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Database: PDB
Entry: 6C9G
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HEADER    TRANSFERASE                             26-JAN-18   6C9G              
TITLE     AMP-ACTIVATED PROTEIN KINASE BOUND TO PHARMACOLOGICAL ACTIVATOR R739  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1, 
COMPND   3 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1;           
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: AMPK SUBUNIT ALPHA-1,ACETYL-COA CARBOXYLASE KINASE,ACACA    
COMPND   6 KINASE,HYDROXYMETHYLGLUTARYL-COA REDUCTASE KINASE,HMGCR KINASE,TAU-  
COMPND   7 PROTEIN KINASE PRKAA1;                                               
COMPND   8 EC: 2.7.11.1,2.7.11.27,2.7.11.31,2.7.11.26;                          
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1;            
COMPND  13 CHAIN: B;                                                            
COMPND  14 SYNONYM: AMPKB;                                                      
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  18 CHAIN: C;                                                            
COMPND  19 SYNONYM: AMPKG;                                                      
COMPND  20 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: PRKAA1, AMPK1;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: PRKAB1, AMPK;                                                  
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: PRKAG1;                                                        
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    AMPK, ACTIVATOR, CRYSTAL, R739, TRANSFERASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.YAN,X.E.ZHOU,S.NOVICK,S.J.SHAW,Y.LI,Y.HITOSHI,J.S.BRUNZELLE,        
AUTHOR   2 P.R.GRIFFIN,H.E.XU,K.MELCHER                                         
REVDAT   6   25-DEC-19 6C9G    1       SEQADV                                   
REVDAT   5   17-APR-19 6C9G    1       REMARK                                   
REVDAT   4   20-FEB-19 6C9G    1       REMARK                                   
REVDAT   3   30-JAN-19 6C9G    1       JRNL                                     
REVDAT   2   12-DEC-18 6C9G    1       JRNL                                     
REVDAT   1   28-NOV-18 6C9G    0                                                
JRNL        AUTH   Y.YAN,X.E.ZHOU,S.J.NOVICK,S.J.SHAW,Y.LI,J.S.BRUNZELLE,       
JRNL        AUTH 2 Y.HITOSHI,P.R.GRIFFIN,H.E.XU,K.MELCHER                       
JRNL        TITL   STRUCTURES OF AMP-ACTIVATED PROTEIN KINASE BOUND TO NOVEL    
JRNL        TITL 2 PHARMACOLOGICAL ACTIVATORS IN PHOSPHORYLATED,                
JRNL        TITL 3 NON-PHOSPHORYLATED, AND NUCLEOTIDE-FREE STATES.              
JRNL        REF    J. BIOL. CHEM.                V. 294   953 2019              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   30478170                                                     
JRNL        DOI    10.1074/JBC.RA118.004883                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.56                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 51004                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3622                            
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 49.5648 -  5.8142    1.00     5136   391  0.1871 0.2304        
REMARK   3     2  5.8142 -  4.6160    1.00     4835   369  0.1719 0.2138        
REMARK   3     3  4.6160 -  4.0328    1.00     4770   360  0.1672 0.2036        
REMARK   3     4  4.0328 -  3.6642    1.00     4674   398  0.1999 0.2218        
REMARK   3     5  3.6642 -  3.4016    1.00     4729   322  0.2144 0.2587        
REMARK   3     6  3.4016 -  3.2011    1.00     4709   339  0.2414 0.2885        
REMARK   3     7  3.2011 -  3.0408    1.00     4667   335  0.2587 0.2964        
REMARK   3     8  3.0408 -  2.9085    1.00     4644   365  0.2591 0.3095        
REMARK   3     9  2.9085 -  2.7965    1.00     4588   365  0.2735 0.2891        
REMARK   3    10  2.7965 -  2.7000    1.00     4630   378  0.2884 0.2997        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
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)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.920           
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      :  0.006           7296                                  
REMARK   3   ANGLE     :  0.954           9909                                  
REMARK   3   CHIRALITY :  0.038           1113                                  
REMARK   3   PLANARITY :  0.005           1225                                  
REMARK   3   DIHEDRAL  : 12.140           2761                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 42 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.1117  26.6498 -32.5463              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4171 T22:   0.4019                                     
REMARK   3      T33:   0.4575 T12:  -0.0956                                     
REMARK   3      T13:   0.0272 T23:  -0.1488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0009 L22:   0.0029                                     
REMARK   3      L33:   0.0026 L12:  -0.0003                                     
REMARK   3      L13:  -0.0012 L23:   0.0012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0075 S12:   0.0062 S13:   0.0067                       
REMARK   3      S21:  -0.0075 S22:  -0.0126 S23:   0.0092                       
REMARK   3      S31:  -0.0014 S32:   0.0174 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 72 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -23.0574  35.9780 -30.6398              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4623 T22:   0.3560                                     
REMARK   3      T33:   0.3060 T12:   0.0214                                     
REMARK   3      T13:  -0.0183 T23:  -0.1242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0010 L22:   0.0024                                     
REMARK   3      L33:   0.0008 L12:   0.0013                                     
