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Database: PDB
Entry: 3BP8
LinkDB: 3BP8
Original site: 3BP8 
HEADER    TRANSCRIPTION                           18-DEC-07   3BP8              
TITLE     CRYSTAL STRUCTURE OF MLC/EIIB COMPLEX                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE NAGC-LIKE TRANSCRIPTIONAL REGULATOR;              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MLC;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PTS SYSTEM GLUCOSE-SPECIFIC EIICB COMPONENT;               
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 FRAGMENT: UNP RESIDUES 401-475;                                      
COMPND  10 SYNONYM: EIIB, EIICB-GLC, EII-GLC;                                   
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 STRAIN: B834(DE3);                                                   
SOURCE   4 GENE: MLC;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PNS100;                                   
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  10 STRAIN: GI698;                                                       
SOURCE  11 GENE: PTSG, GLCA, UMG;                                               
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PJHK                                      
KEYWDS    ENZYME, IICBGLC, GLUCOSE SIGNALING, MLC, PROTEIN-PROTEIN              
KEYWDS   2 INTERACTION, TRANSCRIPTION REGULATION, INNER MEMBRANE,               
KEYWDS   3 KINASE, MEMBRANE, PHOSPHOPROTEIN, PHOSPHOTRANSFERASE SYSTEM,         
KEYWDS   4 SUGAR TRANSPORT, TRANSFERASE, TRANSMEMBRANE, TRANSPORT               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.J.AN,H.I.JUNG,S.S.CHA                                               
REVDAT   2   24-FEB-09 3BP8    1       VERSN                                    
REVDAT   1   27-MAY-08 3BP8    0                                                
JRNL        AUTH   T.W.NAM,H.I.JUNG,Y.J.AN,Y.H.PARK,S.H.LEE,Y.J.SEOK,           
JRNL        AUTH 2 S.S.CHA                                                      
JRNL        TITL   ANALYSES OF MLC-IIBGLC INTERACTION AND A PLAUSIBLE           
JRNL        TITL 2 MOLECULAR MECHANISM OF MLC INACTIVATION BY                   
JRNL        TITL 3 MEMBRANE SEQUESTRATION                                       
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105  3751 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18319344                                                     
JRNL        DOI    10.1073/PNAS.0709295105                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.100                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 206924.270                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 83.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 17850                          
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 SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.301                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1748                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6929                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 17.58000                                             
REMARK   3    B22 (A**2) : 4.01000                                              
REMARK   3    B33 (A**2) : 13.57000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 11.57000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.39                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.82                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.49                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.94                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.78                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.19                                                 
REMARK   3   BSOL        : 10.00                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3BP8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-DEC-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB045795.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 6B                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20356                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1Z6R, 3BP3                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 6K, 0.1M MGCL2, 0.1M SODIUM       
