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Database: PDB
Entry: 3Q6M
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HEADER    CHAPERONE                               03-JAN-11   3Q6M              
TITLE     CRYSTAL STRUCTURE OF HUMAN MC-HSP90 IN C2221 SPACE GROUP              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: MIDDLE AND C-TERMINAL DOMAIN, UNP RESIDUES 293-732;        
COMPND   5 SYNONYM: HSP90, HEAT SHOCK 86 KDA, HSP 86, HSP86, RENAL CARCINOMA    
COMPND   6 ANTIGEN NY-REN-38;                                                   
COMPND   7 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: HSP90AA1, HSP90A, HSPC1, HSPCA;                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1                                 
KEYWDS    THREE DOMAINS, TRIMER OF DIMER, HEXAMER, CHAPERONE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.C.LEE,T.W.LIN,T.P.KO,A.H.-J.WANG                                    
REVDAT   2   05-MAR-14 3Q6M    1       JRNL   VERSN                             
REVDAT   1   01-JUN-11 3Q6M    0                                                
JRNL        AUTH   C.C.LEE,T.W.LIN,T.P.KO,A.H.-J.WANG                           
JRNL        TITL   THE HEXAMERIC STRUCTURES OF HUMAN HEAT SHOCK PROTEIN 90      
JRNL        REF    PLOS ONE                      V.   6 19961 2011              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   21647436                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0019961                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 41365                          
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) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2185                            
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2909                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 139                          
REMARK   3   BIN FREE R VALUE                    : 0.3330                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9197                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 133                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 104.50                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.51000                                             
REMARK   3    B22 (A**2) : -2.40000                                             
REMARK   3    B33 (A**2) : 2.91000                                              
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): 0.985         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.367         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.302         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.924        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9373 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12592 ; 1.405 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1103 ; 6.332 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   455 ;41.161 ;24.923       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1895 ;21.599 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    54 ;22.224 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1392 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6882 ; 0.005 ; 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):  5568 ; 0.564 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9051 ; 1.109 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3805 ; 1.478 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3541 ; 2.645 ; 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  : 12                                         
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   294        A   349                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.0840 -39.8350  -4.1870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0310 T22:   0.3560                                     
REMARK   3      T33:   0.3251 T12:   0.0102                                     
REMARK   3      T13:   0.0542 T23:   0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.3260 L22:  10.0000                                     
REMARK   3      L33:   5.6767 L12:   0.5494                                     
REMARK   3      L13:  -2.4375 L23:   0.5490                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1648 S12:   0.9210 S13:   0.2407                       
REMARK   3      S21:  -0.4142 S22:  -0.1621 S23:  -0.2853                       
REMARK   3      S31:  -0.3210 S32:  -0.0257 S33:  -0.0027                       
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   359        A   395                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.2690 -35.9720   7.6680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2883 T22:   0.4277                                     
REMARK   3      T33:   0.5445 T12:  -0.1618                                     
REMARK   3      T13:  -0.0431 T23:  -0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  23.1677 L22:   7.1841                                     
REMARK   3      L33:   6.7108 L12:   5.4715                                     
REMARK   3      L13:  -8.3829 L23:   1.6042                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6541 S12:  -2.1393 S13:   0.7811                       
REMARK   3      S21:   0.9372 S22:  -0.7653 S23:   0.2337                       
REMARK   3      S31:  -0.2249 S32:   0.7248 S33:   0.1111                       
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   405        A   615                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.8440 -51.8110  12.9890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2281 T22:   0.4714                                     
REMARK   3      T33:   0.5403 T12:  -0.0792                                     
REMARK   3      T13:   0.1138 T23:  -0.1653                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1593 L22:   4.4504                                     
REMARK   3      L33:   1.0889 L12:   3.1607                                     
REMARK   3      L13:  -2.0566 L23:  -2.1260                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4054 S12:  -0.0572 S13:   0.5293                       
REMARK   3      S21:   0.5099 S22:   0.0050 S23:   0.2220                       
REMARK   3      S31:  -0.2846 S32:   0.0747 S33:  -0.4104                       
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   630        A   697                          
REMARK   3    ORIGIN FOR THE GROUP (A): -56.0270 -75.0010  27.4220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2712 T22:   0.3608                                     
REMARK   3      T33:   0.2198 T12:  -0.0336                                     
REMARK   3      T13:  -0.0972 T23:   0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9518 L22:   5.1924                                     
REMARK   3      L33:   5.2518 L12:  -1.5100                                     
REMARK   3      L13:  -2.2194 L23:   0.6801                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0836 S12:  -0.2864 S13:  -0.0581                       
REMARK   3      S21:   0.5755 S22:   0.1612 S23:   0.2360                       
REMARK   3      S31:   0.3617 S32:   0.2685 S33:  -0.0776                       
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 :   B   294        B   349                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2130 -65.7450  48.0350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1560 T22:   0.1937                                     
