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Database: PDB
Entry: 4OG6
LinkDB: 4OG6
Original site: 4OG6 
HEADER    PROTEIN BINDING/INHIBITOR               15-JAN-14   4OG6              
TITLE     HUMAN MENIN WITH BOUND INHIBITOR MIV-4                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MENIN;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MEN1, SCG2;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN BINDING/INHIBITOR, 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 4OG6    1       JRNL                                     
REVDAT   1   05-MAR-14 4OG6    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.    1.49 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) : 1.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 70287                          
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) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3701                            
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) : 1.49                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.53                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4507                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.78                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 254                          
REMARK   3   BIN FREE R VALUE                    : 0.2470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3678                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 84                                      
REMARK   3   SOLVENT ATOMS            : 463                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.09000                                              
REMARK   3    B22 (A**2) : -0.26000                                             
REMARK   3    B33 (A**2) : 0.17000                                              
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): 0.071         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.072         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.046         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.370         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.959                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3930 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3737 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5326 ; 1.816 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8586 ; 1.054 ; 3.008       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   483 ; 5.759 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   180 ;31.593 ;23.889       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   644 ;12.063 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;16.134 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   589 ; 0.122 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4431 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   912 ; 0.002 ; 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):  1916 ; 2.549 ; 1.389       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1915 ; 2.547 ; 1.387       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2402 ; 3.311 ; 2.166       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2403 ; 3.311 ; 2.168       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2014 ; 4.034 ; 2.391       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2014 ; 4.031 ; 2.391       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2924 ; 5.280 ; 3.297       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4991 ; 8.093 ; 7.327       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4992 ; 8.092 ; 7.334       
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    30                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.4230 -10.4780   1.1810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1579 T22:   0.1991                                     
REMARK   3      T33:   0.1153 T12:   0.0392                                     
REMARK   3      T13:  -0.0078 T23:   0.0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5410 L22:   1.9971                                     
REMARK   3      L33:   1.9004 L12:   0.6958                                     
REMARK   3      L13:  -0.3952 L23:  -0.8863                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0658 S12:  -0.0514 S13:  -0.2139                       
REMARK   3      S21:  -0.1390 S22:   0.0061 S23:  -0.1110                       
REMARK   3      S31:   0.3540 S32:   0.1705 S33:   0.0596                       
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    31        A    97                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.7680  -3.5110   6.0660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1051 T22:   0.2148                                     
REMARK   3      T33:   0.0733 T12:  -0.0004                                     
REMARK   3      T13:  -0.0112 T23:   0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3772 L22:   0.8161                                     
REMARK   3      L33:   1.5104 L12:   0.4881                                     
REMARK   3      L13:   0.2801 L23:   0.0253                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0570 S12:  -0.1700 S13:  -0.0014                       
REMARK   3      S21:   0.0163 S22:  -0.0460 S23:  -0.0150                       
REMARK   3      S31:   0.1409 S32:  -0.0218 S33:  -0.0110                       
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    98        A   127                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.3340 -10.9460 -11.3340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1993 T22:   0.2386                                     
REMARK   3      T33:   0.1277 T12:  -0.0489                                     
REMARK   3      T13:   0.0116 T23:   0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3584 L22:   0.2949                                     
REMARK   3      L33:   3.5063 L12:   0.7070                                     
REMARK   3      L13:   0.3537 L23:  -0.3802                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0060 S12:  -0.1221 S13:  -0.2099                       
REMARK   3      S21:  -0.0388 S22:  -0.0265 S23:  -0.0402                       
REMARK   3      S31:   0.4491 S32:  -0.2098 S33:   0.0325                       
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   128        A   137                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.0760   8.6560   1.4630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1362 T22:   0.2352                                     
REMARK   3      T33:   0.1977 T12:   0.0690                                     
REMARK   3      T13:  -0.0076 T23:  -0.0538                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2205 L22:  20.8304                                     
