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Database: PDB
Entry: 2IX0
LinkDB: 2IX0
Original site: 2IX0 
HEADER    HYDROLASE                               05-JUL-06   2IX0              
TITLE     RNASE II                                                              
CAVEAT     2IX0    MET A 208 C-ALPHA IS PLANAR ALA A 211 C-ALPHA IS PLANAR ASP  
CAVEAT   2 2IX0    A 360 C-ALPHA IS PLANAR VAL A 374 C-ALPHA IS PLANAR LEU A    
CAVEAT   3 2IX0    427 C-ALPHA IS PLANAR ALA A 440 C-ALPHA IS PLANAR            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EXORIBONUCLEASE 2;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 6-644;                                            
COMPND   5 SYNONYM: RNASE II, EXORIBONUCLEASE II, RIBONUCLEASE II;              
COMPND   6 EC: 3.1.13.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
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                                    
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 2IX0    1       REMARK                                   
REVDAT   4   06-MAR-19 2IX0    1       REMARK                                   
REVDAT   3   13-JUL-11 2IX0    1       VERSN                                    
REVDAT   2   24-FEB-09 2IX0    1       VERSN                                    
REVDAT   1   05-OCT-06 2IX0    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.   7   443 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.    2.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 62.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 29969                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1576                            
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) : 2.44                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.51                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2131                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5042                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 145                                     
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) : 39.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.81000                                              
REMARK   3    B22 (A**2) : -0.07000                                             
REMARK   3    B33 (A**2) : -0.74000                                             
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): 0.367         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.249         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.196         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.300        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5287 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4913 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7162 ; 2.320 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11380 ; 4.412 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   638 ; 8.962 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   269 ;36.942 ;23.271       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   933 ;20.785 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    58 ;21.693 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   794 ; 0.415 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5864 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1108 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   970 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4750 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2414 ; 0.173 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3503 ; 0.141 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   178 ; 0.203 ; 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):    18 ; 0.240 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    78 ; 0.294 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.117 ; 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):  3333 ; 2.434 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5183 ; 3.707 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2230 ; 4.984 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1979 ; 7.488 ; 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  : 8                                          
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     4        A    45                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.1828   4.3869   0.7738              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0489 T22:   0.1188                                     
REMARK   3      T33:  -0.0317 T12:  -0.0127                                     
REMARK   3      T13:  -0.0756 T23:   0.0058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1231 L22:   0.8005                                     
REMARK   3      L33:   2.7384 L12:  -0.3041                                     
REMARK   3      L13:  -0.0238 L23:  -0.3080                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0725 S12:   0.1972 S13:   0.1394                       
REMARK   3      S21:  -0.2348 S22:   0.0444 S23:   0.1408                       
REMARK   3      S31:  -0.0647 S32:  -0.2799 S33:  -0.1169                       
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    46        A   169                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.1777   1.0051  26.6490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0237 T22:   0.0844                                     
REMARK   3      T33:   0.0632 T12:  -0.0241                                     
REMARK   3      T13:   0.0078 T23:   0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0322 L22:   0.2706                                     
REMARK   3      L33:   2.7241 L12:  -0.3815                                     
REMARK   3      L13:  -0.9342 L23:  -0.1481                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0103 S12:  -0.0571 S13:   0.0731                       