REMARK   3      T33:   0.3466 T12:  -0.0344                                     
REMARK   3      T13:  -0.0128 T23:   0.0863                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3786 L22:   6.9247                                     
REMARK   3      L33:   7.3289 L12:  -0.4757                                     
REMARK   3      L13:  -0.0573 L23:   1.1757                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2826 S12:  -0.1924 S13:   0.6370                       
REMARK   3      S21:   0.1678 S22:  -0.0436 S23:  -0.1147                       
REMARK   3      S31:  -0.0403 S32:   0.1279 S33:   0.3263                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   359        B   395                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4910 -64.7020  36.1240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2061 T22:   0.4213                                     
REMARK   3      T33:   0.3107 T12:  -0.0246                                     
REMARK   3      T13:   0.0190 T23:   0.2258                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  21.3060 L22:  13.4306                                     
REMARK   3      L33:   5.3572 L12:  13.7397                                     
REMARK   3      L13:  -0.1118 L23:   2.7460                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8268 S12:   1.5437 S13:  -0.0262                       
REMARK   3      S21:  -0.8776 S22:   0.4820 S23:  -0.3054                       
REMARK   3      S31:  -0.3065 S32:   0.2146 S33:   0.3448                       
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 :   B   405        B   615                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.7660 -87.2040  31.0420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1552 T22:   0.4090                                     
REMARK   3      T33:   0.4213 T12:  -0.0036                                     
REMARK   3      T13:   0.1000 T23:  -0.0988                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4103 L22:   2.1153                                     
REMARK   3      L33:   2.7927 L12:   2.1745                                     
REMARK   3      L13:   3.3526 L23:   1.3268                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0860 S12:   0.5818 S13:  -0.4817                       
REMARK   3      S21:  -0.0896 S22:   0.1611 S23:  -0.1047                       
REMARK   3      S31:   0.0642 S32:   0.2588 S33:  -0.2471                       
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 :   B   630        B   699                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.1890 -87.3610  17.0410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1976 T22:   0.6694                                     
REMARK   3      T33:   0.2374 T12:  -0.0023                                     
REMARK   3      T13:  -0.0638 T23:  -0.0754                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3570 L22:   6.9404                                     
REMARK   3      L33:   4.3083 L12:  -3.9793                                     
REMARK   3      L13:   1.9553 L23:   0.3621                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4697 S12:   1.0533 S13:  -0.4549                       
REMARK   3      S21:  -0.6739 S22:  -0.1939 S23:   0.4453                       
REMARK   3      S31:   0.0250 S32:  -0.5865 S33:  -0.2759                       
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 :   C   294        C   349                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.6050 -41.8410  48.7860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1026 T22:   0.2397                                     
REMARK   3      T33:   0.4063 T12:   0.1010                                     
REMARK   3      T13:   0.0713 T23:   0.0540                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.7687 L22:  13.5197                                     
REMARK   3      L33:   5.7409 L12:   2.8608                                     
REMARK   3      L13:   1.0463 L23:  -0.9458                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2391 S12:  -0.7859 S13:  -0.4874                       
REMARK   3      S21:   0.6558 S22:   0.3175 S23:  -0.0668                       
REMARK   3      S31:   0.2421 S32:   0.0432 S33:  -0.0785                       
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 :   C   360        C   395                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.8780 -46.7360  37.2220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3036 T22:   0.2439                                     
REMARK   3      T33:   0.4858 T12:   0.0556                                     
REMARK   3      T13:   0.0279 T23:  -0.0640                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6085 L22:  25.5556                                     
REMARK   3      L33:   6.3676 L12:  -1.1440                                     
REMARK   3      L13:   1.6856 L23:  -3.8337                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1779 S12:   0.5778 S13:  -0.7514                       
REMARK   3      S21:  -2.0859 S22:   0.2151 S23:  -0.0195                       
REMARK   3      S31:   0.4408 S32:   0.2462 S33:  -0.0372                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   406        C   614                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.1750 -10.4380  31.2960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5624 T22:   0.1903                                     
REMARK   3      T33:   0.4477 T12:  -0.0284                                     
REMARK   3      T13:  -0.0913 T23:   0.0912                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2313 L22:  12.9539                                     
REMARK   3      L33:   1.5243 L12:  -0.0055                                     
REMARK   3      L13:   0.2304 L23:  -1.6646                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1359 S12:   0.1345 S13:   0.0888                       
REMARK   3      S21:  -1.8138 S22:   0.3197 S23:   0.9352                       
REMARK   3      S31:  -0.1540 S32:  -0.0801 S33:  -0.1838                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   630        C   697                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2870  11.4830  16.5860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9844 T22:   0.4290                                     
REMARK   3      T33:   0.3202 T12:  -0.0139                                     
REMARK   3      T13:   0.2658 T23:   0.1801                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.7823 L22:   3.4851                                     
REMARK   3      L33:   0.5569 L12:   2.6852                                     
REMARK   3      L13:  -0.5669 L23:  -0.4665                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7187 S12:   0.6395 S13:   0.8918                       
REMARK   3      S21:  -1.4590 S22:   0.7046 S23:   0.1953                       
REMARK   3      S31:   0.4844 S32:  -0.0988 S33:   0.0141                       
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:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  U VALUES: WITH TLS ADDED                                            
REMARK   4                                                                      
