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Database: PDB
Entry: 6BXY
LinkDB: 6BXY
Original site: 6BXY 
HEADER    PROTEIN BINDING, TRANSCRIPTION          19-DEC-17   6BXY              
TITLE     MENIN IN COMPLEX WITH MI-1481                                         
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   2   12-JUN-19 6BXY    1       JRNL                                     
REVDAT   1   28-NOV-18 6BXY    0                                                
JRNL        AUTH   D.BORKIN,S.KLOSSOWSKI,J.POLLOCK,H.MIAO,B.M.LINHARES,         
JRNL        AUTH 2 K.KEMPINSKA,Z.JIN,T.PUROHIT,B.WEN,M.HE,D.SUN,T.CIERPICKI,    
JRNL        AUTH 3 J.GREMBECKA                                                  
JRNL        TITL   COMPLEXITY OF BLOCKING BIVALENT PROTEIN-PROTEIN              
JRNL        TITL 2 INTERACTIONS: DEVELOPMENT OF A HIGHLY POTENT INHIBITOR OF    
JRNL        TITL 3 THE MENIN-MIXED-LINEAGE LEUKEMIA INTERACTION.                
JRNL        REF    J.MED.CHEM.                   V.  61  4832 2018              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   29738674                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.8B00071                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.82 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) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.27                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 42152                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2121                            
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  1.8624 -  1.8201    0.95     2498   132  0.2400 0.3300        
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)     : 0.207            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.730           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.59                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.45                          
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      :  0.015           3859                                  
REMARK   3   ANGLE     :  1.344           5245                                  
REMARK   3   CHIRALITY :  0.080            582                                  
REMARK   3   PLANARITY :  0.009            662                                  
REMARK   3   DIHEDRAL  :  5.297           3110                                  
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): -11.5022 -11.8471 -13.2329              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0714 T22:   0.1446                                     
REMARK   3      T33:   0.1148 T12:   0.0218                                     
REMARK   3      T13:   0.0113 T23:   0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2535 L22:   1.8547                                     
REMARK   3      L33:   1.1184 L12:   0.3108                                     
REMARK   3      L13:   0.1244 L23:   0.9182                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0095 S12:  -0.0443 S13:   0.0371                       
REMARK   3      S21:  -0.0754 S22:  -0.0725 S23:   0.1174                       
REMARK   3      S31:  -0.0766 S32:  -0.0609 S33:   0.0297                       
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 6BXY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000231756.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-APR-15                          
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 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42152                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
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     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67700                            
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   (%): 38.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
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       23.65950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.17050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.26950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.17050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.65950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.26950            
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     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     LEU A  75    CG   CD1  CD2                                       
REMARK 470     ARG A 137    CZ   NH1  NH2                                       
REMARK 470     LYS A 201    CG   CD   CE   NZ                                   
REMARK 470     ASN A 203    CG   OD1  ND2                                       
REMARK 470     GLU A 204    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 205    CG   OD1  OD2                                       
REMARK 470     LYS A 304    CG   CD   CE   NZ                                   
REMARK 470     ARG A 355    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 358    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 362    CG   CD   CE   NZ                                   
REMARK 470     GLU A 384    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 424    CG   CD   OE1  OE2                                  
REMARK 470     SER A 427    OG                                                  
REMARK 470     THR A 429    OG1  CG2                                            
REMARK 470     HIS A 433    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL A 434    CG1  CG2                                            
REMARK 470     ARG A 456    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 569    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    HOH A   984     O    HOH A   986              1.83            
REMARK 500   O    VAL A   434     N    TRP A   436              1.87            
REMARK 500   O    HOH A   746     O    HOH A   916              1.89            
REMARK 500   O    HOH A   906     O    HOH A   969              1.95            
REMARK 500   OE1  GLU A   563     O    HOH A   701              1.97            
REMARK 500   O    HOH A   822     O    HOH A   845              1.99            
REMARK 500   OD2  ASP A   350     O    HOH A   702              2.10            
REMARK 500   OE2  GLU A   316     O    HOH A   703              2.16            
REMARK 500   O    HOH A   864     O    HOH A   972              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG A    92     OG   SER A   381     4545     2.03            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 409   CB    CYS A 409   SG     -0.097                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 177   CB  -  CG  -  CD1 ANGL. DEV. = -11.7 DEGREES          
REMARK 500    ARG A 218   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
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    SER A 178     -166.39   -103.05                                   
REMARK 500    ASP A 180       22.11   -146.83                                   
REMARK 500    ASN A 203     -132.42    -97.97                                   
