GenomeNet

Database: PDB
Entry: 4GQ6
LinkDB: 4GQ6
Original site: 4GQ6 
HEADER    TRANSCRIPTION/TRANSCRIPTION INHIBITOR   22-AUG-12   4GQ6              
TITLE     HUMAN MENIN IN COMPLEX WITH MLL PEPTIDE                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MENIN;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE MLL;                    
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: UNP RESIDUES 6-15;                                         
COMPND  10 SYNONYM: ALL-1, CXXC-TYPE ZINC FINGER PROTEIN 7, LYSINE N-           
COMPND  11 METHYLTRANSFERASE 2A, KMT2A, TRITHORAX-LIKE PROTEIN, ZINC FINGER     
COMPND  12 PROTEIN HRX, MLL CLEAVAGE PRODUCT N320, N-TERMINAL CLEAVAGE PRODUCT  
COMPND  13 OF 320 KDA, P320, MLL CLEAVAGE PRODUCT C180, C-TERMINAL CLEAVAGE     
COMPND  14 PRODUCT OF 180 KDA, P180;                                            
COMPND  15 EC: 2.1.1.43;                                                        
COMPND  16 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;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    TUMOR SUPPRESSOR, NUCLEUS, TRANSCRIPTION-TRANSCRIPTION INHIBITOR      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SHI,M.J.MURAI,S.HE,G.L.LUND,T.HARTLEY,T.PUROHIT,G.REDDY,M.CHRUSZCZ, 
AUTHOR   2 J.GREMBECKA,T.CIERPICKI                                              
REVDAT   4   16-APR-14 4GQ6    1       REMARK                                   
REVDAT   3   02-JAN-13 4GQ6    1       JRNL                                     
REVDAT   2   10-OCT-12 4GQ6    1       TITLE                                    
REVDAT   1   19-SEP-12 4GQ6    0                                                
JRNL        AUTH   A.SHI,M.J.MURAI,S.HE,G.LUND,T.HARTLEY,T.PUROHIT,G.REDDY,     
JRNL        AUTH 2 M.CHRUSZCZ,J.GREMBECKA,T.CIERPICKI                           
JRNL        TITL   STRUCTURAL INSIGHTS INTO INHIBITION OF THE BIVALENT          
JRNL        TITL 2 MENIN-MLL INTERACTION BY SMALL MOLECULES IN LEUKEMIA.        
JRNL        REF    BLOOD                         V. 120  4461 2012              
JRNL        REFN                   ISSN 0006-4971                               
JRNL        PMID   22936661                                                     
JRNL        DOI    10.1182/BLOOD-2012-05-429274                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 66808                          
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3552                            
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) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4565                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.05                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2150                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 259                          
REMARK   3   BIN FREE R VALUE                    : 0.2500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3769                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 479                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.47                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.51000                                              
REMARK   3    B22 (A**2) : -0.58000                                             
REMARK   3    B33 (A**2) : -0.93000                                             
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): 0.075         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.076         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.049         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.847         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3928 ; 0.020 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  2662 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5331 ; 1.925 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6468 ; 1.081 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   490 ; 5.817 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   180 ;32.444 ;23.444       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   652 ;13.204 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;16.983 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   594 ; 0.122 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4355 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   835 ; 0.001 ; 0.020       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
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  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3239  -3.6032   4.1176              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0544 T22:   0.0410                                     
REMARK   3      T33:   0.0352 T12:   0.0097                                     
REMARK   3      T13:  -0.0053 T23:  -0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6776 L22:   0.2842                                     
REMARK   3      L33:   1.0228 L12:  -0.0615                                     
REMARK   3      L13:   0.0463 L23:   0.3408                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0238 S12:   0.1137 S13:  -0.0346                       
REMARK   3      S21:   0.0141 S22:  -0.0209 S23:   0.0114                       
REMARK   3      S31:   0.1292 S32:   0.0008 S33:  -0.0029                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   212        A   228                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0845   9.0014  25.0214              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0568 T22:   0.0297                                     
REMARK   3      T33:   0.0395 T12:   0.0095                                     
REMARK   3      T13:  -0.0005 T23:  -0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2344 L22:   2.7695                                     
REMARK   3      L33:   2.5213 L12:  -0.8915                                     
REMARK   3      L13:   0.8198 L23:   0.0024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0416 S12:  -0.0233 S13:   0.0877                       
REMARK   3      S21:   0.1181 S22:   0.0040 S23:  -0.0570                       
REMARK   3      S31:   0.0933 S32:   0.0657 S33:   0.0376                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   229        A   332                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.5971   8.7770  11.6963              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0113 T22:   0.0648                                     
