GenomeNet

Database: PDB
Entry: 2RCV
LinkDB: 2RCV
Original site: 2RCV 
HEADER    OXIDOREDUCTASE                          20-SEP-07   2RCV              
TITLE     CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS SUPEROXIDE DISMUTASE       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN];                                 
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: GENERAL STRESS PROTEIN 24, GSP24;                           
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 STRAIN: SUBTILIS STR. 168;                                           
SOURCE   5 GENE: SODA, YQGD;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TOP10;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHE25                                     
KEYWDS    BACILLUS SUBTILIS, SUPEROXIDE DISMUTASE, MANGANESE, METAL-BINDING,    
KEYWDS   2 OXIDOREDUCTASE, PHOSPHORYLATION, STRESS RESPONSE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.LIU,H.E.EWIS,Y.J.HUANG,C.D.LU,P.C.TAI,I.T.WEBER                     
REVDAT   3   24-JAN-18 2RCV    1       AUTHOR                                   
REVDAT   2   24-FEB-09 2RCV    1       VERSN                                    
REVDAT   1   26-FEB-08 2RCV    0                                                
JRNL        AUTH   P.LIU,H.E.EWIS,Y.J.HUANG,C.D.LU,P.C.TAI,I.T.WEBER            
JRNL        TITL   STRUCTURE OF BACILLUS SUBTILIS SUPEROXIDE DISMUTASE.         
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  63  1003 2007              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   18084079                                                     
JRNL        DOI    10.1107/S1744309107054127                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 926359.570                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 218119                         
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) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 21751                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 60.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 21781                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE                    : 0.2850                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.10                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 2452                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.006                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12546                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 910                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.18000                                             
REMARK   3    B22 (A**2) : 6.07000                                              
REMARK   3    B33 (A**2) : -1.89000                                             
REMARK   3    B12 (A**2) : 3.48000                                              
REMARK   3    B13 (A**2) : 1.73000                                              
REMARK   3    B23 (A**2) : 1.65000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.13                            
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) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.17                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.100                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.860                           
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        : 0.38                                                 
REMARK   3   BSOL        : 38.33                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2RCV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044706.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 200.0                              
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 243111                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.13300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30500                            
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: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1XUQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% W/V POLYETHYLENE GLYCOL 4000, 0.2M   
REMARK 280  MAGNESIUM CHLORIDE HEXAHYDRATE, AND 0.1 M TRIS HYDROCHLORIDE, PH    
REMARK 280  8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS DIMER                             
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1710 ANGSTROM**2                          
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: 2                                                       