REMARK   3      S21:  -0.0541 S22:   0.0402 S23:  -0.0301                       
REMARK   3      S31:   0.1819 S32:  -0.0299 S33:  -0.0505                       
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   170        A   266                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3641  30.5521  51.7543              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1117 T22:   0.0881                                     
REMARK   3      T33:   0.0821 T12:   0.0203                                     
REMARK   3      T13:  -0.0418 T23:  -0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0633 L22:   1.5620                                     
REMARK   3      L33:   0.0670 L12:  -0.1994                                     
REMARK   3      L13:  -0.0448 L23:   0.1664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2106 S12:  -0.0559 S13:  -0.0897                       
REMARK   3      S21:   0.2721 S22:   0.1386 S23:  -0.0903                       
REMARK   3      S31:  -0.0759 S32:   0.1390 S33:   0.0720                       
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   267        A   359                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.8002  31.4241  52.9513              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1066 T22:  -0.0166                                     
REMARK   3      T33:   0.1168 T12:   0.0983                                     
REMARK   3      T13:   0.0813 T23:   0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0478 L22:   1.1280                                     
REMARK   3      L33:   1.1697 L12:   0.8497                                     
REMARK   3      L13:   0.8643 L23:   0.6390                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0583 S12:  -0.1304 S13:  -0.0965                       
REMARK   3      S21:   0.2538 S22:   0.1193 S23:   0.1656                       
REMARK   3      S31:  -0.0233 S32:   0.0362 S33:  -0.0610                       
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   360        A   387                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.5568   9.2925  46.8825              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1772 T22:   0.1130                                     
REMARK   3      T33:   0.0949 T12:   0.1072                                     
REMARK   3      T13:   0.0823 T23:   0.0404                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6335 L22:   0.8754                                     
REMARK   3      L33:   0.0706 L12:   1.1959                                     
REMARK   3      L13:   0.3396 L23:   0.2486                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3907 S12:  -0.4945 S13:  -0.0801                       
REMARK   3      S21:  -0.5940 S22:  -0.3635 S23:   0.3312                       
REMARK   3      S31:  -0.2851 S32:   0.0079 S33:  -0.0273                       
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   388        A   497                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.3237  28.4922  27.1098              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1038 T22:  -0.0348                                     
REMARK   3      T33:   0.0896 T12:   0.0494                                     
REMARK   3      T13:  -0.0443 T23:   0.0219                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2326 L22:   1.3159                                     
REMARK   3      L33:   1.2824 L12:   0.3085                                     
REMARK   3      L13:   0.3620 L23:   0.1417                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1052 S12:  -0.0389 S13:   0.1559                       
REMARK   3      S21:  -0.3089 S22:  -0.0690 S23:   0.1658                       
REMARK   3      S31:  -0.1007 S32:   0.0089 S33:   0.1742                       
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   498        A   548                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8418  27.7226  38.6742              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0740 T22:   0.0718                                     
REMARK   3      T33:   0.1116 T12:  -0.0029                                     
REMARK   3      T13:   0.0102 T23:  -0.0435                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1986 L22:   3.3767                                     
REMARK   3      L33:   0.6522 L12:   0.6997                                     
REMARK   3      L13:  -0.3127 L23:  -0.7201                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0767 S12:  -0.0102 S13:   0.0803                       
REMARK   3      S21:  -0.1353 S22:   0.1453 S23:  -0.2780                       
REMARK   3      S31:  -0.0414 S32:   0.1446 S33:  -0.2219                       
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   549        A   644                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.3727  -2.6854  26.5952              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0016 T22:   0.0986                                     
REMARK   3      T33:   0.1086 T12:  -0.0421                                     
REMARK   3      T13:   0.0148 T23:   0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4353 L22:   0.6493                                     
REMARK   3      L33:   2.8582 L12:   0.1201                                     
REMARK   3      L13:   1.1152 L23:   0.3353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0652 S12:   0.0244 S13:  -0.0358                       
REMARK   3      S21:   0.0376 S22:   0.0896 S23:   0.1627                       
REMARK   3      S31:  -0.1313 S32:   0.2444 S33:  -0.0244                       
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.DISOREDERED N-TERMINUS UNTIL RESIDUE 4 AND LOOP           
REMARK   3  BETWEEN REIDUES 30-33 AND 67-70 WERE NOT MODELLED.                  