REMARK   4 3Q6M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063259.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAY-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.4-5.8                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43634                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
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 2CGE                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5M AMMONIUM SULFATE, 0.1M TRIS-        
REMARK 280  SODIUM CITRATE, 0.1MM CIS-DICHLORO(ETHYLENEDIAMINE)PLATINUM (II),   
REMARK 280  PH 5.4-5.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298.0K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.81200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       43.81200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       81.35100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      152.27650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       81.35100            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      152.27650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       43.81200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       81.35100            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      152.27650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       43.81200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       81.35100            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      152.27650            
REMARK 290   SMTRY3   8  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: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       43.81200            
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     ALA A   291                                                      
REMARK 465     ALA A   292                                                      
REMARK 465     THR A   293                                                      
REMARK 465     ASP A   350                                                      
REMARK 465     LEU A   351                                                      
REMARK 465     PHE A   352                                                      
REMARK 465     GLU A   353                                                      
REMARK 465     ASN A   354                                                      
REMARK 465     ARG A   355                                                      
REMARK 465     LYS A   356                                                      
REMARK 465     LYS A   357                                                      
REMARK 465     LYS A   358                                                      
REMARK 465     LEU A   396                                                      
REMARK 465     ASN A   397                                                      
REMARK 465     ILE A   398                                                      
REMARK 465     SER A   399                                                      
REMARK 465     ARG A   400                                                      
REMARK 465     GLU A   401                                                      
REMARK 465     MET A   402                                                      
REMARK 465     LEU A   403                                                      
REMARK 465     GLN A   404                                                      
REMARK 465     ALA A   616                                                      
REMARK 465     GLN A   617                                                      
REMARK 465     ALA A   618                                                      
REMARK 465     LEU A   619                                                      
REMARK 465     ARG A   620                                                      
REMARK 465     ASP A   621                                                      
REMARK 465     ASN A   622                                                      
REMARK 465     SER A   623                                                      
REMARK 465     THR A   624                                                      
REMARK 465     MET A   625                                                      
REMARK 465     GLY A   626                                                      
REMARK 465     TYR A   627                                                      
REMARK 465     MET A   628                                                      
REMARK 465     ALA A   629                                                      
REMARK 465     ILE A   698                                                      
REMARK 465     ASP A   699                                                      
REMARK 465     GLU A   700                                                      
REMARK 465     ASP A   701                                                      
REMARK 465     ASP A   702                                                      
REMARK 465     PRO A   703                                                      
REMARK 465     THR A   704                                                      
REMARK 465     ALA A   705                                                      
REMARK 465     ASP A   706                                                      
REMARK 465     ASP A   707                                                      
REMARK 465     THR A   708                                                      
REMARK 465     SER A   709                                                      
REMARK 465     ALA A   710                                                      
REMARK 465     ALA A   711                                                      
REMARK 465     VAL A   712                                                      
REMARK 465     THR A   713                                                      
REMARK 465     GLU A   714                                                      
REMARK 465     GLU A   715                                                      
REMARK 465     MET A   716                                                      
REMARK 465     PRO A   717                                                      
REMARK 465     PRO A   718                                                      
REMARK 465     LEU A   719                                                      
REMARK 465     GLU A   720                                                      
REMARK 465     GLY A   721                                                      
REMARK 465     ASP A   722                                                      
REMARK 465     ASP A   723                                                      
REMARK 465     ASP A   724                                                      
REMARK 465     THR A   725                                                      
REMARK 465     SER A   726                                                      
REMARK 465     ARG A   727                                                      
REMARK 465     MET A   728                                                      
REMARK 465     GLU A   729                                                      
REMARK 465     GLU A   730                                                      
REMARK 465     VAL A   731                                                      
REMARK 465     ASP A   732                                                      
REMARK 465     HIS A   733                                                      
REMARK 465     HIS A   734                                                      
