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Database: PDB
Entry: 5I4Q
LinkDB: 5I4Q
Original site: 5I4Q 
HEADER    TOXIN/ANTITOXIN                         12-FEB-16   5I4Q              
TITLE     CONTACT-DEPENDENT INHIBITION SYSTEM FROM ESCHERICHIA COLI NC101 -     
TITLE    2 TERNARY CDIA/CDII/EF-TU COMPLEX (DOMAINS 2 AND 3)                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CONTACT-DEPENDENT INHIBITOR A;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: TOXIN DOMAIN;                                              
COMPND   5 SYNONYM: CDIA;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: THE CLONED FRAGMENT CORRESPONDS TO VAL3035-LYS3289 OF 
COMPND   8 THE FULL-LENGTH PROTEIN (CDIA-CT). THE FINAL PURIFIED TERNARY COMPLEX
COMPND   9 WAS TREATED WITH TRYPSIN THAT CLEAVED CDIA-CT AFTER LYS3196.;        
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: CONTACT-DEPENDENT INHIBITOR I;                             
COMPND  12 CHAIN: B;                                                            
COMPND  13 SYNONYM: CDII;                                                       
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: ELONGATION FACTOR TU;                                      
COMPND  17 CHAIN: C;                                                            
COMPND  18 SYNONYM: EF-TU;                                                      
COMPND  19 OTHER_DETAILS: TRYPSIN TREATMENT PRIOR TO CRYSTALLIZATION CLEAVED EF-
COMPND  20 TU AFTER LYS177 OR AFTER ARG172, HOWEVER SUBSEQUENT DIGESTION IN SITU
COMPND  21 CANNOT BE EXCLUDED. THE SAMPLE IS A MIXTURE OF TUFA AND TUFB GENE    
COMPND  22 PRODUCTS (GI 947838, 948482).                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI NC101;                         
SOURCE   3 ORGANISM_TAXID: 753642;                                              
SOURCE   4 STRAIN: NC101;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-GOLD;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PMCSG58;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI NC101;                         
SOURCE  12 ORGANISM_TAXID: 753642;                                              
SOURCE  13 STRAIN: NC101;                                                       
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-GOLD;                            
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PMCSG58;                                  
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  21 ORGANISM_TAXID: 469008                                               
KEYWDS    TOXIN, ANTITOXIN, ELONGATION FACTOR, STRUCTURAL GENOMICS, PSI-        
KEYWDS   2 BIOLOGY, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, STRUCTURE-    
KEYWDS   3 FUNCTION ANALYSIS OF POLYMORPHIC CDI TOXIN-IMMUNITY PROTEIN          
KEYWDS   4 COMPLEXES, UC4CDI, TOXIN-ANTITOXIN COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.MICHALSKA,L.STOLS,W.ESCHENFELDT,C.S.HAYES,C.W.GOULDING,             
AUTHOR   2 A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG),          
AUTHOR   3 STRUCTURE-FUNCTION ANALYSIS OF POLYMORPHIC CDI TOXIN-IMMUNITY        
AUTHOR   4 PROTEIN COMPLEXES (UC4CDI)                                           
REVDAT   4   08-NOV-17 5I4Q    1       JRNL                                     
REVDAT   3   01-NOV-17 5I4Q    1       REMARK                                   
REVDAT   2   20-SEP-17 5I4Q    1       REMARK                                   
REVDAT   1   28-JUN-17 5I4Q    0                                                
JRNL        AUTH   K.MICHALSKA,G.C.GUCINSKI,F.GARZA-SANCHEZ,P.M.JOHNSON,        
JRNL        AUTH 2 L.M.STOLS,W.H.ESCHENFELDT,G.BABNIGG,D.A.LOW,C.W.GOULDING,    
JRNL        AUTH 3 A.JOACHIMIAK,C.S.HAYES                                       
JRNL        TITL   STRUCTURE OF A NOVEL ANTIBACTERIAL TOXIN THAT EXPLOITS       
JRNL        TITL 2 ELONGATION FACTOR TU TO CLEAVE SPECIFIC TRANSFER RNAS.       
