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Database: PDB
Entry: 3A4K
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HEADER    HYDROLASE/DNA                           09-JUL-09   3A4K              
TITLE     CRYSTAL STRUCTURAL ANALYSIS OF HINDIII RESTRICTION ENDONUCLEASE IN    
TITLE    2 COMPLEX WITH COGNATE DNA AND DIVALENT CATIONS AT 2.17 ANGSTROM       
TITLE    3 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYPE-2 RESTRICTION ENZYME HINDIII;                         
COMPND   3 CHAIN: A, C, B, D;                                                   
COMPND   4 SYNONYM: HINDIIIR, R.HINDIII, TYPE II RESTRICTION ENZYME HINDIII,    
COMPND   5 ENDONUCLEASE HINDIII;                                                
COMPND   6 EC: 3.1.21.4;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: DNA (5'-D(*GP*CP*CP*A)-3');                                
COMPND  10 CHAIN: E, G, I, K;                                                   
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 OTHER_DETAILS: 5'-FRAGMENT OF CLEAVED COGNATE DNA WITH HINDIIIR;     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA (5'-D(P*AP*GP*CP*TP*TP*GP*GP*C)-3');                   
COMPND  15 CHAIN: F, H, J, L;                                                   
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 OTHER_DETAILS: 3'-FRAGMENT OF CLEAVED COGNATE DNA WITH HINDIIIR;     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: DNA (5'-D(*GP*CP*CP*AP*AP*GP*CP*TP*TP*GP*GP*C)-3');        
COMPND  20 CHAIN: M, N;                                                         
COMPND  21 ENGINEERED: YES;                                                     
COMPND  22 OTHER_DETAILS: COGNATE DNA                                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;                         
SOURCE   3 ORGANISM_TAXID: 71421;                                               
SOURCE   4 STRAIN: RD KW20;                                                     
SOURCE   5 GENE: HINDIIIR;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET16B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 SYNTHETIC: YES;                                                      
SOURCE  15 MOL_ID: 4;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 OTHER_DETAILS: THIS DNA SEQUENCE SYNTHESIZED CHEMICALLY CONTAINS     
SOURCE  18 COGNATE HINDIIIR RECOGNITION SEQUENCE AND ELONGATED SCAFFOLDS ON     
SOURCE  19 BOTH SIDES                                                           
KEYWDS    TYPE II RESTRICTION ENZYME HINDIII(E.C.3.1.21.4)/DNA, HYDROLASE-DNA   
KEYWDS   2 COMPLEX, ENDONUCLEASE, HYDROLASE, NUCLEASE, RESTRICTION SYSTEM       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.WATANABE,C.SATO,Y.TAKASAKI,I.TANAKA                                 
REVDAT   3   05-MAR-14 3A4K    1       JRNL                                     
REVDAT   2   13-JUL-11 3A4K    1       VERSN                                    
REVDAT   1   20-OCT-09 3A4K    0                                                
JRNL        AUTH   N.WATANABE,Y.TAKASAKI,C.SATO,S.ANDO,I.TANAKA                 
JRNL        TITL   STRUCTURES OF RESTRICTION ENDONUCLEASE HINDIII IN COMPLEX    
JRNL        TITL 2 WITH ITS COGNATE DNA AND DIVALENT CATIONS                    
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  65  1326 2009              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   19966419                                                     
JRNL        DOI    10.1107/S0907444909041134                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.17 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0062                                      
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) : 2.17                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 100399                         
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) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5018                            
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) : 2.17                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6827                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.32                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 374                          
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9775                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1462                                    
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 573                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.05000                                              
REMARK   3    B22 (A**2) : 0.51000                                              
REMARK   3    B33 (A**2) : -0.17000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.53000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.195         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.176         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.125         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.791         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11594 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15887 ; 1.779 ; 2.133       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1182 ; 6.215 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   485 ;41.522 ;25.753       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1991 ;16.570 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;15.567 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1783 ; 0.120 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8057 ; 0.008 ; 0.020       
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):  5954 ; 0.969 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9619 ; 1.829 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5640 ; 2.804 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6268 ; 4.287 ; 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 : 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: NULL                                      
REMARK   4                                                                      
REMARK   4 3A4K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JUL-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB028802.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4R                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 100664                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.170                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
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 2E52                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, AMMONIUM ACETATE, MAGNESIUM     
