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Database: PDB
Entry: 3RG6
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HEADER    PHOTOSYNTHESIS                          07-APR-11   3RG6              
TITLE     CRYSTAL STRUCTURE OF A CHAPERONE-BOUND ASSEMBLY INTERMEDIATE OF FORM I
TITLE    2 RUBISCO                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: RUBISCO LARGE SUBUNIT;                                      
COMPND   5 EC: 4.1.1.39;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RBCX PROTEIN;                                              
COMPND   9 CHAIN: C, D, E, F;                                                   
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;                        
SOURCE   3 ORGANISM_TAXID: 269084;                                              
SOURCE   4 STRAIN: ATCC 27144 / PCC 6301 / SAUG 1402/1;                         
SOURCE   5 GENE: CBBL, RBCA, RBCL, SYC0130_C;                                   
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: PET11A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: ANABAENA SP.;                                   
SOURCE  13 ORGANISM_TAXID: 1167;                                                
SOURCE  14 GENE: RBCX;                                                          
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    PHOTOSYNTHESIS, ASSEMBLY CHAPERONE, TIM BARREL (RBCL), CARBON         
KEYWDS   2 FIXATION (RBCL) COMPLEX ASSEMBLY, PROTEIN FOLDING, CHAPERONE (RBCX), 
KEYWDS   3 RBCS (RBCL)                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.BRACHER,A.STARLING-WINDHOF,F.U.HARTL,M.HAYER-HARTL                  
REVDAT   4   16-JUL-14 3RG6    1       REMARK                                   
REVDAT   3   17-AUG-11 3RG6    1       JRNL                                     
REVDAT   2   03-AUG-11 3RG6    1       JRNL                                     
REVDAT   1   20-JUL-11 3RG6    0                                                
JRNL        AUTH   A.BRACHER,A.STARLING-WINDHOF,F.U.HARTL,M.HAYER-HARTL         
JRNL        TITL   CRYSTAL STRUCTURE OF A CHAPERONE-BOUND ASSEMBLY INTERMEDIATE 
JRNL        TITL 2 OF FORM I RUBISCO.                                           
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  18   875 2011              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   21765418                                                     
JRNL        DOI    10.1038/NSMB.2090                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.LIU,A.L.YOUNG,A.STARLING-WINDHOF,A.BRACHER,                
REMARK   1  AUTH 2 S.SASCHENBRECKER,B.V.RAO,K.V.RAO,O.BERNINGHAUSEN,T.MIELKE,   
REMARK   1  AUTH 3 F.U.HARTL,R.BECKMANN,M.HAYER-HARTL                           
REMARK   1  TITL   COUPLED CHAPERONE ACTION IN FOLDING AND ASSEMBLY OF          
REMARK   1  TITL 2 HEXADECAMERIC RUBISCO.                                       
REMARK   1  REF    NATURE                        V. 463   197 2010              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   20075914                                                     
REMARK   1  DOI    10.1038/NATURE08651                                          
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   S.SASCHENBRECKER,A.BRACHER,K.V.RAO,B.V.RAO,F.U.HARTL,        
REMARK   1  AUTH 2 M.HAYER-HARTL                                                
REMARK   1  TITL   STRUCTURE AND FUNCTION OF RBCX, AN ASSEMBLY CHAPERONE FOR    
REMARK   1  TITL 2 HEXADECAMERIC RUBISCO.                                       
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V. 129  1189 2007              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1  PMID   17574029                                                     
REMARK   1  DOI    10.1016/J.CELL.2007.04.025                                   
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.NEWMAN,C.I.BRANDEN,T.A.JONES                               
REMARK   1  TITL   STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE           
REMARK   1  TITL 2 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE FROM SYNECHOCOCCUS    
REMARK   1  TITL 3 PCC6301.                                                     
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  49   548 1993              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   15299492                                                     
REMARK   1  DOI    10.1107/S090744499300530X                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 41214                          
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) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2067                            
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) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1439                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 42.74                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 71                           
REMARK   3   BIN FREE R VALUE                    : 0.3410                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10078                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 89.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.33000                                              
REMARK   3    B22 (A**2) : 3.33000                                              
REMARK   3    B33 (A**2) : -6.66000                                             
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): 0.429         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.320         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 42.556        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.913                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.876                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10302 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14002 ; 1.073 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1311 ; 5.178 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   462 ;34.153 ;23.658       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1591 ;20.117 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    68 ;17.329 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1573 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7910 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5007 ; 0.209 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  7049 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   326 ; 0.156 ; 0.200       
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):    31 ; 0.221 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.183 ; 0.200       
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):  6686 ; 0.174 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10411 ; 0.331 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4045 ; 0.546 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3591 ; 0.954 ; 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 : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 4                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     18       A      61      4                      
REMARK   3           1     B     18       B      61      4                      
REMARK   3           2     A     72       A     329      4                      
REMARK   3           2     B     72       B     329      4                      
REMARK   3           3     A    334       A     401      4                      
REMARK   3           3     B    334       B     401      4                      
REMARK   3           4     A    405       A     469      4                      
REMARK   3           4     B    405       B     469      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3333 ; 0.230 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3333 ; 0.200 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : C E                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      2       C     115      4                      
REMARK   3           1     E      2       E     115      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    C    (A):    851 ; 0.310 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    C (A**2):    851 ; 0.080 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : D E                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D      1       D     105      4                      
REMARK   3           1     E      1       E     105      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    D    (A):    767 ; 0.450 ; 0.500           