REMARK   3      L33:   5.1437 L12:  11.0769                                     
REMARK   3      L13:   2.0688 L23:  -2.4346                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1370 S12:  -0.2883 S13:   0.7825                       
REMARK   3      S21:   0.3633 S22:  -0.0476 S23:   1.0693                       
REMARK   3      S31:  -0.4934 S32:  -0.3784 S33:   0.1846                       
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   227                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.9740   1.8730 -13.6620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0898 T22:   0.1879                                     
REMARK   3      T33:   0.0756 T12:  -0.0277                                     
REMARK   3      T13:  -0.0085 T23:   0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5390 L22:   0.3555                                     
REMARK   3      L33:   1.3460 L12:  -0.1004                                     
REMARK   3      L13:   0.3429 L23:  -0.0964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0412 S12:  -0.0515 S13:  -0.0002                       
REMARK   3      S21:  -0.0136 S22:   0.0175 S23:   0.0630                       
REMARK   3      S31:   0.1100 S32:  -0.1281 S33:  -0.0587                       
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   228        A   333                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.7900   8.8470 -11.8840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0756 T22:   0.2007                                     
REMARK   3      T33:   0.0922 T12:  -0.0001                                     
REMARK   3      T13:  -0.0013 T23:   0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3920 L22:   0.5367                                     
REMARK   3      L33:   1.1619 L12:  -0.0433                                     
REMARK   3      L13:   0.2694 L23:  -0.5132                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0107 S12:  -0.0069 S13:   0.0462                       
REMARK   3      S21:   0.0155 S22:  -0.0743 S23:  -0.0974                       
REMARK   3      S31:  -0.0058 S32:   0.1399 S33:   0.0850                       
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   334        A   443                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8040  28.6400 -21.9700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0690 T22:   0.1868                                     
REMARK   3      T33:   0.0703 T12:   0.0084                                     
REMARK   3      T13:  -0.0035 T23:   0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5438 L22:   1.2597                                     
REMARK   3      L33:   0.8827 L12:   0.3749                                     
REMARK   3      L13:   0.0201 L23:   0.0923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0090 S12:  -0.0627 S13:  -0.0003                       
REMARK   3      S21:   0.0114 S22:  -0.0438 S23:   0.0059                       
REMARK   3      S31:  -0.0042 S32:   0.0004 S33:   0.0348                       
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   444        A   448                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.2340  40.9020 -23.5100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1448 T22:   0.3174                                     
REMARK   3      T33:   0.1052 T12:  -0.0591                                     
REMARK   3      T13:   0.0078 T23:   0.0248                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.9249 L22:   0.2812                                     
REMARK   3      L33:   8.0822 L12:   1.7048                                     
REMARK   3      L13:  -7.8570 L23:  -0.8025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2988 S12:  -0.1338 S13:   0.6149                       
REMARK   3      S21:  -0.0018 S22:   0.0439 S23:   0.1042                       
REMARK   3      S31:  -0.6757 S32:   0.6069 S33:  -0.3427                       
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   449        A   561                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.8050  33.8340 -35.9410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1457 T22:   0.2141                                     
REMARK   3      T33:   0.0831 T12:  -0.0078                                     
REMARK   3      T13:   0.0131 T23:  -0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2809 L22:   2.9070                                     
REMARK   3      L33:   0.7653 L12:   3.4720                                     
REMARK   3      L13:   1.5344 L23:   1.0342                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2089 S12:   0.3400 S13:  -0.2273                       
REMARK   3      S21:  -0.3391 S22:   0.2449 S23:  -0.2331                       
REMARK   3      S31:  -0.2102 S32:   0.1450 S33:  -0.0360                       
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   562        A   588                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.5170  42.5260 -30.7570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1842 T22:   0.1870                                     
REMARK   3      T33:   0.1218 T12:   0.0348                                     
REMARK   3      T13:  -0.0461 T23:  -0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5406 L22:   2.2686                                     
REMARK   3      L33:   1.4369 L12:  -2.1223                                     
REMARK   3      L13:   1.7103 L23:  -0.2589                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1757 S12:  -0.0755 S13:   0.2795                       
REMARK   3      S21:   0.3058 S22:   0.1061 S23:  -0.2253                       
REMARK   3      S31:   0.0292 S32:  -0.0158 S33:   0.0696                       
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 4OG6 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 RCSB084451.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-AUG-12                          
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-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : C(111)                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74065                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.490                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.020                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.3800                            
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: PDB ENTRY 4GPQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M HEPES PH   
REMARK 280  7.5 AND 25% W/V PEG 3,350. THIS SOLUTION WAS MIXED 1:1 WITH         
REMARK 280  2.5MG/ML PROTEIN IN 50MM TRIS-HCL (PH 8.0), 50MM NACL, AND 1MM      
REMARK 280  TCEP. PRIOR TO DATA COLLECTION, CRYSTALS WERE TRANSFERRED INTO A    