REMARK 465     HIS A   735                                                      
REMARK 465     HIS A   736                                                      
REMARK 465     HIS A   737                                                      
REMARK 465     HIS A   738                                                      
REMARK 465     ALA B   291                                                      
REMARK 465     ALA B   292                                                      
REMARK 465     THR B   293                                                      
REMARK 465     ASP B   350                                                      
REMARK 465     LEU B   351                                                      
REMARK 465     PHE B   352                                                      
REMARK 465     GLU B   353                                                      
REMARK 465     ASN B   354                                                      
REMARK 465     ARG B   355                                                      
REMARK 465     LYS B   356                                                      
REMARK 465     LYS B   357                                                      
REMARK 465     LYS B   358                                                      
REMARK 465     LEU B   396                                                      
REMARK 465     ASN B   397                                                      
REMARK 465     ILE B   398                                                      
REMARK 465     SER B   399                                                      
REMARK 465     ARG B   400                                                      
REMARK 465     GLU B   401                                                      
REMARK 465     MET B   402                                                      
REMARK 465     LEU B   403                                                      
REMARK 465     GLN B   404                                                      
REMARK 465     ALA B   616                                                      
REMARK 465     GLN B   617                                                      
REMARK 465     ALA B   618                                                      
REMARK 465     LEU B   619                                                      
REMARK 465     ARG B   620                                                      
REMARK 465     ASP B   621                                                      
REMARK 465     ASN B   622                                                      
REMARK 465     SER B   623                                                      
REMARK 465     THR B   624                                                      
REMARK 465     MET B   625                                                      
REMARK 465     GLY B   626                                                      
REMARK 465     TYR B   627                                                      
REMARK 465     MET B   628                                                      
REMARK 465     ALA B   629                                                      
REMARK 465     GLU B   700                                                      
REMARK 465     ASP B   701                                                      
REMARK 465     ASP B   702                                                      
REMARK 465     PRO B   703                                                      
REMARK 465     THR B   704                                                      
REMARK 465     ALA B   705                                                      
REMARK 465     ASP B   706                                                      
REMARK 465     ASP B   707                                                      
REMARK 465     THR B   708                                                      
REMARK 465     SER B   709                                                      
REMARK 465     ALA B   710                                                      
REMARK 465     ALA B   711                                                      
REMARK 465     VAL B   712                                                      
REMARK 465     THR B   713                                                      
REMARK 465     GLU B   714                                                      
REMARK 465     GLU B   715                                                      
REMARK 465     MET B   716                                                      
REMARK 465     PRO B   717                                                      
REMARK 465     PRO B   718                                                      
REMARK 465     LEU B   719                                                      
REMARK 465     GLU B   720                                                      
REMARK 465     GLY B   721                                                      
REMARK 465     ASP B   722                                                      
REMARK 465     ASP B   723                                                      
REMARK 465     ASP B   724                                                      
REMARK 465     THR B   725                                                      
REMARK 465     SER B   726                                                      
REMARK 465     ARG B   727                                                      
REMARK 465     MET B   728                                                      
REMARK 465     GLU B   729                                                      
REMARK 465     GLU B   730                                                      
REMARK 465     VAL B   731                                                      
REMARK 465     ASP B   732                                                      
REMARK 465     HIS B   733                                                      
REMARK 465     HIS B   734                                                      
REMARK 465     HIS B   735                                                      
REMARK 465     HIS B   736                                                      
REMARK 465     HIS B   737                                                      
REMARK 465     HIS B   738                                                      
REMARK 465     ALA C   291                                                      
REMARK 465     ALA C   292                                                      
REMARK 465     THR C   293                                                      
REMARK 465     ASP C   350                                                      
REMARK 465     LEU C   351                                                      
REMARK 465     PHE C   352                                                      
REMARK 465     GLU C   353                                                      
REMARK 465     ASN C   354                                                      
REMARK 465     ARG C   355                                                      
REMARK 465     LYS C   356                                                      
REMARK 465     LYS C   357                                                      
REMARK 465     LYS C   358                                                      
REMARK 465     ASN C   359                                                      
REMARK 465     LEU C   396                                                      
REMARK 465     ASN C   397                                                      