REMARK   3      L13:   0.0008 L23:   0.0002                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0181 S12:   0.0033 S13:  -0.0017                       
REMARK   3      S21:  -0.0080 S22:   0.0058 S23:  -0.0043                       
REMARK   3      S31:  -0.0215 S32:  -0.0153 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 73 THROUGH 162 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -19.2676  24.9762 -16.4354              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3409 T22:   0.2701                                     
REMARK   3      T33:   0.2758 T12:   0.0093                                     
REMARK   3      T13:  -0.0214 T23:  -0.1464                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0050 L22:   0.0152                                     
REMARK   3      L33:   0.0054 L12:  -0.0060                                     
REMARK   3      L13:   0.0004 L23:  -0.0021                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0163 S12:  -0.0182 S13:  -0.0188                       
REMARK   3      S21:   0.0178 S22:   0.0093 S23:  -0.0314                       
REMARK   3      S31:  -0.0433 S32:   0.0173 S33:   0.0040                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 163 THROUGH 250 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -36.6447  20.3373 -12.1120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3590 T22:   0.4207                                     
REMARK   3      T33:   0.2948 T12:   0.0453                                     
REMARK   3      T13:  -0.0009 T23:  -0.1801                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0090 L22:   0.0096                                     
REMARK   3      L33:   0.0072 L12:  -0.0043                                     
REMARK   3      L13:  -0.0069 L23:   0.0073                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0039 S12:   0.0274 S13:  -0.0187                       
REMARK   3      S21:   0.0008 S22:  -0.0629 S23:   0.0344                       
REMARK   3      S31:  -0.0355 S32:  -0.0861 S33:   0.0009                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 251 THROUGH 341 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -25.6758  32.3502   1.3667              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4694 T22:   0.4313                                     
REMARK   3      T33:   0.3949 T12:   0.0178                                     
REMARK   3      T13:   0.0049 T23:  -0.1418                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0018 L22:   0.0053                                     
REMARK   3      L33:   0.0072 L12:  -0.0037                                     
REMARK   3      L13:  -0.0020 L23:   0.0055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0043 S12:   0.0114 S13:   0.0139                       
REMARK   3      S21:   0.0264 S22:  -0.0207 S23:  -0.0131                       
REMARK   3      S31:   0.0046 S32:  -0.0024 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 342 THROUGH 549 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -51.9755  51.1437 -15.3552              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9716 T22:   0.8566                                     
REMARK   3      T33:   0.7451 T12:   0.4006                                     
REMARK   3      T13:  -0.0760 T23:  -0.1990                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0080 L22:   0.0117                                     
REMARK   3      L33:   0.0066 L12:  -0.0104                                     
REMARK   3      L13:   0.0008 L23:   0.0040                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0278 S12:   0.0427 S13:   0.0310                       
REMARK   3      S21:  -0.0253 S22:  -0.0181 S23:   0.0224                       
REMARK   3      S31:  -0.0566 S32:  -0.0048 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 74 THROUGH 161 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4447  33.7269 -51.5599              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5670 T22:   0.5122                                     
REMARK   3      T33:   0.4611 T12:  -0.0666                                     
REMARK   3      T13:  -0.0084 T23:  -0.1227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0072 L22:   0.0042                                     
REMARK   3      L33:   0.0061 L12:  -0.0036                                     
REMARK   3      L13:  -0.0000 L23:   0.0025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0014 S12:   0.0318 S13:   0.0249                       
REMARK   3      S21:   0.0249 S22:  -0.0419 S23:   0.0125                       
REMARK   3      S31:  -0.0434 S32:  -0.0231 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 162 THROUGH 270 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.0704  47.8418  -9.4944              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8222 T22:   0.8461                                     
REMARK   3      T33:   0.7606 T12:   0.3327                                     
REMARK   3      T13:   0.0230 T23:  -0.2039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0125 L22:   0.0127                                     
REMARK   3      L33:   0.0070 L12:   0.0117                                     
REMARK   3      L13:   0.0019 L23:   0.0088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0213 S12:  -0.0112 S13:  -0.0162                       
REMARK   3      S21:  -0.0200 S22:   0.0291 S23:   0.0178                       
REMARK   3      S31:  -0.0327 S32:  -0.0158 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 25 THROUGH 48 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -23.8540  59.8318   5.4792              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6320 T22:   0.7079                                     
REMARK   3      T33:   0.7051 T12:   0.0298                                     
REMARK   3      T13:   0.1280 T23:  -0.0865                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0012 L22:   0.0005                                     
REMARK   3      L33:   0.0011 L12:  -0.0008                                     
