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Database: PDB
Entry: 2I80
LinkDB: 2I80
Original site: 2I80 
ANISOU 4009  N   GLY A 648     2266   1810   2508    207    -36   -155       N  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    HYDROLASE/HYDROLASE INHIBITOR           30-NOV-12   4I74              
TITLE     CRYSTAL STRUCTURE OF THE TRYPANOSOMA BRUCEI INOSINE-ADENOSINE-        
TITLE    2 GUANOSINE NUCLEOSIDE HYDROLASE IN COMPLEX WITH COMPOUND UAMC-00312   
TITLE    3 AND ALLOSTERICALLY INHIBITED BY A NI2+ ION                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INOSINE-ADENOSINE-GUANOSINE-NUCLEOSIDE HYDROLASE;          
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.2.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI BRUCEI;                      
SOURCE   3 ORGANISM_TAXID: 999953;                                              
SOURCE   4 STRAIN: 927/4 GUTAT10.1;                                             
SOURCE   5 GENE: TB927.3.2960;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    NUCLEOSIDE HYDROLASE, OPEN (ALPHA,BETA) STRUCTURE, NH FOLD,           
KEYWDS   2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.GIANNESE,M.DEGANO                                                   
REVDAT   2   18-DEC-13 4I74    1       JRNL                                     
REVDAT   1   07-AUG-13 4I74    0                                                
JRNL        AUTH   F.GIANNESE,M.BERG,P.VAN DER VEKEN,V.CASTAGNA,P.TORNAGHI,     
JRNL        AUTH 2 K.AUGUSTYNS,M.DEGANO                                         
JRNL        TITL   STRUCTURES OF PURINE NUCLEOSIDASE FROM TRYPANOSOMA BRUCEI    
JRNL        TITL 2 BOUND TO ISOZYME-SPECIFIC TRYPANOCIDALS AND A NOVEL          
JRNL        TITL 3 METALORGANIC INHIBITOR                                       
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  69  1553 2013              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   23897478                                                     
JRNL        DOI    10.1107/S0907444913010792                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.VERSEES,J.BARLOW,J.STEYAERT                                
REMARK   1  TITL   TRANSITION-STATE COMPLEX OF THE PURINE-SPECIFIC NUCLEOSIDE   
REMARK   1  TITL 2 HYDROLASE OF T. VIVAX: ENZYME CONFORMATIONAL CHANGES AND     
REMARK   1  TITL 3 IMPLICATIONS FOR CATALYSIS                                   
REMARK   1  REF    J.MOL.BIOL.                   V. 359   331 2006              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   16630632                                                     
REMARK   1  DOI    10.1016/J.JMB.2006.03.026                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.VANDEMEULEBROUCKE,C.MINICI,I.BRUNO,L.MUZZOLINI,P.TORNAGHI, 
REMARK   1  AUTH 2 D.W.PARKIN,W.VERSEES,J.STEYAERT,M.DEGANO                     
REMARK   1  TITL   STRUCTURE AND MECHANISM OF THE 6-OXOPURINE NUCLEOSIDASE FROM 
REMARK   1  TITL 2 TRYPANOSOMA BRUCEI BRUCEI                                    
REMARK   1  REF    BIOCHEMISTRY                  V.  49  8999 2010              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   20825170                                                     
REMARK   1  DOI    10.1021/BI100697D                                            
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   D.W.PARKIN                                                   
REMARK   1  TITL   PURINE-SPECIFIC NUCLEOSIDE N-RIBOHYDROLASE FROM TRYPANOSOMA  
REMARK   1  TITL 2 BRUCEI BRUCEI. PURIFICATION, SPECIFICITY, AND KINETIC        
REMARK   1  TITL 3 MECHANISM                                                    
REMARK   1  REF    J.BIOL.CHEM.                  V. 271 21713 1996              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   8702965                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.68 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.68                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.91                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 31439                          
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) : 0.152                           
REMARK   3   R VALUE            (WORKING SET) : 0.150                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1590                            
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) : 1.68                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.72                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2166                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 115                          
REMARK   3   BIN FREE R VALUE                    : 0.2660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2506                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 281                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.25                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.42000                                             
REMARK   3    B22 (A**2) : -0.21000                                             
REMARK   3    B33 (A**2) : 0.63000                                              
