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Database: PDB
Entry: 4FD2
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HEADER    CHAPERONE                               25-MAY-12   4FD2              
TITLE     CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF CLPB                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHAPERONE PROTEIN CLPB;                                    
COMPND   3 CHAIN: A, B, D;                                                      
COMPND   4 FRAGMENT: UNP RESIDUES 545-852;                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   3 ORGANISM_TAXID: 300852;                                              
SOURCE   4 STRAIN: HB8 / ATCC 27634 / DSM 579;                                  
SOURCE   5 GENE: CLPB, TTHA1487;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL CODONPLUS;                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET24                                     
KEYWDS    AAA DOMAIN, CHAPERONE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.B.BITER,S.LEE,N.SUNG,F.T.F.TSAI                                     
REVDAT   4   28-FEB-24 4FD2    1       REMARK SEQADV                            
REVDAT   3   18-APR-18 4FD2    1       REMARK                                   
REVDAT   2   22-AUG-12 4FD2    1       JRNL                                     
REVDAT   1   18-JUL-12 4FD2    0                                                
JRNL        AUTH   A.B.BITER,S.LEE,N.SUNG,F.T.TSAI                              
JRNL        TITL   STRUCTURAL BASIS FOR INTERSUBUNIT SIGNALING IN A PROTEIN     
JRNL        TITL 2 DISAGGREGATING MACHINE.                                      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109 12515 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22802670                                                     
JRNL        DOI    10.1073/PNAS.1207040109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 24567                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.279                           
REMARK   3   R VALUE            (WORKING SET) : 0.278                           
REMARK   3   FREE R VALUE                     : 0.298                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1001                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1696                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.53                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3550                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 81                           
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7386                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
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) : 109.4                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -25.04000                                            
REMARK   3    B22 (A**2) : -25.04000                                            
REMARK   3    B33 (A**2) : 50.07000                                             
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): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.500         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 72.784        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.901                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.882                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7599 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10284 ; 1.515 ; 2.001       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   921 ; 5.745 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   366 ;35.023 ;22.623       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1368 ;20.350 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    96 ;19.958 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1161 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5718 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4599 ; 1.707 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7431 ; 3.225 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3000 ; 3.985 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2853 ; 7.443 ; 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 D                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    545       A     756      4                      
REMARK   3           1     B    545       B     756      4                      
REMARK   3           1     D    545       D     756      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1702 ; 0.150 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1702 ; 0.180 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1702 ; 0.140 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1702 ; 1.500 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1702 ; 1.020 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1702 ; 0.840 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B D                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    757       A     852      4                      
REMARK   3           1     B    757       B     852      4                      
REMARK   3           1     D    757       D     852      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    760 ; 0.120 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    760 ; 0.200 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    D    (A):    760 ; 0.150 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    760 ; 1.400 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    B (A**2):    760 ; 1.240 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    D (A**2):    760 ; 0.590 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B D                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    853       A     853      4                      