REMARK   3      L13:  -0.0022 L23:   0.0044                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0148 S12:   0.0057 S13:  -0.0072                       
REMARK   3      S21:   0.0039 S22:  -0.0309 S23:  -0.0075                       
REMARK   3      S31:  -0.0057 S32:   0.0123 S33:  -0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 49 THROUGH 120 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -52.5226  68.6511   8.7180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6514 T22:   0.5293                                     
REMARK   3      T33:   0.6146 T12:   0.2225                                     
REMARK   3      T13:   0.1149 T23:  -0.1322                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0024 L22:   0.0033                                     
REMARK   3      L33:   0.0023 L12:  -0.0031                                     
REMARK   3      L13:   0.0007 L23:  -0.0027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0395 S12:  -0.0094 S13:   0.0240                       
REMARK   3      S21:  -0.0475 S22:  -0.0608 S23:  -0.0283                       
REMARK   3      S31:  -0.0246 S32:  -0.0376 S33:   0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 121 THROUGH 146 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -32.2297  72.6114   4.1901              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0989 T22:   1.0801                                     
REMARK   3      T33:   1.1059 T12:  -0.0534                                     
REMARK   3      T13:   0.1230 T23:  -0.0349                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0009 L22:   0.0002                                     
REMARK   3      L33:   0.0003 L12:   0.0008                                     
REMARK   3      L13:  -0.0008 L23:  -0.0004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0171 S12:   0.0054 S13:  -0.0008                       
REMARK   3      S21:  -0.0117 S22:   0.0054 S23:  -0.0133                       
REMARK   3      S31:  -0.0044 S32:  -0.0016 S33:   0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 147 THROUGH 181 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2686  61.6447   7.5557              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7616 T22:   0.7868                                     
REMARK   3      T33:   0.8530 T12:   0.0204                                     
REMARK   3      T13:   0.1761 T23:  -0.0903                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0008 L22:  -0.0000                                     
REMARK   3      L33:   0.0015 L12:  -0.0010                                     
REMARK   3      L13:  -0.0001 L23:   0.0020                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0035 S12:  -0.0091 S13:   0.0040                       
REMARK   3      S21:   0.0056 S22:  -0.0073 S23:  -0.0143                       
REMARK   3      S31:  -0.0090 S32:   0.0114 S33:  -0.0000                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 182 THROUGH 235 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -33.0420  70.8498  29.0344              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4943 T22:   0.5161                                     
REMARK   3      T33:   0.7326 T12:   0.0413                                     
REMARK   3      T13:   0.0727 T23:  -0.1334                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0022 L22:   0.0075                                     
REMARK   3      L33:   0.0018 L12:   0.0024                                     
REMARK   3      L13:   0.0027 L23:   0.0099                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0211 S12:  -0.0047 S13:   0.0102                       
REMARK   3      S21:   0.0315 S22:   0.0299 S23:   0.0119                       
REMARK   3      S31:  -0.0172 S32:   0.0237 S33:   0.0000                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 236 THROUGH 283 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.9860  61.3950  28.6072              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5309 T22:   0.6140                                     
REMARK   3      T33:   0.8033 T12:   0.0959                                     
REMARK   3      T13:   0.0235 T23:  -0.0870                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0028 L22:   0.0101                                     
REMARK   3      L33:   0.0022 L12:  -0.0065                                     
REMARK   3      L13:  -0.0019 L23:   0.0049                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0012 S12:   0.0050 S13:  -0.0202                       
REMARK   3      S21:   0.0117 S22:   0.0020 S23:  -0.0710                       
REMARK   3      S31:   0.0009 S32:  -0.0297 S33:  -0.0000                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 284 THROUGH 324 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.6744  65.1861  26.4450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7003 T22:   0.7908                                     
REMARK   3      T33:   0.9642 T12:  -0.0162                                     
REMARK   3      T13:   0.1051 T23:  -0.1589                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0021 L22:   0.0009                                     
REMARK   3      L33:   0.0002 L12:   0.0016                                     
REMARK   3      L13:   0.0009 L23:   0.0014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0001 S12:   0.0007 S13:  -0.0096                       
REMARK   3      S21:   0.0117 S22:  -0.0045 S23:  -0.0148                       
REMARK   3      S31:  -0.0053 S32:   0.0050 S33:   0.0000                       
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 6C9G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232354.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51131                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 28.30                              
REMARK 200  R MERGE                    (I) : 0.18100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.02380                            
