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Database: PDB
Entry: 4OG8
LinkDB: 4OG8
Original site: 4OG8 
HEADER    PROTEIN BINDING/INHIBITOR               15-JAN-14   4OG8              
TITLE     HUMAN MENIN WITH BOUND INHIBITOR MIV-6R                               
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 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 4OG8    1       JRNL                                     
REVDAT   1   05-MAR-14 4OG8    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.    1.53 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) : 1.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 69656                          
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) : 0.152                           
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.176                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3693                            
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) : 1.53                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4816                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 230                          
REMARK   3   BIN FREE R VALUE                    : 0.2460                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3669                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 429                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.03000                                             
REMARK   3    B22 (A**2) : -0.05000                                             
REMARK   3    B33 (A**2) : 0.08000                                              
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): 0.067         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.068         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.040         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.130         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.964                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3905 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3697 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5299 ; 1.735 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8490 ; 1.061 ; 3.007       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   483 ; 5.711 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   175 ;31.680 ;23.943       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   636 ;11.363 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;16.015 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   589 ; 0.120 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4418 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   907 ; 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):  1918 ; 2.491 ; 1.580       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1918 ; 2.491 ; 1.581       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2404 ; 3.237 ; 2.447       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2405 ; 3.237 ; 2.452       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1987 ; 4.544 ; 2.607       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1987 ; 4.544 ; 2.608       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2895 ; 6.520 ; 3.644       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4873 ; 8.132 ; 7.564       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4874 ; 8.132 ; 7.575       
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):   4.5580 -10.2940  -1.1850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1732 T22:   0.1397                                     
REMARK   3      T33:   0.1399 T12:  -0.0237                                     
REMARK   3      T13:  -0.0182 T23:  -0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9293 L22:   1.8021                                     
REMARK   3      L33:   2.2227 L12:  -0.7400                                     
REMARK   3      L13:  -0.2830 L23:   1.0178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0418 S12:   0.0931 S13:  -0.2569                       
REMARK   3      S21:   0.0862 S22:  -0.0123 S23:   0.1130                       
REMARK   3      S31:   0.3845 S32:  -0.1060 S33:   0.0541                       
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):  12.8890  -3.3360  -5.9890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1264 T22:   0.1626                                     
REMARK   3      T33:   0.0829 T12:   0.0042                                     
REMARK   3      T13:  -0.0150 T23:  -0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4245 L22:   1.1603                                     
REMARK   3      L33:   1.4659 L12:  -0.5119                                     
REMARK   3      L13:   0.1881 L23:  -0.1652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0465 S12:   0.2178 S13:   0.0071                       
REMARK   3      S21:  -0.0362 S22:  -0.0386 S23:   0.0126                       
REMARK   3      S31:   0.1013 S32:   0.0168 S33:  -0.0079                       
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):  30.4680 -10.7280  11.1890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1659 T22:   0.1491                                     
REMARK   3      T33:   0.1280 T12:   0.0261                                     
REMARK   3      T13:  -0.0199 T23:  -0.0293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9257 L22:   1.2099                                     
REMARK   3      L33:   2.3910 L12:  -0.7033                                     
REMARK   3      L13:   0.3414 L23:  -0.1202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0368 S12:   0.0985 S13:  -0.2423                       
REMARK   3      S21:  -0.0388 S22:  -0.0124 S23:  -0.0672                       
REMARK   3      S31:   0.2753 S32:   0.1703 S33:  -0.0244                       
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):  27.7390   9.1290  -1.0740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1656 T22:   0.2089                                     
REMARK   3      T33:   0.2770 T12:  -0.0587                                     
REMARK   3      T13:   0.0183 T23:   0.0891                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0894 L22:  20.3469                                     
REMARK   3      L33:   5.3220 L12: -10.1433                                     
REMARK   3      L13:   1.2137 L23:   3.7253                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0529 S12:   0.3452 S13:   0.7178                       
REMARK   3      S21:  -0.4646 S22:  -0.2022 S23:  -0.8918                       
REMARK   3      S31:  -0.5023 S32:   0.3346 S33:   0.2551                       
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   204                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4120  -0.0290  10.2930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1162 T22:   0.1351                                     
REMARK   3      T33:   0.0906 T12:   0.0354                                     