REMARK 465     ILE C   398                                                      
REMARK 465     SER C   399                                                      
REMARK 465     ARG C   400                                                      
REMARK 465     GLU C   401                                                      
REMARK 465     MET C   402                                                      
REMARK 465     LEU C   403                                                      
REMARK 465     GLN C   404                                                      
REMARK 465     GLN C   405                                                      
REMARK 465     LYS C   615                                                      
REMARK 465     ALA C   616                                                      
REMARK 465     GLN C   617                                                      
REMARK 465     ALA C   618                                                      
REMARK 465     LEU C   619                                                      
REMARK 465     ARG C   620                                                      
REMARK 465     ASP C   621                                                      
REMARK 465     ASN C   622                                                      
REMARK 465     SER C   623                                                      
REMARK 465     THR C   624                                                      
REMARK 465     MET C   625                                                      
REMARK 465     GLY C   626                                                      
REMARK 465     TYR C   627                                                      
REMARK 465     MET C   628                                                      
REMARK 465     ALA C   629                                                      
REMARK 465     ILE C   698                                                      
REMARK 465     ASP C   699                                                      
REMARK 465     GLU C   700                                                      
REMARK 465     ASP C   701                                                      
REMARK 465     ASP C   702                                                      
REMARK 465     PRO C   703                                                      
REMARK 465     THR C   704                                                      
REMARK 465     ALA C   705                                                      
REMARK 465     ASP C   706                                                      
REMARK 465     ASP C   707                                                      
REMARK 465     THR C   708                                                      
REMARK 465     SER C   709                                                      
REMARK 465     ALA C   710                                                      
REMARK 465     ALA C   711                                                      
REMARK 465     VAL C   712                                                      
REMARK 465     THR C   713                                                      
REMARK 465     GLU C   714                                                      
REMARK 465     GLU C   715                                                      
REMARK 465     MET C   716                                                      
REMARK 465     PRO C   717                                                      
REMARK 465     PRO C   718                                                      
REMARK 465     LEU C   719                                                      
REMARK 465     GLU C   720                                                      
REMARK 465     GLY C   721                                                      
REMARK 465     ASP C   722                                                      
REMARK 465     ASP C   723                                                      
REMARK 465     ASP C   724                                                      
REMARK 465     THR C   725                                                      
REMARK 465     SER C   726                                                      
REMARK 465     ARG C   727                                                      
REMARK 465     MET C   728                                                      
REMARK 465     GLU C   729                                                      
REMARK 465     GLU C   730                                                      
REMARK 465     VAL C   731                                                      
REMARK 465     ASP C   732                                                      
REMARK 465     HIS C   733                                                      
REMARK 465     HIS C   734                                                      
REMARK 465     HIS C   735                                                      
REMARK 465     HIS C   736                                                      
REMARK 465     HIS C   737                                                      
REMARK 465     HIS C   738                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU B 646   CA  -  CB  -  CG  ANGL. DEV. =  17.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 376       43.34     70.71                                   
REMARK 500    LEU A 394      112.15   -161.28                                   
REMARK 500    SER A 406     -161.39   -174.35                                   
REMARK 500    GLU A 429     -148.55    -68.61                                   
REMARK 500    ASP A 430       72.42     22.12                                   
REMARK 500    LYS A 485     -162.12    -71.04                                   
REMARK 500    ASN A 487       12.64     81.73                                   
REMARK 500    GLU A 555      -39.99    -32.72                                   
REMARK 500    GLU A 580      -97.20      5.79                                   
REMARK 500    VAL A 593      -57.16   -127.66                                   
REMARK 500    THR A 607     -165.88    -72.02                                   
REMARK 500    LEU A 694      -73.85    -58.76                                   
REMARK 500    LEU A 696      -21.63   -173.28                                   
REMARK 500    ASN B 318       22.23     48.58                                   
REMARK 500    ASN B 360       54.02   -153.08                                   
REMARK 500    ASP B 372        4.56   -153.51                                   
REMARK 500    CYS B 374       84.36    -64.18                                   
REMARK 500    GLU B 376      -20.73   -178.73                                   
REMARK 500    GLU B 392       39.97    -83.96                                   
REMARK 500    ASP B 393      108.34    105.34                                   
REMARK 500    SER B 406       97.35     54.82                                   
REMARK 500    LYS B 407       -9.31   -160.94                                   
REMARK 500    ASP B 452       66.56   -111.36                                   
REMARK 500    SER B 468       -9.31    -58.78                                   
REMARK 500    ASP B 472       35.34    -96.58                                   
REMARK 500    LYS B 485     -153.54    -78.62                                   
REMARK 500    GLU B 486      -66.27    -92.12                                   
REMARK 500    LEU B 579        1.52    -60.72                                   
