GenomeNet

Database: PDB
Entry: 6B41
LinkDB: 6B41
Original site: 6B41 
HEADER    PROTEIN BINDING/INHIBITOR               25-SEP-17   6B41              
TITLE     MENIN BOUND TO M-525                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MENIN;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 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                                         
KEYWDS    COVALENT INHIBITOR, MEN1 SYNDROME, LEUKEMIA, PROTEIN BINDING-         
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.STUCKEY                                                           
REVDAT   2   14-FEB-18 6B41    1       JRNL                                     
REVDAT   1   24-JAN-18 6B41    0                                                
JRNL        AUTH   S.XU,A.AGUILAR,T.XU,K.ZHENG,L.HUANG,J.STUCKEY,K.CHINNASWAMY, 
JRNL        AUTH 2 D.BERNARD,E.FERNANDEZ-SALAS,L.LIU,M.WANG,D.MCEACHERN,        
JRNL        AUTH 3 S.PRZYBRANOWSKI,C.FOSTER,S.WANG                              
JRNL        TITL   DESIGN OF THE FIRST-IN-CLASS, HIGHLY POTENT IRREVERSIBLE     
JRNL        TITL 2 INHIBITOR TARGETING THE MENIN-MLL PROTEIN-PROTEIN            
JRNL        TITL 3 INTERACTION.                                                 
JRNL        REF    ANGEW. CHEM. INT. ED. ENGL.   V.  57  1601 2018              
JRNL        REFN                   ESSN 1521-3773                               
JRNL        PMID   29284071                                                     
JRNL        DOI    10.1002/ANIE.201711828                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 25715                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.211                          
REMARK   3   R VALUE            (WORKING SET)  : 0.209                          
REMARK   3   FREE R VALUE                      : 0.252                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1285                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 13                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.61                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.72                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 58.62                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1929                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2265                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1844                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2242                   
REMARK   3   BIN FREE R VALUE                        : 0.2754                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.41                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 85                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3714                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 104                                     
REMARK   3   SOLVENT ATOMS            : 141                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.84                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.82030                                              
REMARK   3    B22 (A**2) : 0.82030                                              
REMARK   3    B33 (A**2) : -1.64050                                             
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.380               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.352               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.263               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.367               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.269               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.865                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.818                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3999   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5514   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1348   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 84     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 606    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3999   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 494    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4545   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.14                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.66                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.52                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6B41 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000230252.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-AUG-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
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-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29090                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.610                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 12.10                              
REMARK 200  R MERGE                    (I) : 0.10200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.61                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.66500                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 3U84                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.96 M NACL, 89 MM BIS-TRIS PH 6.8,      
REMARK 280  0.178 M MGCL2 AND 10.7 MM PR ACETATE, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y,Z                                                 
REMARK 290       7555   -Y+1/2,X,Z+3/4                                          
REMARK 290       8555   Y,-X+1/2,Z+1/4                                          
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       76.96000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       76.96000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.80900            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       76.96000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       20.40450            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       76.96000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       61.21350            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       76.96000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       76.96000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       40.80900            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       76.96000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       61.21350            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       76.96000            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       20.40450            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     PRO A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     GLY A    73                                                      