REMARK 280  ION, GLYCEROL, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE   
REMARK 280  293K                                                                
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       66.10550            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14170 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F, J, E, I                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14180 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H, L, K, G                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 4460 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N                                  
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     HIS A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     LYS A     1                                                      
REMARK 465     ARG A    88                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     MET C     0                                                      
REMARK 465     LYS C     1                                                      
REMARK 465     ARG C    88                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     LYS B     1                                                      
REMARK 465     ARG B    88                                                      
REMARK 465     HIS D    -1                                                      
REMARK 465     MET D     0                                                      
REMARK 465     LYS D     1                                                      
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    GLU A 181   CD    GLU A 181   OE2     0.082                       
REMARK 500    GLU B 282   CG    GLU B 282   CD      0.094                       
REMARK 500     DA F   1   P      DA F   1   OP3    -0.124                       
REMARK 500     DG F   2   O3'    DG F   2   C3'    -0.055                       
REMARK 500     DT F   4   C6     DT F   4   N1      0.047                       
REMARK 500     DA H   1   P      DA H   1   OP3    -0.119                       
REMARK 500     DA H   1   O3'    DA H   1   C3'    -0.040                       
REMARK 500     DA J   1   P      DA J   1   OP3    -0.141                       
REMARK 500     DC K   3   O3'    DC K   3   C3'    -0.049                       
REMARK 500     DA L   1   P      DA L   1   OP3    -0.153                       
REMARK 500     DG L   6   O3'    DG L   6   C3'    -0.038                       
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    ARG C 116   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG C 116   NE  -  CZ  -  NH1 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG C 116   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    ARG D  88   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG D  88   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500     DC E   2   O4' -  C1' -  N1  ANGL. DEV. =  -6.1 DEGREES          
REMARK 500     DA E   4   O4' -  C1' -  N9  ANGL. DEV. =  -8.1 DEGREES          
REMARK 500     DA F   1   O4' -  C4' -  C3' ANGL. DEV. =  -5.7 DEGREES          
REMARK 500     DG F   2   O5' -  C5' -  C4' ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DG F   2   O4' -  C1' -  N9  ANGL. DEV. =   3.9 DEGREES          
REMARK 500     DG F   2   C2  -  N3  -  C4  ANGL. DEV. =   3.6 DEGREES          
REMARK 500     DG F   2   N7  -  C8  -  N9  ANGL. DEV. =  -3.4 DEGREES          
REMARK 500     DC F   3   O4' -  C4' -  C3' ANGL. DEV. =  -6.4 DEGREES          
REMARK 500     DT F   5   O4' -  C1' -  N1  ANGL. DEV. =  -8.2 DEGREES          
REMARK 500     DG F   6   C3' -  C2' -  C1' ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DA G   4   O4' -  C1' -  N9  ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DA H   1   O4' -  C4' -  C3' ANGL. DEV. =  -5.4 DEGREES          
REMARK 500     DA H   1   C3' -  C2' -  C1' ANGL. DEV. =  -9.0 DEGREES          
REMARK 500     DG H   2   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DC H   3   O4' -  C4' -  C3' ANGL. DEV. =  -4.7 DEGREES          
REMARK 500     DC H   3   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DT H   5   O5' -  C5' -  C4' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DT H   5   O4' -  C1' -  N1  ANGL. DEV. =  -7.1 DEGREES          
REMARK 500     DT H   5   C4  -  C5  -  C7  ANGL. DEV. =   5.0 DEGREES          
REMARK 500     DT H   5   C6  -  C5  -  C7  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500     DG H   6   O4' -  C1' -  N9  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DA I   4   O4' -  C1' -  N9  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DA J   1   O4' -  C4' -  C3' ANGL. DEV. =  -4.3 DEGREES          
REMARK 500     DA J   1   C3' -  C2' -  C1' ANGL. DEV. =  -6.1 DEGREES          
REMARK 500     DG J   2   O4' -  C1' -  N9  ANGL. DEV. =   4.6 DEGREES          
REMARK 500     DC J   3   C5  -  C4  -  N4  ANGL. DEV. =   4.4 DEGREES          
REMARK 500     DT J   5   O4' -  C1' -  N1  ANGL. DEV. =  -6.5 DEGREES          
REMARK 500     DT J   5   N3  -  C4  -  O4  ANGL. DEV. =   4.6 DEGREES          
REMARK 500     DG J   6   C3' -  C2' -  C1' ANGL. DEV. =  -6.0 DEGREES          
REMARK 500     DG J   6   O4' -  C1' -  N9  ANGL. DEV. =   3.4 DEGREES          
REMARK 500     DG J   6   C5  -  C6  -  N1  ANGL. DEV. =   4.3 DEGREES          
REMARK 500     DC J   8   C2  -  N3  -  C4  ANGL. DEV. =   3.5 DEGREES          
REMARK 500     DC J   8   C4  -  C5  -  C6  ANGL. DEV. =  -4.0 DEGREES          
REMARK 500     DC K   2   N3  -  C4  -  N4  ANGL. DEV. =  -7.0 DEGREES          
REMARK 500     DC K   2   C5  -  C4  -  N4  ANGL. DEV. =   5.3 DEGREES          
REMARK 500     DC K   3   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DA K   4   O4' -  C1' -  N9  ANGL. DEV. = -10.8 DEGREES          
REMARK 500     DA L   1   O4' -  C4' -  C3' ANGL. DEV. =  -4.1 DEGREES          
REMARK 500     DA L   1   N1  -  C2  -  N3  ANGL. DEV. =  -3.4 DEGREES          
REMARK 500     DG L   2   O4' -  C4' -  C3' ANGL. DEV. =  -3.2 DEGREES          
REMARK 500     DC L   3   O4' -  C4' -  C3' ANGL. DEV. =  -4.7 DEGREES          
REMARK 500     DT L   4   O4' -  C1' -  N1  ANGL. DEV. =  -4.6 DEGREES          
REMARK 500     DT L   5   O4' -  C1' -  N1  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500     DG L   6   C3' -  C2' -  C1' ANGL. DEV. =  -6.4 DEGREES          
REMARK 500     DG L   6   C5  -  C6  -  N1  ANGL. DEV. =   3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      81 ANGLE DEVIATIONS.                             