REMARK 280  ACETATE, PH5.5                                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      100.71350            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.71200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      100.71350            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       27.71200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     ILE A    10                                                      
REMARK 465     ILE A    65                                                      
REMARK 465     LYS A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     ALA A    68                                                      
REMARK 465     GLY A    69                                                      
REMARK 465     ASN A    70                                                      
REMARK 465     ARG A    71                                                      
REMARK 465     GLY A    72                                                      
REMARK 465     ARG A    73                                                      
REMARK 465     PRO A    74                                                      
REMARK 465     ALA A    75                                                      
REMARK 465     SER A   287                                                      
REMARK 465     SER A   288                                                      
REMARK 465     MET A   289                                                      
REMARK 465     LEU A   290                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ASN B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     PRO B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     HIS B     9                                                      
REMARK 465     ILE B    10                                                      
REMARK 465     ASP B    11                                                      
REMARK 465     GLU B    64                                                      
REMARK 465     ILE B    65                                                      
REMARK 465     LYS B    66                                                      
REMARK 465     GLU B    67                                                      
REMARK 465     ALA B    68                                                      
REMARK 465     GLY B    69                                                      
REMARK 465     ASN B    70                                                      
REMARK 465     ARG B    71                                                      
REMARK 465     GLY B    72                                                      
REMARK 465     ARG B    73                                                      
REMARK 465     PRO B    74                                                      
REMARK 465     ALA B    75                                                      
REMARK 465     GLN B   381                                                      
REMARK 465     GLY B   382                                                      
REMARK 465     THR B   383                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ASP A   11   CG    OD1   OD2                                     
REMARK 480     LEU A   42   CG    CD1   CD2                                     
REMARK 480     LYS A   49   CG    CD    CE    NZ                                
REMARK 480     GLU A   64   CG    CD    OE1   OE2                               
REMARK 480     GLU A  112   CG    CD    OE1   OE2                               
REMARK 480     LEU A  118   CG    CD1   CD2                                     
REMARK 480     LYS A  119   CG    CD    CE    NZ                                
REMARK 480     ASP A  121   CG    OD1   OD2                                     
REMARK 480     GLN A  140   CG    CD    OE1   NE2                               
REMARK 480     LYS A  141   CG    CD    CE    NZ                                
REMARK 480     LYS A  142   CG    CD    CE    NZ                                
REMARK 480     GLU A  160   CG    CD    OE1   OE2                               
REMARK 480     GLU A  171   CG    CD    OE1   OE2                               
REMARK 480     LYS A  174   CG    CD    CE    NZ                                
REMARK 480     HIS A  262   CG    ND1   CD2   CE1   NE2                         
REMARK 480     MET A  286   CG    SD    CE                                      
REMARK 480     GLN A  293   CG    CD    OE1   NE2                               
REMARK 480     ASP A  357   CG    OD1   OD2                                     