REMARK 500    GLU B 580     -126.98     37.02                                   
REMARK 500    LYS B 581       43.89    -95.88                                   
REMARK 500    GLN C 334      -76.50    -13.02                                   
REMARK 500    PRO C 348     -151.23    -75.91                                   
REMARK 500    ASN C 373      -47.03    -29.17                                   
REMARK 500    CYS C 374       98.31     -4.95                                   
REMARK 500    GLU C 432       19.45    -45.16                                   
REMARK 500    ASN C 433        1.46   -172.91                                   
REMARK 500    LYS C 565        1.10    -63.30                                   
REMARK 500    LEU C 579       26.47   -143.46                                   
REMARK 500    LYS C 581      -33.10     96.30                                   
REMARK 500    LYS C 585      135.02     88.98                                   
REMARK 500    SER C 602     -149.17     48.28                                   
REMARK 500    THR C 603      -46.36   -130.56                                   
REMARK 500    LYS C 631       79.74   -102.81                                   
REMARK 500    ARG C 647      -86.48    -66.61                                   
REMARK 500    ASP C 653       91.49     52.90                                   
REMARK 500    ASN C 655     -144.70   -130.55                                   
REMARK 500    ASP C 656      137.23     66.77                                   
REMARK 500    LEU C 696       -8.81   -153.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN B 433        22.2      L          L   OUTSIDE RANGE           
REMARK 500    GLU B 486        21.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A  25        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH A  39        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH A  41        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH A  44        DISTANCE =  8.73 ANGSTROMS                       
REMARK 525    HOH A  80        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH A  99        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH A 125        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH A 127        DISTANCE =  7.81 ANGSTROMS                       
REMARK 525    HOH B   6        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH B  28        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH B  43        DISTANCE =  7.56 ANGSTROMS                       
REMARK 525    HOH B  66        DISTANCE = 10.19 ANGSTROMS                       
REMARK 525    HOH B  67        DISTANCE =  7.36 ANGSTROMS                       
REMARK 525    HOH B  75        DISTANCE = 10.17 ANGSTROMS                       
REMARK 525    HOH B  76        DISTANCE =  7.73 ANGSTROMS                       
REMARK 525    HOH B  84        DISTANCE =  5.61 ANGSTROMS                       
REMARK 525    HOH B 133        DISTANCE =  7.09 ANGSTROMS                       
REMARK 525    HOH C  22        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH C  48        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH C  78        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH C  79        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH C  90        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH C 131        DISTANCE =  7.15 ANGSTROMS                       
REMARK 525    HOH C 132        DISTANCE =  7.21 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 3                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3Q6N   RELATED DB: PDB                                   
DBREF  3Q6M A  293   732  UNP    P07900   HS90A_HUMAN    293    732             
DBREF  3Q6M B  293   732  UNP    P07900   HS90A_HUMAN    293    732             
DBREF  3Q6M C  293   732  UNP    P07900   HS90A_HUMAN    293    732             
SEQADV 3Q6M ALA A  291  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M ALA A  292  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS A  733  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS A  734  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS A  735  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS A  736  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS A  737  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS A  738  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M ALA B  291  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M ALA B  292  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS B  733  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS B  734  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS B  735  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS B  736  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS B  737  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS B  738  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M ALA C  291  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M ALA C  292  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS C  733  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS C  734  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS C  735  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS C  736  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS C  737  UNP  P07900              EXPRESSION TAG                 
SEQADV 3Q6M HIS C  738  UNP  P07900              EXPRESSION TAG                 
SEQRES   1 A  448  ALA ALA THR LYS PRO ILE TRP THR ARG ASN PRO ASP ASP          
SEQRES   2 A  448  ILE THR ASN GLU GLU TYR GLY GLU PHE TYR LYS SER LEU          
SEQRES   3 A  448  THR ASN ASP TRP GLU ASP HIS LEU ALA VAL LYS HIS PHE          
SEQRES   4 A  448  SER VAL GLU GLY GLN LEU GLU PHE ARG ALA LEU LEU PHE          
SEQRES   5 A  448  VAL PRO ARG ARG ALA PRO PHE ASP LEU PHE GLU ASN ARG          
SEQRES   6 A  448  LYS LYS LYS ASN ASN ILE LYS LEU TYR VAL ARG ARG VAL          
SEQRES   7 A  448  PHE ILE MET ASP ASN CYS GLU GLU LEU ILE PRO GLU TYR          
SEQRES   8 A  448  LEU ASN PHE ILE ARG GLY VAL VAL ASP SER GLU ASP LEU          
SEQRES   9 A  448  PRO LEU ASN ILE SER ARG GLU MET LEU GLN GLN SER LYS          
SEQRES  10 A  448  ILE LEU LYS VAL ILE ARG LYS ASN LEU VAL LYS LYS CYS          
SEQRES  11 A  448  LEU GLU LEU PHE THR GLU LEU ALA GLU ASP LYS GLU ASN          
SEQRES  12 A  448  TYR LYS LYS PHE TYR GLU GLN PHE SER LYS ASN ILE LYS          
SEQRES  13 A  448  LEU GLY ILE HIS GLU ASP SER GLN ASN ARG LYS LYS LEU          
SEQRES  14 A  448  SER GLU LEU LEU ARG TYR TYR THR SER ALA SER GLY ASP          
SEQRES  15 A  448  GLU MET VAL SER LEU LYS ASP TYR CYS THR ARG MET LYS          
SEQRES  16 A  448  GLU ASN GLN LYS HIS ILE TYR TYR ILE THR GLY GLU THR          
SEQRES  17 A  448  LYS ASP GLN VAL ALA ASN SER ALA PHE VAL GLU ARG LEU          
SEQRES  18 A  448  ARG LYS HIS GLY LEU GLU VAL ILE TYR MET ILE GLU PRO          
SEQRES  19 A  448  ILE ASP GLU TYR CYS VAL GLN GLN LEU LYS GLU PHE GLU          
SEQRES  20 A  448  GLY LYS THR LEU VAL SER VAL THR LYS GLU GLY LEU GLU          
SEQRES  21 A  448  LEU PRO GLU ASP GLU GLU GLU LYS LYS LYS GLN GLU GLU          
SEQRES  22 A  448  LYS LYS THR LYS PHE GLU ASN LEU CYS LYS ILE MET LYS          
SEQRES  23 A  448  ASP ILE LEU GLU LYS LYS VAL GLU LYS VAL VAL VAL SER          
SEQRES  24 A  448  ASN ARG LEU VAL THR SER PRO CYS CYS ILE VAL THR SER          
SEQRES  25 A  448  THR TYR GLY TRP THR ALA ASN MET GLU ARG ILE MET LYS          