REMARK   3   MEDIUM THERMAL     3    D (A**2):    767 ; 0.140 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    18        A    63                          
REMARK   3    RESIDUE RANGE :   A    71        A   401                          
REMARK   3    RESIDUE RANGE :   A   405        A   458                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.6360  15.8845  12.9478              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3890 T22:  -0.2752                                     
REMARK   3      T33:  -0.4432 T12:   0.1658                                     
REMARK   3      T13:   0.0135 T23:  -0.0976                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8660 L22:   1.0938                                     
REMARK   3      L33:   2.2522 L12:  -0.2968                                     
REMARK   3      L13:   0.3152 L23:  -0.4237                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0164 S12:  -0.0827 S13:   0.2249                       
REMARK   3      S21:   0.0744 S22:  -0.0844 S23:   0.2114                       
REMARK   3      S31:  -0.4846 S32:  -0.6422 S33:   0.1008                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    18        B    61                          
REMARK   3    RESIDUE RANGE :   B    71        B   331                          
REMARK   3    RESIDUE RANGE :   B   334        B   401                          
REMARK   3    RESIDUE RANGE :   B   405        B   458                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0778  27.4682 -12.9232              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3255 T22:  -0.4028                                     
REMARK   3      T33:  -0.4283 T12:   0.2425                                     
REMARK   3      T13:  -0.0975 T23:   0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0614 L22:   2.0594                                     
REMARK   3      L33:   2.3648 L12:  -0.3267                                     
REMARK   3      L13:  -0.6672 L23:   0.3694                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1050 S12:   0.0552 S13:   0.1233                       
REMARK   3      S21:  -0.0869 S22:   0.0661 S23:   0.2651                       
REMARK   3      S31:  -0.4312 S32:  -0.6930 S33:   0.0388                       
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 :   C     1        C   115                          
REMARK   3    ORIGIN FOR THE GROUP (A): -50.1541  53.0446 -31.7337              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8662 T22:   0.6381                                     
REMARK   3      T33:   0.6761 T12:   0.4944                                     
REMARK   3      T13:  -0.1853 T23:   0.2909                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2369 L22:   5.8512                                     
REMARK   3      L33:   5.8975 L12:  -0.6401                                     
REMARK   3      L13:  -0.4124 L23:   0.5489                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0572 S12:   0.2916 S13:   0.8923                       
REMARK   3      S21:  -0.8046 S22:   0.2318 S23:   0.0203                       
REMARK   3      S31:  -1.4238 S32:   0.2529 S33:  -0.1745                       
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 :   D     1        D   107                          
REMARK   3    ORIGIN FOR THE GROUP (A): -50.2352  41.7221 -25.9675              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3975 T22:   0.4701                                     
REMARK   3      T33:   0.0591 T12:   0.6281                                     
REMARK   3      T13:  -0.2072 T23:   0.0879                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2269 L22:   7.1088                                     
REMARK   3      L33:   4.9943 L12:  -1.0506                                     
REMARK   3      L13:   0.0774 L23:  -0.4010                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1730 S12:   0.3717 S13:   0.5485                       
REMARK   3      S21:  -0.1830 S22:   0.1110 S23:   0.0813                       
REMARK   3      S31:  -1.1126 S32:  -0.4685 S33:  -0.2840                       
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 :   E     2        E   115                          
REMARK   3    ORIGIN FOR THE GROUP (A): -62.8986  39.2355  31.7365              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7522 T22:   0.7163                                     
REMARK   3      T33:   0.7850 T12:   0.3223                                     
REMARK   3      T13:   0.3817 T23:  -0.0550                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2186 L22:   1.1958                                     
REMARK   3      L33:   5.7587 L12:  -0.0839                                     
REMARK   3      L13:   0.8382 L23:  -0.2804                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2753 S12:  -0.7037 S13:  -0.3035                       
REMARK   3      S21:   0.3306 S22:   0.1203 S23:   1.1047                       
REMARK   3      S31:   0.7854 S32:  -1.4320 S33:  -0.3956                       
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 :   F     1        F   106                          
REMARK   3    ORIGIN FOR THE GROUP (A): -51.4581  40.7804  25.8693              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4374 T22:   0.0046                                     
REMARK   3      T33:   0.1187 T12:   0.5801                                     
REMARK   3      T13:   0.1440 T23:  -0.1773                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0618 L22:   3.9222                                     
REMARK   3      L33:   4.6827 L12:   1.1716                                     
REMARK   3      L13:   0.2191 L23:   0.2565                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0451 S12:  -0.3198 S13:  -0.0075                       
REMARK   3      S21:   0.1914 S22:   0.0767 S23:   1.0180                       
REMARK   3      S31:  -0.0407 S32:  -0.7894 S33:  -0.1218                       
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   459        A   469                          
REMARK   3    ORIGIN FOR THE GROUP (A): -49.2786  37.9518  36.4137              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0122 T22:   0.0017                                     
REMARK   3      T33:   0.0246 T12:   0.0313                                     
REMARK   3      T13:  -0.0580 T23:  -0.0125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  78.9139 L22:  17.4776                                     
REMARK   3      L33:  20.9288 L12: -15.0324                                     
REMARK   3      L13: -16.4215 L23:   3.1017                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5681 S12:   3.3852 S13:  -3.0380                       
REMARK   3      S21:   0.8414 S22:  -0.6307 S23:   1.7318                       
REMARK   3      S31:   0.4818 S32:  -0.5664 S33:   0.0626                       
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   459        B   469                          
REMARK   3    ORIGIN FOR THE GROUP (A): -46.6758  39.8841 -36.3528              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0078 T22:   0.0039                                     
REMARK   3      T33:   0.0048 T12:   0.0013                                     
REMARK   3      T13:  -0.0088 T23:   0.0089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.2703 L22:  73.8894                                     
REMARK   3      L33:  39.8265 L12: -26.9248                                     
REMARK   3      L13:  17.3178 L23: -33.6510                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -2.5300 S12:  -1.4737 S13:   1.2146                       
REMARK   3      S21:   2.2811 S22:   3.7128 S23:  -2.0892                       
REMARK   3      S31:  -2.5468 S32:  -0.9235 S33:  -1.1828                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3RG6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064890.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-SEP-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97908                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41265                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.999                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.8                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.10900                            