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: 1710 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, 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: 1710 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4                                                       
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: 1710 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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     LYS A   202                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B    44                                                      
REMARK 465     GLY B    45                                                      
REMARK 465     ASN B    46                                                      
REMARK 465     LYS B   202                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LYS C   202                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D    47                                                      
REMARK 465     ALA D    48                                                      
REMARK 465     LEU D    49                                                      
REMARK 465     LYS D   202                                                      
REMARK 465     MET E     1                                                      
REMARK 465     LYS E   202                                                      
REMARK 465     MET F     1                                                      
REMARK 465     LYS F   202                                                      
REMARK 465     MET G     1                                                      
REMARK 465     LYS G   202                                                      
REMARK 465     MET H     1                                                      
REMARK 465     GLU H    44                                                      
REMARK 465     GLY H    45                                                      
REMARK 465     ASN H    46                                                      
REMARK 465     LYS H   202                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG F 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG G 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG H 201    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    ASN A 148     -118.64     49.21                                   
REMARK 500    TYR A 170       -6.55   -141.37                                   
REMARK 500    GLN A 175     -128.36     46.83                                   
REMARK 500    ASN B 148     -120.22     48.32                                   
REMARK 500    TYR B 170       -2.75   -142.08                                   
REMARK 500    GLN B 175     -129.60     48.81                                   
REMARK 500    ASN C 148     -118.45     45.39                                   
REMARK 500    TYR C 170       -4.77   -146.32                                   
REMARK 500    GLN C 175     -129.12     48.30                                   
REMARK 500    ASN D 148     -120.17     48.97                                   
REMARK 500    TYR D 170       -4.17   -143.73                                   
REMARK 500    GLN D 175     -129.05     47.88                                   
REMARK 500    ASN E 148     -121.26     46.24                                   
REMARK 500    TYR E 170       -4.55   -145.20                                   
REMARK 500    GLN E 175     -133.55     48.63                                   
REMARK 500    ASN F  51       51.97    -99.45                                   
REMARK 500    ASN F 148     -119.02     50.00                                   
REMARK 500    TYR F 170       -6.08   -145.14                                   
REMARK 500    GLN F 175     -127.16     50.26                                   
REMARK 500    ASN G 148     -121.10     49.54                                   
REMARK 500    TYR G 170       -3.37   -144.06                                   
REMARK 500    GLN G 175     -131.50     48.63                                   
REMARK 500    ASN H 148     -120.34     49.66                                   
REMARK 500    TYR H 170       -6.84   -142.38                                   
REMARK 500    GLN H 175     -127.38     52.97                                   
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                              MN A 203  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 164   OD2                                                    
