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Database: PDB
Entry: 2P4K
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Original site: 2P4K 
HEADER    OXIDOREDUCTASE                          12-MAR-07   2P4K              
TITLE     CONTRIBUTION TO STRUCTURE AND CATALYSIS OF TYROSINE 34 IN             
TITLE    2 HUMAN MANGANESE SUPEROXIDE DISMUTASE                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: QC774I (SOD --);                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTRC99A                                   
KEYWDS    MNSOD, MANGANESE SUPEROXIDE DISMUTASE, Y34N MUTATION,                 
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.J.PERRY                                                             
REVDAT   4   26-MAY-09 2P4K    1       JRNL                                     
REVDAT   3   07-APR-09 2P4K    1       JRNL                                     
REVDAT   2   24-FEB-09 2P4K    1       VERSN                                    
REVDAT   1   03-APR-07 2P4K    0                                                
JRNL        AUTH   J.J.PERRY,A.S.HEARN,D.E.CABELLI,H.S.NICK,                    
JRNL        AUTH 2 J.A.TAINER,D.N.SILVERMAN                                     
JRNL        TITL   CONTRIBUTION OF HUMAN MANGANESE SUPEROXIDE                   
JRNL        TITL 2 DISMUTASE TYROSINE 34 TO STRUCTURE AND CATALYSIS.            
JRNL        REF    BIOCHEMISTRY                  V.  48  3417 2009              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   19265433                                                     
JRNL        DOI    10.1021/BI8023288                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.48 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.48                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.160                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.222                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 128773                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 115223                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 6276                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 4                                             
REMARK   3   SOLVENT ATOMS      : 1202                                          
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 7482.00                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 0                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 61276                   
REMARK   3   NUMBER OF RESTRAINTS                     : 73318                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.009                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.026                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.025                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.044                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.054                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.016                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.003                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.052                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228        
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2P4K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041957.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JAN-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03                               
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL SI(311) BENT        
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 115223                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.480                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06000                            
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) : 1.48                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
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: PDB ENTRY 1N0J                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 MM K2HPO4, 22% POLYETHYLENE           
REMARK 280  GLYCOL (PEG) 2000 MONOMETHYL ETHER, PH 7.8, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
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       36.77950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.04850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.89900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.04850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.77950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.89900            
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: 8450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TYR A  11   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    TYR A  45   CB  -  CG  -  CD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    TYR B  11   CB  -  CG  -  CD2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG B  99   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    TYR B 176   CB  -  CG  -  CD2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG B 192   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    TYR C 176   CB  -  CG  -  CD2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    TYR D  45   CB  -  CG  -  CD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    CYS D 196   CB  -  CA  -  C   ANGL. DEV. = -13.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  29      -60.73   -109.43                                   
REMARK 500    ASN A 142     -127.75     56.92                                   
REMARK 500    TYR A 165      -16.87   -144.91                                   
REMARK 500    LYS A 170     -134.50     53.02                                   
