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Database: PDB
Entry: 5N5M
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Original site: 5N5M 
HEADER    TRANSFERASE                             14-FEB-17   5N5M              
TITLE     CRYSTAL STRUCTURE OF HUMAN PIM-1 KINASE IN COMPLEX WITH A             
TITLE    2 CONSENSUSPEPTIDE AND (R)-3-(2-((ISOQUINOLIN-5-YLMETHYL)(METHYL)      
TITLE    3 CARBAMOYL)PHENYL)PYRROLIDIN-1-IUM                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PIM-1;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.11.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 OTHER_DETAILS: ISOFROM 2 OF PIM-1 KINASE;                            
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PIMTIDE;                                                   
COMPND  10 CHAIN: B;                                                            
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 OTHER_DETAILS: PIM-1 CONSENSUS PEPTIDE                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PIM1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: PLYSS;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PLIC-SGC;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606                                                 
KEYWDS    SERINE THREONINE KINASE, TRANSFERASE, PROTO-ONCOGENE, FRAGMENT, PIM-  
KEYWDS   2 1, CONSENSUS PEPTIDE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.SIEFKER,A.HEINE,G.KLEBE                                             
REVDAT   3   17-JAN-24 5N5M    1       REMARK                                   
REVDAT   2   14-AUG-19 5N5M    1       REMARK                                   
REVDAT   1   07-MAR-18 5N5M    0                                                
JRNL        AUTH   C.SIEFKER,A.HEINE,C.TAYLOR,P.KOLB,K.HARDES,A.STEINMETZER,    
JRNL        AUTH 2 G.KLEBE                                                      
JRNL        TITL   A CRYSTALLOGRAPHIC FRAGMENT STUDY WITH HUMAN PIM-1 KINASE    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.21 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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) : 2.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.30                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22230                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1112                            
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 49.3147 -  4.4244    1.00     2689   142  0.1669 0.2099        
REMARK   3     2  4.4244 -  3.5121    1.00     2649   140  0.1482 0.1828        
REMARK   3     3  3.5121 -  3.0682    1.00     2637   138  0.1594 0.1947        
REMARK   3     4  3.0682 -  2.7877    1.00     2636   139  0.1625 0.1994        
REMARK   3     5  2.7877 -  2.5879    1.00     2620   138  0.1726 0.2118        
REMARK   3     6  2.5879 -  2.4353    1.00     2629   138  0.1730 0.2023        
REMARK   3     7  2.4353 -  2.3134    1.00     2626   139  0.1944 0.2701        
REMARK   3     8  2.3134 -  2.2127    1.00     2632   138  0.2140 0.2515        
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)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.400           
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      :  0.008           2352                                  
REMARK   3   ANGLE     :  0.763           3196                                  
REMARK   3   CHIRALITY :  0.051            338                                  
REMARK   3   PLANARITY :  0.005            438                                  
REMARK   3   DIHEDRAL  : 19.820           1395                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 33 THROUGH 96 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -86.4405  88.3425 -11.2022              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4123 T22:   0.2925                                     
REMARK   3      T33:   0.3770 T12:   0.0397                                     
REMARK   3      T13:   0.0623 T23:  -0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2284 L22:   0.4028                                     
REMARK   3      L33:   0.2452 L12:   0.2636                                     
REMARK   3      L13:  -0.0159 L23:  -0.0524                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0220 S12:  -0.0393 S13:   0.2565                       
REMARK   3      S21:  -0.1645 S22:   0.0563 S23:  -0.0034                       
REMARK   3      S31:  -0.2387 S32:   0.0756 S33:   0.0001                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 140 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -92.6579  81.9271  -6.1215              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3168 T22:   0.1836                                     
