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Database: PDB
Entry: 3U85
LinkDB: 3U85
Original site: 3U85 
HEADER    TRANSCRIPTION                           15-OCT-11   3U85              
TITLE     CRYSTAL STRUCTURE OF HUMAN MENIN IN COMPLEX WITH MLL1                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MENIN;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE 2A;                     
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: LYSINE N-METHYLTRANSFERASE 2A,ALL-1,CXXC-TYPE ZINC FINGER   
COMPND   9 PROTEIN 7,MYELOID/LYMPHOID OR MIXED-LINEAGE LEUKEMIA,MYELOID/LYMPHOID
COMPND  10 OR MIXED-LINEAGE LEUKEMIA PROTEIN 1,TRITHORAX-LIKE PROTEIN,ZINC      
COMPND  11 FINGER PROTEIN HRX;                                                  
COMPND  12 EC: 2.1.1.43;                                                        
COMPND  13 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: MEN1, SCG2;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: KMT2A, ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1;                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    MENIN, MEN1, MLL, JUND, LEDGF, TPR, TRANSCRIPTION, EPIGENETICS,       
KEYWDS   2 CANCER                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.HUANG,B.WAN,M.LEI                                                   
REVDAT   4   08-NOV-17 3U85    1       REMARK                                   
REVDAT   3   21-JUN-17 3U85    1       DBREF                                    
REVDAT   2   07-MAR-12 3U85    1       JRNL                                     
REVDAT   1   15-FEB-12 3U85    0                                                
JRNL        AUTH   J.HUANG,B.GURUNG,B.WAN,S.MATKAR,N.A.VENIAMINOVA,K.WAN,       
JRNL        AUTH 2 J.L.MERCHANT,X.HUA,M.LEI                                     
JRNL        TITL   THE SAME POCKET IN MENIN BINDS BOTH MLL AND JUND BUT HAS     
JRNL        TITL 2 OPPOSITE EFFECTS ON TRANSCRIPTION.                           
JRNL        REF    NATURE                        V. 482   542 2012              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   22327296                                                     
JRNL        DOI    10.1038/NATURE10806                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7_650                                       
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.28                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.200                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 18424                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.810                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1808                            
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 33.2844 -  7.0337    0.99     1451   162  0.2056 0.2510        
REMARK   3     2  7.0337 -  5.5915    1.00     1385   158  0.2126 0.2379        
REMARK   3     3  5.5915 -  4.8872    1.00     1344   153  0.1902 0.2120        
REMARK   3     4  4.8872 -  4.4415    1.00     1337   160  0.1856 0.2192        
REMARK   3     5  4.4415 -  4.1237    1.00     1352   151  0.1864 0.2265        
REMARK   3     6  4.1237 -  3.8810    0.99     1328   147  0.2011 0.2496        
REMARK   3     7  3.8810 -  3.6869    0.99     1315   151  0.2182 0.2540        
REMARK   3     8  3.6869 -  3.5266    0.99     1340   125  0.2373 0.3199        
REMARK   3     9  3.5266 -  3.3910    0.97     1307   116  0.2725 0.3241        
REMARK   3    10  3.3910 -  3.2740    0.95     1262   135  0.3004 0.3431        
REMARK   3    11  3.2740 -  3.1718    0.88     1149   143  0.3033 0.3374        
REMARK   3    12  3.1718 -  3.0812    0.78     1017   116  0.3183 0.3483        
REMARK   3    13  3.0812 -  3.0000    0.75     1029    91  0.3441 0.4114        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 0.50                                          
REMARK   3   SHRINKAGE RADIUS   : 0.16                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 79.03                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.750           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 111.0                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -43.22740                                            
REMARK   3    B22 (A**2) : -43.22740                                            
REMARK   3    B33 (A**2) : 95.09290                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.004           3988                                  
REMARK   3   ANGLE     :  0.809           5416                                  
REMARK   3   CHIRALITY :  0.052            601                                  
REMARK   3   PLANARITY :  0.004            698                                  
REMARK   3   DIHEDRAL  : 15.375           1458                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3U85 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000068426.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-10                          