REMARK 620 2 HOH A 204   O    83.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 203  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 164   OD2                                                    
REMARK 620 2 HOH B 205   O    85.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 203  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 164   OD2                                                    
REMARK 620 2 HOH C 204   O    86.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 203  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 164   OD2                                                    
REMARK 620 2 HOH D 212   O    88.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E 203  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 164   OD2                                                    
REMARK 620 2 HOH E 209   O    84.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN F 203  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 164   OD2                                                    
REMARK 620 2 HOH F 209   O    88.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G 203  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 164   OD2                                                    
REMARK 620 2 HOH G 207   O    82.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN H 203  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H 164   OD2                                                    
REMARK 620 2 HOH H 204   O    84.8                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN F 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN H 203                  
DBREF  2RCV A    1   202  UNP    P54375   SODM_BACSU       1    202             
DBREF  2RCV B    1   202  UNP    P54375   SODM_BACSU       1    202             
DBREF  2RCV C    1   202  UNP    P54375   SODM_BACSU       1    202             
DBREF  2RCV D    1   202  UNP    P54375   SODM_BACSU       1    202             
DBREF  2RCV E    1   202  UNP    P54375   SODM_BACSU       1    202             
DBREF  2RCV F    1   202  UNP    P54375   SODM_BACSU       1    202             
DBREF  2RCV G    1   202  UNP    P54375   SODM_BACSU       1    202             
DBREF  2RCV H    1   202  UNP    P54375   SODM_BACSU       1    202             
SEQRES   1 A  202  MET ALA TYR GLU LEU PRO GLU LEU PRO TYR ALA TYR ASP          
SEQRES   2 A  202  ALA LEU GLU PRO HIS ILE ASP LYS GLU THR MET THR ILE          
SEQRES   3 A  202  HIS HIS THR LYS HIS HIS ASN THR TYR VAL THR ASN LEU          
SEQRES   4 A  202  ASN LYS ALA VAL GLU GLY ASN THR ALA LEU ALA ASN LYS          
SEQRES   5 A  202  SER VAL GLU GLU LEU VAL ALA ASP LEU ASP SER VAL PRO          
SEQRES   6 A  202  GLU ASN ILE ARG THR ALA VAL ARG ASN ASN GLY GLY GLY          
SEQRES   7 A  202  HIS ALA ASN HIS LYS LEU PHE TRP THR LEU LEU SER PRO          
SEQRES   8 A  202  ASN GLY GLY GLY GLU PRO THR GLY ALA LEU ALA GLU GLU          
SEQRES   9 A  202  ILE ASN SER VAL PHE GLY SER PHE ASP LYS PHE LYS GLU          
SEQRES  10 A  202  GLN PHE ALA ALA ALA ALA ALA GLY ARG PHE GLY SER GLY          
SEQRES  11 A  202  TRP ALA TRP LEU VAL VAL ASN ASN GLY LYS LEU GLU ILE          
SEQRES  12 A  202  THR SER THR PRO ASN GLN ASP SER PRO LEU SER GLU GLY          
SEQRES  13 A  202  LYS THR PRO ILE LEU GLY LEU ASP VAL TRP GLU HIS ALA          
SEQRES  14 A  202  TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO ASP TYR ILE          
SEQRES  15 A  202  SER ALA PHE TRP ASN VAL VAL ASN TRP ASP GLU VAL ALA          
SEQRES  16 A  202  ARG LEU TYR SER GLU ARG LYS                                  
SEQRES   1 B  202  MET ALA TYR GLU LEU PRO GLU LEU PRO TYR ALA TYR ASP          
SEQRES   2 B  202  ALA LEU GLU PRO HIS ILE ASP LYS GLU THR MET THR ILE          
SEQRES   3 B  202  HIS HIS THR LYS HIS HIS ASN THR TYR VAL THR ASN LEU          
SEQRES   4 B  202  ASN LYS ALA VAL GLU GLY ASN THR ALA LEU ALA ASN LYS          
SEQRES   5 B  202  SER VAL GLU GLU LEU VAL ALA ASP LEU ASP SER VAL PRO          
SEQRES   6 B  202  GLU ASN ILE ARG THR ALA VAL ARG ASN ASN GLY GLY GLY          
SEQRES   7 B  202  HIS ALA ASN HIS LYS LEU PHE TRP THR LEU LEU SER PRO          
SEQRES   8 B  202  ASN GLY GLY GLY GLU PRO THR GLY ALA LEU ALA GLU GLU          
SEQRES   9 B  202  ILE ASN SER VAL PHE GLY SER PHE ASP LYS PHE LYS GLU          
SEQRES  10 B  202  GLN PHE ALA ALA ALA ALA ALA GLY ARG PHE GLY SER GLY          
SEQRES  11 B  202  TRP ALA TRP LEU VAL VAL ASN ASN GLY LYS LEU GLU ILE          
SEQRES  12 B  202  THR SER THR PRO ASN GLN ASP SER PRO LEU SER GLU GLY          
