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Database: PDB
Entry: 4OG3
LinkDB: 4OG3
Original site: 4OG3 
HEADER    PROTEIN BINDING/INHIBITOR               15-JAN-14   4OG3              
TITLE     HUMAN MENIN WITH BOUND INHIBITOR MIV-3R                               
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, PROTEIN BINDING-INHIBITOR COMPLEX                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.HE,T.J.SENTER,J.W.POLLOCK,C.HAN,S.K.UPADHYAY,T.PUROHIT,             
AUTHOR   2 R.D.GOGLIOTTI,C.W.LINDSLEY,T.CIERPICKI,S.R.STAUFFER,J.GREMBECKA      
REVDAT   2   19-MAR-14 4OG3    1       JRNL                                     
REVDAT   1   05-MAR-14 4OG3    0                                                
JRNL        AUTH   S.HE,T.J.SENTER,J.POLLOCK,C.HAN,S.K.UPADHYAY,T.PUROHIT,      
JRNL        AUTH 2 R.D.GOGLIOTTI,C.W.LINDSLEY,T.CIERPICKI,S.R.STAUFFER,         
JRNL        AUTH 3 J.GREMBECKA                                                  
JRNL        TITL   HIGH-AFFINITY SMALL-MOLECULE INHIBITORS OF THE MENIN-MIXED   
JRNL        TITL 2 LINEAGE LEUKEMIA (MLL) INTERACTION CLOSELY MIMIC A NATURAL   
JRNL        TITL 3 PROTEIN-PROTEIN INTERACTION.                                 
JRNL        REF    J.MED.CHEM.                   V.  57  1543 2014              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   24472025                                                     
JRNL        DOI    10.1021/JM401868D                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 31704                          
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) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1691                            
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) : 2.01                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.06                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2278                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.59                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 106                          
REMARK   3   BIN FREE R VALUE                    : 0.2570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3626                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 79                                      
REMARK   3   SOLVENT ATOMS            : 322                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : 0.06000                                              
REMARK   3    B33 (A**2) : -0.04000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.163         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.152         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.098         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.805         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3806 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3609 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5155 ; 1.833 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8273 ; 1.103 ; 3.008       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   468 ; 5.923 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   168 ;30.894 ;23.690       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   608 ;12.128 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;15.911 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   576 ; 0.114 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4274 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   887 ; 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):  1874 ; 1.543 ; 1.608       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1873 ; 1.543 ; 1.607       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2341 ; 2.336 ; 2.399       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2342 ; 2.336 ; 2.399       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1932 ; 2.166 ; 1.884       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1933 ; 2.166 ; 1.886       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2815 ; 3.251 ; 2.704       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4678 ; 6.000 ;14.156       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4679 ; 5.999 ;14.168       
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  : 10                                         
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    28                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.2260  -9.6480   2.2280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0719 T22:   0.0230                                     
REMARK   3      T33:   0.0811 T12:   0.0157                                     
REMARK   3      T13:  -0.0242 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6149 L22:   1.9888                                     
REMARK   3      L33:   2.5665 L12:  -0.2472                                     
REMARK   3      L13:  -0.6009 L23:  -0.6245                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0542 S12:  -0.1010 S13:  -0.2710                       
REMARK   3      S21:   0.0485 S22:  -0.0393 S23:  -0.0716                       
REMARK   3      S31:   0.3006 S32:   0.1056 S33:   0.0935                       
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    29        A    96                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.3120  -3.8560   5.4380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0590 T22:   0.0657                                     
REMARK   3      T33:   0.0376 T12:   0.0019                                     
REMARK   3      T13:  -0.0080 T23:   0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7489 L22:   2.0491                                     