REMARK   4                                                                      
REMARK   4 2IX0 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_1290029287.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID13                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.975                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31569                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.440                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.940                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.44                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2IX1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOUR DIFFUSION IN SITTING DROPS WITH   
REMARK 280  1.5 MICRO-L OF PROTEIN SOLUTION, 8-12 MG/ML 3% GLYCEROL 1 MM        
REMARK 280  MGCL2 100 MM KCL AND 100 MM TRIS-HCL PH 8.0, AND 1.5 MICRO-L OF     
REMARK 280  WELL SOLUTION, 22 % PEG 4K, 0.6M CA ACETATE AND 0.1M TRIS-HCL PH    
REMARK 280  8.5, AT 293 K, PH 8.50, VAPOR DIFFUSION, SITTING DROP               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       62.85950            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   -18                                                      
REMARK 465     GLY A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     SER 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     HIS A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     VAL A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     ARG A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     MET A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     GLY A    32                                                      
REMARK 465     LYS A    68                                                      
REMARK 465     GLU A    69                                                      
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     THR A 180    CB   OG1  CG2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   C    LEU A   456     H    ASP A   457              1.48            
REMARK 500   O    HOH A  2004     O    HOH A  2020              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    LEU A 456   C     ASP A 457   N       0.138                       
REMARK 500    ASP A 457   C     ASP A 457   O       0.120                       
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    PRO A   6   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    PHE A  35   CG  -  CD2 -  CE2 ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG A 113   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    HIS A 120   N   -  CA  -  C   ANGL. DEV. =  18.4 DEGREES          
REMARK 500    VAL A 188   CA  -  CB  -  CG2 ANGL. DEV. =  11.8 DEGREES          
REMARK 500    ALA A 211   N   -  CA  -  CB  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    LEU A 212   N   -  CA  -  C   ANGL. DEV. =  19.4 DEGREES          
REMARK 500    ILE A 225   CG1 -  CB  -  CG2 ANGL. DEV. =  17.3 DEGREES          
REMARK 500    THR A 232   CA  -  CB  -  CG2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ASN A 252   CB  -  CA  -  C   ANGL. DEV. =  14.2 DEGREES          
REMARK 500    TYR A 253   CG  -  CD1 -  CE1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    PHE A 257   CD1 -  CE1 -  CZ  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG A 264   N   -  CA  -  C   ANGL. DEV. =  17.2 DEGREES          
REMARK 500    VAL A 281   CG1 -  CB  -  CG2 ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ALA A 309   N   -  CA  -  CB  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    TYR A 313   CG  -  CD2 -  CE2 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    VAL A 357   CG1 -  CB  -  CG2 ANGL. DEV. = -11.2 DEGREES          
REMARK 500    VAL A 357   CA  -  CB  -  CG2 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    VAL A 374   CB  -  CA  -  C   ANGL. DEV. =  13.1 DEGREES          
REMARK 500    HIS A 416   CB  -  CA  -  C   ANGL. DEV. =  13.0 DEGREES          
REMARK 500    LEU A 427   CB  -  CA  -  C   ANGL. DEV. =  11.8 DEGREES          
REMARK 500    ASP A 457   CB  -  CA  -  C   ANGL. DEV. = -12.9 DEGREES          
REMARK 500    ARG A 534   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 539   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ALA A 596   N   -  CA  -  C   ANGL. DEV. =  16.5 DEGREES          