REMARK 200  R SYM                      (I) : 0.10900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 48.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.31100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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 1RBL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-17 % 2-METHYL-2,4-PENTANEDIOL, 0.1    
REMARK 280  M KCL, 0.1 M TRIS-HCL, PH 8.7, VAPOR DIFFUSION, TEMPERATURE 277K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,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        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  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      122.37500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      122.37500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       49.83450            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000      122.37500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      122.37500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       49.83450            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000      122.37500            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000      122.37500            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       49.83450            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000      122.37500            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000      122.37500            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       49.83450            
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 300 REMARK: AUTHORS STATE THAT THIS COMPLEX COMPOSITION HAS BEEN         
REMARK 300 VERIFIED BY ELECTRON MICROSCOPY AND SIZE EXCLUSION CHROMATOGRAPHY    
REMARK 300 (SEE REFERENCE 1).                                                   
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: 24-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, B, E, F                      
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        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  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     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     TYR A    10                                                      
REMARK 465     LYS A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     LYS A    15                                                      
REMARK 465     ASP A    16                                                      
REMARK 465     TYR A    17                                                      
REMARK 465     THR A    64                                                      
REMARK 465     THR A    65                                                      
REMARK 465     VAL A    66                                                      
REMARK 465     TRP A    67                                                      
REMARK 465     THR A    68                                                      
REMARK 465     ASP A    69                                                      
REMARK 465     LEU A    70                                                      
REMARK 465     GLY A   402                                                      
REMARK 465     THR A   403                                                      
REMARK 465     LEU A   404                                                      
REMARK 465     ASP A   470                                                      
REMARK 465     LYS A   471                                                      
REMARK 465     LEU A   472                                                      
REMARK 465     MET C   -19                                                      
REMARK 465     GLY C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     PRO C   116                                                      
REMARK 465     SER C   117                                                      
REMARK 465     PRO C   118                                                      
REMARK 465     GLU C   119                                                      
REMARK 465     SER C   120                                                      
REMARK 465     GLU C   121                                                      
REMARK 465     GLN C   122                                                      
REMARK 465     GLN C   123                                                      
REMARK 465     GLN C   124                                                      
REMARK 465     PHE C   125                                                      
REMARK 465     SER C   126                                                      
REMARK 465     ASP C   127                                                      
REMARK 465     PRO C   128                                                      
REMARK 465     ASP C   129                                                      
REMARK 465     TRP C   130                                                      
REMARK 465     ASP C   131                                                      
REMARK 465     ASN C   132                                                      
REMARK 465     LEU C   133                                                      
REMARK 465     ALA C   134                                                      
REMARK 465     SER C   135                                                      
REMARK 465     MET D   -19                                                      
REMARK 465     GLY D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D   108                                                      
REMARK 465     THR D   109                                                      
REMARK 465     GLN D   110                                                      
REMARK 465     VAL D   111                                                      
REMARK 465     SER D   112                                                      
REMARK 465     LEU D   113                                                      
REMARK 465     SER D   114                                                      
REMARK 465     HIS D   115                                                      
REMARK 465     PRO D   116                                                      
REMARK 465     SER D   117                                                      
REMARK 465     PRO D   118                                                      
REMARK 465     GLU D   119                                                      
REMARK 465     SER D   120                                                      
REMARK 465     GLU D   121                                                      
REMARK 465     GLN D   122                                                      
REMARK 465     GLN D   123                                                      
REMARK 465     GLN D   124                                                      
REMARK 465     PHE D   125                                                      
REMARK 465     SER D   126                                                      
REMARK 465     ASP D   127                                                      
REMARK 465     PRO D   128                                                      
REMARK 465     ASP D   129                                                      
REMARK 465     TRP D   130                                                      
REMARK 465     ASP D   131                                                      
REMARK 465     ASN D   132                                                      
REMARK 465     LEU D   133                                                      
REMARK 465     ALA D   134                                                      
REMARK 465     SER D   135                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     TYR B    10                                                      
REMARK 465     LYS B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     LYS B    15                                                      
REMARK 465     ASP B    16                                                      
REMARK 465     TYR B    17                                                      
REMARK 465     THR B    62                                                      
REMARK 465     TRP B    63                                                      
REMARK 465     THR B    64                                                      
REMARK 465     THR B    65                                                      
REMARK 465     VAL B    66                                                      
REMARK 465     TRP B    67                                                      