REMARK   3      L33:   2.0699 L12:   0.8276                                     
REMARK   3      L13:   0.5598 L23:   0.5890                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0459 S12:  -0.1708 S13:  -0.0521                       
REMARK   3      S21:  -0.0053 S22:   0.0260 S23:  -0.0124                       
REMARK   3      S31:   0.0756 S32:   0.0570 S33:  -0.0719                       
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    97        A   130                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.3560  -9.7900  -9.9840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0811 T22:   0.0447                                     
REMARK   3      T33:   0.0791 T12:  -0.0308                                     
REMARK   3      T13:   0.0045 T23:   0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6141 L22:   1.2967                                     
REMARK   3      L33:   3.4698 L12:   0.2457                                     
REMARK   3      L13:   0.3625 L23:   0.0922                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0088 S12:  -0.0390 S13:  -0.2887                       
REMARK   3      S21:  -0.1218 S22:  -0.0163 S23:   0.0038                       
REMARK   3      S31:   0.2172 S32:  -0.0713 S33:   0.0074                       
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   131        A   137                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.8900  10.7920   1.1840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0814 T22:   0.0597                                     
REMARK   3      T33:   0.3068 T12:   0.0137                                     
REMARK   3      T13:   0.0113 T23:  -0.0426                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  23.9186 L22:  22.6766                                     
REMARK   3      L33:   2.3090 L12:  -1.4688                                     
REMARK   3      L13:  -2.3722 L23:  -1.9456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0061 S12:  -0.0512 S13:   1.1797                       
REMARK   3      S21:   0.5443 S22:  -0.1713 S23:   1.6706                       
REMARK   3      S31:  -0.1705 S32:  -0.0234 S33:   0.1774                       
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   138        A   228                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.0020   2.0550 -13.8050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0563 T22:   0.0375                                     
REMARK   3      T33:   0.0680 T12:  -0.0262                                     
REMARK   3      T13:  -0.0110 T23:  -0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6900 L22:   0.4595                                     
REMARK   3      L33:   1.3958 L12:  -0.0354                                     
REMARK   3      L13:   0.1567 L23:  -0.1821                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0263 S12:  -0.0077 S13:   0.0454                       
REMARK   3      S21:  -0.0152 S22:   0.0042 S23:   0.0850                       
REMARK   3      S31:   0.0320 S32:  -0.1411 S33:  -0.0306                       
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 :   A   229        A   289                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.1060   5.2100  -7.3230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0584 T22:   0.0209                                     
REMARK   3      T33:   0.0729 T12:   0.0029                                     
REMARK   3      T13:  -0.0032 T23:   0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6250 L22:   0.7471                                     
REMARK   3      L33:   1.3684 L12:   0.1492                                     
REMARK   3      L13:   0.1470 L23:  -0.3649                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0281 S12:  -0.0456 S13:   0.1017                       
REMARK   3      S21:   0.0157 S22:  -0.0923 S23:  -0.0405                       
REMARK   3      S31:  -0.0336 S32:   0.0639 S33:   0.0642                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   290        A   355                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.9550  16.1540 -20.0440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0418 T22:   0.0322                                     
REMARK   3      T33:   0.0847 T12:  -0.0058                                     
REMARK   3      T13:   0.0121 T23:   0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7496 L22:   1.3860                                     
REMARK   3      L33:   1.2702 L12:  -0.2852                                     
REMARK   3      L13:   0.3684 L23:  -0.4672                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0097 S12:  -0.0131 S13:   0.0728                       
REMARK   3      S21:   0.0162 S22:  -0.0513 S23:  -0.0919                       
REMARK   3      S31:  -0.0158 S32:   0.0870 S33:   0.0610                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   356        A   401                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.4860  30.3890 -15.7740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0523 T22:   0.0508                                     
REMARK   3      T33:   0.0220 T12:   0.0121                                     
REMARK   3      T13:  -0.0023 T23:   0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9300 L22:   3.8936                                     
REMARK   3      L33:   1.0719 L12:   3.3388                                     
REMARK   3      L13:   0.7267 L23:   0.3383                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0687 S12:  -0.2450 S13:   0.0429                       