REMARK 280  CRYO-SOLUTION CONTAINING 20% PEG550 MME AND FLASH-FROZEN IN         
REMARK 280  LIQUID NITROGEN, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 283K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.28400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.23200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.93250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.23200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.28400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.93250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A   539                                                      
REMARK 465     PRO A   540                                                      
REMARK 465     THR 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     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 201    CG   CD   CE   NZ                                   
REMARK 470     ARG A 355    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 456    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 460    CG1  CG2                                            
REMARK 470     GLY A 548    N    CA                                             
REMARK 470     LYS A 569    CG   CD   CE   NZ                                   
REMARK 470     GLN A 586    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 588    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 231   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  77      -64.70   -159.73                                   
REMARK 500    ASN A 189       18.82     56.76                                   
REMARK 500    GLU A 356       -0.52     92.10                                   
REMARK 500    ASP A 370      -57.48   -135.75                                   
REMARK 500    ALA A 581       26.56     49.75                                   
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     PEG A  610                                                       
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 2S9 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 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 610                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OG3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OG4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OG5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OG7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OG8   RELATED DB: PDB                                   
DBREF  4OG6 A    1   593  UNP    O00255   MEN1_HUMAN       1    593             
SEQADV 4OG6 GLY A   -4  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG6 GLY A   -3  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG6 SER A   -2  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG6 SER A   -1  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG6 SER A    0  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG6     A       UNP  O00255    ILE    54 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO    55 DELETION                       
SEQADV 4OG6     A       UNP  O00255    THR    56 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ASN    57 DELETION                       
SEQADV 4OG6     A       UNP  O00255    VAL    58 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO    59 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU    60 DELETION                       
SEQADV 4OG6     A       UNP  O00255    LEU    61 DELETION                       
SEQADV 4OG6     A       UNP  O00255    THR    62 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PHE    63 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLN    64 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO    65 DELETION                       
SEQADV 4OG6     A       UNP  O00255    SER    66 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO    67 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ALA    68 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO    69 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ASP    70 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO    71 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO    72 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY    73 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   387 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   388 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ARG   389 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   390 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   391 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   392 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLN   393 DELETION                       
SEQADV 4OG6     A       UNP  O00255    SER   394 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLN   395 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   396 DELETION                       
SEQADV 4OG6     A       UNP  O00255    THR   397 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLN   398 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ARG   460 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   461 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ALA   462 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   463 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ALA   464 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ALA   465 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   466 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ALA   467 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   468 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   469 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   470 DELETION                       
SEQADV 4OG6     A       UNP  O00255    TRP   471 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   472 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   473 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   474 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ALA   475 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ARG   476 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   477 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   478 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ARG   479 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ARG   480 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ARG   481 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   482 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   483 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ARG   484 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ARG   485 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   486 DELETION                       
SEQADV 4OG6     A       UNP  O00255    SER   487 DELETION                       