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  56       -2.59     80.09                                   
REMARK 500    ASN A  79       36.89     74.36                                   
REMARK 500    PHE A 101     -162.99   -125.11                                   
REMARK 500    THR A 117     -103.64    -86.61                                   
REMARK 500    GLU A 134     -116.85     55.49                                   
REMARK 500    THR A 151      -57.27   -124.02                                   
REMARK 500    SER C  56       -5.62     67.72                                   
REMARK 500    ASN C  79       41.50     73.10                                   
REMARK 500    PHE C 101     -158.90   -120.09                                   
REMARK 500    THR C 117     -101.33    -92.62                                   
REMARK 500    GLU C 134     -111.76     53.40                                   
REMARK 500    THR C 151      -54.76   -125.45                                   
REMARK 500    SER C 153      145.57   -179.39                                   
REMARK 500    ASN C 261       48.32   -103.85                                   
REMARK 500    LEU B  34      134.06    -38.82                                   
REMARK 500    ASN B  79       37.10     78.58                                   
REMARK 500    PHE B 101     -161.28   -125.14                                   
REMARK 500    THR B 117     -106.40    -83.19                                   
REMARK 500    GLU B 134     -119.54     54.75                                   
REMARK 500    THR B 151      -53.58   -122.89                                   
REMARK 500    ASN D  79       40.63     73.02                                   
REMARK 500    ARG D  88      -87.57   -100.17                                   
REMARK 500    PHE D 101     -168.76   -120.48                                   
REMARK 500    THR D 117     -103.19    -82.84                                   
REMARK 500    GLU D 134     -121.57     59.35                                   
REMARK 500    THR D 151      -55.58   -129.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR D  16        24.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 MG ION WAS USED IN THE EXPERIMENT, BUT METAL IONS AT SITES O, P, Q   
REMARK 600 AND R IN THE STRUCTURE HAVE BEEN DEDUCED AS MN ION USING REFINED     
REMARK 600 TEMPERATURE FACTORS.                                                 
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 A 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2  DA E   4   O3' 168.4                                              
REMARK 620 3  DA F   1   OP2 102.1  87.7                                        
REMARK 620 4 HOH A 320   O    97.1  89.7  85.7                                  
REMARK 620 5 HOH A 386   O    90.8  80.5 106.0 164.3                            
REMARK 620 6 HOH E 258   O    93.3  78.2 161.8  82.9  83.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 302  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD2                                                    
REMARK 620 2 ASP A 108   OD2  85.3                                              
REMARK 620 3 ALA A 109   O   114.7  88.9                                        
REMARK 620 4  DA F   1   OP3 143.5  89.4 101.3                                  
REMARK 620 5 HOH A 570   O    89.6 168.2  83.6 100.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  93   OD1                                                    
REMARK 620 2  DA G   4   O3' 162.1                                              
REMARK 620 3  DA H   1   OP3  96.7  87.8                                        
REMARK 620 4 HOH C 421   O    75.7  86.5 102.1                                  
REMARK 620 5 HOH H  84   O   102.1  95.7  78.7 177.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 302  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  93   OD2                                                    
REMARK 620 2 ASP C 108   OD2  84.3                                              
REMARK 620 3 ALA C 109   O   107.8  85.2                                        
REMARK 620 4  DA H   1   OP1 158.3  92.7  93.3                                  
REMARK 620 5 HOH C 573   O    88.1 163.5  83.1  99.6                            
REMARK 620 6  DA H   1   OP3 101.2  95.5 151.0  57.7 100.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  93   OD1                                                    
REMARK 620 2  DA I   4   O3' 154.8                                              
REMARK 620 3  DA J   1   OP2  94.7  93.8                                        
REMARK 620 4 HOH B 342   O    78.1  77.5  96.2                                  
REMARK 620 5 HOH B 378   O    88.7  85.1 174.1  89.2                            
REMARK 620 6 HOH B 333   O    95.2 109.4  82.9 173.1  92.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 302  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  93   OD2                                                    
REMARK 620 2 ASP B 108   OD1  86.0                                              
REMARK 620 3 ALA B 109   O   110.4  90.2                                        
REMARK 620 4  DA J   1   OP3 152.9  94.4  96.8                                  
REMARK 620 5 HOH B 494   O    82.4 163.1  82.3 101.6                            
