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Database: PDB
Entry: 2E52
LinkDB: 2E52
Original site: 2E52 
HEADER    HYDROLASE/DNA                           18-DEC-06   2E52              
TITLE     CRYSTAL STRUCTURAL ANALYSIS OF HINDIII RESTRICTION ENDONUCLEASE IN    
TITLE    2 COMPLEX WITH COGNATE DNA AT 2.0 ANGSTROM RESOLUTION                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYPE II RESTRICTION ENZYME HINDIII;                        
COMPND   3 CHAIN: A, C, B, D;                                                   
COMPND   4 SYNONYM: ENDONUCLEASE HINDIII, R.HINDIII;                            
COMPND   5 EC: 3.1.21.4;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-D(*DGP*DCP*DCP*DAP*DAP*DGP*DCP*DTP*DTP*DGP*DGP*DC)-
COMPND   9 3');                                                                 
COMPND  10 CHAIN: E, F, G, H, I, J;                                             
COMPND  11 ENGINEERED: YES                                                      
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                                                       
KEYWDS    TYPE II RESTRICTION ENZYME HINDIII(E.C.3.1.21.4)/DNA, HYDROLASE-DNA   
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.WATANABE,C.SATO,I.TANAKA                                            
REVDAT   6   05-MAR-14 2E52    1       JRNL                                     
REVDAT   5   13-JUL-11 2E52    1       VERSN                                    
REVDAT   4   20-OCT-09 2E52    1       JRNL                                     
REVDAT   3   04-AUG-09 2E52    1       HELIX  REMARK                            
REVDAT   2   24-FEB-09 2E52    1       VERSN                                    
REVDAT   1   18-DEC-07 2E52    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.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 119772                         
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6327                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.86                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1800                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 469                          
REMARK   3   BIN FREE R VALUE                    : 0.2580                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9826                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1458                                    
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 968                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.19000                                              
REMARK   3    B22 (A**2) : 0.14000                                              
REMARK   3    B33 (A**2) : 0.09000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.59000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.141         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.084         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.872         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11655 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15971 ; 1.503 ; 2.133       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1190 ; 5.827 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   488 ;38.799 ;25.656       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2008 ;14.930 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;13.294 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1788 ; 0.111 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8088 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5417 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  8039 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1071 ; 0.140 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    57 ; 0.226 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.123 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6227 ; 0.952 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9666 ; 1.508 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6726 ; 2.227 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6305 ; 3.364 ; 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   : 1.40                                          