REMARK   3      S21:   0.1589 S22:  -0.1277 S23:   0.0396                       
REMARK   3      S31:  -0.0035 S32:   0.0209 S33:   0.0590                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   402        A   548                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1470  33.0220 -27.3390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0582 T22:   0.0236                                     
REMARK   3      T33:   0.0585 T12:   0.0190                                     
REMARK   3      T13:  -0.0143 T23:   0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4813 L22:   1.8495                                     
REMARK   3      L33:   1.8185 L12:   1.2369                                     
REMARK   3      L13:  -0.3523 L23:  -0.0617                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0419 S12:  -0.0015 S13:  -0.0791                       
REMARK   3      S21:  -0.0948 S22:   0.0312 S23:  -0.0212                       
REMARK   3      S31:  -0.0822 S32:  -0.0183 S33:   0.0107                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   549        A   586                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6730  38.0280 -32.5730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0974 T22:   0.0270                                     
REMARK   3      T33:   0.0506 T12:   0.0304                                     
REMARK   3      T13:  -0.0480 T23:   0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8086 L22:   4.6461                                     
REMARK   3      L33:   0.4517 L12:  -1.4184                                     
REMARK   3      L13:   0.6785 L23:   0.3705                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1080 S12:   0.0784 S13:   0.2299                       
REMARK   3      S21:   0.0947 S22:   0.0400 S23:  -0.2255                       
REMARK   3      S31:  -0.1332 S32:  -0.0216 S33:   0.0680                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4OG3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084448.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-OCT-11                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-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                  : C(111)                             
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   : 33475                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.010                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.581                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.14500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.8900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M HEPES      
REMARK 280  AND 25% W/V PEG 3,350. THIS SOLUTION WAS MIXED 1:1 WITH 2.5MG/ML    
REMARK 280  PROTEIN IN 50MM TRIS-HCL, 50MM NACL, AND 1MM TCEP. PRIOR TO DATA    
REMARK 280  COLLECTION, CRYSTALS WERE TRANSFERRED INTO A CRYO-SOLUTION          
REMARK 280  CONTAINING 20% PEG550 MME AND FLASH-FROZEN IN LIQUID NITROGEN,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 283K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.43400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.35900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.12800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.35900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.43400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.12800            
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     MET A   587                                                      
REMARK 465     LYS A   588                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     GLN A   590                                                      
REMARK 465     LYS A   591                                                      
REMARK 465     VAL A   592                                                      
REMARK 465     SER A   593                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   4    CE   NZ                                             
REMARK 470     LEU A  10    CD1  CD2                                            
REMARK 470     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 137    CZ   NH1  NH2                                       
REMARK 470     ARG A 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 204    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 249    CG   CD1  CD2                                       
REMARK 470     GLN A 400    CD   OE1  NE2                                       
REMARK 470     GLU A 408    OE1  OE2                                            
REMARK 470     GLU A 448    CD   OE1  OE2                                       
REMARK 470     ARG A 456    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 458    CG1  CG2                                            
REMARK 470     VAL A 460    CG1  CG2                                            
REMARK 470     PRO A 461    C    O    CB   CG   CD                              
REMARK 470     ALA A 548    N    CA   O    CB                                   
REMARK 470     LYS A 562    CG   CD   CE   NZ                                   
REMARK 470     LYS A 569    CG   CD   CE   NZ                                   
REMARK 470     LYS A 576    CG   CD   CE   NZ                                   
REMARK 470     SER A 583    OG                                                  
REMARK 470     GLN A 586    CG   CD   OE1  NE2                                  
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      -58.04   -159.67                                   
REMARK 500    ASP A 180       10.09   -155.10                                   
