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Database: PDB
Entry: 2IX1
LinkDB: 2IX1
Original site: 2IX1 
HEADER    HYDROLASE                               05-JUL-06   2IX1              
TITLE     RNASE II D209N MUTANT                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EXORIBONUCLEASE 2;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 6-644;                                            
COMPND   5 SYNONYM: RNASE II D209N MUTANT, EXORIBONUCLEASE II, RIBONUCLEASE II, 
COMPND   6 RNASE II;                                                            
COMPND   7 EC: 3.1.13.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: 5'-D(*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP *AP*AP*A)-3';          
COMPND  12 CHAIN: B;                                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: CHAIN B CONSISTS OF A 13 NUCLEOTIDE RNA FRAGMENT      
COMPND  15 TRAPPED BY THE INACTIVE RNASE II D209N MUTANT DURING PURIFICATION. IT
COMPND  16 WAS PUTATIVELY MODELLED AS A POLY-ADENINE OLIGONUCLEOTIDE.           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 STRAIN: C600;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET;                                       
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES                                                       
KEYWDS    S1, RNA, CSD, RNB, NUCLEASE, RNASE II, HYDROLASE, RNA- BINDING,       
KEYWDS   2 EXONUCLEASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.FRAZAO,C.E.MCVEY,M.AMBLAR,A.BARBAS,C.VONRHEIN,C.M.ARRAIANO,         
AUTHOR   2 M.A.CARRONDO                                                         
REVDAT   5   08-MAY-19 2IX1    1       REMARK                                   
REVDAT   4   06-MAR-19 2IX1    1       REMARK                                   
REVDAT   3   13-JUL-11 2IX1    1       VERSN                                    
REVDAT   2   24-FEB-09 2IX1    1       VERSN                                    
REVDAT   1   05-OCT-06 2IX1    0                                                
JRNL        AUTH   C.FRAZAO,C.E.MCVEY,M.AMBLAR,A.BARBAS,C.VONRHEIN,             
JRNL        AUTH 2 C.M.ARRAIANO,M.A.CARRONDO                                    
JRNL        TITL   UNRAVELLING THE DYNAMICS OF RNA DEGRADATION BY RIBONUCLEASE  
JRNL        TITL 2 II AND ITS RNA-BOUND COMPLEX                                 
JRNL        REF    NATURE                        V. 443   110 2006              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   16957732                                                     
JRNL        DOI    10.1038/NATURE05080                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.E.MCVEY,M.AMBLAR,A.BARBAS,F.CAIRRAO,R.COELHO,C.ROMAO,      
REMARK   1  AUTH 2 C.M.ARRAIANO,M.A.CARRONDO,C.FRAZAO                           
REMARK   1  TITL   EXPRESSION, PURIFICATION, CRYSTALLIZATION AND PRELIMINARY    
REMARK   1  TITL 2 DIFFRACTION DATA CHARACTERIZATION OF ESCHERICHIA COLI        
REMARK   1  TITL 3 RIBONUCLEASE II (RNASE II)                                   
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  62   684 2006              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   16820694                                                     
REMARK   1  DOI    10.1107/S1744309106021506                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.AMBLAR,A.BARBAS,A.M.FIALHO,C.M.ARRAIANO                    
REMARK   1  TITL   CHARACTERIZATION OF THE FUNCTIONAL DOMAINS OF ESCHERICHIA    
REMARK   1  TITL 2 COLI RNASE II.                                               
REMARK   1  REF    J.MOL.BIOL.                   V. 360   921 2006              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   16806266                                                     
REMARK   1  DOI    10.1016/J.JMB.2006.05.043                                    
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   R.ZILHAO,L.CAMELO,C.M.ARRAIANO                               
REMARK   1  TITL   DNA SEQUENCING AND EXPRESSION OF THE GENE RNB ENCODING       
REMARK   1  TITL 2 ESCHERICHIA COLI RIBONUCLEASE II                             
REMARK   1  REF    MOL.MICROBIOL.                V.   8    43 1993              
REMARK   1  REFN                   ISSN 0950-382X                               
REMARK   1  PMID   8497196                                                      
REMARK   1  DOI    10.1111/J.1365-2958.1993.TB01201.X                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.74 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 29091                          
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) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1547                            
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) : 2.74                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.81                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2144                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 99                           
REMARK   3   BIN FREE R VALUE                    : 0.4030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5092                                    