REMARK 620 6  DA J   1   OP2  96.3  95.7 153.1  56.7  97.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  93   OD1                                                    
REMARK 620 2  DA K   4   O3' 164.6                                              
REMARK 620 3  DA L   1   OP2 100.8  84.5                                        
REMARK 620 4 HOH K 337   O    95.1  81.0 163.6                                  
REMARK 620 5 HOH D 572   O    83.5  81.2 102.3  83.3                            
REMARK 620 6 HOH L 168   O   100.0  95.3  78.4  95.1 176.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 302  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  93   OD2                                                    
REMARK 620 2 ASP D 108   OD2  83.0                                              
REMARK 620 3 ALA D 109   O   111.4  88.6                                        
REMARK 620 4  DA L   1   OP3 150.3  93.8  97.9                                  
REMARK 620 5 HOH D 571   O    89.7 167.8  84.9  97.4                            
REMARK 620 6  DA L   1   OP2  97.6  93.8 150.9  53.0  96.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED                              
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 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 303                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2E52   RELATED DB: PDB                                   
REMARK 900 HINDIII/DNA COMPLEX (NOT CLEAVED)                                    
DBREF  3A4K A    0   299  UNP    P43870   T2D3_HAEIN       1    300             
DBREF  3A4K C    0   299  UNP    P43870   T2D3_HAEIN       1    300             
DBREF  3A4K B    0   299  UNP    P43870   T2D3_HAEIN       1    300             
DBREF  3A4K D    0   299  UNP    P43870   T2D3_HAEIN       1    300             
DBREF  3A4K E    1     4  PDB    3A4K     3A4K             1      4             
DBREF  3A4K F    1     8  PDB    3A4K     3A4K             1      8             
DBREF  3A4K G    1     4  PDB    3A4K     3A4K             1      4             
DBREF  3A4K H    1     8  PDB    3A4K     3A4K             1      8             
DBREF  3A4K I    1     4  PDB    3A4K     3A4K             1      4             
DBREF  3A4K J    1     8  PDB    3A4K     3A4K             1      8             
DBREF  3A4K K    1     4  PDB    3A4K     3A4K             1      4             
DBREF  3A4K L    1     8  PDB    3A4K     3A4K             1      8             
DBREF  3A4K M    1    12  PDB    3A4K     3A4K             1     12             
DBREF  3A4K N    1    12  PDB    3A4K     3A4K             1     12             
SEQADV 3A4K HIS A   -1  UNP  P43870              EXPRESSION TAG                 
SEQADV 3A4K HIS C   -1  UNP  P43870              EXPRESSION TAG                 
SEQADV 3A4K HIS B   -1  UNP  P43870              EXPRESSION TAG                 
SEQADV 3A4K HIS D   -1  UNP  P43870              EXPRESSION TAG                 
SEQRES   1 A  301  HIS MET LYS LYS SER ALA LEU GLU LYS LEU LEU SER LEU          
SEQRES   2 A  301  ILE GLU ASN LEU THR ASN GLN GLU PHE LYS GLN ALA THR          
SEQRES   3 A  301  ASN SER LEU ILE SER PHE ILE TYR LYS LEU ASN ARG ASN          
SEQRES   4 A  301  GLU VAL ILE GLU LEU VAL ARG SER ILE GLY ILE LEU PRO          
SEQRES   5 A  301  GLU ALA ILE LYS PRO SER SER THR GLN GLU LYS LEU PHE          
SEQRES   6 A  301  SER LYS ALA GLY ASP ILE VAL LEU ALA LYS ALA PHE GLN          
SEQRES   7 A  301  LEU LEU ASN LEU ASN SER LYS PRO LEU GLU GLN ARG GLY          
SEQRES   8 A  301  ASN ALA GLY ASP VAL ILE ALA LEU SER LYS GLU PHE ASN          
SEQRES   9 A  301  TYR GLY LEU VAL ALA ASP ALA LYS SER PHE ARG LEU SER          
SEQRES  10 A  301  ARG THR ALA LYS ASN GLN LYS ASP PHE LYS VAL LYS ALA          
SEQRES  11 A  301  LEU SER GLU TRP ARG GLU ASP LYS ASP TYR ALA VAL LEU          
SEQRES  12 A  301  THR ALA PRO PHE PHE GLN TYR PRO THR THR LYS SER GLN          
SEQRES  13 A  301  ILE PHE LYS GLN SER LEU ASP GLU ASN VAL LEU LEU PHE          
SEQRES  14 A  301  SER TRP GLU HIS LEU ALA ILE LEU LEU GLN LEU ASP LEU          
SEQRES  15 A  301  GLU GLU THR ASN ILE PHE SER PHE GLU GLN LEU TRP ASN          
SEQRES  16 A  301  PHE PRO LYS LYS GLN SER LYS LYS THR SER VAL SER ASP          
SEQRES  17 A  301  ALA GLU ASN ASN PHE MET ARG ASP PHE ASN LYS TYR PHE          
SEQRES  18 A  301  MET ASP LEU PHE LYS ILE ASP LYS ASP THR LEU ASN GLN          
SEQRES  19 A  301  LEU LEU GLN LYS GLU ILE ASN PHE ILE GLU GLU ARG SER          
SEQRES  20 A  301  LEU ILE GLU LYS GLU TYR TRP LYS LYS GLN ILE ASN ILE          
SEQRES  21 A  301  ILE LYS ASN PHE THR ARG GLU GLU ALA ILE GLU ALA LEU          
SEQRES  22 A  301  LEU LYS ASP ILE ASN MET SER SER LYS ILE GLU THR ILE          
SEQRES  23 A  301  ASP SER PHE ILE LYS GLY ILE LYS SER ASN ASP ARG LEU          
SEQRES  24 A  301  TYR LEU                                                      
SEQRES   1 C  301  HIS MET LYS LYS SER ALA LEU GLU LYS LEU LEU SER LEU          
SEQRES   2 C  301  ILE GLU ASN LEU THR ASN GLN GLU PHE LYS GLN ALA THR          
SEQRES   3 C  301  ASN SER LEU ILE SER PHE ILE TYR LYS LEU ASN ARG ASN          
SEQRES   4 C  301  GLU VAL ILE GLU LEU VAL ARG SER ILE GLY ILE LEU PRO          
SEQRES   5 C  301  GLU ALA ILE LYS PRO SER SER THR GLN GLU LYS LEU PHE          