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: 4RER                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRI-SODIUM ACETATE PH 5.6, 0.2 M   
REMARK 280  AMMONIUM ACETATE, 15% W/V PEG 4000, VAPOR DIFFUSION, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      135.34933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      270.69867            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      203.02400            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      338.37333            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       67.67467            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      135.34933            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      270.69867            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      338.37333            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      203.02400            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       67.67467            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13830 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     ASP A   282                                                      
REMARK 465     PRO A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     TYR A   285                                                      
REMARK 465     SER A   286                                                      
REMARK 465     SER A   287                                                      
REMARK 465     THR A   288                                                      
REMARK 465     MET A   289                                                      
REMARK 465     ILE A   290                                                      
REMARK 465     ASP A   291                                                      
REMARK 465     ASP A   292                                                      
REMARK 465     GLU A   293                                                      
REMARK 465     ALA A   294                                                      
REMARK 465     LEU A   295                                                      
REMARK 465     LYS A   296                                                      
REMARK 465     GLU A   297                                                      
REMARK 465     VAL A   298                                                      
REMARK 465     CYS A   299                                                      
REMARK 465     GLU A   300                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     PHE A   302                                                      
REMARK 465     GLU A   303                                                      
REMARK 465     CYS A   304                                                      
REMARK 465     SER A   305                                                      
REMARK 465     GLU A   306                                                      
REMARK 465     GLU A   307                                                      
REMARK 465     GLU A   308                                                      
REMARK 465     VAL A   309                                                      
REMARK 465     LEU A   310                                                      
REMARK 465     SER A   311                                                      
REMARK 465     CYS A   312                                                      
REMARK 465     LEU A   313                                                      
REMARK 465     TYR A   314                                                      
REMARK 465     ASN A   315                                                      
REMARK 465     ARG A   316                                                      
REMARK 465     ASN A   317                                                      
REMARK 465     HIS A   318                                                      
REMARK 465     GLN A   319                                                      
REMARK 465     ASP A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     LEU A   322                                                      
REMARK 465     ALA A   323                                                      
REMARK 465     VAL A   324                                                      
REMARK 465     ALA A   325                                                      
REMARK 465     TYR A   326                                                      
REMARK 465     HIS A   327                                                      
REMARK 465     LEU A   328                                                      
REMARK 465     ILE A   329                                                      
REMARK 465     TYR A   343                                                      
REMARK 465     LEU A   344                                                      
REMARK 465     ALA A   345                                                      
REMARK 465     THR A   346                                                      
REMARK 465     SER A   347                                                      
REMARK 465     PRO A   348                                                      
REMARK 465     PRO A   349                                                      
REMARK 465     ASP A   350                                                      
REMARK 465     SER A   351                                                      
REMARK 465     PHE A   352                                                      
REMARK 465     LEU A   353                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     ASP A   355                                                      
REMARK 465     HIS A   356                                                      
REMARK 465     HIS A   357                                                      
REMARK 465     LEU A   358                                                      
REMARK 465     THR A   359                                                      
REMARK 465     ARG A   360                                                      
REMARK 465     PRO A   361                                                      
REMARK 465     HIS A   362                                                      