JRNL        REF    NUCLEIC ACIDS RES.            V.  45 10306 2017              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   28973472                                                     
JRNL        DOI    10.1093/NAR/GKX700                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 22536                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1125                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1568                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.49                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 66                           
REMARK   3   BIN FREE R VALUE                    : 0.3110                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3061                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 92                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.38000                                              
REMARK   3    B22 (A**2) : 0.38000                                              
REMARK   3    B33 (A**2) : -0.76000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.245         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.195         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.153         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.941        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3134 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3021 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4223 ; 1.633 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6967 ; 1.367 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   378 ; 5.665 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   148 ;33.738 ;23.311       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   549 ;14.744 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;22.626 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   445 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3496 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   716 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1521 ; 3.097 ; 3.234       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1520 ; 3.065 ; 3.233       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1896 ; 4.803 ; 4.832       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1897 ; 4.802 ; 4.834       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1613 ; 4.550 ; 3.817       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1609 ; 4.484 ; 3.798       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2321 ; 7.129 ; 5.424       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3383 ; 9.078 ;25.355       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3369 ; 9.044 ;25.280       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
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   168        A   176                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.6824  46.2286   2.2072              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1637 T22:   0.1863                                     
REMARK   3      T33:   0.2700 T12:   0.0781                                     
REMARK   3      T13:   0.0137 T23:  -0.0253                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5658 L22:   0.9020                                     
REMARK   3      L33:  13.0879 L12:   0.4869                                     
REMARK   3      L13:   2.4968 L23:   1.5629                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0753 S12:  -0.0606 S13:   0.0790                       
REMARK   3      S21:   0.0833 S22:   0.0966 S23:   0.2948                       
REMARK   3      S31:  -0.0653 S32:  -0.5075 S33:  -0.1718                       
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   177        A   195                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.1468  39.8623  11.0969              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1452 T22:   0.2509                                     
REMARK   3      T33:   0.2067 T12:   0.0655                                     
REMARK   3      T13:   0.0077 T23:  -0.1154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1032 L22:   1.8116                                     
REMARK   3      L33:   3.6929 L12:  -1.6581                                     
REMARK   3      L13:  -1.6694 L23:  -1.4546                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1067 S12:  -0.1174 S13:  -0.0048                       
REMARK   3      S21:   0.1619 S22:   0.0963 S23:   0.1053                       
REMARK   3      S31:  -0.3251 S32:  -0.0496 S33:  -0.2030                       
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   196        A   204                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2431  34.7034   5.5807              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1339 T22:   0.3124                                     
REMARK   3      T33:   0.1412 T12:   0.0276                                     