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                                                           
REMARK   4                                                                      
REMARK   4 2E52 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-DEC-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB026234.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUN-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 126130                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.684                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : 0.05500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.15600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 11.800                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 3350, 0.08M AMMONIUM ACETATE,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 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       65.76600            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13680 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13750 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F, H                            
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: 4570 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     MET C     0                                                      
REMARK 465     MET B     0                                                      
REMARK 465     LYS B     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     DT F   8   C6     DT F   8   N1      0.046                       
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   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG C 116   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.1 DEGREES          
REMARK 500     DA E   4   O4' -  C1' -  C2' ANGL. DEV. =   3.4 DEGREES          
REMARK 500     DC E   7   O4' -  C4' -  C3' ANGL. DEV. =  -2.7 DEGREES          
REMARK 500     DT E   9   O4' -  C1' -  N1  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500     DG E  10   C3' -  C2' -  C1' ANGL. DEV. =  -5.3 DEGREES          
REMARK 500     DG E  10   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DG F   1   C5  -  C6  -  O6  ANGL. DEV. =  -4.6 DEGREES          
REMARK 500     DA F   5   O4' -  C4' -  C3' ANGL. DEV. =  -3.1 DEGREES          
REMARK 500     DG F   6   O4' -  C1' -  N9  ANGL. DEV. =   3.4 DEGREES          
REMARK 500     DC F   7   O4' -  C4' -  C3' ANGL. DEV. =  -2.9 DEGREES          
REMARK 500     DC F   7   O4' -  C1' -  N1  ANGL. DEV. =   4.1 DEGREES          
REMARK 500     DT F   9   O4' -  C1' -  N1  ANGL. DEV. =  -6.5 DEGREES          
REMARK 500     DG F  11   O4' -  C1' -  N9  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500     DC G   2   O4' -  C1' -  N1  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DC G   3   C1' -  O4' -  C4' ANGL. DEV. =  -7.0 DEGREES          
REMARK 500     DA G   4   O4' -  C4' -  C3' ANGL. DEV. =  -2.8 DEGREES          
REMARK 500     DA G   4   N9  -  C1' -  C2' ANGL. DEV. =   9.5 DEGREES          
REMARK 500     DA G   5   O4' -  C4' -  C3' ANGL. DEV. =  -2.6 DEGREES          
REMARK 500     DT G   9   O4' -  C1' -  N1  ANGL. DEV. =  -7.3 DEGREES          
REMARK 500     DG G  11   O4' -  C1' -  N9  ANGL. DEV. =  -6.3 DEGREES          
REMARK 500     DA H   5   O4' -  C4' -  C3' ANGL. DEV. =  -3.9 DEGREES          
REMARK 500     DC H   7   O4' -  C4' -  C3' ANGL. DEV. =  -3.3 DEGREES          
REMARK 500     DT H   8   N3  -  C4  -  O4  ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DT H   9   O4' -  C1' -  N1  ANGL. DEV. =  -6.5 DEGREES          
REMARK 500     DC I   3   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DG I   6   O4' -  C1' -  N9  ANGL. DEV. =   5.8 DEGREES          
REMARK 500     DC I   7   O3' -  P   -  O5' ANGL. DEV. = -22.4 DEGREES          
REMARK 500     DC I   7   O3' -  P   -  OP2 ANGL. DEV. = -14.5 DEGREES          
REMARK 500     DC I   7   O3' -  P   -  OP1 ANGL. DEV. = -19.4 DEGREES          
REMARK 500     DT I   8   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DG I  10   O4' -  C1' -  N9  ANGL. DEV. =   3.6 DEGREES          