SEQADV 4OG6     A       UNP  O00255    LYS   488 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   489 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   490 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   491 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   492 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   493 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   494 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   495 DELETION                       
SEQADV 4OG6     A       UNP  O00255    LYS   496 DELETION                       
SEQADV 4OG6     A       UNP  O00255    LYS   497 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   498 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ALA   499 DELETION                       
SEQADV 4OG6     A       UNP  O00255    LEU   500 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ASP   501 DELETION                       
SEQADV 4OG6     A       UNP  O00255    LYS   502 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   503 DELETION                       
SEQADV 4OG6     A       UNP  O00255    LEU   504 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   505 DELETION                       
SEQADV 4OG6     A       UNP  O00255    THR   506 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   507 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLN   508 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   509 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ALA   510 DELETION                       
SEQADV 4OG6     A       UNP  O00255    VAL   511 DELETION                       
SEQADV 4OG6     A       UNP  O00255    SER   512 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   513 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   514 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   515 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ARG   516 DELETION                       
SEQADV 4OG6     A       UNP  O00255    LYS   517 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   518 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   519 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   520 DELETION                       
SEQADV 4OG6     A       UNP  O00255    THR   521 DELETION                       
SEQADV 4OG6     A       UNP  O00255    VAL   522 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ALA   523 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   524 DELETION                       
SEQADV 4OG6     A       UNP  O00255    THR   525 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ALA   526 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ARG   527 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   528 DELETION                       
SEQADV 4OG6     A       UNP  O00255    PRO   529 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLU   530 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   531 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLY   532 DELETION                       
SEQADV 4OG6     A       UNP  O00255    SER   533 DELETION                       
SEQADV 4OG6     A       UNP  O00255    THR   534 DELETION                       
SEQADV 4OG6     A       UNP  O00255    ALA   535 DELETION                       
SEQADV 4OG6     A       UNP  O00255    GLN   536 DELETION                       
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 THR ALA SER PRO PRO PRO          
SEQRES  35 A  489  GLU GLY PRO VAL LEU THR PHE GLN SER GLU LYS MET LYS          
SEQRES  36 A  489  GLY MET LYS GLU LEU LEU VAL ALA THR LYS ILE ASN SER          
SEQRES  37 A  489  SER ALA ILE LYS LEU GLN LEU THR ALA GLN SER GLN VAL          
SEQRES  38 A  489  GLN MET LYS LYS GLN LYS VAL SER                              
HET    SO4  A 601       5                                                       
HET    2S9  A 602      32                                                       
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                                                       
HET    PEG  A 610       4                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     2S9 4-(3-{4-[(R)-CYCLOPENTYL(3-FLUOROPHENYL)                         
HETNAM   2 2S9  HYDROXYMETHYL]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  2S9    C27 H33 F N2 O2                                              
FORMUL   4  PG4    C8 H18 O5                                                    
FORMUL   5  PEG    3(C4 H10 O3)                                                 
FORMUL   7  DMS    4(C2 H6 O S)                                                 
FORMUL  12  HOH   *463(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  GLY A  271  1                                  19    
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  LEU A  565  5                                   3    
HELIX   27  27 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  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  VAL A 458  0                                        
SHEET    2   C 2 VAL A 550  THR A 552  1  O  LEU A 551   N  VAL A 458           
CISPEP   1 GLY A    2    LEU A    3          0        -9.76                     
CISPEP   2 PHE A   11    PRO A   12          0         3.75                     
CISPEP   3 VAL A  460    PRO A  461          0        -2.12                     
SITE     1 AC1  4 TYR A 133  PHE A 134  ARG A 137  ARG A 332                    
SITE     1 AC2 16 SER A 155  SER A 178  ASP A 180  HIS A 181                    
SITE     2 AC2 16 ALA A 182  PHE A 238  ALA A 242  MET A 278                    
SITE     3 AC2 16 TYR A 319  MET A 322  TYR A 323  TRP A 341                    
SITE     4 AC2 16 GLU A 363  HOH A1032  HOH A1048  HOH A1078                    
SITE     1 AC3  7 LEU A  75  THR A  76  PHE A 365  HOH A 735                    
SITE     2 AC3  7 HOH A 776  HOH A 856  HOH A 875                               
SITE     1 AC4  3 TRP A 126  LYS A 135  TRP A 198                               
SITE     1 AC5  3 TYR A 268  ASP A 269  GLY A 271                               
SITE     1 AC6  4 PRO A  12  ARG A  14  HOH A 977  HOH A1100                    
SITE     1 AC7  6 VAL A 185  GLY A 190  GLU A 191  TYR A 227                    
SITE     2 AC7  6 ARG A 229  SER A 583                                          
SITE     1 AC8  4 ARG A 332  VAL A 334  ARG A 335  ALA A 403                    
SITE     1 AC9  4 PHE A  47  GLY A 386  GLN A 400  HOH A 794                    
SITE     1 BC1  6 HIS A  46  ASN A  51  LEU A 382  HOH A1144                    
SITE     2 BC1  6 HOH A1161  HOH A1163                                          
CRYST1   48.568   79.865  124.464  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      0.020590  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012521  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008034        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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