REMARK 480     GLN A  381   CG    CD    OE1   NE2                               
REMARK 480     GLN B   12   CG    CD    OE1   NE2                               
REMARK 480     LYS B   14   CG    CD    CE    NZ                                
REMARK 480     ASN B   17   CG    OD1   ND2                                     
REMARK 480     LEU B   24   CG    CD1   CD2                                     
REMARK 480     ARG B   33   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     ARG B   38   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     LEU B   39   CG    CD1   CD2                                     
REMARK 480     LEU B   42   CG    CD1   CD2                                     
REMARK 480     ILE B   47   CG1   CG2   CD1                                     
REMARK 480     LYS B   49   CG    CD    CE    NZ                                
REMARK 480     ILE B   50   CD1                                                 
REMARK 480     ARG B   52   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     GLU B   56   CG    CD    OE1   OE2                               
REMARK 480     GLU B   81   CG    CD    OE1   OE2                               
REMARK 480     ARG B   91   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     ILE B   92   CD1                                                 
REMARK 480     ARG B   94   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     LEU B  101   CG    CD1   CD2                                     
REMARK 480     GLU B  112   CG    CD    OE1   OE2                               
REMARK 480     GLU B  115   CG    CD    OE1   OE2                               
REMARK 480     LYS B  119   CG    CD    CE    NZ                                
REMARK 480     SER B  122   OG                                                  
REMARK 480     GLN B  140   CG    CD    OE1   NE2                               
REMARK 480     LYS B  141   CG    CD    CE    NZ                                
REMARK 480     LYS B  142   CG    CD    CE    NZ                                
REMARK 480     GLU B  160   CG    CD    OE1   OE2                               
REMARK 480     ARG B  166   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     PHE B  169   CG    CD1   CD2   CE1   CE2   CZ                    
REMARK 480     GLU B  171   CG    CD    OE1   OE2                               
REMARK 480     LYS B  174   CG    CD    CE    NZ                                
REMARK 480     GLU B  180   CG    CD    OE1   OE2                               
REMARK 480     GLU B  183   CG    CD    OE1   OE2                               
REMARK 480     MET B  286   CG    SD    CE                                      
REMARK 480     MET B  289   CG    SD    CE                                      
REMARK 480     LEU B  290   CG    CD1   CD2                                     
REMARK 480     GLN B  293   CG    CD    OE1   NE2                               
REMARK 480     PRO B  335   CD                                                  
REMARK 480     ASN B  380   CG    OD1   ND2                                     
REMARK 480     MET B  384   CG    SD    CE                                      
REMARK 480     LYS B  391   CG    CD    CE    NZ                                
REMARK 480     ASN B  396   CG    OD1   ND2                                     
REMARK 480     ARG B  402   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     LYS C   24   CG    CD    CE    NZ                                
REMARK 480     ILE C   34   CG1   CG2   CD1                                     
REMARK 480     ARG C   38   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     LYS C   54   CG    CD    CE    NZ                                
REMARK 480     LYS C   74   CG    CD    CE    NZ                                
REMARK 480     ASP C   76   CG    OD1   OD2                                     
REMARK 480     ARG C   87   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     LYS D   24   CG    CD    CE    NZ                                
REMARK 480     LEU D   30   CG    CD1   CD2                                     
REMARK 480     ARG D   38   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     LYS D   54   CG    CD    CE    NZ                                
REMARK 480     LYS D   74   CG    CD    CE    NZ                                
REMARK 480     ASP D   76   CG    OD1   OD2                                     