SEQRES   6 C  301  SER LYS ALA GLY ASP ILE VAL LEU ALA LYS ALA PHE GLN          
SEQRES   7 C  301  LEU LEU ASN LEU ASN SER LYS PRO LEU GLU GLN ARG GLY          
SEQRES   8 C  301  ASN ALA GLY ASP VAL ILE ALA LEU SER LYS GLU PHE ASN          
SEQRES   9 C  301  TYR GLY LEU VAL ALA ASP ALA LYS SER PHE ARG LEU SER          
SEQRES  10 C  301  ARG THR ALA LYS ASN GLN LYS ASP PHE LYS VAL LYS ALA          
SEQRES  11 C  301  LEU SER GLU TRP ARG GLU ASP LYS ASP TYR ALA VAL LEU          
SEQRES  12 C  301  THR ALA PRO PHE PHE GLN TYR PRO THR THR LYS SER GLN          
SEQRES  13 C  301  ILE PHE LYS GLN SER LEU ASP GLU ASN VAL LEU LEU PHE          
SEQRES  14 C  301  SER TRP GLU HIS LEU ALA ILE LEU LEU GLN LEU ASP LEU          
SEQRES  15 C  301  GLU GLU THR ASN ILE PHE SER PHE GLU GLN LEU TRP ASN          
SEQRES  16 C  301  PHE PRO LYS LYS GLN SER LYS LYS THR SER VAL SER ASP          
SEQRES  17 C  301  ALA GLU ASN ASN PHE MET ARG ASP PHE ASN LYS TYR PHE          
SEQRES  18 C  301  MET ASP LEU PHE LYS ILE ASP LYS ASP THR LEU ASN GLN          
SEQRES  19 C  301  LEU LEU GLN LYS GLU ILE ASN PHE ILE GLU GLU ARG SER          
SEQRES  20 C  301  LEU ILE GLU LYS GLU TYR TRP LYS LYS GLN ILE ASN ILE          
SEQRES  21 C  301  ILE LYS ASN PHE THR ARG GLU GLU ALA ILE GLU ALA LEU          
SEQRES  22 C  301  LEU LYS ASP ILE ASN MET SER SER LYS ILE GLU THR ILE          
SEQRES  23 C  301  ASP SER PHE ILE LYS GLY ILE LYS SER ASN ASP ARG LEU          
SEQRES  24 C  301  TYR LEU                                                      
SEQRES   1 B  301  HIS MET LYS LYS SER ALA LEU GLU LYS LEU LEU SER LEU          
SEQRES   2 B  301  ILE GLU ASN LEU THR ASN GLN GLU PHE LYS GLN ALA THR          
SEQRES   3 B  301  ASN SER LEU ILE SER PHE ILE TYR LYS LEU ASN ARG ASN          
SEQRES   4 B  301  GLU VAL ILE GLU LEU VAL ARG SER ILE GLY ILE LEU PRO          
SEQRES   5 B  301  GLU ALA ILE LYS PRO SER SER THR GLN GLU LYS LEU PHE          
SEQRES   6 B  301  SER LYS ALA GLY ASP ILE VAL LEU ALA LYS ALA PHE GLN          
SEQRES   7 B  301  LEU LEU ASN LEU ASN SER LYS PRO LEU GLU GLN ARG GLY          
SEQRES   8 B  301  ASN ALA GLY ASP VAL ILE ALA LEU SER LYS GLU PHE ASN          
SEQRES   9 B  301  TYR GLY LEU VAL ALA ASP ALA LYS SER PHE ARG LEU SER          
SEQRES  10 B  301  ARG THR ALA LYS ASN GLN LYS ASP PHE LYS VAL LYS ALA          
SEQRES  11 B  301  LEU SER GLU TRP ARG GLU ASP LYS ASP TYR ALA VAL LEU          
SEQRES  12 B  301  THR ALA PRO PHE PHE GLN TYR PRO THR THR LYS SER GLN          
SEQRES  13 B  301  ILE PHE LYS GLN SER LEU ASP GLU ASN VAL LEU LEU PHE          
SEQRES  14 B  301  SER TRP GLU HIS LEU ALA ILE LEU LEU GLN LEU ASP LEU          
SEQRES  15 B  301  GLU GLU THR ASN ILE PHE SER PHE GLU GLN LEU TRP ASN          
SEQRES  16 B  301  PHE PRO LYS LYS GLN SER LYS LYS THR SER VAL SER ASP          
SEQRES  17 B  301  ALA GLU ASN ASN PHE MET ARG ASP PHE ASN LYS TYR PHE          
SEQRES  18 B  301  MET ASP LEU PHE LYS ILE ASP LYS ASP THR LEU ASN GLN          
SEQRES  19 B  301  LEU LEU GLN LYS GLU ILE ASN PHE ILE GLU GLU ARG SER          
SEQRES  20 B  301  LEU ILE GLU LYS GLU TYR TRP LYS LYS GLN ILE ASN ILE          
SEQRES  21 B  301  ILE LYS ASN PHE THR ARG GLU GLU ALA ILE GLU ALA LEU          
SEQRES  22 B  301  LEU LYS ASP ILE ASN MET SER SER LYS ILE GLU THR ILE          
SEQRES  23 B  301  ASP SER PHE ILE LYS GLY ILE LYS SER ASN ASP ARG LEU          
SEQRES  24 B  301  TYR LEU                                                      
SEQRES   1 D  301  HIS MET LYS LYS SER ALA LEU GLU LYS LEU LEU SER LEU          
SEQRES   2 D  301  ILE GLU ASN LEU THR ASN GLN GLU PHE LYS GLN ALA THR          
SEQRES   3 D  301  ASN SER LEU ILE SER PHE ILE TYR LYS LEU ASN ARG ASN          
SEQRES   4 D  301  GLU VAL ILE GLU LEU VAL ARG SER ILE GLY ILE LEU PRO          
SEQRES   5 D  301  GLU ALA ILE LYS PRO SER SER THR GLN GLU LYS LEU PHE          
SEQRES   6 D  301  SER LYS ALA GLY ASP ILE VAL LEU ALA LYS ALA PHE GLN          
SEQRES   7 D  301  LEU LEU ASN LEU ASN SER LYS PRO LEU GLU GLN ARG GLY          
SEQRES   8 D  301  ASN ALA GLY ASP VAL ILE ALA LEU SER LYS GLU PHE ASN          
SEQRES   9 D  301  TYR GLY LEU VAL ALA ASP ALA LYS SER PHE ARG LEU SER          
SEQRES  10 D  301  ARG THR ALA LYS ASN GLN LYS ASP PHE LYS VAL LYS ALA          
SEQRES  11 D  301  LEU SER GLU TRP ARG GLU ASP LYS ASP TYR ALA VAL LEU          
SEQRES  12 D  301  THR ALA PRO PHE PHE GLN TYR PRO THR THR LYS SER GLN          
SEQRES  13 D  301  ILE PHE LYS GLN SER LEU ASP GLU ASN VAL LEU LEU PHE          
SEQRES  14 D  301  SER TRP GLU HIS LEU ALA ILE LEU LEU GLN LEU ASP LEU          
SEQRES  15 D  301  GLU GLU THR ASN ILE PHE SER PHE GLU GLN LEU TRP ASN          
SEQRES  16 D  301  PHE PRO LYS LYS GLN SER LYS LYS THR SER VAL SER ASP          
SEQRES  17 D  301  ALA GLU ASN ASN PHE MET ARG ASP PHE ASN LYS TYR PHE          
SEQRES  18 D  301  MET ASP LEU PHE LYS ILE ASP LYS ASP THR LEU ASN GLN          
SEQRES  19 D  301  LEU LEU GLN LYS GLU ILE ASN PHE ILE GLU GLU ARG SER          
SEQRES  20 D  301  LEU ILE GLU LYS GLU TYR TRP LYS LYS GLN ILE ASN ILE          
SEQRES  21 D  301  ILE LYS ASN PHE THR ARG GLU GLU ALA ILE GLU ALA LEU          
SEQRES  22 D  301  LEU LYS ASP ILE ASN MET SER SER LYS ILE GLU THR ILE          
SEQRES  23 D  301  ASP SER PHE ILE LYS GLY ILE LYS SER ASN ASP ARG LEU          