REMARK 500    ASN B 142     -122.83     49.02                                   
REMARK 500    TYR B 165      -17.61   -149.19                                   
REMARK 500    LYS B 170     -136.51     56.78                                   
REMARK 500    ASN C 142     -126.90     52.12                                   
REMARK 500    TYR C 165      -15.55   -149.38                                   
REMARK 500    LYS C 170     -137.77     53.47                                   
REMARK 500    ASN D 142     -122.76     53.62                                   
REMARK 500    TYR D 165      -17.13   -148.48                                   
REMARK 500    LYS D 170     -137.54     53.80                                   
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 A 211        DISTANCE =  8.33 ANGSTROMS                       
REMARK 525    HOH A 314        DISTANCE =  5.62 ANGSTROMS                       
REMARK 525    HOH D 430        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH B 454        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH D 471        DISTANCE =  5.05 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 A 199  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 159   OD2                                                    
REMARK 620 2 HIS A  26   NE2  83.0                                              
REMARK 620 3 HIS A  74   NE2 110.6  89.3                                        
REMARK 620 4 HIS A 163   NE2 119.9  92.8 129.3                                  
REMARK 620 5 HOH A 511   O    85.6 168.5  93.8  93.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 199  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 159   OD2                                                    
REMARK 620 2 HIS B  26   NE2  85.7                                              
REMARK 620 3 HIS B  74   NE2 110.3  90.3                                        
REMARK 620 4 HIS B 163   NE2 122.9  90.0 126.7                                  
REMARK 620 5 HOH B 528   O    85.2 170.9  92.7  95.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 199  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 159   OD2                                                    
REMARK 620 2 HIS C  26   NE2  83.8                                              
REMARK 620 3 HIS C  74   NE2 112.2  88.1                                        
REMARK 620 4 HIS C 163   NE2 118.0  92.4 129.5                                  
REMARK 620 5 HOH C 465   O    86.4 170.2  94.7  93.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 199  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 159   OD2                                                    
REMARK 620 2 HIS D  26   NE2  83.8                                              
REMARK 620 3 HIS D  74   NE2 111.5  88.4                                        
REMARK 620 4 HIS D 163   NE2 121.2  89.5 126.7                                  
REMARK 620 5 HOH D 494   O    89.0 172.6  95.7  92.9                            
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 199                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 199                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 199                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 199                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ZTE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1ZUQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1ZSP   RELATED DB: PDB                                   
DBREF  2P4K A    1   198  UNP    P04179   SODM_HUMAN      25    222             
DBREF  2P4K B    1   198  UNP    P04179   SODM_HUMAN      25    222             
DBREF  2P4K C    1   198  UNP    P04179   SODM_HUMAN      25    222             
DBREF  2P4K D    1   198  UNP    P04179   SODM_HUMAN      25    222             
SEQADV 2P4K ASN A   34  UNP  P04179    TYR    58 ENGINEERED                     
SEQADV 2P4K ASN B   34  UNP  P04179    TYR    58 ENGINEERED                     
SEQADV 2P4K ASN C   34  UNP  P04179    TYR    58 ENGINEERED                     
SEQADV 2P4K ASN D   34  UNP  P04179    TYR    58 ENGINEERED                     
SEQRES   1 A  198  LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA          
SEQRES   2 A  198  LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS          
SEQRES   3 A  198  HIS SER LYS HIS HIS ALA ALA ASN VAL ASN ASN LEU ASN          
SEQRES   4 A  198  VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY          
SEQRES   5 A  198  ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 A  198  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 A  198  THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY          
SEQRES   8 A  198  GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE          
SEQRES   9 A  198  ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY          
SEQRES  10 A  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS          
SEQRES  11 A  198  GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN GLN          
SEQRES  12 A  198  ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU          
SEQRES  13 A  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR          
SEQRES  14 A  198  LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN          
SEQRES  15 A  198  VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA          
SEQRES  16 A  198  CYS LYS LYS                                                  
SEQRES   1 B  198  LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA          
SEQRES   2 B  198  LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS          
SEQRES   3 B  198  HIS SER LYS HIS HIS ALA ALA ASN VAL ASN ASN LEU ASN          