REMARK 500    TYR A 618   CD1 -  CE1 -  CZ  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG A 636   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 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    ASP A   5      122.02    151.69                                   
REMARK 500    THR A  29      -97.47   -171.99                                   
REMARK 500    HIS A  56      129.62    -39.92                                   
REMARK 500    THR A  84      -99.32   -113.47                                   
REMARK 500    ASN A  94      -29.53    -17.64                                   
REMARK 500    ASP A  95       20.88    -44.75                                   
REMARK 500    ARG A  96      112.79    125.74                                   
REMARK 500    HIS A 103      105.47    -21.40                                   
REMARK 500    HIS A 120      115.05     -3.11                                   
REMARK 500    ILE A 151      -84.26    -71.43                                   
REMARK 500    VAL A 159      -69.98    -14.40                                   
REMARK 500    GLU A 181      121.24      7.31                                   
REMARK 500    MET A 208      106.26    -49.57                                   
REMARK 500    PRO A 218      164.24    -48.91                                   
REMARK 500    ALA A 249      -40.01     64.06                                   
REMARK 500    PHE A 257      116.40   -165.11                                   
REMARK 500    ASP A 269      -82.98   -133.62                                   
REMARK 500    ASN A 297       12.53    -37.45                                   
REMARK 500    ALA A 309      117.69   -165.79                                   
REMARK 500    ALA A 355     -140.81   -144.70                                   
REMARK 500    ASP A 360      109.19    -25.92                                   
REMARK 500    ALA A 379       91.35    -58.97                                   
REMARK 500    ASP A 465      -71.02    -24.91                                   
REMARK 500    ALA A 475      116.66    -31.66                                   
REMARK 500    TYR A 492      102.47    177.46                                   
REMARK 500    ALA A 558      117.70    -34.60                                   
REMARK 500    THR A 562      125.91    -36.43                                   
REMARK 500    ARG A 573      -56.07    -28.00                                   
REMARK 500    THR A 621      -12.38     88.96                                   
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 ASP A    5     PRO A    6                 -133.83                    
REMARK 500 ALA A   28     THR A   29                  147.72                    
REMARK 500 GLY A   92     LYS A   93                 -127.73                    
REMARK 500 LYS A   93     ASN A   94                 -146.22                    
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 A1646  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 201   OD1                                                    
REMARK 620 2 ASP A 210   OD1 170.2                                              
REMARK 620 3 HOH A2059   O   100.5  87.1                                        
REMARK 620 4 HOH A2060   O    82.8  92.1  82.9                                  
REMARK 620 5 HOH A2055   O    82.7  92.5 158.5 118.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1647  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO A 101   O                                                      
REMARK 620 2 HIS A 103   O   102.2                                              
REMARK 620 3 HOH A2004   O   101.7 127.2                                        
REMARK 620 4 HOH A2020   O    95.8  87.3  43.9                                  
REMARK 620 5 HOH A2021   O   149.0  97.7  47.4  61.5                            
REMARK 620 6 LEU A 106   O    95.8  91.2 131.8 168.4 107.4                      
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 A 1646                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1647                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C5P A 1645                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2IX1   RELATED DB: PDB                                   
REMARK 900 RNASE II D209N MUTANT                                                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-TERMINAL HIS-TAGGED PROTEIN, WHERE THE FIRST 5 RESIDUES,           
REMARK 999 MFQDN, ARE REPLACED BY MGSSHHHHHHSSGLVPRGSHMLED. N-                  