REMARK 465     THR B    68                                                      
REMARK 465     ASP B    69                                                      
REMARK 465     LEU B    70                                                      
REMARK 465     LEU B   332                                                      
REMARK 465     GLU B   333                                                      
REMARK 465     GLY B   402                                                      
REMARK 465     THR B   403                                                      
REMARK 465     LEU B   404                                                      
REMARK 465     ASP B   470                                                      
REMARK 465     LYS B   471                                                      
REMARK 465     LEU B   472                                                      
REMARK 465     MET E   -19                                                      
REMARK 465     GLY E   -18                                                      
REMARK 465     SER E   -17                                                      
REMARK 465     SER E   -16                                                      
REMARK 465     HIS E   -15                                                      
REMARK 465     HIS E   -14                                                      
REMARK 465     HIS E   -13                                                      
REMARK 465     HIS E   -12                                                      
REMARK 465     HIS E   -11                                                      
REMARK 465     HIS E   -10                                                      
REMARK 465     SER E    -9                                                      
REMARK 465     SER E    -8                                                      
REMARK 465     GLY E    -7                                                      
REMARK 465     LEU E    -6                                                      
REMARK 465     VAL E    -5                                                      
REMARK 465     PRO E    -4                                                      
REMARK 465     ARG E    -3                                                      
REMARK 465     GLY E    -2                                                      
REMARK 465     SER E    -1                                                      
REMARK 465     HIS E     0                                                      
REMARK 465     MET E     1                                                      
REMARK 465     PRO E   116                                                      
REMARK 465     SER E   117                                                      
REMARK 465     PRO E   118                                                      
REMARK 465     GLU E   119                                                      
REMARK 465     SER E   120                                                      
REMARK 465     GLU E   121                                                      
REMARK 465     GLN E   122                                                      
REMARK 465     GLN E   123                                                      
REMARK 465     GLN E   124                                                      
REMARK 465     PHE E   125                                                      
REMARK 465     SER E   126                                                      
REMARK 465     ASP E   127                                                      
REMARK 465     PRO E   128                                                      
REMARK 465     ASP E   129                                                      
REMARK 465     TRP E   130                                                      
REMARK 465     ASP E   131                                                      
REMARK 465     ASN E   132                                                      
REMARK 465     LEU E   133                                                      
REMARK 465     ALA E   134                                                      
REMARK 465     SER E   135                                                      
REMARK 465     MET F   -19                                                      
REMARK 465     GLY F   -18                                                      
REMARK 465     SER F   -17                                                      
REMARK 465     SER F   -16                                                      
REMARK 465     HIS F   -15                                                      
REMARK 465     HIS F   -14                                                      
REMARK 465     HIS F   -13                                                      
REMARK 465     HIS F   -12                                                      
REMARK 465     HIS F   -11                                                      
REMARK 465     HIS F   -10                                                      
REMARK 465     SER F    -9                                                      
REMARK 465     SER F    -8                                                      
REMARK 465     GLY F    -7                                                      
REMARK 465     LEU F    -6                                                      
REMARK 465     VAL F    -5                                                      
REMARK 465     PRO F    -4                                                      
REMARK 465     ARG F    -3                                                      
REMARK 465     GLY F    -2                                                      
REMARK 465     SER F    -1                                                      
REMARK 465     HIS F     0                                                      
REMARK 465     ARG F   107                                                      
REMARK 465     MET F   108                                                      
REMARK 465     THR F   109                                                      
REMARK 465     GLN F   110                                                      
REMARK 465     VAL F   111                                                      
REMARK 465     SER F   112                                                      
REMARK 465     LEU F   113                                                      
REMARK 465     SER F   114                                                      
REMARK 465     HIS F   115                                                      
REMARK 465     PRO F   116                                                      
REMARK 465     SER F   117                                                      
REMARK 465     PRO F   118                                                      
REMARK 465     GLU F   119                                                      
REMARK 465     SER F   120                                                      
REMARK 465     GLU F   121                                                      
REMARK 465     GLN F   122                                                      
REMARK 465     GLN F   123                                                      
REMARK 465     GLN F   124                                                      
REMARK 465     PHE F   125                                                      
REMARK 465     SER F   126                                                      
REMARK 465     ASP F   127                                                      
REMARK 465     PRO F   128                                                      
REMARK 465     ASP F   129                                                      
REMARK 465     TRP F   130                                                      
REMARK 465     ASP F   131                                                      
REMARK 465     ASN F   132                                                      
REMARK 465     LEU F   133                                                      
REMARK 465     ALA F   134                                                      
REMARK 465     SER F   135                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  18    CG   CD   CE   NZ                                   
REMARK 470     THR A  62    OG1  CG2                                            
REMARK 470     LEU A  71    CG   CD1  CD2                                       
REMARK 470     THR A  72    OG1  CG2                                            
REMARK 470     ASP A  73    CG   OD1  OD2                                       