REMARK 500     DC I  12   C1' -  O4' -  C4' ANGL. DEV. =  -7.3 DEGREES          
REMARK 500     DC I  12   O4' -  C1' -  N1  ANGL. DEV. =   6.9 DEGREES          
REMARK 500     DC J   3   O4' -  C4' -  C3' ANGL. DEV. =  -3.6 DEGREES          
REMARK 500     DC J   3   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DC J   3   C3' -  O3' -  P   ANGL. DEV. =   9.5 DEGREES          
REMARK 500     DA J   4   C3' -  O3' -  P   ANGL. DEV. =   8.0 DEGREES          
REMARK 500     DA J   5   C3' -  O3' -  P   ANGL. DEV. =   8.3 DEGREES          
REMARK 500     DC J   7   O4' -  C1' -  N1  ANGL. DEV. =   3.4 DEGREES          
REMARK 500     DT J   9   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DG J  10   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  79       34.78     76.33                                   
REMARK 500    ARG A  88      -70.41   -113.99                                   
REMARK 500    PHE A 101     -169.13   -128.31                                   
REMARK 500    THR A 117     -100.80    -84.68                                   
REMARK 500    GLU A 134     -118.55     52.01                                   
REMARK 500    THR A 151      -57.28   -127.29                                   
REMARK 500    ASN C  79       36.90     73.68                                   
REMARK 500    ARG C  88      -78.86   -100.92                                   
REMARK 500    THR C 117      -99.62    -89.43                                   
REMARK 500    GLU C 134     -116.29     51.70                                   
REMARK 500    THR C 151      -52.96   -125.64                                   
REMARK 500    SER C 153      146.95   -173.83                                   
REMARK 500    PHE C 262      106.52     57.87                                   
REMARK 500    ASN B  17       -1.92     78.03                                   
REMARK 500    ASN B  79       36.06     72.93                                   
REMARK 500    ARG B  88      -78.81   -108.71                                   
REMARK 500    THR B 117     -108.82    -87.55                                   
REMARK 500    GLU B 134     -116.89     49.84                                   
REMARK 500    THR B 151      -50.71   -127.61                                   
REMARK 500    SER B 153      144.72   -172.59                                   
REMARK 500    ASN D  79       38.66     70.46                                   
REMARK 500    ARG D  88      -76.73   -108.69                                   
REMARK 500    PHE D 101     -168.08   -125.83                                   
REMARK 500    THR D 117      -97.13    -87.40                                   
REMARK 500    GLU D 134     -117.65     50.56                                   
REMARK 500    THR D 151      -57.49   -131.05                                   
REMARK 500    ARG D 264      -55.90    151.95                                   
REMARK 500    GLU D 265      -98.57    109.92                                   
REMARK 500    ASN D 276       37.28     70.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE D  262     THR D  263                  146.81                    
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    PHE C 262        18.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 B2192        DISTANCE =  5.90 ANGSTROMS                       
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 ACT C 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 2003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1004                
DBREF  2E52 A    0   299  UNP    P43870   T2D3_HAEIN       1    300             
DBREF  2E52 C    0   299  UNP    P43870   T2D3_HAEIN       1    300             
DBREF  2E52 B    0   299  UNP    P43870   T2D3_HAEIN       1    300             
DBREF  2E52 D    0   299  UNP    P43870   T2D3_HAEIN       1    300             
DBREF  2E52 E    1    12  PDB    2E52     2E52             1     12             
DBREF  2E52 F    1    12  PDB    2E52     2E52             1     12             
DBREF  2E52 G    1    12  PDB    2E52     2E52             1     12             
DBREF  2E52 H    1    12  PDB    2E52     2E52             1     12             
