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Database: PDB
Entry: 5T5G
LinkDB: 5T5G
Original site: 5T5G 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       30-AUG-16   5T5G              
TITLE     HUMAN SETD8 IN COMPLEX WITH MS2177                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE KMT5A;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 234-380;                                      
COMPND   5 SYNONYM: H4-K20-HMTASE KMT5A,HISTONE-LYSINE N-METHYLTRANSFERASE      
COMPND   6 KMT5A,LYSINE N-METHYLTRANSFERASE 5A,LYSINE-SPECIFIC METHYLASE 5A,    
COMPND   7 PR/SET DOMAIN-CONTAINING PROTEIN 07,PR/SET07,SET DOMAIN-CONTAINING   
COMPND   8 PROTEIN 8;                                                           
COMPND   9 EC: 2.1.1.-,2.1.1.43;                                                
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KMT5A, PRSET7, SET07, SET8, SETD8;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-V2R-PRARE2;                           
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28MHL                                  
KEYWDS    STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,             
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.YU,W.TEMPEL,N.BABAULT,A.MA,K.V.BUTLER,J.JIN,C.H.ARROWSMITH,         
AUTHOR   2 C.BOUNTRA,A.M.EDWARDS,P.J.BROWN,STRUCTURAL GENOMICS CONSORTIUM (SGC) 
REVDAT   4   23-MAY-18 5T5G    1       JRNL                                     
REVDAT   3   22-NOV-17 5T5G    1       REMARK                                   
REVDAT   2   26-OCT-16 5T5G    1       REMARK                                   
REVDAT   1   28-SEP-16 5T5G    0                                                
JRNL        AUTH   K.V.BUTLER,A.MA,W.YU,F.LI,W.TEMPEL,N.BABAULT,                
JRNL        AUTH 2 F.PITTELLA-SILVA,J.SHAO,J.WANG,M.LUO,M.VEDADI,P.J.BROWN,     
JRNL        AUTH 3 C.H.ARROWSMITH,J.JIN                                         
JRNL        TITL   STRUCTURE-BASED DESIGN OF A COVALENT INHIBITOR OF THE SET    
JRNL        TITL 2 DOMAIN-CONTAINING PROTEIN 8 (SETD8) LYSINE                   
JRNL        TITL 3 METHYLTRANSFERASE.                                           
JRNL        REF    J. MED. CHEM.                 V.  59  9881 2016              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   27804297                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B01244                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0151                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 8998                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 519                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 654                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 34                           
REMARK   3   BIN FREE R VALUE                    : 0.2930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1072                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 19                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.78000                                              
REMARK   3    B22 (A**2) : 0.78000                                              
REMARK   3    B33 (A**2) : -2.54000                                             
REMARK   3    B12 (A**2) : 0.39000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.223         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.174         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.145         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.702        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1141 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1047 ; 0.002 ; 0.019       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1542 ; 1.485 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2396 ; 0.917 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   143 ; 6.390 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    50 ;30.465 ;23.600       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   170 ;12.832 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;14.145 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   166 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1364 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   256 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   575 ; 2.096 ; 3.473       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   574 ; 2.057 ; 3.471       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   717 ; 3.053 ; 5.201       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   235        A   377                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.7135  47.0093   4.4023              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0175 T22:   0.1253                                     
REMARK   3      T33:   0.0429 T12:  -0.0069                                     
REMARK   3      T13:   0.0134 T23:   0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9342 L22:   1.4929                                     
REMARK   3      L33:   3.4439 L12:  -0.9213                                     
REMARK   3      L13:  -0.8274 L23:   0.0538                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1014 S12:  -0.2657 S13:  -0.3861                       
REMARK   3      S21:   0.0949 S22:   0.0381 S23:   0.1946                       
REMARK   3      S31:   0.0421 S32:  -0.5602 S33:   0.0634                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: REFINED USING COOT, REFMAC, MOLPROBITY    
REMARK   3  AND RESTRAINTS FROM PRODRG AND GRADE.                               