REMARK   3      T13:  -0.0105 T23:  -0.0690                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8108 L22:   1.5616                                     
REMARK   3      L33:   0.1720 L12:  -2.3089                                     
REMARK   3      L13:   0.2987 L23:  -0.4713                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1064 S12:  -0.2670 S13:   0.0090                       
REMARK   3      S21:  -0.1144 S22:   0.1825 S23:   0.1775                       
REMARK   3      S31:   0.0632 S32:  -0.0175 S33:  -0.0761                       
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   205        A   225                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4473  26.1030   8.7946              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1044 T22:   0.3595                                     
REMARK   3      T33:   0.1526 T12:  -0.0137                                     
REMARK   3      T13:  -0.0383 T23:  -0.0408                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8205 L22:   1.1572                                     
REMARK   3      L33:   2.5512 L12:   0.8210                                     
REMARK   3      L13:  -0.0405 L23:  -0.1322                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0068 S12:  -0.3147 S13:   0.3484                       
REMARK   3      S21:  -0.2767 S22:  -0.0854 S23:   0.3204                       
REMARK   3      S31:   0.1501 S32:  -0.1710 S33:   0.0922                       
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   226        A   238                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.8249  25.1294  10.5406              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1115 T22:   0.3946                                     
REMARK   3      T33:   0.1898 T12:  -0.0063                                     
REMARK   3      T13:  -0.0154 T23:  -0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1074 L22:   0.0099                                     
REMARK   3      L33:   6.9716 L12:   0.0141                                     
REMARK   3      L13:  -0.5411 L23:  -0.0911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0168 S12:  -0.1229 S13:  -0.0627                       
REMARK   3      S21:  -0.0266 S22:  -0.0194 S23:   0.0045                       
REMARK   3      S31:  -0.0941 S32:  -0.1024 S33:   0.0025                       
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   239        A   255                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.9296  26.6910  11.0530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2653 T22:   0.5544                                     
REMARK   3      T33:   0.0584 T12:  -0.1666                                     
REMARK   3      T13:   0.0053 T23:  -0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7646 L22:   1.8749                                     
REMARK   3      L33:   1.5757 L12:  -1.1379                                     
REMARK   3      L13:  -1.4372 L23:   1.4553                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2006 S12:  -0.2594 S13:   0.0484                       
REMARK   3      S21:   0.0222 S22:  -0.1518 S23:  -0.1359                       
REMARK   3      S31:   0.1977 S32:  -0.3472 S33:  -0.0488                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    12                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.2445  21.1998 -11.4942              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2362 T22:   0.1251                                     
REMARK   3      T33:   0.1649 T12:   0.0065                                     
REMARK   3      T13:   0.0296 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8353 L22:   0.5829                                     
REMARK   3      L33:  10.8581 L12:  -1.2777                                     
REMARK   3      L13:  -1.1149 L23:   0.6463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0095 S12:   0.0291 S13:  -0.0524                       
REMARK   3      S21:  -0.0413 S22:  -0.0181 S23:   0.0170                       
REMARK   3      S31:  -0.3161 S32:   0.2396 S33:   0.0086                       
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    13        B    28                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.0373  19.9938   8.3476              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2471 T22:   0.3382                                     
REMARK   3      T33:   0.1072 T12:   0.0903                                     
REMARK   3      T13:   0.0097 T23:   0.0148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9609 L22:   0.3067                                     
REMARK   3      L33:   7.8157 L12:  -1.1478                                     
REMARK   3      L13:  -6.2107 L23:   1.4353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0781 S12:  -0.4222 S13:   0.0168                       