SEQRES  13 B  202  LYS THR PRO ILE LEU GLY LEU ASP VAL TRP GLU HIS ALA          
SEQRES  14 B  202  TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO ASP TYR ILE          
SEQRES  15 B  202  SER ALA PHE TRP ASN VAL VAL ASN TRP ASP GLU VAL ALA          
SEQRES  16 B  202  ARG LEU TYR SER GLU ARG LYS                                  
SEQRES   1 C  202  MET ALA TYR GLU LEU PRO GLU LEU PRO TYR ALA TYR ASP          
SEQRES   2 C  202  ALA LEU GLU PRO HIS ILE ASP LYS GLU THR MET THR ILE          
SEQRES   3 C  202  HIS HIS THR LYS HIS HIS ASN THR TYR VAL THR ASN LEU          
SEQRES   4 C  202  ASN LYS ALA VAL GLU GLY ASN THR ALA LEU ALA ASN LYS          
SEQRES   5 C  202  SER VAL GLU GLU LEU VAL ALA ASP LEU ASP SER VAL PRO          
SEQRES   6 C  202  GLU ASN ILE ARG THR ALA VAL ARG ASN ASN GLY GLY GLY          
SEQRES   7 C  202  HIS ALA ASN HIS LYS LEU PHE TRP THR LEU LEU SER PRO          
SEQRES   8 C  202  ASN GLY GLY GLY GLU PRO THR GLY ALA LEU ALA GLU GLU          
SEQRES   9 C  202  ILE ASN SER VAL PHE GLY SER PHE ASP LYS PHE LYS GLU          
SEQRES  10 C  202  GLN PHE ALA ALA ALA ALA ALA GLY ARG PHE GLY SER GLY          
SEQRES  11 C  202  TRP ALA TRP LEU VAL VAL ASN ASN GLY LYS LEU GLU ILE          
SEQRES  12 C  202  THR SER THR PRO ASN GLN ASP SER PRO LEU SER GLU GLY          
SEQRES  13 C  202  LYS THR PRO ILE LEU GLY LEU ASP VAL TRP GLU HIS ALA          
SEQRES  14 C  202  TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO ASP TYR ILE          
SEQRES  15 C  202  SER ALA PHE TRP ASN VAL VAL ASN TRP ASP GLU VAL ALA          
SEQRES  16 C  202  ARG LEU TYR SER GLU ARG LYS                                  
SEQRES   1 D  202  MET ALA TYR GLU LEU PRO GLU LEU PRO TYR ALA TYR ASP          
SEQRES   2 D  202  ALA LEU GLU PRO HIS ILE ASP LYS GLU THR MET THR ILE          
SEQRES   3 D  202  HIS HIS THR LYS HIS HIS ASN THR TYR VAL THR ASN LEU          
SEQRES   4 D  202  ASN LYS ALA VAL GLU GLY ASN THR ALA LEU ALA ASN LYS          
SEQRES   5 D  202  SER VAL GLU GLU LEU VAL ALA ASP LEU ASP SER VAL PRO          
SEQRES   6 D  202  GLU ASN ILE ARG THR ALA VAL ARG ASN ASN GLY GLY GLY          
SEQRES   7 D  202  HIS ALA ASN HIS LYS LEU PHE TRP THR LEU LEU SER PRO          
SEQRES   8 D  202  ASN GLY GLY GLY GLU PRO THR GLY ALA LEU ALA GLU GLU          
SEQRES   9 D  202  ILE ASN SER VAL PHE GLY SER PHE ASP LYS PHE LYS GLU          
SEQRES  10 D  202  GLN PHE ALA ALA ALA ALA ALA GLY ARG PHE GLY SER GLY          
SEQRES  11 D  202  TRP ALA TRP LEU VAL VAL ASN ASN GLY LYS LEU GLU ILE          
SEQRES  12 D  202  THR SER THR PRO ASN GLN ASP SER PRO LEU SER GLU GLY          
SEQRES  13 D  202  LYS THR PRO ILE LEU GLY LEU ASP VAL TRP GLU HIS ALA          
SEQRES  14 D  202  TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO ASP TYR ILE          
SEQRES  15 D  202  SER ALA PHE TRP ASN VAL VAL ASN TRP ASP GLU VAL ALA          
SEQRES  16 D  202  ARG LEU TYR SER GLU ARG LYS                                  
SEQRES   1 E  202  MET ALA TYR GLU LEU PRO GLU LEU PRO TYR ALA TYR ASP          
SEQRES   2 E  202  ALA LEU GLU PRO HIS ILE ASP LYS GLU THR MET THR ILE          
SEQRES   3 E  202  HIS HIS THR LYS HIS HIS ASN THR TYR VAL THR ASN LEU          
SEQRES   4 E  202  ASN LYS ALA VAL GLU GLY ASN THR ALA LEU ALA ASN LYS          
SEQRES   5 E  202  SER VAL GLU GLU LEU VAL ALA ASP LEU ASP SER VAL PRO          
SEQRES   6 E  202  GLU ASN ILE ARG THR ALA VAL ARG ASN ASN GLY GLY GLY          
SEQRES   7 E  202  HIS ALA ASN HIS LYS LEU PHE TRP THR LEU LEU SER PRO          
SEQRES   8 E  202  ASN GLY GLY GLY GLU PRO THR GLY ALA LEU ALA GLU GLU          
SEQRES   9 E  202  ILE ASN SER VAL PHE GLY SER PHE ASP LYS PHE LYS GLU          
SEQRES  10 E  202  GLN PHE ALA ALA ALA ALA ALA GLY ARG PHE GLY SER GLY          
SEQRES  11 E  202  TRP ALA TRP LEU VAL VAL ASN ASN GLY LYS LEU GLU ILE          
SEQRES  12 E  202  THR SER THR PRO ASN GLN ASP SER PRO LEU SER GLU GLY          
SEQRES  13 E  202  LYS THR PRO ILE LEU GLY LEU ASP VAL TRP GLU HIS ALA          
SEQRES  14 E  202  TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO ASP TYR ILE          
SEQRES  15 E  202  SER ALA PHE TRP ASN VAL VAL ASN TRP ASP GLU VAL ALA          
SEQRES  16 E  202  ARG LEU TYR SER GLU ARG LYS                                  
SEQRES   1 F  202  MET ALA TYR GLU LEU PRO GLU LEU PRO TYR ALA TYR ASP          
SEQRES   2 F  202  ALA LEU GLU PRO HIS ILE ASP LYS GLU THR MET THR ILE          
SEQRES   3 F  202  HIS HIS THR LYS HIS HIS ASN THR TYR VAL THR ASN LEU          
