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Entry: 3SMQ
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HEADER    TRANSFERASE                             28-JUN-11   3SMQ              
TITLE     CRYSTAL STRUCTURE OF PROTEIN ARGININE METHYLTRANSFERASE 3             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN ARGININE N-METHYLTRANSFERASE 3;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 211-531;                                      
COMPND   5 SYNONYM: HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN METHYLTRANSFERASE-  
COMPND   6 LIKE PROTEIN 3;                                                      
COMPND   7 EC: 2.1.1.-;                                                         
COMPND   8 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: PRMT3, HRMT1L3;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-V2R-PRAR2;                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC                                
KEYWDS    STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, PRMT3,      
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.DOBROVETSKY,A.DONG,J.R.WALKER,A.SIARHEYEVA,G.SENISTERRA,G.A.WASNEY, 
AUTHOR   2 D.SMIL,Y.BOLSHAN,K.T.NGUYEN,A.ALLALI-HASSANI,T.HAJIAN,G.PODA,        
AUTHOR   3 C.BOUNTRA,J.WEIGELT,A.M.EDWARDS,R.AL-AWAR,P.J.BROWN,M.SCHAPIRA,      
AUTHOR   4 C.H.ARROWSMITH,M.VEDADI,STRUCTURAL GENOMICS CONSORTIUM (SGC)         
REVDAT   3   13-SEP-23 3SMQ    1       REMARK SEQADV                            
REVDAT   2   24-JUL-13 3SMQ    1       JRNL                                     
REVDAT   1   31-AUG-11 3SMQ    0                                                
JRNL        AUTH   A.SIARHEYEVA,G.SENISTERRA,A.ALLALI-HASSANI,A.DONG,           
JRNL        AUTH 2 E.DOBROVETSKY,G.A.WASNEY,I.CHAU,R.MARCELLUS,T.HAJIAN,F.LIU,  
JRNL        AUTH 3 I.KORBOUKH,D.SMIL,Y.BOLSHAN,J.MIN,H.WU,H.ZENG,P.LOPPNAU,     
JRNL        AUTH 4 G.PODA,C.GRIFFIN,A.AMAN,P.J.BROWN,J.JIN,R.AL-AWAR,           
JRNL        AUTH 5 C.H.ARROWSMITH,M.SCHAPIRA,M.VEDADI                           
JRNL        TITL   AN ALLOSTERIC INHIBITOR OF PROTEIN ARGININE                  
JRNL        TITL 2 METHYLTRANSFERASE 3.                                         
JRNL        REF    STRUCTURE                     V.  20  1425 2012              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   22795084                                                     
JRNL        DOI    10.1016/J.STR.2012.06.001                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 28754                          
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) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 954                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1776                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 66                           
REMARK   3   BIN FREE R VALUE                    : 0.3180                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2330                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 223                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.54000                                             
REMARK   3    B22 (A**2) : -0.54000                                             
REMARK   3    B33 (A**2) : 1.08000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.133         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.089         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.030         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2450 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3324 ; 1.214 ; 1.968       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   307 ; 5.788 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    94 ;35.162 ;24.787       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   434 ;11.952 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ;18.008 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   386 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1795 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  1514 ; 0.524 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2468 ; 1.027 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   936 ; 1.750 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   856 ; 2.901 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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   243        A   253                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.8556  12.0996  -3.8731              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1414 T22:   0.0900                                     
REMARK   3      T33:   0.2269 T12:   0.0760                                     
REMARK   3      T13:  -0.0199 T23:   0.0769                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5507 L22:   3.8413                                     
REMARK   3      L33:  11.9432 L12:   3.2745                                     
REMARK   3      L13:  -3.7164 L23:  -7.2377                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0409 S12:  -0.1931 S13:  -0.1542                       
REMARK   3      S21:  -0.0070 S22:  -0.3129 S23:  -0.5362                       
REMARK   3      S31:   0.3613 S32:   0.1300 S33:   0.3538                       
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   254        A   294                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.1681  23.6402   2.5944              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1127 T22:   0.1384                                     
REMARK   3      T33:   0.1483 T12:   0.0373                                     
REMARK   3      T13:   0.0078 T23:   0.0269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5825 L22:   1.0477                                     