DBREF  2E52 I    1    12  PDB    2E52     2E52             1     12             
DBREF  2E52 J    1    12  PDB    2E52     2E52             1     12             
SEQRES   1 A  300  MET LYS LYS SER ALA LEU GLU LYS LEU LEU SER LEU ILE          
SEQRES   2 A  300  GLU ASN LEU THR ASN GLN GLU PHE LYS GLN ALA THR ASN          
SEQRES   3 A  300  SER LEU ILE SER PHE ILE TYR LYS LEU ASN ARG ASN GLU          
SEQRES   4 A  300  VAL ILE GLU LEU VAL ARG SER ILE GLY ILE LEU PRO GLU          
SEQRES   5 A  300  ALA ILE LYS PRO SER SER THR GLN GLU LYS LEU PHE SER          
SEQRES   6 A  300  LYS ALA GLY ASP ILE VAL LEU ALA LYS ALA PHE GLN LEU          
SEQRES   7 A  300  LEU ASN LEU ASN SER LYS PRO LEU GLU GLN ARG GLY ASN          
SEQRES   8 A  300  ALA GLY ASP VAL ILE ALA LEU SER LYS GLU PHE ASN TYR          
SEQRES   9 A  300  GLY LEU VAL ALA ASP ALA LYS SER PHE ARG LEU SER ARG          
SEQRES  10 A  300  THR ALA LYS ASN GLN LYS ASP PHE LYS VAL LYS ALA LEU          
SEQRES  11 A  300  SER GLU TRP ARG GLU ASP LYS ASP TYR ALA VAL LEU THR          
SEQRES  12 A  300  ALA PRO PHE PHE GLN TYR PRO THR THR LYS SER GLN ILE          
SEQRES  13 A  300  PHE LYS GLN SER LEU ASP GLU ASN VAL LEU LEU PHE SER          
SEQRES  14 A  300  TRP GLU HIS LEU ALA ILE LEU LEU GLN LEU ASP LEU GLU          
SEQRES  15 A  300  GLU THR ASN ILE PHE SER PHE GLU GLN LEU TRP ASN PHE          
SEQRES  16 A  300  PRO LYS LYS GLN SER LYS LYS THR SER VAL SER ASP ALA          
SEQRES  17 A  300  GLU ASN ASN PHE MET ARG ASP PHE ASN LYS TYR PHE MET          
SEQRES  18 A  300  ASP LEU PHE LYS ILE ASP LYS ASP THR LEU ASN GLN LEU          
SEQRES  19 A  300  LEU GLN LYS GLU ILE ASN PHE ILE GLU GLU ARG SER LEU          
SEQRES  20 A  300  ILE GLU LYS GLU TYR TRP LYS LYS GLN ILE ASN ILE ILE          
SEQRES  21 A  300  LYS ASN PHE THR ARG GLU GLU ALA ILE GLU ALA LEU LEU          
SEQRES  22 A  300  LYS ASP ILE ASN MET SER SER LYS ILE GLU THR ILE ASP          
SEQRES  23 A  300  SER PHE ILE LYS GLY ILE LYS SER ASN ASP ARG LEU TYR          
SEQRES  24 A  300  LEU                                                          
SEQRES   1 C  300  MET LYS LYS SER ALA LEU GLU LYS LEU LEU SER LEU ILE          
SEQRES   2 C  300  GLU ASN LEU THR ASN GLN GLU PHE LYS GLN ALA THR ASN          
SEQRES   3 C  300  SER LEU ILE SER PHE ILE TYR LYS LEU ASN ARG ASN GLU          
SEQRES   4 C  300  VAL ILE GLU LEU VAL ARG SER ILE GLY ILE LEU PRO GLU          
SEQRES   5 C  300  ALA ILE LYS PRO SER SER THR GLN GLU LYS LEU PHE SER          
SEQRES   6 C  300  LYS ALA GLY ASP ILE VAL LEU ALA LYS ALA PHE GLN LEU          
SEQRES   7 C  300  LEU ASN LEU ASN SER LYS PRO LEU GLU GLN ARG GLY ASN          
SEQRES   8 C  300  ALA GLY ASP VAL ILE ALA LEU SER LYS GLU PHE ASN TYR          
SEQRES   9 C  300  GLY LEU VAL ALA ASP ALA LYS SER PHE ARG LEU SER ARG          
SEQRES  10 C  300  THR ALA LYS ASN GLN LYS ASP PHE LYS VAL LYS ALA LEU          
SEQRES  11 C  300  SER GLU TRP ARG GLU ASP LYS ASP TYR ALA VAL LEU THR          
SEQRES  12 C  300  ALA PRO PHE PHE GLN TYR PRO THR THR LYS SER GLN ILE          
SEQRES  13 C  300  PHE LYS GLN SER LEU ASP GLU ASN VAL LEU LEU PHE SER          
SEQRES  14 C  300  TRP GLU HIS LEU ALA ILE LEU LEU GLN LEU ASP LEU GLU          
SEQRES  15 C  300  GLU THR ASN ILE PHE SER PHE GLU GLN LEU TRP ASN PHE          
SEQRES  16 C  300  PRO LYS LYS GLN SER LYS LYS THR SER VAL SER ASP ALA          
SEQRES  17 C  300  GLU ASN ASN PHE MET ARG ASP PHE ASN LYS TYR PHE MET          
SEQRES  18 C  300  ASP LEU PHE LYS ILE ASP LYS ASP THR LEU ASN GLN LEU          
SEQRES  19 C  300  LEU GLN LYS GLU ILE ASN PHE ILE GLU GLU ARG SER LEU          
SEQRES  20 C  300  ILE GLU LYS GLU TYR TRP LYS LYS GLN ILE ASN ILE ILE          
SEQRES  21 C  300  LYS ASN PHE THR ARG GLU GLU ALA ILE GLU ALA LEU LEU          
SEQRES  22 C  300  LYS ASP ILE ASN MET SER SER LYS ILE GLU THR ILE ASP          
SEQRES  23 C  300  SER PHE ILE LYS GLY ILE LYS SER ASN ASP ARG LEU TYR          
SEQRES  24 C  300  LEU                                                          
SEQRES   1 B  300  MET LYS LYS SER ALA LEU GLU LYS LEU LEU SER LEU ILE          
SEQRES   2 B  300  GLU ASN LEU THR ASN GLN GLU PHE LYS GLN ALA THR ASN          