REMARK   3           1     B    853       B     853      4                      
REMARK   3           1     D    853       D     853      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    A    (A):     27 ; 0.320 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    B    (A):     27 ; 0.400 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    D    (A):     27 ; 0.530 ; 0.500           
REMARK   3   MEDIUM THERMAL     3    A (A**2):     27 ; 0.200 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    B (A**2):     27 ; 0.290 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    D (A**2):     27 ; 0.210 ; 2.000           
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.497                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : H+K,-K,-L                                       
REMARK   3      TWIN FRACTION : 0.503                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 21                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   545        A   573                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.4804  -2.8295  41.3899              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4111 T22:   0.5226                                     
REMARK   3      T33:   0.0436 T12:   0.2569                                     
REMARK   3      T13:   0.0374 T23:   0.0271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.7635 L22:  23.4111                                     
REMARK   3      L33:   1.0309 L12:  13.4796                                     
REMARK   3      L13:  -1.9313 L23:  -5.2274                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3374 S12:   0.9198 S13:  -0.7641                       
REMARK   3      S21:   0.4823 S22:  -0.4809 S23:  -0.7095                       
REMARK   3      S31:   0.0301 S32:   0.3771 S33:   0.1435                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   574        A   628                          
REMARK   3    ORIGIN FOR THE GROUP (A): -55.9172   7.3322  37.4749              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4081 T22:   0.5499                                     
REMARK   3      T33:   0.1808 T12:  -0.0155                                     
REMARK   3      T13:   0.0541 T23:   0.0579                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0239 L22:   2.4797                                     
REMARK   3      L33:   1.8345 L12:   0.8251                                     
REMARK   3      L13:   1.1028 L23:   0.1019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0800 S12:   0.1287 S13:   0.2115                       
REMARK   3      S21:  -0.3104 S22:  -0.1758 S23:   0.2051                       
REMARK   3      S31:  -0.2490 S32:   0.0796 S33:   0.0958                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   629        A   640                          
REMARK   3    ORIGIN FOR THE GROUP (A): -67.6004  25.4094  30.4338              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9179 T22:   0.8976                                     
REMARK   3      T33:   0.9235 T12:  -0.3563                                     
REMARK   3      T13:  -0.6659 T23:   0.2566                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9238 L22:  42.8971                                     
REMARK   3      L33:   6.2052 L12:  -5.3171                                     
REMARK   3      L13:  -6.6102 L23:  -8.8245                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7124 S12:  -0.3763 S13:   2.0730                       
REMARK   3      S21:  -4.3670 S22:   3.3573 S23:   3.6502                       
REMARK   3      S31:   1.4961 S32:  -0.6493 S33:  -2.6449                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   641        A   651                          
REMARK   3    ORIGIN FOR THE GROUP (A): -68.6007  23.9254  20.9087              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1008 T22:   1.8312                                     
REMARK   3      T33:   3.9076 T12:   0.4155                                     
REMARK   3      T13:   0.5029 T23:  -0.1480                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9666 L22:  68.8646                                     
REMARK   3      L33:  15.8944 L12: -24.3745                                     
REMARK   3      L13:   7.0618 L23: -28.0721                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -2.4043 S12:   1.3486 S13:  -1.2115                       
REMARK   3      S21:   6.9868 S22:  -1.3222 S23:   1.5535                       
REMARK   3      S31:  -2.3902 S32:  -0.4457 S33:   3.7266                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   652        A   712                          
REMARK   3    ORIGIN FOR THE GROUP (A): -64.4884  13.1780  34.3742              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4480 T22:   0.5466                                     
REMARK   3      T33:   0.2361 T12:   0.1035                                     
REMARK   3      T13:   0.0555 T23:   0.0464                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2041 L22:   1.5250                                     
REMARK   3      L33:   2.6271 L12:   1.0279                                     
REMARK   3      L13:   2.4081 L23:  -1.2415                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1112 S12:  -0.0205 S13:   0.8032                       
REMARK   3      S21:   0.0905 S22:   0.0163 S23:   0.3068                       
REMARK   3      S31:  -0.2569 S32:  -0.0804 S33:   0.0949                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   713        A   743                          