REMARK   3   NUCLEIC ACID ATOMS       : 287                                     
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 48                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.09000                                              
REMARK   3    B12 (A**2) : -0.03000                                             
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): 0.445         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.272         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.217         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.858        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5533 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7559 ; 1.428 ; 2.030       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   642 ; 6.408 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   256 ;35.052 ;23.516       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   910 ;20.332 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    51 ;19.713 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   849 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4124 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2446 ; 0.220 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3690 ; 0.313 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   200 ; 0.134 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    51 ; 0.218 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.092 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3278 ; 2.003 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5174 ; 3.396 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2598 ; 4.874 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2385 ; 7.574 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
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     1        A    21                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.6120  71.6152  12.8406              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2309 T22:   0.0251                                     
REMARK   3      T33:   0.0528 T12:  -0.0671                                     
REMARK   3      T13:  -0.0795 T23:   0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7757 L22:  17.9893                                     
REMARK   3      L33:   4.9508 L12:   2.2610                                     
REMARK   3      L13:   2.3797 L23:   2.8253                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2851 S12:  -0.3981 S13:   0.4120                       
REMARK   3      S21:   1.7131 S22:  -0.0225 S23:  -1.5980                       
REMARK   3      S31:   0.1715 S32:   0.7118 S33:  -0.2626                       
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    22        A    82                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.8443  49.0548  11.6725              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1993 T22:  -0.0273                                     
REMARK   3      T33:   0.0850 T12:  -0.1052                                     
REMARK   3      T13:   0.0377 T23:   0.0730                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2043 L22:   7.0158                                     
REMARK   3      L33:   7.5080 L12:   0.1693                                     
REMARK   3      L13:  -0.9094 L23:  -4.0740                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2245 S12:   0.0650 S13:  -0.1889                       
REMARK   3      S21:  -0.5520 S22:  -0.4543 S23:  -0.2307                       
REMARK   3      S31:   0.4545 S32:   0.2512 S33:   0.2298                       
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    83        A   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8942  39.3641  33.6623              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0835 T22:   0.1318                                     
REMARK   3      T33:   0.0850 T12:  -0.2201                                     
REMARK   3      T13:  -0.0031 T23:   0.1196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1684 L22:   4.1900                                     
REMARK   3      L33:   5.3882 L12:  -0.0946                                     
REMARK   3      L13:   1.0631 L23:  -2.3976                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0159 S12:  -0.2956 S13:   0.1075                       
REMARK   3      S21:   0.3575 S22:  -0.3305 S23:  -0.5522                       
REMARK   3      S31:  -0.7177 S32:   0.8593 S33:   0.3146                       
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   151        A   265                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.0410  18.8587  41.4269              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1043 T22:   0.1005                                     
REMARK   3      T33:   0.1166 T12:   0.0155                                     
REMARK   3      T13:   0.0032 T23:   0.0431                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9691 L22:   1.1661                                     
REMARK   3      L33:   1.5785 L12:   0.7964                                     