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               : 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) : 0.97941                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18712                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY                : 23.70                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 20.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.33400                            
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.3 M NACL, 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 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.77500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       70.60250            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       70.60250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       23.38750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       70.60250            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       70.60250            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       70.16250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       70.60250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       70.60250            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       23.38750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       70.60250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       70.60250            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       70.16250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       46.77500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 1460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 350   BIOMT1   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       46.77500            
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     SER A     1                                                      
REMARK 465     GLY A   386                                                      
REMARK 465     GLU A   387                                                      
REMARK 465     GLU A   388                                                      
REMARK 465     ARG A   389                                                      
REMARK 465     PRO A   390                                                      
REMARK 465     GLY A   391                                                      
REMARK 465     GLU A   392                                                      
REMARK 465     GLN A   393                                                      
REMARK 465     SER A   394                                                      
REMARK 465     GLN A   395                                                      
REMARK 465     GLY A   396                                                      
REMARK 465     THR A   397                                                      
REMARK 465     GLN A   398                                                      
REMARK 465     SER A   399                                                      
REMARK 465     GLN A   400                                                      
REMARK 465     GLY A   401                                                      
REMARK 465     GLY A   528                                                      
REMARK 465     PRO A   529                                                      
REMARK 465     GLU A   530                                                      
REMARK 465     GLY A   531                                                      
REMARK 465     GLY A   532                                                      
REMARK 465     SER A   533                                                      
REMARK 465     THR A   534                                                      
REMARK 465     ALA A   535                                                      
REMARK 465     GLN A   536                                                      
REMARK 465     VAL A   537                                                      
REMARK 465     PRO A   538                                                      
REMARK 465     ALA A   539                                                      
REMARK 465     PRO A   540                                                      
REMARK 465     THR A   541                                                      
REMARK 465     ALA A   542                                                      
REMARK 465     SER A   543                                                      
REMARK 465     PRO A   544                                                      
REMARK 465     PRO A   545                                                      
REMARK 465     PRO A   546                                                      
REMARK 465     GLU A   547                                                      
REMARK 465     GLN A   582                                                      
REMARK 465     SER A   583                                                      
REMARK 465     GLN A   584                                                      
REMARK 465     VAL A   585                                                      
REMARK 465     GLN A   586                                                      