REMARK 500    ASP A 205       63.45   -103.10                                   
REMARK 500    SER A 226       48.69    -94.30                                   
REMARK 500    ASP A 370      -54.77   -122.38                                   
REMARK 500    SER A 427     -169.80    -77.08                                   
REMARK 500    PRO A 428      -63.16    -96.04                                   
REMARK 500    PRO A 430     -121.45    -70.09                                   
REMARK 500    VAL A 434      178.90     92.05                                   
REMARK 500    ALA A 581       19.40     58.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS A  433     VAL A  434                  147.60                    
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 987        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH A 988        DISTANCE =  7.49 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EEV 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 DMS 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 PG4 A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 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 EDO A 610                 
DBREF  6BXY A   -4   593  PDB    6BXY     6BXY            -4    593             
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    EEV  A 601      42                                                       
HET    DMS  A 602       4                                                       
HET    DMS  A 603       4                                                       
HET    DMS  A 604       4                                                       
HET    PG4  A 605      13                                                       
HET    PG4  A 606      13                                                       
HET    SO4  A 607       5                                                       
HET    SO4  A 608       5                                                       
HET    SO4  A 609       5                                                       
HET    EDO  A 610       4                                                       
HETNAM     EEV 4-METHYL-1-{[(2S)-5-OXOMORPHOLIN-2-YL]METHYL}-5-[(4-             
HETNAM   2 EEV  {[6-(2,2,2-TRIFLUOROETHYL)THIENO[2,3-D]PYRIMIDIN-4-             
HETNAM   3 EEV  YL]AMINO}PIPERIDIN-1-YL)METHYL]-1H-INDOLE-2-                    
HETNAM   4 EEV  CARBONITRILE                                                    
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  EEV    C29 H30 F3 N7 O2 S                                           
FORMUL   3  DMS    3(C2 H6 O S)                                                 
FORMUL   6  PG4    2(C8 H18 O5)                                                 
FORMUL   8  SO4    3(O4 S 2-)                                                   
FORMUL  11  EDO    C2 H6 O2                                                     
FORMUL  12  HOH   *288(H2 O)                                                    
HELIX    1 AA1 LYS A    4  LYS A    8  5                                   5    
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 SER A  114  LEU A  129  1                                  16    
HELIX    7 AA7 SER A  142  THR A  150  1                                   9    
HELIX    8 AA8 ASP A  153  LEU A  168  1                                  16    
HELIX    9 AA9 GLY A  187  GLU A  191  5                                   5    
HELIX   10 AB1 VAL A  211  GLU A  217  1                                   7    
HELIX   11 AB2 SER A  219  SER A  226  5                                   8    
HELIX   12 AB3 ASP A  231  ALA A  242  1                                  12    
HELIX   13 AB4 SER A  253  LEU A  270  1                                  18    
HELIX   14 AB5 TYR A  276  GLU A  290  1                                  15    
HELIX   15 AB6 ASP A  297  TYR A  313  1                                  17    
HELIX   16 AB7 ILE A  318  ASN A  331  1                                  14    
HELIX   17 AB8 ASN A  333  GLN A  349  1                                  17    
HELIX   18 AB9 CYS A  354  GLU A  356  5                                   3    
HELIX   19 AC1 ASP A  357  ASP A  370  1                                  14    
HELIX   20 AC2 ASP A  370  GLY A  386  1                                  17    
HELIX   21 AC3 SER A  402  GLN A  405  5                                   4    
HELIX   22 AC4 ASP A  406  GLY A  426  1                                  21    
HELIX   23 AC5 GLY A  435  ARG A  446  1                                  12    
HELIX   24 AC6 GLU A  448  GLN A  453  1                                   6    
HELIX   25 AC7 SER A  555  GLY A  560  1                                   6    
HELIX   26 AC8 MET A  561  ALA A  567  5                                   7    
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  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         3.86                     
CISPEP   2 PHE A   11    PRO A   12          0         3.07                     
CISPEP   3 VAL A  460    PRO A  461          0        -1.37                     
SITE     1 AC1 19 SER A 155  LEU A 177  SER A 178  ASP A 180                    
SITE     2 AC1 19 HIS A 181  ALA A 182  PHE A 238  TYR A 276                    
SITE     3 AC1 19 MET A 278  MET A 322  TYR A 323  TRP A 341                    
SITE     4 AC1 19 GLU A 363  GLU A 366  DMS A 602  PG4 A 606                    
SITE     5 AC1 19 HOH A 783  HOH A 792  HOH A 846                               
SITE     1 AC2  2 SER A 155  EEV A 601                                          
SITE     1 AC3  5 PHE A  43  PHE A  47  GLY A  74  PRO A  79                    
SITE     2 AC3  5 VAL A  80                                                     
SITE     1 AC4  8 VAL A 434  GLY A 435  TRP A 436  ALA A 437                    
SITE     2 AC4  8 THR A 438  HOH A 805  HOH A 807  HOH A 820                    
SITE     1 AC5  7 TYR A  77  PHE A 365  ASN A 369  GLY A 435                    
SITE     2 AC5  7 PHE A 439  HOH A 794  HOH A 892                               
SITE     1 AC6  5 GLY A 326  EEV A 601  HOH A 767  HOH A 880                    
SITE     2 AC6  5 HOH A 917                                                     
SITE     1 AC7  5 TYR A 133  PHE A 134  ARG A 137  LYS A 151                    
SITE     2 AC7  5 ARG A 332                                                     
SITE     1 AC8  3 ARG A 446  HOH A 711  HOH A 743                               
SITE     1 AC9  6 ARG A 108  GLY A 111  GLY A 169  ARG A 171                    
SITE     2 AC9  6 HOH A 708  HOH A 777                                          
SITE     1 AD1  4 LYS A 135  TRP A 198  GLY A 294  HOH A 869                    
CRYST1   47.319   80.539  122.341  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      0.021133  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012416  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008174        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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