REMARK   3      T33:   0.2449 T12:   0.0313                                     
REMARK   3      T13:   0.0397 T23:  -0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3007 L22:   0.6895                                     
REMARK   3      L33:   0.9064 L12:   0.0231                                     
REMARK   3      L13:   0.5244 L23:   0.0475                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0188 S12:  -0.0227 S13:   0.2478                       
REMARK   3      S21:   0.0262 S22:   0.1693 S23:   0.2316                       
REMARK   3      S31:  -0.2950 S32:  -0.2356 S33:   0.2086                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 141 THROUGH 305 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -88.9326  63.9215  -2.2331              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1850 T22:   0.1795                                     
REMARK   3      T33:   0.1912 T12:   0.0217                                     
REMARK   3      T13:  -0.0131 T23:  -0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7156 L22:   0.8482                                     
REMARK   3      L33:   1.6524 L12:   0.0191                                     
REMARK   3      L13:  -0.4176 L23:  -0.0300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0690 S12:  -0.0762 S13:  -0.0176                       
REMARK   3      S21:   0.0109 S22:  -0.0496 S23:  -0.0255                       
REMARK   3      S31:   0.0769 S32:   0.0349 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 10 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -84.7211  74.1284   9.6829              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4510 T22:   0.4007                                     
REMARK   3      T33:   0.3483 T12:  -0.0677                                     
REMARK   3      T13:   0.0142 T23:  -0.1432                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1267 L22:   0.1781                                     
REMARK   3      L33:   0.0527 L12:  -0.0063                                     
REMARK   3      L13:   0.0787 L23:   0.0238                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1228 S12:  -0.2786 S13:   0.1047                       
REMARK   3      S21:  -0.0308 S22:   0.2152 S23:  -0.3055                       
REMARK   3      S31:  -0.0378 S32:   0.1229 S33:   0.0626                       
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 5N5M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003387.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-SEP-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.2                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873                              
REMARK 200  MONOCHROMATOR                  : SI-111 CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : SILICON                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22235                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.210                              
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                : 6.930                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.98                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.210                              
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: 3WE8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: HEXAGONAL ROD                                                
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES MGCL2 GLYCEROL DTT BIS-TRIS        
REMARK 280  -PROPANE PEG3350 ETHYLENE-GLYCOL DMSO, PH 7.0, VAPOR DIFFUSION,     
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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       53.51133            
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       26.75567            
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       40.13350            
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       13.37783            
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       66.88917            
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: 1160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     HIS A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     CYS A    17                                                      
REMARK 465     ASN A    18                                                      
REMARK 465     ASP A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     HIS A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     LYS A    24                                                      
REMARK 465     LEU A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     GLY A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     SER A   306                                                      