SEQRES   4 B  198  VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY          
SEQRES   5 B  198  ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 B  198  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 B  198  THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY          
SEQRES   8 B  198  GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE          
SEQRES   9 B  198  ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY          
SEQRES  10 B  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS          
SEQRES  11 B  198  GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN GLN          
SEQRES  12 B  198  ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU          
SEQRES  13 B  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR          
SEQRES  14 B  198  LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN          
SEQRES  15 B  198  VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA          
SEQRES  16 B  198  CYS LYS LYS                                                  
SEQRES   1 C  198  LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA          
SEQRES   2 C  198  LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS          
SEQRES   3 C  198  HIS SER LYS HIS HIS ALA ALA ASN VAL ASN ASN LEU ASN          
SEQRES   4 C  198  VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY          
SEQRES   5 C  198  ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 C  198  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 C  198  THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY          
SEQRES   8 C  198  GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE          
SEQRES   9 C  198  ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY          
SEQRES  10 C  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS          
SEQRES  11 C  198  GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN GLN          
SEQRES  12 C  198  ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU          
SEQRES  13 C  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR          
SEQRES  14 C  198  LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN          
SEQRES  15 C  198  VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA          
SEQRES  16 C  198  CYS LYS LYS                                                  
SEQRES   1 D  198  LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA          
SEQRES   2 D  198  LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS          
SEQRES   3 D  198  HIS SER LYS HIS HIS ALA ALA ASN VAL ASN ASN LEU ASN          
SEQRES   4 D  198  VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY          
SEQRES   5 D  198  ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 D  198  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 D  198  THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY          
SEQRES   8 D  198  GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE          
SEQRES   9 D  198  ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY          
SEQRES  10 D  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS          
SEQRES  11 D  198  GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN GLN          
SEQRES  12 D  198  ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU          
SEQRES  13 D  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR          
SEQRES  14 D  198  LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN          
SEQRES  15 D  198  VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA          
SEQRES  16 D  198  CYS LYS LYS                                                  
HET     MN  A 199       1                                                       
HET     MN  B 199       1                                                       
HET     MN  C 199       1                                                       
HET     MN  D 199       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   9  HOH   *1202(H2 O)                                                   
HELIX    1   1 ASN A   19  LYS A   29  1                                  11    
HELIX    2   2 LYS A   29  GLY A   52  1                                  24    
HELIX    3   3 ASP A   53  ASN A   80  1                                  28    
HELIX    4   4 LYS A   90  GLY A  102  1                                  13    
HELIX    5   5 SER A  103  GLY A  117  1                                  15    
HELIX    6   6 PRO A  145  GLY A  151  1                                   7    
HELIX    7   7 TRP A  161  ALA A  164  5                                   4    
HELIX    8   8 TYR A  165  LYS A  170  1                                   6    
HELIX    9   9 VAL A  172  TRP A  181  1                                  10    
HELIX   10  10 ASN A  182  ILE A  184  5                                   3    
HELIX   11  11 ASN A  185  ALA A  195  1                                  11    
HELIX   12  12 CYS A  196  LYS A  198  5                                   3    
HELIX   13  13 ASN B   19  LYS B   29  1                                  11    
HELIX   14  14 LYS B   29  GLY B   52  1                                  24    
HELIX   15  15 ASP B   53  ASN B   80  1                                  28    
HELIX   16  16 GLY B   91  GLY B  102  1                                  12    
HELIX   17  17 SER B  103  GLY B  117  1                                  15    
HELIX   18  18 PRO B  145  GLY B  151  1                                   7    
HELIX   19  19 TRP B  161  ALA B  164  5                                   4    
HELIX   20  20 TYR B  165  LYS B  170  1                                   6    
HELIX   21  21 VAL B  172  TRP B  181  1                                  10    
