GenomeNet

Database: PDB
Entry: 6BXH
LinkDB: 6BXH
Original site: 6BXH 
HEADER    PROTEIN BINDING, TRANSCRIPTION          18-DEC-17   6BXH              
TITLE     MENIN IN COMPLEX WITH MI-853                                          
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    PROTEIN BINDING, INHIBITOR, TRANSCRIPTION                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.BORKIN,S.KLOSSOWSKI,J.POLLOCK,B.LINHARES,T.CIERPICKI,J.GREMBECKA    
REVDAT   1   28-NOV-18 6BXH    0                                                
JRNL        AUTH   D.BORKIN,S.KLOSSOWSKI,J.POLLOCK,B.LINHARES,T.CIERPICKI,      
JRNL        AUTH 2 J.GREMBECKA                                                  
JRNL        TITL   MENIN IN COMPLEX WITH MI-853                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 17430                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 892                             
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 47.9220 -  4.4424    0.99     2896   155  0.2030 0.2580        
REMARK   3     2  4.4424 -  3.5264    0.99     2746   163  0.1710 0.2210        
REMARK   3     3  3.5264 -  3.0807    1.00     2761   144  0.2020 0.2600        
REMARK   3     4  3.0807 -  2.7991    1.00     2726   157  0.2110 0.2920        
REMARK   3     5  2.7991 -  2.5985    1.00     2748   131  0.2210 0.2740        
REMARK   3     6  2.5985 -  2.4450    0.99     2661   142  0.2370 0.2930        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.247            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.210           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           3827                                  
REMARK   3   ANGLE     :  0.710           5204                                  
REMARK   3   CHIRALITY :  0.039            578                                  
REMARK   3   PLANARITY :  0.005            660                                  
REMARK   3   DIHEDRAL  :  4.496           3131                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESSEQ 2:588)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -12.8799  10.9364 -12.9072              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1653 T22:   0.3056                                     
REMARK   3      T33:   0.1983 T12:   0.0249                                     
REMARK   3      T13:   0.0013 T23:  -0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8158 L22:   3.4054                                     
REMARK   3      L33:   2.2281 L12:   0.7153                                     
REMARK   3      L13:  -0.3223 L23:  -1.4892                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0217 S12:  -0.1177 S13:  -0.0807                       
REMARK   3      S21:   0.0178 S22:  -0.0472 S23:  -0.1452                       
REMARK   3      S31:   0.1564 S32:   0.0435 S33:   0.0179                       
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 6BXH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000231751.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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) : 1.0331                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17430                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.445                              
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     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.13600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.81000                            
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: 4X5Y                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M HEPES      
REMARK 280  AND 25% W/V PEG 3,350. THIS SOLUTION WAS MIXED 1:1 WITH 2.5MG/ML    
REMARK 280  PROTEIN IN 50MM TRIS-HCL, 50MM NACL, AND 1MM TCEP. PRIOR TO DATA    
REMARK 280  COLLECTION, CRYSTALS WERE TRANSFERRED INTO A CRYO-SOLUTION          
REMARK 280  CONTAINING 20% PEG550 MME AND FLASH-FROZEN IN LIQUID NITROGEN,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 283K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
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       24.01700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.66300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.05900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.66300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.01700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.05900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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     GLY A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ILE A    54                                                      
REMARK 465     PRO A    55                                                      
REMARK 465     THR A    56                                                      
REMARK 465     ASN A    57                                                      
REMARK 465     VAL A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     GLU A    60                                                      
REMARK 465     LEU A    61                                                      
REMARK 465     THR A    62                                                      
REMARK 465     PHE A    63                                                      
REMARK 465     GLN A    64                                                      
REMARK 465     PRO A    65                                                      
REMARK 465     SER A    66                                                      