REMARK   3      L33:   1.1270 L12:  -0.3720                                     
REMARK   3      L13:  -0.3571 L23:  -0.1512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0334 S12:   0.0957 S13:   0.0525                       
REMARK   3      S21:  -0.0236 S22:  -0.0233 S23:  -0.0091                       
REMARK   3      S31:   0.0300 S32:  -0.1015 S33:  -0.0100                       
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   295        A   337                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.4118  30.2660  -4.8683              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0966 T22:   0.0951                                     
REMARK   3      T33:   0.2026 T12:   0.0046                                     
REMARK   3      T13:   0.0516 T23:   0.0890                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1349 L22:   1.0556                                     
REMARK   3      L33:   1.9990 L12:   0.1513                                     
REMARK   3      L13:   0.4248 L23:   0.7290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0299 S12:   0.1815 S13:   0.1750                       
REMARK   3      S21:  -0.1401 S22:  -0.0416 S23:  -0.2084                       
REMARK   3      S31:  -0.2149 S32:   0.1530 S33:   0.0117                       
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   338        A   379                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.8974  25.1563  11.3920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1294 T22:   0.1166                                     
REMARK   3      T33:   0.1817 T12:   0.0056                                     
REMARK   3      T13:  -0.0155 T23:  -0.0241                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7247 L22:   2.3688                                     
REMARK   3      L33:   0.3990 L12:  -1.1110                                     
REMARK   3      L13:   0.3530 L23:  -0.7901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0171 S12:  -0.0188 S13:   0.0915                       
REMARK   3      S21:   0.1052 S22:  -0.0443 S23:  -0.1427                       
REMARK   3      S31:  -0.0861 S32:   0.0938 S33:   0.0614                       
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   380        A   412                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.0877  -8.4137  14.7124              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1783 T22:   0.1235                                     
REMARK   3      T33:   0.1038 T12:   0.0289                                     
REMARK   3      T13:  -0.0038 T23:   0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4808 L22:   0.9301                                     
REMARK   3      L33:   0.4431 L12:  -0.8606                                     
REMARK   3      L13:  -0.5045 L23:   0.6727                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0173 S12:   0.0327 S13:  -0.0812                       
REMARK   3      S21:   0.0792 S22:   0.0252 S23:   0.0581                       
REMARK   3      S31:   0.1006 S32:   0.0165 S33:  -0.0078                       
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   413        A   438                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0130   0.9207  18.2255              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1271 T22:   0.0956                                     
REMARK   3      T33:   0.1319 T12:  -0.0029                                     
REMARK   3      T13:  -0.0023 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0655 L22:   1.3349                                     
REMARK   3      L33:   0.8388 L12:  -0.8622                                     
REMARK   3      L13:   0.6796 L23:   0.1143                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0351 S12:  -0.0061 S13:  -0.0273                       
REMARK   3      S21:  -0.0308 S22:  -0.0137 S23:   0.0926                       
REMARK   3      S31:   0.0644 S32:  -0.0174 S33:  -0.0214                       
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   439        A   465                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.4378  10.6707  24.7069              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0773 T22:   0.1106                                     
REMARK   3      T33:   0.1503 T12:   0.0246                                     
REMARK   3      T13:  -0.0030 T23:  -0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6020 L22:   3.7098                                     
REMARK   3      L33:   0.8206 L12:  -0.2728                                     
REMARK   3      L13:   0.4162 L23:  -0.7315                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1293 S12:  -0.2294 S13:   0.0859                       
REMARK   3      S21:   0.1230 S22:   0.0055 S23:  -0.0751                       
REMARK   3      S31:  -0.0492 S32:  -0.1209 S33:   0.1238                       
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   466        A   494                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.6711  12.2243  14.6784              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1490 T22:   0.1495                                     
REMARK   3      T33:   0.1510 T12:   0.0189                                     
REMARK   3      T13:   0.0093 T23:   0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7779 L22:   1.4566                                     
REMARK   3      L33:   0.1692 L12:  -1.1329                                     
REMARK   3      L13:   0.4670 L23:  -0.6484                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0476 S12:  -0.0841 S13:  -0.0395                       