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 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     GLU A  30    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  57    CG   OD1  ND2                                       
REMARK 470     ARG A 108    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 131    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 201    CG   CD   CE   NZ                                   
REMARK 470     ASN A 203    CG   OD1  ND2                                       
REMARK 470     GLU A 204    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 206    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 249    CG   CD1  CD2                                       
REMARK 470     HIS A 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 332    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 355    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 358    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 442    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 467    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 562    CG   CD   CE   NZ                                   
REMARK 470     THR A 568    OG1  CG2                                            
REMARK 470     LYS A 569    CG   CD   CE   NZ                                   
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    ALA A  49      -43.33   -136.52                                   
REMARK 500    SER A 178     -157.31   -112.05                                   
REMARK 500    TRP A 183     -167.85   -161.39                                   
REMARK 500    ARG A 218       44.80     75.41                                   
REMARK 500    LYS A 224       24.77     47.25                                   
REMARK 500    ARG A 314       25.12     45.94                                   
REMARK 500    ASN A 333       76.83   -103.71                                   
REMARK 500    ASP A 370      -54.21   -139.36                                   
REMARK 500    LYS A 562      -65.34    -29.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 937        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH A 938        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH A 939        DISTANCE =  6.83 ANGSTROMS                       
REMARK 525    HOH A 940        DISTANCE =  8.07 ANGSTROMS                       
REMARK 525    HOH A 941        DISTANCE =  9.71 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CJV A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7PR A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7PR A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7PR A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7PR A 705                 
DBREF  6B41 A    2   610  UNP    O00255   MEN1_HUMAN       2    610             
SEQADV 6B41 SER A    1  UNP  O00255              EXPRESSION TAG                 
SEQADV 6B41     A       UNP  O00255    ARG   460 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLU   461 DELETION                       
SEQADV 6B41     A       UNP  O00255    ALA   462 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLU   463 DELETION                       
SEQADV 6B41     A       UNP  O00255    ALA   464 DELETION                       
SEQADV 6B41     A       UNP  O00255    ALA   465 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLU   466 DELETION                       
SEQADV 6B41     A       UNP  O00255    ALA   467 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLU   468 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLU   469 DELETION                       
SEQADV 6B41     A       UNP  O00255    PRO   470 DELETION                       
SEQADV 6B41     A       UNP  O00255    TRP   471 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLY   472 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLU   473 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLU   474 DELETION                       
SEQADV 6B41     A       UNP  O00255    ALA   475 DELETION                       
SEQADV 6B41     A       UNP  O00255    ARG   476 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLU   477 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLY   478 DELETION                       
SEQADV 6B41     A       UNP  O00255    ARG   479 DELETION                       
SEQADV 6B41     A       UNP  O00255    ARG   480 DELETION                       
SEQADV 6B41     A       UNP  O00255    ARG   481 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLY   482 DELETION                       
SEQADV 6B41     A       UNP  O00255    PRO   483 DELETION                       
SEQADV 6B41     A       UNP  O00255    ARG   484 DELETION                       
SEQADV 6B41     A       UNP  O00255    ARG   485 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLU   486 DELETION                       
SEQADV 6B41     A       UNP  O00255    SER   487 DELETION                       
SEQADV 6B41     A       UNP  O00255    LYS   488 DELETION                       
SEQADV 6B41     A       UNP  O00255    PRO   489 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLU   490 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLU   491 DELETION                       
SEQADV 6B41     A       UNP  O00255    PRO   492 DELETION                       
SEQADV 6B41     A       UNP  O00255    PRO   493 DELETION                       
SEQADV 6B41     A       UNP  O00255    PRO   494 DELETION                       
SEQADV 6B41     A       UNP  O00255    PRO   495 DELETION                       
SEQADV 6B41     A       UNP  O00255    LYS   496 DELETION                       
SEQADV 6B41     A       UNP  O00255    LYS   497 DELETION                       
SEQADV 6B41     A       UNP  O00255    PRO   498 DELETION                       
SEQADV 6B41     A       UNP  O00255    ALA   499 DELETION                       
SEQADV 6B41     A       UNP  O00255    LEU   500 DELETION                       