REMARK   3      T13:  -0.0096 T23:  -0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8246 L22:   0.3892                                     
REMARK   3      L33:   1.4033 L12:   0.0247                                     
REMARK   3      L13:   0.2872 L23:   0.2463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0517 S12:   0.0804 S13:  -0.0051                       
REMARK   3      S21:  -0.0207 S22:   0.0384 S23:  -0.0511                       
REMARK   3      S31:   0.1350 S32:   0.1333 S33:  -0.0901                       
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   205        A   222                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8660   7.3850  22.4940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0902 T22:   0.1441                                     
REMARK   3      T33:   0.1293 T12:   0.0148                                     
REMARK   3      T13:  -0.0011 T23:   0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4191 L22:   4.9153                                     
REMARK   3      L33:   1.6816 L12:  -2.0108                                     
REMARK   3      L13:   0.4253 L23:   0.7707                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0479 S12:   0.0027 S13:   0.2333                       
REMARK   3      S21:  -0.0146 S22:   0.0280 S23:  -0.4544                       
REMARK   3      S31:   0.0869 S32:   0.2580 S33:  -0.0759                       
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   223        A   289                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.2370   5.4190   8.8560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1043 T22:   0.1217                                     
REMARK   3      T33:   0.0999 T12:   0.0045                                     
REMARK   3      T13:  -0.0027 T23:  -0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8984 L22:   0.4650                                     
REMARK   3      L33:   1.0735 L12:   0.0019                                     
REMARK   3      L13:   0.4775 L23:   0.4435                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0065 S12:   0.0361 S13:   0.0556                       
REMARK   3      S21:  -0.0349 S22:  -0.0654 S23:   0.0705                       
REMARK   3      S31:   0.0279 S32:  -0.0801 S33:   0.0589                       
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   290        A   428                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.8660  22.7420  20.4260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0844 T22:   0.1248                                     
REMARK   3      T33:   0.0936 T12:   0.0086                                     
REMARK   3      T13:  -0.0045 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1180 L22:   1.2356                                     
REMARK   3      L33:   0.4073 L12:  -0.0329                                     
REMARK   3      L13:  -0.0649 L23:   0.2487                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0046 S12:   0.0281 S13:   0.0019                       
REMARK   3      S21:  -0.0460 S22:  -0.0457 S23:   0.0768                       
REMARK   3      S31:  -0.0118 S32:  -0.0564 S33:   0.0411                       
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   429        A   461                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0390  36.4650  27.7260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1284 T22:   0.1365                                     
REMARK   3      T33:   0.0950 T12:  -0.0169                                     
REMARK   3      T13:  -0.0233 T23:  -0.0124                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7583 L22:   2.2520                                     
REMARK   3      L33:   2.2510 L12:  -2.2788                                     
REMARK   3      L13:  -2.4422 L23:   0.9081                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1155 S12:  -0.2016 S13:   0.0299                       
REMARK   3      S21:   0.1424 S22:   0.1035 S23:  -0.0210                       
REMARK   3      S31:  -0.0989 S32:   0.1549 S33:   0.0120                       
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   548        A   588                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9750  38.5960  32.5500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1753 T22:   0.1124                                     
REMARK   3      T33:   0.1213 T12:  -0.0166                                     
REMARK   3      T13:  -0.0610 T23:  -0.0024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7686 L22:   3.6436                                     
REMARK   3      L33:   0.8349 L12:   1.4876                                     
REMARK   3      L13:   1.1778 L23:   0.3256                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2582 S12:   0.0166 S13:   0.3185                       
REMARK   3      S21:  -0.1576 S22:   0.1031 S23:   0.2343                       
REMARK   3      S31:  -0.2260 S32:   0.0039 S33:   0.1552                       
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 4OG8 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 RCSB084453.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-13                          
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   : 73430                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.530                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.680                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06900                            
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   (%): 44.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
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       24.39100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.34550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.11200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.34550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.39100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.11200            
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     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 131    CG   CD   NE   CZ   NH1  NH2                        
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                                                   
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: 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      -61.83   -159.20                                   
REMARK 500    ASN A 189       15.95     55.61                                   
REMARK 500    SER A 226       43.30    -91.41                                   
REMARK 500    GLU A 356       -1.40     81.91                                   
REMARK 500    ASP A 370      -57.38   -134.71                                   
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     TBF A  601                                                       
REMARK 610     PGA A  608                                                       