SEQRES  26 A  448  ALA GLN ALA LEU ARG ASP ASN SER THR MET GLY TYR MET          
SEQRES  27 A  448  ALA ALA LYS LYS HIS LEU GLU ILE ASN PRO ASP HIS SER          
SEQRES  28 A  448  ILE ILE GLU THR LEU ARG GLN LYS ALA GLU ALA ASP LYS          
SEQRES  29 A  448  ASN ASP LYS SER VAL LYS ASP LEU VAL ILE LEU LEU TYR          
SEQRES  30 A  448  GLU THR ALA LEU LEU SER SER GLY PHE SER LEU GLU ASP          
SEQRES  31 A  448  PRO GLN THR HIS ALA ASN ARG ILE TYR ARG MET ILE LYS          
SEQRES  32 A  448  LEU GLY LEU GLY ILE ASP GLU ASP ASP PRO THR ALA ASP          
SEQRES  33 A  448  ASP THR SER ALA ALA VAL THR GLU GLU MET PRO PRO LEU          
SEQRES  34 A  448  GLU GLY ASP ASP ASP THR SER ARG MET GLU GLU VAL ASP          
SEQRES  35 A  448  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 B  448  ALA ALA THR LYS PRO ILE TRP THR ARG ASN PRO ASP ASP          
SEQRES   2 B  448  ILE THR ASN GLU GLU TYR GLY GLU PHE TYR LYS SER LEU          
SEQRES   3 B  448  THR ASN ASP TRP GLU ASP HIS LEU ALA VAL LYS HIS PHE          
SEQRES   4 B  448  SER VAL GLU GLY GLN LEU GLU PHE ARG ALA LEU LEU PHE          
SEQRES   5 B  448  VAL PRO ARG ARG ALA PRO PHE ASP LEU PHE GLU ASN ARG          
SEQRES   6 B  448  LYS LYS LYS ASN ASN ILE LYS LEU TYR VAL ARG ARG VAL          
SEQRES   7 B  448  PHE ILE MET ASP ASN CYS GLU GLU LEU ILE PRO GLU TYR          
SEQRES   8 B  448  LEU ASN PHE ILE ARG GLY VAL VAL ASP SER GLU ASP LEU          
SEQRES   9 B  448  PRO LEU ASN ILE SER ARG GLU MET LEU GLN GLN SER LYS          
SEQRES  10 B  448  ILE LEU LYS VAL ILE ARG LYS ASN LEU VAL LYS LYS CYS          
SEQRES  11 B  448  LEU GLU LEU PHE THR GLU LEU ALA GLU ASP LYS GLU ASN          
SEQRES  12 B  448  TYR LYS LYS PHE TYR GLU GLN PHE SER LYS ASN ILE LYS          
SEQRES  13 B  448  LEU GLY ILE HIS GLU ASP SER GLN ASN ARG LYS LYS LEU          
SEQRES  14 B  448  SER GLU LEU LEU ARG TYR TYR THR SER ALA SER GLY ASP          
SEQRES  15 B  448  GLU MET VAL SER LEU LYS ASP TYR CYS THR ARG MET LYS          
SEQRES  16 B  448  GLU ASN GLN LYS HIS ILE TYR TYR ILE THR GLY GLU THR          
SEQRES  17 B  448  LYS ASP GLN VAL ALA ASN SER ALA PHE VAL GLU ARG LEU          
SEQRES  18 B  448  ARG LYS HIS GLY LEU GLU VAL ILE TYR MET ILE GLU PRO          
SEQRES  19 B  448  ILE ASP GLU TYR CYS VAL GLN GLN LEU LYS GLU PHE GLU          
SEQRES  20 B  448  GLY LYS THR LEU VAL SER VAL THR LYS GLU GLY LEU GLU          
SEQRES  21 B  448  LEU PRO GLU ASP GLU GLU GLU LYS LYS LYS GLN GLU GLU          
SEQRES  22 B  448  LYS LYS THR LYS PHE GLU ASN LEU CYS LYS ILE MET LYS          
SEQRES  23 B  448  ASP ILE LEU GLU LYS LYS VAL GLU LYS VAL VAL VAL SER          
SEQRES  24 B  448  ASN ARG LEU VAL THR SER PRO CYS CYS ILE VAL THR SER          
SEQRES  25 B  448  THR TYR GLY TRP THR ALA ASN MET GLU ARG ILE MET LYS          
SEQRES  26 B  448  ALA GLN ALA LEU ARG ASP ASN SER THR MET GLY TYR MET          
SEQRES  27 B  448  ALA ALA LYS LYS HIS LEU GLU ILE ASN PRO ASP HIS SER          
SEQRES  28 B  448  ILE ILE GLU THR LEU ARG GLN LYS ALA GLU ALA ASP LYS          
SEQRES  29 B  448  ASN ASP LYS SER VAL LYS ASP LEU VAL ILE LEU LEU TYR          
SEQRES  30 B  448  GLU THR ALA LEU LEU SER SER GLY PHE SER LEU GLU ASP          
SEQRES  31 B  448  PRO GLN THR HIS ALA ASN ARG ILE TYR ARG MET ILE LYS          
SEQRES  32 B  448  LEU GLY LEU GLY ILE ASP GLU ASP ASP PRO THR ALA ASP          
SEQRES  33 B  448  ASP THR SER ALA ALA VAL THR GLU GLU MET PRO PRO LEU          
SEQRES  34 B  448  GLU GLY ASP ASP ASP THR SER ARG MET GLU GLU VAL ASP          
SEQRES  35 B  448  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 C  448  ALA ALA THR LYS PRO ILE TRP THR ARG ASN PRO ASP ASP          
SEQRES   2 C  448  ILE THR ASN GLU GLU TYR GLY GLU PHE TYR LYS SER LEU          
SEQRES   3 C  448  THR ASN ASP TRP GLU ASP HIS LEU ALA VAL LYS HIS PHE          
SEQRES   4 C  448  SER VAL GLU GLY GLN LEU GLU PHE ARG ALA LEU LEU PHE          
SEQRES   5 C  448  VAL PRO ARG ARG ALA PRO PHE ASP LEU PHE GLU ASN ARG          
SEQRES   6 C  448  LYS LYS LYS ASN ASN ILE LYS LEU TYR VAL ARG ARG VAL          
SEQRES   7 C  448  PHE ILE MET ASP ASN CYS GLU GLU LEU ILE PRO GLU TYR          
SEQRES   8 C  448  LEU ASN PHE ILE ARG GLY VAL VAL ASP SER GLU ASP LEU          
SEQRES   9 C  448  PRO LEU ASN ILE SER ARG GLU MET LEU GLN GLN SER LYS          
SEQRES  10 C  448  ILE LEU LYS VAL ILE ARG LYS ASN LEU VAL LYS LYS CYS          
SEQRES  11 C  448  LEU GLU LEU PHE THR GLU LEU ALA GLU ASP LYS GLU ASN          
SEQRES  12 C  448  TYR LYS LYS PHE TYR GLU GLN PHE SER LYS ASN ILE LYS          
SEQRES  13 C  448  LEU GLY ILE HIS GLU ASP SER GLN ASN ARG LYS LYS LEU          
SEQRES  14 C  448  SER GLU LEU LEU ARG TYR TYR THR SER ALA SER GLY ASP          
SEQRES  15 C  448  GLU MET VAL SER LEU LYS ASP TYR CYS THR ARG MET LYS          
SEQRES  16 C  448  GLU ASN GLN LYS HIS ILE TYR TYR ILE THR GLY GLU THR          
SEQRES  17 C  448  LYS ASP GLN VAL ALA ASN SER ALA PHE VAL GLU ARG LEU          
SEQRES  18 C  448  ARG LYS HIS GLY LEU GLU VAL ILE TYR MET ILE GLU PRO          
SEQRES  19 C  448  ILE ASP GLU TYR CYS VAL GLN GLN LEU LYS GLU PHE GLU          
SEQRES  20 C  448  GLY LYS THR LEU VAL SER VAL THR LYS GLU GLY LEU GLU          
SEQRES  21 C  448  LEU PRO GLU ASP GLU GLU GLU LYS LYS LYS GLN GLU GLU          
SEQRES  22 C  448  LYS LYS THR LYS PHE GLU ASN LEU CYS LYS ILE MET LYS          
SEQRES  23 C  448  ASP ILE LEU GLU LYS LYS VAL GLU LYS VAL VAL VAL SER          
SEQRES  24 C  448  ASN ARG LEU VAL THR SER PRO CYS CYS ILE VAL THR SER          
SEQRES  25 C  448  THR TYR GLY TRP THR ALA ASN MET GLU ARG ILE MET LYS          
SEQRES  26 C  448  ALA GLN ALA LEU ARG ASP ASN SER THR MET GLY TYR MET          
SEQRES  27 C  448  ALA ALA LYS LYS HIS LEU GLU ILE ASN PRO ASP HIS SER          
SEQRES  28 C  448  ILE ILE GLU THR LEU ARG GLN LYS ALA GLU ALA ASP LYS          
SEQRES  29 C  448  ASN ASP LYS SER VAL LYS ASP LEU VAL ILE LEU LEU TYR          
SEQRES  30 C  448  GLU THR ALA LEU LEU SER SER GLY PHE SER LEU GLU ASP          
SEQRES  31 C  448  PRO GLN THR HIS ALA ASN ARG ILE TYR ARG MET ILE LYS          
SEQRES  32 C  448  LEU GLY LEU GLY ILE ASP GLU ASP ASP PRO THR ALA ASP          
SEQRES  33 C  448  ASP THR SER ALA ALA VAL THR GLU GLU MET PRO PRO LEU          
SEQRES  34 C  448  GLU GLY ASP ASP ASP THR SER ARG MET GLU GLU VAL ASP          
SEQRES  35 C  448  HIS HIS HIS HIS HIS HIS                                      
HET    SO4  A   1       5                                                       
HET    SO4  B   2       5                                                       
HET    SO4  C   3       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   4  SO4    3(O4 S 2-)                                                   
FORMUL   7  HOH   *133(H2 O)                                                    
HELIX    1   1 PRO A  295  ARG A  299  5                                   5    
HELIX    2   2 THR A  305  ASN A  318  1                                  14    
HELIX    3   3 PRO A  379  ASN A  383  5                                   5    
HELIX    4   4 LYS A  407  ALA A  428  1                                  22    
HELIX    5   5 ASP A  430  ASP A  452  1                                  23    
HELIX    6   6 ASN A  455  GLU A  461  1                                   7    
HELIX    7   7 LEU A  477  ARG A  483  1                                   7    
HELIX    8   8 THR A  498  ASN A  504  1                                   7    