REMARK   3      T33:   0.0603 T12:  -0.0106                                     
REMARK   3      T13:   0.0093 T23:  -0.0290                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6469 L22:   0.8182                                     
REMARK   3      L33:   0.7911 L12:  -0.4556                                     
REMARK   3      L13:   0.1826 L23:   0.2746                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0479 S12:   0.0736 S13:   0.0107                       
REMARK   3      S21:  -0.0135 S22:  -0.1420 S23:   0.1056                       
REMARK   3      S31:   0.0218 S32:  -0.1226 S33:   0.0942                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   333        A   554                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.9712  30.4659  24.2518              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0078 T22:   0.0401                                     
REMARK   3      T33:   0.0477 T12:  -0.0008                                     
REMARK   3      T13:  -0.0056 T23:  -0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5621 L22:   1.0332                                     
REMARK   3      L33:   0.5883 L12:  -0.5390                                     
REMARK   3      L13:  -0.0893 L23:   0.1058                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0095 S12:   0.0568 S13:  -0.0374                       
REMARK   3      S21:   0.0365 S22:  -0.0273 S23:   0.0401                       
REMARK   3      S31:  -0.0170 S32:  -0.0434 S33:   0.0368                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   555        A   587                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.8877  40.0286  31.5662              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0967 T22:   0.0423                                     
REMARK   3      T33:   0.0754 T12:  -0.0185                                     
REMARK   3      T13:  -0.0372 T23:  -0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7826 L22:   1.6357                                     
REMARK   3      L33:   0.1302 L12:   1.2319                                     
REMARK   3      L13:   0.4352 L23:   0.4309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1125 S12:   0.0034 S13:   0.1721                       
REMARK   3      S21:  -0.2352 S22:   0.0583 S23:   0.1619                       
REMARK   3      S31:  -0.0475 S32:   0.0142 S33:   0.0541                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     4        B    15                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.1754  14.8851   6.5582              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1520 T22:   0.2021                                     
REMARK   3      T33:   0.1748 T12:   0.0077                                     
REMARK   3      T13:   0.0215 T23:   0.0869                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0476 L22:   3.9505                                     
REMARK   3      L33:   6.5139 L12:  -0.4238                                     
REMARK   3      L13:  -0.5445 L23:   5.0727                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0859 S12:   0.0226 S13:   0.0224                       
REMARK   3      S21:  -0.5276 S22:  -0.0073 S23:  -0.0824                       
REMARK   3      S31:  -0.6824 S32:  -0.0448 S33:  -0.0786                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4GQ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB074499.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70700                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
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     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.58300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M HEPES 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), NBM1 PEPTIDE, 50MM      
REMARK 280  NACL, AND 1MM TCEP. PRIOR TO DATA COLLECTION, CRYSTALS WERE         
REMARK 280  TRANSFERRED INTO A CRYO-SOLUTION CONTAINING 20% PEG550 MME AND      
REMARK 280  FLASH-FROZEN IN LIQUID NITROGEN, 1:1 MOLAR RATIO WITH MBM1          
REMARK 280  PEPTIDE, 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       24.30050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.27550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.02800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.27550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.30050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.02800            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     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     LYS A   589                                                      
REMARK 465     GLN A   590                                                      
REMARK 465     LYS A   591                                                      
REMARK 465     VAL A   592                                                      
REMARK 465     SER A   593                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 131    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 355    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 366    CD   OE1  OE2                                       
REMARK 470     VAL A 460    CG1  CG2                                            
REMARK 470     GLU A 563    CG   CD   OE1  OE2                                  
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: 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      -60.71   -155.24                                   
REMARK 500    ASP A 180       12.00   -147.47                                   
REMARK 500    ASN A 189       13.97     56.35                                   
REMARK 500    SER A 226       47.51    -92.58                                   
REMARK 500    ASP A 370      -56.81   -135.02                                   
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     1PE A  604                                                       
REMARK 610     1PE 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 SO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF HISTONE-LYSINE N-      
REMARK 800  METHYLTRANSFERASE MLL                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GPQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GQ3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GQ4   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CRYSTALLIZED SEQUENCE CORRESPONDING TO THE HUMAN MENIN ISOFORM 2 