SEQRES   4 F  202  ASN LYS ALA VAL GLU GLY ASN THR ALA LEU ALA ASN LYS          
SEQRES   5 F  202  SER VAL GLU GLU LEU VAL ALA ASP LEU ASP SER VAL PRO          
SEQRES   6 F  202  GLU ASN ILE ARG THR ALA VAL ARG ASN ASN GLY GLY GLY          
SEQRES   7 F  202  HIS ALA ASN HIS LYS LEU PHE TRP THR LEU LEU SER PRO          
SEQRES   8 F  202  ASN GLY GLY GLY GLU PRO THR GLY ALA LEU ALA GLU GLU          
SEQRES   9 F  202  ILE ASN SER VAL PHE GLY SER PHE ASP LYS PHE LYS GLU          
SEQRES  10 F  202  GLN PHE ALA ALA ALA ALA ALA GLY ARG PHE GLY SER GLY          
SEQRES  11 F  202  TRP ALA TRP LEU VAL VAL ASN ASN GLY LYS LEU GLU ILE          
SEQRES  12 F  202  THR SER THR PRO ASN GLN ASP SER PRO LEU SER GLU GLY          
SEQRES  13 F  202  LYS THR PRO ILE LEU GLY LEU ASP VAL TRP GLU HIS ALA          
SEQRES  14 F  202  TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO ASP TYR ILE          
SEQRES  15 F  202  SER ALA PHE TRP ASN VAL VAL ASN TRP ASP GLU VAL ALA          
SEQRES  16 F  202  ARG LEU TYR SER GLU ARG LYS                                  
SEQRES   1 G  202  MET ALA TYR GLU LEU PRO GLU LEU PRO TYR ALA TYR ASP          
SEQRES   2 G  202  ALA LEU GLU PRO HIS ILE ASP LYS GLU THR MET THR ILE          
SEQRES   3 G  202  HIS HIS THR LYS HIS HIS ASN THR TYR VAL THR ASN LEU          
SEQRES   4 G  202  ASN LYS ALA VAL GLU GLY ASN THR ALA LEU ALA ASN LYS          
SEQRES   5 G  202  SER VAL GLU GLU LEU VAL ALA ASP LEU ASP SER VAL PRO          
SEQRES   6 G  202  GLU ASN ILE ARG THR ALA VAL ARG ASN ASN GLY GLY GLY          
SEQRES   7 G  202  HIS ALA ASN HIS LYS LEU PHE TRP THR LEU LEU SER PRO          
SEQRES   8 G  202  ASN GLY GLY GLY GLU PRO THR GLY ALA LEU ALA GLU GLU          
SEQRES   9 G  202  ILE ASN SER VAL PHE GLY SER PHE ASP LYS PHE LYS GLU          
SEQRES  10 G  202  GLN PHE ALA ALA ALA ALA ALA GLY ARG PHE GLY SER GLY          
SEQRES  11 G  202  TRP ALA TRP LEU VAL VAL ASN ASN GLY LYS LEU GLU ILE          
SEQRES  12 G  202  THR SER THR PRO ASN GLN ASP SER PRO LEU SER GLU GLY          
SEQRES  13 G  202  LYS THR PRO ILE LEU GLY LEU ASP VAL TRP GLU HIS ALA          
SEQRES  14 G  202  TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO ASP TYR ILE          
SEQRES  15 G  202  SER ALA PHE TRP ASN VAL VAL ASN TRP ASP GLU VAL ALA          
SEQRES  16 G  202  ARG LEU TYR SER GLU ARG LYS                                  
SEQRES   1 H  202  MET ALA TYR GLU LEU PRO GLU LEU PRO TYR ALA TYR ASP          
SEQRES   2 H  202  ALA LEU GLU PRO HIS ILE ASP LYS GLU THR MET THR ILE          
SEQRES   3 H  202  HIS HIS THR LYS HIS HIS ASN THR TYR VAL THR ASN LEU          
SEQRES   4 H  202  ASN LYS ALA VAL GLU GLY ASN THR ALA LEU ALA ASN LYS          
SEQRES   5 H  202  SER VAL GLU GLU LEU VAL ALA ASP LEU ASP SER VAL PRO          
SEQRES   6 H  202  GLU ASN ILE ARG THR ALA VAL ARG ASN ASN GLY GLY GLY          
SEQRES   7 H  202  HIS ALA ASN HIS LYS LEU PHE TRP THR LEU LEU SER PRO          
SEQRES   8 H  202  ASN GLY GLY GLY GLU PRO THR GLY ALA LEU ALA GLU GLU          
SEQRES   9 H  202  ILE ASN SER VAL PHE GLY SER PHE ASP LYS PHE LYS GLU          
SEQRES  10 H  202  GLN PHE ALA ALA ALA ALA ALA GLY ARG PHE GLY SER GLY          
SEQRES  11 H  202  TRP ALA TRP LEU VAL VAL ASN ASN GLY LYS LEU GLU ILE          
SEQRES  12 H  202  THR SER THR PRO ASN GLN ASP SER PRO LEU SER GLU GLY          
SEQRES  13 H  202  LYS THR PRO ILE LEU GLY LEU ASP VAL TRP GLU HIS ALA          
SEQRES  14 H  202  TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO ASP TYR ILE          
SEQRES  15 H  202  SER ALA PHE TRP ASN VAL VAL ASN TRP ASP GLU VAL ALA          
SEQRES  16 H  202  ARG LEU TYR SER GLU ARG LYS                                  
HET     MN  A 203       1                                                       
HET     MN  B 203       1                                                       
HET     MN  C 203       1                                                       
HET     MN  D 203       1                                                       
HET     MN  E 203       1                                                       
HET     MN  F 203       1                                                       
HET     MN  G 203       1                                                       
HET     MN  H 203       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   9   MN    8(MN 2+)                                                     
FORMUL  17  HOH   *910(H2 O)                                                    
HELIX    1   1 ASP A   20  LYS A   30  1                                  11    