REMARK 999 TERMINUS INVISIBLE IN ELECTRON DENSITY.                              
DBREF  2IX0 A  -18     5  PDB    2IX0     2IX0           -18      5             
DBREF  2IX0 A    6   644  UNP    P30850   RNB_ECOLI        6    644             
SEQRES   1 A  663  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  663  LEU VAL PRO ARG GLY SER HIS MET LEU ASP ASP PRO LEU          
SEQRES   3 A  663  LEU ALA GLN LEU LYS GLN GLN LEU HIS SER GLN THR PRO          
SEQRES   4 A  663  ARG ALA GLU GLY VAL VAL LYS ALA THR GLU LYS GLY PHE          
SEQRES   5 A  663  GLY PHE LEU GLU VAL ASP ALA GLN LYS SER TYR PHE ILE          
SEQRES   6 A  663  PRO PRO PRO GLN MET LYS LYS VAL MET HIS GLY ASP ARG          
SEQRES   7 A  663  ILE ILE ALA VAL ILE HIS SER GLU LYS GLU ARG GLU SER          
SEQRES   8 A  663  ALA GLU PRO GLU GLU LEU VAL GLU PRO PHE LEU THR ARG          
SEQRES   9 A  663  PHE VAL GLY LYS VAL GLN GLY LYS ASN ASP ARG LEU ALA          
SEQRES  10 A  663  ILE VAL PRO ASP HIS PRO LEU LEU LYS ASP ALA ILE PRO          
SEQRES  11 A  663  CYS ARG ALA ALA ARG GLY LEU ASN HIS GLU PHE LYS GLU          
SEQRES  12 A  663  GLY ASP TRP ALA VAL ALA GLU MET ARG ARG HIS PRO LEU          
SEQRES  13 A  663  LYS GLY ASP ARG SER PHE TYR ALA GLU LEU THR GLN TYR          
SEQRES  14 A  663  ILE THR PHE GLY ASP ASP HIS PHE VAL PRO TRP TRP VAL          
SEQRES  15 A  663  THR LEU ALA ARG HIS ASN LEU GLU LYS GLU ALA PRO ASP          
SEQRES  16 A  663  GLY VAL ALA THR GLU MET LEU ASP GLU GLY LEU VAL ARG          
SEQRES  17 A  663  GLU ASP LEU THR ALA LEU ASP PHE VAL THR ILE ASP SER          
SEQRES  18 A  663  ALA SER THR GLU ASP MET ASP ASP ALA LEU PHE ALA LYS          
SEQRES  19 A  663  ALA LEU PRO ASP ASP LYS LEU GLN LEU ILE VAL ALA ILE          
SEQRES  20 A  663  ALA ASP PRO THR ALA TRP ILE ALA GLU GLY SER LYS LEU          
SEQRES  21 A  663  ASP LYS ALA ALA LYS ILE ARG ALA PHE THR ASN TYR LEU          
SEQRES  22 A  663  PRO GLY PHE ASN ILE PRO MET LEU PRO ARG GLU LEU SER          
SEQRES  23 A  663  ASP ASP LEU CYS SER LEU ARG ALA ASN GLU VAL ARG PRO          
SEQRES  24 A  663  VAL LEU ALA CYS ARG MET THR LEU SER ALA ASP GLY THR          
SEQRES  25 A  663  ILE GLU ASP ASN ILE GLU PHE PHE ALA ALA THR ILE GLU          
SEQRES  26 A  663  SER LYS ALA LYS LEU VAL TYR ASP GLN VAL SER ASP TRP          
SEQRES  27 A  663  LEU GLU ASN THR GLY ASP TRP GLN PRO GLU SER GLU ALA          
SEQRES  28 A  663  ILE ALA GLU GLN VAL ARG LEU LEU ALA GLN ILE CYS GLN          
SEQRES  29 A  663  ARG ARG GLY GLU TRP ARG HIS ASN HIS ALA LEU VAL PHE          
SEQRES  30 A  663  LYS ASP ARG PRO ASP TYR ARG PHE ILE LEU GLY GLU LYS          
SEQRES  31 A  663  GLY GLU VAL LEU ASP ILE VAL ALA GLU PRO ARG ARG ILE          
SEQRES  32 A  663  ALA ASN ARG ILE VAL GLU GLU ALA MET ILE ALA ALA ASN          
SEQRES  33 A  663  ILE CYS ALA ALA ARG VAL LEU ARG ASP LYS LEU GLY PHE          
SEQRES  34 A  663  GLY ILE TYR ASN VAL HIS MET GLY PHE ASP PRO ALA ASN          
SEQRES  35 A  663  ALA ASP ALA LEU ALA ALA LEU LEU LYS THR HIS GLY LEU          
SEQRES  36 A  663  HIS VAL ASP ALA GLU GLU VAL LEU THR LEU ASP GLY PHE          
SEQRES  37 A  663  CYS LYS LEU ARG ARG GLU LEU ASP ALA GLN PRO THR GLY          
SEQRES  38 A  663  PHE LEU ASP SER ARG ILE ARG ARG PHE GLN SER PHE ALA          
SEQRES  39 A  663  GLU ILE SER THR GLU PRO GLY PRO HIS PHE GLY LEU GLY          
SEQRES  40 A  663  LEU GLU ALA TYR ALA THR TRP THR SER PRO ILE ARG LYS          
SEQRES  41 A  663  TYR GLY ASP MET ILE ASN HIS ARG LEU LEU LYS ALA VAL          
SEQRES  42 A  663  ILE LYS GLY GLU THR ALA THR ARG PRO GLN ASP GLU ILE          
SEQRES  43 A  663  THR VAL GLN MET ALA GLU ARG ARG ARG LEU ASN ARG MET          
SEQRES  44 A  663  ALA GLU ARG ASP VAL GLY ASP TRP LEU TYR ALA ARG PHE          
SEQRES  45 A  663  LEU LYS ASP LYS ALA GLY THR ASP THR ARG PHE ALA ALA          
SEQRES  46 A  663  GLU ILE VAL ASP ILE SER ARG GLY GLY MET ARG VAL ARG          
SEQRES  47 A  663  LEU VAL ASP ASN GLY ALA ILE ALA PHE ILE PRO ALA PRO          
SEQRES  48 A  663  PHE LEU HIS ALA VAL ARG ASP GLU LEU VAL CYS SER GLN          
SEQRES  49 A  663  GLU ASN GLY THR VAL GLN ILE LYS GLY GLU THR VAL TYR          
SEQRES  50 A  663  LYS VAL THR ASP VAL ILE ASP VAL THR ILE ALA GLU VAL          
SEQRES  51 A  663  ARG MET GLU THR ARG SER ILE ILE ALA ARG PRO VAL ALA          
HET    C5P  A1645      21                                                       
HET     MG  A1646       1                                                       