REMARK 465     MET A   587                                                      
REMARK 465     LYS A   588                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     GLN A   590                                                      
REMARK 465     LYS A   591                                                      
REMARK 465     VAL A   592                                                      
REMARK 465     SER A   593                                                      
REMARK 465     THR A   594                                                      
REMARK 465     PRO A   595                                                      
REMARK 465     SER A   596                                                      
REMARK 465     ASP A   597                                                      
REMARK 465     TYR A   598                                                      
REMARK 465     THR A   599                                                      
REMARK 465     LEU A   600                                                      
REMARK 465     SER A   601                                                      
REMARK 465     PHE A   602                                                      
REMARK 465     LEU A   603                                                      
REMARK 465     LYS A   604                                                      
REMARK 465     ARG A   605                                                      
REMARK 465     GLN A   606                                                      
REMARK 465     ARG A   607                                                      
REMARK 465     LYS A   608                                                      
REMARK 465     GLY A   609                                                      
REMARK 465     LEU A   610                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     THR B    15                                                      
REMARK 465     THR B    16                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     GLY B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     GLY B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     ARG B    24                                                      
REMARK 465     ARG B    25                                                      
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    ILE A  97      -71.19    -74.14                                   
REMARK 500    TYR A 106       75.05   -119.35                                   
REMARK 500    HIS A 139       44.56     74.24                                   
REMARK 500    ASN A 203        3.28    -61.47                                   
REMARK 500    PRO A 373       -7.22    -57.70                                   
REMARK 500    ARG A 452       -6.31    -57.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3U84   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3U86   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3U88   RELATED DB: PDB                                   
DBREF  3U85 A    2   459  UNP    O00255   MEN1_HUMAN       2    459             
DBREF  3U85 A  520   610  UNP    O00255   MEN1_HUMAN     520    610             
DBREF  3U85 B    6    25  UNP    Q03164   KMT2A_HUMAN      6     25             
SEQADV 3U85 SER A    1  UNP  O00255              EXPRESSION TAG                 
SEQADV 3U85 SER B    5  UNP  Q03164              EXPRESSION TAG                 
SEQRES   1 A  550  SER GLY LEU LYS ALA ALA GLN LYS THR LEU PHE PRO LEU          
SEQRES   2 A  550  ARG SER ILE ASP ASP VAL VAL ARG LEU PHE ALA ALA GLU          
SEQRES   3 A  550  LEU GLY ARG GLU GLU PRO ASP LEU VAL LEU LEU SER LEU          
SEQRES   4 A  550  VAL LEU GLY PHE VAL GLU HIS PHE LEU ALA VAL ASN ARG          
SEQRES   5 A  550  VAL ILE PRO THR ASN VAL PRO GLU LEU THR PHE GLN PRO          
SEQRES   6 A  550  SER PRO ALA PRO ASP PRO PRO GLY GLY LEU THR TYR PHE          
SEQRES   7 A  550  PRO VAL ALA ASP LEU SER ILE ILE ALA ALA LEU TYR ALA          
SEQRES   8 A  550  ARG PHE THR ALA GLN ILE ARG GLY ALA VAL ASP LEU SER          
SEQRES   9 A  550  LEU TYR PRO ARG GLU GLY GLY VAL SER SER ARG GLU LEU          
SEQRES  10 A  550  VAL LYS LYS VAL SER ASP VAL ILE TRP ASN SER LEU SER          
SEQRES  11 A  550  ARG SER TYR PHE LYS ASP ARG ALA HIS ILE GLN SER LEU          
SEQRES  12 A  550  PHE SER PHE ILE THR GLY THR LYS LEU ASP SER SER GLY          
SEQRES  13 A  550  VAL ALA PHE ALA VAL VAL GLY ALA CYS GLN ALA LEU GLY          
SEQRES  14 A  550  LEU ARG ASP VAL HIS LEU ALA LEU SER GLU ASP HIS ALA          
SEQRES  15 A  550  TRP VAL VAL PHE GLY PRO ASN GLY GLU GLN THR ALA GLU          
SEQRES  16 A  550  VAL THR TRP HIS GLY LYS GLY ASN GLU ASP ARG ARG GLY          
SEQRES  17 A  550  GLN THR VAL ASN ALA GLY VAL ALA GLU ARG SER TRP LEU          
SEQRES  18 A  550  TYR LEU LYS GLY SER TYR MET ARG CYS ASP ARG LYS MET          
SEQRES  19 A  550  GLU VAL ALA PHE MET VAL CYS ALA ILE ASN PRO SER ILE          
SEQRES  20 A  550  ASP LEU HIS THR ASP SER LEU GLU LEU LEU GLN LEU GLN          
SEQRES  21 A  550  GLN LYS LEU LEU TRP LEU LEU TYR ASP LEU GLY HIS LEU          