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): 0.102         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.100         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.064         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.905         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2655 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1754 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3625 ; 1.680 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4331 ; 1.002 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   345 ; 5.236 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   106 ;35.694 ;25.189       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   449 ;12.352 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;14.250 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   415 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2942 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   499 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1670 ; 0.887 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   669 ; 0.258 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2712 ; 1.561 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   985 ; 2.475 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   905 ; 4.124 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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   : 1.40                                          
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 U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 4I74 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-DEC-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB076387.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : DIAMOND (001)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31441                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.680                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.910                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.9400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.940                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 23% PEGMME2000, 10MM          
REMARK 280  NI2SO4, PH 7.6, VAPOR DIFFUSION, TEMPERATURE 292K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.11500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.11500            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       30.06000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       34.71000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       30.06000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       34.71000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       65.11500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       30.06000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       34.71000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       65.11500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       30.06000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       34.71000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -60.12000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -65.11500            
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     GLU A   300                                                      
REMARK 465     GLY A   301                                                      
REMARK 465     LYS A   302                                                      
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  NI     NI A   402     O    HOH A   764              1.14            
REMARK 500  NI     NI A   402     O    HOH A   696              1.52            
REMARK 500   O    HOH A   751     O    HOH A   764              1.90            
REMARK 500   O    HOH A   730     O    HOH A   752              1.95            
REMARK 500   O    HOH A   737     O    HOH A   766              1.98            
REMARK 500   OE2  GLU A   277     O    HOH A   621              2.03            
REMARK 500   O    HOH A   518     O    HOH A   721              2.04            
REMARK 500   O    HOH A   705     O    HOH A   757              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500  NI     NI A   403     O    HOH A   737     5555     1.11            
REMARK 500   O    HOH A   733     O    HOH A   734     7444     1.57            
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    SER A  -1       -4.36   -160.02                                   
REMARK 500    ASP A  38       48.91    -76.02                                   
REMARK 500    ALA A  39      -92.40   -103.35                                   
REMARK 500    VAL A 168      -63.47    -96.31                                   
REMARK 500    ASP A 190       82.02   -155.50                                   
REMARK 500    HIS A 247     -128.43     49.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 MBY 408 AND NI 406, TRS 409 PLACE THE ALTERNATE POSITIONS.           
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                              NI A 406  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRS A 409   O1                                                     
REMARK 620 2 HOH A 742   O    88.3                                              
REMARK 620 3 TRS A 409   N    89.2 168.2                                        
REMARK 620 4 ASP A  14   OD2 102.6  93.1  98.7                                  