REMARK   4                                                                      
REMARK   4 5T5G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221215.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5-7.3                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.25, XDS                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9530                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 10.70                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.98500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
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: 4IJ8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG-2000-MME, 0.1 M POSTASSIUM       
REMARK 280  THIOCYANATE, 0.1 M BIS-TRIS, VAPOR DIFFUSION, TEMPERATURE 291K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
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   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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       23.32600            
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       11.66300            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       11.66300            
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       23.32600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     GLY A   233                                                      
REMARK 465     LYS A   234                                                      
REMARK 465     GLY A   378                                                      
REMARK 465     ASP A   379                                                      
REMARK 465     ARG A   380                                                      
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     SER A 235    OG                                                  
REMARK 470     LYS A 236    CG   CD   CE   NZ                                   
REMARK 470     GLU A 238    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 239    CG   CD1  CD2                                       
REMARK 470     GLN A 240    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 242    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 244    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 245    CG   CD   CE   NZ                                   
REMARK 470     GLU A 249    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 252    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 255    CD   CE   NZ                                        
REMARK 470     LYS A 267    CG   CD   CE   NZ                                   
REMARK 470     GLU A 292    CD   OE1  OE2                                       
REMARK 470     ILE A 293    CG1  CG2  CD1                                       
REMARK 470     LYS A 298    CG   CD   CE   NZ                                   
REMARK 470     ASP A 306    CG   OD1  OD2                                       
REMARK 470     SER A 308    OG                                                  
REMARK 470     SER A 320    OG                                                  
REMARK 470     LYS A 321    CG   CD   CE   NZ                                   
REMARK 470     LYS A 342    CG   CD   CE   NZ                                   
REMARK 470     VAL A 356    CG1  CG2                                            
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    VAL A 283      -60.59   -108.07                                   
REMARK 500    LEU A 319     -129.19     54.71                                   
REMARK 500    SER A 343       62.32   -117.94                                   
REMARK 500    ASP A 354       62.24     30.24                                   
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 75P A 407                 
DBREF  5T5G A  234   380  UNP    Q9NQR1   KMT5A_HUMAN    234    380             
SEQADV 5T5G GLY A  233  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 5T5G SER A  343  UNP  Q9NQR1    CYS   343 ENGINEERED MUTATION            
SEQRES   1 A  148  GLY LYS SER LYS ALA GLU LEU GLN SER GLU GLU ARG LYS          
SEQRES   2 A  148  ARG ILE ASP GLU LEU ILE GLU SER GLY LYS GLU GLU GLY          
SEQRES   3 A  148  MET LYS ILE ASP LEU ILE ASP GLY LYS GLY ARG GLY VAL          
SEQRES   4 A  148  ILE ALA THR LYS GLN PHE SER ARG GLY ASP PHE VAL VAL          
SEQRES   5 A  148  GLU TYR HIS GLY ASP LEU ILE GLU ILE THR ASP ALA LYS          
SEQRES   6 A  148  LYS ARG GLU ALA LEU TYR ALA GLN ASP PRO SER THR GLY          
SEQRES   7 A  148  CYS TYR MET TYR TYR PHE GLN TYR LEU SER LYS THR TYR          
SEQRES   8 A  148  CYS VAL ASP ALA THR ARG GLU THR ASN ARG LEU GLY ARG          
SEQRES   9 A  148  LEU ILE ASN HIS SER LYS SER GLY ASN CYS GLN THR LYS          
SEQRES  10 A  148  LEU HIS ASP ILE ASP GLY VAL PRO HIS LEU ILE LEU ILE          
SEQRES  11 A  148  ALA SER ARG ASP ILE ALA ALA GLY GLU GLU LEU LEU TYR          
SEQRES  12 A  148  ASP TYR GLY ASP ARG                                          
HET    UNX  A 401       1                                                       
HET    UNX  A 402       1                                                       
HET    UNX  A 403       1                                                       
HET    UNX  A 404       1                                                       
HET    UNX  A 405       1                                                       
HET    UNX  A 406       1                                                       
HET    75P  A 407      43                                                       
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM     75P 7-(2-AMINOETHOXY)-6-METHOXY-2-(PYRROLIDIN-1-YL)-N-[5-            
HETNAM   2 75P  (PYRROLIDIN-1-YL)PENTYL]QUINAZOLIN-4-AMINE                      
FORMUL   2  UNX    6(X)                                                         
FORMUL   8  75P    C24 H38 N6 O2                                                
FORMUL   9  HOH   *19(H2 O)                                                     
HELIX    1 AA1 SER A  235  GLY A  254  1                                  20    
HELIX    2 AA2 ILE A  293  ALA A  304  1                                  12    
HELIX    3 AA3 LEU A  334  ILE A  338  5                                   5    
SHEET    1 AA1 2 MET A 259  ILE A 264  0                                        
SHEET    2 AA1 2 LYS A 267  ALA A 273 -1  O  ILE A 272   N  LYS A 260           
SHEET    1 AA2 5 PHE A 282  GLU A 285  0                                        
SHEET    2 AA2 5 VAL A 356  ALA A 363 -1  O  LEU A 361   N  VAL A 284           
SHEET    3 AA2 5 CYS A 346  ILE A 353 -1  N  HIS A 351   O  HIS A 358           
SHEET    4 AA2 5 LEU A 374  ASP A 376  1  O  LEU A 374   N  CYS A 346           
SHEET    5 AA2 5 ASN A 339  HIS A 340  1  N  ASN A 339   O  TYR A 375           
SHEET    1 AA3 3 ASP A 289  GLU A 292  0                                        
SHEET    2 AA3 3 LYS A 321  ASP A 326 -1  O  ASP A 326   N  ASP A 289           
SHEET    3 AA3 3 MET A 313  TYR A 318 -1  N  TYR A 318   O  LYS A 321           
SSBOND   1 CYS A  311    CYS A  311                          1555   4555  2.42  
SITE     1 AC1 16 TYR A 286  GLU A 300  TYR A 303  THR A 309                    
SITE     2 AC1 16 GLY A 310  CYS A 311  TYR A 312  MET A 313                    
SITE     3 AC1 16 ARG A 336  LEU A 337  ILE A 338  ASN A 339                    
SITE     4 AC1 16 LEU A 359  TYR A 375  TYR A 377  HOH A 510                    
CRYST1   88.957   88.957   34.989  90.00  90.00 120.00 P 32 2 1      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      0.011241  0.006490  0.000000        0.00000                         
SCALE2      0.000000  0.012980  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.028580        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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