REMARK 610     TBF A  611                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TBF A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2SF 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 SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 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 PGA 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 DMS A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TBF A 611                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CRYSTALLIZED SEQUENCE CORRESPONDS TO THE HUMAN MENIN ISOFORM 2   
DBREF  4OG8 A    1   593  UNP    O00255   MEN1_HUMAN       1    593             
SEQADV 4OG8 GLY A   -4  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG8 GLY A   -3  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG8 SER A   -2  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG8 SER A   -1  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG8 SER A    0  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG8     A       UNP  O00255    ILE    54 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO    55 DELETION                       
SEQADV 4OG8     A       UNP  O00255    THR    56 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ASN    57 DELETION                       
SEQADV 4OG8     A       UNP  O00255    VAL    58 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO    59 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU    60 DELETION                       
SEQADV 4OG8     A       UNP  O00255    LEU    61 DELETION                       
SEQADV 4OG8     A       UNP  O00255    THR    62 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PHE    63 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLN    64 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO    65 DELETION                       
SEQADV 4OG8     A       UNP  O00255    SER    66 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO    67 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ALA    68 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO    69 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ASP    70 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO    71 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO    72 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY    73 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   387 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   388 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ARG   389 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   390 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   391 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   392 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLN   393 DELETION                       
SEQADV 4OG8     A       UNP  O00255    SER   394 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLN   395 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   396 DELETION                       
SEQADV 4OG8     A       UNP  O00255    THR   397 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLN   398 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ARG   460 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   461 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ALA   462 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   463 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ALA   464 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ALA   465 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   466 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ALA   467 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   468 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   469 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   470 DELETION                       
SEQADV 4OG8     A       UNP  O00255    TRP   471 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   472 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   473 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   474 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ALA   475 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ARG   476 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   477 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   478 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ARG   479 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ARG   480 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ARG   481 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   482 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   483 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ARG   484 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ARG   485 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   486 DELETION                       
SEQADV 4OG8     A       UNP  O00255    SER   487 DELETION                       
SEQADV 4OG8     A       UNP  O00255    LYS   488 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   489 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   490 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   491 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   492 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   493 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   494 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   495 DELETION                       
SEQADV 4OG8     A       UNP  O00255    LYS   496 DELETION                       
SEQADV 4OG8     A       UNP  O00255    LYS   497 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   498 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ALA   499 DELETION                       
SEQADV 4OG8     A       UNP  O00255    LEU   500 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ASP   501 DELETION                       
SEQADV 4OG8     A       UNP  O00255    LYS   502 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   503 DELETION                       
SEQADV 4OG8     A       UNP  O00255    LEU   504 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   505 DELETION                       
SEQADV 4OG8     A       UNP  O00255    THR   506 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   507 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLN   508 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   509 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ALA   510 DELETION                       
SEQADV 4OG8     A       UNP  O00255    VAL   511 DELETION                       
SEQADV 4OG8     A       UNP  O00255    SER   512 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   513 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   514 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   515 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ARG   516 DELETION                       
SEQADV 4OG8     A       UNP  O00255    LYS   517 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   518 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   519 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   520 DELETION                       
SEQADV 4OG8     A       UNP  O00255    THR   521 DELETION                       