REMARK 500    SER A 226       44.93    -89.69                                   
REMARK 500    GLU A 356       -6.49     86.49                                   
REMARK 500    ASP A 370      -53.24   -137.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 2S6 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 609                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OG4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OG5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OG6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OG7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OG8   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CRYSTALLIZED SEQUENCE CORRESPONDS TO THE HUMAN MENIN ISOFORM 2   
DBREF  4OG3 A    1   593  UNP    O00255   MEN1_HUMAN       1    593             
SEQADV 4OG3 GLY A   -4  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG3 GLY A   -3  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG3 SER A   -2  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG3 SER A   -1  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG3 SER A    0  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG3     A       UNP  O00255    ILE    54 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO    55 DELETION                       
SEQADV 4OG3     A       UNP  O00255    THR    56 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ASN    57 DELETION                       
SEQADV 4OG3     A       UNP  O00255    VAL    58 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO    59 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU    60 DELETION                       
SEQADV 4OG3     A       UNP  O00255    LEU    61 DELETION                       
SEQADV 4OG3     A       UNP  O00255    THR    62 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PHE    63 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLN    64 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO    65 DELETION                       
SEQADV 4OG3     A       UNP  O00255    SER    66 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO    67 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ALA    68 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO    69 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ASP    70 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO    71 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO    72 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY    73 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   387 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   388 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ARG   389 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   390 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   391 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   392 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLN   393 DELETION                       
SEQADV 4OG3     A       UNP  O00255    SER   394 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLN   395 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   396 DELETION                       
SEQADV 4OG3     A       UNP  O00255    THR   397 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLN   398 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ARG   460 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   461 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ALA   462 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   463 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ALA   464 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ALA   465 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   466 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ALA   467 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   468 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   469 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   470 DELETION                       
SEQADV 4OG3     A       UNP  O00255    TRP   471 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   472 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   473 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   474 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ALA   475 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ARG   476 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   477 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   478 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ARG   479 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ARG   480 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ARG   481 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   482 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   483 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ARG   484 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ARG   485 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   486 DELETION                       
SEQADV 4OG3     A       UNP  O00255    SER   487 DELETION                       
SEQADV 4OG3     A       UNP  O00255    LYS   488 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   489 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   490 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   491 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   492 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   493 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   494 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   495 DELETION                       
SEQADV 4OG3     A       UNP  O00255    LYS   496 DELETION                       
