1.1237 L12:  -0.5525                                     
REMARK   3      L13:   0.2566 L23:   0.3176                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1015 S12:  -0.0684 S13:   0.0713                       
REMARK   3      S21:  -0.1237 S22:  -0.0165 S23:  -0.0101                       
REMARK   3      S31:   0.6599 S32:  -0.0044 S33:  -0.1307                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6CQD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000233214.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-SEP-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35007                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.120                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 12% PEG8000,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K                     
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       73.44300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.94100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       73.44300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.94100            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 519  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     LYS A    49                                                      
REMARK 465     MET A    50                                                      
REMARK 465     GLU A    51                                                      
REMARK 465     PRO A    52                                                      
REMARK 465     ASN A   295                                                      
REMARK 465     SER A   296                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     ASN B   295                                                      
REMARK 465     SER B   296                                                      
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    ASP A  54     -145.26    -89.02                                   
REMARK 500    LEU A  84     -121.52     49.62                                   
REMARK 500    GLN A  85       32.98    -98.32                                   
REMARK 500    ARG A 136       -6.64     70.86                                   
REMARK 500    ASP A 155       83.06     65.60                                   
REMARK 500    LEU A 188      -65.55    -90.01                                   
REMARK 500    LEU A 255       40.96    -92.97                                   
REMARK 500    ASN A 293      -95.35   -117.27                                   
REMARK 500    LEU B  20     -102.69   -114.19                                   
REMARK 500    ASP B 137       39.07   -145.98                                   
REMARK 500    ASP B 155       77.54     58.68                                   
REMARK 500    PHE B 156       33.74    -93.97                                   
REMARK 500    LYS B 189       60.83   -172.59                                   
REMARK 500    LEU B 211       -2.32     71.95                                   
REMARK 500    LEU B 255       47.80    -92.43                                   
REMARK 500    ASN B 293      -87.74   -139.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 492        DISTANCE =  5.85 ANGSTROMS                       
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 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 142   OD1                                                    
REMARK 620 2 ASP A 155   OD2  86.1                                              
REMARK 620 3 ANP A 301   O1G 152.0 119.6                                        
REMARK 620 4 ANP A 301   O2A  98.8  61.8 103.1                                  
REMARK 620 5 HOH A 402   O    93.8 173.6  62.0 112.0                            
REMARK 620 6 HOH A 445   O    96.0  81.6  78.5 139.1 104.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 155   OD1                                                    
REMARK 620 2 ASP A 155   OD2  62.0                                              
REMARK 620 3 ANP A 301   O3G 130.2  84.6                                        
REMARK 620 4 ANP A 301   O2B  84.9  87.7  56.2                                  