HELIX    2   2 LYS A   30  VAL A   43  1                                  14    
HELIX    3   3 ASN A   46  ASN A   51  1                                   6    
HELIX    4   4 SER A   53  ASP A   60  1                                   8    
HELIX    5   5 LEU A   61  VAL A   64  5                                   4    
HELIX    6   6 ILE A   68  LEU A   88  1                                  21    
HELIX    7   7 THR A   98  GLY A  110  1                                  13    
HELIX    8   8 SER A  111  ARG A  126  1                                  16    
HELIX    9   9 SER A  151  GLY A  156  5                                   6    
HELIX   10  10 TRP A  166  ALA A  169  5                                   4    
HELIX   11  11 TYR A  170  GLN A  175  1                                   6    
HELIX   12  12 ARG A  177  TRP A  186  1                                  10    
HELIX   13  13 ASN A  190  ARG A  201  1                                  12    
HELIX   14  14 ASP B   20  LYS B   30  1                                  11    
HELIX   15  15 LYS B   30  VAL B   43  1                                  14    
HELIX   16  16 ALA B   48  LYS B   52  5                                   5    
HELIX   17  17 SER B   53  ASP B   60  1                                   8    
HELIX   18  18 LEU B   61  VAL B   64  5                                   4    
HELIX   19  19 ILE B   68  LEU B   88  1                                  21    
HELIX   20  20 THR B   98  GLY B  110  1                                  13    
HELIX   21  21 SER B  111  ARG B  126  1                                  16    
HELIX   22  22 SER B  151  GLY B  156  5                                   6    
HELIX   23  23 TRP B  166  ALA B  169  5                                   4    
HELIX   24  24 TYR B  170  GLN B  175  1                                   6    
HELIX   25  25 ARG B  177  TRP B  186  1                                  10    
HELIX   26  26 ASN B  190  ARG B  201  1                                  12    
HELIX   27  27 ASP C   20  LYS C   30  1                                  11    
HELIX   28  28 LYS C   30  VAL C   43  1                                  14    
HELIX   29  29 ASN C   46  ASN C   51  1                                   6    
HELIX   30  30 SER C   53  ASP C   60  1                                   8    
HELIX   31  31 ILE C   68  LEU C   88  1                                  21    
HELIX   32  32 THR C   98  GLY C  110  1                                  13    
HELIX   33  33 SER C  111  ARG C  126  1                                  16    
HELIX   34  34 SER C  151  GLY C  156  5                                   6    
HELIX   35  35 TRP C  166  ALA C  169  5                                   4    
HELIX   36  36 TYR C  170  GLN C  175  1                                   6    
HELIX   37  37 ARG C  177  TRP C  186  1                                  10    
HELIX   38  38 ASN C  190  ARG C  201  1                                  12    
HELIX   39  39 ASP D   20  LYS D   30  1                                  11    
HELIX   40  40 LYS D   30  GLU D   44  1                                  15    
HELIX   41  41 SER D   53  ASP D   60  1                                   8    
HELIX   42  42 LEU D   61  VAL D   64  5                                   4    
HELIX   43  43 ILE D   68  LEU D   88  1                                  21    
HELIX   44  44 THR D   98  GLY D  110  1                                  13    
HELIX   45  45 SER D  111  GLY D  125  1                                  15    
HELIX   46  46 SER D  151  GLY D  156  5                                   6    
HELIX   47  47 TRP D  166  ALA D  169  5                                   4    
HELIX   48  48 TYR D  170  GLN D  175  1                                   6    
HELIX   49  49 ARG D  177  TRP D  186  1                                  10    
HELIX   50  50 ASN D  190  ARG D  201  1                                  12    
HELIX   51  51 ASP E   20  LYS E   30  1                                  11    
HELIX   52  52 LYS E   30  GLU E   44  1                                  15    
HELIX   53  53 ASN E   46  ASN E   51  1                                   6    
HELIX   54  54 SER E   53  ASP E   60  1                                   8    
HELIX   55  55 LEU E   61  VAL E   64  5                                   4    
HELIX   56  56 PRO E   65  LEU E   88  1                                  24    
HELIX   57  57 THR E   98  GLY E  110  1                                  13    
HELIX   58  58 SER E  111  ARG E  126  1                                  16    