REMARK   3    ORIGIN FOR THE GROUP (A): -54.8987  13.2649  57.0878              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3330 T22:   0.8502                                     
REMARK   3      T33:   0.1044 T12:  -0.2120                                     
REMARK   3      T13:   0.1990 T23:   0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  30.2297 L22:  10.4819                                     
REMARK   3      L33:  18.4936 L12:  -7.3139                                     
REMARK   3      L13:  17.0310 L23:  -3.8443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2387 S12:  -3.6177 S13:  -0.6391                       
REMARK   3      S21:   0.4823 S22:  -0.5998 S23:   0.7311                       
REMARK   3      S31:   0.6535 S32:  -1.0340 S33:   0.3612                       
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   744        A   852                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2677  12.1431  36.1919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4356 T22:   0.4198                                     
REMARK   3      T33:   0.3181 T12:   0.0105                                     
REMARK   3      T13:  -0.0335 T23:   0.0996                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5610 L22:   0.5010                                     
REMARK   3      L33:   2.7282 L12:   1.2435                                     
REMARK   3      L13:  -3.6866 L23:  -0.5006                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0194 S12:  -0.1726 S13:  -0.2898                       
REMARK   3      S21:   0.1142 S22:  -0.1016 S23:  -0.1170                       
REMARK   3      S31:  -0.0416 S32:   0.1837 S33:   0.0822                       
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   545        B   573                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.1383  -5.8435 -37.0306              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5113 T22:   0.6207                                     
REMARK   3      T33:   0.0875 T12:   0.1613                                     
REMARK   3      T13:   0.0887 T23:  -0.1602                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.3320 L22:  15.0753                                     
REMARK   3      L33:   1.6619 L12:   8.5892                                     
REMARK   3      L13:   4.7576 L23:   3.2632                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0088 S12:  -0.0573 S13:   0.0806                       
REMARK   3      S21:   0.7422 S22:  -0.0708 S23:   0.6735                       
REMARK   3      S31:  -0.0176 S32:  -0.2114 S33:   0.0795                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   574        B   628                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.8330  -7.4677 -32.8015              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6720 T22:   0.6624                                     
REMARK   3      T33:   0.5161 T12:   0.0094                                     
REMARK   3      T13:   0.0165 T23:  -0.0503                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1931 L22:   3.5670                                     
REMARK   3      L33:   2.0445 L12:  -0.0816                                     
REMARK   3      L13:  -0.8021 L23:  -0.9947                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0400 S12:  -0.0788 S13:  -0.0359                       
REMARK   3      S21:   0.3410 S22:  -0.0101 S23:  -0.4432                       
REMARK   3      S31:  -0.1297 S32:   0.1865 S33:   0.0502                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   629        B   651                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1777  -9.8297 -20.5239              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7174 T22:   1.3684                                     
REMARK   3      T33:   1.7801 T12:  -0.0848                                     
REMARK   3      T13:   0.0700 T23:   0.2957                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7765 L22:   4.4634                                     
REMARK   3      L33:  55.0495 L12:  -5.7543                                     
REMARK   3      L13:  -4.2821 L23:   7.3159                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.3872 S12:  -0.6548 S13:  -0.5646                       
REMARK   3      S21:   1.1984 S22:   0.5658 S23:   0.1907                       
REMARK   3      S31:  -1.7815 S32:   4.1225 S33:   0.8215                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   652        B   708                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.6720 -12.9355 -28.6220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5857 T22:   0.6937                                     
REMARK   3      T33:   0.4747 T12:   0.0732                                     
REMARK   3      T13:  -0.0580 T23:  -0.0916                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6870 L22:   5.7287                                     
REMARK   3      L33:   0.7240 L12:   0.5316                                     
REMARK   3      L13:   0.9633 L23:  -0.9292                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0788 S12:  -0.0569 S13:  -0.1773                       
REMARK   3      S21:   0.1166 S22:   0.1417 S23:  -0.9823                       
REMARK   3      S31:   0.0773 S32:   0.4161 S33:  -0.0629                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   709        B   743                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.9725  -2.3437 -51.5397              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6739 T22:   0.9724                                     