REMARK   3      L13:  -0.1320 L23:  -0.1439                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0552 S12:  -0.1281 S13:  -0.0360                       
REMARK   3      S21:   0.0705 S22:  -0.0601 S23:  -0.0159                       
REMARK   3      S31:  -0.0047 S32:  -0.0595 S33:   0.1153                       
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   266        A   358                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.2346   6.8759  33.1064              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0828 T22:   0.0522                                     
REMARK   3      T33:   0.1173 T12:  -0.0758                                     
REMARK   3      T13:   0.0382 T23:   0.0256                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4366 L22:   1.7530                                     
REMARK   3      L33:   3.1328 L12:   0.2113                                     
REMARK   3      L13:   0.2932 L23:   0.0103                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0743 S12:   0.0661 S13:  -0.2137                       
REMARK   3      S21:  -0.1397 S22:   0.0099 S23:   0.0113                       
REMARK   3      S31:   0.4600 S32:  -0.1789 S33:   0.0644                       
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   359        A   382                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9620  10.5093  26.0350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0991 T22:  -0.0199                                     
REMARK   3      T33:   0.2398 T12:  -0.0053                                     
REMARK   3      T13:   0.2015 T23:   0.0493                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.1143 L22:   3.9894                                     
REMARK   3      L33:  10.8133 L12:   2.5932                                     
REMARK   3      L13:   9.2357 L23:   2.9091                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2308 S12:   0.0093 S13:  -1.0479                       
REMARK   3      S21:  -0.2991 S22:   0.0258 S23:  -0.3289                       
REMARK   3      S31:   0.1604 S32:  -0.3587 S33:   0.2050                       
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   383        A   507                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.8520  25.6998  18.9505              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1229 T22:   0.0198                                     
REMARK   3      T33:   0.0921 T12:  -0.0261                                     
REMARK   3      T13:  -0.0511 T23:   0.0211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3638 L22:   0.0993                                     
REMARK   3      L33:   2.9677 L12:  -0.1332                                     
REMARK   3      L13:   0.3153 L23:  -0.4845                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1135 S12:   0.1075 S13:   0.0983                       
REMARK   3      S21:  -0.1295 S22:  -0.0129 S23:   0.0374                       
REMARK   3      S31:  -0.4119 S32:  -0.0372 S33:   0.1264                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   508        A   549                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.0734  29.7436  35.0879              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1867 T22:   0.0427                                     
REMARK   3      T33:   0.1873 T12:   0.0087                                     
REMARK   3      T13:  -0.0368 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8284 L22:   0.8335                                     
REMARK   3      L33:   1.0865 L12:   0.0773                                     
REMARK   3      L13:  -0.7771 L23:  -0.2913                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1710 S12:   0.1172 S13:   0.7030                       
REMARK   3      S21:  -0.0490 S22:  -0.1624 S23:   0.0910                       
REMARK   3      S31:  -0.3719 S32:  -0.1384 S33:  -0.0086                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   550        A   643                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8017  19.4618   8.1427              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0203 T22:   0.1179                                     
REMARK   3      T33:   0.0979 T12:   0.0136                                     
REMARK   3      T13:   0.1212 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5381 L22:   2.1922                                     
REMARK   3      L33:   6.7430 L12:  -0.2312                                     
REMARK   3      L13:   2.0751 L23:  -1.1966                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0742 S12:   0.9020 S13:  -0.0172                       
REMARK   3      S21:  -0.3220 S22:   0.0355 S23:   0.0263                       
REMARK   3      S31:  -0.1004 S32:   0.6479 S33:   0.0387                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. DISORDERED C-TERMINUS WAS NOT MODELLED.                  
REMARK   4                                                                      
REMARK   4 2IX1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-JUL-06.                  