REMARK   3      S21:  -0.0705 S22:   0.1042 S23:  -0.0237                       
REMARK   3      S31:   0.0427 S32:   0.4207 S33:  -0.0261                       
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    29        B    56                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.3310  24.2188  27.8988              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1198 T22:   0.4811                                     
REMARK   3      T33:   0.0104 T12:  -0.0370                                     
REMARK   3      T13:  -0.0262 T23:  -0.0188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3475 L22:   0.6509                                     
REMARK   3      L33:   3.4339 L12:  -0.9799                                     
REMARK   3      L13:  -1.3403 L23:  -0.2315                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0407 S12:  -0.2325 S13:   0.0833                       
REMARK   3      S21:  -0.0117 S22:  -0.0033 S23:  -0.0398                       
REMARK   3      S31:  -0.0170 S32:   0.2600 S33:  -0.0373                       
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    57        B    90                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.3966  23.0993  12.9241              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1446 T22:   0.3712                                     
REMARK   3      T33:   0.0929 T12:   0.0286                                     
REMARK   3      T13:   0.0182 T23:  -0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9638 L22:   0.4668                                     
REMARK   3      L33:   1.2165 L12:  -0.0840                                     
REMARK   3      L13:  -1.6983 L23:   0.3242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0430 S12:  -0.1364 S13:  -0.1236                       
REMARK   3      S21:  -0.0122 S22:  -0.0330 S23:  -0.0808                       
REMARK   3      S31:   0.0842 S32:  -0.0563 S33:   0.0760                       
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    91        B   107                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.6714  17.9677  26.1211              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1452 T22:   0.3265                                     
REMARK   3      T33:   0.1050 T12:  -0.0392                                     
REMARK   3      T13:   0.0151 T23:   0.0242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1827 L22:   2.0522                                     
REMARK   3      L33:   6.4410 L12:  -2.9717                                     
REMARK   3      L13:   0.9059 L23:  -2.6551                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0002 S12:  -0.2635 S13:  -0.7079                       
REMARK   3      S21:  -0.2027 S22:   0.1709 S23:   0.3201                       
REMARK   3      S31:   0.5460 S32:  -0.2607 S33:  -0.1707                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   209        C   299                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.7924  36.3998  -9.4330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1527 T22:   0.2252                                     
REMARK   3      T33:   0.1811 T12:   0.0101                                     
REMARK   3      T13:  -0.0642 T23:  -0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4064 L22:   0.9684                                     
REMARK   3      L33:   2.0362 L12:  -0.4969                                     
REMARK   3      L13:  -1.0537 L23:   0.2019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0635 S12:   0.1322 S13:   0.2207                       
REMARK   3      S21:  -0.0084 S22:   0.0980 S23:   0.0664                       
REMARK   3      S31:   0.1259 S32:  -0.1263 S33:  -0.0345                       
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 :   C   300        C   369                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.4319  39.3260 -17.5154              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1027 T22:   0.2847                                     
REMARK   3      T33:   0.2373 T12:  -0.0256                                     
REMARK   3      T13:   0.0450 T23:  -0.1682                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3495 L22:   1.7491                                     
REMARK   3      L33:   1.4384 L12:   1.9923                                     
REMARK   3      L13:   0.7102 L23:   0.5595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0960 S12:   0.2947 S13:  -0.2021                       
REMARK   3      S21:  -0.1055 S22:   0.3811 S23:  -0.2451                       
REMARK   3      S31:   0.0613 S32:   0.0759 S33:  -0.2851                       
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 :   C   370        C   394                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.8950  42.3388 -15.7759              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0670 T22:   0.1328                                     