REMARK 480     GLU D   84   CG    CD    OE1   OE2                               
REMARK 480     ARG D   87   CG    CD    NE    CZ    NH1   NH2                   
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    GLN A  12      -41.33   -148.33                                   
REMARK 500    VAL A  80      152.47    -40.65                                   
REMARK 500    ARG A  94       97.56     58.57                                   
REMARK 500    SER A 106        8.65     85.14                                   
REMARK 500    GLN A 114     -158.71   -110.74                                   
REMARK 500    LEU A 116       -4.85   -159.28                                   
REMARK 500    ALA A 117      -38.59     62.00                                   
REMARK 500    LEU A 118      -56.48     95.38                                   
REMARK 500    GLU A 144     -133.16   -118.89                                   
REMARK 500    SER A 148     -178.06   -175.75                                   
REMARK 500    PHE A 169      -49.66     84.51                                   
REMARK 500    VAL A 173      -80.39   -113.22                                   
REMARK 500    LYS A 174      103.62     49.01                                   
REMARK 500    PRO A 177       44.47    -74.61                                   
REMARK 500    THR A 186      -38.58   -134.99                                   
REMARK 500    ALA A 208      -72.63     11.60                                   
REMARK 500    SER A 209       44.40    -97.36                                   
REMARK 500    ASP A 221     -129.29   -142.72                                   
REMARK 500    ASP A 231      -35.03     65.86                                   
REMARK 500    SER A 239      -90.82    -90.69                                   
REMARK 500    SER A 241       63.93     13.38                                   
REMARK 500    LEU A 242      156.61    -43.87                                   
REMARK 500    ILE A 245        1.51    -64.42                                   
REMARK 500    HIS A 247       64.82   -110.56                                   
REMARK 500    GLN A 249       89.52    -47.04                                   
REMARK 500    PRO A 252        6.66    -52.37                                   
REMARK 500    TYR A 253      -69.47   -138.25                                   
REMARK 500    TYR A 258        5.69    -67.94                                   
REMARK 500    ASN A 261     -160.33    -64.88                                   
REMARK 500    THR A 267      -12.81   -164.66                                   
REMARK 500    LEU A 280       15.05    -57.36                                   
REMARK 500    GLN A 284       55.19   -118.74                                   
REMARK 500    SER A 285      162.73     72.99                                   
REMARK 500    PRO A 294      154.46    -47.03                                   
REMARK 500    ASN A 334       61.11     65.85                                   
REMARK 500    ILE A 371      116.72   -172.31                                   
REMARK 500    SER A 398       39.25    -66.02                                   
REMARK 500    LEU A 399      -44.00   -167.48                                   
REMARK 500    ASP B  26      -24.31    164.59                                   
REMARK 500    GLN B  41       76.50     56.92                                   
REMARK 500    ILE B  47      -21.96   -153.78                                   
REMARK 500    GLU B  83      -41.53   -147.69                                   
REMARK 500    ALA B 100      146.33   -171.43                                   
REMARK 500    SER B 113       27.25   -152.17                                   
REMARK 500    ALA B 117      179.72     71.92                                   
REMARK 500    LEU B 118      -64.74   -105.91                                   
REMARK 500    PRO B 123     -130.61    -57.80                                   
REMARK 500    PHE B 135      -38.62    -36.62                                   
REMARK 500    HIS B 139       41.37    -76.16                                   
REMARK 500    ARG B 145      115.35    169.98                                   
REMARK 500    THR B 159      -53.49     53.52                                   
REMARK 500    HIS B 165      -71.34    -72.79                                   
REMARK 500    GLU B 175       72.61     66.67                                   