REMARK 100 THE DEPOSITION ID IS D_1290029291.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30737                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.740                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 51.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.200                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS                        
REMARK 200 SOFTWARE USED: SHELXCD, SHELXD, SHELXE, SHARP                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOUR DIFFUSION IN SITTING DROPS WITH   
REMARK 280  1.5 MICRO-L OF PROTEIN SOLUTION, 20 MM TRIS-HCL PH 8, 150 MM        
REMARK 280  NACL, 10% GLYCEROL AND 1 MM DTT, AND 1.5 MICRO-L OF WELL            
REMARK 280  SOLUTION,2.4 M SODIUM MALONATE PH 6.0, AT 293 K, PH 6.00, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP                                             
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      186.16333            
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       93.08167            
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      139.62250            
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       46.54083            
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      232.70417            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASP 209 TO ASN                        
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     ALA A   644                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET A   1   N     MET A   1   CA      0.124                       
REMARK 500    MET A   1   CG    MET A   1   SD      0.226                       
REMARK 500      A B   1   P       A B   1   OP3    -0.124                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 266   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500      A B   2   C3' -  O3' -  P   ANGL. DEV. =   7.9 DEGREES          
REMARK 500      A B   3   C5' -  C4' -  O4' ANGL. DEV. =   5.8 DEGREES          
REMARK 500      A B   5   C1' -  O4' -  C4' ANGL. DEV. =  -4.6 DEGREES          
REMARK 500      A B   5   O4' -  C1' -  N9  ANGL. DEV. =   8.0 DEGREES          
REMARK 500      A B  10   O4' -  C4' -  C3' ANGL. DEV. =  -8.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A   6      -93.93     -7.64                                   
REMARK 500    THR A  84      -94.13   -120.50                                   
REMARK 500    ASN A  94       96.75     22.91                                   
REMARK 500    ARG A  96       79.04   -160.10                                   
REMARK 500    GLU A 181      132.82    176.71                                   
REMARK 500    ASP A 207       78.10   -117.43                                   
REMARK 500    ASP A 269      -73.86   -146.49                                   
REMARK 500    ASN A 297       48.14    -76.08                                   
REMARK 500    ASN A 322       80.24     39.25                                   
REMARK 500    GLU A 329       59.50    -93.58                                   
REMARK 500    SER A 330      133.46    163.43                                   
REMARK 500    ALA A 355     -143.40   -148.35                                   
REMARK 500    LYS A 371       30.70    -91.03                                   
REMARK 500    ARG A 383     -163.62   -105.87                                   
REMARK 500    LYS A 407      -33.28   -130.69                                   
REMARK 500    ARG A 470      -17.30    -43.90                                   
REMARK 500    HIS A 595      -46.00   -145.03                                   
REMARK 500    ALA A 596      -27.60     86.13                                   
REMARK 500    LYS A 613       18.75     58.12                                   
REMARK 500    VAL A 620       87.27    -62.52                                   