REMARK 465     LEU A   307                                                      
REMARK 465     SER A   308                                                      
REMARK 465     PRO A   309                                                      
REMARK 465     GLY A   310                                                      
REMARK 465     PRO A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     LYS A   313                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     PRO B    11                                                      
REMARK 465     PRO B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PRO A  33    CG   CD                                             
REMARK 470     LEU A  34    CD1  CD2                                            
REMARK 470     GLU A  35    CG   CD   OE1  OE2                                  
REMARK 470     SER A  36    OG                                                  
REMARK 470     GLN A  39    CD   OE1  NE2                                       
REMARK 470     VAL A  58    CG1  CG2                                            
REMARK 470     SER A  59    OG                                                  
REMARK 470     ARG A  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A  74    CD1                                                 
REMARK 470     SER A  75    OG                                                  
REMARK 470     ASP A  76    OD1  OD2                                            
REMARK 470     GLU A  79    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  80    CG   CD1  CD2                                       
REMARK 470     PRO A  81    CG   CD                                             
REMARK 470     ASN A  82    OD1  ND2                                            
REMARK 470     THR A  84    OG1  CG2                                            
REMARK 470     ARG A  85    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  94    CD   CE   NZ                                        
REMARK 470     SER A  98    OG                                                  
REMARK 470     PHE A 100    CD1  CE1  CZ                                        
REMARK 470     ARG A 105    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 183    NZ                                                  
REMARK 470     ASP A 202    OD1  OD2                                            
REMARK 470     GLN A 252    OE1  NE2                                            
REMARK 470     ARG A 274    CZ   NH1  NH2                                       
REMARK 470     GLN A 297    OE1  NE2                                            
REMARK 470     LYS B   3    CD   CE   NZ                                        
REMARK 470     HIS B   7    O                                                   
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  60       17.60   -141.48                                   
REMARK 500    SER A 101     -178.46   -170.43                                   
REMARK 500    ASP A 167       46.07   -146.02                                   
REMARK 500    ASP A 186       81.96     60.49                                   
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 8O8 A 401                 
DBREF  5N5M A    1   313  UNP    P11309   PIM1_HUMAN       1    313             
DBREF  5N5M B    1    14  PDB    5N5M     5N5M             1     14             
SEQADV 5N5M GLY A  250  UNP  P11309    ARG   250 ENGINEERED MUTATION            
SEQRES   1 A  313  MET LEU LEU SER LYS ILE ASN SER LEU ALA HIS LEU ARG          
SEQRES   2 A  313  ALA ALA PRO CYS ASN ASP LEU HIS ALA THR LYS LEU ALA          
SEQRES   3 A  313  PRO GLY LYS GLU LYS GLU PRO LEU GLU SER GLN TYR GLN          
SEQRES   4 A  313  VAL GLY PRO LEU LEU GLY SER GLY GLY PHE GLY SER VAL          
SEQRES   5 A  313  TYR SER GLY ILE ARG VAL SER ASP ASN LEU PRO VAL ALA          
SEQRES   6 A  313  ILE LYS HIS VAL GLU LYS ASP ARG ILE SER ASP TRP GLY          
SEQRES   7 A  313  GLU LEU PRO ASN GLY THR ARG VAL PRO MET GLU VAL VAL          
SEQRES   8 A  313  LEU LEU LYS LYS VAL SER SER GLY PHE SER GLY VAL ILE          
SEQRES   9 A  313  ARG LEU LEU ASP TRP PHE GLU ARG PRO ASP SER PHE VAL          
SEQRES  10 A  313  LEU ILE LEU GLU ARG PRO GLU PRO VAL GLN ASP LEU PHE          
SEQRES  11 A  313  ASP PHE ILE THR GLU ARG GLY ALA LEU GLN GLU GLU LEU          
SEQRES  12 A  313  ALA ARG SER PHE PHE TRP GLN VAL LEU GLU ALA VAL ARG          
SEQRES  13 A  313  HIS CYS HIS ASN CYS GLY VAL LEU HIS ARG ASP ILE LYS          
SEQRES  14 A  313  ASP GLU ASN ILE LEU ILE ASP LEU ASN ARG GLY GLU LEU          
SEQRES  15 A  313  LYS LEU ILE ASP PHE GLY SER GLY ALA LEU LEU LYS ASP          