REMARK 465     PRO A    67                                                      
REMARK 465     ALA A    68                                                      
REMARK 465     PRO A    69                                                      
REMARK 465     ASP A    70                                                      
REMARK 465     PRO A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     GLY A    73                                                      
REMARK 465     ALA A   539                                                      
REMARK 465     PRO A   540                                                      
REMARK 465     ALA 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     GLY A   548                                                      
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 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     ARG A 137    CZ   NH1  NH2                                       
REMARK 470     LYS A 201    CG   CD   CE   NZ                                   
REMARK 470     GLU A 290    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 448    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 456    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 569    CG   CD   CE   NZ                                   
REMARK 470     LYS A 576    CG   CD   CE   NZ                                   
REMARK 470     LYS A 588    CG   CD   CE   NZ                                   
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   O    ALA A   385     N    SER A   399              2.12            
REMARK 500   O    THR A     9     N    PHE A    11              2.18            
REMARK 500   OE1  GLU A   425     O    HOH A   701              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    ALA A   5       43.21     81.25                                   
REMARK 500    LYS A   8       34.57   -156.35                                   
REMARK 500    THR A   9     -106.84    -81.59                                   
REMARK 500    LEU A  10      -36.23     53.66                                   
REMARK 500    ASP A  33       98.54    -68.28                                   
REMARK 500    TYR A  77      -80.25    -77.69                                   
REMARK 500    PRO A 107     -148.57    -75.74                                   
REMARK 500    GLU A 109       76.43    -52.40                                   
REMARK 500    LYS A 135        3.78    -68.17                                   
REMARK 500    SER A 178     -160.01   -106.52                                   
REMARK 500    ASP A 180        4.62   -160.98                                   
REMARK 500    TRP A 183     -156.23   -154.35                                   
REMARK 500    PHE A 186     -164.32   -164.98                                   
REMARK 500    ASN A 189      108.55    -44.15                                   
REMARK 500    ARG A 206       50.68   -111.57                                   
REMARK 500    SER A 226       38.71    -87.73                                   
REMARK 500    ASP A 248     -147.07   -145.55                                   
REMARK 500    GLU A 356      -19.64     92.86                                   
REMARK 500    ASP A 370      -56.17   -142.04                                   
REMARK 500    SER A 399       91.17    -66.73                                   
REMARK 500    ALA A 581       17.50     57.55                                   
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 827        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH A 828        DISTANCE =  6.73 ANGSTROMS                       
REMARK 525    HOH A 829        DISTANCE =  7.71 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EE7 A 603                 
DBREF  6BXH A    1   459  UNP    O00255   MEN1_HUMAN       1    459             
SEQADV 6BXH GLY A   -4  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH GLY A   -3  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH SER A   -2  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH SER A   -1  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH SER A    0  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH     A       UNP  O00255    GLU   387 DELETION                       
SEQADV 6BXH     A       UNP  O00255    GLU   388 DELETION                       
SEQADV 6BXH     A       UNP  O00255    ARG   389 DELETION                       
SEQADV 6BXH     A       UNP  O00255    PRO   390 DELETION                       
SEQADV 6BXH     A       UNP  O00255    GLY   391 DELETION                       
SEQADV 6BXH     A       UNP  O00255    GLU   392 DELETION                       
SEQADV 6BXH     A       UNP  O00255    GLN   393 DELETION                       
SEQADV 6BXH     A       UNP  O00255    SER   394 DELETION                       
SEQADV 6BXH     A       UNP  O00255    GLN   395 DELETION                       
SEQADV 6BXH     A       UNP  O00255    GLY   396 DELETION                       
SEQADV 6BXH     A       UNP  O00255    THR   397 DELETION                       
SEQADV 6BXH     A       UNP  O00255    GLN   398 DELETION                       