REMARK 500    THR A 621      -20.33    159.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA A    4     ASP A    5                 -149.95                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1644  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A B  12   O3'                                                    
REMARK 620 2   A B  13   OP1  61.0                                              
REMARK 620 3 ASP A 201   OD1  98.7 114.4                                        
REMARK 620 4 ASP A 210   OD2  83.0  82.4 161.8                                  
REMARK 620 5 HOH A2011   O    91.3 150.9  76.1  85.8                            
REMARK 620 6 HOH A2013   O   160.2  99.8  93.7  90.0 106.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1644                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2IX0   RELATED DB: PDB                                   
REMARK 900 RNASE II                                                             
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-TERMINAL HIS-TAGGED PROTEIN, WHERE THE FIRST 5 RESIDUES,           
REMARK 999 MFQDN, ARE REPLACED BY MGSSHHHHHHSSGLVPRGSHMLEAD. N-                 
REMARK 999 TERMINUS INVISIBLE IN ELECTRON DENSITY.                              
DBREF  2IX1 A  -19     5  PDB    2IX1     2IX1           -19      5             
DBREF  2IX1 A    6   644  UNP    P30850   RNB_ECOLI        6    644             
DBREF  2IX1 B    1    13  PDB    2IX1     2IX1             1     13             
SEQADV 2IX1 ASN A  209  UNP  P30850    ASP   209 ENGINEERED MUTATION            
SEQRES   1 A  664  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  664  LEU VAL PRO ARG GLY SER HIS MET LEU GLU ALA ASP PRO          
SEQRES   3 A  664  LEU LEU ALA GLN LEU LYS GLN GLN LEU HIS SER GLN THR          
SEQRES   4 A  664  PRO ARG ALA GLU GLY VAL VAL LYS ALA THR GLU LYS GLY          
SEQRES   5 A  664  PHE GLY PHE LEU GLU VAL ASP ALA GLN LYS SER TYR PHE          
SEQRES   6 A  664  ILE PRO PRO PRO GLN MET LYS LYS VAL MET HIS GLY ASP          
SEQRES   7 A  664  ARG ILE ILE ALA VAL ILE HIS SER GLU LYS GLU ARG GLU          
SEQRES   8 A  664  SER ALA GLU PRO GLU GLU LEU VAL GLU PRO PHE LEU THR          
SEQRES   9 A  664  ARG PHE VAL GLY LYS VAL GLN GLY LYS ASN ASP ARG LEU          
SEQRES  10 A  664  ALA ILE VAL PRO ASP HIS PRO LEU LEU LYS ASP ALA ILE          
SEQRES  11 A  664  PRO CYS ARG ALA ALA ARG GLY LEU ASN HIS GLU PHE LYS          
SEQRES  12 A  664  GLU GLY ASP TRP ALA VAL ALA GLU MET ARG ARG HIS PRO          
SEQRES  13 A  664  LEU LYS GLY ASP ARG SER PHE TYR ALA GLU LEU THR GLN          
SEQRES  14 A  664  TYR ILE THR PHE GLY ASP ASP HIS PHE VAL PRO TRP TRP          
SEQRES  15 A  664  VAL THR LEU ALA ARG HIS ASN LEU GLU LYS GLU ALA PRO          
SEQRES  16 A  664  ASP GLY VAL ALA THR GLU MET LEU ASP GLU GLY LEU VAL          
SEQRES  17 A  664  ARG GLU ASP LEU THR ALA LEU ASP PHE VAL THR ILE ASP          
SEQRES  18 A  664  SER ALA SER THR GLU ASP MET ASN ASP ALA LEU PHE ALA          
SEQRES  19 A  664  LYS ALA LEU PRO ASP ASP LYS LEU GLN LEU ILE VAL ALA          
SEQRES  20 A  664  ILE ALA ASP PRO THR ALA TRP ILE ALA GLU GLY SER LYS          
SEQRES  21 A  664  LEU ASP LYS ALA ALA LYS ILE ARG ALA PHE THR ASN TYR          
SEQRES  22 A  664  LEU PRO GLY PHE ASN ILE PRO MET LEU PRO ARG GLU LEU          
SEQRES  23 A  664  SER ASP ASP LEU CYS SER LEU ARG ALA ASN GLU VAL ARG          
SEQRES  24 A  664  PRO VAL LEU ALA CYS ARG MET THR LEU SER ALA ASP GLY          
SEQRES  25 A  664  THR ILE GLU ASP ASN ILE GLU PHE PHE ALA ALA THR ILE          
SEQRES  26 A  664  GLU SER LYS ALA LYS LEU VAL TYR ASP GLN VAL SER ASP          
SEQRES  27 A  664  TRP LEU GLU ASN THR GLY ASP TRP GLN PRO GLU SER GLU          
SEQRES  28 A  664  ALA ILE ALA GLU GLN VAL ARG LEU LEU ALA GLN ILE CYS          
SEQRES  29 A  664  GLN ARG ARG GLY GLU TRP ARG HIS ASN HIS ALA LEU VAL          
