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Database: PDB
Entry: 1KKC
LinkDB: 1KKC
Original site: 1KKC 
HEADER    OXIDOREDUCTASE                          07-DEC-01   1KKC              
TITLE     CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS MNSOD                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MANGANESE SUPEROXIDE DISMUTASE;                            
COMPND   3 CHAIN: A, B, X, Y;                                                   
COMPND   4 SYNONYM: MNSOD;                                                      
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATUS;                          
SOURCE   3 ORGANISM_TAXID: 5085;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: M15;                                       
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PQE16                                 
KEYWDS    HOMOTETRAMER, OXIDOREDUCTASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.FLUCKIGER,P.R.E.MITTL,L.SCAPOZZA,H.FIJTEN,G.FOLKERS,                
AUTHOR   2 M.G.GRUTTER,K.BLASER,R.CRAMERI                                       
REVDAT   5   24-FEB-09 1KKC    1       VERSN                                    
REVDAT   4   01-APR-03 1KKC    1       JRNL                                     
REVDAT   3   30-JAN-02 1KKC    1       JRNL                                     
REVDAT   2   16-JAN-02 1KKC    1       REMARK                                   
REVDAT   1   28-DEC-01 1KKC    0                                                
JRNL        AUTH   S.FLUCKIGER,P.R.MITTL,L.SCAPOZZA,H.FIJTEN,                   
JRNL        AUTH 2 G.FOLKERS,M.G.GRUTTER,K.BLASER,R.CRAMERI                     
JRNL        TITL   COMPARISON OF THE CRYSTAL STRUCTURES OF THE HUMAN            
JRNL        TITL 2 MANGANESE SUPEROXIDE DISMUTASE AND THE HOMOLOGOUS            
JRNL        TITL 3 ASPERGILLUS FUMIGATUS ALLERGEN AT 2-A RESOLUTION.            
JRNL        REF    J.IMMUNOL.                    V. 168  1267 2002              
JRNL        REFN                   ISSN 0022-1767                               
JRNL        PMID   11801664                                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 56538                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 5744                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
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            : 6310                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 745                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.54400                                             
REMARK   3    B22 (A**2) : -2.68400                                             
REMARK   3    B33 (A**2) : 5.22800                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
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 : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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 1KKC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB015044.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR591                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : PROPHYSICS MIRRORS                 
REMARK 200  OPTICS                         : DOUBLE-FOCUSING MIRROR SYSTEM      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : PROPHYSICS XRM-216                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56622                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
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) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 34.8                               
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: AMORE                                                 
REMARK 200 STARTING MODEL: HOMOLOGY MODEL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, PH 8.0, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 296K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       32.94100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.64050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.34850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.64050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.94100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.34850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, X, Y                            
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     GLY A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     ILE A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     ILE A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     GLY A   214                                                      