SEQADV 6BXH VAL A  460  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH PRO A  461  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH ALA A  539  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH PRO A  540  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH ALA A  541  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH ALA A  542  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH SER A  543  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH PRO A  544  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH PRO A  545  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH PRO A  546  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH GLU A  547  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH GLY A  548  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH PRO A  549  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH VAL A  550  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH LEU A  551  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH THR A  552  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH PHE A  553  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH GLN A  554  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH SER A  555  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH GLU A  556  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH LYS A  557  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH MET A  558  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH LYS A  559  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH GLY A  560  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH MET A  561  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH LYS A  562  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH GLU A  563  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH LEU A  564  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH LEU A  565  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH VAL A  566  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH ALA A  567  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH THR A  568  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH LYS A  569  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH ILE A  570  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH ASN A  571  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH SER A  572  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH SER A  573  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH ALA A  574  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH ILE A  575  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH LYS A  576  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH LEU A  577  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH GLN A  578  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH LEU A  579  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH THR A  580  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH ALA A  581  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH GLN A  582  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH SER A  583  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH GLN A  584  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH VAL A  585  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH GLN A  586  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH MET A  587  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH LYS A  588  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH LYS A  589  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH GLN A  590  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH LYS A  591  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH VAL A  592  UNP  O00255              EXPRESSION TAG                 
SEQADV 6BXH SER A  593  UNP  O00255              EXPRESSION TAG                 
SEQRES   1 A  509  GLY GLY SER SER SER MET GLY LEU LYS ALA ALA GLN LYS          
SEQRES   2 A  509  THR LEU PHE PRO LEU ARG SER ILE ASP ASP VAL VAL ARG          
SEQRES   3 A  509  LEU PHE ALA ALA GLU LEU GLY ARG GLU GLU PRO ASP LEU          
SEQRES   4 A  509  VAL LEU LEU SER LEU VAL LEU GLY PHE VAL GLU HIS PHE          
SEQRES   5 A  509  LEU ALA VAL ASN ARG VAL ILE PRO THR ASN VAL PRO GLU          
SEQRES   6 A  509  LEU THR PHE GLN PRO SER PRO ALA PRO ASP PRO PRO GLY          
SEQRES   7 A  509  GLY LEU THR TYR PHE PRO VAL ALA ASP LEU SER ILE ILE          
SEQRES   8 A  509  ALA ALA LEU TYR ALA ARG PHE THR ALA GLN ILE ARG GLY          
SEQRES   9 A  509  ALA VAL ASP LEU SER LEU TYR PRO ARG GLU GLY GLY VAL          
SEQRES  10 A  509  SER SER ARG GLU LEU VAL LYS LYS VAL SER ASP VAL ILE          
SEQRES  11 A  509  TRP ASN SER LEU SER ARG SER TYR PHE LYS ASP ARG ALA          
SEQRES  12 A  509  HIS ILE GLN SER LEU PHE SER PHE ILE THR GLY THR LYS          
SEQRES  13 A  509  LEU ASP SER SER GLY VAL ALA PHE ALA VAL VAL GLY ALA          
SEQRES  14 A  509  CYS GLN ALA LEU GLY LEU ARG ASP VAL HIS LEU ALA LEU          
SEQRES  15 A  509  SER GLU ASP HIS ALA TRP VAL VAL PHE GLY PRO ASN GLY          
SEQRES  16 A  509  GLU GLN THR ALA GLU VAL THR TRP HIS GLY LYS GLY ASN          
SEQRES  17 A  509  GLU ASP ARG ARG GLY GLN THR VAL ASN ALA GLY VAL ALA          
SEQRES  18 A  509  GLU ARG SER TRP LEU TYR LEU LYS GLY SER TYR MET ARG          
SEQRES  19 A  509  CYS ASP ARG LYS MET GLU VAL ALA PHE MET VAL CYS ALA          
SEQRES  20 A  509  ILE ASN PRO SER ILE ASP LEU HIS THR ASP SER LEU GLU          
SEQRES  21 A  509  LEU LEU GLN LEU GLN GLN LYS LEU LEU TRP LEU LEU TYR          
SEQRES  22 A  509  ASP LEU GLY HIS LEU GLU ARG TYR PRO MET ALA LEU GLY          
SEQRES  23 A  509  ASN LEU ALA ASP LEU GLU GLU LEU GLU PRO THR PRO GLY          
SEQRES  24 A  509  ARG PRO ASP PRO LEU THR LEU TYR HIS LYS GLY ILE ALA          
SEQRES  25 A  509  SER ALA LYS THR TYR TYR ARG ASP GLU HIS ILE TYR PRO          
SEQRES  26 A  509  TYR MET TYR LEU ALA GLY TYR HIS CYS ARG ASN ARG ASN          
SEQRES  27 A  509  VAL ARG GLU ALA LEU GLN ALA TRP ALA ASP THR ALA THR          