SEQADV 4OG8     A       UNP  O00255    VAL   522 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ALA   523 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   524 DELETION                       
SEQADV 4OG8     A       UNP  O00255    THR   525 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ALA   526 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ARG   527 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   528 DELETION                       
SEQADV 4OG8     A       UNP  O00255    PRO   529 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLU   530 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   531 DELETION                       
SEQADV 4OG8     A       UNP  O00255    GLY   532 DELETION                       
SEQADV 4OG8     A       UNP  O00255    SER   533 DELETION                       
SEQADV 4OG8     A       UNP  O00255    THR   534 DELETION                       
SEQADV 4OG8     A       UNP  O00255    ALA   535 DELETION                       
SEQADV 4OG8     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    TBF  A 601       3                                                       
HET    2SF  A 602      31                                                       
HET    PG4  A 603      13                                                       
HET    SO4  A 604       5                                                       
HET    SO4  A 605       5                                                       
HET    SO4  A 606       5                                                       
HET    DMS  A 607       4                                                       
HET    PGA  A 608       4                                                       
HET    DMS  A 609       4                                                       
HET    DMS  A 610       4                                                       
HET    TBF  A 611       3                                                       
HETNAM     TBF TERT-BUTYL FORMATE                                               
HETNAM     2SF 4-(3-{4-[(R)-AMINO(CYCLOPENTYL)PHENYLMETHYL]PIPERIDIN-           
HETNAM   2 2SF  1-YL}PROPOXY)BENZONITRILE                                       
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     PGA 2-PHOSPHOGLYCOLIC ACID                                           
HETSYN     TBF TERTIARY BUTOXY CARBONYL                                         
FORMUL   2  TBF    2(C5 H10 O2)                                                 
FORMUL   3  2SF    C27 H35 N3 O                                                 
FORMUL   4  PG4    C8 H18 O5                                                    
FORMUL   5  SO4    3(O4 S 2-)                                                   
FORMUL   8  DMS    3(C2 H6 O S)                                                 
FORMUL   9  PGA    C2 H5 O6 P                                                   
FORMUL  13  HOH   *429(H2 O)                                                    
HELIX    1   1 LYS A    4  THR A    9  1                                   6    
HELIX    2   2 SER A   15  GLY A   28  1                                  14    
HELIX    3   3 ASP A   33  VAL A   50  1                                  18    
HELIX    4   4 ASP A   82  VAL A  101  1                                  20    
HELIX    5   5 ASP A  102  TYR A  106  5                                   5    
HELIX    6   6 ARG A  108  VAL A  112  5                                   5    
HELIX    7   7 SER A  114  LEU A  129  1                                  16    
HELIX    8   8 SER A  142  THR A  150  1                                   9    
HELIX    9   9 ASP A  153  LEU A  168  1                                  16    
HELIX   10  10 GLY A  187  GLU A  191  5                                   5    
HELIX   11  11 VAL A  211  GLU A  217  1                                   7    
HELIX   12  12 SER A  219  SER A  226  5                                   8    
HELIX   13  13 ASP A  231  ALA A  242  1                                  12    
HELIX   14  14 SER A  253  LEU A  270  1                                  18    
HELIX   15  15 TYR A  276  GLU A  290  1                                  15    
HELIX   16  16 ASP A  297  TYR A  313  1                                  17    
HELIX   17  17 ILE A  318  ASN A  331  1                                  14    
HELIX   18  18 ASN A  333  GLN A  349  1                                  17    
HELIX   19  19 ASP A  357  ASP A  370  1                                  14    
HELIX   20  20 ASP A  370  ALA A  385  1                                  16    
HELIX   21  21 SER A  402  GLN A  405  5                                   4    
HELIX   22  22 ASP A  406  GLU A  425  1                                  20    
HELIX   23  23 HIS A  433  ARG A  446  1                                  14    
HELIX   24  24 GLU A  448  GLN A  453  1                                   6    
HELIX   25  25 SER A  555  LYS A  562  1                                   8    
HELIX   26  26 GLU A  563  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         4.49                     
CISPEP   2 PHE A   11    PRO A   12          0        -1.68                     
CISPEP   3 VAL A  460    PRO A  461          0        -6.18                     
SITE     1 AC1  4 SER A 154  SER A 155  2SF A 602  HOH A1045                    
SITE     1 AC2 14 SER A 155  SER A 178  HIS A 181  ALA A 242                    
SITE     2 AC2 14 MET A 278  TYR A 319  MET A 322  TYR A 323                    
SITE     3 AC2 14 TRP A 341  GLU A 363  TBF A 601  TBF A 611                    
SITE     4 AC2 14 HOH A 747  HOH A1070                                          
SITE     1 AC3  8 LEU A  75  THR A  76  TYR A 361  PHE A 365                    
SITE     2 AC3  8 HIS A 433  HOH A 735  HOH A 795  HOH A1024                    
SITE     1 AC4  5 TYR A 133  PHE A 134  ARG A 137  ARG A 332                    
SITE     2 AC4  5 HOH A1022                                                     
SITE     1 AC5  3 PRO A  12  ARG A  14  HOH A1031                               
SITE     1 AC6  2 LYS A 377  ARG A 446                                          
SITE     1 AC7  7 PHE A  43  PHE A  47  PRO A  79  GLY A 386                    
SITE     2 AC7  7 GLN A 400  HOH A 845  HOH A 895                               
SITE     1 AC8  2 TRP A 126  LYS A 135                                          
SITE     1 AC9  6 VAL A 185  GLY A 190  GLU A 191  TYR A 227                    
SITE     2 AC9  6 ARG A 229  SER A 583                                          
SITE     1 BC1  6 VAL A 334  ARG A 335  ALA A 403  HOH A 803                    
SITE     2 BC1  6 HOH A1104  HOH A1129                                          
SITE     1 BC2  1 2SF A 602                                                     
CRYST1   48.782   80.224  124.691  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      0.020499  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012465  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008020        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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