SEQRES  30 A  664  PHE LYS ASP ARG PRO ASP TYR ARG PHE ILE LEU GLY GLU          
SEQRES  31 A  664  LYS GLY GLU VAL LEU ASP ILE VAL ALA GLU PRO ARG ARG          
SEQRES  32 A  664  ILE ALA ASN ARG ILE VAL GLU GLU ALA MET ILE ALA ALA          
SEQRES  33 A  664  ASN ILE CYS ALA ALA ARG VAL LEU ARG ASP LYS LEU GLY          
SEQRES  34 A  664  PHE GLY ILE TYR ASN VAL HIS MET GLY PHE ASP PRO ALA          
SEQRES  35 A  664  ASN ALA ASP ALA LEU ALA ALA LEU LEU LYS THR HIS GLY          
SEQRES  36 A  664  LEU HIS VAL ASP ALA GLU GLU VAL LEU THR LEU ASP GLY          
SEQRES  37 A  664  PHE CYS LYS LEU ARG ARG GLU LEU ASP ALA GLN PRO THR          
SEQRES  38 A  664  GLY PHE LEU ASP SER ARG ILE ARG ARG PHE GLN SER PHE          
SEQRES  39 A  664  ALA GLU ILE SER THR GLU PRO GLY PRO HIS PHE GLY LEU          
SEQRES  40 A  664  GLY LEU GLU ALA TYR ALA THR TRP THR SER PRO ILE ARG          
SEQRES  41 A  664  LYS TYR GLY ASP MET ILE ASN HIS ARG LEU LEU LYS ALA          
SEQRES  42 A  664  VAL ILE LYS GLY GLU THR ALA THR ARG PRO GLN ASP GLU          
SEQRES  43 A  664  ILE THR VAL GLN MET ALA GLU ARG ARG ARG LEU ASN ARG          
SEQRES  44 A  664  MET ALA GLU ARG ASP VAL GLY ASP TRP LEU TYR ALA ARG          
SEQRES  45 A  664  PHE LEU LYS ASP LYS ALA GLY THR ASP THR ARG PHE ALA          
SEQRES  46 A  664  ALA GLU ILE VAL ASP ILE SER ARG GLY GLY MET ARG VAL          
SEQRES  47 A  664  ARG LEU VAL ASP ASN GLY ALA ILE ALA PHE ILE PRO ALA          
SEQRES  48 A  664  PRO PHE LEU HIS ALA VAL ARG ASP GLU LEU VAL CYS SER          
SEQRES  49 A  664  GLN GLU ASN GLY THR VAL GLN ILE LYS GLY GLU THR VAL          
SEQRES  50 A  664  TYR LYS VAL THR ASP VAL ILE ASP VAL THR ILE ALA GLU          
SEQRES  51 A  664  VAL ARG MET GLU THR ARG SER ILE ILE ALA ARG PRO VAL          
SEQRES  52 A  664  ALA                                                          
SEQRES   1 B   13    A   A   A   A   A   A   A   A   A   A   A   A   A          
HET     MG  A1644       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  HOH   *48(H2 O)                                                     
HELIX    1   1 LEU A    7  SER A   17  1                                  11    
HELIX    2   2 PRO A   47  LYS A   52  1                                   6    
HELIX    3   3 HIS A  135  GLY A  139  5                                   5    
HELIX    4   4 PHE A  158  HIS A  168  1                                  11    
HELIX    5   5 PRO A  231  TRP A  234  5                                   4    
HELIX    6   6 SER A  239  ARG A  248  1                                  10    
HELIX    7   7 PRO A  263  ASP A  268  1                                   6    
HELIX    8   8 TYR A  313  GLU A  321  1                                   9    
HELIX    9   9 SER A  330  ALA A  355  1                                  26    
HELIX   10  10 ARG A  383  LEU A  408  1                                  26    
HELIX   11  11 ASP A  420  ALA A  422  5                                   3    
HELIX   12  12 ASN A  423  HIS A  434  1                                  12    
HELIX   13  13 GLU A  441  LEU A  444  5                                   4    
HELIX   14  14 THR A  445  ALA A  458  1                                  14    
HELIX   15  15 GLY A  462  ARG A  469  1                                   8    
HELIX   16  16 LYS A  501  GLY A  517  1                                  17    
HELIX   17  17 GLU A  526  LYS A  555  1                                  30    
HELIX   18  18 ASP A  556  ALA A  558  5                                   3    
HELIX   19  19 PRO A  592  HIS A  595  5                                   4    
HELIX   20  20 VAL A  597  ASP A  599  5                                   3    
HELIX   21  21 MET A  633  ARG A  636  5                                   4    
SHEET    1  AA 7 ARG A  21  LYS A  27  0                                        