HELIX   59  59 SER E  151  GLY E  156  5                                   6    
HELIX   60  60 TRP E  166  ALA E  169  5                                   4    
HELIX   61  61 TYR E  170  GLN E  175  1                                   6    
HELIX   62  62 ARG E  177  TRP E  186  1                                  10    
HELIX   63  63 ASN E  190  ARG E  201  1                                  12    
HELIX   64  64 ASP F   20  LYS F   30  1                                  11    
HELIX   65  65 LYS F   30  VAL F   43  1                                  14    
HELIX   66  66 ASN F   46  ASN F   51  1                                   6    
HELIX   67  67 SER F   53  ASP F   60  1                                   8    
HELIX   68  68 LEU F   61  VAL F   64  5                                   4    
HELIX   69  69 ILE F   68  LEU F   88  1                                  21    
HELIX   70  70 THR F   98  GLY F  110  1                                  13    
HELIX   71  71 SER F  111  ARG F  126  1                                  16    
HELIX   72  72 SER F  151  GLY F  156  5                                   6    
HELIX   73  73 TRP F  166  ALA F  169  5                                   4    
HELIX   74  74 TYR F  170  GLN F  175  1                                   6    
HELIX   75  75 ARG F  177  TRP F  186  1                                  10    
HELIX   76  76 ASN F  190  ARG F  201  1                                  12    
HELIX   77  77 ASP G   20  LYS G   30  1                                  11    
HELIX   78  78 LYS G   30  GLU G   44  1                                  15    
HELIX   79  79 ASN G   46  ASN G   51  1                                   6    
HELIX   80  80 SER G   53  ASP G   60  1                                   8    
HELIX   81  81 LEU G   61  VAL G   64  5                                   4    
HELIX   82  82 PRO G   65  LEU G   88  1                                  24    
HELIX   83  83 THR G   98  GLY G  110  1                                  13    
HELIX   84  84 SER G  111  ARG G  126  1                                  16    
HELIX   85  85 SER G  151  GLY G  156  5                                   6    
HELIX   86  86 TRP G  166  ALA G  169  5                                   4    
HELIX   87  87 TYR G  170  GLN G  175  1                                   6    
HELIX   88  88 ARG G  177  TRP G  186  1                                  10    
HELIX   89  89 ASN G  190  ARG G  201  1                                  12    
HELIX   90  90 ASP H   20  LYS H   30  1                                  11    
HELIX   91  91 LYS H   30  VAL H   43  1                                  14    
HELIX   92  92 THR H   47  ASN H   51  5                                   5    
HELIX   93  93 SER H   53  ALA H   59  1                                   7    
HELIX   94  94 ASP H   60  VAL H   64  5                                   5    
HELIX   95  95 PRO H   65  LEU H   88  1                                  24    
HELIX   96  96 THR H   98  GLY H  110  1                                  13    
HELIX   97  97 SER H  111  ARG H  126  1                                  16    
HELIX   98  98 SER H  151  GLY H  156  5                                   6    
HELIX   99  99 TRP H  166  ALA H  169  5                                   4    
HELIX  100 100 TYR H  170  GLN H  175  1                                   6    
HELIX  101 101 ARG H  177  TRP H  186  1                                  10    
HELIX  102 102 ASN H  190  ARG H  201  1                                  12    
SHEET    1   A 3 LYS A 140  PRO A 147  0                                        
SHEET    2   A 3 GLY A 130  ASN A 137 -1  N  ASN A 137   O  LYS A 140           
SHEET    3   A 3 THR A 158  ASP A 164 -1  O  ILE A 160   N  LEU A 134           
SHEET    1   B 3 LYS B 140  PRO B 147  0                                        
SHEET    2   B 3 GLY B 130  ASN B 137 -1  N  TRP B 133   O  THR B 144           
SHEET    3   B 3 THR B 158  ASP B 164 -1  O  ILE B 160   N  LEU B 134           
SHEET    1   C 3 LYS C 140  PRO C 147  0                                        
SHEET    2   C 3 GLY C 130  ASN C 137 -1  N  TRP C 133   O  THR C 144           
SHEET    3   C 3 THR C 158  ASP C 164 -1  O  ILE C 160   N  LEU C 134           
SHEET    1   D 3 LYS D 140  PRO D 147  0                                        
SHEET    2   D 3 GLY D 130  ASN D 137 -1  N  TRP D 133   O  THR D 144           
SHEET    3   D 3 THR D 158  ASP D 164 -1  O  ILE D 160   N  LEU D 134           