REMARK 500    THR B 186      -52.10   -142.86                                   
REMARK 500    PHE B 206       -9.22   -168.57                                   
REMARK 500    ASP B 221     -124.37   -130.93                                   
REMARK 500    HIS B 236     -155.14    -97.10                                   
REMARK 500    LEU B 242      149.34     76.18                                   
REMARK 500    GLU B 244       51.84    -99.22                                   
REMARK 500    ARG B 256      151.30    -48.99                                   
REMARK 500    GLN B 284     -157.39   -102.01                                   
REMARK 500    SER B 288      131.76   -171.48                                   
REMARK 500    MET B 289       14.83    -61.62                                   
REMARK 500    LYS B 312      -73.08    -54.74                                   
REMARK 500    ASN B 334       70.35     33.68                                   
REMARK 500    ASP B 349        5.49    -60.64                                   
REMARK 500    LEU B 351      -78.07    -76.00                                   
REMARK 500    LEU B 364       98.63    -46.34                                   
REMARK 500    PRO B 365      -67.71    -26.22                                   
REMARK 500    HIS B 370       30.30   -157.62                                   
REMARK 500    SER B 379     -112.00   -145.51                                   
REMARK 500    ALA B 385      126.07     99.78                                   
REMARK 500    ALA B 387      -50.75     50.39                                   
REMARK 500    GLU C  25       23.94    -79.19                                   
REMARK 500    ASN C  26      -24.65   -146.09                                   
REMARK 500    THR C  35       -0.26   -140.20                                   
REMARK 500    LYS C  74       28.06    -71.01                                   
REMARK 500    ILE C  86       42.01    -88.61                                   
REMARK 500    LYS D  24      -27.44    -39.75                                   
REMARK 500    CYS D  33     -142.33    -92.64                                   
REMARK 500    ARG D  38       88.33    -51.46                                   
REMARK 500    VAL D  62       71.47   -110.78                                   
REMARK 500    TYR D  85       37.84    -80.17                                   
REMARK 500    ILE D  86      -37.04   -134.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 410  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 247   ND1                                                    
REMARK 620 2 CYS A 257   SG  113.5                                              
REMARK 620 3 CYS A 259   SG  110.8  93.9                                        
REMARK 620 4 CYS A 264   SG  109.7 124.5 101.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 407  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 257   SG                                                     
REMARK 620 2 CYS B 259   SG  111.2                                              
REMARK 620 3 CYS B 264   SG  126.9 117.1                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 408                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 409                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 410                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 407                  
DBREF  3BP8 A    1   406  UNP    Q8X787   Q8X787_ECO57     1    406             
DBREF  3BP8 B    1   406  UNP    Q8X787   Q8X787_ECO57     1    406             
DBREF  3BP8 C   13    87  UNP    P69786   PTGCB_ECOLI    401    475             
DBREF  3BP8 D   13    87  UNP    P69786   PTGCB_ECOLI    401    475             
SEQRES   1 A  406  MET VAL ALA GLU ASN GLN PRO GLY HIS ILE ASP GLN ILE          
SEQRES   2 A  406  LYS GLN THR ASN ALA GLY ALA VAL TYR ARG LEU ILE ASP          
SEQRES   3 A  406  GLN LEU GLY PRO VAL SER ARG ILE ASP LEU SER ARG LEU          
SEQRES   4 A  406  ALA GLN LEU ALA PRO ALA SER ILE THR LYS ILE VAL ARG          
SEQRES   5 A  406  GLU MET LEU GLU ALA HIS LEU VAL GLN GLU LEU GLU ILE          
SEQRES   6 A  406  LYS GLU ALA GLY ASN ARG GLY ARG PRO ALA VAL GLY LEU          
SEQRES   7 A  406  VAL VAL GLU THR GLU ALA TRP HIS TYR LEU SER LEU ARG          
SEQRES   8 A  406  ILE SER ARG GLY GLU ILE PHE LEU ALA LEU ARG ASP LEU          
SEQRES   9 A  406  SER SER LYS LEU VAL VAL GLU GLU SER GLN GLU LEU ALA          