REMARK 620 5 HOH A 405   O   137.3  93.7  75.7 131.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 142   OD1                                                    
REMARK 620 2 ASP B 155   OD2  88.4                                              
REMARK 620 3 ANP B 302   O2G 162.3  94.3                                        
REMARK 620 4 ANP B 302   O3A 134.7  66.0  61.4                                  
REMARK 620 5 ANP B 302   O2A  82.6  86.0 115.1  60.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP B 302                 
DBREF  6CQD A    2   293  UNP    Q92918   M4K1_HUMAN       2    293             
DBREF  6CQD B    2   293  UNP    Q92918   M4K1_HUMAN       2    293             
SEQADV 6CQD GLY A    0  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6CQD SER A    1  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6CQD GLU A  165  UNP  Q92918    THR   165 CONFLICT                       
SEQADV 6CQD GLU A  171  UNP  Q92918    SER   171 CONFLICT                       
SEQADV 6CQD GLY A  294  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6CQD ASN A  295  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6CQD SER A  296  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6CQD GLY B    0  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6CQD SER B    1  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6CQD GLU B  165  UNP  Q92918    THR   165 CONFLICT                       
SEQADV 6CQD GLU B  171  UNP  Q92918    SER   171 CONFLICT                       
SEQADV 6CQD GLY B  294  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6CQD ASN B  295  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6CQD SER B  296  UNP  Q92918              EXPRESSION TAG                 
SEQRES   1 A  297  GLY SER ASP VAL VAL ASP PRO ASP ILE PHE ASN ARG ASP          
SEQRES   2 A  297  PRO ARG ASP HIS TYR ASP LEU LEU GLN ARG LEU GLY GLY          
SEQRES   3 A  297  GLY THR TYR GLY GLU VAL PHE LYS ALA ARG ASP LYS VAL          
SEQRES   4 A  297  SER GLY ASP LEU VAL ALA LEU LYS MET VAL LYS MET GLU          
SEQRES   5 A  297  PRO ASP ASP ASP VAL SER THR LEU GLN LYS GLU ILE LEU          
SEQRES   6 A  297  ILE LEU LYS THR CYS ARG HIS ALA ASN ILE VAL ALA TYR          
SEQRES   7 A  297  HIS GLY SER TYR LEU TRP LEU GLN LYS LEU TRP ILE CYS          
SEQRES   8 A  297  MET GLU PHE CYS GLY ALA GLY SER LEU GLN ASP ILE TYR          
SEQRES   9 A  297  GLN VAL THR GLY SER LEU SER GLU LEU GLN ILE SER TYR          
SEQRES  10 A  297  VAL CYS ARG GLU VAL LEU GLN GLY LEU ALA TYR LEU HIS          
SEQRES  11 A  297  SER GLN LYS LYS ILE HIS ARG ASP ILE LYS GLY ALA ASN          
SEQRES  12 A  297  ILE LEU ILE ASN ASP ALA GLY GLU VAL ARG LEU ALA ASP          
SEQRES  13 A  297  PHE GLY ILE SER ALA GLN ILE GLY ALA GLU LEU ALA ARG          
SEQRES  14 A  297  ARG LEU GLU PHE ILE GLY THR PRO TYR TRP MET ALA PRO          
SEQRES  15 A  297  GLU VAL ALA ALA VAL ALA LEU LYS GLY GLY TYR ASN GLU          
SEQRES  16 A  297  LEU CYS ASP ILE TRP SER LEU GLY ILE THR ALA ILE GLU          
SEQRES  17 A  297  LEU ALA GLU LEU GLN PRO PRO LEU PHE ASP VAL HIS PRO          
SEQRES  18 A  297  LEU ARG VAL LEU PHE LEU MET THR LYS SER GLY TYR GLN          
SEQRES  19 A  297  PRO PRO ARG LEU LYS GLU LYS GLY LYS TRP SER ALA ALA          
SEQRES  20 A  297  PHE HIS ASN PHE ILE LYS VAL THR LEU THR LYS SER PRO          
SEQRES  21 A  297  LYS LYS ARG PRO SER ALA THR LYS MET LEU SER HIS GLN          
SEQRES  22 A  297  LEU VAL SER GLN PRO GLY LEU ASN ARG GLY LEU ILE LEU          
SEQRES  23 A  297  ASP LEU LEU ASP LYS LEU LYS ASN GLY ASN SER                  
SEQRES   1 B  297  GLY SER ASP VAL VAL ASP PRO ASP ILE PHE ASN ARG ASP          
SEQRES   2 B  297  PRO ARG ASP HIS TYR ASP LEU LEU GLN ARG LEU GLY GLY          
SEQRES   3 B  297  GLY THR TYR GLY GLU VAL PHE LYS ALA ARG ASP LYS VAL          
SEQRES   4 B  297  SER GLY ASP LEU VAL ALA LEU LYS MET VAL LYS MET GLU          
SEQRES   5 B  297  PRO ASP ASP ASP VAL SER THR LEU GLN LYS GLU ILE LEU          
SEQRES   6 B  297  ILE LEU LYS THR CYS ARG HIS ALA ASN ILE VAL ALA TYR          
SEQRES   7 B  297  HIS GLY SER TYR LEU TRP LEU GLN LYS LEU TRP ILE CYS          