SEQADV 6B41     A       UNP  O00255    ASP   501 DELETION                       
SEQADV 6B41     A       UNP  O00255    LYS   502 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLY   503 DELETION                       
SEQADV 6B41     A       UNP  O00255    LEU   504 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLY   505 DELETION                       
SEQADV 6B41     A       UNP  O00255    THR   506 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLY   507 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLN   508 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLY   509 DELETION                       
SEQADV 6B41     A       UNP  O00255    ALA   510 DELETION                       
SEQADV 6B41     A       UNP  O00255    VAL   511 DELETION                       
SEQADV 6B41     A       UNP  O00255    SER   512 DELETION                       
SEQADV 6B41     A       UNP  O00255    GLY   513 DELETION                       
SEQADV 6B41     A       UNP  O00255    PRO   514 DELETION                       
SEQADV 6B41     A       UNP  O00255    PRO   515 DELETION                       
SEQADV 6B41     A       UNP  O00255    ARG   516 DELETION                       
SEQADV 6B41     A       UNP  O00255    LYS   517 DELETION                       
SEQADV 6B41     A       UNP  O00255    PRO   518 DELETION                       
SEQADV 6B41     A       UNP  O00255    PRO   519 DELETION                       
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                                              
HET    CJV  A 701     104                                                       
HET    7PR  A 702      26                                                       
HET    7PR  A 703      22                                                       
HET    7PR  A 704      22                                                       
HET    7PR  A 705      22                                                       
HETNAM     CJV METHYL {(1S,2R)-2-[(S)-CYANO[1-({1-[4-({1-[4-                    
HETNAM   2 CJV  (DIMETHYLAMINO)BUTANOYL]AZETIDIN-3-YL}SULFONYL)                 
HETNAM   3 CJV  PHENYL]AZETIDIN-3-YL}METHYL)PIPERIDIN-4-YL](3-                  
HETNAM   4 CJV  FLUOROPHENYL)METHYL]CYCLOPENTYL}CARBAMATE                       
HETNAM     7PR PRASEODYMIUM TRIACETATE                                          
FORMUL   2  CJV    C39 H53 F N6 O5 S                                            
FORMUL   3  7PR    4(C6 H9 O6 PR)                                               
FORMUL   7  HOH   *141(H2 O)                                                    
HELIX    1 AA1 LYS A    4  THR A    9  1                                   6    
HELIX    2 AA2 SER A   15  LEU A   27  1                                  13    
HELIX    3 AA3 ASP A   33  ALA A   49  1                                  17    
HELIX    4 AA4 ASP A   82  VAL A  101  1                                  20    
HELIX    5 AA5 SER A  114  LEU A  129  1                                  16    
HELIX    6 AA6 SER A  142  GLY A  149  1                                   8    
HELIX    7 AA7 ASP A  153  GLY A  169  1                                  17    
HELIX    8 AA8 VAL A  211  GLU A  217  1                                   7    
HELIX    9 AA9 SER A  219  SER A  226  5                                   8    
HELIX   10 AB1 ASP A  231  ALA A  242  1                                  12    
HELIX   11 AB2 SER A  253  LEU A  270  1                                  18    
HELIX   12 AB3 TYR A  276  GLU A  290  1                                  15    
HELIX   13 AB4 ASP A  297  TYR A  313  1                                  17    
HELIX   14 AB5 ILE A  318  ASN A  331  1                                  14    
HELIX   15 AB6 ASN A  333  GLN A  349  1                                  17    
HELIX   16 AB7 CYS A  354  GLU A  356  5                                   3    
HELIX   17 AB8 ASP A  357  ASP A  370  1                                  14    
HELIX   18 AB9 ASP A  370  LEU A  383  1                                  14    
HELIX   19 AC1 ASP A  406  GLU A  425  1                                  20    
HELIX   20 AC2 HIS A  433  GLY A  445  1                                  13    
HELIX   21 AC3 GLU A  448  LYS A  454  1                                   7    
HELIX   22 AC4 SER A  555  ALA A  567  1                                  13    
HELIX   23 AC5 ASN A  571  ALA A  581  1                                  11    
SHEET    1 AA1 2 PHE A  63  GLN A  64  0                                        
SHEET    2 AA1 2 PHE A  78  PRO A  79 -1  O  PHE A  78   N  GLN A  64           
SHEET    1 AA2 4 GLN A 192  ALA A 194  0                                        
SHEET    2 AA2 4 ALA A 182  PHE A 186 -1  N  PHE A 186   O  GLN A 192           
SHEET    3 AA2 4 HIS A 174  LEU A 177 -1  N  HIS A 174   O  VAL A 185           
SHEET    4 AA2 4 MET A 228  ARG A 229 -1  O  MET A 228   N  LEU A 177           
SHEET    1 AA3 2 ARG A 456  ILE A 457  0                                        
SHEET    2 AA3 2 VAL A 550  LEU A 551  1  O  LEU A 551   N  ARG A 456           
LINK         SG  CYS A 329                 C28 CJV A 701     1555   1555  1.86  
CISPEP   1 PHE A   11    PRO A   12          0         0.45                     
SITE     1 AC1 18 SER A 155  SER A 178  GLU A 179  ASP A 180                    
SITE     2 AC1 18 HIS A 181  PHE A 238  CYS A 241  TYR A 276                    
SITE     3 AC1 18 MET A 278  ASN A 282  MET A 322  TYR A 323                    
SITE     4 AC1 18 GLY A 326  CYS A 329  TRP A 341  GLU A 363                    
SITE     5 AC1 18 VAL A 367  VAL A 371                                          
SITE     1 AC2  4 PHE A 365  GLU A 366  ASN A 369  ASP A 370                    
SITE     1 AC3  5 TRP A 126  LEU A 129  SER A 130  ARG A 131                    
SITE     2 AC3  5 TRP A 198                                                     
SITE     1 AC4  2 LEU A 249  LEU A 289                                          
SITE     1 AC5  2 THR A  56  HOH A 832                                          
CRYST1  153.920  153.920   81.618  90.00  90.00  90.00 I 41          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      0.006497  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006497  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012252        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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