REMARK 620 5 TRS A 409   O3   74.6  86.1  82.2 177.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 402  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 661   O                                                      
REMARK 620 2 HOH A 751   O   176.6                                              
REMARK 620 3 HIS A  58   NE2  88.0  90.0                                        
REMARK 620 4 HOH A 704   O    86.9  94.9 172.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 404  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 725   O                                                      
REMARK 620 2 HOH A 772   O   102.4                                              
REMARK 620 3 HIS A 317   NE2 113.1  93.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 407  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 729   O                                                      
REMARK 620 2 HOH A 728   O   111.6                                              
REMARK 620 3 ASP A 190   OD2  87.8  84.4                                        
REMARK 620 4 HOH A 780   O    78.7 169.2 100.0                                  
REMARK 620 5 HOH A 755   O    99.1  85.3 169.2  89.6                            
REMARK 620 6 HOH A 540   O   155.4  92.8  98.4  76.8  78.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 405  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  -1   N                                                      
REMARK 620 2 HIS A   0   ND1 168.1                                              
REMARK 620 3 HIS A   0   N    88.1  93.0                                        
REMARK 620 4 GLY A  -2   N    79.6  99.4 167.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 410  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 757   O                                                      
REMARK 620 2 HIS A 247   NE2  90.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 137   O                                                      
REMARK 620 2 ASP A  10   OD1  94.4                                              
REMARK 620 3 HOH A 742   O   149.9  98.3                                        
REMARK 620 4 ASP A 261   OD2  85.9 146.8  97.7                                  
REMARK 620 5 ASP A  15   OD2 135.2  78.6  74.3  78.0                            
REMARK 620 6 MBY A 408   O2' 132.7 127.7  29.5  70.5  80.3                      
REMARK 620 7 ASP A  15   OD1  83.6  74.8 126.0  72.2  51.8 123.8                
REMARK 620 8 HOH A 527   O    92.3  71.7  66.5 141.6 125.6  83.3 145.8          
REMARK 620 9 MBY A 408   O3'  73.5 140.0  79.3  71.8 136.4  60.5 138.3  70.9    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 407                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MBY A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 410                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3EPW   RELATED DB: PDB                                   
REMARK 900 T.VIVAX IAGNH BOUND TO A N-METHYLARYL IMINORIBITOL INHIBITOR         
REMARK 900 RELATED ID: 3FZ0   RELATED DB: PDB                                   
REMARK 900 T. BRUCEI IGNH                                                       
REMARK 900 RELATED ID: 4I70   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4I71   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4I72   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4I73   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4I75   RELATED DB: PDB                                   
DBREF  4I74 A    1   327  UNP    Q57ZL6   Q57ZL6_TRYB2     1    327             
SEQADV 4I74 GLY A   -2  UNP  Q57ZL6              EXPRESSION TAG                 
SEQADV 4I74 SER A   -1  UNP  Q57ZL6              EXPRESSION TAG                 
SEQADV 4I74 HIS A    0  UNP  Q57ZL6              EXPRESSION TAG                 
SEQRES   1 A  330  GLY SER HIS MET ALA LYS THR VAL ILE LEU ASP HIS ASP          
SEQRES   2 A  330  GLY ASN LYS ASP ASP PHE VAL ALA MET ILE LEU LEU LEU          
SEQRES   3 A  330  SER ASN PRO LYS LYS VAL ASN LEU ILE GLY CYS ILE CYS          
SEQRES   4 A  330  THR ASP ALA ASP CYS PHE VAL GLU ASN GLY PHE ASP VAL          
SEQRES   5 A  330  THR GLY LYS ILE MET CYS ALA MET HIS ARG LEU ILE LYS          
SEQRES   6 A  330  THR PRO LEU PHE PRO ILE GLY LYS SER THR ALA THR ALA          
SEQRES   7 A  330  VAL ASN ALA PHE PRO THR GLU TRP ARG PHE SER ALA LYS          
SEQRES   8 A  330  ASN LEU ASP ASP MET PRO PHE LEU ASN ILE VAL GLU ASP          
SEQRES   9 A  330  VAL ALA LEU TRP GLU LYS LEU LYS PRO GLU ASN GLU ALA          
SEQRES  10 A  330  HIS ASN GLY GLN GLN LEU LEU ALA ASP LEU VAL MET LYS          
SEQRES  11 A  330  SER LYS GLU LYS VAL THR VAL CYS VAL THR GLY PRO LEU          
SEQRES  12 A  330  SER ASN MET ALA TRP CYS ILE GLU LYS TYR GLY GLU ALA          
SEQRES  13 A  330  PHE THR SER LYS VAL GLU GLU CYS VAL ILE MET GLY GLY          
SEQRES  14 A  330  ALA VAL ASP VAL GLY GLY ASN VAL PHE LEU PRO THR THR          
SEQRES  15 A  330  ASP GLY SER ALA GLU TRP ASN ILE TYR TRP ASP PRO PRO          
SEQRES  16 A  330  ALA ALA LYS LYS VAL LEU CYS CYS PRO ASN ILE ARG CYS          
SEQRES  17 A  330  VAL LEU PHE SER LEU ASP ALA THR ASN THR VAL PRO VAL          
SEQRES  18 A  330  ARG SER VAL ASP VAL LYS GLY PHE GLY ALA GLN ASN GLN          
SEQRES  19 A  330  TYR LEU LEU SER GLN MET VAL GLY THR MET TRP ALA MET          
SEQRES  20 A  330  SER THR HIS GLU GLU ILE LEU ARG ASP GLY ASP ALA TYR          