REMARK 465     PRO A   363                                                      
REMARK 465     GLU A   364                                                      
REMARK 465     ARG A   365                                                      
REMARK 465     VAL A   366                                                      
REMARK 465     PRO A   367                                                      
REMARK 465     PHE A   368                                                      
REMARK 465     LEU A   369                                                      
REMARK 465     VAL A   370                                                      
REMARK 465     ALA A   371                                                      
REMARK 465     GLU A   372                                                      
REMARK 465     THR A   373                                                      
REMARK 465     PRO A   374                                                      
REMARK 465     ARG A   375                                                      
REMARK 465     ALA A   376                                                      
REMARK 465     ARG A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     THR A   379                                                      
REMARK 465     LEU A   380                                                      
REMARK 465     ASP A   381                                                      
REMARK 465     GLU A   382                                                      
REMARK 465     LEU A   383                                                      
REMARK 465     ASN A   384                                                      
REMARK 465     PRO A   385                                                      
REMARK 465     GLN A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     SER A   388                                                      
REMARK 465     LYS A   389                                                      
REMARK 465     HIS A   390                                                      
REMARK 465     GLN A   391                                                      
REMARK 465     GLY A   392                                                      
REMARK 465     VAL A   393                                                      
REMARK 465     GLN A   550                                                      
REMARK 465     MET B    67                                                      
REMARK 465     GLU B    68                                                      
REMARK 465     VAL B    69                                                      
REMARK 465     ASN B    70                                                      
REMARK 465     ASP B    71                                                      
REMARK 465     LYS B    72                                                      
REMARK 465     ALA B    73                                                      
REMARK 465     CYS B   173                                                      
REMARK 465     SER B   174                                                      
REMARK 465     ASP B   175                                                      
REMARK 465     VAL B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     GLU B   178                                                      
REMARK 465     LEU B   179                                                      
REMARK 465     SER B   180                                                      
REMARK 465     SER B   181                                                      
REMARK 465     SER B   182                                                      
REMARK 465     PRO B   183                                                      
REMARK 465     PRO B   184                                                      
REMARK 465     GLY B   185                                                      
REMARK 465     PRO B   186                                                      
REMARK 465     TYR B   187                                                      
REMARK 465     PRO B   196                                                      
REMARK 465     GLU B   197                                                      
REMARK 465     GLU B   198                                                      
REMARK 465     ARG B   199                                                      
REMARK 465     PHE B   200                                                      
REMARK 465     MET C     0                                                      
REMARK 465     GLU C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     VAL C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     ASP C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     VAL C    12                                                      
REMARK 465     GLU C    13                                                      
REMARK 465     ASN C    14                                                      
REMARK 465     GLU C    15                                                      
REMARK 465     HIS C    16                                                      
REMARK 465     PRO C    17                                                      
REMARK 465     GLN C    18                                                      
REMARK 465     GLU C    19                                                      
REMARK 465     THR C    20                                                      
REMARK 465     PRO C    21                                                      
REMARK 465     GLU C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     ASN C    24                                                      
REMARK 465     GLY C   325                                                      
REMARK 465     GLY C   326                                                      
REMARK 465     GLU C   327                                                      
REMARK 465     LYS C   328                                                      
REMARK 465     LYS C   329                                                      
