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Database: PDB
Entry: 3U86
LinkDB: 3U86
Original site: 3U86 
HEADER    TRANSCRIPTION                           15-OCT-11   3U86              
TITLE     CRYSTAL STRUCTURE OF HUMAN MENIN IN COMPLEX WITH JUND                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MENIN;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TRANSCRIPTION FACTOR JUN-D;                                
COMPND   7 CHAIN: B;                                                            
COMPND   8 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: 469008;                                     
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: JUND;                                                          
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 3U86    1       REMARK                                   
REVDAT   3   21-JUN-17 3U86    1       DBREF                                    
REVDAT   2   07-MAR-12 3U86    1       JRNL                                     
REVDAT   1   15-FEB-12 3U86    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.    2.84 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) : 2.84                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 21352                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.060                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2148                            
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 33.9868 -  6.9935    0.99     1478   146  0.2008 0.2132        
REMARK   3     2  6.9935 -  5.5588    1.00     1391   154  0.2260 0.2302        
REMARK   3     3  5.5588 -  4.8584    1.00     1354   161  0.2034 0.2109        
REMARK   3     4  4.8584 -  4.4152    1.00     1364   147  0.1831 0.2044        
REMARK   3     5  4.4152 -  4.0994    1.00     1359   144  0.1889 0.2399        
REMARK   3     6  4.0994 -  3.8580    1.00     1341   143  0.1972 0.2305        
REMARK   3     7  3.8580 -  3.6650    1.00     1342   154  0.2044 0.2021        
REMARK   3     8  3.6650 -  3.5057    1.00     1343   142  0.2152 0.2632        
REMARK   3     9  3.5057 -  3.3708    0.99     1311   142  0.2307 0.3226        
REMARK   3    10  3.3708 -  3.2546    0.99     1308   165  0.2509 0.3127        
REMARK   3    11  3.2546 -  3.1529    0.96     1253   154  0.2642 0.3021        
REMARK   3    12  3.1529 -  3.0629    0.92     1211   146  0.2913 0.3644        
REMARK   3    13  3.0629 -  2.9823    0.87     1141   132  0.3081 0.3458        
REMARK   3    14  2.9823 -  2.9096    0.77     1006   120  0.2789 0.3233        
REMARK   3    15  2.9096 -  2.8430    0.74     1002    98  0.2972 0.2942        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 62.96                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.640           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 95.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -37.55940                                            
REMARK   3    B22 (A**2) : -37.55940                                            
REMARK   3    B33 (A**2) : 75.11880                                             
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      :  0.007           3994                                  
REMARK   3   ANGLE     :  1.032           5424                                  
REMARK   3   CHIRALITY :  0.073            605                                  
REMARK   3   PLANARITY :  0.004            699                                  
REMARK   3   DIHEDRAL  : 15.722           1462                                  
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 3U86 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_1000068427.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-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) : 0.98019                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21430                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.843                              
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     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 11.50                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44600                            
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   (%): 66.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68                     
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       46.55300            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       70.32350            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       70.32350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       23.27650            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       70.32350            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       70.32350            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       69.82950            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       70.32350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       70.32350            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       23.27650            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       70.32350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       70.32350            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       69.82950            
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       46.55300            
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: 1530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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     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     SER B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     GLY B    29                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A    31     NH1  ARG A   232              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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  70     -168.34   -120.52                                   
REMARK 500    LEU A 103       -4.18    -58.02                                   
REMARK 500    SER A 130      139.28    -38.80                                   
REMARK 500    SER A 132       69.79   -105.52                                   
REMARK 500    HIS A 139       30.59     77.53                                   
REMARK 500    SER A 178     -159.51    -99.53                                   
REMARK 500    ASP A 180       17.81   -146.78                                   
REMARK 500    TRP A 183     -156.87   -157.59                                   
REMARK 500    ASN A 189        5.99     58.80                                   
REMARK 500    LYS A 562       -3.97    -55.55                                   
REMARK 500    ASN A 571       82.83    -67.81                                   
REMARK 500    THR A 580      145.81   -179.11                                   
REMARK 500    LYS B  46     -179.60    -65.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3U84   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3U85   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3U88   RELATED DB: PDB                                   
DBREF  3U86 A    2   459  UNP    O00255   MEN1_HUMAN       2    459             
DBREF  3U86 A  520   610  UNP    O00255   MEN1_HUMAN     520    610             
DBREF  3U86 B   27    47  PDB    3U86     3U86            27     47             
SEQADV 3U86 SER A    1  UNP  O00255              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   15  SER PRO GLY ARG LEU PHE PRO GLY ALA PRO PRO THR ALA          
SEQRES   2 B   15  LYS LYS                                                      
HELIX    1   1 LYS A    4  THR A    9  1                                   6    
HELIX    2   2 SER A   15  GLY A   28  1                                  14    
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 SER A  114  SER A  128  1                                  15    
HELIX    6   6 SER A  142  GLY A  149  1                                   8    
HELIX    7   7 ASP A  153  LEU A  168  1                                  16    
HELIX    8   8 VAL A  211  GLU A  217  1                                   7    
HELIX    9   9 TYR A  222  SER A  226  5                                   5    
HELIX   10  10 ASP A  231  ILE A  243  1                                  13    
HELIX   11  11 SER A  253  LEU A  270  1                                  18    
HELIX   12  12 TYR A  276  GLU A  290  1                                  15    
HELIX   13  13 ASP A  297  ARG A  314  1                                  18    
HELIX   14  14 ILE A  318  ASN A  331  1                                  14    
HELIX   15  15 ASN A  333  GLN A  349  1                                  17    
HELIX   16  16 CYS A  354  GLU A  356  5                                   3    
HELIX   17  17 ASP A  357  ASP A  370  1                                  14    
HELIX   18  18 ASP A  370  ALA A  380  1                                  11    
HELIX   19  19 ASP A  406  GLU A  425  1                                  20    
HELIX   20  20 HIS A  433  GLY A  445  1                                  13    
HELIX   21  21 GLU A  448  GLN A  453  1                                   6    
HELIX   22  22 SER A  555  MET A  561  1                                   7    
HELIX   23  23 MET A  561  VAL A  566  1                                   6    
HELIX   24  24 ASN A  571  LEU A  579  1                                   9    
SHEET    1   A 2 PHE A  63  PRO A  67  0                                        
SHEET    2   A 2 LEU A  75  PRO A  79 -1  O  PHE A  78   N  GLN A  64           
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       -11.07                     
CISPEP   2 GLY A   73    GLY A   74          0        -0.69                     
CRYST1  140.647  140.647   93.106  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      0.007110  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007110  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010740        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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