REMARK 465     GLY A   215                                                      
REMARK 465     HIS A   216                                                      
REMARK 465     PRO A   217                                                      
REMARK 465     PHE A   218                                                      
REMARK 465     MET A   219                                                      
REMARK 465     LYS A   220                                                      
REMARK 465     LEU A   221                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     ILE B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     ILE B     9                                                      
REMARK 465     ASN B    10                                                      
REMARK 465     THR B    11                                                      
REMARK 465     MET B    12                                                      
REMARK 465     SER B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     GLY B   214                                                      
REMARK 465     GLY B   215                                                      
REMARK 465     HIS B   216                                                      
REMARK 465     PRO B   217                                                      
REMARK 465     PHE B   218                                                      
REMARK 465     MET B   219                                                      
REMARK 465     LYS B   220                                                      
REMARK 465     LEU B   221                                                      
REMARK 465     GLY X     1                                                      
REMARK 465     THR X     2                                                      
REMARK 465     SER X     3                                                      
REMARK 465     PRO X     4                                                      
REMARK 465     ILE X     5                                                      
REMARK 465     GLN X     6                                                      
REMARK 465     THR X     7                                                      
REMARK 465     PRO X     8                                                      
REMARK 465     ILE X     9                                                      
REMARK 465     ASN X    10                                                      
REMARK 465     THR X    11                                                      
REMARK 465     MET X    12                                                      
REMARK 465     SER X    13                                                      
REMARK 465     GLN X    14                                                      
REMARK 465     GLY X   215                                                      
REMARK 465     HIS X   216                                                      
REMARK 465     PRO X   217                                                      
REMARK 465     PHE X   218                                                      
REMARK 465     MET X   219                                                      
REMARK 465     LYS X   220                                                      
REMARK 465     LEU X   221                                                      
REMARK 465     GLY Y     1                                                      
REMARK 465     THR Y     2                                                      
REMARK 465     SER Y     3                                                      
REMARK 465     PRO Y     4                                                      
REMARK 465     ILE Y     5                                                      
REMARK 465     GLN Y     6                                                      
REMARK 465     THR Y     7                                                      
REMARK 465     PRO Y     8                                                      
REMARK 465     ILE Y     9                                                      
REMARK 465     ASN Y    10                                                      
REMARK 465     THR Y    11                                                      
REMARK 465     MET Y    12                                                      
REMARK 465     SER Y    13                                                      
REMARK 465     GLY Y   214                                                      
REMARK 465     GLY Y   215                                                      
REMARK 465     HIS Y   216                                                      