REMARK 465     PRO C   330                                                      
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    LEU A  39      -60.40    -98.90                                   
REMARK 500    ARG A 140      -16.14     68.49                                   
REMARK 500    ASP A 159       77.63     60.34                                   
REMARK 500    THR A 527     -169.94    -76.98                                   
REMARK 500    HIS B 109     -115.07     51.30                                   
REMARK 500    ASN B 237       -7.82     69.70                                   
REMARK 500    LYS B 258     -118.67     53.71                                   
REMARK 500    LYS C  99      -61.22   -120.44                                   
REMARK 500    ASP C 238     -179.33   -171.58                                   
REMARK 500    ASP C 306       -1.59     76.68                                   
REMARK 500    LEU C 323      -68.49    -99.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue R93 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue STU A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP C 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP C 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP C 1103                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6C9F   RELATED DB: PDB                                   
DBREF  6C9G A   13   471  UNP    Q13131   AAPK1_HUMAN     22    480             
DBREF  6C9G A  526   550  UNP    Q13131   AAPK1_HUMAN    535    559             
DBREF  6C9G B   68   270  UNP    Q9Y478   AAKB1_HUMAN     68    270             
DBREF  6C9G C    0   330  UNP    P54619   AAKG1_HUMAN      1    331             
SEQADV 6C9G MET A    3  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9G GLY A    4  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9G HIS A    5  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9G HIS A    6  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9G HIS A    7  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9G HIS A    8  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9G HIS A    9  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9G HIS A   10  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9G GLY A   11  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9G SER A   12  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9G MET B   67  UNP  Q9Y478              INITIATING METHIONINE          
SEQADV 6C9G ASP B  108  UNP  Q9Y478    SER   108 ENGINEERED MUTATION            
SEQRES   1 A  494  MET GLY HIS HIS HIS HIS HIS HIS GLY SER VAL LYS ILE          
SEQRES   2 A  494  GLY HIS TYR ILE LEU GLY ASP THR LEU GLY VAL GLY THR          
SEQRES   3 A  494  PHE GLY LYS VAL LYS VAL GLY LYS HIS GLU LEU THR GLY          
SEQRES   4 A  494  HIS LYS VAL ALA VAL LYS ILE LEU ASN ARG GLN LYS ILE          
SEQRES   5 A  494  ARG SER LEU ASP VAL VAL GLY LYS ILE ARG ARG GLU ILE          
SEQRES   6 A  494  GLN ASN LEU LYS LEU PHE ARG HIS PRO HIS ILE ILE LYS          
SEQRES   7 A  494  LEU TYR GLN VAL ILE SER THR PRO SER ASP ILE PHE MET          
SEQRES   8 A  494  VAL MET GLU TYR VAL SER GLY GLY GLU LEU PHE ASP TYR          
SEQRES   9 A  494  ILE CYS LYS ASN GLY ARG LEU ASP GLU LYS GLU SER ARG          
SEQRES  10 A  494  ARG LEU PHE GLN GLN ILE LEU SER GLY VAL ASP TYR CYS          
SEQRES  11 A  494  HIS ARG HIS MET VAL VAL HIS ARG ASP LEU LYS PRO GLU          
SEQRES  12 A  494  ASN VAL LEU LEU ASP ALA HIS MET ASN ALA LYS ILE ALA          
SEQRES  13 A  494  ASP PHE GLY LEU SER ASN MET MET SER ASP GLY GLU PHE          
SEQRES  14 A  494  LEU ARG TPO SER CYS GLY SER PRO ASN TYR ALA ALA PRO          
SEQRES  15 A  494  GLU VAL ILE SER GLY ARG LEU TYR ALA GLY PRO GLU VAL          
SEQRES  16 A  494  ASP ILE TRP SER SER GLY VAL ILE LEU TYR ALA LEU LEU          
SEQRES  17 A  494  CYS GLY THR LEU PRO PHE ASP ASP ASP HIS VAL PRO THR          
SEQRES  18 A  494  LEU PHE LYS LYS ILE CYS ASP GLY ILE PHE TYR THR PRO          
SEQRES  19 A  494  GLN TYR LEU ASN PRO SER VAL ILE SER LEU LEU LYS HIS          
SEQRES  20 A  494  MET LEU GLN VAL ASP PRO MET LYS ARG ALA THR ILE LYS          
SEQRES  21 A  494  ASP ILE ARG GLU HIS GLU TRP PHE LYS GLN ASP LEU PRO          
SEQRES  22 A  494  LYS TYR LEU PHE PRO GLU ASP PRO SER TYR SER SER THR          
SEQRES  23 A  494  MET ILE ASP ASP GLU ALA LEU LYS GLU VAL CYS GLU LYS          
SEQRES  24 A  494  PHE GLU CYS SER GLU GLU GLU VAL LEU SER CYS LEU TYR          
SEQRES  25 A  494  ASN ARG ASN HIS GLN ASP PRO LEU ALA VAL ALA TYR HIS          
SEQRES  26 A  494  LEU ILE ILE ASP ASN ARG ARG ILE MET ASN GLU ALA LYS          
SEQRES  27 A  494  ASP PHE TYR LEU ALA THR SER PRO PRO ASP SER PHE LEU          
SEQRES  28 A  494  ASP ASP HIS HIS LEU THR ARG PRO HIS PRO GLU ARG VAL          
SEQRES  29 A  494  PRO PHE LEU VAL ALA GLU THR PRO ARG ALA ARG HIS THR          
SEQRES  30 A  494  LEU ASP GLU LEU ASN PRO GLN LYS SER LYS HIS GLN GLY          
SEQRES  31 A  494  VAL ARG LYS ALA LYS TRP HIS LEU GLY ILE ARG SER GLN          
SEQRES  32 A  494  SER ARG PRO ASN ASP ILE MET ALA GLU VAL CYS ARG ALA          
SEQRES  33 A  494  ILE LYS GLN LEU ASP TYR GLU TRP LYS VAL VAL ASN PRO          
SEQRES  34 A  494  TYR TYR LEU ARG VAL ARG ARG LYS ASN PRO VAL THR SER          
SEQRES  35 A  494  THR TYR SER LYS MET SER LEU GLN LEU TYR GLN VAL ASP          
SEQRES  36 A  494  SER ARG THR TYR LEU LEU ASP PHE ARG SER ILE ASP ASP          
SEQRES  37 A  494  GLU LEU THR PRO ARG PRO GLY SER HIS THR ILE GLU PHE          
SEQRES  38 A  494  PHE GLU MET CYS ALA ASN LEU ILE LYS ILE LEU ALA GLN          
SEQRES   1 B  204  MET GLU VAL ASN ASP LYS ALA PRO ALA GLN ALA ARG PRO          
SEQRES   2 B  204  THR VAL PHE ARG TRP THR GLY GLY GLY LYS GLU VAL TYR          
SEQRES   3 B  204  LEU SER GLY SER PHE ASN ASN TRP SER LYS LEU PRO LEU          
SEQRES   4 B  204  THR ARG ASP HIS ASN ASN PHE VAL ALA ILE LEU ASP LEU          
SEQRES   5 B  204  PRO GLU GLY GLU HIS GLN TYR LYS PHE PHE VAL ASP GLY          
SEQRES   6 B  204  GLN TRP THR HIS ASP PRO SER GLU PRO ILE VAL THR SER          
SEQRES   7 B  204  GLN LEU GLY THR VAL ASN ASN ILE ILE GLN VAL LYS LYS          