REMARK   3      T33:   0.2549 T12:  -0.0474                                     
REMARK   3      T13:   0.0372 T23:  -0.0785                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1823 L22:   3.1540                                     
REMARK   3      L33:   0.9778 L12:  -0.0911                                     
REMARK   3      L13:  -0.3092 L23:  -0.3201                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0508 S12:  -0.1186 S13:   0.5463                       
REMARK   3      S21:  -0.1182 S22:   0.3745 S23:  -0.1432                       
REMARK   3      S31:  -0.0636 S32:   0.0635 S33:  -0.3237                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 5I4Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218255.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : 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) : 0.97929                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23688                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.100                              
REMARK 200  R MERGE                    (I) : 0.12500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.95300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: HKL-3000                                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NACL, 0.1 M BIS-TRIS PH 6.5, 1.5   
REMARK 280  M AMMONIUM SULFATE, TRYPSIN 40 NG/MICROL, CRYO 28% SUCROSE,         
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2                         
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+1/2,X+1/2,Z                                          
REMARK 290       4555   Y+1/2,-X+1/2,Z                                          
REMARK 290       5555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       6555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       65.57750            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       65.57750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       65.57750            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       65.57750            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       65.57750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.57750            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       65.57750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.57750            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: HEXAMER ACCORDING TO SIZE EXCLUSION CHROMATOGRAPHY           
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A   164                                                      
REMARK 465     SER A   165                                                      
REMARK 465     TYR A   166                                                      
REMARK 465     LEU A   167                                                      
REMARK 465     GLY B   108                                                      
REMARK 465     HIS B   109                                                      
REMARK 465     HIS B   110                                                      
REMARK 465     HIS B   111                                                      
REMARK 465     HIS B   112                                                      
REMARK 465     HIS B   113                                                      
REMARK 465     HIS B   114                                                      
REMARK 465     ALA C   178                                                      
REMARK 465     LEU C   179                                                      
REMARK 465     GLU C   180                                                      
REMARK 465     GLY C   181                                                      
REMARK 465     ASP C   182                                                      
REMARK 465     ALA C   183                                                      
REMARK 465     GLU C   184                                                      
REMARK 465     TRP C   185                                                      
REMARK 465     GLU C   186                                                      
REMARK 465     ALA C   187                                                      
REMARK 465     LYS C   188                                                      
REMARK 465     ILE C   189                                                      
REMARK 465     LEU C   190                                                      
REMARK 465     GLU C   191                                                      
REMARK 465     LEU C   192                                                      
REMARK 465     ALA C   193                                                      
REMARK 465     GLY C   194                                                      
REMARK 465     PHE C   195                                                      
REMARK 465     LEU C   196                                                      
REMARK 465     ASP C   197                                                      