REMARK 465     PRO Y   217                                                      
REMARK 465     PHE Y   218                                                      
REMARK 465     MET Y   219                                                      
REMARK 465     LYS Y   220                                                      
REMARK 465     LEU Y   221                                                      
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    LYS A  43      -64.38   -109.70                                   
REMARK 500    ALA A  96      148.67   -171.83                                   
REMARK 500    ASP A 160     -115.30     46.45                                   
REMARK 500    TYR A 180      -14.82   -153.13                                   
REMARK 500    LEU A 185     -134.28     56.38                                   
REMARK 500    LYS B  43      -69.31   -104.69                                   
REMARK 500    ASN B  94       30.28    -98.99                                   
REMARK 500    LYS B  99        6.02    -69.06                                   
REMARK 500    ASP B 160     -120.56     51.06                                   
REMARK 500    TYR B 180      -16.22   -151.00                                   
REMARK 500    LEU B 185     -135.39     56.13                                   
REMARK 500    LYS X  43      -71.13   -103.36                                   
REMARK 500    ALA X  96      146.93   -172.14                                   
REMARK 500    ASP X 160     -116.06     50.14                                   
REMARK 500    TYR X 180      -15.13   -150.98                                   
REMARK 500    LEU X 185     -137.16     59.73                                   
REMARK 500    LYS Y  43      -67.84   -105.36                                   
REMARK 500    ASP Y 160     -115.25     55.56                                   
REMARK 500    TYR Y 180      -19.56   -151.59                                   
REMARK 500    LEU Y 185     -136.63     55.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A  31         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2157        DISTANCE =  6.08 ANGSTROMS                       
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 A2001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  40   NE2                                                    
REMARK 620 2 HIS A  88   NE2  89.6                                              
REMARK 620 3 HIS A 178   NE2  93.1 130.4                                        
REMARK 620 4 HOH A2005   O   171.3  96.0  88.3                                  
REMARK 620 5 ASP A 174   OD2  88.4 112.4 117.1  83.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B2002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  40   NE2                                                    
REMARK 620 2 HIS B  88   NE2  87.3                                              
REMARK 620 3 ASP B 174   OD2  88.4 104.3                                        
REMARK 620 4 HIS B 178   NE2  96.5 131.0 124.6                                  
REMARK 620 5 HOH B2003   O   169.8  95.3  81.4  89.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN X2003  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP X 174   OD2                                                    
REMARK 620 2 HOH X2004   O    83.9                                              
REMARK 620 3 HIS X  40   NE2  80.7 164.6                                        
REMARK 620 4 HIS X 178   NE2 117.2  98.2  87.7                                  
REMARK 620 5 HIS X  88   NE2 107.5  97.7  88.2 133.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN Y2004  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP Y 174   OD2                                                    
REMARK 620 2 HIS Y 178   NE2 120.3                                              
REMARK 620 3 HIS Y  40   NE2  92.6  95.5                                        
REMARK 620 4 HIS Y  88   NE2 110.7 128.6  87.8                                  
REMARK 620 5 HOH Y2006   O    80.8  93.8 170.4  88.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 2001                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 2002                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN X 2003                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN Y 2004                 
DBREF  1KKC A    1   221  UNP    Q92450   SODM_ASPFU       1    221             
DBREF  1KKC B    1   221  UNP    Q92450   SODM_ASPFU       1    221             
DBREF  1KKC X    1   221  UNP    Q92450   SODM_ASPFU       1    221             
DBREF  1KKC Y    1   221  UNP    Q92450   SODM_ASPFU       1    221             