SEQRES  21 A  330  TYR ALA TRP ASP ALA LEU THR ALA ALA TYR ILE LEU GLU          
SEQRES  22 A  330  PRO THR ILE ALA THR LEU GLU PRO VAL ALA LEU ASP VAL          
SEQRES  23 A  330  ASP VAL SER LYS GLY LYS SER GLU GLY ARG THR PRO ARG          
SEQRES  24 A  330  ALA SER GLY GLU GLY LYS PRO CYS VAL HIS VAL ALA ARG          
SEQRES  25 A  330  ASN PRO SER LYS GLN MET PHE HIS ASP LEU VAL PHE ALA          
SEQRES  26 A  330  SER THR ARG VAL CYS                                          
HET     CA  A 401       1                                                       
HET     NI  A 402       1                                                       
HET     NI  A 403       1                                                       
HET     NI  A 404       1                                                       
HET     NI  A 405       1                                                       
HET     NI  A 406       1                                                       
HET     NI  A 407       1                                                       
HET    MBY  A 408      20                                                       
HET    TRS  A 409       8                                                       
HET     NI  A 410       2                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      NI NICKEL (II) ION                                                  
HETNAM     MBY (2R,3R,4S)-2-(HYDROXYMETHYL)-1-[(4-HYDROXYTHIENO[3,2-            
HETNAM   2 MBY  D]PYRIMIDIN-7-YL)METHYL]PYRROLIDINE-3,4-DIOL                    
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   2   CA    CA 2+                                                        
FORMUL   3   NI    7(NI 2+)                                                     
FORMUL   9  MBY    C12 H15 N3 O4 S                                              
FORMUL  10  TRS    C4 H12 N O3 1+                                               
FORMUL  12  HOH   *281(H2 O)                                                    
HELIX    1   1 ASN A   12  SER A   24  1                                  13    
HELIX    2   2 PHE A   42  LYS A   62  1                                  21    
HELIX    3   3 PRO A   80  PHE A   85  1                                   6    
HELIX    4   4 PHE A   85  ASP A   92  1                                   8    
HELIX    5   5 MET A   93  ASN A   97  5                                   5    
HELIX    6   6 ILE A   98  ALA A  114  1                                  17    
HELIX    7   7 ASN A  116  SER A  128  1                                  13    
HELIX    8   8 LEU A  140  GLY A  151  1                                  12    
HELIX    9   9 GLY A  151  SER A  156  1                                   6    
HELIX   10  10 GLU A  184  ASP A  190  1                                   7    
HELIX   11  11 ASP A  190  CYS A  199  1                                  10    
HELIX   12  12 SER A  209  ASN A  214  1                                   6    
HELIX   13  13 SER A  220  LYS A  224  1                                   5    
HELIX   14  14 GLY A  225  ASN A  230  5                                   6    
HELIX   15  15 TYR A  232  MET A  244  1                                  13    
HELIX   16  16 THR A  246  ILE A  250  5                                   5    
HELIX   17  17 ALA A  259  GLU A  270  1                                  12    
HELIX   18  18 PRO A  271  ALA A  274  5                                   4    
HELIX   19  19 SER A  312  THR A  324  1                                  13    
SHEET    1   A 8 ILE A  68  LYS A  70  0                                        
SHEET    2   A 8 VAL A  29  CYS A  36  1  N  CYS A  36   O  GLY A  69           
SHEET    3   A 8 LYS A   3  HIS A   9  1  N  LYS A   3   O  ASN A  30           
SHEET    4   A 8 VAL A 132  VAL A 136  1  O  THR A 133   N  THR A   4           
SHEET    5   A 8 VAL A 158  MET A 164  1  O  VAL A 162   N  VAL A 136           
SHEET    6   A 8 CYS A 205  PHE A 208  1  O  PHE A 208   N  ILE A 163           
SHEET    7   A 8 VAL A 305  ARG A 309  1  O  ALA A 308   N  LEU A 207           
SHEET    8   A 8 THR A 275  VAL A 279 -1  N  VAL A 279   O  VAL A 305           
SHEET    1   B 2 VAL A 218  ARG A 219  0                                        
SHEET    2   B 2 ALA A 256  TYR A 257 -1  O  TYR A 257   N  VAL A 218           
SSBOND   1 CYS A  199    CYS A  304                          1555   1555  2.08  
LINK        NI  B NI A 406                 O1 BTRS A 409     1555   1555  1.82  
LINK        NI    NI A 402                 O   HOH A 661     1555   1555  1.85  
LINK        NI    NI A 402                 O   HOH A 751     1555   1555  1.90  
LINK        NI    NI A 404                 O   HOH A 725     1555   1555  1.91  
LINK        NI  B NI A 406                 O   HOH A 742     1555   1555  1.91  
LINK        NI    NI A 407                 O   HOH A 729     1555   1555  1.94  
LINK         N   SER A  -1                NI    NI A 405     1555   1555  1.95  
LINK         ND1 HIS A   0                NI    NI A 405     1555   1555  1.97  
LINK        NI    NI A 407                 O   HOH A 728     1555   1555  2.01  
LINK         N   HIS A   0                NI    NI A 405     1555   1555  2.05  
LINK         OD2 ASP A 190                NI    NI A 407     1555   1555  2.07  
LINK        NI  B NI A 406                 N  BTRS A 409     1555   1555  2.09  