REMARK 465     SER C   198                                                      
REMARK 465     TYR C   199                                                      
REMARK 465     ILE C   200                                                      
REMARK 465     PRO C   201                                                      
REMARK 465     GLU C   202                                                      
REMARK 465     PRO C   203                                                      
REMARK 465     GLU C   204                                                      
REMARK 465     ARG C   205                                                      
REMARK 465     ALA C   206                                                      
REMARK 465     ILE C   207                                                      
REMARK 465     ASP C   208                                                      
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     MSE B   1    CG  SE    CE                                        
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    VAL A 182      141.39   -173.71                                   
REMARK 500    ARG A 200       68.30   -120.00                                   
REMARK 500    ILE C 248      -59.42     59.28                                   
REMARK 500    ARG C 263       -0.87     69.37                                   
REMARK 500    ARG C 334      -75.71     67.01                                   
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 CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: MCSG-CPX200205   RELATED DB: TARGETTRACK                 
REMARK 900 RELATED ID: MCSG-APC111455   RELATED DB: TARGETTRACK                 
REMARK 900 RELATED ID: MCSG-APC111472   RELATED DB: TARGETTRACK                 
DBREF  5I4Q A  164   255  PDB    5I4Q     5I4Q           164    255             
DBREF  5I4Q B    1   114  PDB    5I4Q     5I4Q             1    114             
DBREF  5I4Q C  178   394  UNP    J7R9V6   J7R9V6_ECOLX   193    409             
SEQRES   1 A   92  LEU SER TYR LEU GLY ILE GLY LYS LYS ILE SER PHE ASP          
SEQRES   2 A   92  GLY ASP PHE TYR THR VAL ASP GLY MSE LYS PHE SER LYS          
SEQRES   3 A   92  SER TYR TYR GLU LYS LEU TRP GLU GLN GLY ARG PRO ALA          
SEQRES   4 A   92  PRO PHE VAL GLN ALA ARG GLU VAL LEU ASN SER ASN PRO          
SEQRES   5 A   92  LYS ILE GLU PRO ASP PRO ARG GLY ALA PRO GLY TYR LEU          
SEQRES   6 A   92  ARG TYR GLU GLY ALA GLY LEU GLU MSE ILE TYR ASN PRO          
SEQRES   7 A   92  LYS THR GLY GLN VAL GLY HIS ILE GLN PRO VAL LYS VAL          
SEQRES   8 A   92  LYS                                                          
SEQRES   1 B  114  MSE ASP ILE TRP PRO GLU PHE GLN ARG ASP LEU GLU MSE          
SEQRES   2 B  114  TYR ARG ASP VAL VAL LEU SER ILE LYS ARG ASN LEU ARG          
SEQRES   3 B  114  LEU TYR GLU GLU CYS ILE GLU SER LEU VAL HIS GLN ILE          
SEQRES   4 B  114  GLY SER THR ASN PHE ASP ASN ALA GLN PRO LEU PHE ASP          
SEQRES   5 B  114  ASP LEU PHE ARG MSE GLN SER GLU LEU ALA THR MSE LEU          
SEQRES   6 B  114  TYR LYS TYR GLU TYR LYS PRO GLY LYS ARG ILE GLN ASP          
SEQRES   7 B  114  LEU ILE TYR HIS LEU ASP ARG ASP ASP PHE TYR SER ARG          
SEQRES   8 B  114  LYS TYR TRP HIS LYS LYS PHE SER ASP GLY LEU ALA TRP          
SEQRES   9 B  114  PRO GLU ALA GLY HIS HIS HIS HIS HIS HIS                      
SEQRES   1 C  217  ALA LEU GLU GLY ASP ALA GLU TRP GLU ALA LYS ILE LEU          
SEQRES   2 C  217  GLU LEU ALA GLY PHE LEU ASP SER TYR ILE PRO GLU PRO          
SEQRES   3 C  217  GLU ARG ALA ILE ASP LYS PRO PHE LEU LEU PRO ILE GLU          
SEQRES   4 C  217  ASP VAL PHE SER ILE SER GLY ARG GLY THR VAL VAL THR          
SEQRES   5 C  217  GLY ARG VAL GLU ARG GLY ILE ILE LYS VAL GLY GLU GLU          
SEQRES   6 C  217  VAL GLU ILE VAL GLY ILE LYS GLU THR GLN LYS SER THR          
SEQRES   7 C  217  CYS THR GLY VAL GLU MET PHE ARG LYS LEU LEU ASP GLU          
SEQRES   8 C  217  GLY ARG ALA GLY GLU ASN VAL GLY VAL LEU LEU ARG GLY          
SEQRES   9 C  217  ILE LYS ARG GLU GLU ILE GLU ARG GLY GLN VAL LEU ALA          
SEQRES  10 C  217  LYS PRO GLY THR ILE LYS PRO HIS THR LYS PHE GLU SER          
SEQRES  11 C  217  GLU VAL TYR ILE LEU SER LYS ASP GLU GLY GLY ARG HIS          
SEQRES  12 C  217  THR PRO PHE PHE LYS GLY TYR ARG PRO GLN PHE TYR PHE          
SEQRES  13 C  217  ARG THR THR ASP VAL THR GLY THR ILE GLU LEU PRO GLU          
SEQRES  14 C  217  GLY VAL GLU MET VAL MET PRO GLY ASP ASN ILE LYS MET          
SEQRES  15 C  217  VAL VAL THR LEU ILE HIS PRO ILE ALA MET ASP ASP GLY          
SEQRES  16 C  217  LEU ARG PHE ALA ILE ARG GLU GLY GLY ARG THR VAL GLY          
SEQRES  17 C  217  ALA GLY VAL VAL ALA LYS VAL LEU GLY                          
HET    MSE  A 185       8                                                       
HET    MSE  A 237       8                                                       
HET    MSE  B   1       5                                                       