SEQRES   3 B  300  SER LEU ILE SER PHE ILE TYR LYS LEU ASN ARG ASN GLU          
SEQRES   4 B  300  VAL ILE GLU LEU VAL ARG SER ILE GLY ILE LEU PRO GLU          
SEQRES   5 B  300  ALA ILE LYS PRO SER SER THR GLN GLU LYS LEU PHE SER          
SEQRES   6 B  300  LYS ALA GLY ASP ILE VAL LEU ALA LYS ALA PHE GLN LEU          
SEQRES   7 B  300  LEU ASN LEU ASN SER LYS PRO LEU GLU GLN ARG GLY ASN          
SEQRES   8 B  300  ALA GLY ASP VAL ILE ALA LEU SER LYS GLU PHE ASN TYR          
SEQRES   9 B  300  GLY LEU VAL ALA ASP ALA LYS SER PHE ARG LEU SER ARG          
SEQRES  10 B  300  THR ALA LYS ASN GLN LYS ASP PHE LYS VAL LYS ALA LEU          
SEQRES  11 B  300  SER GLU TRP ARG GLU ASP LYS ASP TYR ALA VAL LEU THR          
SEQRES  12 B  300  ALA PRO PHE PHE GLN TYR PRO THR THR LYS SER GLN ILE          
SEQRES  13 B  300  PHE LYS GLN SER LEU ASP GLU ASN VAL LEU LEU PHE SER          
SEQRES  14 B  300  TRP GLU HIS LEU ALA ILE LEU LEU GLN LEU ASP LEU GLU          
SEQRES  15 B  300  GLU THR ASN ILE PHE SER PHE GLU GLN LEU TRP ASN PHE          
SEQRES  16 B  300  PRO LYS LYS GLN SER LYS LYS THR SER VAL SER ASP ALA          
SEQRES  17 B  300  GLU ASN ASN PHE MET ARG ASP PHE ASN LYS TYR PHE MET          
SEQRES  18 B  300  ASP LEU PHE LYS ILE ASP LYS ASP THR LEU ASN GLN LEU          
SEQRES  19 B  300  LEU GLN LYS GLU ILE ASN PHE ILE GLU GLU ARG SER LEU          
SEQRES  20 B  300  ILE GLU LYS GLU TYR TRP LYS LYS GLN ILE ASN ILE ILE          
SEQRES  21 B  300  LYS ASN PHE THR ARG GLU GLU ALA ILE GLU ALA LEU LEU          
SEQRES  22 B  300  LYS ASP ILE ASN MET SER SER LYS ILE GLU THR ILE ASP          
SEQRES  23 B  300  SER PHE ILE LYS GLY ILE LYS SER ASN ASP ARG LEU TYR          
SEQRES  24 B  300  LEU                                                          
SEQRES   1 D  300  MET LYS LYS SER ALA LEU GLU LYS LEU LEU SER LEU ILE          
SEQRES   2 D  300  GLU ASN LEU THR ASN GLN GLU PHE LYS GLN ALA THR ASN          
SEQRES   3 D  300  SER LEU ILE SER PHE ILE TYR LYS LEU ASN ARG ASN GLU          
SEQRES   4 D  300  VAL ILE GLU LEU VAL ARG SER ILE GLY ILE LEU PRO GLU          
SEQRES   5 D  300  ALA ILE LYS PRO SER SER THR GLN GLU LYS LEU PHE SER          
SEQRES   6 D  300  LYS ALA GLY ASP ILE VAL LEU ALA LYS ALA PHE GLN LEU          
SEQRES   7 D  300  LEU ASN LEU ASN SER LYS PRO LEU GLU GLN ARG GLY ASN          
SEQRES   8 D  300  ALA GLY ASP VAL ILE ALA LEU SER LYS GLU PHE ASN TYR          
SEQRES   9 D  300  GLY LEU VAL ALA ASP ALA LYS SER PHE ARG LEU SER ARG          
SEQRES  10 D  300  THR ALA LYS ASN GLN LYS ASP PHE LYS VAL LYS ALA LEU          
SEQRES  11 D  300  SER GLU TRP ARG GLU ASP LYS ASP TYR ALA VAL LEU THR          
SEQRES  12 D  300  ALA PRO PHE PHE GLN TYR PRO THR THR LYS SER GLN ILE          
SEQRES  13 D  300  PHE LYS GLN SER LEU ASP GLU ASN VAL LEU LEU PHE SER          
SEQRES  14 D  300  TRP GLU HIS LEU ALA ILE LEU LEU GLN LEU ASP LEU GLU          
SEQRES  15 D  300  GLU THR ASN ILE PHE SER PHE GLU GLN LEU TRP ASN PHE          
SEQRES  16 D  300  PRO LYS LYS GLN SER LYS LYS THR SER VAL SER ASP ALA          
SEQRES  17 D  300  GLU ASN ASN PHE MET ARG ASP PHE ASN LYS TYR PHE MET          
SEQRES  18 D  300  ASP LEU PHE LYS ILE ASP LYS ASP THR LEU ASN GLN LEU          
SEQRES  19 D  300  LEU GLN LYS GLU ILE ASN PHE ILE GLU GLU ARG SER LEU          
SEQRES  20 D  300  ILE GLU LYS GLU TYR TRP LYS LYS GLN ILE ASN ILE ILE          
SEQRES  21 D  300  LYS ASN PHE THR ARG GLU GLU ALA ILE GLU ALA LEU LEU          
SEQRES  22 D  300  LYS ASP ILE ASN MET SER SER LYS ILE GLU THR ILE ASP          
SEQRES  23 D  300  SER PHE ILE LYS GLY ILE LYS SER ASN ASP ARG LEU TYR          
SEQRES  24 D  300  LEU                                                          
SEQRES   1 E   12   DG  DC  DC  DA  DA  DG  DC  DT  DT  DG  DG  DC              
SEQRES   1 F   12   DG  DC  DC  DA  DA  DG  DC  DT  DT  DG  DG  DC              
SEQRES   1 G   12   DG  DC  DC  DA  DA  DG  DC  DT  DT  DG  DG  DC              
SEQRES   1 H   12   DG  DC  DC  DA  DA  DG  DC  DT  DT  DG  DG  DC              
SEQRES   1 I   12   DG  DC  DC  DA  DA  DG  DC  DT  DT  DG  DG  DC              
SEQRES   1 J   12   DG  DC  DC  DA  DA  DG  DC  DT  DT  DG  DG  DC              