SEQRES  24 D  301  TYR LEU                                                      
SEQRES   1 E    4   DG  DC  DC  DA                                              
SEQRES   1 F    8   DA  DG  DC  DT  DT  DG  DG  DC                              
SEQRES   1 G    4   DG  DC  DC  DA                                              
SEQRES   1 H    8   DA  DG  DC  DT  DT  DG  DG  DC                              
SEQRES   1 I    4   DG  DC  DC  DA                                              
SEQRES   1 J    8   DA  DG  DC  DT  DT  DG  DG  DC                              
SEQRES   1 K    4   DG  DC  DC  DA                                              
SEQRES   1 L    8   DA  DG  DC  DT  DT  DG  DG  DC                              
SEQRES   1 M   12   DG  DC  DC  DA  DA  DG  DC  DT  DT  DG  DG  DC              
SEQRES   1 N   12   DG  DC  DC  DA  DA  DG  DC  DT  DT  DG  DG  DC              
HET     MG  A 301       1                                                       
HET     MN  A 302       1                                                       
HET    GOL  A 300       6                                                       
HET     MG  C 301       1                                                       
HET     MN  C 302       1                                                       
HET    ACT  C 300       4                                                       
HET     MG  B 301       1                                                       
HET     MN  B 302       1                                                       
HET    ACT  B 300       4                                                       
HET    ACT  B 303       4                                                       
HET     MG  D 301       1                                                       
HET     MN  D 302       1                                                       
HET    GOL  D 300       6                                                       
HET    ACT  D 303       4                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     GOL GLYCEROL                                                         
HETNAM     ACT ACETATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL  15   MG    4(MG 2+)                                                     
FORMUL  16   MN    4(MN 2+)                                                     
FORMUL  17  GOL    2(C3 H8 O3)                                                  
FORMUL  20  ACT    4(C2 H3 O2 1-)                                               
FORMUL  29  HOH   *573(H2 O)                                                    
HELIX    1   1 ALA A    4  GLU A   13  1                                  10    
HELIX    2   2 PHE A   20  LYS A   33  1                                  14    
HELIX    3   3 ARG A   36  ILE A   46  1                                  11    
HELIX    4   4 THR A   58  LEU A   77  1                                  20    
HELIX    5   5 GLN A  121  PHE A  124  1                                   4    
HELIX    6   6 VAL A  126  TRP A  132  1                                   7    
HELIX    7   7 PHE A  145  GLN A  147  5                                   3    
HELIX    8   8 GLN A  154  GLU A  162  1                                   9    
HELIX    9   9 TRP A  169  GLN A  177  1                                   9    
HELIX   10  10 GLU A  189  SER A  199  1                                  11    
HELIX   11  11 VAL A  204  ASP A  206  5                                   3    
HELIX   12  12 MET A  212  PHE A  223  1                                  12    
HELIX   13  13 LYS A  227  ILE A  258  1                                  32    
HELIX   14  14 ARG A  264  ASP A  274  1                                  11    
HELIX   15  15 MET A  277  LYS A  292  1                                  16    
HELIX   16  16 ASN A  294  LEU A  297  5                                   4    
HELIX   17  17 ALA C    4  ASN C   14  1                                  11    
HELIX   18  18 PHE C   20  TYR C   32  1                                  13    
HELIX   19  19 ARG C   36  ILE C   46  1                                  11    
HELIX   20  20 THR C   58  LEU C   77  1                                  20    
HELIX   21  21 GLN C  121  PHE C  124  1                                   4    
HELIX   22  22 VAL C  126  TRP C  132  1                                   7    
HELIX   23  23 PHE C  145  GLN C  147  5                                   3    
HELIX   24  24 GLN C  154  GLU C  162  1                                   9    
HELIX   25  25 TRP C  169  GLN C  177  1                                   9    
HELIX   26  26 GLU C  189  SER C  199  1                                  11    
HELIX   27  27 VAL C  204  ASP C  206  5                                   3    
HELIX   28  28 MET C  212  PHE C  223  1                                  12    
HELIX   29  29 LYS C  227  LYS C  260  1                                  34    
HELIX   30  30 ARG C  264  ILE C  275  1                                  12    
HELIX   31  31 MET C  277  LYS C  292  1                                  16    
HELIX   32  32 ASN C  294  LEU C  297  5                                   4    
HELIX   33  33 ALA B    4  LEU B   15  1                                  12    