SEQRES  16 A  313  THR VAL TYR THR ASP PHE ASP GLY THR ARG VAL TYR SER          
SEQRES  17 A  313  PRO PRO GLU TRP ILE ARG TYR HIS ARG TYR HIS GLY ARG          
SEQRES  18 A  313  SER ALA ALA VAL TRP SER LEU GLY ILE LEU LEU TYR ASP          
SEQRES  19 A  313  MET VAL CYS GLY ASP ILE PRO PHE GLU HIS ASP GLU GLU          
SEQRES  20 A  313  ILE ILE GLY GLY GLN VAL PHE PHE ARG GLN ARG VAL SER          
SEQRES  21 A  313  SEP GLU CYS GLN HIS LEU ILE ARG TRP CYS LEU ALA LEU          
SEQRES  22 A  313  ARG PRO SER ASP ARG PRO THR PHE GLU GLU ILE GLN ASN          
SEQRES  23 A  313  HIS PRO TRP MET GLN ASP VAL LEU LEU PRO GLN GLU THR          
SEQRES  24 A  313  ALA GLU ILE HIS LEU HIS SER LEU SER PRO GLY PRO SER          
SEQRES  25 A  313  LYS                                                          
SEQRES   1 B   14  ALA ARG LYS ARG ARG ARG HIS PRO SER GLY PRO PRO THR          
SEQRES   2 B   14  ALA                                                          
MODRES 5N5M SEP A  261  SER  MODIFIED RESIDUE                                   
HET    SEP  A 261      10                                                       
HET    8O8  A 401      26                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     8O8 ~{N}-(ISOQUINOLIN-5-YLMETHYL)-~{N}-METHYL-2-[(3~{R})-            
HETNAM   2 8O8  PYRROLIDIN-3-YL]BENZAMIDE                                       
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3  8O8    C22 H23 N3 O                                                 
FORMUL   4  HOH   *135(H2 O)                                                    
HELIX    1 AA1 PRO A   33  GLN A   37  1                                   5    
HELIX    2 AA2 ASP A   72  ILE A   74  5                                   3    
HELIX    3 AA3 MET A   88  SER A   97  1                                  10    
HELIX    4 AA4 LEU A  129  GLY A  137  1                                   9    
HELIX    5 AA5 GLN A  140  CYS A  161  1                                  22    
HELIX    6 AA6 LYS A  169  GLU A  171  5                                   3    
HELIX    7 AA7 THR A  204  SER A  208  5                                   5    
HELIX    8 AA8 PRO A  209  HIS A  216  1                                   8    
HELIX    9 AA9 HIS A  219  GLY A  238  1                                  20    
HELIX   10 AB1 HIS A  244  GLY A  251  1                                   8    
HELIX   11 AB2 SER A  260  LEU A  271  1                                  12    
HELIX   12 AB3 ARG A  274  ARG A  278  5                                   5    
HELIX   13 AB4 THR A  280  ASN A  286  1                                   7    
HELIX   14 AB5 HIS A  287  GLN A  291  5                                   5    
HELIX   15 AB6 LEU A  295  LEU A  304  1                                  10    
SHEET    1 AA1 5 TYR A  38  GLY A  47  0                                        
SHEET    2 AA1 5 GLY A  50  ARG A  57 -1  O  VAL A  52   N  LEU A  44           
SHEET    3 AA1 5 PRO A  63  GLU A  70 -1  O  ILE A  66   N  TYR A  53           
SHEET    4 AA1 5 SER A 115  GLU A 121 -1  O  LEU A 120   N  ALA A  65           
SHEET    5 AA1 5 LEU A 106  GLU A 111 -1  N  LEU A 107   O  ILE A 119           
SHEET    1 AA2 2 TRP A  77  GLU A  79  0                                        
SHEET    2 AA2 2 ARG A  85  PRO A  87 -1  O  VAL A  86   N  GLY A  78           
SHEET    1 AA3 3 VAL A 126  ASP A 128  0                                        
SHEET    2 AA3 3 ILE A 173  ASP A 176 -1  O  ILE A 175   N  GLN A 127           
SHEET    3 AA3 3 GLU A 181  LEU A 184 -1  O  GLU A 181   N  ASP A 176           
SHEET    1 AA4 2 VAL A 163  LEU A 164  0                                        
SHEET    2 AA4 2 ALA A 191  LEU A 192 -1  O  ALA A 191   N  LEU A 164           
LINK         C   SER A 260                 N   SEP A 261     1555   1555  1.33  
LINK         C   SEP A 261                 N  AGLU A 262     1555   1555  1.33  
LINK         C   SEP A 261                 N  BGLU A 262     1555   1555  1.33  
CISPEP   1 GLU A  124    PRO A  125          0        -0.12                     
SITE     1 AC1 10 GLY A  45  PHE A  49  ALA A  65  GLU A 121                    
SITE     2 AC1 10 ARG A 122  GLU A 171  ASN A 172  LEU A 174                    
SITE     3 AC1 10 ASP A 186  HOH A 550                                          
CRYST1   98.605   98.605   80.267  90.00  90.00 120.00 P 65          6          
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      0.010141  0.005855  0.000000        0.00000                         
SCALE2      0.000000  0.011710  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012458        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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