REMARK   3      S21:   0.1127 S22:   0.0751 S23:   0.0677                       
REMARK   3      S31:   0.0098 S32:  -0.0619 S33:  -0.0275                       
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   495        A   519                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9063  -0.5274  22.1766              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1356 T22:   0.1133                                     
REMARK   3      T33:   0.1324 T12:  -0.0124                                     
REMARK   3      T13:   0.0208 T23:   0.0355                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0590 L22:   1.2791                                     
REMARK   3      L33:   0.2727 L12:  -0.7388                                     
REMARK   3      L13:   0.4967 L23:  -0.0796                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0516 S12:   0.0098 S13:  -0.1056                       
REMARK   3      S21:   0.0568 S22:  -0.0565 S23:   0.0523                       
REMARK   3      S31:   0.0098 S32:   0.0940 S33:   0.0049                       
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   520        A   547                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.6695   6.8105  23.2092              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1229 T22:   0.1368                                     
REMARK   3      T33:   0.1398 T12:  -0.0198                                     
REMARK   3      T13:  -0.0102 T23:   0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6415 L22:   1.0050                                     
REMARK   3      L33:   1.8020 L12:  -0.8364                                     
REMARK   3      L13:   0.4379 L23:   0.2191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0277 S12:   0.1018 S13:   0.1018                       
REMARK   3      S21:   0.0721 S22:  -0.0006 S23:  -0.1973                       
REMARK   3      S31:  -0.0875 S32:   0.0341 S33:   0.0283                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3SMQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUL-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000066393.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAY-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29893                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 11.50                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 36.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.55800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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: 2FYT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20.0% PEG 4K, 0.2M MG OAC, 0.1M NA       
REMARK 280  CACO PH6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.98850            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       35.32450            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       35.32450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      128.98275            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       35.32450            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       35.32450            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       42.99425            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       35.32450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.32450            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      128.98275            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       35.32450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.32450            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       42.99425            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       85.98850            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL                        
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 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     MET A   209                                                      
REMARK 465     GLY A   210                                                      
REMARK 465     SER A   211                                                      
REMARK 465     SER A   212                                                      
REMARK 465     HIS A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     HIS A   215                                                      
REMARK 465     HIS A   216                                                      
REMARK 465     HIS A   217                                                      
REMARK 465     HIS A   218                                                      
REMARK 465     SER A   219                                                      
REMARK 465     SER A   220                                                      
REMARK 465     GLY A   221                                                      
REMARK 465     LEU A   222                                                      
REMARK 465     VAL A   223                                                      
REMARK 465     PRO A   224                                                      
REMARK 465     ARG A   225                                                      
REMARK 465     GLY A   226                                                      
REMARK 465     SER A   227                                                      
REMARK 465     ASP A   228                                                      
REMARK 465     LEU A   229                                                      
REMARK 465     GLN A   230                                                      