SEQRES  22 A  550  GLU ARG TYR PRO MET ALA LEU GLY ASN LEU ALA ASP LEU          
SEQRES  23 A  550  GLU GLU LEU GLU PRO THR PRO GLY ARG PRO ASP PRO LEU          
SEQRES  24 A  550  THR LEU TYR HIS LYS GLY ILE ALA SER ALA LYS THR TYR          
SEQRES  25 A  550  TYR ARG ASP GLU HIS ILE TYR PRO TYR MET TYR LEU ALA          
SEQRES  26 A  550  GLY TYR HIS CYS ARG ASN ARG ASN VAL ARG GLU ALA LEU          
SEQRES  27 A  550  GLN ALA TRP ALA ASP THR ALA THR VAL ILE GLN ASP TYR          
SEQRES  28 A  550  ASN TYR CYS ARG GLU ASP GLU GLU ILE TYR LYS GLU PHE          
SEQRES  29 A  550  PHE GLU VAL ALA ASN ASP VAL ILE PRO ASN LEU LEU LYS          
SEQRES  30 A  550  GLU ALA ALA SER LEU LEU GLU ALA GLY GLU GLU ARG PRO          
SEQRES  31 A  550  GLY GLU GLN SER GLN GLY THR GLN SER GLN GLY SER ALA          
SEQRES  32 A  550  LEU GLN ASP PRO GLU CYS PHE ALA HIS LEU LEU ARG PHE          
SEQRES  33 A  550  TYR ASP GLY ILE CYS LYS TRP GLU GLU GLY SER PRO THR          
SEQRES  34 A  550  PRO VAL LEU HIS VAL GLY TRP ALA THR PHE LEU VAL GLN          
SEQRES  35 A  550  SER LEU GLY ARG PHE GLU GLY GLN VAL ARG GLN LYS VAL          
SEQRES  36 A  550  ARG ILE VAL SER GLY THR VAL ALA GLY THR ALA ARG GLY          
SEQRES  37 A  550  PRO GLU GLY GLY SER THR ALA GLN VAL PRO ALA PRO THR          
SEQRES  38 A  550  ALA SER PRO PRO PRO GLU GLY PRO VAL LEU THR PHE GLN          
SEQRES  39 A  550  SER GLU LYS MET LYS GLY MET LYS GLU LEU LEU VAL ALA          
SEQRES  40 A  550  THR LYS ILE ASN SER SER ALA ILE LYS LEU GLN LEU THR          
SEQRES  41 A  550  ALA GLN SER GLN VAL GLN MET LYS LYS GLN LYS VAL SER          
SEQRES  42 A  550  THR PRO SER ASP TYR THR LEU SER PHE LEU LYS ARG GLN          
SEQRES  43 A  550  ARG LYS GLY LEU                                              
SEQRES   1 B   21  SER ARG TRP ARG PHE PRO ALA ARG PRO GLY THR THR GLY          
SEQRES   2 B   21  GLY GLY GLY GLY GLY GLY ARG ARG                              
HELIX    1   1 LYS A    4  THR A    9  1                                   6    
HELIX    2   2 SER A   15  LEU A   27  1                                  13    
HELIX    3   3 ASP A   33  VAL A   50  1                                  18    
HELIX    4   4 ASP A   82  VAL A  101  1                                  20    
HELIX    5   5 ASP A  102  TYR A  106  5                                   5    
HELIX    6   6 SER A  114  SER A  128  1                                  15    
HELIX    7   7 SER A  142  THR A  150  1                                   9    
HELIX    8   8 ASP A  153  GLY A  169  1                                  17    
HELIX    9   9 VAL A  211  GLU A  217  1                                   7    
HELIX   10  10 TYR A  222  SER A  226  5                                   5    
HELIX   11  11 ASP A  231  ILE A  243  1                                  13    
HELIX   12  12 SER A  253  LEU A  270  1                                  18    
HELIX   13  13 TYR A  276  GLU A  290  1                                  15    
HELIX   14  14 ASP A  297  ARG A  314  1                                  18    
HELIX   15  15 ILE A  318  ASN A  331  1                                  14    
HELIX   16  16 ASN A  333  GLN A  349  1                                  17    
HELIX   17  17 CYS A  354  GLU A  356  5                                   3    
HELIX   18  18 ASP A  357  ASP A  370  1                                  14    
HELIX   19  19 ASP A  370  LEU A  383  1                                  14    
HELIX   20  20 ASP A  406  GLU A  425  1                                  20    
HELIX   21  21 HIS A  433  GLY A  445  1                                  13    
HELIX   22  22 GLU A  448  GLN A  453  1                                   6    
HELIX   23  23 SER A  555  GLY A  560  1                                   6    
HELIX   24  24 MET A  561  LYS A  562  5                                   2    
HELIX   25  25 GLU A  563  ALA A  567  5                                   5    
HELIX   26  26 ASN A  571  THR A  580  1                                  10    
SHEET    1   A 2 PHE A  63  PRO A  67  0                                        
SHEET    2   A 2 LEU A  75  PRO A  79 -1  O  THR A  76   N  SER A  66           
SHEET    1   B 4 GLN A 192  ALA A 194  0                                        
SHEET    2   B 4 ALA A 182  PHE A 186 -1  N  PHE A 186   O  GLN A 192           
SHEET    3   B 4 HIS A 174  LEU A 177 -1  N  HIS A 174   O  VAL A 185           
SHEET    4   B 4 MET A 228  ARG A 229 -1  O  MET A 228   N  LEU A 177           
SHEET    1   C 2 ARG A 456  ILE A 457  0                                        
SHEET    2   C 2 VAL A 550  LEU A 551  1  O  LEU A 551   N  ARG A 456           
CISPEP   1 PHE A   11    PRO A   12          0        -5.36                     
CRYST1  141.205  141.205   93.550  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007082  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007082  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010689        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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