DBREF  4GQ6 A    1   593  UNP    O00255   MEN1_HUMAN       1    593             
DBREF  4GQ6 B    6    15  UNP    Q03164   MLL1_HUMAN       6     15             
SEQADV 4GQ6 GLY A   -4  UNP  O00255              EXPRESSION TAG                 
SEQADV 4GQ6 GLY A   -3  UNP  O00255              EXPRESSION TAG                 
SEQADV 4GQ6 SER A   -2  UNP  O00255              EXPRESSION TAG                 
SEQADV 4GQ6 SER A   -1  UNP  O00255              EXPRESSION TAG                 
SEQADV 4GQ6 SER A    0  UNP  O00255              EXPRESSION TAG                 
SEQADV 4GQ6     A       UNP  O00255    ILE    54 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO    55 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    THR    56 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ASN    57 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    VAL    58 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO    59 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU    60 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    LEU    61 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    THR    62 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PHE    63 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLN    64 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO    65 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    SER    66 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO    67 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ALA    68 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO    69 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ASP    70 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO    71 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO    72 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY    73 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   387 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   388 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ARG   389 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   390 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   391 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   392 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLN   393 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    SER   394 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLN   395 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   396 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    THR   397 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLN   398 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ARG   460 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   461 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ALA   462 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   463 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ALA   464 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ALA   465 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   466 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ALA   467 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   468 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   469 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   470 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    TRP   471 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   472 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   473 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   474 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ALA   475 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ARG   476 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   477 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   478 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ARG   479 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ARG   480 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ARG   481 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   482 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   483 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ARG   484 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ARG   485 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   486 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    SER   487 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    LYS   488 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   489 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   490 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   491 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   492 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   493 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   494 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   495 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    LYS   496 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    LYS   497 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   498 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ALA   499 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    LEU   500 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ASP   501 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    LYS   502 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   503 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    LEU   504 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   505 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    THR   506 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   507 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLN   508 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   509 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ALA   510 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    VAL   511 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    SER   512 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   513 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   514 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   515 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ARG   516 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    LYS   517 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   518 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   519 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   520 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    THR   521 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    VAL   522 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ALA   523 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   524 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    THR   525 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ALA   526 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ARG   527 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   528 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    PRO   529 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLU   530 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   531 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLY   532 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    SER   533 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    THR   534 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    ALA   535 DELETION                       