REMARK 465     GLU A   231                                                      
REMARK 465     ASP A   232                                                      
REMARK 465     GLU A   233                                                      
REMARK 465     ASP A   234                                                      
REMARK 465     GLY A   235                                                      
REMARK 465     VAL A   236                                                      
REMARK 465     TYR A   237                                                      
REMARK 465     PHE A   238                                                      
REMARK 465     SER A   239                                                      
REMARK 465     SER A   240                                                      
REMARK 465     TYR A   241                                                      
REMARK 465     GLY A   242                                                      
REMARK 465     ASN A   525                                                      
REMARK 465     LYS A   526                                                      
REMARK 465     LYS A   527                                                      
REMARK 465     ASP A   528                                                      
REMARK 465     PRO A   529                                                      
REMARK 465     ARG A   530                                                      
REMARK 465     GLN A   548                                                      
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     HIS A 243    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE A 246    CD1                                                 
REMARK 470     GLU A 305    CD   OE1  OE2                                       
REMARK 470     ARG A 315    CZ   NH1  NH2                                       
REMARK 470     LYS A 329    CE   NZ                                             
REMARK 470     GLU A 355    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 367    CE   NZ                                             
REMARK 470     LYS A 371    CD   CE   NZ                                        
REMARK 470     LYS A 427    CE   NZ                                             
REMARK 470     ILE A 446    CD1                                                 
REMARK 470     LYS A 458    NZ                                                  
REMARK 470     LYS A 524    CG   CD   CE   NZ                                   
REMARK 470     SER A 531    OG                                                  
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    LEU A 352      -51.58     67.70                                   
REMARK 500    ASP A 389       77.21   -153.37                                   
REMARK 500    GLU A 477      -55.08   -124.12                                   
REMARK 500    GLU A 477      -42.13   -131.13                                   
REMARK 500    LYS A 498     -139.92     47.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TDU A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1000                 
DBREF  3SMQ A  228   548  UNP    O60678   ANM3_HUMAN     211    531             
SEQADV 3SMQ MET A  209  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ GLY A  210  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ SER A  211  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ SER A  212  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ HIS A  213  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ HIS A  214  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ HIS A  215  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ HIS A  216  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ HIS A  217  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ HIS A  218  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ SER A  219  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ SER A  220  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ GLY A  221  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ LEU A  222  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ VAL A  223  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ PRO A  224  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ ARG A  225  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ GLY A  226  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ SER A  227  UNP  O60678              EXPRESSION TAG                 
SEQADV 3SMQ ASN A  525  UNP  O60678    SER   508 VARIANT                        
SEQRES   1 A  340  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  340  LEU VAL PRO ARG GLY SER ASP LEU GLN GLU ASP GLU ASP          
SEQRES   3 A  340  GLY VAL TYR PHE SER SER TYR GLY HIS TYR GLY ILE HIS          
SEQRES   4 A  340  GLU GLU MET LEU LYS ASP LYS ILE ARG THR GLU SER TYR          
SEQRES   5 A  340  ARG ASP PHE ILE TYR GLN ASN PRO HIS ILE PHE LYS ASP          
SEQRES   6 A  340  LYS VAL VAL LEU ASP VAL GLY CYS GLY THR GLY ILE LEU          
SEQRES   7 A  340  SER MET PHE ALA ALA LYS ALA GLY ALA LYS LYS VAL LEU          
SEQRES   8 A  340  GLY VAL ASP GLN SER GLU ILE LEU TYR GLN ALA MET ASP          
SEQRES   9 A  340  ILE ILE ARG LEU ASN LYS LEU GLU ASP THR ILE THR LEU          
SEQRES  10 A  340  ILE LYS GLY LYS ILE GLU GLU VAL HIS LEU PRO VAL GLU          
SEQRES  11 A  340  LYS VAL ASP VAL ILE ILE SER GLU TRP MET GLY TYR PHE          
SEQRES  12 A  340  LEU LEU PHE GLU SER MET LEU ASP SER VAL LEU TYR ALA          
SEQRES  13 A  340  LYS ASN LYS TYR LEU ALA LYS GLY GLY SER VAL TYR PRO          
SEQRES  14 A  340  ASP ILE CYS THR ILE SER LEU VAL ALA VAL SER ASP VAL          
SEQRES  15 A  340  ASN LYS HIS ALA ASP ARG ILE ALA PHE TRP ASP ASP VAL          