HELIX   34  34 PHE B   20  LYS B   33  1                                  14    
HELIX   35  35 ARG B   36  ILE B   46  1                                  11    
HELIX   36  36 THR B   58  LEU B   77  1                                  20    
HELIX   37  37 GLN B  121  PHE B  124  1                                   4    
HELIX   38  38 VAL B  126  TRP B  132  1                                   7    
HELIX   39  39 PHE B  145  GLN B  147  5                                   3    
HELIX   40  40 GLN B  154  GLU B  162  1                                   9    
HELIX   41  41 TRP B  169  GLN B  177  1                                   9    
HELIX   42  42 GLU B  189  LYS B  200  1                                  12    
HELIX   43  43 MET B  212  PHE B  223  1                                  12    
HELIX   44  44 LYS B  227  LYS B  260  1                                  34    
HELIX   45  45 ARG B  264  ILE B  275  1                                  12    
HELIX   46  46 MET B  277  ILE B  291  1                                  15    
HELIX   47  47 ASN B  294  LEU B  297  5                                   4    
HELIX   48  48 ALA D    4  GLU D   13  1                                  10    
HELIX   49  49 PHE D   20  TYR D   32  1                                  13    
HELIX   50  50 ARG D   36  SER D   45  1                                  10    
HELIX   51  51 THR D   58  LEU D   77  1                                  20    
HELIX   52  52 GLN D  121  PHE D  124  1                                   4    
HELIX   53  53 VAL D  126  TRP D  132  1                                   7    
HELIX   54  54 PHE D  145  GLN D  147  5                                   3    
HELIX   55  55 GLN D  154  GLU D  162  1                                   9    
HELIX   56  56 TRP D  169  GLN D  177  1                                   9    
HELIX   57  57 GLU D  189  SER D  199  1                                  11    
HELIX   58  58 MET D  212  PHE D  223  1                                  12    
HELIX   59  59 LYS D  227  LYS D  260  1                                  34    
HELIX   60  60 ARG D  264  ILE D  275  1                                  12    
HELIX   61  61 MET D  277  ILE D  291  1                                  15    
HELIX   62  62 ASN D  294  LEU D  297  5                                   4    
SHEET    1   A 2 ILE A  48  LEU A  49  0                                        
SHEET    2   A 2 PHE A 112  ARG A 113  1  O  PHE A 112   N  LEU A  49           
SHEET    1   B 5 LEU A  80  PRO A  84  0                                        
SHEET    2   B 5 VAL A  94  SER A  98 -1  O  LEU A  97   N  ASN A  81           
SHEET    3   B 5 GLY A 104  ALA A 109 -1  O  ALA A 107   N  VAL A  94           
SHEET    4   B 5 TYR A 138  ALA A 143  1  O  THR A 142   N  ASP A 108           
SHEET    5   B 5 VAL A 164  SER A 168  1  O  PHE A 167   N  LEU A 141           
SHEET    1   C 2 ILE C  48  LEU C  49  0                                        
SHEET    2   C 2 PHE C 112  ARG C 113  1  O  PHE C 112   N  LEU C  49           
SHEET    1   D 5 LEU C  80  PRO C  84  0                                        
SHEET    2   D 5 VAL C  94  SER C  98 -1  O  LEU C  97   N  ASN C  81           
SHEET    3   D 5 GLY C 104  ALA C 109 -1  O  ALA C 107   N  VAL C  94           
SHEET    4   D 5 TYR C 138  ALA C 143  1  O  THR C 142   N  ASP C 108           
SHEET    5   D 5 LEU C 165  SER C 168  1  O  LEU C 165   N  LEU C 141           
SHEET    1   E 2 ILE B  48  LEU B  49  0                                        
SHEET    2   E 2 PHE B 112  ARG B 113  1  O  PHE B 112   N  LEU B  49           
SHEET    1   F 5 LEU B  80  PRO B  84  0                                        
SHEET    2   F 5 VAL B  94  SER B  98 -1  O  LEU B  97   N  ASN B  81           
SHEET    3   F 5 GLY B 104  ALA B 109 -1  O  ALA B 107   N  VAL B  94           
SHEET    4   F 5 TYR B 138  ALA B 143  1  O  THR B 142   N  ASP B 108           
SHEET    5   F 5 VAL B 164  SER B 168  1  O  LEU B 165   N  LEU B 141           
SHEET    1   G 2 ILE D  48  LEU D  49  0                                        
SHEET    2   G 2 PHE D 112  ARG D 113  1  O  PHE D 112   N  LEU D  49           
SHEET    1   H 5 LEU D  80  PRO D  84  0                                        
SHEET    2   H 5 VAL D  94  SER D  98 -1  O  LEU D  97   N  ASN D  81           
SHEET    3   H 5 GLY D 104  ALA D 109 -1  O  ALA D 107   N  VAL D  94           
SHEET    4   H 5 TYR D 138  ALA D 143  1  O  THR D 142   N  ASP D 108           
SHEET    5   H 5 LEU D 165  SER D 168  1  O  LEU D 165   N  LEU D 141           
LINK         OD1 ASP A  93                MG    MG A 301     1555   1555  1.92  
LINK         OD2 ASP A  93                MN    MN A 302     1555   1555  2.01  
LINK         OD2 ASP A 108                MN    MN A 302     1555   1555  2.12  
LINK         O   ALA A 109                MN    MN A 302     1555   1555  2.05  
LINK         OD1 ASP C  93                MG    MG C 301     1555   1555  2.15  
LINK         OD2 ASP C  93                MN    MN C 302     1555   1555  1.98  
LINK         OD2 ASP C 108                MN    MN C 302     1555   1555  2.23  
LINK         O   ALA C 109                MN    MN C 302     1555   1555  2.14  
LINK         OD1 ASP B  93                MG    MG B 301     1555   1555  2.08  