HELIX    9   9 SER A  505  PHE A  507  5                                   3    
HELIX   10  10 VAL A  508  GLY A  515  1                                   8    
HELIX   11  11 PRO A  524  VAL A  530  1                                   7    
HELIX   12  12 ASP A  554  PHE A  568  1                                  15    
HELIX   13  13 PHE A  568  LEU A  579  1                                  12    
HELIX   14  14 GLU A  580  VAL A  583  5                                   4    
HELIX   15  15 THR A  607  MET A  614  1                                   8    
HELIX   16  16 HIS A  640  ASP A  653  1                                  14    
HELIX   17  17 ASP A  656  SER A  674  1                                  19    
HELIX   18  18 ASP A  680  GLY A  695  1                                  16    
HELIX   19  19 PRO B  295  ARG B  299  5                                   5    
HELIX   20  20 THR B  305  ASN B  318  1                                  14    
HELIX   21  21 PRO B  379  ASN B  383  5                                   5    
HELIX   22  22 LYS B  407  ASP B  430  1                                  24    
HELIX   23  23 TYR B  434  ASP B  452  1                                  19    
HELIX   24  24 ASN B  455  GLU B  461  1                                   7    
HELIX   25  25 SER B  476  MET B  484  1                                   9    
HELIX   26  26 THR B  498  ASN B  504  1                                   7    
HELIX   27  27 SER B  505  PHE B  507  5                                   3    
HELIX   28  28 VAL B  508  GLY B  515  1                                   8    
HELIX   29  29 GLU B  523  GLN B  531  1                                   9    
HELIX   30  30 GLU B  556  PHE B  568  1                                  13    
HELIX   31  31 PHE B  568  LEU B  579  1                                  12    
HELIX   32  32 GLU B  580  VAL B  583  5                                   4    
HELIX   33  33 THR B  607  MET B  614  1                                   8    
HELIX   34  34 HIS B  640  ASP B  653  1                                  14    
HELIX   35  35 ASP B  656  SER B  674  1                                  19    
HELIX   36  36 ASP B  680  LEU B  696  1                                  17    
HELIX   37  37 PRO C  295  ARG C  299  5                                   5    
HELIX   38  38 THR C  305  ASN C  318  1                                  14    
HELIX   39  39 PRO C  379  ASN C  383  5                                   5    
HELIX   40  40 ILE C  408  ASP C  430  1                                  23    
HELIX   41  41 ASN C  433  ASP C  452  1                                  20    
HELIX   42  42 ASN C  455  GLU C  461  1                                   7    
HELIX   43  43 ALA C  469  GLY C  471  5                                   3    
HELIX   44  44 LEU C  477  ARG C  483  1                                   7    
HELIX   45  45 THR C  498  ASN C  504  1                                   7    
HELIX   46  46 SER C  505  PHE C  507  5                                   3    
HELIX   47  47 VAL C  508  HIS C  514  1                                   7    
HELIX   48  48 GLU C  523  VAL C  530  1                                   8    
HELIX   49  49 ASP C  554  PHE C  568  1                                  15    
HELIX   50  50 PHE C  568  ILE C  578  1                                  11    
HELIX   51  51 HIS C  640  ALA C  652  1                                  13    
HELIX   52  52 ASN C  655  SER C  674  1                                  20    
HELIX   53  53 ASP C  680  LEU C  694  1                                  15    
SHEET    1   A 5 ALA A 325  VAL A 331  0                                        
SHEET    2   A 5 PHE A 337  VAL A 343 -1  O  LEU A 341   N  LYS A 327           
SHEET    3   A 5 ARG A 386  SER A 391 -1  O  ARG A 386   N  PHE A 342           
SHEET    4   A 5 ILE A 361  VAL A 365  1  N  TYR A 364   O  VAL A 389           
SHEET    5   A 5 VAL A 368  MET A 371 -1  O  MET A 371   N  LEU A 363           
SHEET    1   B 6 VAL A 475  SER A 476  0                                        
SHEET    2   B 6 ARG A 464  THR A 467 -1  N  TYR A 465   O  VAL A 475           
SHEET    3   B 6 VAL A 518  MET A 521 -1  O  TYR A 520   N  TYR A 466           
SHEET    4   B 6 HIS A 490  THR A 495  1  N  ILE A 494   O  MET A 521           
SHEET    5   B 6 LYS A 539  SER A 543  1  O  VAL A 542   N  ILE A 491           
SHEET    6   B 6 GLU A 535  PHE A 536 -1  N  PHE A 536   O  LYS A 539           
SHEET    1   C 3 LYS A 585  VAL A 588  0                                        
SHEET    2   C 3 LYS A 632  ILE A 636  1  O  ILE A 636   N  VAL A 587           
SHEET    3   C 3 CYS A 597  THR A 601 -1  N  VAL A 600   O  HIS A 633           
SHEET    1   D 5 ALA B 325  VAL B 331  0                                        
SHEET    2   D 5 PHE B 337  VAL B 343 -1  O  LEU B 341   N  LYS B 327           
SHEET    3   D 5 ARG B 386  SER B 391 -1  O  ARG B 386   N  PHE B 342           
SHEET    4   D 5 ILE B 361  VAL B 365  1  N  TYR B 364   O  VAL B 389           
SHEET    5   D 5 VAL B 368  MET B 371 -1  O  MET B 371   N  LEU B 363           
SHEET    1   E 5 TYR B 466  THR B 467  0                                        
SHEET    2   E 5 VAL B 518  MET B 521 -1  O  TYR B 520   N  TYR B 466           
SHEET    3   E 5 HIS B 490  THR B 495  1  N  ILE B 494   O  MET B 521           
SHEET    4   E 5 LYS B 539  SER B 543  1  O  VAL B 542   N  ILE B 491           
SHEET    5   E 5 GLU B 535  PHE B 536 -1  N  PHE B 536   O  LYS B 539           
SHEET    1   F 3 LYS B 585  VAL B 588  0                                        
SHEET    2   F 3 LYS B 632  ILE B 636  1  O  ILE B 636   N  VAL B 587           
SHEET    3   F 3 CYS B 597  THR B 601 -1  N  VAL B 600   O  HIS B 633           
SHEET    1   G 5 ALA C 325  VAL C 331  0                                        
SHEET    2   G 5 PHE C 337  VAL C 343 -1  O  LEU C 341   N  LYS C 327           
SHEET    3   G 5 ARG C 386  SER C 391 -1  O  ASP C 390   N  ARG C 338           
SHEET    4   G 5 ILE C 361  VAL C 365  1  N  TYR C 364   O  VAL C 389           
SHEET    5   G 5 VAL C 368  MET C 371 -1  O  MET C 371   N  LEU C 363           
SHEET    1   H 6 VAL C 475  SER C 476  0                                        
SHEET    2   H 6 ARG C 464  THR C 467 -1  N  TYR C 465   O  VAL C 475           
SHEET    3   H 6 VAL C 518  MET C 521 -1  O  TYR C 520   N  TYR C 466           
SHEET    4   H 6 HIS C 490  THR C 495  1  N  ILE C 494   O  ILE C 519           
SHEET    5   H 6 LYS C 539  SER C 543  1  O  THR C 540   N  ILE C 491           
SHEET    6   H 6 GLU C 535  PHE C 536 -1  N  PHE C 536   O  LYS C 539           
SHEET    1   I 3 VAL C 586  VAL C 588  0                                        
SHEET    2   I 3 HIS C 633  ILE C 636  1  O  LEU C 634   N  VAL C 587           
SHEET    3   I 3 CYS C 597  VAL C 600 -1  N  VAL C 600   O  HIS C 633           
SITE     1 AC1  3 ARG A 510  LYS A 513  HIS A 514                               
SITE     1 AC2  3 ARG B 510  LYS B 513  HIS B 514                               
SITE     1 AC3  2 ARG C 510  HIS C 514                                          
CRYST1  162.702  304.553   87.624  90.00  90.00  90.00 C 2 2 21     24          
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      0.006146  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003284  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011412        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system