HELIX   22  22 ASN B  182  ILE B  184  5                                   3    
HELIX   23  23 ASN B  185  ALA B  195  1                                  11    
HELIX   24  24 ASN C   19  LYS C   29  1                                  11    
HELIX   25  25 LYS C   29  GLY C   52  1                                  24    
HELIX   26  26 ASP C   53  ASN C   80  1                                  28    
HELIX   27  27 LYS C   90  GLY C  102  1                                  13    
HELIX   28  28 SER C  103  GLY C  117  1                                  15    
HELIX   29  29 PRO C  145  GLY C  151  1                                   7    
HELIX   30  30 TRP C  161  ALA C  164  5                                   4    
HELIX   31  31 TYR C  165  LYS C  170  1                                   6    
HELIX   32  32 VAL C  172  TRP C  181  1                                  10    
HELIX   33  33 ASN C  182  ILE C  184  5                                   3    
HELIX   34  34 ASN C  185  CYS C  196  1                                  12    
HELIX   35  35 ASN D   19  LYS D   29  1                                  11    
HELIX   36  36 LYS D   29  GLY D   52  1                                  24    
HELIX   37  37 ASP D   53  ASN D   80  1                                  28    
HELIX   38  38 LYS D   90  GLY D  102  1                                  13    
HELIX   39  39 SER D  103  GLY D  117  1                                  15    
HELIX   40  40 PRO D  145  GLY D  151  1                                   7    
HELIX   41  41 TRP D  161  ALA D  164  5                                   4    
HELIX   42  42 TYR D  165  LYS D  170  1                                   6    
HELIX   43  43 VAL D  172  TRP D  181  1                                  10    
HELIX   44  44 ASN D  182  ILE D  184  5                                   3    
HELIX   45  45 ASN D  185  ALA D  195  1                                  11    
SHEET    1   A 3 HIS A 134  PRO A 141  0                                        
SHEET    2   A 3 GLY A 122  ASN A 129 -1  N  ASN A 129   O  HIS A 134           
SHEET    3   A 3 ILE A 153  ASP A 159 -1  O  LEU A 156   N  LEU A 126           
SHEET    1   B 3 HIS B 134  PRO B 141  0                                        
SHEET    2   B 3 GLY B 122  ASN B 129 -1  N  GLY B 127   O  GLN B 136           
SHEET    3   B 3 ILE B 153  ASP B 159 -1  O  LEU B 156   N  LEU B 126           
SHEET    1   C 3 HIS C 134  PRO C 141  0                                        
SHEET    2   C 3 GLY C 122  ASN C 129 -1  N  GLY C 127   O  GLN C 136           
SHEET    3   C 3 ILE C 153  ASP C 159 -1  O  LEU C 156   N  LEU C 126           
SHEET    1   D 3 HIS D 134  PRO D 141  0                                        
SHEET    2   D 3 GLY D 122  ASN D 129 -1  N  GLY D 127   O  GLN D 136           
SHEET    3   D 3 ILE D 153  ASP D 159 -1  O  LEU D 156   N  LEU D 126           
LINK         OD2 ASP A 159                MN    MN A 199     1555   1555  2.07  
LINK         OD2 ASP B 159                MN    MN B 199     1555   1555  2.04  
LINK         OD2 ASP C 159                MN    MN C 199     1555   1555  2.05  
LINK         OD2 ASP D 159                MN    MN D 199     1555   1555  2.07  
LINK         NE2 HIS A  26                MN    MN A 199     1555   1555  2.18  
LINK         NE2 HIS A  74                MN    MN A 199     1555   1555  2.21  
LINK         NE2 HIS A 163                MN    MN A 199     1555   1555  2.16  
LINK         NE2 HIS B  26                MN    MN B 199     1555   1555  2.19  
LINK         NE2 HIS B  74                MN    MN B 199     1555   1555  2.20  
LINK         NE2 HIS B 163                MN    MN B 199     1555   1555  2.16  
LINK         NE2 HIS C  26                MN    MN C 199     1555   1555  2.23  
LINK         NE2 HIS C  74                MN    MN C 199     1555   1555  2.20  
LINK         NE2 HIS C 163                MN    MN C 199     1555   1555  2.16  
LINK         NE2 HIS D  26                MN    MN D 199     1555   1555  2.21  
LINK         NE2 HIS D  74                MN    MN D 199     1555   1555  2.19  
LINK         NE2 HIS D 163                MN    MN D 199     1555   1555  2.16  
LINK        MN    MN A 199                 O   HOH A 511     1555   1555  2.27  
LINK        MN    MN B 199                 O   HOH B 528     1555   1555  2.26  
LINK        MN    MN C 199                 O   HOH C 465     1555   1555  2.27  
LINK        MN    MN D 199                 O   HOH D 494     1555   1555  2.27  
CISPEP   1 GLU A   15    PRO A   16          0        -2.34                     
CISPEP   2 GLU B   15    PRO B   16          0        -1.95                     
CISPEP   3 GLU C   15    PRO C   16          0        -0.19                     
CISPEP   4 GLU D   15    PRO D   16          0        -4.55                     
SITE     1 AC1  5 HIS A  26  HIS A  74  ASP A 159  HIS A 163                    
SITE     2 AC1  5 HOH A 511                                                     
SITE     1 AC2  5 HIS B  26  HIS B  74  ASP B 159  HIS B 163                    
SITE     2 AC2  5 HOH B 528                                                     
SITE     1 AC3  5 HIS C  26  HIS C  74  ASP C 159  HIS C 163                    
SITE     2 AC3  5 HOH C 465                                                     
SITE     1 AC4  5 HIS D  26  HIS D  74  ASP D 159  HIS D 163                    
SITE     2 AC4  5 HOH D 494                                                     
CRYST1   73.559   77.798  136.097  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      0.013595  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012854  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007348        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system