REMARK   3      T33:   0.1443 T12:   0.1368                                     
REMARK   3      T13:   0.3036 T23:  -0.1157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  23.7923 L22:  18.3518                                     
REMARK   3      L33:   6.5858 L12: -13.5413                                     
REMARK   3      L13:   9.9332 L23:  -8.7219                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2899 S12:   2.4456 S13:  -0.0217                       
REMARK   3      S21:  -1.2721 S22:  -0.7307 S23:  -0.4307                       
REMARK   3      S31:   0.5596 S32:   0.2194 S33:   0.4408                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   744        B   780                          
REMARK   3    ORIGIN FOR THE GROUP (A): -37.2648   6.5815 -35.0756              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5972 T22:   0.6954                                     
REMARK   3      T33:   0.4558 T12:   0.0029                                     
REMARK   3      T13:  -0.0762 T23:  -0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4520 L22:   2.3262                                     
REMARK   3      L33:   2.9853 L12:  -0.4524                                     
REMARK   3      L13:  -0.4694 L23:   0.8996                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2202 S12:   0.1802 S13:   0.0473                       
REMARK   3      S21:  -0.2206 S22:  -0.1664 S23:   0.4996                       
REMARK   3      S31:  -0.3310 S32:  -0.0834 S33:   0.3867                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   781        B   852                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.3794  24.5318 -29.0750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6545 T22:   0.5413                                     
REMARK   3      T33:   0.6137 T12:  -0.0962                                     
REMARK   3      T13:  -0.0409 T23:  -0.0573                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4658 L22:   4.8516                                     
REMARK   3      L33:   4.5955 L12:  -2.5609                                     
REMARK   3      L13:  -0.9892 L23:   0.6795                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1375 S12:   0.1113 S13:   0.3790                       
REMARK   3      S21:  -0.0315 S22:   0.4001 S23:   0.2617                       
REMARK   3      S31:   0.2049 S32:  -0.1254 S33:  -0.2626                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   545        D   573                          
REMARK   3    ORIGIN FOR THE GROUP (A): -38.2017  -3.1318  -1.7965              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4548 T22:   0.2982                                     
REMARK   3      T33:   0.0206 T12:  -0.1228                                     
REMARK   3      T13:  -0.0358 T23:   0.0481                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  34.9651 L22:   5.9388                                     
REMARK   3      L33:   1.0181 L12:  -2.5568                                     
REMARK   3      L13:   3.1620 L23:   2.3117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7780 S12:  -0.0304 S13:   0.9447                       
REMARK   3      S21:  -0.8053 S22:  -0.8724 S23:  -0.1529                       
REMARK   3      S31:  -0.3175 S32:  -0.2949 S33:   0.0944                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   574        D   628                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.2464 -14.6548  -5.7228              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4281 T22:   0.4388                                     
REMARK   3      T33:   0.1783 T12:   0.0228                                     
REMARK   3      T13:  -0.0539 T23:  -0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8824 L22:   2.5213                                     
REMARK   3      L33:   1.9315 L12:  -0.0001                                     
REMARK   3      L13:  -0.8024 L23:   0.6547                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0028 S12:   0.1611 S13:  -0.5465                       
REMARK   3      S21:  -0.3085 S22:  -0.0385 S23:   0.1445                       
REMARK   3      S31:   0.2366 S32:  -0.2975 S33:   0.0412                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   629        D   651                          
REMARK   3    ORIGIN FOR THE GROUP (A): -52.1687 -33.9190 -17.2652              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3189 T22:   1.1511                                     
REMARK   3      T33:   1.3305 T12:  -0.2578                                     
REMARK   3      T13:   0.0650 T23:  -0.2015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0050 L22:   4.1442                                     
REMARK   3      L33:  -0.0364 L12:  -2.7216                                     
REMARK   3      L13:   1.6544 L23:  -1.8016                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4174 S12:   0.5634 S13:  -0.4214                       
REMARK   3      S21:  -0.9557 S22:  -0.4280 S23:   0.3093                       
REMARK   3      S31:   0.3572 S32:   0.2160 S33:   0.0106                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   652        D   708                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.3478 -25.4147  -9.7066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5731 T22:   0.4221                                     
REMARK   3      T33:   0.2991 T12:  -0.0607                                     
REMARK   3      T13:  -0.0939 T23:  -0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0627 L22:   5.2135                                     