LINK         OD2 ASP B  93                MN    MN B 302     1555   1555  2.01  
LINK         OD1 ASP B 108                MN    MN B 302     1555   1555  2.16  
LINK         O   ALA B 109                MN    MN B 302     1555   1555  2.04  
LINK         OD1 ASP D  93                MG    MG D 301     1555   1555  1.91  
LINK         OD2 ASP D  93                MN    MN D 302     1555   1555  2.07  
LINK         OD2 ASP D 108                MN    MN D 302     1555   1555  2.17  
LINK         O   ALA D 109                MN    MN D 302     1555   1555  2.09  
LINK         O3'  DA E   4                MG    MG A 301     1555   1555  2.12  
LINK         OP3  DA F   1                MN    MN A 302     1555   1555  1.89  
LINK         OP2  DA F   1                MG    MG A 301     1555   1555  1.93  
LINK         O3'  DA G   4                MG    MG C 301     1555   1555  2.11  
LINK         OP3  DA H   1                MG    MG C 301     1555   1555  2.02  
LINK         OP1  DA H   1                MN    MN C 302     1555   1555  1.98  
LINK         O3'  DA I   4                MG    MG B 301     1555   1555  2.38  
LINK         OP3  DA J   1                MN    MN B 302     1555   1555  1.99  
LINK         OP2  DA J   1                MG    MG B 301     1555   1555  2.12  
LINK         O3'  DA K   4                MG    MG D 301     1555   1555  2.06  
LINK         OP3  DA L   1                MN    MN D 302     1555   1555  2.00  
LINK         OP2  DA L   1                MG    MG D 301     1555   1555  2.12  
LINK        MG    MG A 301                 O   HOH A 320     1555   1555  2.06  
LINK        MG    MG A 301                 O   HOH A 386     1555   1555  2.03  
LINK        MG    MG A 301                 O   HOH E 258     1555   1555  2.30  
LINK        MN    MN A 302                 O   HOH A 570     1555   1555  2.07  
LINK        MG    MG C 301                 O   HOH C 421     1555   1555  2.26  
LINK        MG    MG C 301                 O   HOH H  84     1555   1555  2.10  
LINK        MN    MN C 302                 O   HOH C 573     1555   1555  2.28  
LINK        MG    MG B 301                 O   HOH B 342     1555   1555  2.20  
LINK        MG    MG B 301                 O   HOH B 378     1555   1555  2.12  
LINK        MG    MG B 301                 O   HOH B 333     1555   1555  2.10  
LINK        MN    MN B 302                 O   HOH B 494     1555   1555  2.17  
LINK        MG    MG D 301                 O   HOH K 337     1555   1555  2.15  
LINK        MG    MG D 301                 O   HOH D 572     1555   1555  1.97  
LINK        MG    MG D 301                 O   HOH L 168     1555   1555  2.10  
LINK        MN    MN D 302                 O   HOH D 571     1555   1555  2.15  
LINK         OP2  DA J   1                MN    MN B 302     1555   1555  2.58  
LINK         OP3  DA H   1                MN    MN C 302     1555   1555  2.66  
LINK         OP2  DA L   1                MN    MN D 302     1555   1555  2.67  
SITE     1 AC1  6 ASP A  93  HOH A 320  HOH A 386   DA E   4                    
SITE     2 AC1  6 HOH E 258   DA F   1                                          
SITE     1 AC2  5 ASP A  93  ASP A 108  ALA A 109  HOH A 570                    
SITE     2 AC2  5  DA F   1                                                     
SITE     1 AC3  3 GLU A 100  ASN A 102  ASP D 221                               
SITE     1 AC4  5 ASP C  93  HOH C 421   DA G   4   DA H   1                    
SITE     2 AC4  5 HOH H  84                                                     
SITE     1 AC5  5 ASP C  93  ASP C 108  ALA C 109  HOH C 573                    
SITE     2 AC5  5  DA H   1                                                     
SITE     1 AC6  4 ASP C 161  SER C 199  THR C 202  VAL C 204                    
SITE     1 AC7  6 ASP B  93  HOH B 333  HOH B 342  HOH B 378                    
SITE     2 AC7  6  DA I   4   DA J   1                                          
SITE     1 AC8  5 ASP B  93  ASP B 108  ALA B 109  HOH B 494                    
SITE     2 AC8  5  DA J   1                                                     
SITE     1 AC9  4 LYS B  99  GLU B 100  ASN B 102  ASP C 221                    
SITE     1 BC1  3 ASP B 161  SER B 199  THR B 202                               
SITE     1 BC2  6 ASP D  93  HOH D 572   DA K   4  HOH K 337                    
SITE     2 BC2  6  DA L   1  HOH L 168                                          
SITE     1 BC3  5 ASP D  93  ASP D 108  ALA D 109  HOH D 571                    
SITE     2 BC3  5  DA L   1                                                     
SITE     1 BC4  6 LYS D 201  ASN D 209  ASN D 210  ASP D 214                    
SITE     2 BC4  6 HOH D 338  HOH D 376                                          
SITE     1 BC5  5 ASP D 161  SER D 199  THR D 202  SER D 203                    
SITE     2 BC5  5 ALA D 207                                                     
CRYST1   83.460  132.211   94.070  90.00 111.03  90.00 P 1 21 1      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      0.011982  0.000000  0.004607        0.00000                         
SCALE2      0.000000  0.007564  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011389        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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