SEQRES  28 A  509  VAL ILE GLN ASP TYR ASN TYR CYS ARG GLU ASP GLU GLU          
SEQRES  29 A  509  ILE TYR LYS GLU PHE PHE GLU VAL ALA ASN ASP VAL ILE          
SEQRES  30 A  509  PRO ASN LEU LEU LYS GLU ALA ALA SER LEU LEU GLU ALA          
SEQRES  31 A  509  GLY SER GLN GLY SER ALA LEU GLN ASP PRO GLU CYS PHE          
SEQRES  32 A  509  ALA HIS LEU LEU ARG PHE TYR ASP GLY ILE CYS LYS TRP          
SEQRES  33 A  509  GLU GLU GLY SER PRO THR PRO VAL LEU HIS VAL GLY TRP          
SEQRES  34 A  509  ALA THR PHE LEU VAL GLN SER LEU GLY ARG PHE GLU GLY          
SEQRES  35 A  509  GLN VAL ARG GLN LYS VAL ARG ILE VAL SER VAL PRO ALA          
SEQRES  36 A  509  PRO ALA ALA SER PRO PRO PRO GLU GLY PRO VAL LEU THR          
SEQRES  37 A  509  PHE GLN SER GLU LYS MET LYS GLY MET LYS GLU LEU LEU          
SEQRES  38 A  509  VAL ALA THR LYS ILE ASN SER SER ALA ILE LYS LEU GLN          
SEQRES  39 A  509  LEU THR ALA GLN SER GLN VAL GLN MET LYS LYS GLN LYS          
SEQRES  40 A  509  VAL SER                                                      
HET    DMS  A 601       4                                                       
HET    SO4  A 602       5                                                       
HET    EE7  A 603      46                                                       
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EE7 1-{2-[4-(FLUOROACETYL)PIPERAZIN-1-YL]ETHYL}-4-METHYL-5-          
HETNAM   2 EE7  [(4-{[6-(2,2,2-TRIFLUOROETHYL)THIENO[2,3-D]PYRIMIDIN-           
HETNAM   3 EE7  4-YL]AMINO}PIPERIDIN-1-YL)METHYL]-1H-INDOLE-2-                  
HETNAM   4 EE7  CARBONITRILE                                                    
FORMUL   2  DMS    C2 H6 O S                                                    
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  EE7    C32 H36 F4 N8 O S                                            
FORMUL   5  HOH   *129(H2 O)                                                    
HELIX    1 AA1 SER A   15  LEU A   27  1                                  13    
HELIX    2 AA2 ASP A   33  VAL A   50  1                                  18    
HELIX    3 AA3 ASP A   82  VAL A  101  1                                  20    
HELIX    4 AA4 SER A  114  ASN A  127  1                                  14    
HELIX    5 AA5 SER A  142  THR A  150  1                                   9    
HELIX    6 AA6 ASP A  153  GLY A  169  1                                  17    
HELIX    7 AA7 VAL A  211  GLU A  217  1                                   7    
HELIX    8 AA8 SER A  219  SER A  226  5                                   8    
HELIX    9 AA9 ASP A  231  ALA A  242  1                                  12    
HELIX   10 AB1 SER A  253  GLY A  271  1                                  19    
HELIX   11 AB2 TYR A  276  GLU A  290  1                                  15    
HELIX   12 AB3 ASP A  297  TYR A  313  1                                  17    
HELIX   13 AB4 ILE A  318  ASN A  331  1                                  14    
HELIX   14 AB5 ASN A  333  GLN A  349  1                                  17    
HELIX   15 AB6 ASP A  357  ASP A  370  1                                  14    
HELIX   16 AB7 ASP A  370  ALA A  385  1                                  16    
HELIX   17 AB8 SER A  402  GLN A  405  5                                   4    
HELIX   18 AB9 ASP A  406  GLU A  425  1                                  20    
HELIX   19 AC1 HIS A  433  PHE A  447  1                                  15    
HELIX   20 AC2 GLU A  448  GLN A  453  1                                   6    
HELIX   21 AC3 SER A  555  GLY A  560  1                                   6    
HELIX   22 AC4 MET A  561  VAL A  566  1                                   6    
HELIX   23 AC5 ASN A  571  THR A  580  1                                  10    
SHEET    1 AA1 4 GLN A 192  ALA A 194  0                                        
SHEET    2 AA1 4 ALA A 182  PHE A 186 -1  N  PHE A 186   O  GLN A 192           
SHEET    3 AA1 4 HIS A 174  LEU A 177 -1  N  ALA A 176   O  TRP A 183           
SHEET    4 AA1 4 MET A 228  ARG A 229 -1  O  MET A 228   N  LEU A 177           
SHEET    1 AA2 2 ARG A 456  ILE A 457  0                                        
SHEET    2 AA2 2 VAL A 550  LEU A 551  1  O  LEU A 551   N  ARG A 456           
CISPEP   1 GLY A    2    LEU A    3          0        -1.25                     
CISPEP   2 PHE A   11    PRO A   12          0         2.12                     
CISPEP   3 ASN A  189    GLY A  190          0        -6.81                     
CISPEP   4 VAL A  460    PRO A  461          0       -12.41                     
SITE     1 AC1  3 CYS A 241  ALA A 242  EE7 A 603                               
SITE     1 AC2  1 ARG A 446                                                     
SITE     1 AC3 19 PHE A 134  SER A 155  LEU A 177  SER A 178                    
SITE     2 AC3 19 ASP A 180  HIS A 181  PHE A 238  TYR A 276                    
SITE     3 AC3 19 MET A 278  MET A 322  TYR A 323  GLY A 326                    
SITE     4 AC3 19 CYS A 329  ARG A 330  TRP A 341  GLU A 363                    
SITE     5 AC3 19 GLU A 366  DMS A 601  HOH A 753                               
CRYST1   48.034   78.118  121.326  90.00  90.00  90.00 P 21 21 21    4          
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      0.020819  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012801  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008242        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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