SEQRES  10 A  406  LEU LYS ASP ASP SER PRO LEU LEU ASP ARG ILE ILE SER          
SEQRES  11 A  406  HIS ILE ASP GLN PHE PHE ILE ARG HIS GLN LYS LYS LEU          
SEQRES  12 A  406  GLU ARG LEU THR SER ILE ALA ILE THR LEU PRO GLY ILE          
SEQRES  13 A  406  ILE ASP THR GLU ASN GLY ILE VAL HIS ARG MET PRO PHE          
SEQRES  14 A  406  TYR GLU ASP VAL LYS GLU MET PRO LEU GLY GLU ALA LEU          
SEQRES  15 A  406  GLU GLN HIS THR GLY VAL PRO VAL TYR ILE GLN HIS ASP          
SEQRES  16 A  406  ILE SER ALA TRP THR MET ALA GLU ALA LEU PHE GLY ALA          
SEQRES  17 A  406  SER ARG GLY ALA ARG ASP VAL ILE GLN VAL VAL ILE ASP          
SEQRES  18 A  406  HIS ASN VAL GLY ALA GLY VAL ILE THR ASP GLY HIS LEU          
SEQRES  19 A  406  LEU HIS ALA GLY SER SER SER LEU VAL GLU ILE GLY HIS          
SEQRES  20 A  406  THR GLN VAL ASP PRO TYR GLY LYS ARG CYS TYR CYS GLY          
SEQRES  21 A  406  ASN HIS GLY CYS LEU GLU THR ILE ALA SER VAL ASP SER          
SEQRES  22 A  406  ILE LEU GLU LEU ALA GLN LEU ARG LEU ASN GLN SER MET          
SEQRES  23 A  406  SER SER MET LEU HIS GLY GLN PRO LEU THR VAL ASP SER          
SEQRES  24 A  406  LEU CYS GLN ALA ALA LEU ARG GLY ASP LEU LEU ALA LYS          
SEQRES  25 A  406  ASP ILE ILE THR GLY VAL GLY ALA HIS VAL GLY ARG ILE          
SEQRES  26 A  406  LEU ALA ILE MET VAL ASN LEU PHE ASN PRO GLN LYS ILE          
SEQRES  27 A  406  LEU ILE GLY SER PRO LEU SER LYS ALA ALA ASP ILE LEU          
SEQRES  28 A  406  PHE PRO VAL ILE SER ASP SER ILE ARG GLN GLN ALA LEU          
SEQRES  29 A  406  PRO ALA TYR SER GLN HIS ILE SER VAL GLU SER THR GLN          
SEQRES  30 A  406  PHE SER ASN GLN GLY THR MET ALA GLY ALA ALA LEU VAL          
SEQRES  31 A  406  LYS ASP ALA MET TYR ASN GLY SER LEU LEU ILE ARG LEU          
SEQRES  32 A  406  LEU GLN GLY                                                  
SEQRES   1 B  406  MET VAL ALA GLU ASN GLN PRO GLY HIS ILE ASP GLN ILE          
SEQRES   2 B  406  LYS GLN THR ASN ALA GLY ALA VAL TYR ARG LEU ILE ASP          
SEQRES   3 B  406  GLN LEU GLY PRO VAL SER ARG ILE ASP LEU SER ARG LEU          
SEQRES   4 B  406  ALA GLN LEU ALA PRO ALA SER ILE THR LYS ILE VAL ARG          
SEQRES   5 B  406  GLU MET LEU GLU ALA HIS LEU VAL GLN GLU LEU GLU ILE          
SEQRES   6 B  406  LYS GLU ALA GLY ASN ARG GLY ARG PRO ALA VAL GLY LEU          
SEQRES   7 B  406  VAL VAL GLU THR GLU ALA TRP HIS TYR LEU SER LEU ARG          
SEQRES   8 B  406  ILE SER ARG GLY GLU ILE PHE LEU ALA LEU ARG ASP LEU          
SEQRES   9 B  406  SER SER LYS LEU VAL VAL GLU GLU SER GLN GLU LEU ALA          
SEQRES  10 B  406  LEU LYS ASP ASP SER PRO LEU LEU ASP ARG ILE ILE SER          
SEQRES  11 B  406  HIS ILE ASP GLN PHE PHE ILE ARG HIS GLN LYS LYS LEU          
SEQRES  12 B  406  GLU ARG LEU THR SER ILE ALA ILE THR LEU PRO GLY ILE          
SEQRES  13 B  406  ILE ASP THR GLU ASN GLY ILE VAL HIS ARG MET PRO PHE          
SEQRES  14 B  406  TYR GLU ASP VAL LYS GLU MET PRO LEU GLY GLU ALA LEU          
SEQRES  15 B  406  GLU GLN HIS THR GLY VAL PRO VAL TYR ILE GLN HIS ASP          
SEQRES  16 B  406  ILE SER ALA TRP THR MET ALA GLU ALA LEU PHE GLY ALA          
SEQRES  17 B  406  SER ARG GLY ALA ARG ASP VAL ILE GLN VAL VAL ILE ASP          
SEQRES  18 B  406  HIS ASN VAL GLY ALA GLY VAL ILE THR ASP GLY HIS LEU          
SEQRES  19 B  406  LEU HIS ALA GLY SER SER SER LEU VAL GLU ILE GLY HIS          
SEQRES  20 B  406  THR GLN VAL ASP PRO TYR GLY LYS ARG CYS TYR CYS GLY          
SEQRES  21 B  406  ASN HIS GLY CYS LEU GLU THR ILE ALA SER VAL ASP SER          
SEQRES  22 B  406  ILE LEU GLU LEU ALA GLN LEU ARG LEU ASN GLN SER MET          
SEQRES  23 B  406  SER SER MET LEU HIS GLY GLN PRO LEU THR VAL ASP SER          
SEQRES  24 B  406  LEU CYS GLN ALA ALA LEU ARG GLY ASP LEU LEU ALA LYS          
SEQRES  25 B  406  ASP ILE ILE THR GLY VAL GLY ALA HIS VAL GLY ARG ILE          
SEQRES  26 B  406  LEU ALA ILE MET VAL ASN LEU PHE ASN PRO GLN LYS ILE          
SEQRES  27 B  406  LEU ILE GLY SER PRO LEU SER LYS ALA ALA ASP ILE LEU          
SEQRES  28 B  406  PHE PRO VAL ILE SER ASP SER ILE ARG GLN GLN ALA LEU          
SEQRES  29 B  406  PRO ALA TYR SER GLN HIS ILE SER VAL GLU SER THR GLN          
SEQRES  30 B  406  PHE SER ASN GLN GLY THR MET ALA GLY ALA ALA LEU VAL          
SEQRES  31 B  406  LYS ASP ALA MET TYR ASN GLY SER LEU LEU ILE ARG LEU          
SEQRES  32 B  406  LEU GLN GLY                                                  