SEQRES   8 B  204  THR ASP PHE GLU VAL PHE ASP ALA LEU MET VAL ASP SER          
SEQRES   9 B  204  GLN LYS CYS SER ASP VAL SER GLU LEU SER SER SER PRO          
SEQRES  10 B  204  PRO GLY PRO TYR HIS GLN GLU PRO TYR VAL CYS LYS PRO          
SEQRES  11 B  204  GLU GLU ARG PHE ARG ALA PRO PRO ILE LEU PRO PRO HIS          
SEQRES  12 B  204  LEU LEU GLN VAL ILE LEU ASN LYS ASP THR GLY ILE SER          
SEQRES  13 B  204  CYS ASP PRO ALA LEU LEU PRO GLU PRO ASN HIS VAL MET          
SEQRES  14 B  204  LEU ASN HIS LEU TYR ALA LEU SER ILE LYS ASP GLY VAL          
SEQRES  15 B  204  MET VAL LEU SER ALA THR HIS ARG TYR LYS LYS LYS TYR          
SEQRES  16 B  204  VAL THR THR LEU LEU TYR LYS PRO ILE                          
SEQRES   1 C  331  MET GLU THR VAL ILE SER SER ASP SER SER PRO ALA VAL          
SEQRES   2 C  331  GLU ASN GLU HIS PRO GLN GLU THR PRO GLU SER ASN ASN          
SEQRES   3 C  331  SER VAL TYR THR SER PHE MET LYS SER HIS ARG CYS TYR          
SEQRES   4 C  331  ASP LEU ILE PRO THR SER SER LYS LEU VAL VAL PHE ASP          
SEQRES   5 C  331  THR SER LEU GLN VAL LYS LYS ALA PHE PHE ALA LEU VAL          
SEQRES   6 C  331  THR ASN GLY VAL ARG ALA ALA PRO LEU TRP ASP SER LYS          
SEQRES   7 C  331  LYS GLN SER PHE VAL GLY MET LEU THR ILE THR ASP PHE          
SEQRES   8 C  331  ILE ASN ILE LEU HIS ARG TYR TYR LYS SER ALA LEU VAL          
SEQRES   9 C  331  GLN ILE TYR GLU LEU GLU GLU HIS LYS ILE GLU THR TRP          
SEQRES  10 C  331  ARG GLU VAL TYR LEU GLN ASP SER PHE LYS PRO LEU VAL          
SEQRES  11 C  331  CYS ILE SER PRO ASN ALA SER LEU PHE ASP ALA VAL SER          
SEQRES  12 C  331  SER LEU ILE ARG ASN LYS ILE HIS ARG LEU PRO VAL ILE          
SEQRES  13 C  331  ASP PRO GLU SER GLY ASN THR LEU TYR ILE LEU THR HIS          
SEQRES  14 C  331  LYS ARG ILE LEU LYS PHE LEU LYS LEU PHE ILE THR GLU          
SEQRES  15 C  331  PHE PRO LYS PRO GLU PHE MET SER LYS SER LEU GLU GLU          
SEQRES  16 C  331  LEU GLN ILE GLY THR TYR ALA ASN ILE ALA MET VAL ARG          
SEQRES  17 C  331  THR THR THR PRO VAL TYR VAL ALA LEU GLY ILE PHE VAL          
SEQRES  18 C  331  GLN HIS ARG VAL SER ALA LEU PRO VAL VAL ASP GLU LYS          
SEQRES  19 C  331  GLY ARG VAL VAL ASP ILE TYR SER LYS PHE ASP VAL ILE          
SEQRES  20 C  331  ASN LEU ALA ALA GLU LYS THR TYR ASN ASN LEU ASP VAL          
SEQRES  21 C  331  SER VAL THR LYS ALA LEU GLN HIS ARG SER HIS TYR PHE          
SEQRES  22 C  331  GLU GLY VAL LEU LYS CYS TYR LEU HIS GLU THR LEU GLU          
SEQRES  23 C  331  THR ILE ILE ASN ARG LEU VAL GLU ALA GLU VAL HIS ARG          
SEQRES  24 C  331  LEU VAL VAL VAL ASP GLU ASN ASP VAL VAL LYS GLY ILE          
SEQRES  25 C  331  VAL SER LEU SER ASP ILE LEU GLN ALA LEU VAL LEU THR          
SEQRES  26 C  331  GLY GLY GLU LYS LYS PRO                                      
MODRES 6C9G TPO A  174  THR  MODIFIED RESIDUE                                   
HET    TPO  A 174      11                                                       
HET    R93  A 601      35                                                       
HET    STU  A 602      35                                                       
HET    AMP  C1101      23                                                       
HET    AMP  C1102      23                                                       
HET    AMP  C1103      23                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     R93 5-{[6-CHLORO-5-(2'-HYDROXY[1,1'-BIPHENYL]-4-YL)-1H-              
HETNAM   2 R93  BENZIMIDAZOL-2-YL]OXY}-N-HYDROXY-2-METHYLBENZAMIDE              
HETNAM     STU STAUROSPORINE                                                    
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   4  R93    C27 H20 CL N3 O4                                             
FORMUL   5  STU    C28 H26 N4 O3                                                
FORMUL   6  AMP    3(C10 H14 N5 O7 P)                                           
FORMUL   9  HOH   *52(H2 O)                                                     
HELIX    1 AA1 ARG A   51  LEU A   57  1                                   7    
HELIX    2 AA2 VAL A   59  PHE A   73  1                                  15    
HELIX    3 AA3 LEU A  103  GLY A  111  1                                   9    
HELIX    4 AA4 ASP A  114  HIS A  135  1                                  22    
HELIX    5 AA5 ASP A  159  SER A  163  5                                   5    
HELIX    6 AA6 SER A  178  ALA A  182  5                                   5    
HELIX    7 AA7 ALA A  183  SER A  188  1                                   6    
HELIX    8 AA8 GLY A  194  GLY A  212  1                                  19    
HELIX    9 AA9 HIS A  220  GLY A  231  1                                  12    
HELIX   10 AB1 ASN A  240  LEU A  251  1                                  12    
HELIX   11 AB2 THR A  260  HIS A  267  1                                   8    
HELIX   12 AB3 HIS A  267  GLN A  272  1                                   6    
HELIX   13 AB4 PRO A  275  PHE A  279  5                                   5    
HELIX   14 AB5 ASP A  331  PHE A  342  1                                  12    
HELIX   15 AB6 ARG A  407  LEU A  422  1                                  16    
HELIX   16 AB7 SER A  532  ALA A  549  1                                  18    
HELIX   17 AB8 PHE B   97  ASN B   99  5                                   3    
HELIX   18 AB9 LYS B  156  PHE B  160  5                                   5    
HELIX   19 AC1 GLU B  161  LYS B  172  1                                  12    
HELIX   20 AC2 PRO B  207  GLN B  212  5                                   6    
HELIX   21 AC3 ASN B  232  LEU B  236  5                                   5    
HELIX   22 AC4 SER C   26  HIS C   35  1                                  10    
HELIX   23 AC5 ARG C   36  LEU C   40  5                                   5    
HELIX   24 AC6 GLN C   55  ASN C   66  1                                  12    
HELIX   25 AC7 THR C   86  TYR C   98  1                                  13    
HELIX   26 AC8 ILE C  105  HIS C  111  1                                   7    
HELIX   27 AC9 LYS C  112  LEU C  121  1                                  10    
