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Database: PDB
Entry: 5DD9
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Original site: 5DD9 
HEADER    PROTEIN BINDING/INHIBITOR               24-AUG-15   5DD9              
TITLE     MENIN IN COMPLEX WITH MI-326                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MENIN;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-459, 537-593;                               
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MEN1, SCG2;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN BINDING-INHIBITOR COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.POLLOCK,B.DMITRY,T.CIERPICKI,J.GREMBECKA                            
REVDAT   4   04-DEC-19 5DD9    1       REMARK                                   
REVDAT   3   27-SEP-17 5DD9    1       JRNL   REMARK                            
REVDAT   2   14-OCT-15 5DD9    1       JRNL                                     
REVDAT   1   09-SEP-15 5DD9    0                                                
JRNL        AUTH   J.POLLOCK,D.BORKIN,G.LUND,T.PUROHIT,E.DYGUDA-KAZIMIEROWICZ,  
JRNL        AUTH 2 J.GREMBECKA,T.CIERPICKI                                      
JRNL        TITL   RATIONAL DESIGN OF ORTHOGONAL MULTIPOLAR INTERACTIONS WITH   
JRNL        TITL 2 FLUORINE IN PROTEIN-LIGAND COMPLEXES.                        
JRNL        REF    J.MED.CHEM.                   V.  58  7465 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   26288158                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B00975                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.62 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 60127                          
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) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3211                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.62                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.66                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4359                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.70                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 221                          
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3641                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 97                                      
REMARK   3   SOLVENT ATOMS            : 493                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.13000                                              
REMARK   3    B22 (A**2) : -0.09000                                             
REMARK   3    B33 (A**2) : -1.04000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.084         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.086         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3886 ; 0.016 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5279 ; 1.658 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   488 ; 5.223 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   174 ;31.115 ;23.793       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   635 ;11.949 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;16.851 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   592 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2920 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1887 ; 4.118 ; 6.182       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2359 ; 5.104 ; 9.649       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1999 ; 6.346 ; 7.268       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   4                                                                      
REMARK   4 5DD9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213031.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 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) : 0.97857                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63572                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.620                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
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: 4GPQ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M HEPES PH   
REMARK 280  7.5 AND 25% W/V PEG 3,350. THIS SOLUTION WAS MIXED 1:1 WITH         
REMARK 280  2.5MG/ML PROTEIN IN 50MM TRIS-HCL (PH 8.0), 50MM NACL, AND 1MM      
REMARK 280  TCEP. PRIOR TO DATA COLLECTION, CRYSTALS WERE TRANSFERRED INTO A    
REMARK 280  CRYO-SOLUTION CONTAINING 20% PEG550 MME AND FLASH-FROZEN IN         
REMARK 280  LIQUID NITROGEN, 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       24.41500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.61400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.11500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.61400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.41500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.11500            
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     VAL A   537                                                      
REMARK 465     PRO A   538                                                      