LINK         NE2 HIS A  58                NI    NI A 402     1555   1555  2.09  
LINK         NE2 HIS A 115                NI    NI A 403     1555   1555  2.12  
LINK        NI    NI A 407                 O   HOH A 780     1555   1555  2.15  
LINK         OD2BASP A  14                NI  B NI A 406     1555   1555  2.18  
LINK         N   GLY A  -2                NI    NI A 405     1555   1555  2.19  
LINK        NI  A NI A 410                 O   HOH A 757     1555   1555  2.22  
LINK        NI  B NI A 406                 O3 BTRS A 409     1555   1555  2.23  
LINK        NI    NI A 402                 O   HOH A 704     1555   1555  2.24  
LINK        NI    NI A 407                 O   HOH A 755     1555   1555  2.28  
LINK        NI    NI A 404                 O   HOH A 772     1555   1555  2.29  
LINK         NE2 HIS A 247                NI  B NI A 410     1555   1555  2.31  
LINK         O   THR A 137                CA    CA A 401     1555   1555  2.32  
LINK         OD1 ASP A  10                CA    CA A 401     1555   1555  2.33  
LINK        CA    CA A 401                 O   HOH A 742     1555   1555  2.34  
LINK         OD2 ASP A 261                CA    CA A 401     1555   1555  2.42  
LINK         OD2 ASP A  15                CA    CA A 401     1555   1555  2.47  
LINK        CA    CA A 401                 O2'AMBY A 408     1555   1555  2.53  
LINK         OD1 ASP A  15                CA    CA A 401     1555   1555  2.57  
LINK        CA    CA A 401                 O   HOH A 527     1555   1555  2.58  
LINK        CA    CA A 401                 O3'AMBY A 408     1555   1555  2.74  
LINK        NI    NI A 407                 O   HOH A 540     1555   1555  2.77  
LINK         NE2 HIS A 317                NI    NI A 404     1555   1555  2.77  
LINK         NE2 HIS A 247                NI  A NI A 410     1555   1555  2.77  
LINK        CA    CA A 401                 O1 BTRS A 409     1555   1555  2.80  
SITE     1 AC1  9 ASP A  10  ASP A  15  THR A 137  ASP A 261                    
SITE     2 AC1  9  NI A 406  MBY A 408  TRS A 409  HOH A 527                    
SITE     3 AC1  9 HOH A 742                                                     
SITE     1 AC2  6 HIS A  58  HOH A 661  HOH A 696  HOH A 704                    
SITE     2 AC2  6 HOH A 751  HOH A 764                                          
SITE     1 AC3  6 HIS A 115  HOH A 639  HOH A 735  HOH A 737                    
SITE     2 AC3  6 HOH A 765  HOH A 766                                          
SITE     1 AC4  5 HIS A 317  HOH A 541  HOH A 703  HOH A 725                    
SITE     2 AC4  5 HOH A 772                                                     
SITE     1 AC5  4 GLY A  -2  SER A  -1  HIS A   0  MET A   1                    
SITE     1 AC6  5 ASP A  14  ASP A  40   CA A 401  TRS A 409                    
SITE     2 AC6  5 HOH A 742                                                     
SITE     1 AC7  6 ASP A 190  HOH A 540  HOH A 728  HOH A 729                    
SITE     2 AC7  6 HOH A 755  HOH A 780                                          
SITE     1 AC8 20 ASN A  12  ASP A  14  ASP A  15  ASP A  40                    
SITE     2 AC8 20 PHE A  79  TRP A  83  THR A 137  MET A 164                    
SITE     3 AC8 20 ASN A 173  GLU A 184  TRP A 185  ASN A 186                    
SITE     4 AC8 20 GLU A 248  GLU A 249  TRP A 260  ASP A 261                    
SITE     5 AC8 20  CA A 401  HOH A 527  HOH A 607  HOH A 742                    
SITE     1 AC9 15 ASP A  14  ASP A  40  PHE A  79  THR A 137                    
SITE     2 AC9 15 MET A 164  ASN A 173  GLU A 184  TRP A 185                    
SITE     3 AC9 15 ASN A 186  TRP A 260  ASP A 261   CA A 401                    
SITE     4 AC9 15  NI A 406  HOH A 527  HOH A 742                               
SITE     1 BC1  4 GLU A  82  HIS A 247  HOH A 720  HOH A 757                    
CRYST1   60.120   69.420  130.230  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016633  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014405  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007679        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    TRANSCRIPTION REGULATOR                 04-MAR-10   3M1E              
TITLE     CRYSTAL STRUCTURE OF BENM_DBD                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HTH-TYPE TRANSCRIPTIONAL REGULATOR BENM;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: DNA BINDING DOMAIN;                                        
COMPND   5 SYNONYM: BEN AND CAT OPERON TRANSCRIPTIONAL REGULATOR;               
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ACINETOBACTER SP. ADP1;                         
SOURCE   3 ORGANISM_TAXID: 62977;                                               
SOURCE   4 STRAIN: ADP1;                                                        
SOURCE   5 GENE: ACIAD1435, BENM, BENR;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21B                                    
KEYWDS    WHTH, ACTIVATOR, AROMATIC HYDROCARBONS CATABOLISM, DNA-BINDING,       
KEYWDS   2 TRANSCRIPTION, TRANSCRIPTION REGULATION, TRANSCRIPTION REGULATOR     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ALANAZI,C.MOMANY,E.L.NEIDLE                                         
REVDAT   2   10-JUL-13 3M1E    1       JRNL   VERSN                             