SEQRES   1 A  221  GLY THR SER PRO ILE GLN THR PRO ILE ASN THR MET SER          
SEQRES   2 A  221  GLN GLN TYR THR LEU PRO PRO LEU PRO TYR PRO TYR ASP          
SEQRES   3 A  221  ALA LEU GLN PRO TYR ILE SER GLN GLN ILE MET GLU LEU          
SEQRES   4 A  221  HIS HIS LYS LYS HIS HIS GLN THR TYR VAL ASN GLY LEU          
SEQRES   5 A  221  ASN ALA ALA LEU GLU ALA GLN LYS LYS ALA ALA GLU ALA          
SEQRES   6 A  221  THR ASP VAL PRO LYS LEU VAL SER VAL GLN GLN ALA ILE          
SEQRES   7 A  221  LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER LEU PHE          
SEQRES   8 A  221  TRP LYS ASN LEU ALA PRO GLU LYS SER GLY GLY GLY LYS          
SEQRES   9 A  221  ILE ASP GLN ALA PRO VAL LEU LYS ALA ALA ILE GLU GLN          
SEQRES  10 A  221  ARG TRP GLY SER PHE ASP LYS PHE LYS ASP ALA PHE ASN          
SEQRES  11 A  221  THR THR LEU LEU GLY ILE GLN GLY SER GLY TRP GLY TRP          
SEQRES  12 A  221  LEU VAL THR ASP GLY PRO LYS GLY LYS LEU ASP ILE THR          
SEQRES  13 A  221  THR THR HIS ASP GLN ASP PRO VAL THR GLY ALA ALA PRO          
SEQRES  14 A  221  VAL PHE GLY VAL ASP MET TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 A  221  GLN TYR LEU ASN ASP LYS ALA SER TYR ALA LYS GLY ILE          
SEQRES  16 A  221  TRP ASN VAL ILE ASN TRP ALA GLU ALA GLU ASN ARG TYR          
SEQRES  17 A  221  ILE ALA GLY ASP LYS GLY GLY HIS PRO PHE MET LYS LEU          
SEQRES   1 B  221  GLY THR SER PRO ILE GLN THR PRO ILE ASN THR MET SER          
SEQRES   2 B  221  GLN GLN TYR THR LEU PRO PRO LEU PRO TYR PRO TYR ASP          
SEQRES   3 B  221  ALA LEU GLN PRO TYR ILE SER GLN GLN ILE MET GLU LEU          
SEQRES   4 B  221  HIS HIS LYS LYS HIS HIS GLN THR TYR VAL ASN GLY LEU          
SEQRES   5 B  221  ASN ALA ALA LEU GLU ALA GLN LYS LYS ALA ALA GLU ALA          
SEQRES   6 B  221  THR ASP VAL PRO LYS LEU VAL SER VAL GLN GLN ALA ILE          
SEQRES   7 B  221  LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER LEU PHE          
SEQRES   8 B  221  TRP LYS ASN LEU ALA PRO GLU LYS SER GLY GLY GLY LYS          
SEQRES   9 B  221  ILE ASP GLN ALA PRO VAL LEU LYS ALA ALA ILE GLU GLN          
SEQRES  10 B  221  ARG TRP GLY SER PHE ASP LYS PHE LYS ASP ALA PHE ASN          
SEQRES  11 B  221  THR THR LEU LEU GLY ILE GLN GLY SER GLY TRP GLY TRP          
SEQRES  12 B  221  LEU VAL THR ASP GLY PRO LYS GLY LYS LEU ASP ILE THR          
SEQRES  13 B  221  THR THR HIS ASP GLN ASP PRO VAL THR GLY ALA ALA PRO          
SEQRES  14 B  221  VAL PHE GLY VAL ASP MET TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 B  221  GLN TYR LEU ASN ASP LYS ALA SER TYR ALA LYS GLY ILE          
SEQRES  16 B  221  TRP ASN VAL ILE ASN TRP ALA GLU ALA GLU ASN ARG TYR          
SEQRES  17 B  221  ILE ALA GLY ASP LYS GLY GLY HIS PRO PHE MET LYS LEU          
SEQRES   1 X  221  GLY THR SER PRO ILE GLN THR PRO ILE ASN THR MET SER          
SEQRES   2 X  221  GLN GLN TYR THR LEU PRO PRO LEU PRO TYR PRO TYR ASP          
SEQRES   3 X  221  ALA LEU GLN PRO TYR ILE SER GLN GLN ILE MET GLU LEU          
SEQRES   4 X  221  HIS HIS LYS LYS HIS HIS GLN THR TYR VAL ASN GLY LEU          
SEQRES   5 X  221  ASN ALA ALA LEU GLU ALA GLN LYS LYS ALA ALA GLU ALA          
SEQRES   6 X  221  THR ASP VAL PRO LYS LEU VAL SER VAL GLN GLN ALA ILE          
SEQRES   7 X  221  LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER LEU PHE          
SEQRES   8 X  221  TRP LYS ASN LEU ALA PRO GLU LYS SER GLY GLY GLY LYS          
SEQRES   9 X  221  ILE ASP GLN ALA PRO VAL LEU LYS ALA ALA ILE GLU GLN          
SEQRES  10 X  221  ARG TRP GLY SER PHE ASP LYS PHE LYS ASP ALA PHE ASN          
SEQRES  11 X  221  THR THR LEU LEU GLY ILE GLN GLY SER GLY TRP GLY TRP          
SEQRES  12 X  221  LEU VAL THR ASP GLY PRO LYS GLY LYS LEU ASP ILE THR          
SEQRES  13 X  221  THR THR HIS ASP GLN ASP PRO VAL THR GLY ALA ALA PRO          
SEQRES  14 X  221  VAL PHE GLY VAL ASP MET TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 X  221  GLN TYR LEU ASN ASP LYS ALA SER TYR ALA LYS GLY ILE          
SEQRES  16 X  221  TRP ASN VAL ILE ASN TRP ALA GLU ALA GLU ASN ARG TYR          
SEQRES  17 X  221  ILE ALA GLY ASP LYS GLY GLY HIS PRO PHE MET LYS LEU          
SEQRES   1 Y  221  GLY THR SER PRO ILE GLN THR PRO ILE ASN THR MET SER          
SEQRES   2 Y  221  GLN GLN TYR THR LEU PRO PRO LEU PRO TYR PRO TYR ASP          
SEQRES   3 Y  221  ALA LEU GLN PRO TYR ILE SER GLN GLN ILE MET GLU LEU          
SEQRES   4 Y  221  HIS HIS LYS LYS HIS HIS GLN THR TYR VAL ASN GLY LEU          
SEQRES   5 Y  221  ASN ALA ALA LEU GLU ALA GLN LYS LYS ALA ALA GLU ALA          
SEQRES   6 Y  221  THR ASP VAL PRO LYS LEU VAL SER VAL GLN GLN ALA ILE          