HET    GOL  E1001       6                                                       
HET    GOL  A1004       6                                                       
HET    ACT  C2001       4                                                       
HET    ACT  C2003       4                                                       
HET    GOL  C1002       6                                                       
HET    GOL  C1003       6                                                       
HET    ACT  B2002       4                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     ACT ACETATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL  11  GOL    4(C3 H8 O3)                                                  
FORMUL  13  ACT    3(C2 H3 O2 1-)                                               
FORMUL  18  HOH   *968(H2 O)                                                    
HELIX    1   1 ALA A    4  ASN A   14  1                                  11    
HELIX    2   2 PHE A   20  TYR A   32  1                                  13    
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  TYR A  148  5                                   4    
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  LYS A  260  1                                  34    
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  ILE C  291  1                                  15    
HELIX   32  32 ASN C  294  LEU C  297  5                                   4    
HELIX   33  33 ALA B    4  GLU B   13  1                                  10    
HELIX   34  34 PHE B   20  LYS B   33  1                                  14    
HELIX   35  35 ARG B   36  SER B   45  1                                  10    
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  ASN D   14  1                                  11    
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 VAL D  204  ASP D  206  5                                   3    
HELIX   59  59 MET D  212  PHE D  223  1                                  12    
HELIX   60  60 LYS D  227  LYS D  260  1                                  34    
HELIX   61  61 GLU D  266  ILE D  275  1                                  10    
HELIX   62  62 MET D  277  ILE D  291  1                                  15    
HELIX   63  63 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  LEU A 165   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 VAL C 164  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 LEU B 165  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           
CISPEP   1 ASN C  261    PHE C  262          0        -2.30                     
CISPEP   2 THR D  263    ARG D  264          0        21.38                     
CISPEP   3 ARG D  264    GLU D  265          0       -12.26                     
SITE     1 AC1  3 ASN C 209  ASP C 214  HOH C2016                               
SITE     1 AC2  4 ASP B 161  SER B 199  THR B 202  ALA B 207                    
SITE     1 AC3  5 PHE C 186  LEU C 222  PHE C 223  LYS C 224                    
SITE     2 AC3  5 HOH C2145                                                     
SITE     1 AC4  7 GLY A  89  LYS B 152   DC E   2   DC E   3                    
SITE     2 AC4  7 HOH E1007  HOH E1010   DG G  11                               
SITE     1 AC5  8 ARG C 296  TYR C 298  PHE D 145  PHE D 146                    
SITE     2 AC5  8 TYR D 148  PRO D 149  ASN D 210  MET D 212                    
SITE     1 AC6  8 PHE C 145  PHE C 146  TYR C 148  PRO C 149                    
SITE     2 AC6  8 ASN C 210  MET C 212  ARG D 296  TYR D 298                    
SITE     1 AC7  8 PHE A 145  PHE A 146  TYR A 148  PRO A 149                    
SITE     2 AC7  8 ASN A 210  MET A 212  ARG B 296  TYR B 298                    
CRYST1   83.125  131.532   93.718  90.00 111.20  90.00 P 1 21 1     12          
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      0.012030  0.000000  0.004666        0.00000                         
SCALE2      0.000000  0.007603  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011445        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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