REVDAT   1   27-APR-11 3M1E    0                                                
JRNL        AUTH   A.ALANAZI,E.L.NEIDLE,C.MOMANY                                
JRNL        TITL   CRYSTAL STRUCTURE OF THE UNBOUND LYSR-TYPE TRANSCRIPTIONAL   
JRNL        TITL 2 REGULATOR BENM DNA BINDING DOMAIN                            
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D                   2013              
JRNL        REFN                   ISSN 0907-4449                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 8754                           
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 437                             
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 577                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 32                           
REMARK   3   BIN FREE R VALUE                    : 0.2930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 704                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 97                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.45000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.45000                                             
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): 0.132         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.131         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.098         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.255         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   737 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):   994 ; 0.917 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):    92 ; 3.438 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    34 ;30.840 ;23.824       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   145 ;13.434 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;16.431 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   114 ; 0.057 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   542 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):    11 ; 0.720 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):    18 ; 1.503 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):     8 ; 3.096 ; 7.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):     6 ; 3.739 ;10.000       
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  : 1                                          
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    87                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9260 -11.8290   8.5020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0574 T22:   0.0622                                     
REMARK   3      T33:   0.0282 T12:  -0.0017                                     
REMARK   3      T13:  -0.0128 T23:  -0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1267 L22:   2.3231                                     
REMARK   3      L33:   4.4060 L12:  -0.1633                                     
REMARK   3      L13:  -0.7001 L23:   2.8307                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0026 S12:   0.0005 S13:  -0.0473                       
REMARK   3      S21:   0.0180 S22:  -0.0068 S23:  -0.0137                       
REMARK   3      S31:   0.0420 S32:   0.0468 S33:   0.0042                       
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   : 1.40                                          
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 U VALUES : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 3M1E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057985.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0080                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : MAR                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9300                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.070                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: EQUAL VOLUMES OF PRECIPITANT AND         
REMARK 280  PROTEIN SOLUTION. PRECIPITANT:CRYSTAL SCREEN 2 # 30 - 0.1 M HEPES   
REMARK 280  PH 7.5, 10% PEG 6000, 5% MPD. PROTEIN: 20 MM TRIS BASE (PH 8.0),    
REMARK 280  0.5 M NACL, 10% GLYCEROL, 150 MM IMIDAZOLE, 10 MM BME, MICROBATCH   
REMARK 280  UNDER OIL, TEMPERATURE 288K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       34.36700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       34.36700            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       16.68000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       42.07300            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       16.68000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       42.07300            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       34.36700            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       16.68000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       42.07300            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       34.36700            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       16.68000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       42.07300            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9260 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       34.36700            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 189  LIES ON A SPECIAL POSITION.                          