REMARK   3      L33:   3.1695 L12:  -3.1135                                     
REMARK   3      L13:  -0.6817 L23:   3.1972                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2615 S12:   0.0994 S13:  -0.9589                       
REMARK   3      S21:  -0.1153 S22:  -0.2911 S23:   0.7866                       
REMARK   3      S31:   0.3484 S32:  -0.3977 S33:   0.0295                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   709        D   743                          
REMARK   3    ORIGIN FOR THE GROUP (A): -49.4831 -16.7788  13.2936              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4295 T22:   0.6998                                     
REMARK   3      T33:   0.5950 T12:   0.2640                                     
REMARK   3      T13:  -0.1042 T23:   0.2408                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.3035 L22:  25.3438                                     
REMARK   3      L33:  17.7046 L12:  -2.2356                                     
REMARK   3      L13:   4.9880 L23:  17.3934                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.8868 S12:  -1.8958 S13:  -0.2814                       
REMARK   3      S21:   1.0951 S22:   2.1743 S23:  -1.4618                       
REMARK   3      S31:  -0.5134 S32:   0.7941 S33:  -0.2875                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   744        D   763                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.1383  -9.8032   4.9597              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3922 T22:   0.4858                                     
REMARK   3      T33:   0.1003 T12:  -0.1223                                     
REMARK   3      T13:   0.1308 T23:   0.0355                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4105 L22:  12.4714                                     
REMARK   3      L33:   4.7510 L12:  -6.3314                                     
REMARK   3      L13:   4.4395 L23:  -1.9665                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3254 S12:  -1.1149 S13:  -0.1253                       
REMARK   3      S21:   0.2734 S22:   0.3133 S23:   0.2993                       
REMARK   3      S31:   0.0410 S32:  -0.2731 S33:   0.0121                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   764        D   852                          
REMARK   3    ORIGIN FOR THE GROUP (A): -63.9043   9.9587  -9.9890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4211 T22:   0.4866                                     
REMARK   3      T33:   0.3816 T12:  -0.0237                                     
REMARK   3      T13:  -0.0309 T23:  -0.0719                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1978 L22:   3.5899                                     
REMARK   3      L33:   4.8366 L12:  -2.5766                                     
REMARK   3      L13:   1.2123 L23:  -2.5563                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0174 S12:   0.0076 S13:   0.2812                       
REMARK   3      S21:  -0.1147 S22:  -0.1510 S23:  -0.3097                       
REMARK   3      S31:  -0.2328 S32:  -0.1105 S33:   0.1336                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   4                                                                      
REMARK   4 4FD2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000072748.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24567                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CITRIC ACID, ISOPROPANOL, PH 5.0,        
REMARK 280  HANGING DROP, TEMPERATURE 294K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       86.26733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       43.13367            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       64.70050            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       21.56683            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      107.83417            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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 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    ARG A 578      177.75    -58.35                                   
REMARK 500    ALA A 579      -26.42     65.16                                   
REMARK 500    ASN A 585       32.74    -85.23                                   
REMARK 500    THR A 615      143.88   -174.54                                   
REMARK 500    ALA A 618       28.93    -75.58                                   
REMARK 500    ALA A 632      -74.19    -72.02                                   
REMARK 500    VAL A 633      -58.32    -23.41                                   
REMARK 500    ALA A 639       56.40   -101.03                                   
REMARK 500    PRO A 640     -129.95    -95.26                                   
REMARK 500    TYR A 643       93.83    -55.50                                   
REMARK 500    VAL A 644     -145.11     48.45                                   
REMARK 500    ASP A 685      -73.03    -75.53                                   
REMARK 500    LYS A 721      -62.65      7.20                                   
REMARK 500    PRO A 724     -125.13    -96.45                                   
REMARK 500    TYR A 725      -80.61    -55.44                                   
REMARK 500    GLU A 726     -160.94    -79.79                                   
REMARK 500    ARG A 727      -25.34     81.74                                   
REMARK 500    LYS A 759      -18.72    -37.10                                   
REMARK 500    ARG A 851      -93.48    -20.30                                   
REMARK 500    ARG B 578      178.23    -59.58                                   