SHEET    2  AA 7 ARG A  59  SER A  66 -1  O  ILE A  60   N  GLY A  24           
SHEET    3  AA 7 GLU A  71  GLU A  80 -1  O  SER A  72   N  HIS A  65           
SHEET    4  AA 7 LYS A  42  ILE A  46  1  O  PHE A  45   N  ALA A  73           
SHEET    5  AA 7 GLY A  34  ASP A  39 -1  O  GLY A  34   N  ILE A  46           
SHEET    6  AA 7 ARG A  21  LYS A  27 -1  O  VAL A  25   N  GLU A  37           
SHEET    7  AA 7 ARG A  21  LYS A  27  0                                        
SHEET    1  AB 7 ARG A  85  LYS A  93  0                                        
SHEET    2  AB 7 TRP A 127  ARG A 134 -1  O  ALA A 128   N  GLY A  88           
SHEET    3  AB 7 TYR A 144  THR A 152 -1  O  TYR A 144   N  ARG A 133           
SHEET    4  AB 7 ILE A 110  ALA A 114  1  O  PRO A 111   N  ALA A 145           
SHEET    5  AB 7 ARG A  96  PRO A 101 -1  O  LEU A  97   N  CYS A 112           
SHEET    6  AB 7 ARG A  85  LYS A  93 -1  O  LYS A  89   N  VAL A 100           
SHEET    7  AB 7 ARG A  85  LYS A  93  0                                        
SHEET    1  AC 5 GLU A 190  ASP A 191  0                                        
SHEET    2  AC 5 GLU A 299  GLU A 306  1  O  ALA A 302   N  GLU A 190           
SHEET    3  AC 5 VAL A 278  LEU A 288 -1  O  ARG A 279   N  ILE A 305           
SHEET    4  AC 5 LYS A 221  ALA A 229 -1  O  LEU A 222   N  LEU A 288           
SHEET    5  AC 5 ASP A 210  LEU A 217 -1  O  ALA A 211   N  ALA A 227           
SHEET    1  AD 2 THR A 199  ASP A 201  0                                        
SHEET    2  AD 2 LYS A 310  VAL A 312  1  O  LEU A 311   N  ASP A 201           
SHEET    1  AE 2 ASN A 252  LEU A 254  0                                        
SHEET    2  AE 2 PHE A 257  ILE A 259 -1  O  PHE A 257   N  LEU A 254           
SHEET    1  AF 2 ASP A 363  LEU A 368  0                                        
SHEET    2  AF 2 VAL A 374  GLU A 380 -1  N  LEU A 375   O  ILE A 367           
SHEET    1  AG 2 TYR A 413  VAL A 415  0                                        
SHEET    2  AG 2 GLU A 476  SER A 478 -1  O  GLU A 476   N  VAL A 415           
SHEET    1  AH 6 PHE A 564  SER A 572  0                                        
SHEET    2  AH 6 VAL A 623  ARG A 632 -1  O  ILE A 624   N  ALA A 566           
SHEET    3  AH 6 SER A 637  PRO A 642 -1  O  SER A 637   N  ARG A 632           
SHEET    4  AH 6 ILE A 586  PRO A 590  1  O  PHE A 588   N  ALA A 640           
SHEET    5  AH 6 GLY A 575  LEU A 580 -1  O  MET A 576   N  ILE A 589           
SHEET    6  AH 6 PHE A 564  SER A 572 -1  O  GLU A 567   N  ARG A 579           
SHEET    1  AI 3 LEU A 601  SER A 604  0                                        
SHEET    2  AI 3 THR A 609  ILE A 612 -1  O  THR A 609   N  SER A 604           
SHEET    3  AI 3 GLU A 615  LYS A 619 -1  O  GLU A 615   N  ILE A 612           
LINK        MG    MG A1644                 O3'   A B  12     1555   1555  2.56  
LINK        MG    MG A1644                 OP1   A B  13     1555   1555  2.48  
LINK        MG    MG A1644                 OD1 ASP A 201     1555   1555  2.37  
LINK        MG    MG A1644                 OD2 ASP A 210     1555   1555  2.42  
LINK        MG    MG A1644                 O   HOH A2011     1555   1555  2.17  
LINK        MG    MG A1644                 O   HOH A2013     1555   1555  2.24  
SITE     1 AC1  6 ASP A 201  ASP A 210  HOH A2011  HOH A2013                    
SITE     2 AC1  6   A B  12    A B  13                                          
CRYST1   86.316   86.316  279.245  90.00  90.00 120.00 P 65          6          
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      0.011585  0.006689  0.000000        0.00000                         
SCALE2      0.000000  0.013378  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003581        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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