SEQADV 4GQ6     A       UNP  O00255    GLN   536 DELETION                       
SEQADV 4GQ6 ALA A  541  UNP  O00255    THR   541 ENGINEERED MUTATION            
SEQADV 4GQ6 SER B    4  UNP  Q03164              EXPRESSION TAG                 
SEQADV 4GQ6 ALA B    5  UNP  Q03164              EXPRESSION TAG                 
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                              
SEQRES   1 B   12  SER ALA ARG TRP ARG PHE PRO ALA ARG PRO GLY THR              
HET    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    1PE  A 604      11                                                       
HET    1PE  A 605       8                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETSYN     1PE PEG400                                                           
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   6  1PE    2(C10 H22 O6)                                                
FORMUL   8  HOH   *479(H2 O)                                                    
HELIX    1   1 LYS A    4  THR A    9  1                                   6    
HELIX    2   2 SER A   15  GLY A   28  1                                  14    
HELIX    3   3 ASP A   33  VAL A   50  1                                  18    
HELIX    4   4 ASP A   82  VAL A  101  1                                  20    
HELIX    5   5 ASP A  102  TYR A  106  5                                   5    
HELIX    6   6 ARG A  108  VAL A  112  5                                   5    
HELIX    7   7 SER A  114  LEU A  129  1                                  16    
HELIX    8   8 SER A  142  THR A  150  1                                   9    
HELIX    9   9 ASP A  153  LEU A  168  1                                  16    
HELIX   10  10 GLY A  187  GLU A  191  5                                   5    
HELIX   11  11 VAL A  211  GLU A  217  1                                   7    
HELIX   12  12 SER A  219  SER A  226  5                                   8    
HELIX   13  13 ASP A  231  ALA A  242  1                                  12    
HELIX   14  14 SER A  253  LEU A  270  1                                  18    
HELIX   15  15 TYR A  276  GLU A  290  1                                  15    
HELIX   16  16 ASP A  297  TYR A  313  1                                  17    
HELIX   17  17 ILE A  318  ASN A  331  1                                  14    
HELIX   18  18 ASN A  333  GLN A  349  1                                  17    
HELIX   19  19 ASP A  357  ASP A  370  1                                  14    
HELIX   20  20 ASP A  370  ALA A  385  1                                  16    
HELIX   21  21 SER A  402  GLN A  405  5                                   4    
HELIX   22  22 ASP A  406  GLU A  425  1                                  20    
HELIX   23  23 HIS A  433  ARG A  446  1                                  14    
HELIX   24  24 GLU A  448  GLN A  453  1                                   6    
HELIX   25  25 SER A  555  LYS A  562  1                                   8    
HELIX   26  26 GLU A  563  VAL A  566  5                                   4    
HELIX   27  27 ASN A  571  THR A  580  1                                  10    
SHEET    1   A 4 GLN A 192  ALA A 194  0                                        
SHEET    2   A 4 ALA A 182  PHE A 186 -1  N  VAL A 184   O  ALA A 194           
SHEET    3   A 4 HIS A 174  LEU A 177 -1  N  ALA A 176   O  TRP A 183           
SHEET    4   A 4 MET A 228  ARG A 229 -1  O  MET A 228   N  LEU A 177           
SHEET    1   B 2 SER A 246  ASP A 248  0                                        
SHEET    2   B 2 THR A 251  ASP A 252 -1  O  THR A 251   N  ILE A 247           
SHEET    1   C 2 ARG A 456  ILE A 457  0                                        
SHEET    2   C 2 VAL A 550  LEU A 551  1  O  LEU A 551   N  ARG A 456           
CISPEP   1 PHE A   11    PRO A   12          0         4.15                     
SITE     1 AC1  5 TYR A 133  PHE A 134  ARG A 137  LYS A 151                    
SITE     2 AC1  5 ARG A 332                                                     
SITE     1 AC2  5 ARG A 332  VAL A 334  ARG A 335  ALA A 403                    
SITE     2 AC2  5 HOH A1043                                                     
SITE     1 AC3  5 ARG A 108  GLY A 111  GLY A 169  ARG A 171                    
SITE     2 AC3  5 HOH A1104                                                     
SITE     1 AC4  8 LEU A  75  THR A  76  TYR A 361  LYS A 362                    
SITE     2 AC4  8 PHE A 365  HOH A 729  HOH A 953  HOH A1161                    
SITE     1 AC5  4 TRP A 126  SER A 130  ARG A 131  LYS A 135                    
SITE     1 AC6 28 ASP A 136  ARG A 137  ALA A 138  ASP A 153                    
SITE     2 AC6 28 SER A 154  SER A 155  GLU A 179  ASP A 180                    
SITE     3 AC6 28 HIS A 181  PHE A 238  ASN A 244  MET A 278                    
SITE     4 AC6 28 GLU A 290  TYR A 319  TYR A 323  GLU A 359                    
SITE     5 AC6 28 GLU A 363  HOH A 724  HOH A 820  HOH A1044                    
SITE     6 AC6 28 SER B   4  ALA B   5  HOH B 101  HOH B 102                    
SITE     7 AC6 28 HOH B 104  HOH B 105  HOH B 107  HOH B 109                    
CRYST1   48.601   80.056  124.551  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      0.020576  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012491  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008029        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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