REMARK 500    ALA B 579      -27.67     64.48                                   
REMARK 500    ASN B 585       39.62    -90.22                                   
REMARK 500    ALA B 618       34.95    -76.36                                   
REMARK 500    ALA B 632      -77.97    -70.71                                   
REMARK 500    VAL B 633      -54.34    -21.68                                   
REMARK 500    PRO B 640     -130.78    -52.48                                   
REMARK 500    PRO B 641     -134.72    -76.46                                   
REMARK 500    VAL B 644     -144.85     54.43                                   
REMARK 500    ASP B 685      -73.42    -75.21                                   
REMARK 500    ASP B 691     -165.12    -74.61                                   
REMARK 500    LYS B 721      -56.48     -7.19                                   
REMARK 500    PRO B 724     -127.39    -92.27                                   
REMARK 500    LYS B 759      -12.23    -42.37                                   
REMARK 500    LEU B 786     -167.31    -76.41                                   
REMARK 500    LEU B 816      -65.11   -106.78                                   
REMARK 500    PRO B 849       47.38    -88.00                                   
REMARK 500    ALA B 850     -129.47     48.95                                   
REMARK 500    ARG B 851      -77.10   -140.88                                   
REMARK 500    ARG D 578      172.45    -59.13                                   
REMARK 500    ALA D 579      -27.56     70.98                                   
REMARK 500    ASN D 585       32.21    -86.15                                   
REMARK 500    PRO D 587      152.99    -47.55                                   
REMARK 500    THR D 615      140.78   -175.03                                   
REMARK 500    ALA D 618       28.84    -75.39                                   
REMARK 500    ALA D 632      -77.58    -72.02                                   
REMARK 500    VAL D 633      -54.61    -21.28                                   
REMARK 500    ALA D 639       57.09    -98.79                                   
REMARK 500    PRO D 640     -135.06    -92.61                                   
REMARK 500    VAL D 644     -146.47     51.47                                   
REMARK 500    ASP D 685      -70.08    -81.49                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 901                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FCT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FCV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FCW   RELATED DB: PDB                                   
DBREF  4FD2 A  545   852  UNP    Q9RA63   CLPB_THET8     545    852             
DBREF  4FD2 B  545   852  UNP    Q9RA63   CLPB_THET8     545    852             
DBREF  4FD2 D  545   852  UNP    Q9RA63   CLPB_THET8     545    852             
SEQADV 4FD2 ALA A  668  UNP  Q9RA63    GLU   668 ENGINEERED MUTATION            
SEQADV 4FD2 ALA B  668  UNP  Q9RA63    GLU   668 ENGINEERED MUTATION            
SEQADV 4FD2 ALA D  668  UNP  Q9RA63    GLU   668 ENGINEERED MUTATION            
SEQRES   1 A  308  GLU ARG GLU LYS LEU LEU ARG LEU GLU GLU GLU LEU HIS          
SEQRES   2 A  308  LYS ARG VAL VAL GLY GLN ASP GLU ALA ILE ARG ALA VAL          
SEQRES   3 A  308  ALA ASP ALA ILE ARG ARG ALA ARG ALA GLY LEU LYS ASP          
SEQRES   4 A  308  PRO ASN ARG PRO ILE GLY SER PHE LEU PHE LEU GLY PRO          
SEQRES   5 A  308  THR GLY VAL GLY LYS THR GLU LEU ALA LYS THR LEU ALA          
SEQRES   6 A  308  ALA THR LEU PHE ASP THR GLU GLU ALA MET ILE ARG ILE          
SEQRES   7 A  308  ASP MET THR GLU TYR MET GLU LYS HIS ALA VAL SER ARG          
SEQRES   8 A  308  LEU ILE GLY ALA PRO PRO GLY TYR VAL GLY TYR GLU GLU          
SEQRES   9 A  308  GLY GLY GLN LEU THR GLU ALA VAL ARG ARG ARG PRO TYR          
SEQRES  10 A  308  SER VAL ILE LEU PHE ASP ALA ILE GLU LYS ALA HIS PRO          
SEQRES  11 A  308  ASP VAL PHE ASN ILE LEU LEU GLN ILE LEU ASP ASP GLY          
SEQRES  12 A  308  ARG LEU THR ASP SER HIS GLY ARG THR VAL ASP PHE ARG          
SEQRES  13 A  308  ASN THR VAL ILE ILE LEU THR SER ASN LEU GLY SER PRO          
SEQRES  14 A  308  LEU ILE LEU GLU GLY LEU GLN LYS GLY TRP PRO TYR GLU          
SEQRES  15 A  308  ARG ILE ARG ASP GLU VAL PHE LYS VAL LEU GLN GLN HIS          
SEQRES  16 A  308  PHE ARG PRO GLU PHE LEU ASN ARG LEU ASP GLU ILE VAL          
SEQRES  17 A  308  VAL PHE ARG PRO LEU THR LYS GLU GLN ILE ARG GLN ILE          
SEQRES  18 A  308  VAL GLU ILE GLN LEU SER TYR LEU ARG ALA ARG LEU ALA          
SEQRES  19 A  308  GLU LYS ARG ILE SER LEU GLU LEU THR GLU ALA ALA LYS          
SEQRES  20 A  308  ASP PHE LEU ALA GLU ARG GLY TYR ASP PRO VAL PHE GLY          
SEQRES  21 A  308  ALA ARG PRO LEU ARG ARG VAL ILE GLN ARG GLU LEU GLU          
SEQRES  22 A  308  THR PRO LEU ALA GLN LYS ILE LEU ALA GLY GLU VAL LYS          
SEQRES  23 A  308  GLU GLY ASP ARG VAL GLN VAL ASP VAL GLY PRO ALA GLY          
SEQRES  24 A  308  LEU VAL PHE ALA VAL PRO ALA ARG VAL                          
SEQRES   1 B  308  GLU ARG GLU LYS LEU LEU ARG LEU GLU GLU GLU LEU HIS          
SEQRES   2 B  308  LYS ARG VAL VAL GLY GLN ASP GLU ALA ILE ARG ALA VAL          
SEQRES   3 B  308  ALA ASP ALA ILE ARG ARG ALA ARG ALA GLY LEU LYS ASP          
SEQRES   4 B  308  PRO ASN ARG PRO ILE GLY SER PHE LEU PHE LEU GLY PRO          
SEQRES   5 B  308  THR GLY VAL GLY LYS THR GLU LEU ALA LYS THR LEU ALA          
SEQRES   6 B  308  ALA THR LEU PHE ASP THR GLU GLU ALA MET ILE ARG ILE          
SEQRES   7 B  308  ASP MET THR GLU TYR MET GLU LYS HIS ALA VAL SER ARG          
SEQRES   8 B  308  LEU ILE GLY ALA PRO PRO GLY TYR VAL GLY TYR GLU GLU          