HET     CA  A1647       1                                                       
HETNAM     C5P CYTIDINE-5'-MONOPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  C5P    C9 H14 N3 O8 P                                               
FORMUL   3   MG    MG 2+                                                        
FORMUL   4   CA    CA 2+                                                        
FORMUL   5  HOH   *145(H2 O)                                                    
HELIX    1   1 ASP A    5  GLN A   18  1                                  14    
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  218  ASP A  220  5                                   3    
HELIX    6   6 ASP A  230  TRP A  234  5                                   5    
HELIX    7   7 SER A  239  ALA A  249  1                                  11    
HELIX    8   8 PRO A  263  ASP A  269  1                                   7    
HELIX    9   9 TYR A  313  GLU A  321  1                                   9    
HELIX   10  10 SER A  330  ALA A  355  1                                  26    
HELIX   11  11 ARG A  383  LEU A  408  1                                  26    
HELIX   12  12 ASP A  420  ALA A  422  5                                   3    
HELIX   13  13 ASN A  423  HIS A  434  1                                  12    
HELIX   14  14 GLU A  441  LEU A  444  5                                   4    
HELIX   15  15 THR A  445  GLN A  459  1                                  15    
HELIX   16  16 GLY A  462  ILE A  468  1                                   7    
HELIX   17  17 ARG A  469  GLN A  472  5                                   4    
HELIX   18  18 LYS A  501  GLY A  517  1                                  17    
HELIX   19  19 GLN A  524  LYS A  555  1                                  32    
HELIX   20  20 ASP A  556  ALA A  558  5                                   3    
HELIX   21  21 PRO A  592  LEU A  594  5                                   3    
HELIX   22  22 VAL A  597  ASP A  599  5                                   3    
SHEET    1  AA 7 ARG A  21  LYS A  27  0                                        
SHEET    2  AA 7 ARG A  59  HIS A  65 -1  O  ILE A  60   N  GLY A  24           
SHEET    3  AA 7 SER A  72  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  GLN A  91  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  TYR A 150 -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 LEU A  97  PRO A 101 -1  O  LEU A  97   N  CYS A 112           
SHEET    6  AB 7 ARG A  85  GLN A  91 -1  O  LYS A  89   N  VAL A 100           
SHEET    7  AB 7 ARG A  85  GLN A  91  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  ILE A 228 -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 A1646                 OD1 ASP A 201     1555   1555  2.39  
LINK        MG    MG A1646                 OD1 ASP A 210     1555   1555  2.23  
LINK        MG    MG A1646                 O   HOH A2059     1555   1555  2.05  
LINK        MG    MG A1646                 O   HOH A2060     1555   1555  2.34  
LINK        MG    MG A1646                 O   HOH A2055     1555   1555  2.27  
LINK        CA    CA A1647                 O   PRO A 101     1555   1555  2.49  
LINK        CA    CA A1647                 O   HIS A 103     1555   1555  2.38  
LINK        CA    CA A1647                 O   HOH A2004     1555   1555  2.95  
LINK        CA    CA A1647                 O   HOH A2020     1555   1555  2.67  
LINK        CA    CA A1647                 O   HOH A2021     1555   1555  2.87  
LINK        CA    CA A1647                 O   LEU A 106     1555   1555  2.30  
SITE     1 AC1  5 ASP A 201  ASP A 210  HOH A2055  HOH A2059                    
SITE     2 AC1  5 HOH A2060                                                     
SITE     1 AC2  6 PRO A 101  HIS A 103  LEU A 106  HOH A2004                    
SITE     2 AC2  6 HOH A2020  HOH A2021                                          
SITE     1 AC3  7 PHE A  82  PHE A  86  VAL A  87  PRO A 101                    
SITE     2 AC3  7 ASP A 102  HIS A 103  ARG A 167                               
CRYST1   56.836  125.719   66.244  90.00 111.91  90.00 P 1 21 1      2          
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      0.017594  0.000000  0.007077        0.00000                         
SCALE2      0.000000  0.007954  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016271        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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