HELIX   28 AD1 SER C  136  ASN C  147  1                                  12    
HELIX   29 AD2 THR C  167  PHE C  182  1                                  16    
HELIX   30 AD3 PRO C  185  LYS C  190  1                                   6    
HELIX   31 AD4 SER C  191  GLN C  196  1                                   6    
HELIX   32 AD5 PRO C  211  ARG C  223  1                                  13    
HELIX   33 AD6 LYS C  242  GLU C  251  1                                  10    
HELIX   34 AD7 SER C  260  GLN C  266  1                                   7    
HELIX   35 AD8 THR C  283  GLU C  295  1                                  13    
HELIX   36 AD9 LEU C  314  THR C  324  1                                  11    
SHEET    1 AA1 6 LYS A  14  ILE A  15  0                                        
SHEET    2 AA1 6 TYR A  18  GLY A  25 -1  O  TYR A  18   N  ILE A  15           
SHEET    3 AA1 6 VAL A  32  HIS A  37 -1  O  LYS A  36   N  ILE A  19           
SHEET    4 AA1 6 LYS A  43  ASN A  50 -1  O  VAL A  46   N  LYS A  33           
SHEET    5 AA1 6 ASP A  90  GLU A  96 -1  O  ILE A  91   N  LEU A  49           
SHEET    6 AA1 6 LEU A  81  SER A  86 -1  N  ILE A  85   O  PHE A  92           
SHEET    1 AA2 3 GLY A 101  GLU A 102  0                                        
SHEET    2 AA2 3 VAL A 147  LEU A 149 -1  O  LEU A 149   N  GLY A 101           
SHEET    3 AA2 3 ALA A 155  ILE A 157 -1  O  LYS A 156   N  LEU A 148           
SHEET    1 AA3 2 VAL A 137  VAL A 138  0                                        
SHEET    2 AA3 2 ASN A 164  MET A 165 -1  O  ASN A 164   N  VAL A 138           
SHEET    1 AA4 7 HIS A 399  LEU A 400  0                                        
SHEET    2 AA4 7 TYR B 240  LYS B 245 -1  O  ALA B 241   N  HIS A 399           
SHEET    3 AA4 7 VAL B 248  TYR B 257 -1  O  SER B 252   N  TYR B 240           
SHEET    4 AA4 7 LYS B 260  PRO B 269 -1  O  LYS B 260   N  TYR B 257           
SHEET    5 AA4 7 SER C  44  ASP C  51  1  O  LEU C  47   N  LEU B 265           
SHEET    6 AA4 7 ALA C  71  ASP C  75  1  O  TRP C  74   N  PHE C  50           
SHEET    7 AA4 7 SER C  80  LEU C  85 -1  O  GLY C  83   N  LEU C  73           
SHEET    1 AA5 5 ILE A 402  SER A 404  0                                        
SHEET    2 AA5 5 TYR A 461  SER A 467 -1  O  LEU A 463   N  ILE A 402           
SHEET    3 AA5 5 TYR A 446  GLN A 455 -1  N  TYR A 454   O  LEU A 462           
SHEET    4 AA5 5 TYR A 433  LYS A 439 -1  N  LEU A 434   O  LEU A 451           
SHEET    5 AA5 5 GLU A 425  ASN A 430 -1  N  GLU A 425   O  ARG A 437           
SHEET    1 AA6 3 PRO B  79  THR B  85  0                                        
SHEET    2 AA6 3 ASN B 111  ASP B 117 -1  O  ALA B 114   N  PHE B  82           
SHEET    3 AA6 3 THR B 106  ASP B 108 -1  N  ASP B 108   O  ASN B 111           
SHEET    1 AA7 4 LEU B 103  PRO B 104  0                                        
SHEET    2 AA7 4 VAL B  91  GLY B  95 -1  N  LEU B  93   O  LEU B 103           
SHEET    3 AA7 4 GLY B 121  VAL B 129 -1  O  LYS B 126   N  SER B  94           
SHEET    4 AA7 4 GLN B 132  THR B 134 -1  O  THR B 134   N  PHE B 127           
SHEET    1 AA8 5 LEU B 103  PRO B 104  0                                        
SHEET    2 AA8 5 VAL B  91  GLY B  95 -1  N  LEU B  93   O  LEU B 103           
SHEET    3 AA8 5 GLY B 121  VAL B 129 -1  O  LYS B 126   N  SER B  94           
SHEET    4 AA8 5 VAL B 149  VAL B 155 -1  O  ASN B 151   N  TYR B 125           
SHEET    5 AA8 5 ILE B 141  THR B 143 -1  N  VAL B 142   O  ASN B 150           
SHEET    1 AA9 2 LEU C 152  ILE C 155  0                                        
SHEET    2 AA9 2 THR C 162  LEU C 166 -1  O  TYR C 164   N  VAL C 154           
SHEET    1 AB1 3 VAL C 206  ARG C 207  0                                        
SHEET    2 AB1 3 ALA C 226  VAL C 230  1  O  VAL C 230   N  VAL C 206           
SHEET    3 AB1 3 VAL C 236  SER C 241 -1  O  TYR C 240   N  LEU C 227           
SHEET    1 AB2 3 LYS C 277  CYS C 278  0                                        
SHEET    2 AB2 3 ARG C 298  VAL C 302  1  O  VAL C 302   N  CYS C 278           
SHEET    3 AB2 3 VAL C 308  SER C 313 -1  O  VAL C 312   N  LEU C 299           
LINK         C   ARG A 173                 N   TPO A 174     1555   1555  1.33  
LINK         C   TPO A 174                 N   SER A 175     1555   1555  1.33  
SITE     1 AC1 14 VAL A  13  LEU A  20  GLY A  21  VAL A  26                    
SITE     2 AC1 14 GLY A  30  LYS A  31  LYS A  33  ASN A  50                    
SITE     3 AC1 14 ASP A  90  ARG B  83  THR B 106  ARG B 107                    
SITE     4 AC1 14 ASP B 108  VAL B 113                                          
SITE     1 AC2 16 LEU A  24  GLY A  25  VAL A  26  VAL A  32                    
SITE     2 AC2 16 ALA A  45  LYS A  47  MET A  95  GLU A  96                    
SITE     3 AC2 16 TYR A  97  VAL A  98  GLY A 101  GLU A 102                    
SITE     4 AC2 16 GLU A 145  ASN A 146  LEU A 148  ASP A 159                    
SITE     1 AC3 11 MET C  84  THR C  86  THR C  88  ASP C  89                    
SITE     2 AC3 11 PRO C 127  LEU C 128  VAL C 129  ILE C 149                    
SITE     3 AC3 11 HIS C 150  ARG C 151  PRO C 153                               
SITE     1 AC4 11 ARG C  69  ILE C 239  SER C 241  PHE C 243                    
SITE     2 AC4 11 ASP C 244  ARG C 268  VAL C 275  LEU C 276                    
SITE     3 AC4 11 VAL C 296  HIS C 297  ARG C 298                               
SITE     1 AC5 12 HIS C 150  THR C 199  ASN C 202  ILE C 203                    
SITE     2 AC5 12 ALA C 204  VAL C 224  SER C 225  ALA C 226                    
SITE     3 AC5 12 HIS C 297  SER C 313  SER C 315  ASP C 316                    
CRYST1  122.986  122.986  406.048  90.00  90.00 120.00 P 61 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008131  0.004694  0.000000        0.00000                         
SCALE2      0.000000  0.009389  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002463        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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