SEQRES   9 B  308  GLY GLY GLN LEU THR GLU ALA VAL ARG ARG ARG PRO TYR          
SEQRES  10 B  308  SER VAL ILE LEU PHE ASP ALA ILE GLU LYS ALA HIS PRO          
SEQRES  11 B  308  ASP VAL PHE ASN ILE LEU LEU GLN ILE LEU ASP ASP GLY          
SEQRES  12 B  308  ARG LEU THR ASP SER HIS GLY ARG THR VAL ASP PHE ARG          
SEQRES  13 B  308  ASN THR VAL ILE ILE LEU THR SER ASN LEU GLY SER PRO          
SEQRES  14 B  308  LEU ILE LEU GLU GLY LEU GLN LYS GLY TRP PRO TYR GLU          
SEQRES  15 B  308  ARG ILE ARG ASP GLU VAL PHE LYS VAL LEU GLN GLN HIS          
SEQRES  16 B  308  PHE ARG PRO GLU PHE LEU ASN ARG LEU ASP GLU ILE VAL          
SEQRES  17 B  308  VAL PHE ARG PRO LEU THR LYS GLU GLN ILE ARG GLN ILE          
SEQRES  18 B  308  VAL GLU ILE GLN LEU SER TYR LEU ARG ALA ARG LEU ALA          
SEQRES  19 B  308  GLU LYS ARG ILE SER LEU GLU LEU THR GLU ALA ALA LYS          
SEQRES  20 B  308  ASP PHE LEU ALA GLU ARG GLY TYR ASP PRO VAL PHE GLY          
SEQRES  21 B  308  ALA ARG PRO LEU ARG ARG VAL ILE GLN ARG GLU LEU GLU          
SEQRES  22 B  308  THR PRO LEU ALA GLN LYS ILE LEU ALA GLY GLU VAL LYS          
SEQRES  23 B  308  GLU GLY ASP ARG VAL GLN VAL ASP VAL GLY PRO ALA GLY          
SEQRES  24 B  308  LEU VAL PHE ALA VAL PRO ALA ARG VAL                          
SEQRES   1 D  308  GLU ARG GLU LYS LEU LEU ARG LEU GLU GLU GLU LEU HIS          
SEQRES   2 D  308  LYS ARG VAL VAL GLY GLN ASP GLU ALA ILE ARG ALA VAL          
SEQRES   3 D  308  ALA ASP ALA ILE ARG ARG ALA ARG ALA GLY LEU LYS ASP          
SEQRES   4 D  308  PRO ASN ARG PRO ILE GLY SER PHE LEU PHE LEU GLY PRO          
SEQRES   5 D  308  THR GLY VAL GLY LYS THR GLU LEU ALA LYS THR LEU ALA          
SEQRES   6 D  308  ALA THR LEU PHE ASP THR GLU GLU ALA MET ILE ARG ILE          
SEQRES   7 D  308  ASP MET THR GLU TYR MET GLU LYS HIS ALA VAL SER ARG          
SEQRES   8 D  308  LEU ILE GLY ALA PRO PRO GLY TYR VAL GLY TYR GLU GLU          
SEQRES   9 D  308  GLY GLY GLN LEU THR GLU ALA VAL ARG ARG ARG PRO TYR          
SEQRES  10 D  308  SER VAL ILE LEU PHE ASP ALA ILE GLU LYS ALA HIS PRO          
SEQRES  11 D  308  ASP VAL PHE ASN ILE LEU LEU GLN ILE LEU ASP ASP GLY          
SEQRES  12 D  308  ARG LEU THR ASP SER HIS GLY ARG THR VAL ASP PHE ARG          
SEQRES  13 D  308  ASN THR VAL ILE ILE LEU THR SER ASN LEU GLY SER PRO          
SEQRES  14 D  308  LEU ILE LEU GLU GLY LEU GLN LYS GLY TRP PRO TYR GLU          
SEQRES  15 D  308  ARG ILE ARG ASP GLU VAL PHE LYS VAL LEU GLN GLN HIS          
SEQRES  16 D  308  PHE ARG PRO GLU PHE LEU ASN ARG LEU ASP GLU ILE VAL          
SEQRES  17 D  308  VAL PHE ARG PRO LEU THR LYS GLU GLN ILE ARG GLN ILE          
SEQRES  18 D  308  VAL GLU ILE GLN LEU SER TYR LEU ARG ALA ARG LEU ALA          
SEQRES  19 D  308  GLU LYS ARG ILE SER LEU GLU LEU THR GLU ALA ALA LYS          
SEQRES  20 D  308  ASP PHE LEU ALA GLU ARG GLY TYR ASP PRO VAL PHE GLY          
SEQRES  21 D  308  ALA ARG PRO LEU ARG ARG VAL ILE GLN ARG GLU LEU GLU          
SEQRES  22 D  308  THR PRO LEU ALA GLN LYS ILE LEU ALA GLY GLU VAL LYS          
SEQRES  23 D  308  GLU GLY ASP ARG VAL GLN VAL ASP VAL GLY PRO ALA GLY          
SEQRES  24 D  308  LEU VAL PHE ALA VAL PRO ALA ARG VAL                          
HET    ADP  A 901      27                                                       
HET    ADP  B 901      27                                                       
HET    ADP  D 901      27                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   4  ADP    3(C10 H15 N5 O10 P2)                                         
HELIX    1   1 GLU A  545  ARG A  551  1                                   7    
HELIX    2   2 ARG A  551  LYS A  558  1                                   8    
HELIX    3   3 GLN A  563  ARG A  578  1                                  16    
HELIX    4   4 GLY A  600  ASP A  614  1                                  15    
HELIX    5   5 GLU A  629  ILE A  637  1                                   9    
HELIX    6   6 GLY A  650  ARG A  659  1                                  10    
HELIX    7   7 ALA A  668  ALA A  672  5                                   5    
HELIX    8   8 HIS A  673  ASP A  686  1                                  14    
HELIX    9   9 GLY A  711  PRO A  713  5                                   3    
HELIX   10  10 LEU A  714  GLN A  720  1                                   7    
HELIX   11  11 ARG A  727  GLN A  737  1                                  11    
HELIX   12  12 ARG A  741  ASN A  746  1                                   6    
HELIX   13  13 THR A  758  GLU A  779  1                                  22    
HELIX   14  14 THR A  787  TYR A  799  1                                  13    
HELIX   15  15 PRO A  807  LEU A  816  1                                  10    
HELIX   16  16 LEU A  816  ALA A  826  1                                  11    
HELIX   17  17 ARG B  546  ARG B  551  1                                   6    
HELIX   18  18 ARG B  551  LYS B  558  1                                   8    
HELIX   19  19 GLN B  563  ARG B  578  1                                  16    
HELIX   20  20 ALA B  579  LEU B  581  5                                   3    
HELIX   21  21 GLY B  600  ASP B  614  1                                  15    
HELIX   22  22 THR B  625  TYR B  627  5                                   3    
HELIX   23  23 ALA B  632  ILE B  637  1                                   6    
HELIX   24  24 GLY B  650  ARG B  659  1                                  10    
HELIX   25  25 ALA B  668  ALA B  672  5                                   5    
HELIX   26  26 HIS B  673  ASP B  686  1                                  14    
HELIX   27  27 GLY B  711  PRO B  713  5                                   3    
HELIX   28  28 LEU B  714  LEU B  719  1                                   6    