SEQADV 4OG3     A       UNP  O00255    LYS   497 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   498 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ALA   499 DELETION                       
SEQADV 4OG3     A       UNP  O00255    LEU   500 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ASP   501 DELETION                       
SEQADV 4OG3     A       UNP  O00255    LYS   502 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   503 DELETION                       
SEQADV 4OG3     A       UNP  O00255    LEU   504 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   505 DELETION                       
SEQADV 4OG3     A       UNP  O00255    THR   506 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   507 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLN   508 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   509 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ALA   510 DELETION                       
SEQADV 4OG3     A       UNP  O00255    VAL   511 DELETION                       
SEQADV 4OG3     A       UNP  O00255    SER   512 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   513 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   514 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   515 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ARG   516 DELETION                       
SEQADV 4OG3     A       UNP  O00255    LYS   517 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   518 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   519 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   520 DELETION                       
SEQADV 4OG3     A       UNP  O00255    THR   521 DELETION                       
SEQADV 4OG3     A       UNP  O00255    VAL   522 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ALA   523 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   524 DELETION                       
SEQADV 4OG3     A       UNP  O00255    THR   525 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ALA   526 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ARG   527 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   528 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   529 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   530 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   531 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   532 DELETION                       
SEQADV 4OG3     A       UNP  O00255    SER   533 DELETION                       
SEQADV 4OG3     A       UNP  O00255    THR   534 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ALA   535 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLN   536 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   540 DELETION                       
SEQADV 4OG3     A       UNP  O00255    THR   541 DELETION                       
SEQADV 4OG3     A       UNP  O00255    ALA   542 DELETION                       
SEQADV 4OG3     A       UNP  O00255    SER   543 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   544 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   545 DELETION                       
SEQADV 4OG3     A       UNP  O00255    PRO   546 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLU   547 DELETION                       
SEQADV 4OG3     A       UNP  O00255    GLY   548 DELETION                       
SEQRES   1 A  480  GLY GLY SER SER SER MET GLY LEU LYS ALA ALA GLN LYS          
SEQRES   2 A  480  THR LEU PHE PRO LEU ARG SER ILE ASP ASP VAL VAL ARG          
SEQRES   3 A  480  LEU PHE ALA ALA GLU LEU GLY ARG GLU GLU PRO ASP LEU          
SEQRES   4 A  480  VAL LEU LEU SER LEU VAL LEU GLY PHE VAL GLU HIS PHE          
SEQRES   5 A  480  LEU ALA VAL ASN ARG VAL GLY LEU THR TYR PHE PRO VAL          
SEQRES   6 A  480  ALA ASP LEU SER ILE ILE ALA ALA LEU TYR ALA ARG PHE          
SEQRES   7 A  480  THR ALA GLN ILE ARG GLY ALA VAL ASP LEU SER LEU TYR          
SEQRES   8 A  480  PRO ARG GLU GLY GLY VAL SER SER ARG GLU LEU VAL LYS          
SEQRES   9 A  480  LYS VAL SER ASP VAL ILE TRP ASN SER LEU SER ARG SER          
SEQRES  10 A  480  TYR PHE LYS ASP ARG ALA HIS ILE GLN SER LEU PHE SER          
SEQRES  11 A  480  PHE ILE THR GLY THR LYS LEU ASP SER SER GLY VAL ALA          
SEQRES  12 A  480  PHE ALA VAL VAL GLY ALA CYS GLN ALA LEU GLY LEU ARG          
SEQRES  13 A  480  ASP VAL HIS LEU ALA LEU SER GLU ASP HIS ALA TRP VAL          
SEQRES  14 A  480  VAL PHE GLY PRO ASN GLY GLU GLN THR ALA GLU VAL THR          
SEQRES  15 A  480  TRP HIS GLY LYS GLY ASN GLU ASP ARG ARG GLY GLN THR          
SEQRES  16 A  480  VAL ASN ALA GLY VAL ALA GLU ARG SER TRP LEU TYR LEU          
SEQRES  17 A  480  LYS GLY SER TYR MET ARG CYS ASP ARG LYS MET GLU VAL          
SEQRES  18 A  480  ALA PHE MET VAL CYS ALA ILE ASN PRO SER ILE ASP LEU          
SEQRES  19 A  480  HIS THR ASP SER LEU GLU LEU LEU GLN LEU GLN GLN LYS          
SEQRES  20 A  480  LEU LEU TRP LEU LEU TYR ASP LEU GLY HIS LEU GLU ARG          
SEQRES  21 A  480  TYR PRO MET ALA LEU GLY ASN LEU ALA ASP LEU GLU GLU          
SEQRES  22 A  480  LEU GLU PRO THR PRO GLY ARG PRO ASP PRO LEU THR LEU          
SEQRES  23 A  480  TYR HIS LYS GLY ILE ALA SER ALA LYS THR TYR TYR ARG          
SEQRES  24 A  480  ASP GLU HIS ILE TYR PRO TYR MET TYR LEU ALA GLY TYR          
SEQRES  25 A  480  HIS CYS ARG ASN ARG ASN VAL ARG GLU ALA LEU GLN ALA          
SEQRES  26 A  480  TRP ALA ASP THR ALA THR VAL ILE GLN ASP TYR ASN TYR          
SEQRES  27 A  480  CYS ARG GLU ASP GLU GLU ILE TYR LYS GLU PHE PHE GLU          
SEQRES  28 A  480  VAL ALA ASN ASP VAL ILE PRO ASN LEU LEU LYS GLU ALA          
SEQRES  29 A  480  ALA SER LEU LEU GLU ALA GLY SER GLN GLY SER ALA LEU          
SEQRES  30 A  480  GLN ASP PRO GLU CYS PHE ALA HIS LEU LEU ARG PHE TYR          