SEQRES   7 Y  221  LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER LEU PHE          
SEQRES   8 Y  221  TRP LYS ASN LEU ALA PRO GLU LYS SER GLY GLY GLY LYS          
SEQRES   9 Y  221  ILE ASP GLN ALA PRO VAL LEU LYS ALA ALA ILE GLU GLN          
SEQRES  10 Y  221  ARG TRP GLY SER PHE ASP LYS PHE LYS ASP ALA PHE ASN          
SEQRES  11 Y  221  THR THR LEU LEU GLY ILE GLN GLY SER GLY TRP GLY TRP          
SEQRES  12 Y  221  LEU VAL THR ASP GLY PRO LYS GLY LYS LEU ASP ILE THR          
SEQRES  13 Y  221  THR THR HIS ASP GLN ASP PRO VAL THR GLY ALA ALA PRO          
SEQRES  14 Y  221  VAL PHE GLY VAL ASP MET TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 Y  221  GLN TYR LEU ASN ASP LYS ALA SER TYR ALA LYS GLY ILE          
SEQRES  16 Y  221  TRP ASN VAL ILE ASN TRP ALA GLU ALA GLU ASN ARG TYR          
SEQRES  17 Y  221  ILE ALA GLY ASP LYS GLY GLY HIS PRO PHE MET LYS LEU          
HET     MN  A2001       1                                                       
HET     MN  B2002       1                                                       
HET     MN  X2003       1                                                       
HET     MN  Y2004       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   9  HOH   *745(H2 O)                                                    
HELIX    1   1 SER A   33  LYS A   43  1                                  11    
HELIX    2   2 LYS A   43  ALA A   65  1                                  23    
HELIX    3   3 ASP A   67  ASN A   94  1                                  28    
HELIX    4   4 PRO A   97  GLY A  101  5                                   5    
HELIX    5   5 LYS A  104  GLN A  107  5                                   4    
HELIX    6   6 ALA A  108  GLY A  120  1                                  13    
HELIX    7   7 SER A  121  ILE A  136  1                                  16    
HELIX    8   8 TRP A  176  ALA A  179  5                                   4    
HELIX    9   9 TYR A  180  LEU A  185  1                                   6    
HELIX   10  10 ASP A  187  TRP A  196  1                                  10    
HELIX   11  11 ASN A  197  ILE A  199  5                                   3    
HELIX   12  12 ASN A  200  GLY A  211  1                                  12    
HELIX   13  13 SER B   33  LYS B   43  1                                  11    
HELIX   14  14 LYS B   43  ALA B   65  1                                  23    
HELIX   15  15 ASP B   67  VAL B   74  1                                   8    
HELIX   16  16 VAL B   74  ASN B   94  1                                  21    
HELIX   17  17 PRO B   97  GLY B  101  5                                   5    
HELIX   18  18 LYS B  104  GLN B  107  5                                   4    
HELIX   19  19 ALA B  108  GLY B  120  1                                  13    
HELIX   20  20 SER B  121  ILE B  136  1                                  16    
HELIX   21  21 TRP B  176  ALA B  179  5                                   4    
HELIX   22  22 TYR B  180  LEU B  185  1                                   6    
HELIX   23  23 ASP B  187  TRP B  196  1                                  10    
HELIX   24  24 ASN B  197  ILE B  199  5                                   3    
HELIX   25  25 ASN B  200  GLY B  211  1                                  12    
HELIX   26  26 SER X   33  LYS X   43  1                                  11    
HELIX   27  27 LYS X   43  ALA X   65  1                                  23    
HELIX   28  28 ASP X   67  VAL X   74  1                                   8    
HELIX   29  29 VAL X   74  ASN X   94  1                                  21    
HELIX   30  30 PRO X   97  GLY X  101  5                                   5    
HELIX   31  31 LYS X  104  GLN X  107  5                                   4    
HELIX   32  32 ALA X  108  GLY X  120  1                                  13    
HELIX   33  33 SER X  121  ILE X  136  1                                  16    
HELIX   34  34 TRP X  176  ALA X  179  5                                   4    
HELIX   35  35 TYR X  180  LEU X  185  1                                   6    
HELIX   36  36 ASP X  187  TRP X  196  1                                  10    
HELIX   37  37 ASN X  197  ILE X  199  5                                   3    
HELIX   38  38 ASN X  200  GLY X  211  1                                  12    
HELIX   39  39 SER Y   33  LYS Y   43  1                                  11    
HELIX   40  40 LYS Y   43  ALA Y   65  1                                  23    
HELIX   41  41 ASP Y   67  ASN Y   94  1                                  28    