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     GLY A    88                                                      
REMARK 465     HIS A    89                                                      
REMARK 465     HIS A    90                                                      
REMARK 465     HIS A    91                                                      
REMARK 465     HIS A    92                                                      
REMARK 465     HIS A    93                                                      
REMARK 465     HIS A    94                                                      
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 189        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH A 190        DISTANCE =  5.33 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 95                   
DBREF  3M1E A    1    87  UNP    O68014   BENM_ACIAD       1     87             
SEQADV 3M1E GLY A   88  UNP  O68014              EXPRESSION TAG                 
SEQADV 3M1E HIS A   89  UNP  O68014              EXPRESSION TAG                 
SEQADV 3M1E HIS A   90  UNP  O68014              EXPRESSION TAG                 
SEQADV 3M1E HIS A   91  UNP  O68014              EXPRESSION TAG                 
SEQADV 3M1E HIS A   92  UNP  O68014              EXPRESSION TAG                 
SEQADV 3M1E HIS A   93  UNP  O68014              EXPRESSION TAG                 
SEQADV 3M1E HIS A   94  UNP  O68014              EXPRESSION TAG                 
SEQRES   1 A   94  MET GLU LEU ARG HIS LEU ARG TYR PHE VAL ALA VAL VAL          
SEQRES   2 A   94  GLU GLU GLN SER PHE THR LYS ALA ALA ASP LYS LEU CYS          
SEQRES   3 A   94  ILE ALA GLN PRO PRO LEU SER ARG GLN ILE GLN ASN LEU          
SEQRES   4 A   94  GLU GLU GLU LEU GLY ILE GLN LEU LEU GLU ARG GLY SER          
SEQRES   5 A   94  ARG PRO VAL LYS THR THR PRO GLU GLY HIS PHE PHE TYR          
SEQRES   6 A   94  GLN TYR ALA ILE LYS LEU LEU SER ASN VAL ASP GLN MET          
SEQRES   7 A   94  VAL SER MET THR LYS ARG ILE ALA SER GLY HIS HIS HIS          
SEQRES   8 A   94  HIS HIS HIS                                                  
HET     NA  A  95       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   2   NA    NA 1+                                                        
FORMUL   3  HOH   *97(H2 O)                                                     
HELIX    1   1 GLU A    2  GLN A   16  1                                  15    
HELIX    2   2 SER A   17  LEU A   25  1                                   9    
HELIX    3   3 ALA A   28  GLY A   44  1                                  17    
HELIX    4   4 THR A   58  SER A   87  1                                  30    
LINK         OE1 GLU A   2                NA    NA A  95     1555   1555  2.00  
CISPEP   1 ARG A   53    PRO A   54          0        -2.58                     
SITE     1 AC1  2 GLU A   2  LEU A   3                                          
CRYST1   33.360   84.146   68.734  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.029976  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011884  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014549        0.00000                         
(ATOM LINES ARE NOT SHOWN.)

DBGET integrated database retrieval system