REMARK 470     GLN A  88    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 125    CG   CD   CE   NZ                                   
REMARK 470     LYS A 172    CG   CD   CE   NZ                                   
REMARK 470     ARG A 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 331    CG   CD   CE   NZ                                   
REMARK 470     LYS A 336    CG   CD   CE   NZ                                   
REMARK 470     TYR A 435    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 436    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 460    CG   CD   CE   NZ                                   
REMARK 470     LYS A 463    CG   CD   CE   NZ                                   
REMARK 470     LYS C   4    CG   CD   CE   NZ                                   
REMARK 470     LYS C   8    CG   CD   CE   NZ                                   
REMARK 470     LYS C  12    CG   CD   CE   NZ                                   
REMARK 470     LYS C  54    CG   CD   CE   NZ                                   
REMARK 470     GLU C  57    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  58    CG   CD   OE1  OE2                                  
REMARK 470     LEU C  61    CG   CD1  CD2                                       
REMARK 470     LYS C  63    CG   CD   CE   NZ                                   
REMARK 470     GLU C  83    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  95    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  99    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 106    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 107    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 110    CG   CD   OE1  NE2                                  
REMARK 470     HIS C 115    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET D   1    CG   SD   CE                                        
REMARK 470     LYS D   4    CG   CD   CE   NZ                                   
REMARK 470     LYS D   8    CG   CD   CE   NZ                                   
REMARK 470     LYS D  12    CG   CD   CE   NZ                                   
REMARK 470     SER D  45    OG                                                  
REMARK 470     LYS D  54    CG   CD   CE   NZ                                   
REMARK 470     GLU D  62    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  87    CG   CD   OE1  OE2                                  
REMARK 470     GLN D  95    CG   CD   OE1  NE2                                  
REMARK 470     MET D  98    CG   SD   CE                                        
REMARK 470     GLU D  99    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 100    CG   CD   CE   NZ                                   
REMARK 470     ARG D 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D 103    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 106    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 107    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  18    CG   CD   CE   NZ                                   
REMARK 470     LEU B  71    CG   CD1  CD2                                       
REMARK 470     THR B  72    OG1  CG2                                            
REMARK 470     ASP B  73    CG   OD1  OD2                                       
REMARK 470     LYS B 125    CG   CD   CE   NZ                                   
REMARK 470     LYS B 172    CG   CD   CE   NZ                                   
REMARK 470     LYS B 174    CG   CD   CE   NZ                                   
REMARK 470     ARG B 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 331    CG   CD   CE   NZ                                   
REMARK 470     ASP B 335    CG   OD1  OD2                                       
REMARK 470     LYS B 336    CG   CD   CE   NZ                                   
REMARK 470     GLU B 389    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 435    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 436    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 460    CG   CD   CE   NZ                                   
REMARK 470     LYS B 463    CG   CD   CE   NZ                                   
REMARK 470     GLU B 465    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 467    CG   CD   OE1  OE2                                  
REMARK 470     LYS E   4    CG   CD   CE   NZ                                   
REMARK 470     LYS E   8    CG   CD   CE   NZ                                   
REMARK 470     LYS E  12    CG   CD   CE   NZ                                   
REMARK 470     LYS E  48    CG   CD   CE   NZ                                   
REMARK 470     LYS E  54    CG   CD   CE   NZ                                   
REMARK 470     GLU E  57    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  58    CG   CD   OE1  OE2                                  
REMARK 470     LEU E  61    CG   CD1  CD2                                       
REMARK 470     LYS E  63    CG   CD   CE   NZ                                   
REMARK 470     GLU E  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  87    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  99    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 106    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 107    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN E 110    CG   CD   OE1  NE2                                  
REMARK 470     HIS E 115    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET F   1    CG   SD   CE                                        
REMARK 470     LYS F   4    CG   CD   CE   NZ                                   
REMARK 470     LYS F   8    CG   CD   CE   NZ                                   
REMARK 470     LYS F  12    CG   CD   CE   NZ                                   
REMARK 470     SER F  45    OG                                                  
REMARK 470     LYS F  54    CG   CD   CE   NZ                                   
REMARK 470     GLU F  57    CG   CD   OE1  OE2                                  
REMARK 470     GLU F  62    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  63    CG   CD   CE   NZ                                   
REMARK 470     GLU F  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU F  87    CG   CD   OE1  OE2                                  
REMARK 470     GLN F  95    CG   CD   OE1  NE2                                  
REMARK 470     MET F  98    CG   SD   CE                                        
REMARK 470     GLU F  99    CG   CD   OE1  OE2                                  
REMARK 470     ARG F 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN F 103    CG   CD   OE1  NE2                                  
REMARK 470     GLU F 106    CG   CD   OE1  OE2                                  
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    SER A  59     -116.01    -96.58                                   
REMARK 500    THR A  60      -71.83    -76.01                                   
REMARK 500    MET A  74      -38.44    -28.15                                   
REMARK 500    ASP A  75      -40.14    -19.30                                   
REMARK 500    VAL A 121      -14.95    -49.52                                   
REMARK 500    HIS A 150      -55.84   -139.33                                   
REMARK 500    LYS A 174     -114.78    -65.82                                   
REMARK 500    LEU A 175     -165.77    -75.34                                   
REMARK 500    ASN A 204      -74.62   -119.96                                   
REMARK 500    GLN A 209       72.24    167.69                                   
REMARK 500    LEU A 332     -169.69   -101.71                                   
REMARK 500    GLU A 333      162.44    -30.21                                   
REMARK 500    PRO A 407       -7.48    -58.56                                   
REMARK 500    GLU C  62      -73.99   -103.38                                   
REMARK 500    ASN D   2      -75.92    -55.69                                   
REMARK 500    ALA D  46      118.74    -36.46                                   
REMARK 500    VAL D  49      -35.11    -27.44                                   
REMARK 500    GLN D  50      -73.01    -25.90                                   
REMARK 500    GLU D  62      -72.17    -86.56                                   
REMARK 500    MET D  88      -39.93   -135.31                                   
REMARK 500    SER B  59      -98.39    -96.69                                   
REMARK 500    THR B  60      -74.54   -102.00                                   