HET    MSE  B  13       8                                                       
HET    MSE  B  57       8                                                       
HET    MSE  B  64       8                                                       
HET     CL  A 301       1                                                       
HET    SO4  C 401       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CL CHLORIDE ION                                                     
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   4   CL    CL 1-                                                        
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   6  HOH   *92(H2 O)                                                     
HELIX    1 AA1 LYS A  189  GLN A  198  1                                  10    
HELIX    2 AA2 ALA A  202  ASN A  212  1                                  11    
HELIX    3 AA3 ILE B    3  SER B   41  1                                  39    
HELIX    4 AA4 ASN B   43  LYS B   67  1                                  25    
HELIX    5 AA5 GLY B   73  LEU B   83  1                                  11    
HELIX    6 AA6 ASP B   87  ASP B  100  1                                  14    
HELIX    7 AA7 LYS C  283  ILE C  287  5                                   5    
HELIX    8 AA8 SER C  313  GLY C  317  5                                   5    
SHEET    1 AA1 6 LYS A 171  LYS A 172  0                                        
SHEET    2 AA1 6 LEU C 265  LEU C 266 -1  O  LEU C 266   N  LYS A 171           
SHEET    3 AA1 6 GLN C 252  MET C 261 -1  N  MET C 261   O  LEU C 265           
SHEET    4 AA1 6 GLU C 242  VAL C 246 -1  N  VAL C 243   O  SER C 254           
SHEET    5 AA1 6 VAL C 292  ALA C 294 -1  O  ALA C 294   N  GLU C 244           
SHEET    6 AA1 6 LEU C 212  PRO C 214 -1  N  LEU C 213   O  LEU C 293           
SHEET    1 AA2 6 LYS A 171  LYS A 172  0                                        
SHEET    2 AA2 6 LEU C 265  LEU C 266 -1  O  LEU C 266   N  LYS A 171           
SHEET    3 AA2 6 GLN C 252  MET C 261 -1  N  MET C 261   O  LEU C 265           
SHEET    4 AA2 6 ASN C 274  LEU C 279 -1  O  LEU C 278   N  GLY C 258           
SHEET    5 AA2 6 GLY C 225  ARG C 231 -1  N  THR C 226   O  LEU C 279           
SHEET    6 AA2 6 ASP C 217  ILE C 221 -1  N  PHE C 219   O  VAL C 227           
SHEET    1 AA3 3 SER A 174  PHE A 175  0                                        
SHEET    2 AA3 3 PHE A 179  VAL A 182 -1  O  THR A 181   N  SER A 174           
SHEET    3 AA3 3 MSE A 185  SER A 188 -1  O  PHE A 187   N  TYR A 180           
SHEET    1 AA4 4 LYS A 216  PRO A 219  0                                        
SHEET    2 AA4 4 LEU A 228  GLY A 232 -1  O  ARG A 229   N  GLU A 218           
SHEET    3 AA4 4 LEU A 235  ASN A 240 -1  O  MSE A 237   N  TYR A 230           
SHEET    4 AA4 4 GLN A 245  PRO A 251 -1  O  HIS A 248   N  ILE A 238           
SHEET    1 AA5 2 ILE C 236  LYS C 238  0                                        
SHEET    2 AA5 2 GLU C 268  ARG C 270 -1  O  GLY C 269   N  ILE C 237           
SHEET    1 AA6 7 LYS C 300  ILE C 311  0                                        
SHEET    2 AA6 7 ASN C 356  MET C 369 -1  O  LEU C 363   N  THR C 303           
SHEET    3 AA6 7 THR C 336  GLU C 343 -1  N  THR C 341   O  THR C 362           
SHEET    4 AA6 7 GLN C 330  PHE C 333 -1  N  PHE C 331   O  VAL C 338           
SHEET    5 AA6 7 ARG C 374  GLU C 379 -1  O  ARG C 378   N  GLN C 330           
SHEET    6 AA6 7 ARG C 382  GLY C 394 -1  O  GLY C 387   N  PHE C 375           
SHEET    7 AA6 7 LYS C 300  ILE C 311 -1  N  GLU C 306   O  ALA C 390           
LINK         C   GLY A 184                 N   MSE A 185     1555   1555  1.34  
LINK         C   MSE A 185                 N   LYS A 186     1555   1555  1.33  
LINK         C   GLU A 236                 N   MSE A 237     1555   1555  1.32  
LINK         C   MSE A 237                 N   ILE A 238     1555   1555  1.32  
LINK         C   MSE B   1                 N   ASP B   2     1555   1555  1.34  
LINK         C   GLU B  12                 N   MSE B  13     1555   1555  1.33  
LINK         C   MSE B  13                 N   TYR B  14     1555   1555  1.33  
LINK         C   ARG B  56                 N   MSE B  57     1555   1555  1.32  
LINK         C   MSE B  57                 N   GLN B  58     1555   1555  1.32  
LINK         C   THR B  63                 N   MSE B  64     1555   1555  1.32  
LINK         C   MSE B  64                 N   LEU B  65     1555   1555  1.33  
SITE     1 AC1  1 ALA A 233                                                     
SITE     1 AC2  2 TYR C 327  HOH C 511                                          
CRYST1  131.155  131.155   63.327  90.00  90.00  90.00 P 4 21 2      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007625  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007625  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015791        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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