SEQRES   8 B  297  MET GLU PHE CYS GLY ALA GLY SER LEU GLN ASP ILE TYR          
SEQRES   9 B  297  GLN VAL THR GLY SER LEU SER GLU LEU GLN ILE SER TYR          
SEQRES  10 B  297  VAL CYS ARG GLU VAL LEU GLN GLY LEU ALA TYR LEU HIS          
SEQRES  11 B  297  SER GLN LYS LYS ILE HIS ARG ASP ILE LYS GLY ALA ASN          
SEQRES  12 B  297  ILE LEU ILE ASN ASP ALA GLY GLU VAL ARG LEU ALA ASP          
SEQRES  13 B  297  PHE GLY ILE SER ALA GLN ILE GLY ALA GLU LEU ALA ARG          
SEQRES  14 B  297  ARG LEU GLU PHE ILE GLY THR PRO TYR TRP MET ALA PRO          
SEQRES  15 B  297  GLU VAL ALA ALA VAL ALA LEU LYS GLY GLY TYR ASN GLU          
SEQRES  16 B  297  LEU CYS ASP ILE TRP SER LEU GLY ILE THR ALA ILE GLU          
SEQRES  17 B  297  LEU ALA GLU LEU GLN PRO PRO LEU PHE ASP VAL HIS PRO          
SEQRES  18 B  297  LEU ARG VAL LEU PHE LEU MET THR LYS SER GLY TYR GLN          
SEQRES  19 B  297  PRO PRO ARG LEU LYS GLU LYS GLY LYS TRP SER ALA ALA          
SEQRES  20 B  297  PHE HIS ASN PHE ILE LYS VAL THR LEU THR LYS SER PRO          
SEQRES  21 B  297  LYS LYS ARG PRO SER ALA THR LYS MET LEU SER HIS GLN          
SEQRES  22 B  297  LEU VAL SER GLN PRO GLY LEU ASN ARG GLY LEU ILE LEU          
SEQRES  23 B  297  ASP LEU LEU ASP LYS LEU LYS ASN GLY ASN SER                  
HET    ANP  A 301      31                                                       
HET     MG  A 302       1                                                       
HET     MG  A 303       1                                                       
HET     MG  B 301       1                                                       
HET    ANP  B 302      31                                                       
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  ANP    2(C10 H17 N6 O12 P3)                                         
FORMUL   4   MG    3(MG 2+)                                                     
FORMUL   8  HOH   *217(H2 O)                                                    
HELIX    1 AA1 ASP A   12  ASP A   15  5                                   4    
HELIX    2 AA2 ASP A   55  GLN A   60  1                                   6    
HELIX    3 AA3 GLN A   60  CYS A   69  1                                  10    
HELIX    4 AA4 SER A   98  GLY A  107  1                                  10    
HELIX    5 AA5 SER A  110  GLN A  131  1                                  22    
HELIX    6 AA6 LYS A  139  ALA A  141  5                                   3    
HELIX    7 AA7 PHE A  156  ARG A  168  1                                  13    
HELIX    8 AA8 THR A  175  MET A  179  5                                   5    
HELIX    9 AA9 ALA A  180  GLY A  190  1                                  11    
HELIX   10 AB1 GLU A  194  LEU A  211  1                                  18    
HELIX   11 AB2 HIS A  219  LYS A  229  1                                  11    
HELIX   12 AB3 SER A  244  LEU A  255  1                                  12    
HELIX   13 AB4 SER A  264  LEU A  269  1                                   6    
HELIX   14 AB5 SER A  270  SER A  275  5                                   6    
HELIX   15 AB6 ARG A  281  ASN A  293  1                                  13    
HELIX   16 AB7 ASP B   12  ASP B   15  5                                   4    
HELIX   17 AB8 VAL B   56  THR B   68  1                                  13    
HELIX   18 AB9 LEU B   99  GLY B  107  1                                   9    
HELIX   19 AC1 SER B  110  SER B  130  1                                  21    
HELIX   20 AC2 LYS B  139  ALA B  141  5                                   3    
HELIX   21 AC3 PHE B  156  GLU B  171  1                                  16    
HELIX   22 AC4 ALA B  180  GLY B  190  1                                  11    
HELIX   23 AC5 LEU B  195  LEU B  211  1                                  17    
HELIX   24 AC6 HIS B  219  LYS B  229  1                                  11    
HELIX   25 AC7 SER B  244  LEU B  255  1                                  12    
HELIX   26 AC8 SER B  264  SER B  270  1                                   7    
HELIX   27 AC9 HIS B  271  GLN B  276  1                                   6    