REMARK 500    GLU B  90      107.06    -48.70                                   
REMARK 500    HIS B 150      -65.93   -138.26                                   
REMARK 500    ILE B 152      -85.10     -0.93                                   
REMARK 500    LYS B 174     -106.28    -77.78                                   
REMARK 500    ASN B 204      -81.74   -108.52                                   
REMARK 500    GLN B 209       76.71    178.08                                   
REMARK 500    ARG B 292       50.69    -96.13                                   
REMARK 500    MET B 294       -4.61     75.74                                   
REMARK 500    ASP B 354       94.29   -162.54                                   
REMARK 500    HIS B 380     -165.73   -103.89                                   
REMARK 500    ASP B 394       78.81   -101.80                                   
REMARK 500    PRO B 407       -7.24    -51.27                                   
REMARK 500    GLU B 467      102.23    -59.63                                   
REMARK 500    GLU E  62      -68.79   -124.27                                   
REMARK 500    GLU F  62      -82.75    -81.26                                   
REMARK 500    GLU F  87        0.73    -66.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WVW   RELATED DB: PDB                                   
REMARK 900 CRYO-EM STRUCTURE MODEL OF THE SAME COMPLEX                          
REMARK 900 RELATED ID: 3HYB   RELATED DB: PDB                                   
REMARK 900 RBCX DIMER COMPLEX STRUCTURE, CRYSTAL FORM II                        
REMARK 900 RELATED ID: 2PEO   RELATED DB: PDB                                   
REMARK 900 RBCX DIMER COMPLEX STRUCTURE, CRYSTAL FORM I                         
REMARK 900 RELATED ID: EMD-1655   RELATED DB: EMDB                              
REMARK 900 CRYO-EM MAP OF THE SAME COMPLEX                                      
REMARK 900 RELATED ID: 1RBL   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE COMPLETED RUBISCO HOLOENZYME, CLOSED FORM           
DBREF  3RG6 A    1   472  UNP    P00880   RBL_SYNP6        1    472             
DBREF  3RG6 C    1   135  UNP    Q44212   Q44212_9NOST     1    135             
DBREF  3RG6 D    1   135  UNP    Q44212   Q44212_9NOST     1    135             
DBREF  3RG6 B    1   472  UNP    P00880   RBL_SYNP6        1    472             
DBREF  3RG6 E    1   135  UNP    Q44212   Q44212_9NOST     1    135             
DBREF  3RG6 F    1   135  UNP    Q44212   Q44212_9NOST     1    135             
SEQADV 3RG6 MET C  -19  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 GLY C  -18  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER C  -17  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER C  -16  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS C  -15  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS C  -14  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS C  -13  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS C  -12  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS C  -11  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS C  -10  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER C   -9  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER C   -8  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 GLY C   -7  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 LEU C   -6  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 VAL C   -5  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 PRO C   -4  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 ARG C   -3  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 GLY C   -2  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER C   -1  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS C    0  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 MET D  -19  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 GLY D  -18  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER D  -17  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER D  -16  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS D  -15  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS D  -14  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS D  -13  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS D  -12  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS D  -11  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS D  -10  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER D   -9  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER D   -8  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 GLY D   -7  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 LEU D   -6  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 VAL D   -5  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 PRO D   -4  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 ARG D   -3  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 GLY D   -2  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER D   -1  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS D    0  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 MET E  -19  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 GLY E  -18  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER E  -17  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER E  -16  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS E  -15  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS E  -14  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS E  -13  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS E  -12  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS E  -11  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS E  -10  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER E   -9  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER E   -8  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 GLY E   -7  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 LEU E   -6  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 VAL E   -5  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 PRO E   -4  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 ARG E   -3  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 GLY E   -2  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER E   -1  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS E    0  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 MET F  -19  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 GLY F  -18  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER F  -17  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER F  -16  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS F  -15  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS F  -14  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS F  -13  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS F  -12  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS F  -11  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS F  -10  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER F   -9  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER F   -8  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 GLY F   -7  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 LEU F   -6  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 VAL F   -5  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 PRO F   -4  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 ARG F   -3  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 GLY F   -2  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 SER F   -1  UNP  Q44212              EXPRESSION TAG                 
SEQADV 3RG6 HIS F    0  UNP  Q44212              EXPRESSION TAG                 
SEQRES   1 A  472  MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY          
SEQRES   2 A  472  VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR          
SEQRES   3 A  472  THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE          
SEQRES   4 A  472  SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA          
SEQRES   5 A  472  ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR          
SEQRES   6 A  472  VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS          
SEQRES   7 A  472  GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU          
SEQRES   8 A  472  ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU          
SEQRES   9 A  472  PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE          
SEQRES  10 A  472  VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU          
SEQRES  11 A  472  ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS          