HELIX   29  29 GLU B  726  GLN B  737  1                                  12    
HELIX   30  30 ARG B  741  ASN B  746  1                                   6    
HELIX   31  31 GLU B  760  GLU B  779  1                                  20    
HELIX   32  32 THR B  787  TYR B  799  1                                  13    
HELIX   33  33 PRO B  807  LEU B  816  1                                  10    
HELIX   34  34 LEU B  816  ALA B  826  1                                  11    
HELIX   35  35 ARG D  546  ARG D  551  1                                   6    
HELIX   36  36 ARG D  551  LYS D  558  1                                   8    
HELIX   37  37 GLN D  563  ARG D  578  1                                  16    
HELIX   38  38 GLY D  600  ASP D  614  1                                  15    
HELIX   39  39 THR D  625  TYR D  627  5                                   3    
HELIX   40  40 GLU D  629  ILE D  637  1                                   9    
HELIX   41  41 GLY D  650  ARG D  659  1                                  10    
HELIX   42  42 ALA D  668  ALA D  672  5                                   5    
HELIX   43  43 HIS D  673  ASP D  686  1                                  14    
HELIX   44  44 GLY D  711  ILE D  715  5                                   5    
HELIX   45  45 GLU D  726  GLN D  737  1                                  12    
HELIX   46  46 ARG D  741  ASN D  746  1                                   6    
HELIX   47  47 GLU D  760  GLN D  769  1                                  10    
HELIX   48  48 LEU D  770  GLU D  779  1                                  10    
HELIX   49  49 THR D  787  TYR D  799  1                                  13    
HELIX   50  50 PRO D  807  LEU D  816  1                                  10    
HELIX   51  51 LEU D  816  ALA D  826  1                                  11    
SHEET    1   A 5 MET A 619  ASP A 623  0                                        
SHEET    2   A 5 VAL A 663  ASP A 667  1  O  LEU A 665   N  ILE A 622           
SHEET    3   A 5 VAL A 703  THR A 707  1  O  ILE A 705   N  ILE A 664           
SHEET    4   A 5 GLY A 589  LEU A 594  1  N  GLY A 589   O  ILE A 704           
SHEET    5   A 5 GLU A 750  VAL A 753  1  O  GLU A 750   N  LEU A 592           
SHEET    1   B 2 ARG A 688  THR A 690  0                                        
SHEET    2   B 2 THR A 696  ASP A 698 -1  O  VAL A 697   N  LEU A 689           
SHEET    1   C 3 SER A 783  GLU A 785  0                                        
SHEET    2   C 3 ARG A 834  ASP A 838  1  O  VAL A 835   N  GLU A 785           
SHEET    3   C 3 VAL A 845  ALA A 847 -1  O  VAL A 845   N  ASP A 838           
SHEET    1   D 5 MET B 619  ASP B 623  0                                        
SHEET    2   D 5 VAL B 663  ASP B 667  1  O  LEU B 665   N  ILE B 620           
SHEET    3   D 5 VAL B 703  THR B 707  1  O  VAL B 703   N  ILE B 664           
SHEET    4   D 5 GLY B 589  LEU B 594  1  N  GLY B 589   O  ILE B 704           
SHEET    5   D 5 GLU B 750  VAL B 753  1  O  GLU B 750   N  LEU B 592           
SHEET    1   E 2 ARG B 688  THR B 690  0                                        
SHEET    2   E 2 THR B 696  ASP B 698 -1  O  VAL B 697   N  LEU B 689           
SHEET    1   F 3 SER B 783  GLU B 785  0                                        
SHEET    2   F 3 ARG B 834  ASP B 838  1  O  VAL B 835   N  GLU B 785           
SHEET    3   F 3 VAL B 845  ALA B 847 -1  O  VAL B 845   N  ASP B 838           
SHEET    1   G 5 MET D 619  ASP D 623  0                                        
SHEET    2   G 5 VAL D 663  ASP D 667  1  O  LEU D 665   N  ILE D 620           
SHEET    3   G 5 VAL D 703  THR D 707  1  O  VAL D 703   N  ILE D 664           
SHEET    4   G 5 GLY D 589  LEU D 594  1  N  GLY D 589   O  ILE D 704           
SHEET    5   G 5 GLU D 750  VAL D 753  1  O  VAL D 752   N  LEU D 592           
SHEET    1   H 2 ARG D 688  THR D 690  0                                        
SHEET    2   H 2 THR D 696  ASP D 698 -1  O  VAL D 697   N  LEU D 689           
SHEET    1   I 3 SER D 783  GLU D 785  0                                        
SHEET    2   I 3 ARG D 834  ASP D 838  1  O  VAL D 835   N  GLU D 785           
SHEET    3   I 3 VAL D 845  ALA D 847 -1  O  VAL D 845   N  ASP D 838           
CISPEP   1 PRO A  640    PRO A  641          0        -2.27                     
CISPEP   2 PRO B  640    PRO B  641          0         2.37                     
CISPEP   3 PRO D  640    PRO D  641          0        -1.28                     
SITE     1 AC1 13 ARG A 559  VAL A 560  VAL A 561  THR A 597                    
SITE     2 AC1 13 GLY A 598  VAL A 599  GLY A 600  LYS A 601                    
SITE     3 AC1 13 THR A 602  GLU A 603  GLN A 769  ALA A 805                    
SITE     4 AC1 13 ARG A 806                                                     
SITE     1 AC2 12 ARG B 559  VAL B 561  THR B 597  GLY B 598                    
SITE     2 AC2 12 VAL B 599  GLY B 600  LYS B 601  THR B 602                    
SITE     3 AC2 12 GLU B 603  ILE B 765  GLN B 769  ALA B 805                    
SITE     1 AC3 12 ARG D 559  VAL D 560  VAL D 561  THR D 597                    
SITE     2 AC3 12 GLY D 598  VAL D 599  GLY D 600  THR D 602                    
SITE     3 AC3 12 GLU D 603  ILE D 765  GLN D 769  ARG D 806                    
CRYST1  129.775  129.775  129.401  90.00  90.00 120.00 P 65         18          
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      0.007706  0.004449  0.000000        0.00000                         
SCALE2      0.000000  0.008898  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007728        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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