SHEET    1   E 3 LYS E 140  PRO E 147  0                                        
SHEET    2   E 3 GLY E 130  ASN E 137 -1  N  TRP E 133   O  THR E 144           
SHEET    3   E 3 THR E 158  ASP E 164 -1  O  ILE E 160   N  LEU E 134           
SHEET    1   F 3 LYS F 140  PRO F 147  0                                        
SHEET    2   F 3 GLY F 130  ASN F 137 -1  N  TRP F 133   O  THR F 144           
SHEET    3   F 3 THR F 158  ASP F 164 -1  O  ILE F 160   N  LEU F 134           
SHEET    1   G 3 LYS G 140  PRO G 147  0                                        
SHEET    2   G 3 GLY G 130  ASN G 137 -1  N  TRP G 133   O  THR G 144           
SHEET    3   G 3 THR G 158  ASP G 164 -1  O  ILE G 160   N  LEU G 134           
SHEET    1   H 3 LYS H 140  PRO H 147  0                                        
SHEET    2   H 3 GLY H 130  ASN H 137 -1  N  ASN H 137   O  LYS H 140           
SHEET    3   H 3 THR H 158  ASP H 164 -1  O  ILE H 160   N  LEU H 134           
LINK         OD2 ASP A 164                MN    MN A 203     1555   1555  2.04  
LINK         OD2 ASP B 164                MN    MN B 203     1555   1555  2.01  
LINK         OD2 ASP C 164                MN    MN C 203     1555   1555  2.04  
LINK         OD2 ASP D 164                MN    MN D 203     1555   1555  2.10  
LINK         OD2 ASP E 164                MN    MN E 203     1555   1555  2.05  
LINK         OD2 ASP F 164                MN    MN F 203     1555   1555  2.05  
LINK         OD2 ASP G 164                MN    MN G 203     1555   1555  2.02  
LINK         OD2 ASP H 164                MN    MN H 203     1555   1555  2.02  
LINK        MN    MN G 203                 O   HOH G 207     1555   1555  2.23  
LINK        MN    MN A 203                 O   HOH A 204     1555   1555  2.17  
LINK        MN    MN E 203                 O   HOH E 209     1555   1555  2.20  
LINK        MN    MN F 203                 O   HOH F 209     1555   1555  2.35  
LINK        MN    MN B 203                 O   HOH B 205     1555   1555  2.26  
LINK        MN    MN C 203                 O   HOH C 204     1555   1555  2.15  
LINK        MN    MN D 203                 O   HOH D 212     1555   1555  2.36  
LINK        MN    MN H 203                 O   HOH H 204     1555   1555  2.18  
CISPEP   1 GLU A   16    PRO A   17          0        -0.03                     
CISPEP   2 GLU B   16    PRO B   17          0         1.08                     
CISPEP   3 GLU C   16    PRO C   17          0         0.22                     
CISPEP   4 GLU D   16    PRO D   17          0        -0.73                     
CISPEP   5 GLU E   16    PRO E   17          0         0.17                     
CISPEP   6 GLU F   16    PRO F   17          0         0.25                     
CISPEP   7 GLU G   16    PRO G   17          0         1.16                     
CISPEP   8 GLU H   16    PRO H   17          0         0.44                     
SITE     1 AC1  5 HIS G  27  HIS G  82  ASP G 164  HIS G 168                    
SITE     2 AC1  5 HOH G 207                                                     
SITE     1 AC2  5 HIS A  27  HIS A  82  ASP A 164  HIS A 168                    
SITE     2 AC2  5 HOH A 204                                                     
SITE     1 AC3  5 HIS E  27  HIS E  82  ASP E 164  HIS E 168                    
SITE     2 AC3  5 HOH E 209                                                     
SITE     1 AC4  5 HIS F  27  HIS F  82  ASP F 164  HIS F 168                    
SITE     2 AC4  5 HOH F 209                                                     
SITE     1 AC5  5 HIS B  27  HIS B  82  ASP B 164  HIS B 168                    
SITE     2 AC5  5 HOH B 205                                                     
SITE     1 AC6  5 HIS C  27  HIS C  82  ASP C 164  HIS C 168                    
SITE     2 AC6  5 HOH C 204                                                     
SITE     1 AC7  5 HIS D  27  HIS D  82  ASP D 164  HIS D 168                    
SITE     2 AC7  5 HOH D 212                                                     
SITE     1 AC8  5 HIS H  27  HIS H  82  ASP H 164  HIS H 168                    
SITE     2 AC8  5 HOH H 204                                                     
CRYST1   68.369   84.034   91.951  99.13 105.98 105.58 P 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      0.014627  0.004077  0.005386        0.00000                         
SCALE2      0.000000  0.012354  0.003206        0.00000                         
SCALE3      0.000000  0.000000  0.011687        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system