SEQRES  12 A  472  THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG          
SEQRES  13 A  472  ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS          
SEQRES  14 A  472  THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR          
SEQRES  15 A  472  GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP          
SEQRES  16 A  472  PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE          
SEQRES  17 A  472  GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA          
SEQRES  18 A  472  ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY          
SEQRES  19 A  472  HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET          
SEQRES  20 A  472  MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO          
SEQRES  21 A  472  ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA          
SEQRES  22 A  472  ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL          
SEQRES  23 A  472  LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP          
SEQRES  24 A  472  ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA          
SEQRES  25 A  472  LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER          
SEQRES  26 A  472  GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER          
SEQRES  27 A  472  THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE          
SEQRES  28 A  472  GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP          
SEQRES  29 A  472  TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY          
SEQRES  30 A  472  GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE          
SEQRES  31 A  472  PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR          
SEQRES  32 A  472  LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA          
SEQRES  33 A  472  ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN          
SEQRES  34 A  472  GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU          
SEQRES  35 A  472  ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA          
SEQRES  36 A  472  LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR          
SEQRES  37 A  472  MET ASP LYS LEU                                              
SEQRES   1 C  155  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  155  LEU VAL PRO ARG GLY SER HIS MET ASN LEU LYS GLN ILE          
SEQRES   3 C  155  ALA LYS ASP THR ALA LYS THR LEU GLN SER TYR LEU THR          
SEQRES   4 C  155  TYR GLN ALA LEU ARG THR VAL LEU ALA GLN LEU GLY GLU          
SEQRES   5 C  155  THR ASN PRO PRO LEU ALA LEU TRP LEU HIS ASN PHE SER          
SEQRES   6 C  155  ALA GLY LYS VAL GLN ASP GLY GLU LYS TYR ILE GLU GLU          
SEQRES   7 C  155  LEU PHE LEU GLU LYS PRO ASP LEU ALA LEU ARG ILE MET          
SEQRES   8 C  155  THR VAL ARG GLU HIS ILE ALA GLU GLU ILE ALA GLU PHE          
SEQRES   9 C  155  LEU PRO GLU MET VAL VAL THR GLY ILE GLN GLN ALA ASN          
SEQRES  10 C  155  MET GLU LYS ARG ARG GLN HIS LEU GLU ARG MET THR GLN          
SEQRES  11 C  155  VAL SER LEU SER HIS PRO SER PRO GLU SER GLU GLN GLN          
SEQRES  12 C  155  GLN PHE SER ASP PRO ASP TRP ASP ASN LEU ALA SER              
SEQRES   1 D  155  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  155  LEU VAL PRO ARG GLY SER HIS MET ASN LEU LYS GLN ILE          
SEQRES   3 D  155  ALA LYS ASP THR ALA LYS THR LEU GLN SER TYR LEU THR          
SEQRES   4 D  155  TYR GLN ALA LEU ARG THR VAL LEU ALA GLN LEU GLY GLU          
SEQRES   5 D  155  THR ASN PRO PRO LEU ALA LEU TRP LEU HIS ASN PHE SER          
SEQRES   6 D  155  ALA GLY LYS VAL GLN ASP GLY GLU LYS TYR ILE GLU GLU          
SEQRES   7 D  155  LEU PHE LEU GLU LYS PRO ASP LEU ALA LEU ARG ILE MET          
SEQRES   8 D  155  THR VAL ARG GLU HIS ILE ALA GLU GLU ILE ALA GLU PHE          
SEQRES   9 D  155  LEU PRO GLU MET VAL VAL THR GLY ILE GLN GLN ALA ASN          
SEQRES  10 D  155  MET GLU LYS ARG ARG GLN HIS LEU GLU ARG MET THR GLN          
SEQRES  11 D  155  VAL SER LEU SER HIS PRO SER PRO GLU SER GLU GLN GLN          
SEQRES  12 D  155  GLN PHE SER ASP PRO ASP TRP ASP ASN LEU ALA SER              
SEQRES   1 B  472  MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY          
SEQRES   2 B  472  VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR          
SEQRES   3 B  472  THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE          
SEQRES   4 B  472  SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA          
SEQRES   5 B  472  ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR          
SEQRES   6 B  472  VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS          
SEQRES   7 B  472  GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU          
SEQRES   8 B  472  ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU          
SEQRES   9 B  472  PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE          
SEQRES  10 B  472  VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU          
SEQRES  11 B  472  ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS          
SEQRES  12 B  472  THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG          
SEQRES  13 B  472  ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS          
SEQRES  14 B  472  THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR          
SEQRES  15 B  472  GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP          
SEQRES  16 B  472  PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE          
SEQRES  17 B  472  GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA          
SEQRES  18 B  472  ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY          
SEQRES  19 B  472  HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET          
SEQRES  20 B  472  MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO          
SEQRES  21 B  472  ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA          
SEQRES  22 B  472  ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL          
SEQRES  23 B  472  LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP          
SEQRES  24 B  472  ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA          
SEQRES  25 B  472  LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER          
SEQRES  26 B  472  GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER          
SEQRES  27 B  472  THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE          
SEQRES  28 B  472  GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP          
SEQRES  29 B  472  TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY          
SEQRES  30 B  472  GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE          
SEQRES  31 B  472  PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR          
SEQRES  32 B  472  LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA          
SEQRES  33 B  472  ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN          
SEQRES  34 B  472  GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU          
SEQRES  35 B  472  ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA          
SEQRES  36 B  472  LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR          
SEQRES  37 B  472  MET ASP LYS LEU                                              
SEQRES   1 E  155  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 E  155  LEU VAL PRO ARG GLY SER HIS MET ASN LEU LYS GLN ILE          
SEQRES   3 E  155  ALA LYS ASP THR ALA LYS THR LEU GLN SER TYR LEU THR          
SEQRES   4 E  155  TYR GLN ALA LEU ARG THR VAL LEU ALA GLN LEU GLY GLU          
SEQRES   5 E  155  THR ASN PRO PRO LEU ALA LEU TRP LEU HIS ASN PHE SER          
SEQRES   6 E  155  ALA GLY LYS VAL GLN ASP GLY GLU LYS TYR ILE GLU GLU          
SEQRES   7 E  155  LEU PHE LEU GLU LYS PRO ASP LEU ALA LEU ARG ILE MET          
SEQRES   8 E  155  THR VAL ARG GLU HIS ILE ALA GLU GLU ILE ALA GLU PHE          
SEQRES   9 E  155  LEU PRO GLU MET VAL VAL THR GLY ILE GLN GLN ALA ASN          
SEQRES  10 E  155  MET GLU LYS ARG ARG GLN HIS LEU GLU ARG MET THR GLN          
SEQRES  11 E  155  VAL SER LEU SER HIS PRO SER PRO GLU SER GLU GLN GLN          
SEQRES  12 E  155  GLN PHE SER ASP PRO ASP TRP ASP ASN LEU ALA SER              
SEQRES   1 F  155  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 F  155  LEU VAL PRO ARG GLY SER HIS MET ASN LEU LYS GLN ILE          
SEQRES   3 F  155  ALA LYS ASP THR ALA LYS THR LEU GLN SER TYR LEU THR          
SEQRES   4 F  155  TYR GLN ALA LEU ARG THR VAL LEU ALA GLN LEU GLY GLU          
SEQRES   5 F  155  THR ASN PRO PRO LEU ALA LEU TRP LEU HIS ASN PHE SER          