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     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     LYS A   4    CE   NZ                                             
REMARK 470     GLU A  30    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 131    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 136    CG   OD1  OD2                                       
REMARK 470     LYS A 201    CG   CD   CE   NZ                                   
REMARK 470     GLU A 204    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 249    CG   CD1  CD2                                       
REMARK 470     ARG A 355    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 456    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 569    CG   CD   CE   NZ                                   
REMARK 470     GLN A 586    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 588    CG   CD   CE   NZ                                   
REMARK 470     LYS A 589    CA   C    O    CB   CG   CD   CE                    
REMARK 470     LYS A 589    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   N    GLY A     2     O    HOH A   701              2.10            
REMARK 500   O    DMS A   607     O    HOH A   702              2.11            
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    TYR A  77      -62.46   -157.17                                   
REMARK 500    SER A 178     -167.04   -102.58                                   
REMARK 500    ASN A 189       16.93     58.12                                   
REMARK 500    SER A 226       40.02    -89.72                                   
REMARK 500    GLU A 356       -2.23     85.99                                   
REMARK 500    ASP A 370      -55.23   -136.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PG4 A  605                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 59K A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 613                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DDA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DDB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DDD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DDE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DDF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DB1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DB0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DB2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DB3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DDC   RELATED DB: PDB                                   
DBREF  5DD9 A    1   459  UNP    O00255   MEN1_HUMAN       1    459             
DBREF  5DD9 A  537   593  UNP    O00255   MEN1_HUMAN     537    593             
SEQADV 5DD9 GLY A   -4  UNP  O00255              EXPRESSION TAG                 
SEQADV 5DD9 GLY A   -3  UNP  O00255              EXPRESSION TAG                 
SEQADV 5DD9 SER A   -2  UNP  O00255              EXPRESSION TAG                 
SEQADV 5DD9 SER A   -1  UNP  O00255              EXPRESSION TAG                 
SEQADV 5DD9 SER A    0  UNP  O00255              EXPRESSION TAG                 
SEQADV 5DD9     A       UNP  O00255    ILE    54 DELETION                       
SEQADV 5DD9     A       UNP  O00255    PRO    55 DELETION                       
SEQADV 5DD9     A       UNP  O00255    THR    56 DELETION                       
SEQADV 5DD9     A       UNP  O00255    ASN    57 DELETION                       
SEQADV 5DD9     A       UNP  O00255    VAL    58 DELETION                       
SEQADV 5DD9     A       UNP  O00255    PRO    59 DELETION                       
SEQADV 5DD9     A       UNP  O00255    GLU    60 DELETION                       
SEQADV 5DD9     A       UNP  O00255    LEU    61 DELETION                       
SEQADV 5DD9     A       UNP  O00255    THR    62 DELETION                       
SEQADV 5DD9     A       UNP  O00255    PHE    63 DELETION                       
SEQADV 5DD9     A       UNP  O00255    GLN    64 DELETION                       
SEQADV 5DD9     A       UNP  O00255    PRO    65 DELETION                       
SEQADV 5DD9     A       UNP  O00255    SER    66 DELETION                       
SEQADV 5DD9     A       UNP  O00255    PRO    67 DELETION                       
SEQADV 5DD9     A       UNP  O00255    ALA    68 DELETION                       
SEQADV 5DD9     A       UNP  O00255    PRO    69 DELETION                       
SEQADV 5DD9     A       UNP  O00255    ASP    70 DELETION                       
SEQADV 5DD9     A       UNP  O00255    PRO    71 DELETION                       
SEQADV 5DD9     A       UNP  O00255    PRO    72 DELETION                       
SEQADV 5DD9     A       UNP  O00255    GLY    73 DELETION                       
SEQADV 5DD9     A       UNP  O00255    GLU   387 DELETION                       
SEQADV 5DD9     A       UNP  O00255    GLU   388 DELETION                       
SEQADV 5DD9     A       UNP  O00255    ARG   389 DELETION                       
SEQADV 5DD9     A       UNP  O00255    PRO   390 DELETION                       
SEQADV 5DD9     A       UNP  O00255    GLY   391 DELETION                       
SEQADV 5DD9     A       UNP  O00255    GLU   392 DELETION                       