SEQRES   1 C   75  MET ALA PRO ALA LEU VAL ALA ALA PHE GLY GLY LYS GLU          
SEQRES   2 C   75  ASN ILE THR ASN LEU ASP ALA CYS ILE THR ARG LEU ARG          
SEQRES   3 C   75  VAL SER VAL ALA ASP VAL SER LYS VAL ASP GLN ALA GLY          
SEQRES   4 C   75  LEU LYS LYS LEU GLY ALA ALA GLY VAL VAL VAL ALA GLY          
SEQRES   5 C   75  SER GLY VAL GLN ALA ILE PHE GLY THR LYS SER ASP ASN          
SEQRES   6 C   75  LEU LYS THR GLU MET ASP GLU TYR ILE ARG                      
SEQRES   1 D   75  MET ALA PRO ALA LEU VAL ALA ALA PHE GLY GLY LYS GLU          
SEQRES   2 D   75  ASN ILE THR ASN LEU ASP ALA CYS ILE THR ARG LEU ARG          
SEQRES   3 D   75  VAL SER VAL ALA ASP VAL SER LYS VAL ASP GLN ALA GLY          
SEQRES   4 D   75  LEU LYS LYS LEU GLY ALA ALA GLY VAL VAL VAL ALA GLY          
SEQRES   5 D   75  SER GLY VAL GLN ALA ILE PHE GLY THR LYS SER ASP ASN          
SEQRES   6 D   75  LEU LYS THR GLU MET ASP GLU TYR ILE ARG                      
HET    ACT  A 407       4                                                       
HET    ACT  A 408       4                                                       
HET    ACT  A 409       4                                                       
HET     ZN  A 410       1                                                       
HET     ZN  B 407       1                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM      ZN ZINC ION                                                         
FORMUL   5  ACT    3(C2 H3 O2 1-)                                               
FORMUL   8   ZN    2(ZN 2+)                                                     
HELIX    1   1 ILE A   13  LEU A   28  1                                  16    
HELIX    2   2 SER A   32  ALA A   40  1                                   9    
HELIX    3   3 ALA A   43  ALA A   57  1                                  15    
HELIX    4   4 PRO A  123  HIS A  139  1                                  17    
HELIX    5   5 GLU A  180  HIS A  185  1                                   6    
HELIX    6   6 ASP A  195  PHE A  206  1                                  12    
HELIX    7   7 GLU A  244  THR A  248  5                                   5    
HELIX    8   8 SER A  270  LEU A  280  1                                  11    
HELIX    9   9 THR A  296  GLY A  307  1                                  12    
HELIX   10  10 ASP A  308  ASN A  334  1                                  27    
HELIX   11  11 SER A  342  LYS A  346  5                                   5    
HELIX   12  12 ALA A  347  ALA A  363  1                                  17    
HELIX   13  13 LEU A  364  GLN A  369  1                                   6    
HELIX   14  14 GLY A  382  ALA A  385  5                                   4    
HELIX   15  15 GLY A  386  ASN A  396  1                                  11    
HELIX   16  16 LEU A  399  LEU A  404  1                                   6    
HELIX   17  17 GLN B   12  ILE B   25  1                                  14    
HELIX   18  18 SER B   32  ALA B   40  1                                   9    
HELIX   19  19 THR B   48  GLU B   56  1                                   9    
HELIX   20  20 LEU B  124  HIS B  139  1                                  16    
HELIX   21  21 PRO B  177  HIS B  185  1                                   9    
HELIX   22  22 HIS B  194  PHE B  206  1                                  13    
HELIX   23  23 GLU B  244  THR B  248  5                                   5    
HELIX   24  24 CYS B  264  ALA B  269  1                                   6    
HELIX   25  25 SER B  270  ASN B  283  1                                  14    
HELIX   26  26 THR B  296  LEU B  305  1                                  10    
HELIX   27  27 ASP B  308  ASN B  334  1                                  27    
HELIX   28  28 SER B  342  ALA B  348  5                                   7    
HELIX   29  29 LEU B  351  GLN B  362  1                                  12    
HELIX   30  30 LEU B  364  GLN B  369  1                                   6    
HELIX   31  31 ALA B  387  ASN B  396  1                                  10    
HELIX   32  32 GLY B  397  GLN B  405  1                                   9    
HELIX   33  33 MET C   13  PHE C   21  1                                   9    
HELIX   34  34 ASP C   43  VAL C   47  5                                   5    
HELIX   35  35 ASP C   48  GLY C   56  1                                   9    
HELIX   36  36 LYS C   74  ILE C   86  1                                  13    