HELIX   42  42 PRO Y   97  GLY Y  101  5                                   5    
HELIX   43  43 LYS Y  104  GLN Y  107  5                                   4    
HELIX   44  44 ALA Y  108  GLY Y  120  1                                  13    
HELIX   45  45 SER Y  121  ILE Y  136  1                                  16    
HELIX   46  46 TRP Y  176  ALA Y  179  5                                   4    
HELIX   47  47 TYR Y  180  LEU Y  185  1                                   6    
HELIX   48  48 ASP Y  187  TRP Y  196  1                                  10    
HELIX   49  49 ASN Y  197  ILE Y  199  5                                   3    
HELIX   50  50 ASN Y  200  GLY Y  211  1                                  12    
SHEET    1   A 3 LEU A 153  HIS A 159  0                                        
SHEET    2   A 3 GLY A 140  THR A 146 -1  N  TRP A 143   O  THR A 156           
SHEET    3   A 3 ALA A 168  ASP A 174 -1  O  VAL A 170   N  LEU A 144           
SHEET    1   B 3 LEU B 153  HIS B 159  0                                        
SHEET    2   B 3 GLY B 140  THR B 146 -1  N  TRP B 143   O  THR B 156           
SHEET    3   B 3 ALA B 168  ASP B 174 -1  O  VAL B 170   N  LEU B 144           
SHEET    1   C 3 LEU X 153  HIS X 159  0                                        
SHEET    2   C 3 GLY X 140  THR X 146 -1  N  VAL X 145   O  ASP X 154           
SHEET    3   C 3 ALA X 168  ASP X 174 -1  O  VAL X 170   N  LEU X 144           
SHEET    1   D 3 LEU Y 153  HIS Y 159  0                                        
SHEET    2   D 3 GLY Y 140  THR Y 146 -1  N  TRP Y 143   O  THR Y 156           
SHEET    3   D 3 ALA Y 168  ASP Y 174 -1  O  ALA Y 168   N  THR Y 146           
LINK        MN    MN A2001                 NE2 HIS A  40     1555   1555  2.18  
LINK        MN    MN A2001                 NE2 HIS A  88     1555   1555  2.21  
LINK        MN    MN A2001                 NE2 HIS A 178     1555   1555  2.23  
LINK        MN    MN A2001                 O   HOH A2005     1555   1555  2.24  
LINK        MN    MN A2001                 OD2 ASP A 174     1555   1555  1.97  
LINK        MN    MN B2002                 NE2 HIS B  40     1555   1555  2.11  
LINK        MN    MN B2002                 NE2 HIS B  88     1555   1555  2.13  
LINK        MN    MN B2002                 OD2 ASP B 174     1555   1555  1.94  
LINK        MN    MN B2002                 NE2 HIS B 178     1555   1555  2.30  
LINK        MN    MN B2002                 O   HOH B2003     1555   1555  2.31  
LINK        MN    MN X2003                 OD2 ASP X 174     1555   1555  2.01  
LINK        MN    MN X2003                 O   HOH X2004     1555   1555  2.20  
LINK        MN    MN X2003                 NE2 HIS X  40     1555   1555  2.18  
LINK        MN    MN X2003                 NE2 HIS X 178     1555   1555  2.16  
LINK        MN    MN X2003                 NE2 HIS X  88     1555   1555  2.17  
LINK        MN    MN Y2004                 OD2 ASP Y 174     1555   1555  2.02  
LINK        MN    MN Y2004                 NE2 HIS Y 178     1555   1555  2.12  
LINK        MN    MN Y2004                 NE2 HIS Y  40     1555   1555  1.98  
LINK        MN    MN Y2004                 NE2 HIS Y  88     1555   1555  2.26  
LINK        MN    MN Y2004                 O   HOH Y2006     1555   1555  2.32  
CISPEP   1 GLN A   29    PRO A   30          0         0.11                     
CISPEP   2 GLN B   29    PRO B   30          0        -0.70                     
CISPEP   3 GLN X   29    PRO X   30          0        -0.79                     
CISPEP   4 GLN Y   29    PRO Y   30          0        -0.60                     
SITE     1 AC1  5 HIS A  40  HIS A  88  ASP A 174  HIS A 178                    
SITE     2 AC1  5 HOH A2005                                                     
SITE     1 AC2  5 HIS B  40  HIS B  88  ASP B 174  HIS B 178                    
SITE     2 AC2  5 HOH B2003                                                     
SITE     1 AC3  5 HIS X  40  HIS X  88  ASP X 174  HIS X 178                    
SITE     2 AC3  5 HOH X2004                                                     
SITE     1 AC4  5 HIS Y  40  HIS Y  88  ASP Y 174  HIS Y 178                    
SITE     2 AC4  5 HOH Y2006                                                     
CRYST1   65.882   98.697  139.281  90.00  90.00  90.00 P 21 21 21   16          
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      0.015179  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010132  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007180        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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