SEQADV 5DD9     A       UNP  O00255    GLN   393 DELETION                       
SEQADV 5DD9     A       UNP  O00255    SER   394 DELETION                       
SEQADV 5DD9     A       UNP  O00255    GLN   395 DELETION                       
SEQADV 5DD9     A       UNP  O00255    GLY   396 DELETION                       
SEQADV 5DD9     A       UNP  O00255    THR   397 DELETION                       
SEQADV 5DD9     A       UNP  O00255    GLN   398 DELETION                       
SEQADV 5DD9 ALA A  541  UNP  O00255    THR   541 ENGINEERED MUTATION            
SEQRES   1 A  489  GLY GLY SER SER SER MET GLY LEU LYS ALA ALA GLN LYS          
SEQRES   2 A  489  THR LEU PHE PRO LEU ARG SER ILE ASP ASP VAL VAL ARG          
SEQRES   3 A  489  LEU PHE ALA ALA GLU LEU GLY ARG GLU GLU PRO ASP LEU          
SEQRES   4 A  489  VAL LEU LEU SER LEU VAL LEU GLY PHE VAL GLU HIS PHE          
SEQRES   5 A  489  LEU ALA VAL ASN ARG VAL GLY LEU THR TYR PHE PRO VAL          
SEQRES   6 A  489  ALA ASP LEU SER ILE ILE ALA ALA LEU TYR ALA ARG PHE          
SEQRES   7 A  489  THR ALA GLN ILE ARG GLY ALA VAL ASP LEU SER LEU TYR          
SEQRES   8 A  489  PRO ARG GLU GLY GLY VAL SER SER ARG GLU LEU VAL LYS          
SEQRES   9 A  489  LYS VAL SER ASP VAL ILE TRP ASN SER LEU SER ARG SER          
SEQRES  10 A  489  TYR PHE LYS ASP ARG ALA HIS ILE GLN SER LEU PHE SER          
SEQRES  11 A  489  PHE ILE THR GLY THR LYS LEU ASP SER SER GLY VAL ALA          
SEQRES  12 A  489  PHE ALA VAL VAL GLY ALA CYS GLN ALA LEU GLY LEU ARG          
SEQRES  13 A  489  ASP VAL HIS LEU ALA LEU SER GLU ASP HIS ALA TRP VAL          
SEQRES  14 A  489  VAL PHE GLY PRO ASN GLY GLU GLN THR ALA GLU VAL THR          
SEQRES  15 A  489  TRP HIS GLY LYS GLY ASN GLU ASP ARG ARG GLY GLN THR          
SEQRES  16 A  489  VAL ASN ALA GLY VAL ALA GLU ARG SER TRP LEU TYR LEU          
SEQRES  17 A  489  LYS GLY SER TYR MET ARG CYS ASP ARG LYS MET GLU VAL          
SEQRES  18 A  489  ALA PHE MET VAL CYS ALA ILE ASN PRO SER ILE ASP LEU          
SEQRES  19 A  489  HIS THR ASP SER LEU GLU LEU LEU GLN LEU GLN GLN LYS          
SEQRES  20 A  489  LEU LEU TRP LEU LEU TYR ASP LEU GLY HIS LEU GLU ARG          
SEQRES  21 A  489  TYR PRO MET ALA LEU GLY ASN LEU ALA ASP LEU GLU GLU          
SEQRES  22 A  489  LEU GLU PRO THR PRO GLY ARG PRO ASP PRO LEU THR LEU          
SEQRES  23 A  489  TYR HIS LYS GLY ILE ALA SER ALA LYS THR TYR TYR ARG          
SEQRES  24 A  489  ASP GLU HIS ILE TYR PRO TYR MET TYR LEU ALA GLY TYR          
SEQRES  25 A  489  HIS CYS ARG ASN ARG ASN VAL ARG GLU ALA LEU GLN ALA          
SEQRES  26 A  489  TRP ALA ASP THR ALA THR VAL ILE GLN ASP TYR ASN TYR          
SEQRES  27 A  489  CYS ARG GLU ASP GLU GLU ILE TYR LYS GLU PHE PHE GLU          
SEQRES  28 A  489  VAL ALA ASN ASP VAL ILE PRO ASN LEU LEU LYS GLU ALA          
SEQRES  29 A  489  ALA SER LEU LEU GLU ALA GLY SER GLN GLY SER ALA LEU          
SEQRES  30 A  489  GLN ASP PRO GLU CYS PHE ALA HIS LEU LEU ARG PHE TYR          
SEQRES  31 A  489  ASP GLY ILE CYS LYS TRP GLU GLU GLY SER PRO THR PRO          
SEQRES  32 A  489  VAL LEU HIS VAL GLY TRP ALA THR PHE LEU VAL GLN SER          
SEQRES  33 A  489  LEU GLY ARG PHE GLU GLY GLN VAL ARG GLN LYS VAL ARG          
SEQRES  34 A  489  ILE VAL SER VAL PRO ALA PRO ALA ALA SER PRO PRO PRO          
SEQRES  35 A  489  GLU GLY PRO VAL LEU THR PHE GLN SER GLU LYS MET LYS          
SEQRES  36 A  489  GLY MET LYS GLU LEU LEU VAL ALA THR LYS ILE ASN SER          
SEQRES  37 A  489  SER ALA ILE LYS LEU GLN LEU THR ALA GLN SER GLN VAL          
SEQRES  38 A  489  GLN MET LYS LYS GLN LYS VAL SER                              
HET    59K  A 601      26                                                       
HET    DMS  A 602       4                                                       
HET    DMS  A 603       4                                                       
HET    PG4  A 604      13                                                       
HET    PG4  A 605       8                                                       
HET    PGE  A 606      10                                                       
HET    DMS  A 607       4                                                       
HET    SO4  A 608       5                                                       
HET    SO4  A 609       5                                                       
HET    SO4  A 610       5                                                       
HET    SO4  A 611       5                                                       
HET    DMS  A 612       4                                                       
HET    DMS  A 613       4                                                       
HETNAM     59K 4-[4-(5-METHYL-1,3,4-THIADIAZOL-2-YL)PIPERAZIN-1-YL]-6-          
HETNAM   2 59K  (2,2,2-TRIFLUOROETHYL)THIENO[2,3-D]PYRIMIDINE                   
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  59K    C15 H15 F3 N6 S2                                             
FORMUL   3  DMS    5(C2 H6 O S)                                                 
FORMUL   5  PG4    2(C8 H18 O5)                                                 