SEQRES  31 A  480  ASP GLY ILE CYS LYS TRP GLU GLU GLY SER PRO THR PRO          
SEQRES  32 A  480  VAL LEU HIS VAL GLY TRP ALA THR PHE LEU VAL GLN SER          
SEQRES  33 A  480  LEU GLY ARG PHE GLU GLY GLN VAL ARG GLN LYS VAL ARG          
SEQRES  34 A  480  ILE VAL SER VAL PRO ALA PRO VAL LEU THR PHE GLN SER          
SEQRES  35 A  480  GLU LYS MET LYS GLY MET LYS GLU LEU LEU VAL ALA THR          
SEQRES  36 A  480  LYS ILE ASN SER SER ALA ILE LYS LEU GLN LEU THR ALA          
SEQRES  37 A  480  GLN SER GLN VAL GLN MET LYS LYS GLN LYS VAL SER              
HET    SO4  A 601       5                                                       
HET    2S6  A 602      31                                                       
HET    PG4  A 603      13                                                       
HET    PEG  A 604       7                                                       
HET    PEG  A 605       7                                                       
HET    DMS  A 606       4                                                       
HET    DMS  A 607       4                                                       
HET    DMS  A 608       4                                                       
HET    DMS  A 609       4                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     2S6 4-(3-{4-[(R)-CYCLOPENTYL(HYDROXY)                                
HETNAM   2 2S6  PHENYLMETHYL]PIPERIDIN-1-YL}PROPOXY)BENZONITRILE                
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     DMS DIMETHYL SULFOXIDE                                               
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  2S6    C27 H34 N2 O2                                                
FORMUL   4  PG4    C8 H18 O5                                                    
FORMUL   5  PEG    2(C4 H10 O3)                                                 
FORMUL   7  DMS    4(C2 H6 O S)                                                 
FORMUL  11  HOH   *322(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 SER A  114  SER A  128  1                                  15    
HELIX    7   7 SER A  142  THR A  150  1                                   9    
HELIX    8   8 ASP A  153  LEU A  168  1                                  16    
HELIX    9   9 GLY A  187  GLU A  191  5                                   5    
HELIX   10  10 VAL A  211  GLU A  217  1                                   7    
HELIX   11  11 SER A  219  SER A  226  5                                   8    
HELIX   12  12 ASP A  231  ALA A  242  1                                  12    
HELIX   13  13 SER A  253  LEU A  270  1                                  18    
HELIX   14  14 TYR A  276  GLU A  290  1                                  15    
HELIX   15  15 ASP A  297  TYR A  313  1                                  17    
HELIX   16  16 ILE A  318  ASN A  331  1                                  14    
HELIX   17  17 ASN A  333  GLN A  349  1                                  17    
HELIX   18  18 ASP A  357  ASP A  370  1                                  14    
HELIX   19  19 ASP A  370  ALA A  385  1                                  16    
HELIX   20  20 SER A  402  GLN A  405  5                                   4    
HELIX   21  21 ASP A  406  GLU A  425  1                                  20    
HELIX   22  22 HIS A  433  ARG A  446  1                                  14    
HELIX   23  23 GLU A  448  GLN A  453  1                                   6    
HELIX   24  24 SER A  555  LYS A  562  1                                   8    
HELIX   25  25 GLU A  563  VAL A  566  5                                   4    
HELIX   26  26 ASN A  571  ALA A  581  1                                  11    
SHEET    1   A 4 GLN A 192  ALA A 194  0                                        
SHEET    2   A 4 ALA A 182  PHE A 186 -1  N  PHE A 186   O  GLN A 192           
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 GLY A    2    LEU A    3          0         6.89                     
CISPEP   2 PHE A   11    PRO A   12          0        -3.88                     
CISPEP   3 VAL A  460    PRO A  461          0        -9.00                     
SITE     1 AC1  4 TYR A 133  PHE A 134  ARG A 137  ARG A 332                    
SITE     1 AC2 14 SER A 155  SER A 178  GLU A 179  HIS A 181                    
SITE     2 AC2 14 ALA A 242  MET A 278  TYR A 319  MET A 322                    
SITE     3 AC2 14 TYR A 323  TRP A 341  GLU A 363  HOH A 995                    
SITE     4 AC2 14 HOH A1005  HOH A1022                                          
SITE     1 AC3  7 LEU A  75  THR A  76  PHE A 365  HOH A 739                    
SITE     2 AC3  7 HOH A 780  HOH A 860  HOH A 876                               
SITE     1 AC4  4 TRP A 126  LYS A 135  PRO A 293  HOH A1019                    
SITE     1 AC5  4 TYR A 268  ASP A 269  GLY A 271  HOH A 994                    
SITE     1 AC6  2 ARG A  14  HOH A 962                                          
SITE     1 AC7  5 VAL A 185  GLY A 190  GLU A 191  ARG A 229                    
SITE     2 AC7  5 SER A 583                                                     
SITE     1 AC8  3 VAL A 334  ARG A 335  ALA A 403                               
SITE     1 AC9  5 PHE A  43  PHE A  47  GLY A 386  GLN A 400                    
SITE     2 AC9  5 HOH A 798                                                     
CRYST1   48.868   80.256  124.718  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      0.020463  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012460  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008018        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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