HELIX   37  37 VAL D   18  GLY D   22  5                                   5    
HELIX   38  38 ASP D   43  VAL D   47  5                                   5    
HELIX   39  39 ASP D   48  LYS D   54  1                                   7    
HELIX   40  40 THR D   73  TYR D   85  1                                  13    
SHEET    1   A 2 VAL A  60  GLU A  62  0                                        
SHEET    2   A 2 LEU A  78  VAL A  80 -1  O  VAL A  79   N  GLN A  61           
SHEET    1   B 5 LEU A 108  GLU A 115  0                                        
SHEET    2   B 5 GLU A  96  ASP A 103 -1  N  ILE A  97   O  GLN A 114           
SHEET    3   B 5 TRP A  85  ILE A  92 -1  N  TYR A  87   O  ARG A 102           
SHEET    4   B 5 ARG A 145  LEU A 153  1  O  ALA A 150   N  LEU A  88           
SHEET    5   B 5 VAL A 190  HIS A 194  1  O  TYR A 191   N  ILE A 151           
SHEET    1   C 2 ILE A 156  ASP A 158  0                                        
SHEET    2   C 2 ILE A 163  ARG A 166 -1  O  ILE A 163   N  ASP A 158           
SHEET    1   D 5 HIS A 233  LEU A 234  0                                        
SHEET    2   D 5 VAL A 224  THR A 230 -1  N  THR A 230   O  HIS A 233           
SHEET    3   D 5 VAL A 215  ILE A 220 -1  N  VAL A 219   O  GLY A 225           
SHEET    4   D 5 LYS A 337  GLY A 341  1  O  GLY A 341   N  VAL A 218           
SHEET    5   D 5 VAL A 373  SER A 375  1  O  GLU A 374   N  ILE A 338           
SHEET    1   E 2 VAL B  60  GLU B  62  0                                        
SHEET    2   E 2 LEU B  78  VAL B  80 -1  O  VAL B  79   N  GLN B  61           
SHEET    1   F 5 LEU B 108  GLU B 111  0                                        
SHEET    2   F 5 ILE B  97  ARG B 102 -1  N  LEU B 101   O  VAL B 109           
SHEET    3   F 5 HIS B  86  ILE B  92 -1  N  SER B  89   O  ALA B 100           
SHEET    4   F 5 LEU B 146  THR B 152  1  O  ALA B 150   N  LEU B  88           
SHEET    5   F 5 VAL B 190  GLN B 193  1  O  TYR B 191   N  ILE B 151           
SHEET    1   G 5 HIS B 233  LEU B 234  0                                        
SHEET    2   G 5 VAL B 224  THR B 230 -1  N  THR B 230   O  HIS B 233           
SHEET    3   G 5 VAL B 215  ILE B 220 -1  N  VAL B 215   O  ILE B 229           
SHEET    4   G 5 LYS B 337  GLY B 341  1  O  LEU B 339   N  ILE B 216           
SHEET    5   G 5 VAL B 373  SER B 375  1  O  GLU B 374   N  ILE B 338           
SHEET    1   H 4 ILE C  27  LEU C  30  0                                        
SHEET    2   H 4 LEU C  37  VAL C  41 -1  O  SER C  40   N  ASN C  29           
SHEET    3   H 4 GLY C  66  ALA C  69 -1  O  ALA C  69   N  LEU C  37           
SHEET    4   H 4 VAL C  60  ALA C  63 -1  N  VAL C  61   O  GLN C  68           
SHEET    1   I 4 ILE D  27  ASN D  29  0                                        
SHEET    2   I 4 ARG D  38  VAL D  41 -1  O  SER D  40   N  ASN D  29           
SHEET    3   I 4 GLY D  66  ALA D  69 -1  O  VAL D  67   N  VAL D  39           
SHEET    4   I 4 VAL D  60  ALA D  63 -1  N  VAL D  61   O  GLN D  68           
LINK         ND1 HIS A 247                ZN    ZN A 410     1555   1555  2.06  
LINK         SG  CYS A 257                ZN    ZN A 410     1555   1555  2.02  
LINK         SG  CYS A 259                ZN    ZN A 410     1555   1555  2.42  
LINK         SG  CYS A 264                ZN    ZN A 410     1555   1555  2.28  
LINK         SG  CYS B 257                ZN    ZN B 407     1555   1555  2.32  
LINK         SG  CYS B 259                ZN    ZN B 407     1555   1555  2.23  
LINK         SG  CYS B 264                ZN    ZN B 407     1555   1555  1.97  
CISPEP   1 GLY A   29    PRO A   30          0         0.12                     
CISPEP   2 GLY B   29    PRO B   30          0         0.03                     
SITE     1 AC1  3 LEU A 234  HIS A 236  THR B 230                               
SITE     1 AC2  2 ASP A 349  ASP B 251                                          
SITE     1 AC3  4 HIS A 247  CYS A 257  CYS A 259  CYS A 264                    
SITE     1 AC4  4 HIS B 247  CYS B 257  CYS B 259  CYS B 264                    
CRYST1  201.427   55.424   82.460  90.00  95.29  90.00 C 1 2 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      0.004965  0.000000  0.000460        0.00000                         
SCALE2      0.000000  0.018043  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012179        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system