FORMUL   7  PGE    C6 H14 O4                                                    
FORMUL   9  SO4    4(O4 S 2-)                                                   
FORMUL  15  HOH   *493(H2 O)                                                    
HELIX    1 AA1 LYS A    4  THR A    9  1                                   6    
HELIX    2 AA2 SER A   15  GLY A   28  1                                  14    
HELIX    3 AA3 ASP A   33  VAL A   50  1                                  18    
HELIX    4 AA4 ASP A   82  VAL A  101  1                                  20    
HELIX    5 AA5 ASP A  102  TYR A  106  5                                   5    
HELIX    6 AA6 ARG A  108  VAL A  112  5                                   5    
HELIX    7 AA7 SER A  114  SER A  128  1                                  15    
HELIX    8 AA8 SER A  142  THR A  150  1                                   9    
HELIX    9 AA9 ASP A  153  LEU A  168  1                                  16    
HELIX   10 AB1 GLY A  187  GLU A  191  5                                   5    
HELIX   11 AB2 VAL A  211  GLU A  217  1                                   7    
HELIX   12 AB3 SER A  219  SER A  226  5                                   8    
HELIX   13 AB4 ASP A  231  ALA A  242  1                                  12    
HELIX   14 AB5 SER A  253  LEU A  270  1                                  18    
HELIX   15 AB6 TYR A  276  GLU A  290  1                                  15    
HELIX   16 AB7 ASP A  297  TYR A  313  1                                  17    
HELIX   17 AB8 ILE A  318  ASN A  331  1                                  14    
HELIX   18 AB9 ASN A  333  GLN A  349  1                                  17    
HELIX   19 AC1 ASP A  357  ASP A  370  1                                  14    
HELIX   20 AC2 ASP A  370  ALA A  385  1                                  16    
HELIX   21 AC3 SER A  402  GLN A  405  5                                   4    
HELIX   22 AC4 ASP A  406  GLU A  425  1                                  20    
HELIX   23 AC5 HIS A  433  ARG A  446  1                                  14    
HELIX   24 AC6 GLU A  448  GLN A  453  1                                   6    
HELIX   25 AC7 SER A  555  LYS A  562  1                                   8    
HELIX   26 AC8 GLU A  563  ALA A  567  5                                   5    
HELIX   27 AC9 ASN A  571  ALA A  581  1                                  11    
SHEET    1 AA1 4 GLN A 192  ALA A 194  0                                        
SHEET    2 AA1 4 ALA A 182  PHE A 186 -1  N  VAL A 184   O  ALA A 194           
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 SER A 246  ASP A 248  0                                        
SHEET    2 AA2 2 THR A 251  ASP A 252 -1  O  THR A 251   N  ILE A 247           
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           
CISPEP   1 PHE A   11    PRO A   12          0         3.98                     
SITE     1 AC1 17 SER A 155  LEU A 177  SER A 178  ASP A 180                    
SITE     2 AC1 17 HIS A 181  ALA A 182  PHE A 238  CYS A 241                    
SITE     3 AC1 17 TYR A 276  MET A 278  ASN A 282  TYR A 319                    
SITE     4 AC1 17 TYR A 323  DMS A 602  DMS A 607  HOH A 761                    
SITE     5 AC1 17 HOH A 800                                                     
SITE     1 AC2  6 SER A 155  PHE A 238  59K A 601  DMS A 607                    
SITE     2 AC2  6 HOH A 702  HOH A 996                                          
SITE     1 AC3  5 PHE A  47  GLY A 386  GLN A 400  HOH A1034                    
SITE     2 AC3  5 HOH A1137                                                     
SITE     1 AC4  6 LEU A  75  THR A  76  TYR A 361  PHE A 365                    
SITE     2 AC4  6 HOH A 754  HOH A 806                                          
SITE     1 AC5  5 TYR A 268  ASP A 269  GLU A 274  LYS A 304                    
SITE     2 AC5  5 HOH A1013                                                     
SITE     1 AC6  4 TRP A 126  LEU A 129  LYS A 135  TRP A 198                    
SITE     1 AC7  6 SER A 155  PHE A 238  ALA A 242  59K A 601                    
SITE     2 AC7  6 DMS A 602  HOH A 702                                          
SITE     1 AC8  4 TYR A 133  PHE A 134  ARG A 137  ARG A 332                    
SITE     1 AC9  3 PRO A  12  ARG A  14  HOH A 760                               
SITE     1 AD1  3 LYS A 377  ARG A 446  HOH A1020                               
SITE     1 AD2  6 ARG A 332  VAL A 334  ARG A 335  GLY A 401                    
SITE     2 AD2  6 ALA A 403  HOH A 938                                          
SITE     1 AD3  3 SER A 130  ARG A 131  ASN A 374                               
SITE     1 AD4  6 VAL A 185  GLY A 190  GLU A 191  TYR A 227                    
SITE     2 AD4  6 ARG A 229  SER A 583                                          
CRYST1   48.830   80.230  125.228  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      0.020479  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012464  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007985        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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