SEQRES  16 A  340  TYR GLY PHE LYS MET SER CYS MET LYS LYS ALA VAL ILE          
SEQRES  17 A  340  PRO GLU ALA VAL VAL GLU VAL LEU ASP PRO LYS THR LEU          
SEQRES  18 A  340  ILE SER GLU PRO CYS GLY ILE LYS HIS ILE ASP CYS HIS          
SEQRES  19 A  340  THR THR SER ILE SER ASP LEU GLU PHE SER SER ASP PHE          
SEQRES  20 A  340  THR LEU LYS ILE THR ARG THR SER MET CYS THR ALA ILE          
SEQRES  21 A  340  ALA GLY TYR PHE ASP ILE TYR PHE GLU LYS ASN CYS HIS          
SEQRES  22 A  340  ASN ARG VAL VAL PHE SER THR GLY PRO GLN SER THR LYS          
SEQRES  23 A  340  THR HIS TRP LYS GLN THR VAL PHE LEU LEU GLU LYS PRO          
SEQRES  24 A  340  PHE SER VAL LYS ALA GLY GLU ALA LEU LYS GLY LYS VAL          
SEQRES  25 A  340  THR VAL HIS LYS ASN LYS LYS ASP PRO ARG SER LEU THR          
SEQRES  26 A  340  VAL THR LEU THR LEU ASN ASN SER THR GLN THR TYR GLY          
SEQRES  27 A  340  LEU GLN                                                      
HET    TDU  A   1      21                                                       
HET     CL  A1000       1                                                       
HET    UNX  A 549       1                                                       
HET    UNX  A   2       1                                                       
HET    UNX  A   3       1                                                       
HET    UNX  A   4       1                                                       
HET    UNX  A   5       1                                                       
HET    UNX  A   7       1                                                       
HET    UNX  A   8       1                                                       
HET    UNX  A   9       1                                                       
HET    UNX  A  11       1                                                       
HET    UNX  A  12       1                                                       
HETNAM     TDU 1-(1,2,3-BENZOTHIADIAZOL-6-YL)-3-[2-(CYCLOHEX-1-EN-1-            
HETNAM   2 TDU  YL)ETHYL]UREA                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETSYN     TDU 1-(BENZO[D][1,2,3]THIADIAZOL-6-YL)-3-(2-                         
HETSYN   2 TDU  CYCLOHEXENYLETHYL)UREA                                          
FORMUL   2  TDU    C15 H18 N4 O S                                               
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  UNX    10(X)                                                        
FORMUL  14  HOH   *223(H2 O)                                                    
HELIX    1   1 HIS A  243  LYS A  252  1                                  10    
HELIX    2   2 ASP A  253  ASN A  267  1                                  15    
HELIX    3   3 PRO A  268  PHE A  271  5                                   4    
HELIX    4   4 GLY A  284  ALA A  293  1                                  10    
HELIX    5   5 GLU A  305  ASN A  317  1                                  13    
HELIX    6   6 MET A  357  TYR A  368  1                                  12    
HELIX    7   7 ASP A  389  ILE A  397  1                                   9    
HELIX    8   8 ALA A  398  ASP A  402  5                                   5    
HELIX    9   9 MET A  408  CYS A  410  5                                   3    
HELIX   10  10 MET A  411  ILE A  416  1                                   6    
HELIX   11  11 ASP A  425  LEU A  429  5                                   5    
HELIX   12  12 SER A  445  GLU A  450  5                                   6    
SHEET    1   A 5 ILE A 323  LYS A 327  0                                        
SHEET    2   A 5 LYS A 297  ASP A 302  1  N  VAL A 298   O  THR A 324           
SHEET    3   A 5 VAL A 275  VAL A 279  1  N  ASP A 278   O  LEU A 299           
SHEET    4   A 5 VAL A 340  ILE A 344  1  O  VAL A 342   N  LEU A 277           
SHEET    5   A 5 LEU A 369  TYR A 376  1  O  ALA A 370   N  VAL A 340           
SHEET    1   B 5 VAL A 420  GLU A 422  0                                        
SHEET    2   B 5 GLN A 499  VAL A 510 -1  O  VAL A 501   N  VAL A 420           
SHEET    3   B 5 SER A 463  PHE A 476 -1  N  SER A 463   O  VAL A 510           
SHEET    4   B 5 ILE A 379  VAL A 387 -1  N  VAL A 385   O  ALA A 469           
SHEET    5   B 5 CYS A 434  ASP A 440 -1  O  ILE A 436   N  ILE A 382           
SHEET    1   C 4 VAL A 420  GLU A 422  0                                        
SHEET    2   C 4 GLN A 499  VAL A 510 -1  O  VAL A 501   N  VAL A 420           
SHEET    3   C 4 SER A 463  PHE A 476 -1  N  SER A 463   O  VAL A 510           
SHEET    4   C 4 VAL A 484  SER A 487 -1  O  VAL A 484   N  PHE A 476           
SHEET    1   D 4 PHE A 451  LYS A 458  0                                        
SHEET    2   D 4 ALA A 515  HIS A 523 -1  O  LEU A 516   N  LEU A 457           
SHEET    3   D 4 THR A 533  LEU A 538 -1  O  THR A 535   N  THR A 521           
SHEET    4   D 4 SER A 541  GLY A 546 -1  O  TYR A 545   N  VAL A 534           
CISPEP   1 TYR A  376    PRO A  377          0        -1.24                     
SITE     1 AC1 11 GLY A 245  GLU A 248  VAL A 387  ASP A 389                    
SITE     2 AC1 11 LYS A 392  HIS A 393  ARG A 396  VAL A 420                    
SITE     3 AC1 11 GLU A 422  THR A 466  ALA A 467                               
SITE     1 AC2  3 SER A 388  SER A 463  MET A 464                               
CRYST1   70.649   70.649  171.977  90.00  90.00  90.00 P 43 21 2     8          
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      0.014154  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014154  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005815        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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