SEQRES   6 F  155  ALA GLY LYS VAL GLN ASP GLY GLU LYS TYR ILE GLU GLU          
SEQRES   7 F  155  LEU PHE LEU GLU LYS PRO ASP LEU ALA LEU ARG ILE MET          
SEQRES   8 F  155  THR VAL ARG GLU HIS ILE ALA GLU GLU ILE ALA GLU PHE          
SEQRES   9 F  155  LEU PRO GLU MET VAL VAL THR GLY ILE GLN GLN ALA ASN          
SEQRES  10 F  155  MET GLU LYS ARG ARG GLN HIS LEU GLU ARG MET THR GLN          
SEQRES  11 F  155  VAL SER LEU SER HIS PRO SER PRO GLU SER GLU GLN GLN          
SEQRES  12 F  155  GLN PHE SER ASP PRO ASP TRP ASP ASN LEU ALA SER              
HELIX    1   1 PRO A   46  SER A   59  1                                  14    
HELIX    2   2 ASP A   73  TYR A   77  5                                   5    
HELIX    3   3 PRO A  101  PHE A  105  5                                   5    
HELIX    4   4 SER A  109  VAL A  118  1                                  10    
HELIX    5   5 ASN A  120  PHE A  124  5                                   5    
HELIX    6   6 PRO A  138  LYS A  143  1                                   6    
HELIX    7   7 GLY A  151  ASN A  160  1                                  10    
HELIX    8   8 SER A  178  GLY A  192  1                                  15    
HELIX    9   9 ARG A  210  GLY A  230  1                                  21    
HELIX   10  10 THR A  243  LEU A  257  1                                  15    
HELIX   11  11 PHE A  266  GLY A  270  1                                   5    
HELIX   12  12 GLY A  270  GLY A  285  1                                  16    
HELIX   13  13 MET A  294  ARG A  300  1                                   7    
HELIX   14  14 HIS A  307  GLY A  319  1                                  13    
HELIX   15  15 GLY A  334  GLU A  348  1                                  15    
HELIX   16  16 ASP A  354  GLY A  358  5                                   5    
HELIX   17  17 HIS A  380  TRP A  382  5                                   3    
HELIX   18  18 HIS A  383  GLY A  392  1                                  10    
HELIX   19  19 GLY A  409  GLY A  431  1                                  23    
HELIX   20  20 GLU A  437  LYS A  447  1                                  11    
HELIX   21  21 SER A  449  LEU A  458  1                                  10    
HELIX   22  22 ASN C    2  LEU C   30  1                                  29    
HELIX   23  23 ASN C   34  SER C   45  1                                  12    
HELIX   24  24 ASP C   51  LEU C   61  1                                  11    
HELIX   25  25 LYS C   63  ALA C   82  1                                  20    
HELIX   26  26 PHE C   84  LEU C  113  1                                  30    
HELIX   27  27 MET D    1  ASN D   34  1                                  34    
HELIX   28  28 ASN D   34  ALA D   46  1                                  13    
HELIX   29  29 GLY D   47  GLN D   50  5                                   4    
HELIX   30  30 ASP D   51  LYS D   63  1                                  13    
HELIX   31  31 LYS D   63  ALA D   82  1                                  20    
HELIX   32  32 LEU D   85  ARG D  107  1                                  23    
HELIX   33  33 PRO B   46  SER B   59  1                                  14    
HELIX   34  34 SER B  109  VAL B  118  1                                  10    
HELIX   35  35 PRO B  138  LYS B  143  1                                   6    
HELIX   36  36 GLY B  151  ASN B  160  1                                  10    
HELIX   37  37 SER B  178  GLY B  192  1                                  15    
HELIX   38  38 ARG B  210  GLY B  230  1                                  21    
HELIX   39  39 THR B  243  LEU B  257  1                                  15    
HELIX   40  40 ASP B  265  GLY B  270  1                                   6    
HELIX   41  41 GLY B  270  ASN B  284  1                                  15    
HELIX   42  42 HIS B  295  ARG B  300  1                                   6    
HELIX   43  43 HIS B  307  GLY B  319  1                                  13    
HELIX   44  44 GLY B  334  GLU B  348  1                                  15    
HELIX   45  45 ASP B  354  GLY B  358  5                                   5    
HELIX   46  46 HIS B  380  TRP B  382  5                                   3    
HELIX   47  47 HIS B  383  GLY B  392  1                                  10    
HELIX   48  48 GLY B  409  GLY B  431  1                                  23    
HELIX   49  49 GLU B  437  GLY B  446  1                                  10    
HELIX   50  50 SER B  449  LEU B  458  1                                  10    
HELIX   51  51 ASN E    2  ASN E   34  1                                  33    
HELIX   52  52 ASN E   34  ALA E   46  1                                  13    
HELIX   53  53 ASP E   51  PHE E   60  1                                  10    
HELIX   54  54 LYS E   63  ALA E   82  1                                  20    
HELIX   55  55 PHE E   84  HIS E  115  1                                  32    
HELIX   56  56 MET F    1  ASN F   34  1                                  34    
HELIX   57  57 ASN F   34  ALA F   46  1                                  13    
HELIX   58  58 GLY F   47  GLN F   50  5                                   4    
HELIX   59  59 ASP F   51  LYS F   63  1                                  13    
HELIX   60  60 LYS F   63  ALA F   82  1                                  20    
HELIX   61  61 LEU F   85  GLU F  106  1                                  22    
SHEET    1   A 5 LYS A  80  PRO A  86  0                                        
SHEET    2   A 5 TYR A  94  TYR A 100 -1  O  PHE A  95   N  GLU A  85           
SHEET    3   A 5 LEU A  33  PRO A  41 -1  N  LEU A  33   O  TYR A 100           
SHEET    4   A 5 ILE A 127  ARG A 136 -1  O  ARG A 128   N  SER A  40           
SHEET    5   A 5 GLY A 305  ILE A 306  1  O  GLY A 305   N  LEU A 132           
SHEET    1   B 4 MET A 166  LEU A 167  0                                        
SHEET    2   B 4 VAL A 396  LEU A 397  1  O  LEU A 397   N  MET A 166           
SHEET    3   B 4 LEU A 372  ALA A 375  1  N  ALA A 375   O  VAL A 396           
SHEET    4   B 4 HIS A 322  HIS A 324  1  N  LEU A 323   O  VAL A 374           
SHEET    1   C 4 PHE A 196  LYS A 198  0                                        
SHEET    2   C 4 GLY A 234  ASN A 238  1  O  TYR A 236   N  THR A 197           
SHEET    3   C 4 ILE A 261  ASP A 265  1  O  MET A 263   N  LEU A 237           
SHEET    4   C 4 LEU A 287  HIS A 291  1  O  HIS A 289   N  ILE A 262           
SHEET    1   D 2 HIS A 350  ILE A 351  0                                        
SHEET    2   D 2 GLN A 363  ASP A 364 -1  O  GLN A 363   N  ILE A 351           
SHEET    1   E 5 LYS B  80  PRO B  86  0                                        
SHEET    2   E 5 TYR B  94  TYR B 100 -1  O  ALA B  99   N  LYS B  80           
SHEET    3   E 5 LEU B  33  PRO B  41 -1  N  LEU B  33   O  TYR B 100           
SHEET    4   E 5 ILE B 127  ARG B 136 -1  O  ARG B 131   N  ARG B  38           
SHEET    5   E 5 GLY B 305  ILE B 306  1  O  GLY B 305   N  LEU B 132           
SHEET    1   F 9 MET B 166  THR B 170  0                                        
SHEET    2   F 9 PHE B 196  LYS B 198  1  O  PHE B 196   N  LEU B 167           
SHEET    3   F 9 GLY B 234  ASN B 238  1  O  TYR B 236   N  THR B 197           
SHEET    4   F 9 ILE B 261  HIS B 264  1  O  MET B 263   N  LEU B 237           
SHEET    5   F 9 LEU B 287  ILE B 290  1  O  HIS B 289   N  ILE B 262           
SHEET    6   F 9 HIS B 322  HIS B 324  1  O  HIS B 322   N  ILE B 290           
SHEET    7   F 9 LEU B 372  ALA B 375  1  O  VAL B 374   N  LEU B 323           
SHEET    8   F 9 VAL B 396  GLN B 398  1  O  VAL B 396   N  ALA B 375           
SHEET    9   F 9 MET B 166  THR B 170  1  N  MET B 166   O  LEU B 397           
SHEET    1   G 2 HIS B 350  ILE B 351  0                                        
SHEET    2   G 2 GLN B 363  ASP B 364 -1  O  GLN B 363   N  ILE B 351           
SSBOND   1 CYS A  244    CYS B  244                          1555   1555  2.05  
CISPEP   1 LYS A  172    PRO A  173          0         5.78                     
CISPEP   2 LYS B  172    PRO B  173          0         1.20                     
CRYST1  244.750  244.750   99.669  90.00  90.00  90.00 I 4          32          
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      0.004086  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004086  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010033        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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