HELIX   28 AD1 ARG B  281  LYS B  292  1                                  12    
SHEET    1 AA1 5 TYR A  17  GLY A  24  0                                        
SHEET    2 AA1 5 VAL A  31  ASP A  36 -1  O  VAL A  31   N  LEU A  23           
SHEET    3 AA1 5 LEU A  42  MET A  47 -1  O  LEU A  45   N  PHE A  32           
SHEET    4 AA1 5 LYS A  86  GLU A  92 -1  O  ILE A  89   N  LYS A  46           
SHEET    5 AA1 5 TYR A  77  TRP A  83 -1  N  GLY A  79   O  CYS A  90           
SHEET    1 AA2 2 ILE A 143  ILE A 145  0                                        
SHEET    2 AA2 2 VAL A 151  LEU A 153 -1  O  ARG A 152   N  LEU A 144           
SHEET    1 AA3 5 TYR B  17  GLY B  24  0                                        
SHEET    2 AA3 5 GLY B  29  ASP B  36 -1  O  VAL B  31   N  LEU B  23           
SHEET    3 AA3 5 LEU B  42  LYS B  49 -1  O  LEU B  45   N  PHE B  32           
SHEET    4 AA3 5 LYS B  86  GLU B  92 -1  O  LEU B  87   N  VAL B  48           
SHEET    5 AA3 5 TYR B  77  TRP B  83 -1  N  TYR B  81   O  TRP B  88           
SHEET    1 AA4 3 GLY B  97  SER B  98  0                                        
SHEET    2 AA4 3 ILE B 143  ILE B 145 -1  O  ILE B 145   N  GLY B  97           
SHEET    3 AA4 3 VAL B 151  LEU B 153 -1  O  ARG B 152   N  LEU B 144           
LINK         OD1 ASN A 142                MG    MG A 302     1555   1555  2.17  
LINK         OD2 ASP A 155                MG    MG A 302     1555   1555  2.15  
LINK         OD1 ASP A 155                MG    MG A 303     1555   1555  2.18  
LINK         OD2 ASP A 155                MG    MG A 303     1555   1555  2.12  
LINK         O1G ANP A 301                MG    MG A 302     1555   1555  2.16  
LINK         O2A ANP A 301                MG    MG A 302     1555   1555  2.15  
LINK         O3G ANP A 301                MG    MG A 303     1555   1555  2.21  
LINK         O2B ANP A 301                MG    MG A 303     1555   1555  2.29  
LINK        MG    MG A 302                 O   HOH A 402     1555   1555  2.15  
LINK        MG    MG A 302                 O   HOH A 445     1555   1555  2.17  
LINK        MG    MG A 303                 O   HOH A 405     1555   1555  2.14  
LINK         OD1 ASN B 142                MG    MG B 301     1555   1555  2.17  
LINK         OD2 ASP B 155                MG    MG B 301     1555   1555  2.17  
LINK        MG    MG B 301                 O2G ANP B 302     1555   1555  2.17  
LINK        MG    MG B 301                 O3A ANP B 302     1555   1555  2.72  
LINK        MG    MG B 301                 O2A ANP B 302     1555   1555  2.17  
SITE     1 AC1 21 LEU A  23  GLY A  26  VAL A  31  ALA A  44                    
SITE     2 AC1 21 LYS A  46  MET A  91  GLU A  92  CYS A  94                    
SITE     3 AC1 21 ASP A 101  ALA A 141  ASN A 142  LEU A 144                    
SITE     4 AC1 21 ASP A 155   MG A 302   MG A 303  HOH A 402                    
SITE     5 AC1 21 HOH A 405  HOH A 418  HOH A 445  HOH A 480                    
SITE     6 AC1 21 HOH A 498                                                     
SITE     1 AC2  5 ASN A 142  ASP A 155  ANP A 301  HOH A 402                    
SITE     2 AC2  5 HOH A 445                                                     
SITE     1 AC3  3 ASP A 155  ANP A 301  HOH A 405                               
SITE     1 AC4  3 ASN B 142  ASP B 155  ANP B 302                               
SITE     1 AC5 15 LEU B  23  GLY B  25  GLY B  26  VAL B  31                    
SITE     2 AC5 15 ALA B  44  LYS B  46  MET B  91  GLU B  92                    
SITE     3 AC5 15 CYS B  94  ASP B 101  ALA B 141  ASN B 142                    
SITE     4 AC5 15 LEU B 144  ASP B 155   MG B 301                               
CRYST1  146.886   51.882  107.500  90.00 131.03  90.00 C 1 2 1       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      0.006808  0.000000  0.005924        0.00000                         
SCALE2      0.000000  0.019275  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012331        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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